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Conserved domains on  [gi|15597498|ref|NP_250992|]
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protein AmbE [Pseudomonas aeruginosa PAO1]

Protein Classification

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List of domain hits

 Name Accession Description Interval E-value
DCL_NRPS-like cd19536
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ...
 1360-1776 1.25e-139

DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal fungal CT domains and Dual Epimerization/Condensation (E/C) domains; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type [D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L))], which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


:

Pssm-ID: 380459 [Multi-domain]  Cd Length: 419  Bit Score: 442.27  E-value: 1.25e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1360 AYPMTSLQQGMLLQSEAS-GDPRLLHNVVLHeVHGRLDGELLARAWAILIGRHAILRTGFDLHGGQVPLQWVHPatAVAA 1438
Cdd:cd19536    1 MYPLSSLQEGMLFHSLLNpGGSVYLHNYTYT-VGRRLNLDLLLEALQVLIDRHDILRTSFIEDGLGQPVQVVHR--QAQV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1439 EVPVHDLCGldGETRRLRLRAWIEEEQATPFDWSRPPLVRLAALALDER-RFALGVAEHHSVLDGWSLQSLVDELLAVYA 1517
Cdd:cd19536   78 PVTELDLTP--LEEQLDPLRAYKEETKIRRFDLGRAPLVRAALVRKDEReRFLLVISDHHSILDGWSLYLLVKEILAVYN 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1518 DLLAGvvAREAEAPAVGFRDYVALEREAEANAASALFWLDYLAGARYRPLPGLAE---EGPRRMAAVRVDVPADSLSrlR 1594
Cdd:cd19536  156 QLLEY--KPLSLPPAQPYRDFVAHERASIQQAASERYWREYLAGATLATLPALSEavgGGPEQDSELLVSVPLPVRS--R 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1595 ALAERSGLPLRSLLLAAHGRALCRFSDADEVVTGFVSHGRPEE-PGADRLLGLFLNTLPCRLSASV-DLLDSARRAFDYE 1672
Cdd:cd19536  232 SLAKRSGIPLSTLLLAAWALVLSRHSGSDDVVFGTVVHGRSEEtTGAERLLGLFLNTLPLRVTLSEeTVEDLLKRAQEQE 311

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1673 RASLEHRRHPLAAIRRRNR-ELRLDSLFNFVDFHQDDAAPA-----GVRHGGILDQVVVDVDVPLAVDFEvaGERLEVGF 1746
Cdd:cd19536  312 LESLSHEQVPLADIQRCSEgEPLFDSIVNFRHFDLDFGLPEwgsdeGMRRGLLFSEFKSNYDVNLSVLPK--QDRLELKL 389

                        410       420       430
                 ....*....|....*....|....*....|
gi 15597498 1747 QYAAGRFPAERAEALAGAYREALLALLGDP 1776
Cdd:cd19536  390 AYNSQVLDEEQAQRLAAYYKSAIAELATAP 419
A_NRPS cd05930
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ...
 462-910 6.38e-135

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: 430.03  E-value: 6.38e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  462 PQAPALLDAHGSLDFATLRARSEAVAEALLAAGVRPGQAVAVMTGRNREAIVALLGVMRAAAVYTPVNPEFPAARVERMR 541
Cdd:cd05930    1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  542 EAGGIVFALADAEcagrareafagacldlstlplagsgmslpapggrDAAYMIFTSGTSGQPKGVVVEHASALNLSQALA 621
Cdd:cd05930   81 EDSGAKLVLTDPD----------------------------------DLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQ 126

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  622 RTVYanvVGEGLRVTVNAPFSFDSSIKQIL-QLLSGHCLVLVPQEVRSDPQRMLGFLEERRIDVLDCTPSLFRLLLQAGL 700
Cdd:cd05930  127 EAYP---LTPGDRVLQFTSFSFDVSVWEIFgALLAGATLVVLPEEVRKDPEALADLLAEEGITVLHLTPSLLRLLLQELE 203

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  701 DDAHPALpGRILVGGERFdeaSWEVAAGWR----RCQVFNLYGPTEATVNASLARVAEH----ARPTIGRALANVDLHVV 772
Cdd:cd05930  204 LAALPSL-RLVLVGGEAL---PPDLVRRWRellpGARLVNLYGPTEATVDATYYRVPPDdeedGRVPIGRPIPNTRVYVL 279

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  773 DGLGRRKTRGASGELWIGGAGVARGYAGDAGEAAGRFVEEGWPGSGRLYRSGDLVRWRADGCLEFLGRIDEQVKINGYRI 852
Cdd:cd05930  280 DENLRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNPFGPGERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRI 359

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15597498  853 ELGEIRSALLEHPAVGEAAVLTDEADAAEPgadrRIVAFVTAAEETADE-----SWLEVDLPS 910
Cdd:cd05930  360 ELGEIEAALLAHPGVREAAVVAREDGDGEK----RLVAYVVPDEGGELDeeelrAHLAERLPD 418
EntF super family cl43309
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
 3-1261 3.07e-127

EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


The actual alignment was detected with superfamily member COG1020:

Pssm-ID: 440643 [Multi-domain]  Cd Length: 1329  Bit Score: 436.21  E-value: 3.07e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498    3 ASEDLQSAVQPAASEALEGFPLSPLQTRAWRRHAERPENTVVGVRLHAPADPVATLERLRRALDGEAQLRVAYRTMPGMS 82
Cdd:COG1020    2 AAAAAAALPPAAAAAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAGR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   83 LPVQVLDGRAADLLVERLPGDGDWAGRFARESARLAASPLGGEGQPVLALGLLLDAAGETLQGLLLAAPAFVVDAASLVA 162
Cdd:COG1020   82 PVQVIQPVVAAPLPVVVLLVDLEALAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDGL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  163 LLRRGLGPAGQASADEGDE----ALLFQHFSEWANEALAGEDGESASGYWREQAAVAAESPLALADDLGEGEWTAR---- 234
Cdd:COG1020  162 LLAELLRLYLAAYAGAPLPlpplPIQYADYALWQREWLQGEELARQLAYWRQQLAGLPPLLELPTDRPRPAVQSYRgarv 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  235 -RLLPRALLERLAA----NGLPEAAALL-AWTQVAGQFQGDE----GLPlemarlVSGRLFNEFAELAGPFAGVAPLCLE 304
Cdd:COG1020  242 sFRLPAELTAALRAlarrHGVTLFMVLLaAFALLLARYSGQDdvvvGTP------VAGRPRPELEGLVGFFVNTLPLRVD 315

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  305 NVRAGSVGERLDALQAAILA------------QEEAAALRDPfaPDWPLAELGFAWLAGELDGAGVAELDCRQPPLGG-- 370
Cdd:COG1020  316 LSGDPSFAELLARVRETLLAayahqdlpferlVEELQPERDL--SRNPLFQVMFVLQNAPADELELPGLTLEPLELDSgt 393

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  371 ---FLELQVLPHGEGRLASLRVRRDH-DGTLAGRLLDAWVECLESIAADRQLPLAGLPLIGAAERERY-QAWQGERVEPA 445
Cdd:COG1020  394 akfDLTLTVVETGDGLRLTLEYNTDLfDAATIERMAGHLVTLLEALAADPDQPLGDLPLLTAAERQQLlAEWNATAAPYP 473

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  446 PVESLVAAFDLRAALQPQAPALLDAHGSLDFATLRARSEAVAEALLAAGVRPGQAVAVMTGRNREAIVALLGVMRAAAVY 525
Cdd:COG1020  474 ADATLHELFEAQAARTPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAY 553

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  526 TPVNPEFPAARVERMREAGGIVFALADAECAGRAREaFAGACLDLSTLPLAGSGMSLPAPGGR--DAAYMIFTSGTSGQP 603
Cdd:COG1020  554 VPLDPAYPAERLAYMLEDAGARLVLTQSALAARLPE-LGVPVLALDALALAAEPATNPPVPVTpdDLAYVIYTSGSTGRP 632

                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  604 KGVVVEHASALNLSQALARTvYAnvVGEGLRVTVNAPFSFDSSIKQIL-QLLSGHCLVLVPQEVRSDPQRMLGFLEERRI 682
Cdd:COG1020  633 KGVMVEHRALVNLLAWMQRR-YG--LGPGDRVLQFASLSFDASVWEIFgALLSGATLVLAPPEARRDPAALAELLARHRV 709

                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  683 DVLDCTPSLFRLLLQAGLDDAHPalPGRILVGGERFDEASWE-VAAGWRRCQVFNLYGPTEATVNASLARV----AEHAR 757
Cdd:COG1020  710 TVLNLTPSLLRALLDAAPEALPS--LRLVLVGGEALPPELVRrWRARLPGARLVNLYGPTETTVDSTYYEVtppdADGGS 787

                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  758 PTIGRALANVDLHVVDGLGRRKTRGASGELWIGGAGVARGYAGDAGEAAGRFVEEGWPGSG-RLYRSGDLVRWRADGCLE 836
Cdd:COG1020  788 VPIGRPIANTRVYVLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPFGFPGaRLYRTGDLARWLPDGNLE 867

                        890       900       910       920       930       940       950       960
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  837 FLGRIDEQVKINGYRIELGEIRSALLEHPAVGEAAVLTDEadaaEPGADRRIVAFVTAAEETADESWLE----------- 905
Cdd:COG1020  868 FLGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVARE----DAPGDKRLVAYVVPEAGAAAAAALLrlalalllppy 943

                        970       980       990      1000      1010      1020      1030      1040
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  906 -----------------VDLPSGHRVAGLNLNETEYVYQEIFVDEVYSRDGIVLPPDAVVLDVGANIGLFSLYIASRAPR 968
Cdd:COG1020  944 mvpaavvlllplpltgnGKLDRLALPAPAAAAAAAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLAL 1023

                       1050      1060      1070      1080      1090      1100      1110      1120
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  969 ARVVAFEPLAPIRRRLEANLGRYAPQVEVFGIGLSDAEREETFTYYPGYSTFSGIAEYADASGERDVIRRYLSNQGEEGG 1048
Cdd:COG1020 1024 ARAARLLLLLLLLLLLFLAAAAAAAAAAAAAAAAAAAAPLAAAAAPLPLPPLLLSLLALLLALLLLLALLALLALLLLLL 1103

                       1130      1140      1150      1160      1170      1180      1190      1200
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1049 ANLLLDNIDEILDDRLRAEAHRCRLRRLDQVIGELGLERIDLLKIDVQRAEMDVLLGLDDAALAKVRQIVLEVHDKRDGA 1128
Cdd:COG1020 1104 LLLLLLALLLLLALLLALLAALRARRAVRQEGPRLRLLVALAAALALAALLALLLAAAAAAAELLAAAALLLLLALLLLA 1183

                       1210      1220      1230      1240      1250      1260      1270      1280
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1129 TAGRADALSDLLRRHGFEVSIRQDALLEGTDRYNCYAVRPGYAESLAERIDWRALAPRPAAALGGELSEQALRGFLEARL 1208
Cdd:COG1020 1184 LLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLAAAAAALLALALLLALLALAALLALAALAALAAALLALA 1263

                       1290      1300      1310      1320      1330
                 ....*....|....*....|....*....|....*....|....*....|...
gi 15597498 1209 PAYMLPSRIARVERLPLTAEGKLDRRALLAALAAEAAAQTLEAPANATEAALL 1261
Cdd:COG1020 1264 LALLALALLLLALALLLPALARARAARTARALALLLLLALLLLLALALALLLL 1316
GrsT COG3208
Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and ...
 1880-2114 1.90e-74

Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and catabolism];


:

Pssm-ID: 442441 [Multi-domain]  Cd Length: 237  Bit Score: 247.84  E-value: 1.90e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1880 SAQPRLRLIALPPAGGNAGTFRGWDARLPADVELLAIQYPGRQERQDEPFVTDVEAMLCAIDDALLPLLDRPFALIGASL 1959
Cdd:COG3208    2 RPDARLRLFCFPYAGGSASAYRPWAAALPPDIEVLAVQLPGRGDRLGEPPLTSLEELADDLAEELAPLLDRPFALFGHSM 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1960 GGMLAYELAARLESLHGLRARQLFVISSRAPGPDLEYPRFHAMGDAELLRTLREYDVLPLEVLDDPELREISLATLRADS 2039
Cdd:COG3208   82 GALLAFELARRLERRGRPLPAHLFVSGRRAPHLPRRRRPLHDLSDAELLAELRRLGGTPEEVLADPELLELFLPILRADF 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15597498 2040 RLAADYRYRPREPLAIPITAILGEQDPGVSRVAIDGWRRHASR-YELETLAGGHGLVVTAAEEVCAILRQRLAPDV 2114
Cdd:COG3208  162 RLLETYRYTPGPPLDCPITALGGDDDPLVSPEELAAWREHTTGpFRLRVFPGGHFFLRDHPAELLALIRAALAALA 237
PRK12467 super family cl36129
peptide synthase; Provisional
 1198-1372 5.54e-21

peptide synthase; Provisional


The actual alignment was detected with superfamily member PRK12467:

Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 101.39  E-value: 5.54e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1198 QALRGFLEARLPAYMLPSRIARVERLPLTAEGKLDRRALLAALAAEAAAQTLeaPANATEAALLEIWKSVLKRPAIGVSD 1277
Cdd:PRK12467 3550 ETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDRKALPDPDAKGSREYVA--PRSEVEQQLAAIWADVLGVEQVGVTD 3627

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1278 NFFQVGGDSIRLIQMQVMAREA-GLAFTLRDVFNHQSIRELA------RLLAAPASPADALGTSAPQSLEPFALL-SAAE 1349
Cdd:PRK12467 3628 NFFELGGDSLLALQVLSRIRQSlGLKLSLRDLMSAPTIAELAgysplgDVPVNLLLDLNRLETGFPALFCRHEGLgTVFD 3707

                         170       180
                  ....*....|....*....|...
gi 15597498  1350 RKRLPEGLDDAYPMTSLQQGMLL 1372
Cdd:PRK12467 3708 YEPLAVILEGDRHVLGLTCRHLL 3730
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
 1792-1850 2.14e-04

Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.


:

Pssm-ID: 425746 [Multi-domain]  Cd Length: 62  Bit Score: 41.01  E-value: 2.14e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15597498   1792 RRVLKVLSRVLGRP---LAADQGFASAGGHSLLGVQAIAELRRLTGRQLSLGLLQGDPDARE 1850
Cdd:pfam00550    1 ERLRELLAEVLGVPaeeIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLAE 62
 
Name Accession Description Interval E-value
DCL_NRPS-like cd19536
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ...
 1360-1776 1.25e-139

DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal fungal CT domains and Dual Epimerization/Condensation (E/C) domains; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type [D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L))], which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380459 [Multi-domain]  Cd Length: 419  Bit Score: 442.27  E-value: 1.25e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1360 AYPMTSLQQGMLLQSEAS-GDPRLLHNVVLHeVHGRLDGELLARAWAILIGRHAILRTGFDLHGGQVPLQWVHPatAVAA 1438
Cdd:cd19536    1 MYPLSSLQEGMLFHSLLNpGGSVYLHNYTYT-VGRRLNLDLLLEALQVLIDRHDILRTSFIEDGLGQPVQVVHR--QAQV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1439 EVPVHDLCGldGETRRLRLRAWIEEEQATPFDWSRPPLVRLAALALDER-RFALGVAEHHSVLDGWSLQSLVDELLAVYA 1517
Cdd:cd19536   78 PVTELDLTP--LEEQLDPLRAYKEETKIRRFDLGRAPLVRAALVRKDEReRFLLVISDHHSILDGWSLYLLVKEILAVYN 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1518 DLLAGvvAREAEAPAVGFRDYVALEREAEANAASALFWLDYLAGARYRPLPGLAE---EGPRRMAAVRVDVPADSLSrlR 1594
Cdd:cd19536  156 QLLEY--KPLSLPPAQPYRDFVAHERASIQQAASERYWREYLAGATLATLPALSEavgGGPEQDSELLVSVPLPVRS--R 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1595 ALAERSGLPLRSLLLAAHGRALCRFSDADEVVTGFVSHGRPEE-PGADRLLGLFLNTLPCRLSASV-DLLDSARRAFDYE 1672
Cdd:cd19536  232 SLAKRSGIPLSTLLLAAWALVLSRHSGSDDVVFGTVVHGRSEEtTGAERLLGLFLNTLPLRVTLSEeTVEDLLKRAQEQE 311

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1673 RASLEHRRHPLAAIRRRNR-ELRLDSLFNFVDFHQDDAAPA-----GVRHGGILDQVVVDVDVPLAVDFEvaGERLEVGF 1746
Cdd:cd19536  312 LESLSHEQVPLADIQRCSEgEPLFDSIVNFRHFDLDFGLPEwgsdeGMRRGLLFSEFKSNYDVNLSVLPK--QDRLELKL 389

                        410       420       430
                 ....*....|....*....|....*....|
gi 15597498 1747 QYAAGRFPAERAEALAGAYREALLALLGDP 1776
Cdd:cd19536  390 AYNSQVLDEEQAQRLAAYYKSAIAELATAP 419
A_NRPS cd05930
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ...
 462-910 6.38e-135

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: 430.03  E-value: 6.38e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  462 PQAPALLDAHGSLDFATLRARSEAVAEALLAAGVRPGQAVAVMTGRNREAIVALLGVMRAAAVYTPVNPEFPAARVERMR 541
Cdd:cd05930    1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  542 EAGGIVFALADAEcagrareafagacldlstlplagsgmslpapggrDAAYMIFTSGTSGQPKGVVVEHASALNLSQALA 621
Cdd:cd05930   81 EDSGAKLVLTDPD----------------------------------DLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQ 126

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  622 RTVYanvVGEGLRVTVNAPFSFDSSIKQIL-QLLSGHCLVLVPQEVRSDPQRMLGFLEERRIDVLDCTPSLFRLLLQAGL 700
Cdd:cd05930  127 EAYP---LTPGDRVLQFTSFSFDVSVWEIFgALLAGATLVVLPEEVRKDPEALADLLAEEGITVLHLTPSLLRLLLQELE 203

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  701 DDAHPALpGRILVGGERFdeaSWEVAAGWR----RCQVFNLYGPTEATVNASLARVAEH----ARPTIGRALANVDLHVV 772
Cdd:cd05930  204 LAALPSL-RLVLVGGEAL---PPDLVRRWRellpGARLVNLYGPTEATVDATYYRVPPDdeedGRVPIGRPIPNTRVYVL 279

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  773 DGLGRRKTRGASGELWIGGAGVARGYAGDAGEAAGRFVEEGWPGSGRLYRSGDLVRWRADGCLEFLGRIDEQVKINGYRI 852
Cdd:cd05930  280 DENLRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNPFGPGERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRI 359

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15597498  853 ELGEIRSALLEHPAVGEAAVLTDEADAAEPgadrRIVAFVTAAEETADE-----SWLEVDLPS 910
Cdd:cd05930  360 ELGEIEAALLAHPGVREAAVVAREDGDGEK----RLVAYVVPDEGGELDeeelrAHLAERLPD 418
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
 3-1261 3.07e-127

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: 436.21  E-value: 3.07e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498    3 ASEDLQSAVQPAASEALEGFPLSPLQTRAWRRHAERPENTVVGVRLHAPADPVATLERLRRALDGEAQLRVAYRTMPGMS 82
Cdd:COG1020    2 AAAAAAALPPAAAAAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAGR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   83 LPVQVLDGRAADLLVERLPGDGDWAGRFARESARLAASPLGGEGQPVLALGLLLDAAGETLQGLLLAAPAFVVDAASLVA 162
Cdd:COG1020   82 PVQVIQPVVAAPLPVVVLLVDLEALAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDGL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  163 LLRRGLGPAGQASADEGDE----ALLFQHFSEWANEALAGEDGESASGYWREQAAVAAESPLALADDLGEGEWTAR---- 234
Cdd:COG1020  162 LLAELLRLYLAAYAGAPLPlpplPIQYADYALWQREWLQGEELARQLAYWRQQLAGLPPLLELPTDRPRPAVQSYRgarv 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  235 -RLLPRALLERLAA----NGLPEAAALL-AWTQVAGQFQGDE----GLPlemarlVSGRLFNEFAELAGPFAGVAPLCLE 304
Cdd:COG1020  242 sFRLPAELTAALRAlarrHGVTLFMVLLaAFALLLARYSGQDdvvvGTP------VAGRPRPELEGLVGFFVNTLPLRVD 315

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  305 NVRAGSVGERLDALQAAILA------------QEEAAALRDPfaPDWPLAELGFAWLAGELDGAGVAELDCRQPPLGG-- 370
Cdd:COG1020  316 LSGDPSFAELLARVRETLLAayahqdlpferlVEELQPERDL--SRNPLFQVMFVLQNAPADELELPGLTLEPLELDSgt 393

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  371 ---FLELQVLPHGEGRLASLRVRRDH-DGTLAGRLLDAWVECLESIAADRQLPLAGLPLIGAAERERY-QAWQGERVEPA 445
Cdd:COG1020  394 akfDLTLTVVETGDGLRLTLEYNTDLfDAATIERMAGHLVTLLEALAADPDQPLGDLPLLTAAERQQLlAEWNATAAPYP 473

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  446 PVESLVAAFDLRAALQPQAPALLDAHGSLDFATLRARSEAVAEALLAAGVRPGQAVAVMTGRNREAIVALLGVMRAAAVY 525
Cdd:COG1020  474 ADATLHELFEAQAARTPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAY 553

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  526 TPVNPEFPAARVERMREAGGIVFALADAECAGRAREaFAGACLDLSTLPLAGSGMSLPAPGGR--DAAYMIFTSGTSGQP 603
Cdd:COG1020  554 VPLDPAYPAERLAYMLEDAGARLVLTQSALAARLPE-LGVPVLALDALALAAEPATNPPVPVTpdDLAYVIYTSGSTGRP 632

                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  604 KGVVVEHASALNLSQALARTvYAnvVGEGLRVTVNAPFSFDSSIKQIL-QLLSGHCLVLVPQEVRSDPQRMLGFLEERRI 682
Cdd:COG1020  633 KGVMVEHRALVNLLAWMQRR-YG--LGPGDRVLQFASLSFDASVWEIFgALLSGATLVLAPPEARRDPAALAELLARHRV 709

                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  683 DVLDCTPSLFRLLLQAGLDDAHPalPGRILVGGERFDEASWE-VAAGWRRCQVFNLYGPTEATVNASLARV----AEHAR 757
Cdd:COG1020  710 TVLNLTPSLLRALLDAAPEALPS--LRLVLVGGEALPPELVRrWRARLPGARLVNLYGPTETTVDSTYYEVtppdADGGS 787

                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  758 PTIGRALANVDLHVVDGLGRRKTRGASGELWIGGAGVARGYAGDAGEAAGRFVEEGWPGSG-RLYRSGDLVRWRADGCLE 836
Cdd:COG1020  788 VPIGRPIANTRVYVLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPFGFPGaRLYRTGDLARWLPDGNLE 867

                        890       900       910       920       930       940       950       960
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  837 FLGRIDEQVKINGYRIELGEIRSALLEHPAVGEAAVLTDEadaaEPGADRRIVAFVTAAEETADESWLE----------- 905
Cdd:COG1020  868 FLGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVARE----DAPGDKRLVAYVVPEAGAAAAAALLrlalalllppy 943

                        970       980       990      1000      1010      1020      1030      1040
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  906 -----------------VDLPSGHRVAGLNLNETEYVYQEIFVDEVYSRDGIVLPPDAVVLDVGANIGLFSLYIASRAPR 968
Cdd:COG1020  944 mvpaavvlllplpltgnGKLDRLALPAPAAAAAAAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLAL 1023

                       1050      1060      1070      1080      1090      1100      1110      1120
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  969 ARVVAFEPLAPIRRRLEANLGRYAPQVEVFGIGLSDAEREETFTYYPGYSTFSGIAEYADASGERDVIRRYLSNQGEEGG 1048
Cdd:COG1020 1024 ARAARLLLLLLLLLLLFLAAAAAAAAAAAAAAAAAAAAPLAAAAAPLPLPPLLLSLLALLLALLLLLALLALLALLLLLL 1103

                       1130      1140      1150      1160      1170      1180      1190      1200
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1049 ANLLLDNIDEILDDRLRAEAHRCRLRRLDQVIGELGLERIDLLKIDVQRAEMDVLLGLDDAALAKVRQIVLEVHDKRDGA 1128
Cdd:COG1020 1104 LLLLLLALLLLLALLLALLAALRARRAVRQEGPRLRLLVALAAALALAALLALLLAAAAAAAELLAAAALLLLLALLLLA 1183

                       1210      1220      1230      1240      1250      1260      1270      1280
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1129 TAGRADALSDLLRRHGFEVSIRQDALLEGTDRYNCYAVRPGYAESLAERIDWRALAPRPAAALGGELSEQALRGFLEARL 1208
Cdd:COG1020 1184 LLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLAAAAAALLALALLLALLALAALLALAALAALAAALLALA 1263

                       1290      1300      1310      1320      1330
                 ....*....|....*....|....*....|....*....|....*....|...
gi 15597498 1209 PAYMLPSRIARVERLPLTAEGKLDRRALLAALAAEAAAQTLEAPANATEAALL 1261
Cdd:COG1020 1264 LALLALALLLLALALLLPALARARAARTARALALLLLLALLLLLALALALLLL 1316
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
 494-872 2.01e-108

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: 352.72  E-value: 2.01e-108
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498    494 GVRPGQAVAVMTGRNREAIVALLGVMRAAAVYTPVNPEFPAARVERMREAGGIVFALADAECAGRARE-AFAGACLDLST 572
Cdd:TIGR01733   21 GVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDSALASRLAGlVLPVILLDPLE 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498    573 LPLAGSGMSLPAP----GGRDAAYMIFTSGTSGQPKGVVVEHASALNLSQALARtvyANVVGEGLRVTVNAPFSFDSSIK 648
Cdd:TIGR01733  101 LAALDDAPAPPPPdapsGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLAR---RYGLDPDDRVLQFASLSFDASVE 177

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498    649 QIL-QLLSGHCLVLVPQEVRSDPQRMLGFL-EERRIDVLDCTPSLFRLLLQAglddAHPALPG--RILVGGERFDEAswe 724
Cdd:TIGR01733  178 EIFgALLAGATLVVPPEDEERDDAALLAALiAEHPVTVLNLTPSLLALLAAA----LPPALASlrLVILGGEALTPA--- 250

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498    725 VAAGWRR----CQVFNLYGPTEATVNASLARVAEHARP-----TIGRALANVDLHVVDGLGRRKTRGASGELWIGGAGVA 795
Cdd:TIGR01733  251 LVDRWRArgpgARLINLYGPTETTVWSTATLVDPDDAPrespvPIGRPLANTRLYVLDDDLRPVPVGVVGELYIGGPGVA 330

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15597498    796 RGYAGDAGEAAGRFVEEGWPGS--GRLYRSGDLVRWRADGCLEFLGRIDEQVKINGYRIELGEIRSALLEHPAVGEAAV 872
Cdd:TIGR01733  331 RGYLNRPELTAERFVPDPFAGGdgARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
PRK12316 PRK12316
peptide synthase; Provisional
 400-1804 4.85e-94

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 342.32  E-value: 4.85e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   400 RLLDAWVECLESIAADRQLPLAGLPLIGAAERERY-QAWQGERVEPAPVESLVAAFDLRAALQPQAPALLDAHGSLDFAT 478
Cdd:PRK12316  462 RMARHWQNLLRGMVENPQARVDELPMLDAEERGQLvEGWNATAAEYPLQRGVHRLFEEQVERTPEAPALAFGEETLDYAE 541

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   479 LRARSEAVAEALLAAGVRPGQAVAVMTGRNREAIVALLGVMRAAAVYTPVNPEFPAARVERMREAGGIVFALADAECAGR 558
Cdd:PRK12316  542 LNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLSQSHLGRK 621

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   559 AREAFAGACLDLSTLPLAGSGMSLPAPG----GRDAAYMIFTSGTSGQPKGVVVEHASALNLSQAlARTVYANVVGEglR 634
Cdd:PRK12316  622 LPLAAGVQVLDLDRPAAWLEGYSEENPGtelnPENLAYVIYTSGSTGKPKGAGNRHRALSNRLCW-MQQAYGLGVGD--T 698

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   635 VTVNAPFSFDSSIKQI-LQLLSGHCLVLVPQEVRSDPQRMLGFLEERRIDVLDCTPSLFRLLLQAGLDDAHPALPgRILV 713
Cdd:PRK12316  699 VLQKTPFSFDVSVWEFfWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVASCTSLR-RIVC 777

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   714 GGERFDEASWE-VAAGWRRCQVFNLYGPTEATVNAS-LARVAEHAR-PTIGRALANVDLHVVDGLGRRKTRGASGELWIG 790
Cdd:PRK12316  778 SGEALPADAQEqVFAKLPQAGLYNLYGPTEAAIDVThWTCVEEGGDsVPIGRPIANLACYILDANLEPVPVGVLGELYLA 857

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   791 GAGVARGYAGDAGEAAGRFVEEGWPGSGRLYRSGDLVRWRADGCLEFLGRIDEQVKINGYRIELGEIRSALLEHPAVGEA 870
Cdd:PRK12316  858 GRGLARGYHGRPGLTAERFVPSPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREA 937

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   871 AV-------------LTDEADA---------------------------------------AEPGADRRIVAFVTAAEET 898
Cdd:PRK12316  938 AVlavdgkqlvgyvvLESEGGDwrealkahlaaslpeymvpaqwlalerlpltpngkldrkALPAPEASVAQQGYVAPRN 1017

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   899 ADESWLEV---DLPSGHRVaGLNLNETEYVYQEIFVDEVYSR---DGIVLPPDavvlDVGANIGLFSLYIASRAPRA--- 969
Cdd:PRK12316 1018 ALERTLAAiwqDVLGVERV-GLDDNFFELGGDSIVSIQVVSRarqAGIQLSPR----DLFQHQTIRSLALVAKAGQAtaa 1092

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   970 ---RVVAFEPLAPIRRRL--EANLGRY--------APQVEVFGIGLSDAEREETFTYYPGYSTFSGIAE-----YADASG 1031
Cdd:PRK12316 1093 dqgPASGEVALAPVQRWFfeQAIPQRQhwnqslllQARQPLDPDRLGRALERLVAHHDALRLRFREEDGgwqqaYAAPQA 1172

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1032 ERDVIRRYLSNQG------EEGGANLLLDNiDEILDDRLRAEAHRCRlrRLDQVIGELGLERID--LLKIDVQRAEMDVL 1103
Cdd:PRK12316 1173 GEVLWQRQAASEEellalcEEAQRSLDLEQ-GPLLRALLVDMADGSQ--RLLLVIHHLVVDGVSwrILLEDLQRAYADLD 1249

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1104 LGLD---------DAALAKVRQIVLEVHDKRDGATAGRADAL------SDLLRRHGFEVSIRQDA--------------- 1153
Cdd:PRK12316 1250 ADLPartssyqawARRLHEHAGARAEELDYWQAQLEDAPHELpcenpdGALENRHERKLELRLDAertrqllqeapaayr 1329

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1154 ------LLEGTDRYNC-YAVRP-------GYA-ESLAERID------WRALAPRPAAALGGELSE------QALRGFLEA 1206
Cdd:PRK12316 1330 tqvndlLLTALARVTCrWSGQAsvlvqleGHGrEDLFEDIDlsrtvgWFTSLFPVRLTPAADLGEsikaikEQLRAVPDK 1409

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1207 RLPAYML-----PSRIARVERLP-----LTAEGKLDRRALLAALAAEAAAQTLeapANATEAALLEIWKSvlkrpaigvs 1276
Cdd:PRK12316 1410 GIGYGLLrylagEEAAARLAALPqpritFNYLGQFDRQFDEAALFVPATESAG---AAQDPCAPLANWLS---------- 1476

                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1277 dnffqvggdsirlIQMQVMAREAGLAFTL-RDVFNHQSIRELAR-----LLAAPASPADALGTSAPQSLEPFALLSAAER 1350
Cdd:PRK12316 1477 -------------IEGQVYGGELSLHWSFsREMFAEATVQRLADdyareLQALIEHCCDERNRGVTPSDFPLAGLSQAQL 1543

                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1351 KRLP---EGLDDAYPMTSLQQGMLLQS---EASGDprlLHNVVLHEVHGrLDGELLARAWAILIGRHAILRTGFDLHGG- 1423
Cdd:PRK12316 1544 DALPlpaGEIADIYPLSPMQQGMLFHSlyeQEAGD---YINQLRVDVQG-LDPDRFRAAWQATVDRHEILRSGFLWQDGl 1619

                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1424 QVPLQWVHPATavaaEVPVHDLCGLDGETRRLRLRAWIEEEQATPFDWSRPPLVRLAALALDERRFALGVAEHHSVLDGW 1503
Cdd:PRK12316 1620 EQPLQVIHKQV----ELPFAELDWRGREDLGQALDALAQAERQKGFDLTRAPLLRLVLVRTGEGRHHLIYTNHHILMDGW 1695

                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1504 SLQSLVDELLAVYAdllagvvAREAEAPAVGFRDYVA-LEREAEanAASALFWLDYLAgaryrplpglAEEGPRRMA-AV 1581
Cdd:PRK12316 1696 SNAQLLGEVLQRYA-------GQPVAAPGGRYRDYIAwLQRQDA--AASEAFWKEQLA----------ALEEPTRLAqAA 1756

                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1582 RVDVP------------ADSLSRLRALAERSGLPLRSLLLAAHGRALCRFSDADEVVTGFVSHGRPEE-PGADRLLGLFL 1648
Cdd:PRK12316 1757 RTEDGqvgygdhqqlldPAQTRALAEFARAQKVTLNTLVQAAWLLLLQRYTGQETVAFGATVAGRPAElPGIEQQIGLFI 1836

                        1450      1460      1470      1480      1490      1500      1510      1520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1649 NTLP--CRLSASVDLLDSARRAFDYERASLEHRRHPLAAIRR---RNRELRLDSLFNFVDFHQDDA----APAGVRHGGI 1719
Cdd:PRK12316 1837 NTLPviAAPRPDQSVADWLQEVQALNLALREHEHTPLYDIQRwagQGGEALFDSLLVFENYPVAEAlkqgAPAGLVFGRV 1916

                        1530      1540      1550      1560      1570      1580      1590      1600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1720 LDQVVVDVDVPLAVDFevaGERLEVGFQYAAGRFPAERAEALAGAYREALLALLGDPVQPPAAAQAEDSVELRRVLKVLS 1799
Cdd:PRK12316 1917 SNHEQTNYPLTLAVTL---GETLSLQYSYDRGHFDAAAIERLDRHLLHLLEQMAEDAQAALGELALLDAGERQRILADWD 1993


                  ....*
gi 15597498  1800 RVLGR 1804
Cdd:PRK12316 1994 RTPEA 1998
PRK12467 PRK12467
peptide synthase; Provisional
 394-895 8.32e-82

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 301.69  E-value: 8.32e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   394 DGTLAGRLLDAWVECLESIAADRQLPLAGLPLIGAAERER-YQAWQGERVEPAPvESLVAAFDLRAALQPQAPALLDAHG 472
Cdd:PRK12467  458 EATTIERLATHWRNLLEAIVAEPRRRLGELPLLDAEERAReLVRWNAPATEYAP-DCVHQLIEAQARQHPERPALVFGEQ 536

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   473 SLDFATLRARSEAVAEALLAAGVRPGQAVAVMTGRNREAIVALLGVMRAAAVYTPVNPEFPAARVERMREAGGIVFALAD 552
Cdd:PRK12467  537 VLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQ 616

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   553 AECAGRAR--EAFAGACLDLSTLPLAGSGMSLPAP--GGRDAAYMIFTSGTSGQPKGVVVEHASALNLSQALARtvyANV 628
Cdd:PRK12467  617 SHLLAQLPvpAGLRSLCLDEPADLLCGYSGHNPEValDPDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAE---RLQ 693

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   629 VGEGLRVTVNAPFSFDSSIKQIL-QLLSGHCLVLVPQEVRSDPQRMLGFLEERRIDVLDCTPSLFRLLLQAGLDdAHPAL 707
Cdd:PRK12467  694 LAADDSMLMVSTFAFDLGVTELFgALASGATLHLLPPDCARDAEAFAALMADQGVTVLKIVPSHLQALLQASRV-ALPRP 772

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   708 PGRILVGGERFdeaSWEVAAGWRR----CQVFNLYGPTEATVNASLARVAEHARPT----IGRALANVDLHVVDGLGRRK 779
Cdd:PRK12467  773 QRALVCGGEAL---QVDLLARVRAlgpgARLINHYGPTETTVGVSTYELSDEERDFgnvpIGQPLANLGLYILDHYLNPV 849

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   780 TRGASGELWIGGAGVARGYAGDAGEAAGRFVEEGW-PGSGRLYRSGDLVRWRADGCLEFLGRIDEQVKINGYRIELGEIR 858
Cdd:PRK12467  850 PVGVVGELYIGGAGLARGYHRRPALTAERFVPDPFgADGGRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIE 929

                         490       500       510
                  ....*....|....*....|....*....|....*...
gi 15597498   859 SALLEHPAVGEAAVLtdeadaAEPG-ADRRIVAFVTAA 895
Cdd:PRK12467  930 ARLLAQPGVREAVVL------AQPGdAGLQLVAYLVPA 961
AMP-binding pfam00501
AMP-binding enzyme;
454-847 4.85e-76

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 259.55  E-value: 4.85e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498    454 FDLRAALQPQAPALL-DAHGSLDFATLRARSEAVAEALLAAGVRPGQAVAVMTGRNREAIVALLGVMRAAAVYTPVNPEF 532
Cdd:pfam00501    1 LERQAARTPDKTALEvGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498    533 PAARVERMREAGGIVFALADAEC-AGRAREAFA------------------GACLDLSTLPLAGSGMSLPAPGGRDAAYM 593
Cdd:pfam00501   81 PAEELAYILEDSGAKVLITDDALkLEELLEALGklevvklvlvldrdpvlkEEPLPEEAKPADVPPPPPPPPDPDDLAYI 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498    594 IFTSGTSGQPKGVVVEHASALNLSQALAR-TVYANVVGEGLRVTVNAPFSFDSSIK--QILQLLSGHCLVLVPQEVRSDP 670
Cdd:pfam00501  161 IYTSGTTGKPKGVMLTHRNLVANVLSIKRvRPRGFGLGPDDRVLSTLPLFHDFGLSlgLLGPLLAGATVVLPPGFPALDP 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498    671 QRMLGFLEERRIDVLDCTPSLFRLLLQAGlDDAHPALPG--RILVGGERFDEASWEVAAGWRRCQVFNLYGPTEATVNAS 748
Cdd:pfam00501  241 AALLELIERYKVTVLYGVPTLLNMLLEAG-APKRALLSSlrLVLSGGAPLPPELARRFRELFGGALVNGYGLTETTGVVT 319

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498    749 LAR---VAEHARPTIGRALANVDLHVVD-GLGRRKTRGASGELWIGGAGVARGYAGDAGEAAGRFVEEGWpgsgrlYRSG 824
Cdd:pfam00501  320 TPLpldEDLRSLGSVGRPLPGTEVKIVDdETGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDEDGW------YRTG 393

                          410       420
                   ....*....|....*....|...
gi 15597498    825 DLVRWRADGCLEFLGRIDEQVKI 847
Cdd:pfam00501  394 DLGRRDEDGYLEIVGRKKDQIKL 416
GrsT COG3208
Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and ...
 1880-2114 1.90e-74

Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442441 [Multi-domain]  Cd Length: 237  Bit Score: 247.84  E-value: 1.90e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1880 SAQPRLRLIALPPAGGNAGTFRGWDARLPADVELLAIQYPGRQERQDEPFVTDVEAMLCAIDDALLPLLDRPFALIGASL 1959
Cdd:COG3208    2 RPDARLRLFCFPYAGGSASAYRPWAAALPPDIEVLAVQLPGRGDRLGEPPLTSLEELADDLAEELAPLLDRPFALFGHSM 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1960 GGMLAYELAARLESLHGLRARQLFVISSRAPGPDLEYPRFHAMGDAELLRTLREYDVLPLEVLDDPELREISLATLRADS 2039
Cdd:COG3208   82 GALLAFELARRLERRGRPLPAHLFVSGRRAPHLPRRRRPLHDLSDAELLAELRRLGGTPEEVLADPELLELFLPILRADF 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15597498 2040 RLAADYRYRPREPLAIPITAILGEQDPGVSRVAIDGWRRHASR-YELETLAGGHGLVVTAAEEVCAILRQRLAPDV 2114
Cdd:COG3208  162 RLLETYRYTPGPPLDCPITALGGDDDPLVSPEELAAWREHTTGpFRLRVFPGGHFFLRDHPAELLALIRAALAALA 237
MenE/FadK COG0318
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ...
 450-901 2.77e-69

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: 241.25  E-value: 2.77e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  450 LVAAFDLRAALQPQAPALLDAHGSLDFATLRARSEAVAEALLAAGVRPGQAVAVMTGRNREAIVALLGVMRAAAVYTPVN 529
Cdd:COG0318    1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  530 PEFPAARVERMreaggivfaLADAECAgrareafagACLdlstlplagsgmslpapggrdAAYMIFTSGTSGQPKGVVVE 609
Cdd:COG0318   81 PRLTAEELAYI---------LEDSGAR---------ALV---------------------TALILYTSGTTGRPKGVMLT 121

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  610 HASALNLSQALARTVYanvVGEGLRVTVNAPFSFDSSIKQILQ--LLSGHCLVLVPqevRSDPQRMLGFLEERRIDVLDC 687
Cdd:COG0318  122 HRNLLANAAAIAAALG---LTPGDVVLVALPLFHVFGLTVGLLapLLAGATLVLLP---RFDPERVLELIERERVTVLFG 195

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  688 TPSLFRLLLQAgLDDAHPALPG--RILVGGERFDEASWEVAAGWRRCQVFNLYGPTEATVNASLARVAEHARP--TIGRA 763
Cdd:COG0318  196 VPTMLARLLRH-PEFARYDLSSlrLVVSGGAPLPPELLERFEERFGVRIVEGYGLTETSPVVTVNPEDPGERRpgSVGRP 274

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  764 LANVDLHVVDGLGRRKTRGASGELWIGGAGVARGYAGDAGEAAGRFvEEGWpgsgrlYRSGDLVRWRADGCLEFLGRIDE 843
Cdd:COG0318  275 LPGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAF-RDGW------LRTGDLGRLDEDGYLYIVGRKKD 347

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15597498  844 QVKINGYRIELGEIRSALLEHPAVGEAAVltdeADAAEPGADRRIVAFVTA---AEETADE 901
Cdd:COG0318  348 MIISGGENVYPAEVEEVLAAHPGVAEAAV----VGVPDEKWGERVVAFVVLrpgAELDAEE 404
Condensation pfam00668
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ...
 1359-1779 2.20e-51

Condensation domain; This domain is found in many multi-domain enzymes which synthesize peptide antibiotics. This domain catalyzes a condensation reaction to form peptide bonds in non- ribosomal peptide biosynthesis. It is usually found to the carboxy side of a phosphopantetheine binding domain (pfam00550). It has been shown that mutations in the HHXXXDG motif abolish activity suggesting this is part of the active site.


Pssm-ID: 395541 [Multi-domain]  Cd Length: 454  Bit Score: 189.08  E-value: 2.20e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   1359 DAYPMTSLQQGMLLQSEASGDPRLLHNVVLHEVHGRLDGELLARAWAILIGRHAILRTGFDLHGGQVPLQWVHPAtaVAA 1438
Cdd:pfam00668    3 DEYPLSPAQKRMWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIRQENGEPVQVILEE--RPF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   1439 EVPVHDLCGLDGETRRLRLRAWIEEEQATPFDWSRPPLVRLAALALDERRFALGVAEHHSVLDGWSLQSLVDELLAVYAD 1518
Cdd:pfam00668   81 ELEIIDISDLSESEEEEAIEAFIQRDLQSPFDLEKGPLFRAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLYQQ 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   1519 LLAGvvaREAEAPAV-GFRDYVALER---EAEANAASALFWLDYLAG-ARYRPLPGLAEEGP-RRMAA--VRVDVPADSL 1590
Cdd:pfam00668  161 LLKG---EPLPLPPKtPYKDYAEWLQqylQSEDYQKDAAYWLEQLEGeLPVLQLPKDYARPAdRSFKGdrLSFTLDEDTE 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   1591 SRLRALAERSGLPLRSLLLAAHGRALCRFSDADEVVTGFVSHGRPeEPGADRLLGLFLNTLPCRL--SASVDLLDSARRA 1668
Cdd:pfam00668  238 ELLRKLAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRP-SPDIERMVGMFVNTLPLRIdpKGGKTFSELIKRV 316

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   1669 FDYERASLEHRRHPLAAIRRR-------NRELRLDSLFNF---------VDFHQDDAAPAGVRhggildqvvvdVDVPLA 1732
Cdd:pfam00668  317 QEDLLSAEPHQGYPFGDLVNDlrlprdlSRHPLFDPMFSFqnylgqdsqEEEFQLSELDLSVS-----------SVIEEE 385

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|...
gi 15597498   1733 VDFEVA------GERLEVGFQYAAGRFPAERAEALAGAYREALLALLGDPVQP 1779
Cdd:pfam00668  386 AKYDLSltaserGGGLTIKIDYNTSLFDEETIERFAEHFKELLEQAIAHPSQP 438
PRK12467 PRK12467
peptide synthase; Provisional
 1199-1825 6.34e-51

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 200.39  E-value: 6.34e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1199 ALRGFLEARLPAYMLPSRIARVERLPLTAEGKLDRRALLAALAAEAAAQTLEaPANATEAALLEIWKSVLKRPAIGVSDN 1278
Cdd:PRK12467  975 ELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKALPKPDASAVQATFVA-PQTELEKRLAAIWADVLKVERVGLTDN 1053

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1279 FFQVGGDSirLIQMQVMAR---EAGLAFTLRDVFNHQSIRELARLLAaPASPADALGTSAPQSLEPFALLSAAERKRLPE 1355
Cdd:PRK12467 1054 FFELGGHS--LLATQVISRvrqRLGIQVPLRTLFEHQTLAGFAQAVA-AQQQGAQPALPDVDRDQPLPLSYAQERQWFLW 1130

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1356 GLDDaypmtslqqgmllQSEASGDPRLLhnvvlhEVHGRLDGELLARAWAILIGRHAILRTGFDLHGGQvPLQWVHPATA 1435
Cdd:PRK12467 1131 QLEP-------------GSAAYHIPQAL------RLKGPLDIEALERSFDALVARHESLRTTFVQEDGR-TRQVIHPVGS 1190

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1436 VAAEVPVHDLCGLDGEtrrlRLRAWIEEEQATPFDWSRPPLVRLAALALDERRFALGVAEHHSVLDGWSLQSLVDELLAV 1515
Cdd:PRK12467 1191 LTLEEPLLLAADKDEA----QLKVYVEAEARQPFDLEQGPLLRVGLLRLAADEHVLVLTLHHIVSDGWSMQVLVDELVAL 1266

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1516 YADLLAGVVAREAEAPaVGFRDYVALEREAEANAASA---LFWLDYLAGAryRPLPGLAEEGPR------RMAAVRVDVP 1586
Cdd:PRK12467 1267 YAAYSQGQSLQLPALP-IQYADYAVWQRQWMDAGERArqlAYWKAQLGGE--QPVLELPTDRPRpavqshRGARLAFELP 1343

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1587 ADSLSRLRALAERSGLPLRSLLLAAHGRALCRFSDADEVVTGFVSHGRPEEPgADRLLGLFLNTLPcrLSASVDLLDSAR 1666
Cdd:PRK12467 1344 PALAEGLRALARREGVTLFMLLLASFQTLLHRYSGQDDIRVGVPIANRNRAE-TEGLIGFFVNTQV--LRAEVDGQASFQ 1420

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1667 RAF-DYERASLEHRRH------PLAAIRRRNRELRLDSLFNFV-----DFHQDDAAPAGVRHGGILDQVVVDVDVPLAVD 1734
Cdd:PRK12467 1421 QLLqQVKQAALEAQAHqdlpfeQLVEALQPERSLSHSPLFQVMfnhqrDDHQAQAQLPGLSVESLSWESQTAQFDLTLDT 1500

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1735 FEvAGERLEVGFQYAAGRFPAERAEALAGAYREALLALLGDPVQPPAAAQAEDSVELRRVLKVLSrvlgrplAADQGFAS 1814
Cdd:PRK12467 1501 YE-SSEGLQASLTYATDLFEASTIERLAGHWLNLLQGLVADPERRLGELDLLDEAERRQILEGWN-------ATHTGYPL 1572

                         650
                  ....*....|..
gi 15597498  1815 AGG-HSLLGVQA 1825
Cdd:PRK12467 1573 ARLvHQLIEDQA 1584
COG4908 COG4908
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ...
 1363-1601 6.60e-41

Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];


Pssm-ID: 443936 [Multi-domain]  Cd Length: 243  Bit Score: 152.11  E-value: 6.60e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1363 MTSLQQGMLlqsEASGDPRLLHNVVLHEVHGRLDGELLARAWAILIGRHAILRTGFDLHGGQvPLQWVHPAtaVAAEVPV 1442
Cdd:COG4908    1 LSPAQKRFL---FLEPGSNAYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFVEEDGE-PVQRIDPD--ADLPLEV 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1443 HDLCGLDGETRRLRLRAWIEEEQATPFDWSRPPLVRLAALALDERRFALGVAEHHSVLDGWSLQSLVDELLAVYADLLAG 1522
Cdd:COG4908   75 VDLSALPEPEREAELEELVAEEASRPFDLARGPLLRAALIRLGEDEHVLLLTIHHIISDGWSLGILLRELAALYAALLEG 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1523 VVAREAEAPaVGFRDYVALEREA---EANAASALFWLDYLAGA-RYRPLPGLAEEGPRRM---AAVRVDVPADSLSRLRA 1595
Cdd:COG4908  155 EPPPLPELP-IQYADYAAWQRAWlqsEALEKQLEYWRQQLAGApPVLELPTDRPRPAVQTfrgATLSFTLPAELTEALKA 233


                 ....*.
gi 15597498 1596 LAERSG 1601
Cdd:COG4908  234 LAKAHG 239
Thioesterase pfam00975
Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of ...
 1886-2110 4.32e-31

Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of peptide antibiotics. Next to the operons encoding these enzymes, in almost all cases, are genes that encode proteins that have similarity to the type II fatty acid thioesterases of vertebrates. There are also modules within the peptide synthetases that also share this similarity. With respect to antibiotic production, thioesterases are required for the addition of the last amino acid to the peptide antibiotic, thereby forming a cyclic antibiotic. Thioesterases (non-integrated) have molecular masses of 25-29 kDa.


Pssm-ID: 395776 [Multi-domain]  Cd Length: 223  Bit Score: 122.88  E-value: 4.32e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   1886 RLIALPPAGGNAGTFRGWDARLPADVELLAIQYPGRQErqDEPFVTDVEAMLCAIDDALLPLLDR-PFALIGASLGGMLA 1964
Cdd:pfam00975    2 PLFCFPPAGGSASSFRSLARRLPPPAEVLAVQYPGRGR--GEPPLNSIEALADEYAEALRQIQPEgPYALFGHSMGGMLA 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   1965 YELAARLESLhGLRARQLFVISSRAPGPDlEYPRFHAMGDAELLRTLREYDVLPLEVLDDPELREISLATLRADSRLAAD 2044
Cdd:pfam00975   80 FEVARRLERQ-GEAVRSLFLSDASAPHTV-RYEASRAPDDDEVVAEFTDEGGTPEELLEDEELLSMLLPALRADYRALES 157

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15597498   2045 YRYRPREplAIPITAILGEQDPGVSRVAIDGWRRHASRYE--LETLAGGHGLVVTAAEEVCAILRQRL 2110
Cdd:pfam00975  158 YSCPPLD--AQSATLFYGSDDPLHDADDLAEWVRDHTPGEfdVHVFDGDHFYLIEHLEAVLEIIEAKL 223
fkbM_fam TIGR01444
methyltransferase, FkbM family; Members of this family are characterized by two well-conserved ...
 947-1122 1.42e-29

methyltransferase, FkbM family; Members of this family are characterized by two well-conserved short regions separated by a variable in both sequence and length. The first of the two regions is found in a large number of proteins outside this subfamily, a number of which have been characterized as methyltransferases. One member of the present family, FkbM, was shown to be required for a specific methylation in the biosynthesis of the immunosuppressant FK506 in Streptomyces strain MA6548.


Pssm-ID: 273628  Cd Length: 143  Bit Score: 115.87  E-value: 1.42e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498    947 VVLDVGANIGLFSLYIASRAPRARVVAFEPLAPIRRRLEANLGRYA-PQVEVFGIGLSDAEREETFTYYPGYSTFSGIAE 1025
Cdd:TIGR01444    1 VVIDVGANIGDTSLYFARKGAEGRVIAFEPLPDAYEILEENVKLNNlPNVVLLNAAVGDRDGELEFNVSDDDTGNSSLLP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   1026 YADASGERDVirrylsnqgeegganllldnideilddrlraeahRCRLRRLDQVIGELGLERIDLLKIDVQRAEMDVLLG 1105
Cdd:TIGR01444   81 TPDADRESEI----------------------------------EVEVVTLDDLVEEFGLDKVDLLKIDVEGAELEVLRG 126

                          170
                   ....*....|....*..
gi 15597498   1106 LDDAALAKVRQIVLEVH 1122
Cdd:TIGR01444  127 AAETLLEKRPVIVLEVH 143
PRK12467 PRK12467
peptide synthase; Provisional
 1198-1372 5.54e-21

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 101.39  E-value: 5.54e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1198 QALRGFLEARLPAYMLPSRIARVERLPLTAEGKLDRRALLAALAAEAAAQTLeaPANATEAALLEIWKSVLKRPAIGVSD 1277
Cdd:PRK12467 3550 ETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDRKALPDPDAKGSREYVA--PRSEVEQQLAAIWADVLGVEQVGVTD 3627

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1278 NFFQVGGDSIRLIQMQVMAREA-GLAFTLRDVFNHQSIRELA------RLLAAPASPADALGTSAPQSLEPFALL-SAAE 1349
Cdd:PRK12467 3628 NFFELGGDSLLALQVLSRIRQSlGLKLSLRDLMSAPTIAELAgysplgDVPVNLLLDLNRLETGFPALFCRHEGLgTVFD 3707

                         170       180
                  ....*....|....*....|...
gi 15597498  1350 RKRLPEGLDDAYPMTSLQQGMLL 1372
Cdd:PRK12467 3708 YEPLAVILEGDRHVLGLTCRHLL 3730
Methyltransf_21 pfam05050
Methyltransferase FkbM domain; This family has members from bacteria to human, and appears to ...
 950-1147 5.48e-16

Methyltransferase FkbM domain; This family has members from bacteria to human, and appears to be a methyltransferase.


Pssm-ID: 428282  Cd Length: 170  Bit Score: 77.61  E-value: 5.48e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498    950 DVGANIGLFSLYIAS----RAPRARVVAFEPLAPIRRRLEANLGRYApqvevfgigLSDAEREETFtyYPGYSTFSGIAE 1025
Cdd:pfam05050    1 DVGANDGVWDSVALLfekkCGGGGEVLAIEPNPNKLEKLDCTLLNLA---------LGNDVGLYEF--YLGGKGGGGYLL 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   1026 YADasgerdvirryLSNQGEEGGANLLLDNIDEIlddrlraeahRCRLRRLDQVIGELGLERIDLLKIDVQRAEMDVLLG 1105
Cdd:pfam05050   70 FAV-----------GDPQGASTSSVLGGEEAKYI----------EVETVTLDSFLEEIKKSDIDLLKIDVEGAELEVLEG 128

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 15597498   1106 lDDAALAKVR--QIVLEVHdKRDGATAGRADALSDLLRRHGFEV 1147
Cdd:pfam05050  129 -AEKTLKRCQpnIIVIEVH-FFHYFGGPLFDEIRQFLRECGYRL 170
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
1793-1971 1.37e-10

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 66.99  E-value: 1.37e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1793 RVLKVLSRVLGR-PLAADQGFASAGGHSLLGVQAIAELRRLTGRQLSLGLLQGDPDAREVVRRCHAADAPPLPPATERAR 1871
Cdd:PRK10252  982 IIAAAFSSLLGCdVVDADADFFALGGHSLLAMKLAAQLSRQFARQVTPGQVMVASTVAKLATLLDAEEDESRRLGFGTIL 1061

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1872 ALwlqRSGSAQPrlrLIALPPAGGNAGTFRGWDARLPADVELLAIQYPGRQERQDEPfvTDVEAMlcaIDDALLPLLDR- 1950
Cdd:PRK10252 1062 PL---REGDGPT---LFCFHPASGFAWQFSVLSRYLDPQWSIYGIQSPRPDGPMQTA--TSLDEV---CEAHLATLLEQq 1130

                         170       180
                  ....*....|....*....|....
gi 15597498  1951 ---PFALIGASLGGMLAYELAARL 1971
Cdd:PRK10252 1131 phgPYHLLGYSLGGTLAQGIAARL 1154
A_NRPS cd05930
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ...
 1192-1234 3.76e-10

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: 64.47  E-value: 3.76e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 15597498 1192 GGELSEQALRGFLEARLPAYMLPSRIARVERLPLTAEGKLDRR 1234
Cdd:cd05930  400 GGELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRK 442
alpha_am_amid TIGR03443
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ...
 1200-1362 1.67e-09

L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.


Pssm-ID: 274582 [Multi-domain]  Cd Length: 1389  Bit Score: 63.55  E-value: 1.67e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   1200 LRGFLEARLPAYMLPSRIARVERLPLTAEGKLDR-------RALLAALAAEAAAQTLEAPANATEAALLEIWKSVL-KRP 1271
Cdd:TIGR03443  786 IREYLKKKLPSYAIPTVIVPLKKLPLNPNGKVDKpalpfpdTAQLAAVAKNRSASAADEEFTETEREIRDLWLELLpNRP 865

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   1272 A-IGVSDNFFQVGGDSIRLIQMqvmareaglAFTLRD----------VFNHQSIRELAR---LLAAPASPADALGTSAPQ 1337
Cdd:TIGR03443  866 AtISPDDSFFDLGGHSILATRM---------IFELRKklnvelplglIFKSPTIKGFAKevdRLKKGEELADEGDSEIEE 936

                          170       180
                   ....*....|....*....|....*
gi 15597498   1338 SLEPFALLSAAERKRLPEGLDDAYP 1362
Cdd:TIGR03443  937 EETVLELDYAKDAKTLVDSLPKSYP 961
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
 1258-1316 2.61e-09

Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.


Pssm-ID: 425746 [Multi-domain]  Cd Length: 62  Bit Score: 54.88  E-value: 2.61e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15597498   1258 AALLEIWKSVLKRPA--IGVSDNFFQVGGDSIRLIQMQVMAREA-GLAFTLRDVFNHQSIRE 1316
Cdd:pfam00550    1 ERLRELLAEVLGVPAeeIDPDTDLFDLGLDSLLAVELIARLEEEfGVEIPPSDLFEHPTLAE 62
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
 1252-1323 5.76e-08

Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440006 [Multi-domain]  Cd Length: 80  Bit Score: 51.78  E-value: 5.76e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15597498 1252 PANATEAALLEIWKSVLKRPA--IGVSDNFFQV-GGDSIRLIQMQVMAREA-GLAFTLRDVFNHQSIRELARLLAA 1323
Cdd:COG0236    2 PREELEERLAEIIAEVLGVDPeeITPDDSFFEDlGLDSLDAVELIAALEEEfGIELPDTELFEYPTVADLADYLEE 77
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
 1792-1850 2.14e-04

Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.


Pssm-ID: 425746 [Multi-domain]  Cd Length: 62  Bit Score: 41.01  E-value: 2.14e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15597498   1792 RRVLKVLSRVLGRP---LAADQGFASAGGHSLLGVQAIAELRRLTGRQLSLGLLQGDPDARE 1850
Cdd:pfam00550    1 ERLRELLAEVLGVPaeeIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLAE 62
PKS_TE smart00824
Thioesterase; Peptide synthetases are involved in the non-ribosomal synthesis of peptide ...
 1926-1991 2.22e-04

Thioesterase; Peptide synthetases are involved in the non-ribosomal synthesis of peptide antibiotics. Next to the operons encoding these enzymes, in almost all cases, are genes that encode proteins that have similarity to the type II fatty acid thioesterases of vertebrates. There are also modules within the peptide synthetases that also share this similarity. With respect to antibiotic production, thioesterases are required for the addition of the last amino acid to the peptide antibiotic, thereby forming a cyclic antibiotic. Thioesterases (non-integrated) have molecular masses of 25-29 kDa.


Pssm-ID: 214835 [Multi-domain]  Cd Length: 212  Bit Score: 44.52  E-value: 2.22e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15597498    1926 DEPFVTDVEAMLCAIDDALLPLL-DRPFALIGASLGGMLAYELAARLESlHGLRARQLFVISSRAPG 1991
Cdd:smart00824   39 GEPLPASADALVEAQAEAVLRAAgGRPFVLVGHSSGGLLAHAVAARLEA-RGIPPAAVVLLDTYPPG 104
 
Name Accession Description Interval E-value
DCL_NRPS-like cd19536
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ...
 1360-1776 1.25e-139

DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal fungal CT domains and Dual Epimerization/Condensation (E/C) domains; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type [D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L))], which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380459 [Multi-domain]  Cd Length: 419  Bit Score: 442.27  E-value: 1.25e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1360 AYPMTSLQQGMLLQSEAS-GDPRLLHNVVLHeVHGRLDGELLARAWAILIGRHAILRTGFDLHGGQVPLQWVHPatAVAA 1438
Cdd:cd19536    1 MYPLSSLQEGMLFHSLLNpGGSVYLHNYTYT-VGRRLNLDLLLEALQVLIDRHDILRTSFIEDGLGQPVQVVHR--QAQV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1439 EVPVHDLCGldGETRRLRLRAWIEEEQATPFDWSRPPLVRLAALALDER-RFALGVAEHHSVLDGWSLQSLVDELLAVYA 1517
Cdd:cd19536   78 PVTELDLTP--LEEQLDPLRAYKEETKIRRFDLGRAPLVRAALVRKDEReRFLLVISDHHSILDGWSLYLLVKEILAVYN 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1518 DLLAGvvAREAEAPAVGFRDYVALEREAEANAASALFWLDYLAGARYRPLPGLAE---EGPRRMAAVRVDVPADSLSrlR 1594
Cdd:cd19536  156 QLLEY--KPLSLPPAQPYRDFVAHERASIQQAASERYWREYLAGATLATLPALSEavgGGPEQDSELLVSVPLPVRS--R 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1595 ALAERSGLPLRSLLLAAHGRALCRFSDADEVVTGFVSHGRPEE-PGADRLLGLFLNTLPCRLSASV-DLLDSARRAFDYE 1672
Cdd:cd19536  232 SLAKRSGIPLSTLLLAAWALVLSRHSGSDDVVFGTVVHGRSEEtTGAERLLGLFLNTLPLRVTLSEeTVEDLLKRAQEQE 311

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1673 RASLEHRRHPLAAIRRRNR-ELRLDSLFNFVDFHQDDAAPA-----GVRHGGILDQVVVDVDVPLAVDFEvaGERLEVGF 1746
Cdd:cd19536  312 LESLSHEQVPLADIQRCSEgEPLFDSIVNFRHFDLDFGLPEwgsdeGMRRGLLFSEFKSNYDVNLSVLPK--QDRLELKL 389

                        410       420       430
                 ....*....|....*....|....*....|
gi 15597498 1747 QYAAGRFPAERAEALAGAYREALLALLGDP 1776
Cdd:cd19536  390 AYNSQVLDEEQAQRLAAYYKSAIAELATAP 419
A_NRPS cd05930
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ...
 462-910 6.38e-135

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: 430.03  E-value: 6.38e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  462 PQAPALLDAHGSLDFATLRARSEAVAEALLAAGVRPGQAVAVMTGRNREAIVALLGVMRAAAVYTPVNPEFPAARVERMR 541
Cdd:cd05930    1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  542 EAGGIVFALADAEcagrareafagacldlstlplagsgmslpapggrDAAYMIFTSGTSGQPKGVVVEHASALNLSQALA 621
Cdd:cd05930   81 EDSGAKLVLTDPD----------------------------------DLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQ 126

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  622 RTVYanvVGEGLRVTVNAPFSFDSSIKQIL-QLLSGHCLVLVPQEVRSDPQRMLGFLEERRIDVLDCTPSLFRLLLQAGL 700
Cdd:cd05930  127 EAYP---LTPGDRVLQFTSFSFDVSVWEIFgALLAGATLVVLPEEVRKDPEALADLLAEEGITVLHLTPSLLRLLLQELE 203

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  701 DDAHPALpGRILVGGERFdeaSWEVAAGWR----RCQVFNLYGPTEATVNASLARVAEH----ARPTIGRALANVDLHVV 772
Cdd:cd05930  204 LAALPSL-RLVLVGGEAL---PPDLVRRWRellpGARLVNLYGPTEATVDATYYRVPPDdeedGRVPIGRPIPNTRVYVL 279

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  773 DGLGRRKTRGASGELWIGGAGVARGYAGDAGEAAGRFVEEGWPGSGRLYRSGDLVRWRADGCLEFLGRIDEQVKINGYRI 852
Cdd:cd05930  280 DENLRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNPFGPGERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRI 359

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15597498  853 ELGEIRSALLEHPAVGEAAVLTDEADAAEPgadrRIVAFVTAAEETADE-----SWLEVDLPS 910
Cdd:cd05930  360 ELGEIEAALLAHPGVREAAVVAREDGDGEK----RLVAYVVPDEGGELDeeelrAHLAERLPD 418
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
 3-1261 3.07e-127

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: 436.21  E-value: 3.07e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498    3 ASEDLQSAVQPAASEALEGFPLSPLQTRAWRRHAERPENTVVGVRLHAPADPVATLERLRRALDGEAQLRVAYRTMPGMS 82
Cdd:COG1020    2 AAAAAAALPPAAAAAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAGR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   83 LPVQVLDGRAADLLVERLPGDGDWAGRFARESARLAASPLGGEGQPVLALGLLLDAAGETLQGLLLAAPAFVVDAASLVA 162
Cdd:COG1020   82 PVQVIQPVVAAPLPVVVLLVDLEALAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDGL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  163 LLRRGLGPAGQASADEGDE----ALLFQHFSEWANEALAGEDGESASGYWREQAAVAAESPLALADDLGEGEWTAR---- 234
Cdd:COG1020  162 LLAELLRLYLAAYAGAPLPlpplPIQYADYALWQREWLQGEELARQLAYWRQQLAGLPPLLELPTDRPRPAVQSYRgarv 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  235 -RLLPRALLERLAA----NGLPEAAALL-AWTQVAGQFQGDE----GLPlemarlVSGRLFNEFAELAGPFAGVAPLCLE 304
Cdd:COG1020  242 sFRLPAELTAALRAlarrHGVTLFMVLLaAFALLLARYSGQDdvvvGTP------VAGRPRPELEGLVGFFVNTLPLRVD 315

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  305 NVRAGSVGERLDALQAAILA------------QEEAAALRDPfaPDWPLAELGFAWLAGELDGAGVAELDCRQPPLGG-- 370
Cdd:COG1020  316 LSGDPSFAELLARVRETLLAayahqdlpferlVEELQPERDL--SRNPLFQVMFVLQNAPADELELPGLTLEPLELDSgt 393

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  371 ---FLELQVLPHGEGRLASLRVRRDH-DGTLAGRLLDAWVECLESIAADRQLPLAGLPLIGAAERERY-QAWQGERVEPA 445
Cdd:COG1020  394 akfDLTLTVVETGDGLRLTLEYNTDLfDAATIERMAGHLVTLLEALAADPDQPLGDLPLLTAAERQQLlAEWNATAAPYP 473

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  446 PVESLVAAFDLRAALQPQAPALLDAHGSLDFATLRARSEAVAEALLAAGVRPGQAVAVMTGRNREAIVALLGVMRAAAVY 525
Cdd:COG1020  474 ADATLHELFEAQAARTPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAY 553

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  526 TPVNPEFPAARVERMREAGGIVFALADAECAGRAREaFAGACLDLSTLPLAGSGMSLPAPGGR--DAAYMIFTSGTSGQP 603
Cdd:COG1020  554 VPLDPAYPAERLAYMLEDAGARLVLTQSALAARLPE-LGVPVLALDALALAAEPATNPPVPVTpdDLAYVIYTSGSTGRP 632

                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  604 KGVVVEHASALNLSQALARTvYAnvVGEGLRVTVNAPFSFDSSIKQIL-QLLSGHCLVLVPQEVRSDPQRMLGFLEERRI 682
Cdd:COG1020  633 KGVMVEHRALVNLLAWMQRR-YG--LGPGDRVLQFASLSFDASVWEIFgALLSGATLVLAPPEARRDPAALAELLARHRV 709

                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  683 DVLDCTPSLFRLLLQAGLDDAHPalPGRILVGGERFDEASWE-VAAGWRRCQVFNLYGPTEATVNASLARV----AEHAR 757
Cdd:COG1020  710 TVLNLTPSLLRALLDAAPEALPS--LRLVLVGGEALPPELVRrWRARLPGARLVNLYGPTETTVDSTYYEVtppdADGGS 787

                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  758 PTIGRALANVDLHVVDGLGRRKTRGASGELWIGGAGVARGYAGDAGEAAGRFVEEGWPGSG-RLYRSGDLVRWRADGCLE 836
Cdd:COG1020  788 VPIGRPIANTRVYVLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPFGFPGaRLYRTGDLARWLPDGNLE 867

                        890       900       910       920       930       940       950       960
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  837 FLGRIDEQVKINGYRIELGEIRSALLEHPAVGEAAVLTDEadaaEPGADRRIVAFVTAAEETADESWLE----------- 905
Cdd:COG1020  868 FLGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVARE----DAPGDKRLVAYVVPEAGAAAAAALLrlalalllppy 943

                        970       980       990      1000      1010      1020      1030      1040
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  906 -----------------VDLPSGHRVAGLNLNETEYVYQEIFVDEVYSRDGIVLPPDAVVLDVGANIGLFSLYIASRAPR 968
Cdd:COG1020  944 mvpaavvlllplpltgnGKLDRLALPAPAAAAAAAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLAL 1023

                       1050      1060      1070      1080      1090      1100      1110      1120
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  969 ARVVAFEPLAPIRRRLEANLGRYAPQVEVFGIGLSDAEREETFTYYPGYSTFSGIAEYADASGERDVIRRYLSNQGEEGG 1048
Cdd:COG1020 1024 ARAARLLLLLLLLLLLFLAAAAAAAAAAAAAAAAAAAAPLAAAAAPLPLPPLLLSLLALLLALLLLLALLALLALLLLLL 1103

                       1130      1140      1150      1160      1170      1180      1190      1200
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1049 ANLLLDNIDEILDDRLRAEAHRCRLRRLDQVIGELGLERIDLLKIDVQRAEMDVLLGLDDAALAKVRQIVLEVHDKRDGA 1128
Cdd:COG1020 1104 LLLLLLALLLLLALLLALLAALRARRAVRQEGPRLRLLVALAAALALAALLALLLAAAAAAAELLAAAALLLLLALLLLA 1183

                       1210      1220      1230      1240      1250      1260      1270      1280
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1129 TAGRADALSDLLRRHGFEVSIRQDALLEGTDRYNCYAVRPGYAESLAERIDWRALAPRPAAALGGELSEQALRGFLEARL 1208
Cdd:COG1020 1184 LLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLAAAAAALLALALLLALLALAALLALAALAALAAALLALA 1263

                       1290      1300      1310      1320      1330
                 ....*....|....*....|....*....|....*....|....*....|...
gi 15597498 1209 PAYMLPSRIARVERLPLTAEGKLDRRALLAALAAEAAAQTLEAPANATEAALL 1261
Cdd:COG1020 1264 LALLALALLLLALALLLPALARARAARTARALALLLLLALLLLLALALALLLL 1316
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
 494-872 2.01e-108

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: 352.72  E-value: 2.01e-108
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498    494 GVRPGQAVAVMTGRNREAIVALLGVMRAAAVYTPVNPEFPAARVERMREAGGIVFALADAECAGRARE-AFAGACLDLST 572
Cdd:TIGR01733   21 GVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDSALASRLAGlVLPVILLDPLE 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498    573 LPLAGSGMSLPAP----GGRDAAYMIFTSGTSGQPKGVVVEHASALNLSQALARtvyANVVGEGLRVTVNAPFSFDSSIK 648
Cdd:TIGR01733  101 LAALDDAPAPPPPdapsGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLAR---RYGLDPDDRVLQFASLSFDASVE 177

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498    649 QIL-QLLSGHCLVLVPQEVRSDPQRMLGFL-EERRIDVLDCTPSLFRLLLQAglddAHPALPG--RILVGGERFDEAswe 724
Cdd:TIGR01733  178 EIFgALLAGATLVVPPEDEERDDAALLAALiAEHPVTVLNLTPSLLALLAAA----LPPALASlrLVILGGEALTPA--- 250

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498    725 VAAGWRR----CQVFNLYGPTEATVNASLARVAEHARP-----TIGRALANVDLHVVDGLGRRKTRGASGELWIGGAGVA 795
Cdd:TIGR01733  251 LVDRWRArgpgARLINLYGPTETTVWSTATLVDPDDAPrespvPIGRPLANTRLYVLDDDLRPVPVGVVGELYIGGPGVA 330

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15597498    796 RGYAGDAGEAAGRFVEEGWPGS--GRLYRSGDLVRWRADGCLEFLGRIDEQVKINGYRIELGEIRSALLEHPAVGEAAV 872
Cdd:TIGR01733  331 RGYLNRPELTAERFVPDPFAGGdgARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
A_NRPS_Bac cd17655
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ...
 454-910 2.22e-102

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: 338.53  E-value: 2.22e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  454 FDLRAALQPQAPALLDAHGSLDFATLRARSEAVAEALLAAGVRPGQAVAVMTGRNREAIVALLGVMRAAAVYTPVNPEFP 533
Cdd:cd17655    3 FEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  534 AARVERMREAGGIVFALADAECAgrAREAFAGACLDLSTLPL-AGSGMSLPAPG-GRDAAYMIFTSGTSGQPKGVVVEHA 611
Cdd:cd17655   83 EERIQYILEDSGADILLTQSHLQ--PPIAFIGLIDLLDEDTIyHEESENLEPVSkSDDLAYVIYTSGSTGKPKGVMIEHR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  612 SALNLSQALARTVYanvVGEGLRVTVNAPFSFDSSIKQILQ-LLSGHCLVLVPQEVRSDPQRMLGFLEERRIDVLDCTPS 690
Cdd:cd17655  161 GVVNLVEWANKVIY---QGEHLRVALFASISFDASVTEIFAsLLSGNTLYIVRKETVLDGQALTQYIRQNRITIIDLTPA 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  691 LFRLLLQAGLDDAHPALpgRILVGGErfdEASWEVAAGW-----RRCQVFNLYGPTEATVNASL----ARVAEHARPTIG 761
Cdd:cd17655  238 HLKLLDAADDSEGLSLK--HLIVGGE---ALSTELAKKIielfgTNPTITNAYGPTETTVDASIyqyePETDQQVSVPIG 312

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  762 RALANVDLHVVDGLGRRKTRGASGELWIGGAGVARGYAGDAGEAAGRFVEEGWPGSGRLYRSGDLVRWRADGCLEFLGRI 841
Cdd:cd17655  313 KPLGNTRIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFVPGERMYRTGDLARWLPDGNIEFLGRI 392

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15597498  842 DEQVKINGYRIELGEIRSALLEHPAVGEAAVLTDEADAAEPgadrRIVAFVTAAEETADE---SWLEVDLPS 910
Cdd:cd17655  393 DHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQN----YLCAYIVSEKELPVAqlrEFLARELPD 460
A_NRPS_Ta1_like cd12116
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ...
 462-899 3.16e-101

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: 334.26  E-value: 3.16e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  462 PQAPALLDAHGSLDFATLRARSEAVAEALLAAGVRPGQAVAVMTGRNREAIVALLGVMRAAAVYTPVNPEFPAARVERMR 541
Cdd:cd12116    1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  542 EAGGIVFALADAECAGRAREAFAGACLDLSTLPLAGSGmSLPAPGGRDAAYMIFTSGTSGQPKGVVVEHASALNLSQALA 621
Cdd:cd12116   81 EDAEPALVLTDDALPDRLPAGLPVLLLALAAAAAAPAA-PRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSMR 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  622 RTVyanVVGEGLRVTVNAPFSFDSSIKQIL-QLLSGHCLVLVPQEVRSDPQRMLGFLEERRIDVLDCTPSLFRLLLQAGL 700
Cdd:cd12116  160 ERL---GLGPGDRLLAVTTYAFDISLLELLlPLLAGARVVIAPRETQRDPEALARLIEAHSITVMQATPATWRMLLDAGW 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  701 DDAHPAlpgRILVGGERFDEaswEVAAGW--RRCQVFNLYGPTEATVNASLARVAEHARP-TIGRALANVDLHVVDGLGR 777
Cdd:cd12116  237 QGRAGL---TALCGGEALPP---DLAARLlsRVGSLWNLYGPTETTIWSTAARVTAAAGPiPIGRPLANTQVYVLDAALR 310

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  778 RKTRGASGELWIGGAGVARGYAGDAGEAAGRFVEEGWPGSG-RLYRSGDLVRWRADGCLEFLGRIDEQVKINGYRIELGE 856
Cdd:cd12116  311 PVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPFAGPGsRLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGE 390

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|...
gi 15597498  857 IRSALLEHPAVGEAAVLTDeadaaEPGADRRIVAFVTAAEETA 899
Cdd:cd12116  391 IEAALAAHPGVAQAAVVVR-----EDGGDRRLVAYVVLKAGAA 428
A_NRPS_Srf_like cd12117
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ...
 452-909 1.32e-99

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: 330.32  E-value: 1.32e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  452 AAFDLRAALQPQAPALLDAHGSLDFATLRARSEAVAEALLAAGVRPGQAVAVMTGRNREAIVALLGVMRAAAVYTPVNPE 531
Cdd:cd12117    1 ELFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  532 FPAARVERMREAGGIVFALADAECAGRAREafaGACLDLSTLPLAGSGMSLPAPGGR--DAAYMIFTSGTSGQPKGVVVE 609
Cdd:cd12117   81 LPAERLAFMLADAGAKVLLTDRSLAGRAGG---LEVAVVIDEALDAGPAGNPAVPVSpdDLAYVMYTSGSTGRPKGVAVT 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  610 HASALnlsqALARTVYANVVGEGLRVTVNAPFSFDSSIKQIL-QLLSGHCLVLVPQEVRSDPQRMLGFLEERRIDVLDCT 688
Cdd:cd12117  158 HRGVV----RLVKNTNYVTLGPDDRVLQTSPLAFDASTFEIWgALLNGARLVLAPKGTLLDPDALGALIAEEGVTVLWLT 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  689 PSLFRLLLQAGLDdahpALPG--RILVGGERFDEASweVAAGWRRC---QVFNLYGPTEATVNASLARVAEHARPT---- 759
Cdd:cd12117  234 AALFNQLADEDPE----CFAGlrELLTGGEVVSPPH--VRRVLAACpglRLVNGYGPTENTTFTTSHVVTELDEVAgsip 307

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  760 IGRALANVDLHVVDGLGRRKTRGASGELWIGGAGVARGYAGDAGEAAGRFVEEGWPGSGRLYRSGDLVRWRADGCLEFLG 839
Cdd:cd12117  308 IGRPIANTRVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPFGPGERLYRTGDLARWLPDGRLEFLG 387

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15597498  840 RIDEQVKINGYRIELGEIRSALLEHPAVGEAAVLTDEADaaepGADRRIVAFVTAAEETADE---SWLEVDLP 909
Cdd:cd12117  388 RIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDA----GGDKRLVAYVVAEGALDAAelrAFLRERLP 456
A_NRPS_VisG_like cd17651
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ...
 454-900 3.62e-98

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: 326.22  E-value: 3.62e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  454 FDLRAALQPQAPALLDAHGSLDFATLRARSEAVAEALLAAGVRPGQAVAVMTGRNREAIVALLGVMRAAAVYTPVNPEFP 533
Cdd:cd17651    1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  534 AARVERMREAGGIVFALADAECAGR-AREAFAGACLDLSTLPLAGSGMSLPAPGGRDAAYMIFTSGTSGQPKGVVVEHAS 612
Cdd:cd17651   81 AERLAFMLADAGPVLVLTHPALAGElAVELVAVTLLDQPGAAAGADAEPDPALDADDLAYVIYTSGSTGRPKGVVMPHRS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  613 ALNLSQALARtvyANVVGEGLRVTVNAPFSFDSSIKQILQ-LLSGHCLVLVPQEVRSDPQRMLGFLEERRIDVLDCTPSL 691
Cdd:cd17651  161 LANLVAWQAR---ASSLGPGARTLQFAGLGFDVSVQEIFStLCAGATLVLPPEEVRTDPPALAAWLDEQRISRVFLPTVA 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  692 FRLLLQAGldDAHPALPGR---ILVGGERF--DEASWEVAAGWRRCQVFNLYGPTEATVNASL---ARVAEH-ARPTIGR 762
Cdd:cd17651  238 LRALAEHG--RPLGVRLAAlryLLTGGEQLvlTEDLREFCAGLPGLRLHNHYGPTETHVVTALslpGDPAAWpAPPPIGR 315

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  763 ALANVDLHVVDGLGRRKTRGASGELWIGGAGVARGYAGDAGEAAGRFVEEGWPGSGRLYRSGDLVRWRADGCLEFLGRID 842
Cdd:cd17651  316 PIDNTRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFVPGARMYRTGDLARWLPDGELEFLGRAD 395

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 15597498  843 EQVKINGYRIELGEIRSALLEHPAVGEAAVLTDEadaaEPGADRRIVAFVTAAEETAD 900
Cdd:cd17651  396 DQVKIRGFRIELGEIEAALARHPGVREAVVLARE----DRPGEKRLVAYVVGDPEAPV 449
A_NRPS_AB3403-like cd17646
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ...
 451-902 6.02e-95

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: 316.91  E-value: 6.02e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  451 VAAFDLRAALQPQAPALLDAHGSLDFATLRARSEAVAEALLAAGVRPGQAVAVMTGRNREAIVALLGVMRAAAVYTPVNP 530
Cdd:cd17646    1 HALVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  531 EFPAARVERMREAGGIVFALADAECAGRAREAFAGACLDLSTLPLAGSGMSLPAPGGRDAAYMIFTSGTSGQPKGVVVEH 610
Cdd:cd17646   81 GYPADRLAYMLADAGPAVVLTTADLAARLPAGGDVALLGDEALAAPPATPPLVPPRPDNLAYVIYTSGSTGRPKGVMVTH 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  611 ASALNlsqALARTVYANVVGEGLRVTVNAPFSFDSSIKQIL-QLLSGHCLVLVPQEVRSDPQRMLGFLEERRIDVLDCTP 689
Cdd:cd17646  161 AGIVN---RLLWMQDEYPLGPGDRVLQKTPLSFDVSVWELFwPLVAGARLVVARPGGHRDPAYLAALIREHGVTTCHFVP 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  690 SLFRLLLQAGLDDAHPALPgRILVGGErfdEASWEVAAGWRR---CQVFNLYGPTEATVNASLARVAEHARPT---IGRA 763
Cdd:cd17646  238 SMLRVFLAEPAAGSCASLR-RVFCSGE---ALPPELAARFLAlpgAELHNLYGPTEAAIDVTHWPVRGPAETPsvpIGRP 313

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  764 LANVDLHVVDGLGRRKTRGASGELWIGGAGVARGYAGDAGEAAGRFVEEGWPGSGRLYRSGDLVRWRADGCLEFLGRIDE 843
Cdd:cd17646  314 VPNTRLYVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPFGPGSRMYRTGDLARWRPDGALEFLGRSDD 393

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 15597498  844 QVKINGYRIELGEIRSALLEHPAVGEAAVLTDEAdaaePGADRRIVAFVTAAEETADES 902
Cdd:cd17646  394 QVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAA----PAGAARLVGYVVPAAGAAGPD 448
PRK12316 PRK12316
peptide synthase; Provisional
 400-1804 4.85e-94

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 342.32  E-value: 4.85e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   400 RLLDAWVECLESIAADRQLPLAGLPLIGAAERERY-QAWQGERVEPAPVESLVAAFDLRAALQPQAPALLDAHGSLDFAT 478
Cdd:PRK12316  462 RMARHWQNLLRGMVENPQARVDELPMLDAEERGQLvEGWNATAAEYPLQRGVHRLFEEQVERTPEAPALAFGEETLDYAE 541

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   479 LRARSEAVAEALLAAGVRPGQAVAVMTGRNREAIVALLGVMRAAAVYTPVNPEFPAARVERMREAGGIVFALADAECAGR 558
Cdd:PRK12316  542 LNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLSQSHLGRK 621

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   559 AREAFAGACLDLSTLPLAGSGMSLPAPG----GRDAAYMIFTSGTSGQPKGVVVEHASALNLSQAlARTVYANVVGEglR 634
Cdd:PRK12316  622 LPLAAGVQVLDLDRPAAWLEGYSEENPGtelnPENLAYVIYTSGSTGKPKGAGNRHRALSNRLCW-MQQAYGLGVGD--T 698

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   635 VTVNAPFSFDSSIKQI-LQLLSGHCLVLVPQEVRSDPQRMLGFLEERRIDVLDCTPSLFRLLLQAGLDDAHPALPgRILV 713
Cdd:PRK12316  699 VLQKTPFSFDVSVWEFfWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVASCTSLR-RIVC 777

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   714 GGERFDEASWE-VAAGWRRCQVFNLYGPTEATVNAS-LARVAEHAR-PTIGRALANVDLHVVDGLGRRKTRGASGELWIG 790
Cdd:PRK12316  778 SGEALPADAQEqVFAKLPQAGLYNLYGPTEAAIDVThWTCVEEGGDsVPIGRPIANLACYILDANLEPVPVGVLGELYLA 857

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   791 GAGVARGYAGDAGEAAGRFVEEGWPGSGRLYRSGDLVRWRADGCLEFLGRIDEQVKINGYRIELGEIRSALLEHPAVGEA 870
Cdd:PRK12316  858 GRGLARGYHGRPGLTAERFVPSPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREA 937

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   871 AV-------------LTDEADA---------------------------------------AEPGADRRIVAFVTAAEET 898
Cdd:PRK12316  938 AVlavdgkqlvgyvvLESEGGDwrealkahlaaslpeymvpaqwlalerlpltpngkldrkALPAPEASVAQQGYVAPRN 1017

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   899 ADESWLEV---DLPSGHRVaGLNLNETEYVYQEIFVDEVYSR---DGIVLPPDavvlDVGANIGLFSLYIASRAPRA--- 969
Cdd:PRK12316 1018 ALERTLAAiwqDVLGVERV-GLDDNFFELGGDSIVSIQVVSRarqAGIQLSPR----DLFQHQTIRSLALVAKAGQAtaa 1092

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   970 ---RVVAFEPLAPIRRRL--EANLGRY--------APQVEVFGIGLSDAEREETFTYYPGYSTFSGIAE-----YADASG 1031
Cdd:PRK12316 1093 dqgPASGEVALAPVQRWFfeQAIPQRQhwnqslllQARQPLDPDRLGRALERLVAHHDALRLRFREEDGgwqqaYAAPQA 1172

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1032 ERDVIRRYLSNQG------EEGGANLLLDNiDEILDDRLRAEAHRCRlrRLDQVIGELGLERID--LLKIDVQRAEMDVL 1103
Cdd:PRK12316 1173 GEVLWQRQAASEEellalcEEAQRSLDLEQ-GPLLRALLVDMADGSQ--RLLLVIHHLVVDGVSwrILLEDLQRAYADLD 1249

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1104 LGLD---------DAALAKVRQIVLEVHDKRDGATAGRADAL------SDLLRRHGFEVSIRQDA--------------- 1153
Cdd:PRK12316 1250 ADLPartssyqawARRLHEHAGARAEELDYWQAQLEDAPHELpcenpdGALENRHERKLELRLDAertrqllqeapaayr 1329

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1154 ------LLEGTDRYNC-YAVRP-------GYA-ESLAERID------WRALAPRPAAALGGELSE------QALRGFLEA 1206
Cdd:PRK12316 1330 tqvndlLLTALARVTCrWSGQAsvlvqleGHGrEDLFEDIDlsrtvgWFTSLFPVRLTPAADLGEsikaikEQLRAVPDK 1409

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1207 RLPAYML-----PSRIARVERLP-----LTAEGKLDRRALLAALAAEAAAQTLeapANATEAALLEIWKSvlkrpaigvs 1276
Cdd:PRK12316 1410 GIGYGLLrylagEEAAARLAALPqpritFNYLGQFDRQFDEAALFVPATESAG---AAQDPCAPLANWLS---------- 1476

                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1277 dnffqvggdsirlIQMQVMAREAGLAFTL-RDVFNHQSIRELAR-----LLAAPASPADALGTSAPQSLEPFALLSAAER 1350
Cdd:PRK12316 1477 -------------IEGQVYGGELSLHWSFsREMFAEATVQRLADdyareLQALIEHCCDERNRGVTPSDFPLAGLSQAQL 1543

                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1351 KRLP---EGLDDAYPMTSLQQGMLLQS---EASGDprlLHNVVLHEVHGrLDGELLARAWAILIGRHAILRTGFDLHGG- 1423
Cdd:PRK12316 1544 DALPlpaGEIADIYPLSPMQQGMLFHSlyeQEAGD---YINQLRVDVQG-LDPDRFRAAWQATVDRHEILRSGFLWQDGl 1619

                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1424 QVPLQWVHPATavaaEVPVHDLCGLDGETRRLRLRAWIEEEQATPFDWSRPPLVRLAALALDERRFALGVAEHHSVLDGW 1503
Cdd:PRK12316 1620 EQPLQVIHKQV----ELPFAELDWRGREDLGQALDALAQAERQKGFDLTRAPLLRLVLVRTGEGRHHLIYTNHHILMDGW 1695

                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1504 SLQSLVDELLAVYAdllagvvAREAEAPAVGFRDYVA-LEREAEanAASALFWLDYLAgaryrplpglAEEGPRRMA-AV 1581
Cdd:PRK12316 1696 SNAQLLGEVLQRYA-------GQPVAAPGGRYRDYIAwLQRQDA--AASEAFWKEQLA----------ALEEPTRLAqAA 1756

                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1582 RVDVP------------ADSLSRLRALAERSGLPLRSLLLAAHGRALCRFSDADEVVTGFVSHGRPEE-PGADRLLGLFL 1648
Cdd:PRK12316 1757 RTEDGqvgygdhqqlldPAQTRALAEFARAQKVTLNTLVQAAWLLLLQRYTGQETVAFGATVAGRPAElPGIEQQIGLFI 1836

                        1450      1460      1470      1480      1490      1500      1510      1520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1649 NTLP--CRLSASVDLLDSARRAFDYERASLEHRRHPLAAIRR---RNRELRLDSLFNFVDFHQDDA----APAGVRHGGI 1719
Cdd:PRK12316 1837 NTLPviAAPRPDQSVADWLQEVQALNLALREHEHTPLYDIQRwagQGGEALFDSLLVFENYPVAEAlkqgAPAGLVFGRV 1916

                        1530      1540      1550      1560      1570      1580      1590      1600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1720 LDQVVVDVDVPLAVDFevaGERLEVGFQYAAGRFPAERAEALAGAYREALLALLGDPVQPPAAAQAEDSVELRRVLKVLS 1799
Cdd:PRK12316 1917 SNHEQTNYPLTLAVTL---GETLSLQYSYDRGHFDAAAIERLDRHLLHLLEQMAEDAQAALGELALLDAGERQRILADWD 1993


                  ....*
gi 15597498  1800 RVLGR 1804
Cdd:PRK12316 1994 RTPEA 1998
A_NRPS_Cytc1-like cd17643
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ...
 462-900 3.28e-91

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: 304.62  E-value: 3.28e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  462 PQAPALLDAHGSLDFATLRARSEAVAEALLAAGVRPGQAVAVMTGRNREAIVALLGVMRAAAVYTPVNPEFPAARVERMR 541
Cdd:cd17643    1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  542 EAGGIVFALADAEcagrareafagacldlstlplagsgmslpapggrDAAYMIFTSGTSGQPKGVVVEHASALNLsqaLA 621
Cdd:cd17643   81 ADSGPSLLLTDPD----------------------------------DLAYVIYTSGSTGRPKGVVVSHANVLAL---FA 123

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  622 RTVYANVVGEGLRVTVNAPFSFDSSIKQI-LQLLSGHCLVLVPQEVRSDPQRMLGFLEERRIDVLDCTPSLFRLLLQAGL 700
Cdd:cd17643  124 ATQRWFGFNEDDVWTLFHSYAFDFSVWEIwGALLHGGRLVVVPYEVARSPEDFARLLRDEGVTVLNQTPSAFYQLVEAAD 203

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  701 DDAHPALPGRILV-GGERFDEA---SWEVAAGWRRCQVFNLYGPTEATVNASLARV-----AEHARPTIGRALANVDLHV 771
Cdd:cd17643  204 RDGRDPLALRYVIfGGEALEAAmlrPWAGRFGLDRPQLVNMYGITETTVHVTFRPLdaadlPAAAASPIGRPLPGLRVYV 283

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  772 VDGLGRRKTRGASGELWIGGAGVARGYAGDAGEAAGRFVEE--GWPGSgRLYRSGDLVRWRADGCLEFLGRIDEQVKING 849
Cdd:cd17643  284 LDADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANpfGGPGS-RMYRTGDLARRLPDGELEYLGRADEQVKIRG 362

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|.
gi 15597498  850 YRIELGEIRSALLEHPAVGEAAVLTDEadaAEPGaDRRIVAFVTAAEETAD 900
Cdd:cd17643  363 FRIELGEIEAALATHPSVRDAAVIVRE---DEPG-DTRLVAYVVADDGAAA 409
A_NRPS_CmdD_like cd17652
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ...
 462-899 7.22e-89

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: 297.63  E-value: 7.22e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  462 PQAPALLDAHGSLDFATLRARSEAVAEALLAAGVRPGQAVAVMTGRNREAIVALLGVMRAAAVYTPVNPEFPAARVERMr 541
Cdd:cd17652    1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYM- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  542 eaggivfaLADAecagrareafaGACLDLSTlplagsgmslpapgGRDAAYMIFTSGTSGQPKGVVVEHASALNLSQALA 621
Cdd:cd17652   80 --------LADA-----------RPALLLTT--------------PDNLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQI 126

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  622 RtvyANVVGEGLRVTVNAPFSFDSSIKQILQ-LLSGHCLVLVPQEVRSDPQRMLGFLEERRIDVLDCTPSLFRLLLQAGL 700
Cdd:cd17652  127 A---AFDVGPGSRVLQFASPSFDASVWELLMaLLAGATLVLAPAEELLPGEPLADLLREHRITHVTLPPAALAALPPDDL 203

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  701 DDAHpalpgRILVGGErfdEASWEVAAGW-RRCQVFNLYGPTEATVNASLARVAE-HARPTIGRALANVDLHVVDGLGRR 778
Cdd:cd17652  204 PDLR-----TLVVAGE---ACPAELVDRWaPGRRMINAYGPTETTVCATMAGPLPgGGVPPIGRPVPGTRVYVLDARLRP 275

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  779 KTRGASGELWIGGAGVARGYAGDAGEAAGRFVEE--GWPGSgRLYRSGDLVRWRADGCLEFLGRIDEQVKINGYRIELGE 856
Cdd:cd17652  276 VPPGVPGELYIAGAGLARGYLNRPGLTAERFVADpfGAPGS-RMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGE 354

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|...
gi 15597498  857 IRSALLEHPAVGEAAVLTDEadaaEPGADRRIVAFVTAAEETA 899
Cdd:cd17652  355 VEAALTEHPGVAEAVVVVRD----DRPGDKRLVAYVVPAPGAA 393
A_NRPS_ApnA-like cd17644
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ...
 454-897 6.26e-88

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: 295.88  E-value: 6.26e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  454 FDLRAALQPQAPALLDAHGSLDFATLRARSEAVAEALLAAGVRPGQAVAVMTGRNREAIVALLGVMRAAAVYTPVNPEFP 533
Cdd:cd17644    6 FEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLDPNYP 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  534 AARVERMREAGGIVFALADAEcagrareafagacldlstlplagsgmslpapggrDAAYMIFTSGTSGQPKGVVVEHASA 613
Cdd:cd17644   86 QERLTYILEDAQISVLLTQPE----------------------------------NLAYVIYTSGSTGKPKGVMIEHQSL 131

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  614 LNLSQALARTVYANvvgEGLRVTVNAPFSFDSSIKQILQ-LLSGHCLVLVPQEVRSDPQRMLGFLEERRIDVLDCTPSLF 692
Cdd:cd17644  132 VNLSHGLIKEYGIT---SSDRVLQFASIAFDVAAEEIYVtLLSGATLVLRPEEMRSSLEDFVQYIQQWQLTVLSLPPAYW 208

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  693 RLLLQAGLDD--AHPALPGRILVGGERFDEASWE--VAAGWRRCQVFNLYGPTEATVNASLARV-----AEHARPTIGRA 763
Cdd:cd17644  209 HLLVLELLLStiDLPSSLRLVIVGGEAVQPELVRqwQKNVGNFIQLINVYGPTEATIAATVCRLtqlteRNITSVPIGRP 288

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  764 LANVDLHVVDGLGRRKTRGASGELWIGGAGVARGYAGDAGEAAGRFVEEGWPGS--GRLYRSGDLVRWRADGCLEFLGRI 841
Cdd:cd17644  289 IANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFNSSesERLYKTGDLARYLPDGNIEYLGRI 368

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 15597498  842 DEQVKINGYRIELGEIRSALLEHPAVGEAAVLTDEadaaEPGADRRIVAFVTAAEE 897
Cdd:cd17644  369 DNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVRE----DQPGNKRLVAYIVPHYE 420
A_NRPS_TlmIV_like cd12114
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ...
 462-897 2.17e-84

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: 286.09  E-value: 2.17e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  462 PQAPALLDAHGSLDFATLRARSEAVAEALLAAGVRPGQAVAVMTGRNREAIVALLGVMRAAAVYTPVNPEFPAARVERMR 541
Cdd:cd12114    1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  542 EAGGIVFALADAECAgrareAFAGACLDLSTLPLAGSGMSLPAPGGR----DAAYMIFTSGTSGQPKGVVVEHASALNLS 617
Cdd:cd12114   81 ADAGARLVLTDGPDA-----QLDVAVFDVLILDLDALAAPAPPPPVDvapdDLAYVIFTSGSTGTPKGVMISHRAALNTI 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  618 QALARtvyANVVGEGLRVTVNAPFSFDSSIKQILQLLS-GHCLVLVPQEVRSDPQRMLGFLEERRIDVLDCTPSLFRLLL 696
Cdd:cd12114  156 LDINR---RFAVGPDDRVLALSSLSFDLSVYDIFGALSaGATLVLPDEARRRDPAHWAELIERHGVTLWNSVPALLEMLL 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  697 QAGLDDAHPALPGR-ILVGGErfdeasW-------EVAAGWRRCQVFNLYGPTEATVNASLARVAEH--ARPTI--GRAL 764
Cdd:cd12114  233 DVLEAAQALLPSLRlVLLSGD------WipldlpaRLRALAPDARLISLGGATEASIWSIYHPIDEVppDWRSIpyGRPL 306

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  765 ANVDLHVVDGLGRRKTRGASGELWIGGAGVARGYAGDAGEAAGRFVEEgwPGSGRLYRSGDLVRWRADGCLEFLGRIDEQ 844
Cdd:cd12114  307 ANQRYRVLDPRGRDCPDWVPGELWIGGRGVALGYLGDPELTAARFVTH--PDGERLYRTGDLGRYRPDGTLEFLGRRDGQ 384

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|...
gi 15597498  845 VKINGYRIELGEIRSALLEHPAVGEAAVLtdeaDAAEPGaDRRIVAFVTAAEE 897
Cdd:cd12114  385 VKVRGYRIELGEIEAALQAHPGVARAVVV----VLGDPG-GKRLAAFVVPDND 432
A_NRPS_PvdJ-like cd17649
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ...
 462-905 8.15e-83

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: 280.41  E-value: 8.15e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  462 PQAPALLDAHGSLDFATLRARSEAVAEALLAAGVRPGQAVAVMTGRNREAIVALLGVMRAAAVYTPVNPEFPAARVERMR 541
Cdd:cd17649    1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  542 EAGGIVFALADaecagrareafagacldlstlplagsgmslpapGGRDAAYMIFTSGTSGQPKGVVVEHASALNLSQALA 621
Cdd:cd17649   81 EDSGAGLLLTH---------------------------------HPRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQATA 127

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  622 RtVYAnvVGEGLRVTVNAPFSFDSSIKQILQ-LLSGHCLVLVPQEVRSDPQRMLGFLEERRIDVLDCTPS-LFRLLLQAG 699
Cdd:cd17649  128 E-RYG--LTPGDRELQFASFNFDGAHEQLLPpLICGACVVLRPDELWASADELAEMVRELGVTVLDLPPAyLQQLAEEAD 204

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  700 LDDAHPALPGRILV-GGERFdeaSWEVAAGWRRCQV--FNLYGPTEATVNASLARVAEH-----ARPTIGRALANVDLHV 771
Cdd:cd17649  205 RTGDGRPPSLRLYIfGGEAL---SPELLRRWLKAPVrlFNAYGPTEATVTPLVWKCEAGaaragASMPIGRPLGGRSAYI 281

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  772 VDGLGRRKTRGASGELWIGGAGVARGYAGDAGEAAGRFVEEGWPGSG-RLYRSGDLVRWRADGCLEFLGRIDEQVKINGY 850
Cdd:cd17649  282 LDADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDPFGAPGsRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGF 361

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 15597498  851 RIELGEIRSALLEHPAVGEAAVLtdeadaAEPGA-DRRIVAFVTAAEETADESWLE 905
Cdd:cd17649  362 RIELGEIEAALLEHPGVREAAVV------ALDGAgGKQLVAYVVLRAAAAQPELRA 411
PRK12467 PRK12467
peptide synthase; Provisional
 394-895 8.32e-82

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 301.69  E-value: 8.32e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   394 DGTLAGRLLDAWVECLESIAADRQLPLAGLPLIGAAERER-YQAWQGERVEPAPvESLVAAFDLRAALQPQAPALLDAHG 472
Cdd:PRK12467  458 EATTIERLATHWRNLLEAIVAEPRRRLGELPLLDAEERAReLVRWNAPATEYAP-DCVHQLIEAQARQHPERPALVFGEQ 536

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   473 SLDFATLRARSEAVAEALLAAGVRPGQAVAVMTGRNREAIVALLGVMRAAAVYTPVNPEFPAARVERMREAGGIVFALAD 552
Cdd:PRK12467  537 VLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQ 616

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   553 AECAGRAR--EAFAGACLDLSTLPLAGSGMSLPAP--GGRDAAYMIFTSGTSGQPKGVVVEHASALNLSQALARtvyANV 628
Cdd:PRK12467  617 SHLLAQLPvpAGLRSLCLDEPADLLCGYSGHNPEValDPDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAE---RLQ 693

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   629 VGEGLRVTVNAPFSFDSSIKQIL-QLLSGHCLVLVPQEVRSDPQRMLGFLEERRIDVLDCTPSLFRLLLQAGLDdAHPAL 707
Cdd:PRK12467  694 LAADDSMLMVSTFAFDLGVTELFgALASGATLHLLPPDCARDAEAFAALMADQGVTVLKIVPSHLQALLQASRV-ALPRP 772

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   708 PGRILVGGERFdeaSWEVAAGWRR----CQVFNLYGPTEATVNASLARVAEHARPT----IGRALANVDLHVVDGLGRRK 779
Cdd:PRK12467  773 QRALVCGGEAL---QVDLLARVRAlgpgARLINHYGPTETTVGVSTYELSDEERDFgnvpIGQPLANLGLYILDHYLNPV 849

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   780 TRGASGELWIGGAGVARGYAGDAGEAAGRFVEEGW-PGSGRLYRSGDLVRWRADGCLEFLGRIDEQVKINGYRIELGEIR 858
Cdd:PRK12467  850 PVGVVGELYIGGAGLARGYHRRPALTAERFVPDPFgADGGRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIE 929

                         490       500       510
                  ....*....|....*....|....*....|....*...
gi 15597498   859 SALLEHPAVGEAAVLtdeadaAEPG-ADRRIVAFVTAA 895
Cdd:PRK12467  930 ARLLAQPGVREAVVL------AQPGdAGLQLVAYLVPA 961
DltA cd05945
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ...
 458-908 1.22e-78

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: 268.35  E-value: 1.22e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  458 AALQPQAPALLDAHGSLDFATLRARSEAVAEALLAAGVRPGQAVAVMTGRNREAIVALLGVMRAAAVYTPVNPEFPAARV 537
Cdd:cd05945    1 AAANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  538 ERMREAGGIVFALADaecagrareafagacldlstlplagsgmslpapgGRDAAYMIFTSGTSGQPKGVVVEHASALN-L 616
Cdd:cd05945   81 REILDAAKPALLIAD----------------------------------GDDNAYIIFTSGSTGRPKGVQISHDNLVSfT 126

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  617 SQALARtvyaNVVGEGLRVTVNAPFSFDSSIKQIL-QLLSGHCLVLVPQEVRSDPQRMLGFLEERRIDVLDCTPSLFRLL 695
Cdd:cd05945  127 NWMLSD----FPLGPGDVFLNQAPFSFDLSVMDLYpALASGATLVPVPRDATADPKQLFRFLAEHGITVWVSTPSFAAMC 202

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  696 LQAGLDDA--HPALPGrILVGGERFDEAsweVAAGWRRC----QVFNLYGPTEATVNASLARV-----AEHARPTIGRAL 764
Cdd:cd05945  203 LLSPTFTPesLPSLRH-FLFCGEVLPHK---TARALQQRfpdaRIYNTYGPTEATVAVTYIEVtpevlDGYDRLPIGYAK 278

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  765 ANVDLHVVDGLGRRKTRGASGELWIGGAGVARGYAGDAGEAAGRFV-EEGWPGsgrlYRSGDLVRWRADGCLEFLGRIDE 843
Cdd:cd05945  279 PGAKLVILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFpDEGQRA----YRTGDLVRLEADGLLFYRGRLDF 354

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15597498  844 QVKINGYRIELGEIRSALLEHPAVGEAAVLTDEADAAEPgadrRIVAFVTAaeETADESWLEVDL 908
Cdd:cd05945  355 QVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVT----ELIAFVVP--KPGAEAGLTKAI 413
A_NRPS_PpsD_like cd17650
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ...
 462-898 5.28e-78

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: 266.64  E-value: 5.28e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  462 PQAPALLDAHGSLDFATLRARSEAVAEALLAAGVRPGQAVAVMTGRNREAIVALLGVMRAAAVYTPVNPEFPAARVERMR 541
Cdd:cd17650    1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  542 EAGGIVFALADAEcagrareafagacldlstlplagsgmslpapggrDAAYMIFTSGTSGQPKGVVVEHASALNLSQALA 621
Cdd:cd17650   81 EDSGAKLLLTQPE----------------------------------DLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAWR 126

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  622 RtVYAnVVGEGLRVTVNAPFSFDSSIKQILQ-LLSGHCLVLVPQEVRSDPQRMLGFLEERRIDVLDCTPSLFRLLL---- 696
Cdd:cd17650  127 R-EYE-LDSFPVRLLQMASFSFDVFAGDFARsLLNGGTLVICPDEVKLDPAALYDLILKSRITLMESTPALIRPVMayvy 204

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  697 QAGLDdaHPALpgRILVGGERFDEASWEVAAGWR---RCQVFNLYGPTEATVNAS-----LARVAEHARPTIGRALANVD 768
Cdd:cd17650  205 RNGLD--LSAM--RLLIVGSDGCKAQDFKTLAARfgqGMRIINSYGVTEATIDSTyyeegRDPLGDSANVPIGRPLPNTA 280

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  769 LHVVDGLGRRKTRGASGELWIGGAGVARGYAGDAGEAAGRFVEEGWPGSGRLYRSGDLVRWRADGCLEFLGRIDEQVKIN 848
Cdd:cd17650  281 MYVLDERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFAPGERMYRTGDLARWRADGNVELLGRVDHQVKIR 360

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|
gi 15597498  849 GYRIELGEIRSALLEHPAVGEAAVLTDEADaaepGADRRIVAFVTAAEET 898
Cdd:cd17650  361 GFRIELGEIESQLARHPAIDEAVVAVREDK----GGEARLCAYVVAAATL 406
A_NRPS_SidN3_like cd05918
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ...
 454-902 8.81e-78

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: 267.10  E-value: 8.81e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  454 FDLRAALQPQAPALLDAHGSLDFATLRARSEAVAEALLAAGVRPGQAVAVMTGRNREAIVALLGVMRAAAVYTPVNPEFP 533
Cdd:cd05918    5 IEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLDPSHP 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  534 AARVERMREAGGIVFALADAECagrareafagacldlstlplagsgmslpapggrDAAYMIFTSGTSGQPKGVVVEHASA 613
Cdd:cd05918   85 LQRLQEILQDTGAKVVLTSSPS---------------------------------DAAYVIFTSGSTGKPKGVVIEHRAL 131

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  614 LNLSQALARTVYanvVGEGLRVTVNAPFSFDSSIKQIL-QLLSGHCLVLVPQEVRsdPQRMLGFLEERRIDVLDCTPSLF 692
Cdd:cd05918  132 STSALAHGRALG---LTSESRVLQFASYTFDVSILEIFtTLAAGGCLCIPSEEDR--LNDLAGFINRLRVTWAFLTPSVA 206

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  693 RLLlqaglddaHPA-LPG--RILVGGERfdeASWEVAAGW-RRCQVFNLYGPTEATVNASLARVAEHARP-TIGRALANV 767
Cdd:cd05918  207 RLL--------DPEdVPSlrTLVLGGEA---LTQSDVDTWaDRVRLINAYGPAECTIAATVSPVVPSTDPrNIGRPLGAT 275

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  768 dLHVVDGLGRRKT--RGASGELWIGGAGVARGYAGDAGEAAGRFVE-------EGWPGSGRLYRSGDLVRWRADGCLEFL 838
Cdd:cd05918  276 -CWVVDPDNHDRLvpIGAVGELLIEGPILARGYLNDPEKTAAAFIEdpawlkqEGSGRGRRLYRTGDLVRYNPDGSLEYV 354

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15597498  839 GRIDEQVKINGYRIELGEIRSALLEHPAVGEAAVltdeADAAEP---GADRRIVAFVTAAEETADES 902
Cdd:cd05918  355 GRKDTQVKIRGQRVELGEIEHHLRQSLPGAKEVV----VEVVKPkdgSSSPQLVAFVVLDGSSSGSG 417
PRK12467 PRK12467
peptide synthase; Provisional
 381-907 2.17e-77

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 287.44  E-value: 2.17e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   381 EGRLASLRVRRD-HDGTLAGRLLDAWVECLESIAADRQLPLAGLPLIGAAERER-YQAWQGERVEPAPVESLVAAFDLRA 458
Cdd:PRK12467 1505 EGLQASLTYATDlFEASTIERLAGHWLNLLQGLVADPERRLGELDLLDEAERRQiLEGWNATHTGYPLARLVHQLIEDQA 1584

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   459 ALQPQAPALLDAHGSLDFATLRARSEAVAEALLAAGVRPGQAVAVMTGRNREAIVALLGVMRAAAVYTPVNPEFPAARVE 538
Cdd:PRK12467 1585 AATPEAVALVFGEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLA 1664

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   539 RMREAGGIVFALADAECAGR--AREAFAGACLDLSTLPLAGSGMSLPA--PGGRDAAYMIFTSGTSGQPKGVVVEHASAL 614
Cdd:PRK12467 1665 YMIEDSGIELLLTQSHLQARlpLPDGLRSLVLDQEDDWLEGYSDSNPAvnLAPQNLAYVIYTSGSTGRPKGAGNRHGALV 1744

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   615 NLSQALaRTVYANVVGEGlrVTVNAPFSFDSSIKQIL-QLLSGHCLVLVPQEVRSDPQRMLGFLEERRIDVLDCTPSLFR 693
Cdd:PRK12467 1745 NRLCAT-QEAYQLSAADV--VLQFTSFAFDVSVWELFwPLINGARLVIAPPGAHRDPEQLIQLIERQQVTTLHFVPSMLQ 1821

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   694 LLLQAGLDDAHPALPGRILVGGERFDEAS---WEVAAGWRrcQVFNLYGPTEATVNASLaRVAEHARPT------IGRAL 764
Cdd:PRK12467 1822 QLLQMDEQVEHPLSLRRVVCGGEALEVEAlrpWLERLPDT--GLFNLYGPTETAVDVTH-WTCRRKDLEgrdsvpIGQPI 1898

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   765 ANVDLHVVDGLGRRKTRGASGELWIGGAGVARGYAGDAGEAAGRFVEE--GWPGsGRLYRSGDLVRWRADGCLEFLGRID 842
Cdd:PRK12467 1899 ANLSTYILDASLNPVPIGVAGELYLGGVGLARGYLNRPALTAERFVADpfGTVG-SRLYRTGDLARYRADGVIEYLGRID 1977

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15597498   843 EQVKINGYRIELGEIRSALLEHPAVGEAAVLtdeadAAEPGADRRIVAFVTaaeeTADESWLEVD 907
Cdd:PRK12467 1978 HQVKIRGFRIELGEIEARLREQGGVREAVVI-----AQDGANGKQLVAYVV----PTDPGLVDDD 2033
PRK12467 PRK12467
peptide synthase; Provisional
 409-906 2.04e-76

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 284.36  E-value: 2.04e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   409 LESIAADRQLPLAGLPLIGAAERER-YQAWQGERVEPAPVESLVAAFDLRAALQPQAPALLDAHGSLDFATLRARSEAVA 487
Cdd:PRK12467 3055 LQAMLNNPAARLGELPTLAAHERRQvLHAWNATAAAYPSERLVHQLIEAQVARTPEAPALVFGDQQLSYAELNRRANRLA 3134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   488 EALLAAGVRPGQAVAVMTGRNREAIVALLGVMRAAAVYTPVNPEFPAARVERMREAGGIVFALADAECAGRAREAFAGAC 567
Cdd:PRK12467 3135 HRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKLLLTQAHLLEQLPAPAGDTA 3214

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   568 LDLSTLPLAGSGMSLPAP--GGRDAAYMIFTSGTSGQPKGVVVEHASALNLSQALARtvyANVVGEGLRVTVNAPFSFDS 645
Cdd:PRK12467 3215 LTLDRLDLNGYSENNPSTrvMGENLAYVIYTSGSTGKPKGVGVRHGALANHLCWIAE---AYELDANDRVLLFMSFSFDG 3291

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   646 SIKQIL-QLLSGHCLVLVPQEVRsDPQRMLGFLEERRIDVLDCTPSLFRLLLQ-AGLDDAHPAlpGRILVGGERFDEASW 723
Cdd:PRK12467 3292 AQERFLwTLICGGCLVVRDNDLW-DPEELWQAIHAHRISIACFPPAYLQQFAEdAGGADCASL--DIYVFGGEAVPPAAF 3368

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   724 E-VAAGWRRCQVFNLYGPTEATVNASLARVAEHARPT-----IGRALANVDLHVVDGLGRRKTRGASGELWIGGAGVARG 797
Cdd:PRK12467 3369 EqVKRKLKPRGLTNGYGPTEAVVTVTLWKCGGDAVCEapyapIGRPVAGRSIYVLDGQLNPVPVGVAGELYIGGVGLARG 3448

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   798 YAGDAGEAAGRFVEEGWPGSG-RLYRSGDLVRWRADGCLEFLGRIDEQVKINGYRIELGEIRSALLEHPAVGEAAVLtde 876
Cdd:PRK12467 3449 YHQRPSLTAERFVADPFSGSGgRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVL--- 3525

                         490       500       510
                  ....*....|....*....|....*....|
gi 15597498   877 adAAEPGADRRIVAFVTAAEETADesWLEV 906
Cdd:PRK12467 3526 --ARDGAGGKQLVAYVVPADPQGD--WRET 3551
AMP-binding pfam00501
AMP-binding enzyme;
454-847 4.85e-76

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 259.55  E-value: 4.85e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498    454 FDLRAALQPQAPALL-DAHGSLDFATLRARSEAVAEALLAAGVRPGQAVAVMTGRNREAIVALLGVMRAAAVYTPVNPEF 532
Cdd:pfam00501    1 LERQAARTPDKTALEvGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498    533 PAARVERMREAGGIVFALADAEC-AGRAREAFA------------------GACLDLSTLPLAGSGMSLPAPGGRDAAYM 593
Cdd:pfam00501   81 PAEELAYILEDSGAKVLITDDALkLEELLEALGklevvklvlvldrdpvlkEEPLPEEAKPADVPPPPPPPPDPDDLAYI 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498    594 IFTSGTSGQPKGVVVEHASALNLSQALAR-TVYANVVGEGLRVTVNAPFSFDSSIK--QILQLLSGHCLVLVPQEVRSDP 670
Cdd:pfam00501  161 IYTSGTTGKPKGVMLTHRNLVANVLSIKRvRPRGFGLGPDDRVLSTLPLFHDFGLSlgLLGPLLAGATVVLPPGFPALDP 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498    671 QRMLGFLEERRIDVLDCTPSLFRLLLQAGlDDAHPALPG--RILVGGERFDEASWEVAAGWRRCQVFNLYGPTEATVNAS 748
Cdd:pfam00501  241 AALLELIERYKVTVLYGVPTLLNMLLEAG-APKRALLSSlrLVLSGGAPLPPELARRFRELFGGALVNGYGLTETTGVVT 319

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498    749 LAR---VAEHARPTIGRALANVDLHVVD-GLGRRKTRGASGELWIGGAGVARGYAGDAGEAAGRFVEEGWpgsgrlYRSG 824
Cdd:pfam00501  320 TPLpldEDLRSLGSVGRPLPGTEVKIVDdETGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDEDGW------YRTG 393

                          410       420
                   ....*....|....*....|...
gi 15597498    825 DLVRWRADGCLEFLGRIDEQVKI 847
Cdd:pfam00501  394 DLGRRDEDGYLEIVGRKKDQIKL 416
A_NRPS_Sfm_like cd12115
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ...
 447-899 2.53e-75

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: 258.79  E-value: 2.53e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  447 VESLVAAFdlrAALQPQAPALLDAHGSLDFATLRARSEAVAEALLAAGVRPGQAVAVMTGRNREAIVALLGVMRAAAVYT 526
Cdd:cd12115    1 LHDLVEAQ---AARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  527 PVNPEFPAARVErmreaggivFALADAECAgrareafagacldlstlplagsgmsLPAPGGRDAAYMIFTSGTSGQPKGV 606
Cdd:cd12115   78 PLDPAYPPERLR---------FILEDAQAR-------------------------LVLTDPDDLAYVIYTSGSTGRPKGV 123

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  607 VVEHASALNLSQALARTVYANVVGEGLRVTvnaPFSFDSSIKQILQLLS-GHCLVLVpqevrSDPQRMLGFLEERRIDVL 685
Cdd:cd12115  124 AIEHRNAAAFLQWAAAAFSAEELAGVLAST---SICFDLSVFELFGPLAtGGKVVLA-----DNVLALPDLPAAAEVTLI 195

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  686 DCTPSLFRLLLQAgldDAHPALPGRILVGGERF-DEASWEVAAGWRRCQVFNLYGPTEATVNASLARVAEHAR--PTIGR 762
Cdd:cd12115  196 NTVPSAAAELLRH---DALPASVRVVNLAGEPLpRDLVQRLYARLQVERVVNLYGPSEDTTYSTVAPVPPGASgeVSIGR 272

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  763 ALANVDLHVVDGLGRRKTRGASGELWIGGAGVARGYAGDAGEAAGRFVEEGWPGSGRLYRSGDLVRWRADGCLEFLGRID 842
Cdd:cd12115  273 PLANTQAYVLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFGPGARLYRTGDLVRWRPDGLLEFLGRAD 352

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 15597498  843 EQVKINGYRIELGEIRSALLEHPAVGEAAVLTDEaDAAepgADRRIVAFVTAAEETA 899
Cdd:cd12115  353 NQVKVRGFRIELGEIEAALRSIPGVREAVVVAIG-DAA---GERRLVAYIVAEPGAA 405
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
409-896 8.42e-75

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 275.38  E-value: 8.42e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   409 LESIAADRQLPLAGLPLIGAAERERYQAWQGERVePAPVESLVAAFDLRAALQPQAPALLDAHGSLDFATLRARSEAVAE 488
Cdd:PRK10252  420 IAQFAADPALLCGDVDILLPGEYAQLAQVNATAV-EIPETTLSALVAQQAAKTPDAPALADARYQFSYREMREQVVALAN 498

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   489 ALLAAGVRPGQAVAVMTGRNREAIVALLGVMRAAAVYTPVNPEFPAARVERMREAGGIVFALADAECAGRAREAFAGACL 568
Cdd:PRK10252  499 LLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLITTADQLPRFADVPDLTSL 578

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   569 DLSTLPLAGSGMSLPAPGGRDAAYMIFTSGTSGQPKGVVVEHASALNLSQALaRTVYAnvVGEGLRVTVNAPFSFDSSIK 648
Cdd:PRK10252  579 CYNAPLAPQGAAPLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWM-QNHYP--LTADDVVLQKTPCSFDVSVW 655

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   649 QI-LQLLSGHCLVLVPQEVRSDPQRMLGFLEERRIDVLDCTPSLFRLLLQA----GLDDAHPALPgRILVGGERFDEA-- 721
Cdd:PRK10252  656 EFfWPFIAGAKLVMAEPEAHRDPLAMQQFFAEYGVTTTHFVPSMLAAFVASltpeGARQSCASLR-QVFCSGEALPADlc 734

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   722 -SWEvaaGWRRCQVFNLYGPTEATVNAS--------LARVAEHARPtIGRALANVDLHVVDGLGRRKTRGASGELWIGGA 792
Cdd:PRK10252  735 rEWQ---QLTGAPLHNLYGPTEAAVDVSwypafgeeLAAVRGSSVP-IGYPVWNTGLRILDARMRPVPPGVAGDLYLTGI 810

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   793 GVARGYAGDAGEAAGRFVEEGWPGSGRLYRSGDLVRWRADGCLEFLGRIDEQVKINGYRIELGEIRSALLEHPAVGEAAV 872
Cdd:PRK10252  811 QLAQGYLGRPDLTASRFIADPFAPGERMYRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVEQAVT 890

                         490       500
                  ....*....|....*....|....*.
gi 15597498   873 LTDE--ADAAEPGADRRIVAFVTAAE 896
Cdd:PRK10252  891 HACVinQAAATGGDARQLVGYLVSQS 916
GrsT COG3208
Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and ...
 1880-2114 1.90e-74

Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442441 [Multi-domain]  Cd Length: 237  Bit Score: 247.84  E-value: 1.90e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1880 SAQPRLRLIALPPAGGNAGTFRGWDARLPADVELLAIQYPGRQERQDEPFVTDVEAMLCAIDDALLPLLDRPFALIGASL 1959
Cdd:COG3208    2 RPDARLRLFCFPYAGGSASAYRPWAAALPPDIEVLAVQLPGRGDRLGEPPLTSLEELADDLAEELAPLLDRPFALFGHSM 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1960 GGMLAYELAARLESLHGLRARQLFVISSRAPGPDLEYPRFHAMGDAELLRTLREYDVLPLEVLDDPELREISLATLRADS 2039
Cdd:COG3208   82 GALLAFELARRLERRGRPLPAHLFVSGRRAPHLPRRRRPLHDLSDAELLAELRRLGGTPEEVLADPELLELFLPILRADF 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15597498 2040 RLAADYRYRPREPLAIPITAILGEQDPGVSRVAIDGWRRHASR-YELETLAGGHGLVVTAAEEVCAILRQRLAPDV 2114
Cdd:COG3208  162 RLLETYRYTPGPPLDCPITALGGDDDPLVSPEELAAWREHTTGpFRLRVFPGGHFFLRDHPAELLALIRAALAALA 237
PRK12316 PRK12316
peptide synthase; Provisional
 196-897 5.07e-74

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 276.45  E-value: 5.07e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   196 LAGEDGESASGYWREQAAvAAESPLALADDL-------GEGEWTARRLLPRALLERLAA---------NGLPEAAALLAW 259
Cdd:PRK12316 4273 LQRQDAAASEAFWREQLA-ALDEPTRLAQAIaradlrsANGYGEHVRELDATATARLREfartqrvtlNTLVQAAWLLLL 4351

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   260 TQVAGQFQGDEGLPlemarlVSGRL--FNEFAELAGPFAGVAPLCLENVRAGSVGERLDALQAAILAQEEAAALrdPFAP 337
Cdd:PRK12316 4352 QRYTGQDTVAFGAT------VAGRPaeLPGIEGQIGLFINTLPVIATPRAQQSVVEWLQQVQRQNLALREHEHT--PLYE 4423

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   338 DWPLAELGFAWLAGEL---DGAGVAELDCRQPPlGGFLELQVLPHGEGR----LA-----SLRVR----RDH-DGTLAGR 400
Cdd:PRK12316 4424 IQRWAGQGGEALFDSLlvfENYPVSEALQQGAP-GGLRFGEVTNHEQTNypltLAvglgeTLSLQfsydRGHfDAATIER 4502

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   401 LLDAWVECLESIAADRQLPLAGLPLIGAAERERY-QAWQGERVE-PAP--VESLVAAfdlRAALQPQAPALLDAHGSLDF 476
Cdd:PRK12316 4503 LARHLTNLLEAMAEDPQRRLGELQLLEKAEQQRIvALWNRTDAGyPATrcVHQLVAE---RARMTPDAVAVVFDEEKLTY 4579

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   477 ATLRARSEAVAEALLAAGVRPGQAVAVMTGRNREAIVALLGVMRAAAVYTPVNPEFPAARVERMREAGGIVFALADAECA 556
Cdd:PRK12316 4580 AELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSGAALLLTQSHLL 4659

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   557 GRAREAFAGACLDLS-TLPLAGSGMSLPAPG--GRDAAYMIFTSGTSGQPKGVVVEHASALNLSQALARtvyANVVGEGL 633
Cdd:PRK12316 4660 QRLPIPDGLASLALDrDEDWEGFPAHDPAVRlhPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGE---RYELTPDD 4736

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   634 RVTVNAPFSFDSSIKQILQLLSGHCLVLVPQEVRSDPQRMLGFLEERRIDVLDCTPSLFRLLLQAGLDDAHPALPGRILV 713
Cdd:PRK12316 4737 RVLQFMSFSFDGSHEGLYHPLINGASVVIRDDSLWDPERLYAEIHEHRVTVLVFPPVYLQQLAEHAERDGEPPSLRVYCF 4816

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   714 GGERFDEASWEVAagWRRCQV---FNLYGPTEATVNASLARVAEHARPT-----IGRALANVDLHVVDGLGRRKTRGASG 785
Cdd:PRK12316 4817 GGEAVAQASYDLA--WRALKPvylFNGYGPTETTVTVLLWKARDGDACGaaympIGTPLGNRSGYVLDGQLNPLPVGVAG 4894

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   786 ELWIGGAGVARGYAGDAGEAAGRFVEE--GWPGsGRLYRSGDLVRWRADGCLEFLGRIDEQVKINGYRIELGEIRSALLE 863
Cdd:PRK12316 4895 ELYLGGEGVARGYLERPALTAERFVPDpfGAPG-GRLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLRE 4973

                         730       740       750
                  ....*....|....*....|....*....|....
gi 15597498   864 HPAVGEAAVLtdeadAAEPGADRRIVAFVTAAEE 897
Cdd:PRK12316 4974 HPAVREAVVI-----AQEGAVGKQLVGYVVPQDP 5002
PRK12316 PRK12316
peptide synthase; Provisional
 196-909 9.78e-74

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 275.68  E-value: 9.78e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   196 LAGEDGESASGYWREQAAvAAESPLALADDL-------GEGEW-------TARRLLPRALLERLAANGLPEAAALLAWTQ 261
Cdd:PRK12316 1727 LQRQDAAASEAFWKEQLA-ALEEPTRLAQAArtedgqvGYGDHqqlldpaQTRALAEFARAQKVTLNTLVQAAWLLLLQR 1805

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   262 VAGQfqgdegLPLEMARLVSGRLfnefAELAGP------FAGVAPLCLENVRAGSVGERLDALQAAILAqeeaaaLRDpf 335
Cdd:PRK12316 1806 YTGQ------ETVAFGATVAGRP----AELPGIeqqiglFINTLPVIAAPRPDQSVADWLQEVQALNLA------LRE-- 1867

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   336 APDWPLAEL-GFAWLAGE--------LDGAGVAELDCRQPPLG-GFLELQV-------LPHGEGRLASLRV-----RRDH 393
Cdd:PRK12316 1868 HEHTPLYDIqRWAGQGGEalfdsllvFENYPVAEALKQGAPAGlVFGRVSNheqtnypLTLAVTLGETLSLqysydRGHF 1947

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   394 DGTLAGRLLDAWVECLESIAADRQLPLAGLPLIGAAERERYQAWQGERVEPAPVESLV-AAFDLRAALQPQAPALLDAHG 472
Cdd:PRK12316 1948 DAAAIERLDRHLLHLLEQMAEDAQAALGELALLDAGERQRILADWDRTPEAYPRGPGVhQRIAEQAARAPEAIAVVFGDQ 2027

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   473 SLDFATLRARSEAVAEALLAAGVRPGQAVAVMTGRNREAIVALLGVMRAAAVYTPVNPEFPAARVERMREAGGIVFALAD 552
Cdd:PRK12316 2028 HLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLTQ 2107

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   553 AECAGRAREAFAGACLDLST-LPLAGSGMSLPAP--GGRDAAYMIFTSGTSGQPKGVVVEHASALNLSQALARTVYanvV 629
Cdd:PRK12316 2108 RHLLERLPLPAGVARLPLDRdAEWADYPDTAPAVqlAGENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERYE---L 2184

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   630 GEGLRVTVNAPFSFDSSIKQILQ-LLSGHCLVLVPQEVRsDPQRMLGFLEERRIDVLDCTPSLFRLLLQAGLDDAHPALP 708
Cdd:PRK12316 2185 SPADCELQFMSFSFDGAHEQWFHpLLNGARVLIRDDELW-DPEQLYDEMERHGVTILDFPPVYLQQLAEHAERDGRPPAV 2263

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   709 GRILVGGERFDEASWE-VAAGWRRCQVFNLYGPTEATVNASL--ARVAE---HARPTIGRALANVDLHVVDGLGRRKTRG 782
Cdd:PRK12316 2264 RVYCFGGEAVPAASLRlAWEALRPVYLFNGYGPTEAVVTPLLwkCRPQDpcgAAYVPIGRALGNRRAYILDADLNLLAPG 2343

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   783 ASGELWIGGAGVARGYAGDAGEAAGRFVEEGWPGSG-RLYRSGDLVRWRADGCLEFLGRIDEQVKINGYRIELGEIRSAL 861
Cdd:PRK12316 2344 MAGELYLGGEGLARGYLNRPGLTAERFVPDPFSASGeRLYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARL 2423

                         730       740       750       760       770
                  ....*....|....*....|....*....|....*....|....*....|...
gi 15597498   862 LEHPAVGEAAVLtdeadAAEPGADRRIVAFV---TAAEETADE--SWLEVDLP 909
Cdd:PRK12316 2424 QAHPAVREAVVV-----AQDGASGKQLVAYVvpdDAAEDLLAElrAWLAARLP 2471
A_NRPS_ACVS-like cd17648
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ...
 462-909 4.71e-73

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: 252.32  E-value: 4.71e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  462 PQAPALLDAHGSLDFATLRARSEAVAEALLAAG-VRPGQAVAVMTGRNREAIVALLGVMRAAAVYTPVNPEFPAARVErm 540
Cdd:cd17648    1 PDRVAVVYGDKRLTYRELNERANRLAHYLLSVAeIRPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQ-- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  541 reaggivFALADAEcagrAReafagacldlstLPLAGSgmslpapggRDAAYMIFTSGTSGQPKGVVVEHASALNLSQAL 620
Cdd:cd17648   79 -------FILEDTG----AR------------VVITNS---------TDLAYAIYTSGTTGKPKGVLVEHGSVVNLRTSL 126

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  621 ARtVYANVVGEGLRVTVNAPFSFDSSIKQI-LQLLSGHCLVLVPQEVRSDPQRMLGFLEERRIDVLDCTPSLFRLLLQAG 699
Cdd:cd17648  127 SE-RYFGRDNGDEAVLFFSNYVFDFFVEQMtLALLNGQKLVVPPDEMRFDPDRFYAYINREKVTYLSGTPSVLQQYDLAR 205

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  700 LDDAHpalpgRILVGGERFDEASWEVAAGWRRCQVFNLYGPTEATVNASLARVAEHAR--PTIGRALANVDLHVVDGLGR 777
Cdd:cd17648  206 LPHLK-----RVDAAGEEFTAPVFEKLRSRFAGLIINAYGPTETTVTNHKRFFPGDQRfdKSLGRPVRNTKCYVLNDAMK 280

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  778 RKTRGASGELWIGGAGVARGYAGDAGEAAGRFV-------EEGWPGS-GRLYRSGDLVRWRADGCLEFLGRIDEQVKING 849
Cdd:cd17648  281 RVPVGAVGELYLGGDGVARGYLNRPELTAERFLpnpfqteQERARGRnARLYKTGDLVRWLPSGELEYLGRNDFQVKIRG 360

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15597498  850 YRIELGEIRSALLEHPAVGEAAVLT-DEADAAEPGADRRIVAFVTAAEETADES----WLEVDLP 909
Cdd:cd17648  361 QRIEPGEVEAALASYPGVRECAVVAkEDASQAQSRIQKYLVGYYLPEPGHVPESdllsFLRAKLP 425
A_NRPS_GliP_like cd17653
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ...
 453-913 1.49e-72

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: 250.30  E-value: 1.49e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  453 AFDLRAALQPQAPALLDAHGSLDFATLRARSEAVAEALLAAGVRPGQAVAVMTGRNREAIVALLGVMRAAAVYTPVNPEF 532
Cdd:cd17653    2 AFERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  533 PAARVERMREAggivfaladaecagrareafAGACLDLSTlplagsgmslpaPGGRDAAYMIFTSGTSGQPKGVVVEHAS 612
Cdd:cd17653   82 PSARIQAILRT--------------------SGATLLLTT------------DSPDDLAYIIFTSGSTGIPKGVMVPHRG 129

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  613 ALNLSQALARTVYanvVGEGLRVTVNAPFSFDSSIKQILQLLS-GHCLVLvpqevrSDPQRMLGFLeERRIDVLDCTPSL 691
Cdd:cd17653  130 VLNYVSQPPARLD---VGPGSRVAQVLSIAFDACIGEIFSTLCnGGTLVL------ADPSDPFAHV-ARTVDALMSTPSI 199

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  692 FRLLLQAGLDDAHpalpgRILVGGErfdEASWEVAAGW--RRCqVFNLYGPTEATVNASLARVAEHARPTIGRALANVDL 769
Cdd:cd17653  200 LSTLSPQDFPNLK-----TIFLGGE---AVPPSLLDRWspGRR-LYNAYGPTECTISSTMTELLPGQPVTIGKPIPNSTC 270

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  770 HVVDGLGRRKTRGASGELWIGGAGVARGYAGDAGEAAGRFVEEG-WPGSgRLYRSGDLVRWRADGCLEFLGRIDEQVKIN 848
Cdd:cd17653  271 YILDADLQPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPfWPGS-RMYRTGDYGRWTEDGGLEFLGREDNQVKVR 349

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  849 GYRIELGEIRS-ALLEHPAVGEAAVLTDEAdaaepgadrRIVAFVTAaeETAD----ESWLEVDLPSGHR 913
Cdd:cd17653  350 GFRINLEEIEEvVLQSQPEVTQAAAIVVNG---------RLVAFVTP--ETVDvdglRSELAKHLPSYAV 408
A_NRPS_LgrA-like cd17645
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ...
 454-909 2.00e-69

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: 241.30  E-value: 2.00e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  454 FDLRAALQPQAPALLDAHGSLDFATLRARSEAVAEALLAAGVRPGQAVAVMTGRNREAIVALLGVMRAAAVYTPVNPEFP 533
Cdd:cd17645    4 FEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYP 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  534 AARVERMREAGGIVFALADAEcagrareafagacldlstlplagsgmslpapggrDAAYMIFTSGTSGQPKGVVVEHASA 613
Cdd:cd17645   84 GERIAYMLADSSAKILLTNPD----------------------------------DLAYVIYTSGSTGLPKGVMIEHHNL 129

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  614 LNLSQaLARTVYAnvVGEGLRVTVNAPFSFDSSIKQIL-QLLSGHCLVLVPQEVRSDPQRMLGFLEERRIDVLdctpslf 692
Cdd:cd17645  130 VNLCE-WHRPYFG--VTPADKSLVYASFSFDASAWEIFpHLTAGAALHVVPSERRLDLDALNDYFNQEGITIS------- 199

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  693 rlLLQAGLDDAHPALPGR----ILVGGE---RFDEASWevaagwrrcQVFNLYGPTEATVNASLARV-AEHARPTIGRAL 764
Cdd:cd17645  200 --FLPTGAAEQFMQLDNQslrvLLTGGDklkKIERKGY---------KLVNNYGPTENTVVATSFEIdKPYANIPIGKPI 268

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  765 ANVDLHVVDGLGRRKTRGASGELWIGGAGVARGYAGDAGEAAGRFVEEGWPGSGRLYRSGDLVRWRADGCLEFLGRIDEQ 844
Cdd:cd17645  269 DNTRVYILDEALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPFVPGERMYRTGDLAKFLPDGNIEFLGRLDQQ 348

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15597498  845 VKINGYRIELGEIRSALLEHPAVGEAAVLTDEadaaEPGADRRIVAFVTAAEETADE---SWLEVDLP 909
Cdd:cd17645  349 VKIRGYRIEPGEIEPFLMNHPLIELAAVLAKE----DADGRKYLVAYVTAPEEIPHEelrEWLKNDLP 412
MenE/FadK COG0318
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ...
 450-901 2.77e-69

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: 241.25  E-value: 2.77e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  450 LVAAFDLRAALQPQAPALLDAHGSLDFATLRARSEAVAEALLAAGVRPGQAVAVMTGRNREAIVALLGVMRAAAVYTPVN 529
Cdd:COG0318    1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  530 PEFPAARVERMreaggivfaLADAECAgrareafagACLdlstlplagsgmslpapggrdAAYMIFTSGTSGQPKGVVVE 609
Cdd:COG0318   81 PRLTAEELAYI---------LEDSGAR---------ALV---------------------TALILYTSGTTGRPKGVMLT 121

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  610 HASALNLSQALARTVYanvVGEGLRVTVNAPFSFDSSIKQILQ--LLSGHCLVLVPqevRSDPQRMLGFLEERRIDVLDC 687
Cdd:COG0318  122 HRNLLANAAAIAAALG---LTPGDVVLVALPLFHVFGLTVGLLapLLAGATLVLLP---RFDPERVLELIERERVTVLFG 195

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  688 TPSLFRLLLQAgLDDAHPALPG--RILVGGERFDEASWEVAAGWRRCQVFNLYGPTEATVNASLARVAEHARP--TIGRA 763
Cdd:COG0318  196 VPTMLARLLRH-PEFARYDLSSlrLVVSGGAPLPPELLERFEERFGVRIVEGYGLTETSPVVTVNPEDPGERRpgSVGRP 274

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  764 LANVDLHVVDGLGRRKTRGASGELWIGGAGVARGYAGDAGEAAGRFvEEGWpgsgrlYRSGDLVRWRADGCLEFLGRIDE 843
Cdd:COG0318  275 LPGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAF-RDGW------LRTGDLGRLDEDGYLYIVGRKKD 347

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15597498  844 QVKINGYRIELGEIRSALLEHPAVGEAAVltdeADAAEPGADRRIVAFVTA---AEETADE 901
Cdd:COG0318  348 MIISGGENVYPAEVEEVLAAHPGVAEAAV----VGVPDEKWGERVVAFVVLrpgAELDAEE 404
PRK05691 PRK05691
peptide synthase; Validated
 400-902 4.29e-69

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 260.10  E-value: 4.29e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   400 RLLDAWVECLESIAADRQLPLAGLPLIGAAERERYQAWQGERVEPAPVeSLVAAFDLRAALQPQAPALLDAHGSLDFATL 479
Cdd:PRK05691 1084 RLAEHFLALLEQVCEDPQRALGDVQLLDAAERAQLAQWGQAPCAPAQA-WLPELLNEQARQTPERIALVWDGGSLDYAEL 1162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   480 RARSEAVAEALLAAGVRPGQAVAVMTGRNREAIVALLGVMRAAAVYTPVNPEFPAARVERMREAGGIVFALADAECAGRA 559
Cdd:PRK05691 1163 HAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSGVELLLTQSHLLERL 1242

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   560 REAFAGACLDLSTLPLAGSGMSlpAPG----GRDAAYMIFTSGTSGQPKGVVVEHASALNLSQALARTvYAnvVGEGLRV 635
Cdd:PRK05691 1243 PQAEGVSAIALDSLHLDSWPSQ--APGlhlhGDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQAT-YA--LDDSDVL 1317

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   636 TVNAPFSFDSSIKQ-ILQLLSGHCLVLV-PQEVRsDPQRMLGFLEERRIDVLDCTPSLFRLLLQAGLDDAHPALPgRILV 713
Cdd:PRK05691 1318 MQKAPISFDVSVWEcFWPLITGCRLVLAgPGEHR-DPQRIAELVQQYGVTTLHFVPPLLQLFIDEPLAAACTSLR-RLFS 1395

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   714 GGERFD-EASWEVAAGWRRCQVFNLYGPTEATVNAS--LARVAEHARPTIGRALANVDLHVVDGLGRRKTRGASGELWIG 790
Cdd:PRK05691 1396 GGEALPaELRNRVLQRLPQVQLHNRYGPTETAINVThwQCQAEDGERSPIGRPLGNVLCRVLDAELNLLPPGVAGELCIG 1475

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   791 GAGVARGYAGDAGEAAGRFVEEGWPGSG-RLYRSGDLVRWRADGCLEFLGRIDEQVKINGYRIELGEIRSALLEHPAVGE 869
Cdd:PRK05691 1476 GAGLARGYLGRPALTAERFVPDPLGEDGaRLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQ 1555

                         490       500       510
                  ....*....|....*....|....*....|...
gi 15597498   870 AAVLTDEaDAAEPgadrRIVAFVTAAEETADES 902
Cdd:PRK05691 1556 AAVLVRE-GAAGA----QLVGYYTGEAGQEAEA 1583
PRK12316 PRK12316
peptide synthase; Provisional
 2-900 9.71e-67

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 252.57  E-value: 9.71e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498     2 SASEDLQSAVQPAASEALEGFPL--SPLQTRAWRRHAERPENTVVGVRLHAPADPVATLERLRRALDGEAQLRVAYRTMP 79
Cdd:PRK12316 2581 ASLESGQTSRAPVLQKVTRVQPLplSHAQQRQWFLWQLEPESAAYHLPSALHLRGVLDQAALEQAFDALVLRHETLRTRF 2660

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498    80 GMSLPVQVLDGRAADLLVERLPGDGDWAGRFARES-ARLAASPLGGEGQPVLALGLLLDAAGEtlQGLLLAAPAFVVDAA 158
Cdd:PRK12316 2661 VEVGEQTRQVILPNMSLRIVLEDCAGVADAAIRQRvAEEIQRPFDLARGPLLRVRLLALDGQE--HVLVITQHHIVSDGW 2738

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   159 SLVALLRRGLGPAGQASADEGDE----ALLFQHFSEWANEALAGEDGESASGYWREQ---AAVAAESPLALADDLGEGEW 231
Cdd:PRK12316 2739 SMQVMVDELVQAYAGARRGEQPTlpplPLQYADYAAWQRAWMDSGEGARQLDYWRERlggEQPVLELPLDRPRPALQSHR 2818

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   232 TARRL------LPRALLERLAANGLPEAAALLAWTQV-----AGQFQGDEGLPlemarlVSGRLFNEFAELAGPFAGVAP 300
Cdd:PRK12316 2819 GARLDvaldvaLSRELLALARREGVTLFMLLLASFQVllhrySGQSDIRVGVP------IANRNRAETERLIGFFVNTQV 2892

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   301 LCLENVRAGSVGERLDALQAAILAQE--EAAALRDPFAPDWPLAELGFAWL-------------AGELDGAGVAELDCRQ 365
Cdd:PRK12316 2893 LRAQVDAQLAFRDLLGQVKEQALGAQahQDLPFEQLVEALQPERSLSHSPLfqvmynhqsgeraAAQLPGLHIESFAWDG 2972

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   366 PPLGGFLELQVLPHGEGRLASLRVRRDH-DGTLAGRLLDAWVECLESIAADRQLPLAGLPLIGAAERER-YQAWQGERVE 443
Cdd:PRK12316 2973 AATQFDLALDTWESAEGLGASLTYATDLfDARTVERLARHWQNLLRGMVENPQRSVDELAMLDAEERGQlLEAWNATAAE 3052

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   444 PAPVESLVAAFDLRAALQPQAPALLDAHGSLDFATLRARSEAVAEALLAAGVRPGQAVAVMTGRNREAIVALLGVMRAAA 523
Cdd:PRK12316 3053 YPLERGVHRLFEEQVERTPDAVALAFGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGG 3132

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   524 VYTPVNPEFPAARVERMREAGGIVFALADAECAGRAREAFAGACLDLSTLPLAGSGMSLPAPGgRDAAYMIFTSGTSGQP 603
Cdd:PRK12316 3133 AYVPLDPEYPEERLAYMLEDSGAQLLLSQSHLRLPLAQGVQVLDLDRGDENYAEANPAIRTMP-ENLAYVIYTSGSTGKP 3211

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   604 KGVVVEHASALNLSQALARTVyanVVGEGLRVTVNAPFSFDSSIKQIL-QLLSGHCLVLVPQEVRSDPQRMLGFLEERRI 682
Cdd:PRK12316 3212 KGVGIRHSALSNHLCWMQQAY---GLGVGDRVLQFTTFSFDVFVEELFwPLMSGARVVLAGPEDWRDPALLVELINSEGV 3288

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   683 DVLDCTPSLFRLLLQAGLDDAHPALPGRILVGGERFDEASWEVAAGWrrcQVFNLYGPTEATVNASLARVAEH--ARPTI 760
Cdd:PRK12316 3289 DVLHAYPSMLQAFLEEEDAHRCTSLKRIVCGGEALPADLQQQVFAGL---PLYNLYGPTEATITVTHWQCVEEgkDAVPI 3365

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   761 GRALANVDLHVVDGLGRRKTRGASGELWIGGAGVARGYAGDAGEAAGRFVEEGWPGSGRLYRSGDLVRWRADGCLEFLGR 840
Cdd:PRK12316 3366 GRPIANRACYILDGSLEPVPVGALGELYLGGEGLARGYHNRPGLTAERFVPDPFVPGERLYRTGDLARYRADGVIEYIGR 3445

                         890       900       910       920       930       940
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   841 IDEQVKINGYRIELGEIRSALLEHPAVGEAAVLTDEAdaaepgadRRIVAFVTAAEETAD 900
Cdd:PRK12316 3446 VDHQVKIRGFRIELGEIEARLLEHPWVREAVVLAVDG--------RQLVAYVVPEDEAGD 3497
PRK05691 PRK05691
peptide synthase; Validated
 400-901 1.49e-64

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 245.08  E-value: 1.49e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   400 RLLDAWVECLESIAADRQLPLAGLPLIGAAERERYQAW-QGERVEPAPVESLVAAFDLRAALQPQAPALLDAHGSLDFAT 478
Cdd:PRK05691 2139 RMAEHWQNLLEALLGDPQQRLAELPLLAAAEQQQLLDSlAGEAGEARLDQTLHGLFAAQAARTPQAPALTFAGQTLSYAE 2218

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   479 LRARSEAVAEALLAAGVRPGQAVAVMTGRNREAIVALLGVMRAAAVYTPVNPEFPAARVERMREAGGIVFALADA---EC 555
Cdd:PRK05691 2219 LDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLHYMIEDSGIGLLLSDRalfEA 2298

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   556 AGRAREAFAGACLDLSTLPLAG-SGMSLPA-PGGRDAAYMIFTSGTSGQPKGVVVEHASALNLSQALARTVyanvvgeGL 633
Cdd:PRK05691 2299 LGELPAGVARWCLEDDAAALAAySDAPLPFlSLPQHQAYLIYTSGSTGKPKGVVVSHGEIAMHCQAVIERF-------GM 2371

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   634 R--------VTVNapfsFDSSIKQIL-QLLSGHCLVLVPQEvRSDPQRMLGFLEERRIDVLDCTPSLFRLLLQAgLDDAH 704
Cdd:PRK05691 2372 RaddcelhfYSIN----FDAASERLLvPLLCGARVVLRAQG-QWGAEEICQLIREQQVSILGFTPSYGSQLAQW-LAGQG 2445

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   705 PALPGRILV-GGERFDEASWE-VAAGWRRCQVFNLYGPTEaTVNASLARVAEHARPT------IGRALANVDLHVVDGLG 776
Cdd:PRK05691 2446 EQLPVRMCItGGEALTGEHLQrIRQAFAPQLFFNAYGPTE-TVVMPLACLAPEQLEEgaasvpIGRVVGARVAYILDADL 2524

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   777 RRKTRGASGELWIGGAGVARGYAGDAGEAAGRFVEEGW-PGSGRLYRSGDLVRWRADGCLEFLGRIDEQVKINGYRIELG 855
Cdd:PRK05691 2525 ALVPQGATGELYVGGAGLAQGYHDRPGLTAERFVADPFaADGGRLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELG 2604

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*.
gi 15597498   856 EIRSALLEHPAVGEAAVLtdeadAAEPGADRRIVAFVTAAEETADE 901
Cdd:PRK05691 2605 EIESRLLEHPAVREAVVL-----ALDTPSGKQLAGYLVSAVAGQDD 2645
A_NRPS_ProA cd17656
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ...
 462-909 2.04e-62

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: 222.35  E-value: 2.04e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  462 PQAPALLDAHGSLDFATLRARSEAVAEALLAAGVRPGQAVAVMTGRNREAIVALLGVMRAAAVYTPVNPEFPAARVERMR 541
Cdd:cd17656    2 PDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIM 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  542 EAGGIVFALADAECAGRAREAFAGACLDLSTLPlAGSGMSLPAP-GGRDAAYMIFTSGTSGQPKGVVVEHASALNLsqaL 620
Cdd:cd17656   82 LDSGVRVVLTQRHLKSKLSFNKSTILLEDPSIS-QEDTSNIDYInNSDDLLYIIYTSGTTGKPKGVQLEHKNMVNL---L 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  621 ARTVYANVVGEGLRVTVNAPFSFDSSIKQILQ-LLSGHCLVLVPQEVRSDPQRMLGFLEERRIDVLDCTPSLFRLLlqAG 699
Cdd:cd17656  158 HFEREKTNINFSDKVLQFATCSFDVCYQEIFStLLSGGTLYIIREETKRDVEQLFDLVKRHNIEVVFLPVAFLKFI--FS 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  700 LDDAHPALP---GRILVGGER------FDEASWEvaagwRRCQVFNLYGPTEATVnASLARVAEHAR----PTIGRALAN 766
Cdd:cd17656  236 EREFINRFPtcvKHIITAGEQlvitneFKEMLHE-----HNVHLHNHYGPSETHV-VTTYTINPEAEipelPPIGKPISN 309

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  767 VDLHVVDGLGRRKTRGASGELWIGGAGVARGYAGDAGEAAGRFVEEGWPGSGRLYRSGDLVRWRADGCLEFLGRIDEQVK 846
Cdd:cd17656  310 TWIYILDQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPFDPNERMYRTGDLARYLPDGNIEFLGRADHQVK 389

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15597498  847 INGYRIELGEIRSALLEHPAVGEAAVLTDEADAAEpgadRRIVAFVTAAEETADE---SWLEVDLP 909
Cdd:cd17656  390 IRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGE----KYLCAYFVMEQELNISqlrEYLAKQLP 451
DCL_NRPS cd19543
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ...
 1361-1776 2.71e-62

DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor; The DCL-type Condensation (C) domain catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. This domain is D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains in addition to the LCL- and DCL-types such as starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380465 [Multi-domain]  Cd Length: 423  Bit Score: 220.15  E-value: 2.71e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1361 YPMTSLQQGMLLQSEASGDPRLLHNVVLHEVHGRLDGELLARAWAILIGRHAILRTGFDLHGGQVPLQWVHPAtaVAAEV 1440
Cdd:cd19543    2 YPLSPMQEGMLFHSLLDPGSGAYVEQMVITLEGPLDPDRFRAAWQAVVDRHPILRTSFVWEGLGEPLQVVLKD--RKLPW 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1441 PVHDLCGLDGETRRLRLRAWIEEEQATPFDWSRPPLVRLAALALDERRFALGVAEHHSVLDGWSLQSLVDELLAVYADLL 1520
Cdd:cd19543   80 RELDLSHLSEAEQEAELEALAEEDRERGFDLARAPLMRLTLIRLGDDRYRLVWSFHHILLDGWSLPILLKELFAIYAALG 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1521 AGvvaREAEAPAVG-FRDYVA-LEREaEANAASAlFWLDYLAGARYR-PLP---GLAEEGPRRMAAVRVDVPADSLSRLR 1594
Cdd:cd19543  160 EG---QPPSLPPVRpYRDYIAwLQRQ-DKEAAEA-YWREYLAGFEEPtPLPkelPADADGSYEPGEVSFELSAELTARLQ 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1595 ALAERSGLPLRSLLLAAHGRALCRFSDADEVVTGFVSHGRPEE-PGADRLLGLFLNTLPCRLSASVDllDSARRAF-DYE 1672
Cdd:cd19543  235 ELARQHGVTLNTVVQGAWALLLSRYSGRDDVVFGTTVSGRPAElPGIETMVGLFINTLPVRVRLDPD--QTVLELLkDLQ 312

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1673 RASLEHRRH---PLAAIRR---RNRELrLDSLFNFVDFhQDDAAPAGVRHGGILDQVVVDVDVPLAVDFEVA---GERLE 1743
Cdd:cd19543  313 AQQLELREHeyvPLYEIQAwseGKQAL-FDHLLVFENY-PVDESLEEEQDEDGLRITDVSAEEQTNYPLTVVaipGEELT 390

                        410       420       430
                 ....*....|....*....|....*....|...
gi 15597498 1744 VGFQYAAGRFPAERAEALAGAYREALLALLGDP 1776
Cdd:cd19543  391 IKLSYDAEVFDEATIERLLGHLRRVLEQVAANP 423
PRK05691 PRK05691
peptide synthase; Validated
 420-909 4.08e-54

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 210.79  E-value: 4.08e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   420 LAGLPLIGAAERE--RYQAWQGERVEPAPvESLVAAFDLRAALQPQ--APALLDAhgSLDFATLRARSEAVAEALLAAGV 495
Cdd:PRK05691 3691 LSELPLLGEQERDflLDGCNRSERDYPLE-QSYVRLFEAQVAAHPQriAASCLDQ--QWSYAELNRAANRLGHALRAAGV 3767

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   496 RPGQAVAVMTGRNREAIVALLGVMRAAAVYTPVNPEFPAARVERMREAGGIVFALADAECAGRAREAFAG-ACLDLSTL- 573
Cdd:PRK05691 3768 GVDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGLPAQRLQRIIELSRTPVLVCSAACREQARALLDElGCANRPRLl 3847

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   574 ---PLAGSGMSLPAPG---GRDA-AYMIFTSGTSGQPKGVVVEHASALNlsQALARTVYANVvGEGLRVTVNAPFSFDSS 646
Cdd:PRK05691 3848 vweEVQAGEVASHNPGiysGPDNlAYVIYTSGSTGLPKGVMVEQRGMLN--NQLSKVPYLAL-SEADVIAQTASQSFDIS 3924

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   647 IKQILQL-LSGHCLVLVPQEVRSDPQRMLGFLEERRIDVLDCTPSLfrllLQAGLDDAHPALPGR--ILVGGERFDEasw 723
Cdd:PRK05691 3925 VWQFLAApLFGARVEIVPNAIAHDPQGLLAHVQAQGITVLESVPSL----IQGMLAEDRQALDGLrwMLPTGEAMPP--- 3997

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   724 EVAAGW--RRCQV--FNLYGPTEATVNASLARV-AEHARPT---IGRALANVDLHVVDGLGRRKTRGASGELWIGGAGVA 795
Cdd:PRK05691 3998 ELARQWlqRYPQIglVNAYGPAECSDDVAFFRVdLASTRGSylpIGSPTDNNRLYLLDEALELVPLGAVGELCVAGTGVG 4077

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   796 RGYAGDAGEAAGRFVEE--GWPGSgRLYRSGDLVRWRADGCLEFLGRIDEQVKINGYRIELGEIRSALLEHPAVGEAAVL 873
Cdd:PRK05691 4078 RGYVGDPLRTALAFVPHpfGAPGE-RLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAVA 4156

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....
gi 15597498   874 TDEADAAepgadRRIVAFVTAAEETADES--------WLEVDLP 909
Cdd:PRK05691 4157 VQEGVNG-----KHLVGYLVPHQTVLAQGallerikqRLRAELP 4195
AFD_class_I cd04433
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ...
 589-904 3.70e-53

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: 190.57  E-value: 3.70e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  589 DAAYMIFTSGTSGQPKGVVVEHASALNLSQALARTVYanvVGEGLRVTVNAPFSFDSSIKQILQ-LLSGHCLVLVPqevR 667
Cdd:cd04433    1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGG---LTEGDVFLSTLPLFHIGGLFGLLGaLLAGGTVVLLP---K 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  668 SDPQRMLGFLEERRIDVLDCTPSLFRLLLQAGLDDAHPALPGRILV-GGERFDEASWEVAAGWRRCQVFNLYGPTEATVN 746
Cdd:cd04433   75 FDPEAALELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVsGGAPLPPELLERFEEAPGIKLVNGYGLTETGGT 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  747 ASLARVAEHAR--PTIGRALANVDLHVVDGLGRRKTRGASGELWIGGAGVARGYAGDAgEAAGRFVEEGWpgsgrlYRSG 824
Cdd:cd04433  155 VATGPPDDDARkpGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNP-EATAAVDEDGW------YRTG 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  825 DLVRWRADGCLEFLGRIDEQVKINGYRIELGEIRSALLEHPAVGEAAVL-TDEADAAEpgadrRIVAFVTAAE-ETADES 902
Cdd:cd04433  228 DLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVgVPDPEWGE-----RVVAVVVLRPgADLDAE 302


                 ..
gi 15597498  903 WL 904
Cdd:cd04433  303 EL 304
Condensation pfam00668
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ...
 1359-1779 2.20e-51

Condensation domain; This domain is found in many multi-domain enzymes which synthesize peptide antibiotics. This domain catalyzes a condensation reaction to form peptide bonds in non- ribosomal peptide biosynthesis. It is usually found to the carboxy side of a phosphopantetheine binding domain (pfam00550). It has been shown that mutations in the HHXXXDG motif abolish activity suggesting this is part of the active site.


Pssm-ID: 395541 [Multi-domain]  Cd Length: 454  Bit Score: 189.08  E-value: 2.20e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   1359 DAYPMTSLQQGMLLQSEASGDPRLLHNVVLHEVHGRLDGELLARAWAILIGRHAILRTGFDLHGGQVPLQWVHPAtaVAA 1438
Cdd:pfam00668    3 DEYPLSPAQKRMWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIRQENGEPVQVILEE--RPF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   1439 EVPVHDLCGLDGETRRLRLRAWIEEEQATPFDWSRPPLVRLAALALDERRFALGVAEHHSVLDGWSLQSLVDELLAVYAD 1518
Cdd:pfam00668   81 ELEIIDISDLSESEEEEAIEAFIQRDLQSPFDLEKGPLFRAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLYQQ 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   1519 LLAGvvaREAEAPAV-GFRDYVALER---EAEANAASALFWLDYLAG-ARYRPLPGLAEEGP-RRMAA--VRVDVPADSL 1590
Cdd:pfam00668  161 LLKG---EPLPLPPKtPYKDYAEWLQqylQSEDYQKDAAYWLEQLEGeLPVLQLPKDYARPAdRSFKGdrLSFTLDEDTE 237

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   1591 SRLRALAERSGLPLRSLLLAAHGRALCRFSDADEVVTGFVSHGRPeEPGADRLLGLFLNTLPCRL--SASVDLLDSARRA 1668
Cdd:pfam00668  238 ELLRKLAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRP-SPDIERMVGMFVNTLPLRIdpKGGKTFSELIKRV 316

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   1669 FDYERASLEHRRHPLAAIRRR-------NRELRLDSLFNF---------VDFHQDDAAPAGVRhggildqvvvdVDVPLA 1732
Cdd:pfam00668  317 QEDLLSAEPHQGYPFGDLVNDlrlprdlSRHPLFDPMFSFqnylgqdsqEEEFQLSELDLSVS-----------SVIEEE 385

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|...
gi 15597498   1733 VDFEVA------GERLEVGFQYAAGRFPAERAEALAGAYREALLALLGDPVQP 1779
Cdd:pfam00668  386 AKYDLSltaserGGGLTIKIDYNTSLFDEETIERFAEHFKELLEQAIAHPSQP 438
PRK12467 PRK12467
peptide synthase; Provisional
 1199-1825 6.34e-51

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 200.39  E-value: 6.34e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1199 ALRGFLEARLPAYMLPSRIARVERLPLTAEGKLDRRALLAALAAEAAAQTLEaPANATEAALLEIWKSVLKRPAIGVSDN 1278
Cdd:PRK12467  975 ELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKALPKPDASAVQATFVA-PQTELEKRLAAIWADVLKVERVGLTDN 1053

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1279 FFQVGGDSirLIQMQVMAR---EAGLAFTLRDVFNHQSIRELARLLAaPASPADALGTSAPQSLEPFALLSAAERKRLPE 1355
Cdd:PRK12467 1054 FFELGGHS--LLATQVISRvrqRLGIQVPLRTLFEHQTLAGFAQAVA-AQQQGAQPALPDVDRDQPLPLSYAQERQWFLW 1130

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1356 GLDDaypmtslqqgmllQSEASGDPRLLhnvvlhEVHGRLDGELLARAWAILIGRHAILRTGFDLHGGQvPLQWVHPATA 1435
Cdd:PRK12467 1131 QLEP-------------GSAAYHIPQAL------RLKGPLDIEALERSFDALVARHESLRTTFVQEDGR-TRQVIHPVGS 1190

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1436 VAAEVPVHDLCGLDGEtrrlRLRAWIEEEQATPFDWSRPPLVRLAALALDERRFALGVAEHHSVLDGWSLQSLVDELLAV 1515
Cdd:PRK12467 1191 LTLEEPLLLAADKDEA----QLKVYVEAEARQPFDLEQGPLLRVGLLRLAADEHVLVLTLHHIVSDGWSMQVLVDELVAL 1266

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1516 YADLLAGVVAREAEAPaVGFRDYVALEREAEANAASA---LFWLDYLAGAryRPLPGLAEEGPR------RMAAVRVDVP 1586
Cdd:PRK12467 1267 YAAYSQGQSLQLPALP-IQYADYAVWQRQWMDAGERArqlAYWKAQLGGE--QPVLELPTDRPRpavqshRGARLAFELP 1343

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1587 ADSLSRLRALAERSGLPLRSLLLAAHGRALCRFSDADEVVTGFVSHGRPEEPgADRLLGLFLNTLPcrLSASVDLLDSAR 1666
Cdd:PRK12467 1344 PALAEGLRALARREGVTLFMLLLASFQTLLHRYSGQDDIRVGVPIANRNRAE-TEGLIGFFVNTQV--LRAEVDGQASFQ 1420

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1667 RAF-DYERASLEHRRH------PLAAIRRRNRELRLDSLFNFV-----DFHQDDAAPAGVRHGGILDQVVVDVDVPLAVD 1734
Cdd:PRK12467 1421 QLLqQVKQAALEAQAHqdlpfeQLVEALQPERSLSHSPLFQVMfnhqrDDHQAQAQLPGLSVESLSWESQTAQFDLTLDT 1500

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1735 FEvAGERLEVGFQYAAGRFPAERAEALAGAYREALLALLGDPVQPPAAAQAEDSVELRRVLKVLSrvlgrplAADQGFAS 1814
Cdd:PRK12467 1501 YE-SSEGLQASLTYATDLFEASTIERLAGHWLNLLQGLVADPERRLGELDLLDEAERRQILEGWN-------ATHTGYPL 1572

                         650
                  ....*....|..
gi 15597498  1815 AGG-HSLLGVQA 1825
Cdd:PRK12467 1573 ARLvHQLIEDQA 1584
PRK12316 PRK12316
peptide synthase; Provisional
 1192-1804 2.79e-50

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 198.26  E-value: 2.79e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1192 GGELSEQALRGFLEARLPAYMLPSRIARVERLPLTAEGKLDRRALLAALAAEAAAQTLEaPANATEAALLEIWKSVLKRP 1271
Cdd:PRK12316 2454 AAEDLLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALPKPDVSQLRQAYVA-PQEGLEQRLAAIWQAVLKVE 2532

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1272 AIGVSDNFFQVGGDSIRLIQMQVMAREA-GLAFTLRDVFNHQSIRELARLLAAPASpADALGTSAPQSLEPFALLSAAER 1350
Cdd:PRK12316 2533 QVGLDDHFFELGGHSLLATQVVSRVRQDlGLEVPLRILFERPTLAAFAASLESGQT-SRAPVLQKVTRVQPLPLSHAQQR 2611

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1351 KRLPEGLDDaypmtslqqgmllQSEASGDPRLLHnvvlheVHGRLDGELLARAWAILIGRHAILRTGFDLHGGQVpLQWV 1430
Cdd:PRK12316 2612 QWFLWQLEP-------------ESAAYHLPSALH------LRGVLDQAALEQAFDALVLRHETLRTRFVEVGEQT-RQVI 2671

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1431 HPATAVAaEVPVHDLCGLDGetrrlRLRAWIEEEQATPFDWSRPPLVRLAALALDERRFALGVAEHHSVLDGWSLQSLVD 1510
Cdd:PRK12316 2672 LPNMSLR-IVLEDCAGVADA-----AIRQRVAEEIQRPFDLARGPLLRVRLLALDGQEHVLVITQHHIVSDGWSMQVMVD 2745

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1511 ELLAVYADLLAGVVAREAEAPaVGFRDYVALER---EAEANAASALFWLDYLAGARY-------RPLPGLAEegpRRMAA 1580
Cdd:PRK12316 2746 ELVQAYAGARRGEQPTLPPLP-LQYADYAAWQRawmDSGEGARQLDYWRERLGGEQPvlelpldRPRPALQS---HRGAR 2821

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1581 VRVDVPADSLSRLRALAERSGLPLRSLLLAAHGRALCRFSDADEVVTGFVSHGRpEEPGADRLLGLFLNTLPCRLS---- 1656
Cdd:PRK12316 2822 LDVALDVALSRELLALARREGVTLFMLLLASFQVLLHRYSGQSDIRVGVPIANR-NRAETERLIGFFVNTQVLRAQvdaq 2900

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1657 -ASVDLLDSARRAFDYERASLEHRRHPLAAIRRRNRELRLDSLFNFVDFHQD---DAAPAGVRHGGILDQVVVDVDVPLA 1732
Cdd:PRK12316 2901 lAFRDLLGQVKEQALGAQAHQDLPFEQLVEALQPERSLSHSPLFQVMYNHQSgerAAAQLPGLHIESFAWDGAATQFDLA 2980

                         570       580       590       600       610       620       630
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15597498  1733 VDFEVAGERLEVGFQYAAGRFPAERAEALAGAYREALLALLGDPVQPPAAAQAEDSVELRRVLKVLSRVLGR 1804
Cdd:PRK12316 2981 LDTWESAEGLGASLTYATDLFDARTVERLARHWQNLLRGMVENPQRSVDELAMLDAEERGQLLEAWNATAAE 3052
CT_NRPS-like cd19542
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ...
 1361-1776 3.71e-48

Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike bacterial NRPS, which typically have specialized terminal thioesterase (TE) domains to cyclize peptide products, many fungal NRPSs employ a terminal condensation-like (CT) domain to produce macrocyclic peptidyl products (e.g. cyclosporine and echinocandin). Domains in this subfamily (which includes both terminal and non-terminal domains) typically have a non-canonical conserved [SN]HxxxDx(14)Y motif at their active site compared to the standard Condensation (C) domain active site motif (HHxxxD). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380464 [Multi-domain]  Cd Length: 401  Bit Score: 178.27  E-value: 3.71e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1361 YPMTSLQQGMLLQSEASGdPRLLHNVVLHeVHGRLDGELLARAWAILIGRHAILRTGFDLHGGQVPLQWVhpaTAVAAEV 1440
Cdd:cd19542    2 YPCTPMQEGMLLSQLRSP-GLYFNHFVFD-LDSSVDVERLRNAWRQLVQRHDILRTVFVESSAEGTFLQV---VLKSLDP 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1441 PVHDLcgldgETRRLRLRAWIEEEQATPFDWSRPPL-VRLAALALDERRFALGVaeHHSVLDGWSLQSLVDELLAVYADL 1519
Cdd:cd19542   77 PIEEV-----ETDEDSLDALTRDLLDDPTLFGQPPHrLTLLETSSGEVYLVLRI--SHALYDGVSLPIILRDLAAAYNGQ 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1520 LagvvareaEAPAVGFRDYVALEREAEANAASAlFWLDYLAGARYRPLPGLAeegPRRMAAVRVDVPADSLSRLRALAER 1599
Cdd:cd19542  150 L--------LPPAPPFSDYISYLQSQSQEESLQ-YWRKYLQGASPCAFPSLS---PKRPAERSLSSTRRSLAKLEAFCAS 217

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1600 SGLPLRSLLLAAHGRALCRFSDADEVVTGFVSHGR--PeEPGADRLLGLFLNTLPCRL----SASV-DLLDSARRAFDye 1672
Cdd:cd19542  218 LGVTLASLFQAAWALVLARYTGSRDVVFGYVVSGRdlP-VPGIDDIVGPCINTLPVRVkldpDWTVlDLLRQLQQQYL-- 294

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1673 rASLEHRRHPLAAIRRRNRELRLDSLFN-FVDFHQDDAAPAGVRHGGILDQVVVDVDVPL---AVDFEVAGERLEVGFQY 1748
Cdd:cd19542  295 -RSLPHQHLSLREIQRALGLWPSGTLFNtLVSYQNFEASPESELSGSSVFELSAAEDPTEypvAVEVEPSGDSLKVSLAY 373

                        410       420
                 ....*....|....*....|....*...
gi 15597498 1749 AAGRFPAERAEALAGAYREALLALLGDP 1776
Cdd:cd19542  374 STSVLSEEQAEELLEQFDDILEALLANP 401
PRK04813 PRK04813
D-alanine--poly(phosphoribitol) ligase subunit DltA;
449-873 2.25e-43

D-alanine--poly(phosphoribitol) ligase subunit DltA;


Pssm-ID: 235313 [Multi-domain]  Cd Length: 503  Bit Score: 166.99  E-value: 2.25e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   449 SLVAAFDLRAALQPQAPALLDAHGSLDFATLRARSEAVAEALLAAGVRPGQAVAVMTGRNREAIVALLGVMRAAAVYTPV 528
Cdd:PRK04813    3 DIIETIEEFAQTQPDFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIPV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   529 NPEFPAARVERMREAGG--IVFALADAEcagrareafagacLDLSTLP------LAGSGMSLPAP------GGRDAAYMI 594
Cdd:PRK04813   83 DVSSPAERIEMIIEVAKpsLIIATEELP-------------LEILGIPvitldeLKDIFATGNPYdfdhavKGDDNYYII 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   595 FTSGTSGQPKGVVVEHASALNLSQALartVYANVVGEGLRVTVNAPFSFDSSIKQI-LQLLSGHCLVLVPQEVRSDPQRM 673
Cdd:PRK04813  150 FTSGTTGKPKGVQISHDNLVSFTNWM---LEDFALPEGPQFLNQAPYSFDLSVMDLyPTLASGGTLVALPKDMTANFKQL 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   674 LGFLEERRIDVLDCTPSLFRL-LLQAGLDDAH-PALPgRILVGGE------------RFDEAswevaagwrrcQVFNLYG 739
Cdd:PRK04813  227 FETLPQLPINVWVSTPSFADMcLLDPSFNEEHlPNLT-HFLFCGEelphktakklleRFPSA-----------TIYNTYG 294

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   740 PTEATVNASLARV-----AEHARPTIGRALANVDLHVVDGLGRRKTRGASGELWIGGAGVARGYAGD-AGEAAGRFVEEG 813
Cdd:PRK04813  295 PTEATVAVTSIEItdemlDQYKRLPIGYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNpEKTAEAFFTFDG 374

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   814 WPGsgrlYRSGDLVRWrADGCLEFLGRIDEQVKINGYRIELGEIRSALLEHPAVGEAAVL 873
Cdd:PRK04813  375 QPA----YHTGDAGYL-EDGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVV 429
A_NRPS_acs4 cd17654
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ...
 499-893 7.24e-43

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: 164.18  E-value: 7.24e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  499 QAVAVMTGRNREAIVALLGVMRAAAVYTPVNPEFPAARVERMREAGGIVFALADaecaGRAREAFagacldlSTLPLAGS 578
Cdd:cd17654   42 RAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVMKKCHVSYLLQN----KELDNAP-------LSFTPEHR 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  579 GMSLPAPGGrdAAYMIFTSGTSGQPKGVVVEHASALNLSQALARTVyaNVVGEGLRVTVNaPFSFDSSIKQI-LQLLSGH 657
Cdd:cd17654  111 HFNIRTDEC--LAYVIHTSGTTGTPKIVAVPHKCILPNIQHFRSLF--NITSEDILFLTS-PLTFDPSVVEIfLSLSSGA 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  658 CLVLVPQEVRSDPQRMLGFLEER-RIDVLDCTPSLFRLLLQAGLDD----AHPALpgRIL-VGGERFdeASWEVAAGWR- 730
Cdd:cd17654  186 TLLIVPTSVKVLPSKLADILFKRhRITVLQATPTLFRRFGSQSIKStvlsATSSL--RVLaLGGEPF--PSLVILSSWRg 261

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  731 ---RCQVFNLYGPTEATVNASLARVAEHARPT-IGRALANVDLHVVDGLGRRKTrgasGELWIGGagVARGYAGDAgeaa 806
Cdd:cd17654  262 kgnRTRIFNIYGITEVSCWALAYKVPEEDSPVqLGSPLLGTVIEVRDQNGSEGT----GQVFLGG--LNRVCILDD---- 331

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  807 grfvEEGWPgSGRLYRSGDLVRwRADGCLEFLGRIDEQVKINGYRIELGEIRSALLEHPAVGEAAVLTDEadaaepgaDR 886
Cdd:cd17654  332 ----EVTVP-KGTMRATGDFVT-VKDGELFFLGRKDSQIKRRGKRINLDLIQQVIESCLGVESCAVTLSD--------QQ 397


                 ....*..
gi 15597498  887 RIVAFVT 893
Cdd:cd17654  398 RLIAFIV 404
PRK12316 PRK12316
peptide synthase; Provisional
 1132-1773 2.19e-42

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 172.45  E-value: 2.19e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1132 RADALSDLLRRHGFEVSIRqDALLEGTDRYNCYAVRPGYAESLAERIDWRALAPRPAAALGGELSEQALRGFLEARLPAY 1211
Cdd:PRK12316 3435 RADGVIEYIGRVDHQVKIR-GFRIELGEIEARLLEHPWVREAVVLAVDGRQLVAYVVPEDEAGDLREALKAHLKASLPEY 3513

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1212 MLPSRIARVERLPLTAEGKLDRRALLAALAAEAAAQTLEaPANATEAALLEIWKSVLKRPAIGVSDNFFQVGGDSIRLIQ 1291
Cdd:PRK12316 3514 MVPAHLLFLERMPLTPNGKLDRKALPRPDAALLQQDYVA-PVNELERRLAAIWADVLKLEQVGLTDNFFELGGDSIISLQ 3592

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1292 MQVMAREAGLAFTLRDVFNHQSIRELARLLAAPASPA-DALGTSAPQSLEPFallsaaerkrlpeglddaypmtslQQGM 1370
Cdd:PRK12316 3593 VVSRARQAGIRFTPKDLFQHQTIQGLARVARVGGGVAvDQGPVSGETLLLPI------------------------QQQF 3648

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1371 LlqSEASGDPRLLHNVVLHEVHGRLDGELLARAWAILIGRHAILRTGFDlhggQVPLQWvhpaTAVAAEVPVHDLCGLDG 1450
Cdd:PRK12316 3649 F--EEPVPERHHWNQSLLLKPREALDAAALEAALQALVEHHDALRLRFV----EDAGGW----TAEHLPVELGGALLWRA 3718

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1451 ETRRLRLRAWIEEEQATPFDWSRPPLVR--LAALALDERRFALgvAEHHSVLDGWSLQSLVDELLAVYADLLAGvvaREA 1528
Cdd:PRK12316 3719 ELDDAEELERLGEEAQRSLDLADGPLLRalLATLADGSQRLLL--VIHHLVVDGVSWRILLEDLQQAYQQLLQG---EAP 3793

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1529 EAPA--VGFRDYVALERE---AEANAASALFWLDYLAGARYRpLPGLAEEGPRRMAAVRVDVPADSLSRLRALAERSGLP 1603
Cdd:PRK12316 3794 RLPAktSSFKAWAERLQEharGEALKAELAYWQEQLQGVSSE-LPCDHPQGALQNRHAASVQTRLDRELTRRLLQQAPAA 3872

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1604 LRS----LLLAAHGRALCRFSDADEVVTGFVSHGRpEEPGAD----RLLGLFLNTLPCRLSASVDLLDSARRAFDYERAS 1675
Cdd:PRK12316 3873 YRTqvndLLLTALARVVCRWTGEASALVQLEGHGR-EDLFADidlsRTVGWFTSLFPVRLSPVEDLGASIKAIKEQLRAI 3951

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1676 LEH-------RRHPLAAIRRRNRELRLDSL-FNFV-------DFHQDDAAPAGVRHGGILDQVVVDVDVPLAVDfEVAGE 1740
Cdd:PRK12316 3952 PNKgigfgllRYLGDEESRRTLAGLPVPRItFNYLgqfdgsfDEEMALFVPAGESAGAEQSPDAPLDNWLSLNG-RVYGG 4030

                         650       660       670
                  ....*....|....*....|....*....|...
gi 15597498  1741 RLEVGFQYAAGRFPAERAEALAGAYREALLALL 1773
Cdd:PRK12316 4031 ELSLDWTFSREMFEEATIQRLADDYAAELTALV 4063
SgcC5_NRPS-like cd19539
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ...
 1365-1776 8.28e-42

SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- bond forming activity and similar C-domains of modular NRPSs; SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. This subfamily also includes similar C-domains of modular NRPSs such as Penicillium chrysogenum N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase PCBAB. Condensation (C) domains of NRPSs normally catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380462 [Multi-domain]  Cd Length: 427  Bit Score: 160.24  E-value: 8.28e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1365 SLQQGMLLQSEASGDPRLLHNVVL-HEVHGRLDGELLARAWAILIGRHAILRTGFDLHGGQVPLQWVHPATAvaAEVPVH 1443
Cdd:cd19539    5 SFAQERLWFIDQGEDGGPAYNIPGaWRLTGPLDVEALREALRDVVARHEALRTLLVRDDGGVPRQEILPPGP--APLEVR 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1444 DLCGLDGETRRlRLRAWIEEEQATPFDWSRPPLVRLAALALDERRFALGVAEHHSVLDGWSLQSLVDELLAVYADLLAGV 1523
Cdd:cd19539   83 DLSDPDSDRER-RLEELLRERESRGFDLDEEPPIRAVLGRFDPDDHVLVLVAHHTAFDAWSLDVFARDLAALYAARRKGP 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1524 VAREAEaPAVGFRDYVALERE---AEANAASALFWLDYLAGARYRPLPG---LAEEGPRRMAAVRVDVPADSLSRLRALA 1597
Cdd:cd19539  162 AAPLPE-LRQQYKEYAAWQREalaAPRAAELLDFWRRRLRGAEPTALPTdrpRPAGFPYPGADLRFELDAELVAALRELA 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1598 ERSGLPLRSLLLAAHGRALCRFSDADEVVTGFVSHGRPeEPGADRLLGLFLNTLPCRL-----SASVDLLDSARR----A 1668
Cdd:cd19539  241 KRARSSLFMVLLAAYCVLLRRYTGQTDIVVGTPVAGRN-HPRFESTVGFFVNLLPLRVdvsdcATFRDLIARVRKalvdA 319

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1669 FDYERASLEHRRHPLAAIRRRNRELRLDSLFNFVDF---HQDDAAPAGVRHGgilDQVVVDVDVPLAVDFEVAGERLEVG 1745
Cdd:cd19539  320 QRHQELPFQQLVAELPVDRDAGRHPLVQIVFQVTNApagELELAGGLSYTEG---SDIPDGAKFDLNLTVTEEGTGLRGS 396

                        410       420       430
                 ....*....|....*....|....*....|.
gi 15597498 1746 FQYAAGRFPAERAEALAGAYREALLALLGDP 1776
Cdd:cd19539  397 LGYATSLFDEETIQGFLADYLQVLRQLLANP 427
LCL_NRPS-like cd19531
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ...
 1391-1776 2.96e-41

LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar domains including the C-domain of SgcC5, a free-standing NRPS with both ester- and amide- bond forming activity; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. Streptomyces globisporus SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380454 [Multi-domain]  Cd Length: 427  Bit Score: 158.67  E-value: 2.96e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1391 VHGRLDGELLARAWAILIGRHAILRTGFDLHGGQvPLQWVHPATAVaaEVPVHDLCGLDGETRRLRLRAWIEEEQATPFD 1470
Cdd:cd19531   32 LRGPLDVAALERALNELVARHEALRTTFVEVDGE-PVQVILPPLPL--PLPVVDLSGLPEAEREAEAQRLAREEARRPFD 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1471 WSRPPLVRLAALALDERRFALGVAEHHSVLDGWSLQSLVDELLAVYADLLAGVVAREAEaPAVGFRDYVALERE---AEA 1547
Cdd:cd19531  109 LARGPLLRATLLRLGEDEHVLLLTMHHIVSDGWSMGVLLRELAALYAAFLAGRPSPLPP-LPIQYADYAVWQREwlqGEV 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1548 NAASALFWLDYLAGAryRPLPGLAEEGPR------RMAAVRVDVPADSLSRLRALAERSGLPLRSLLLAAHGRALCRFSD 1621
Cdd:cd19531  188 LERQLAYWREQLAGA--PPVLELPTDRPRpavqsfRGARVRFTLPAELTAALRALARREGATLFMTLLAAFQVLLHRYSG 265

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1622 ADEVVTGFVSHGRPeEPGADRLLGLFLNTLP--CRLSAS---VDLLDSARR----AFDYERASLEH-----------RRH 1681
Cdd:cd19531  266 QDDIVVGTPVAGRN-RAELEGLIGFFVNTLVlrTDLSGDptfRELLARVREtaleAYAHQDLPFEKlvealqperdlSRS 344

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1682 PLAairrrnrelrlDSLFNFVDFHQDDAAPAGVRhggildqVVVDVDVPLAVDFEVA------GERLEVGFQYAAGRFPA 1755
Cdd:cd19531  345 PLF-----------QVMFVLQNAPAAALELPGLT-------VEPLEVDSGTAKFDLTlsltetDGGLRGSLEYNTDLFDA 406

                        410       420
                 ....*....|....*....|.
gi 15597498 1756 ERAEALAGAYREALLALLGDP 1776
Cdd:cd19531  407 ATIERMAGHFQTLLEAIVADP 427
COG4908 COG4908
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ...
 1363-1601 6.60e-41

Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];


Pssm-ID: 443936 [Multi-domain]  Cd Length: 243  Bit Score: 152.11  E-value: 6.60e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1363 MTSLQQGMLlqsEASGDPRLLHNVVLHEVHGRLDGELLARAWAILIGRHAILRTGFDLHGGQvPLQWVHPAtaVAAEVPV 1442
Cdd:COG4908    1 LSPAQKRFL---FLEPGSNAYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFVEEDGE-PVQRIDPD--ADLPLEV 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1443 HDLCGLDGETRRLRLRAWIEEEQATPFDWSRPPLVRLAALALDERRFALGVAEHHSVLDGWSLQSLVDELLAVYADLLAG 1522
Cdd:COG4908   75 VDLSALPEPEREAELEELVAEEASRPFDLARGPLLRAALIRLGEDEHVLLLTIHHIISDGWSLGILLRELAALYAALLEG 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1523 VVAREAEAPaVGFRDYVALEREA---EANAASALFWLDYLAGA-RYRPLPGLAEEGPRRM---AAVRVDVPADSLSRLRA 1595
Cdd:COG4908  155 EPPPLPELP-IQYADYAAWQRAWlqsEALEKQLEYWRQQLAGApPVLELPTDRPRPAVQTfrgATLSFTLPAELTEALKA 233


                 ....*.
gi 15597498 1596 LAERSG 1601
Cdd:COG4908  234 LAKAHG 239
C_NRPS-like cd19066
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ...
 1361-1776 2.90e-40

Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long, with various activities such as antibiotic, antifungal, antitumor and immunosuppression. There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380453 [Multi-domain]  Cd Length: 427  Bit Score: 156.03  E-value: 2.90e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1361 YPMTSLQQGMLLQSEASGDPRLLHNVVLHEVHGRLDGELLARAWAILIGRHAILRTGFdLHGGQVPLQWVHPATaVAAEV 1440
Cdd:cd19066    2 IPLSPMQRGMWFLKKLATDPSAFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRF-CEEAGRYEQVVLDKT-VRFRI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1441 PVHDLCGLDgeTRRLRLRAWIEEEQATPFDWSRPPLVRLAALALDERRFALGVAEHHSVLDGWSLQSLVDELLAVYADLL 1520
Cdd:cd19066   80 EIIDLRNLA--DPEARLLELIDQIQQTIYDLERGPLVRVALFRLADERDVLVVAIHHIIVDGGSFQILFEDISSVYDAAE 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1521 AGvvAREAEAPAVGFRDYVA-LE--REAEANAASALFWLDYLAG-ARYRPLPGLAEEGPRRMAAVRV---DVPADSLSRL 1593
Cdd:cd19066  158 RQ--KPTLPPPVGSYADYAAwLEkqLESEAAQADLAYWTSYLHGlPPPLPLPKAKRPSQVASYEVLTlefFLRSEETKRL 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1594 RALAERSGLPLRSLLLAAHGRALCRFSDADEVVTGFVSHGRPeEPGADRLLGLFLNTLPCRLSASVD---------LLDS 1664
Cdd:cd19066  236 REVARESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRP-DEAVEDTIGLFLNLLPLRIDTSPDatfpellkrTKEQ 314

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1665 ARRAFDYERASLEHRRHPLAAIRRRNRELRLDSLFNFVDFHQDDAAPAGVRHGGILDQVVVDVDVPLAVDF--EVAGErL 1742
Cdd:cd19066  315 SREAIEHQRVPFIELVRHLGVVPEAPKHPLFEPVFTFKNNQQQLGKTGGFIFTTPVYTSSEGTVFDLDLEAseDPDGD-L 393

                        410       420       430
                 ....*....|....*....|....*....|....
gi 15597498 1743 EVGFQYAAGRFPAERAEALAGAYREALLALLGDP 1776
Cdd:cd19066  394 LLRLEYSRGVYDERTIDRFAERYMTALRQLIENP 427
Acs COG0365
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
453-908 4.64e-40

Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];


Pssm-ID: 440134 [Multi-domain]  Cd Length: 565  Bit Score: 158.35  E-value: 4.64e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  453 AFDLRAALQPQAPALL-----DAHGSLDFATLRARSEAVAEALLAAGVRPGQAVAVMTGRNREAIVALLGVMRAAAVYTP 527
Cdd:COG0365   14 CLDRHAEGRGDKVALIwegedGEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSP 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  528 VNPEF-PAARVERMREAGgIVFALADAECAGRAR-----EAFAGACLDLSTLP----LAGSGMSLPAPGGR--------- 588
Cdd:COG0365   94 VFPGFgAEALADRIEDAE-AKVLITADGGLRGGKvidlkEKVDEALEELPSLEhvivVGRTGADVPMEGDLdwdellaaa 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  589 ------------DAAYMIFTSGTSGQPKGVVveHASALNLSQALARTVYANVVGEGLRVTVNAPFSF---DSSIkQILQL 653
Cdd:COG0365  173 saefepeptdadDPLFILYTSGTTGKPKGVV--HTHGGYLVHAATTAKYVLDLKPGDVFWCTADIGWatgHSYI-VYGPL 249

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  654 LSGHCLVLVP-QEVRSDPQRMLGFLEERRIDVLDCTPSLFRLLLQAGLDDAH----PALpgRILV-GGERFDEASWEVaa 727
Cdd:COG0365  250 LNGATVVLYEgRPDFPDPGRLWELIEKYGVTVFFTAPTAIRALMKAGDEPLKkydlSSL--RLLGsAGEPLNPEVWEW-- 325

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  728 gWRR---CQVFNLYGPTEATVNASLARVAEHARP-TIGRALANVDLHVVDGLGRRKTRGASGELWIGGA--GVARGYAGD 801
Cdd:COG0365  326 -WYEavgVPIVDGWGQTETGGIFISNLPGLPVKPgSMGKPVPGYDVAVVDEDGNPVPPGEEGELVIKGPwpGMFRGYWND 404

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  802 AGeaagRFVEEGWPGSGRLYRSGDLVRWRADGCLEFLGRIDEQVKINGYRIELGEIRSALLEHPAVGEAAVLtdeadaAE 881
Cdd:COG0365  405 PE----RYRETYFGRFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVV------GV 474

                        490       500
                 ....*....|....*....|....*....
gi 15597498  882 PGADR--RIVAFVTAAEETADESWLEVDL 908
Cdd:COG0365  475 PDEIRgqVVKAFVVLKPGVEPSDELAKEL 503
Firefly_Luc_like cd05911
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ...
 466-884 9.39e-40

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: 155.83  E-value: 9.39e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  466 ALLDAHG--SLDFATLRARSEAVAEALLAAGVRPGQAVAVMTGRNREAIVALLGVMRAAAVYTPVNPEFPAARVERMREA 543
Cdd:cd05911    1 AQIDADTgkELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  544 GG--IVF--------ALADAECAG--------RAREAFAGACLDLSTLPLAGSGMSLPAP---GGRDAAYMIFTSGTSGQ 602
Cdd:cd05911   81 SKpkVIFtdpdglekVKEAAKELGpkdkiivlDDKPDGVLSIEDLLSPTLGEEDEDLPPPlkdGKDDTAAILYSSGTTGL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  603 PKGVVVEHASAL-NLSQALARTVYANVVGEglrvTVNAPFSFDSS---IKQILQLLSGHCLVLVPqevRSDPQRMLGFLE 678
Cdd:cd05911  161 PKGVCLSHRNLIaNLSQVQTFLYGNDGSND----VILGFLPLYHIyglFTTLASLLNGATVIIMP---KFDSELFLDLIE 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  679 ERRIDVLDCTPSLFRLLLQAGLDDAHpALPG--RILVGG----ERFDEaswEVAAGWRRCQVFNLYGPTEATVNASLARV 752
Cdd:cd05911  234 KYKITFLYLVPPIAAALAKSPLLDKY-DLSSlrVILSGGaplsKELQE---LLAKRFPNATIKQGYGMTETGGILTVNPD 309

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  753 AEHARPTIGRALANVDLHVVDGLGRRKT-RGASGELWIGGAGVARGYAGDAGEAAGRFVEEGWpgsgrlYRSGDLVRWRA 831
Cdd:cd05911  310 GDDKPGSVGRLLPNVEAKIVDDDGKDSLgPNEPGEICVRGPQVMKGYYNNPEATKETFDEDGW------LHTGDIGYFDE 383

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 15597498  832 DGCLEFLGRIDEQVKINGYRIELGEIRSALLEHPAVGEAAV--LTDEADAAEPGA 884
Cdd:cd05911  384 DGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVigIPDEVSGELPRA 438
PRK12467 PRK12467
peptide synthase; Provisional
 1199-1774 1.69e-38

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 159.56  E-value: 1.69e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1199 ALRGFLEARLPAYMLPSRIARVERLPLTAEGKLDRRALLAALAAEAAAQTLEaPANATEAALLEIWKSVLKRPAIGVSDN 1278
Cdd:PRK12467 2042 ILKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKALPAPDASELQQAYVA-PQSELEQRLAAIWQDVLGLEQVGLHDN 2120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1279 FFQVGGDSIRLIQMQVMAREAGLAFTLRDVFNHQSIRELArllaAPASPADAlGTSAPQSlepfallsaaerkrlpeGLD 1358
Cdd:PRK12467 2121 FFELGGDSIISIQVVSRARQAGIRFTPKDLFQHQTVQSLA----AVAQEGDG-TVSIDQG-----------------PVT 2178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1359 DAYPMTSLQQgmLLQSEASGDPRLLHNVVLHEVHGRLDGELLARAWAILIGRHAILRTGFDLHGGQVPLQWVHPATAVAA 1438
Cdd:PRK12467 2179 GDLPLLPIQQ--MFFADDIPERHHWNQSVLLEPREALDAELLEAALQALLVHHDALRLGFVQEDGGWSAMHRAPEQERRP 2256

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1439 ---EVPVHDlcglDGEtrrlrLRAWIEEEQATpFDWSRPPLVR--LAALALDERRFALGVaeHHSVLDGWSLQSLVDELL 1513
Cdd:PRK12467 2257 llwQVVVAD----KEE-----LEALCEQAQRS-LDLEEGPLLRavLATLPDGSQRLLLVI--HHLVVDGVSWRILLEDLQ 2324

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1514 AVYADLLAG-VVAREAEAPAvgFRDYVA-LEREAE--ANAASALFWLDYLAGARyRPLPGLAEEGP---RRMAAVRVDVP 1586
Cdd:PRK12467 2325 TAYRQLQGGqPVKLPAKTSA--FKAWAErLQTYAAsaALADELGYWQAQLQGAS-TELPCDHPQGGlqrRHAASVTTHLD 2401

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1587 ADSLSRLRALAERS-GLPLRSLLLAAHGRALCRFSDADEVVTGFVSHGRPE-EPGAD--RLLGLFLNTLPCRLSASVDLL 1662
Cdd:PRK12467 2402 SEWTRRLLQEAPAAyRTQVNDLLLTALARVIARWTGQASTLIQLEGHGREDlFDEIDltRTVGWFTSLYPVKLSPTASLA 2481

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1663 DSARRAFDYERASLEH-------RRHPLAAIRRRNREL-RLDSLFNFV-----DFHQDDAA---PAGVRHGGiLDQVVVD 1726
Cdd:PRK12467 2482 TSIKTIKEQLRAVPNKglgfgvlRYLGSEAARQTLQALpVPRITFNYLgqfdgSFDAEKQAlfvPSGEFSGA-EQSEEAP 2560

                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....*...
gi 15597498  1727 VDVPLAVDFEVAGERLEVGFQYAAGRFPAERAEALAGAYREALLALLG 1774
Cdd:PRK12467 2561 LGNWLSINGQVYGGELNLGWTFSQEMFDEATIQRLADAYAEELRALIE 2608
PRK05691 PRK05691
peptide synthase; Validated
 1198-1774 2.03e-37

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 155.71  E-value: 2.03e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1198 QALRGFLEARLPAYMLPSRIARVERLPLTAEGKLDRRALLAALAAEAAAQTLEaPANATEAALLEIWKSVLKRPAIGVSD 1277
Cdd:PRK05691 2653 EALKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRALPAPDPELNRQAYQA-PRSELEQQLAQIWREVLNVERVGLGD 2731

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1278 NFFQVGGDSIRLIQMQVMAREAGLAFTLRDVFNHQSIRELARLLAAPASPADALGTsapqslepfallsaaerkrlpegL 1357
Cdd:PRK05691 2732 NFFELGGDSILSIQVVSRARQLGIHFSPRDLFQHQTVQTLAAVATHSEAAQAEQGP-----------------------L 2788

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1358 DDAYPMTSLQQGMLLQSEAsgDPRLLHNVVLHEVHGRLDGELLARAWAILIGRHAILRTGFDLHGGqvplQWVHPATAVA 1437
Cdd:PRK05691 2789 QGASGLTPIQHWFFDSPVP--QPQHWNQALLLEPRQALDPALLEQALQALVEHHDALRLRFSQADG----RWQAEYRAVT 2862

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1438 AE-----VPVHDLCgldgetrrlRLRAWIEEEQATpFDWSRPPLVRLAALALDERRFALGVAEHHSVLDGWSLQSLVDEL 1512
Cdd:PRK05691 2863 AQellwqVTVADFA---------ECAALFADAQRS-LDLQQGPLLRALLVDGPQGQQRLLLAIHHLVVDGVSWRVLLEDL 2932

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1513 LAVYADLLAGVVAREAeAPAVGFRDYVAlEREAEANAASA----LFWLDYLAGARyRPLPGLAEEGPRRMA-----AVRV 1583
Cdd:PRK05691 2933 QALYRQLSAGAEPALP-AKTSAFRDWAA-RLQAYAGSESLreelGWWQAQLGGPR-AELPCDRPQGGNLNRhaqtvSVRL 3009

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1584 DVpadslSRLRALAERSGLPLRS----LLLAAHGRALCRFSDADEVVTGFVSHGRP---EEPGADRLLGLFLNTLPCRLS 1656
Cdd:PRK05691 3010 DA-----ERTRQLLQQAPAAYRTqvndLLLTALARVLCRWSGQPSVLVQLEGHGREalfDDIDLTRSVGWFTSAYPLRLT 3084

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1657 ASVdLLDSAR----RAFDYERASLEHR-------RHpLA--AIRRRNRELRLDSL-FNFV-DFHQ---DDA------APA 1712
Cdd:PRK05691 3085 PAP-GDDAARgesiKAIKEQLRAVPHKglgygvlRY-LAdaAVREAMAALPQAPItFNYLgQFDQsfaSDAlfrpldEPA 3162

                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15597498  1713 GVRHggildQVVVDVDVPLAVDFEVAGERLEVGFQYAAGRFPAERAEALAGAYREALLALLG 1774
Cdd:PRK05691 3163 GPAH-----DPDAPLPNELSVDGQVYGGELVLRWTYSAERYDEQTIAELAEAYLAELQALIA 3219
PRK12316 PRK12316
peptide synthase; Provisional
 1293-1804 2.24e-37

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 155.89  E-value: 2.24e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1293 QVMAREAGLAFTL-RDVFNHQSIRELA-----RLLAAPASPADALGTSAPQSLEPFALLSAAERKRLP---EGLDDAYPM 1363
Cdd:PRK12316 4026 RVYGGELSLDWTFsREMFEEATIQRLAddyaaELTALVEHCCDAERHGVTPSDFPLAGLDQARLDALPlplGEIEDIYPL 4105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1364 TSLQQGMLLQS---EASGDprlLHNVVLHEVHGrLDGELLARAWAILIGRHAILRTGFDLHGG-QVPLQWVHpaTAVAAE 1439
Cdd:PRK12316 4106 SPMQQGMLFHSlyeQEAGD---YINQMRVDVQG-LDVERFRAAWQAALDRHDVLRSGFVWQGElGRPLQVVH--KQVSLP 4179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1440 VPVHDLCGldGETRRLRLRAWIEEEQATPFDWSRPPLVRLAALALDERRFALGVAEHHSVLDGWSLQSLVDELLAVYAdl 1519
Cdd:PRK12316 4180 FAELDWRG--RADLQAALDALAAAERERGFDLQRAPLLRLVLVRTAEGRHHLIYTNHHILMDGWSNSQLLGEVLERYS-- 4255

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1520 lagvvAREAEAPAVGFRDYVALEREAEANAASAlFWLDYLAG--ARYRPLPGLAEEGPRRMAAV---RVDVPADSLSRLR 1594
Cdd:PRK12316 4256 -----GRPPAQPGGRYRDYIAWLQRQDAAASEA-FWREQLAAldEPTRLAQAIARADLRSANGYgehVRELDATATARLR 4329

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1595 ALAERSGLPLRSLLLAAHGRALCRFSDADEVVTGFVSHGRPEE-PGADRLLGLFLNTLPCRLSASVDL-LDSARRAFDYE 1672
Cdd:PRK12316 4330 EFARTQRVTLNTLVQAAWLLLLQRYTGQDTVAFGATVAGRPAElPGIEGQIGLFINTLPVIATPRAQQsVVEWLQQVQRQ 4409

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1673 RASL-EHRRHPLAAIRR---RNRELRLDSLFNF----VDFHQDDAAPAGVRHGGILDQVVVDVDVPLAVDFevaGERLEV 1744
Cdd:PRK12316 4410 NLALrEHEHTPLYEIQRwagQGGEALFDSLLVFenypVSEALQQGAPGGLRFGEVTNHEQTNYPLTLAVGL---GETLSL 4486

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1745 GFQYAAGRFPAERAEALAGAYREALLALLGDPVQPPAAAQAEDSVELRRVLKVLSRVLGR 1804
Cdd:PRK12316 4487 QFSYDRGHFDAATIERLARHLTNLLEAMAEDPQRRLGELQLLEKAEQQRIVALWNRTDAG 4546
FACL_FadD13-like cd17631
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ...
 454-873 4.10e-37

fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.


Pssm-ID: 341286 [Multi-domain]  Cd Length: 435  Bit Score: 146.60  E-value: 4.10e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  454 FDLRAALQPQAPALLDAHGSLDFATLRARSEAVAEALLAAGVRPGQAVAVMTGRNREAIVALLGVMRAAAVYTPVNPefp 533
Cdd:cd17631    1 LRRRARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNF--- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  534 aarverMREAGGIVFALADAEcagrareafAGACLDlstlplagsgmslpapggrDAAYMIFTSGTSGQPKGVVVEHAsa 613
Cdd:cd17631   78 ------RLTPPEVAYILADSG---------AKVLFD-------------------DLALLMYTSGTTGRPKGAMLTHR-- 121

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  614 lNLSQALARTVYANVVGEGLRVTVNAPFS--FDSSIKQILQLLSGHCLVLVPqevRSDPQRMLGFLEERRIDVLDCTPSL 691
Cdd:cd17631  122 -NLLWNAVNALAALDLGPDDVLLVVAPLFhiGGLGVFTLPTLLRGGTVVILR---KFDPETVLDLIERHRVTSFFLVPTM 197

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  692 FRLLLQaglddaHPALPGR-------ILVGGERFDEASweVAAGWRRCQVF-NLYGPTEATVNASLARVAEHARP--TIG 761
Cdd:cd17631  198 IQALLQ------HPRFATTdlsslraVIYGGAPMPERL--LRALQARGVKFvQGYGMTETSPGVTFLSPEDHRRKlgSAG 269

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  762 RALANVDLHVVDGLGRRKTRGASGELWIGGAGVARGYAGDAgEAAGRFVEEGWpgsgrlYRSGDLVRWRADGCLEFLGRI 841
Cdd:cd17631  270 RPVFFVEVRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRP-EATAAAFRDGW------FHTGDLGRLDEDGYLYIVDRK 342

                        410       420       430
                 ....*....|....*....|....*....|..
gi 15597498  842 DEQVKINGYRIELGEIRSALLEHPAVGEAAVL 873
Cdd:cd17631  343 KDMIISGGENVYPAEVEDVLYEHPAVAEVAVI 374
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
 1344-1795 4.10e-37

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: 153.86  E-value: 4.10e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1344 LLSAAERKRLPEGLDDAYPMTSLQQGMLLQSEASGDPRLLHNVVLHEVHGRLDGELLARAWAILIGRHAILRTGFDLHGG 1423
Cdd:COG1020    1 AAAAAAAALPPAAAAAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1424 QVPLQWVHPataVAAEVPVHDLCGLDGETRRLRLRAWIEEEQATPFDWSRPPLVRLAALALDERRFALGVAEHHSVLDGW 1503
Cdd:COG1020   81 RPVQVIQPV---VAAPLPVVVLLVDLEALAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGL 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1504 SLQSLVDELLAVYADLLAGVVAREAEAPAVGFRDYVALER--EAEANAASALFWLDYLAGAryRPLPGLAEEGPR----- 1576
Cdd:COG1020  158 SDGLLLAELLRLYLAAYAGAPLPLPPLPIQYADYALWQREwlQGEELARQLAYWRQQLAGL--PPLLELPTDRPRpavqs 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1577 -RMAAVRVDVPADSLSRLRALAERSGLPLRSLLLAAHGRALCRFSDADEVVTGFVSHGRPeEPGADRLLGLFLNTLP--C 1653
Cdd:COG1020  236 yRGARVSFRLPAELTAALRALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRP-RPELEGLVGFFVNTLPlrV 314

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1654 RLSASVDLLDSARRAFDYERASLEHRRHPLAAIRRRNRELRL-------DSLFNFVDFHQDDAAPAGVRhGGILDQVVVD 1726
Cdd:COG1020  315 DLSGDPSFAELLARVRETLLAAYAHQDLPFERLVEELQPERDlsrnplfQVMFVLQNAPADELELPGLT-LEPLELDSGT 393

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15597498 1727 VDVPLAVDFEVAGERLEVGFQYAAGRFPAERAEALAGAYREALLALLGDPVQPPAAAQAEDSVELRRVL 1795
Cdd:COG1020  394 AKFDLTLTVVETGDGLRLTLEYNTDLFDAATIERMAGHLVTLLEALAADPDQPLGDLPLLTAAERQQLL 462
MACS_like cd05972
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ...
 476-872 2.97e-36

Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.


Pssm-ID: 341276 [Multi-domain]  Cd Length: 428  Bit Score: 144.02  E-value: 2.97e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  476 FATLRARSEAVAEALLAAGVRPGQAVAVMTGRNREAIVALLGVMRAAAVYTPVNPEFPAARVERMREAGGIVFALADAEc 555
Cdd:cd05972    3 FRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTDAE- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  556 agrareafagacldlstlplagsgmslpapggrDAAYMIFTSGTSGQPKGVVVEHASALNlsqALARTVYANVVGEG-LR 634
Cdd:cd05972   82 ---------------------------------DPALIYFTSGTTGLPKGVLHTHSYPLG---HIPTAAYWLGLRPDdIH 125

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  635 VTVNAP-------FSFdssikqILQLLSGhCLVLVPQEVRSDPQRMLGFLEERRIDVLDCTPSLFRLLLQAGLDDAHPAL 707
Cdd:cd05972  126 WNIADPgwakgawSSF------FGPWLLG-ATVFVYEGPRFDAERILELLERYGVTSFCGPPTAYRMLIKQDLSSYKFSH 198

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  708 PGRILVGGERFDEaswEVAAGWRRC---QVFNLYGPTEATVNASLARVAEHARPTIGRALANVDLHVVDGLGRRKTRGAS 784
Cdd:cd05972  199 LRLVVSAGEPLNP---EVIEWWRAAtglPIRDGYGQTETGLTVGNFPDMPVKPGSMGRPTPGYDVAIIDDDGRELPPGEE 275

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  785 GELWI--GGAGVARGYAGDAGEAAGRFVEeGWpgsgrlYRSGDLVRWRADGCLEFLGRIDEQVKINGYRIELGEIRSALL 862
Cdd:cd05972  276 GDIAIklPPPGLFLGYVGDPEKTEASIRG-DY------YLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALL 348

                        410
                 ....*....|
gi 15597498  863 EHPAVGEAAV 872
Cdd:cd05972  349 EHPAVAEAAV 358
PRK12467 PRK12467
peptide synthase; Provisional
 1290-1776 5.49e-36

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 151.08  E-value: 5.49e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1290 IQMQVMAREAGLAFTL-RDVFNHQSIRELA-----RLLAAPASPADALGTSAPQSLEPFALLSAAERKRLP---EGLDDA 1360
Cdd:PRK12467 2567 INGQVYGGELNLGWTFsQEMFDEATIQRLAdayaeELRALIEHCCSNDQRGVTPSDFPLAGLSQEQLDRLPvavGDIEDI 2646

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1361 YPMTSLQQGMLLQSEASGDPRLLHNVVLHEVHGrLDGELLARAWAILIGRHAILRTGFDLHGG-QVPLQWVHPAtavaAE 1439
Cdd:PRK12467 2647 YPLSPMQQGMLFHTLYEGGAGDYINQMRVDVEG-LDVERFRTAWQAVIDRHEILRSGFLWDGElEEPLQVVYKQ----AR 2721

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1440 VPVHDLCGLDGETRRLRLRAWIEEEQATPFDWSRPPLVRLAALALDERRFALGVAEHHSVLDGWSLQSLVDELLAVYAdl 1519
Cdd:PRK12467 2722 LPFSRLDWRDRADLEQALDALAAADRQQGFDLLSAPLLRLTLVRTGEDRHHLIYTNHHILMDGWSGSQLLGEVLQRYF-- 2799

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1520 lagvvAREAEAPAVGFRDYVALeREAEANAASALFWLDYLAGAR-----YRPLPGLAEEGPRRMAAVRVDVPADSLSRLR 1594
Cdd:PRK12467 2800 -----GQPPPAREGRYRDYIAW-LQAQDAEASEAFWKEQLAALEeptrlARALYPAPAEAVAGHGAHYLHLDATQTRQLI 2873

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1595 ALAERSGLPLRSLLLAAHGRALCRFSDADEVVTGFVSHGRPEE-PGADRLLGLFLNTLPCRLS--ASVDLLDSARRAFDY 1671
Cdd:PRK12467 2874 EFARRHRVTLNTLVQGAWLLLLQRFTGQDTVCFGATVAGRPAQlRGAEQQLGLFINTLPVIASprAEQTVSDWLQQVQAQ 2953

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1672 ERASLEHRRHPLAAIRR---RNRELRLDSLFNF----VDFHQDDAAPAGVRHGGILDQVVVDVDVPLAVDfevAGERLEV 1744
Cdd:PRK12467 2954 NLALREFEHTPLADIQRwagQGGEALFDSILVFenypISEALKQGAPSGLRFGAVSSREQTNYPLTLAVG---LGDTLEL 3030

                         490       500       510
                  ....*....|....*....|....*....|..
gi 15597498  1745 GFQYAAGRFPAERAEALAGAYREALLALLGDP 1776
Cdd:PRK12467 3031 EFSYDRQHFDAAAIERLAESFDRLLQAMLNNP 3062
PRK07656 PRK07656
long-chain-fatty-acid--CoA ligase; Validated
 445-872 2.24e-35

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236072 [Multi-domain]  Cd Length: 513  Bit Score: 143.12  E-value: 2.24e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   445 APVESLVAAFDLRAALQPQAPALLDAHGSLDFATLRARSEAVAEALLAAGVRPGQAVAVMTGRNREAIVALLGVMRAAAV 524
Cdd:PRK07656    2 NEWMTLPELLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   525 YTPVNPEFPAARVERMREAGG--IVFALAD------------------AECAGRAREAFAGACLDLSTLPLAGSGMSLPA 584
Cdd:PRK07656   82 VVPLNTRYTADEAAYILARGDakALFVLGLflgvdysattrlpalehvVICETEEDDPHTEKMKTFTDFLAAGDPAERAP 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   585 P-GGRDAAYMIFTSGTSGQPKGVVVEHASALNLSQALARtvYANVVGE-------------GLRVTVNAPfsfdssikqi 650
Cdd:PRK07656  162 EvDPDDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAE--YLGLTEGdrylaanpffhvfGYKAGVNAP---------- 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   651 lqLLSGHCLVLVPQevrSDPQRMLGFLEERRIDVLDCTPSLFRLLLQaglddaHPALPG------RILVGG--------- 715
Cdd:PRK07656  230 --LMRGATILPLPV---FDPDEVFRLIETERITVLPGPPTMYNSLLQ------HPDRSAedlsslRLAVTGaasmpvall 298

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   716 ERFDE--ASWEVAAGwrrcqvfnlYGPTEATVNASLAR---VAEHARPTIGRALANVDLHVVDGLGRRKTRGASGELWIG 790
Cdd:PRK07656  299 ERFESelGVDIVLTG---------YGLSEASGVTTFNRlddDRKTVAGTIGTAIAGVENKIVNELGEEVPVGEVGELLVR 369

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   791 GAGVARGYAGDAGEAAGRFVEEGWpgsgrLYrSGDLVRWRADGCLEFLGRIDEQVKINGYRIELGEIRSALLEHPAVGEA 870
Cdd:PRK07656  370 GPNVMKGYYDDPEATAAAIDADGW-----LH-TGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEA 443


                  ..
gi 15597498   871 AV 872
Cdd:PRK07656  444 AV 445
PRK12467 PRK12467
peptide synthase; Provisional
 1393-1825 2.49e-33

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 142.22  E-value: 2.49e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1393 GRLDGELLARAWAILIGRHAILRTGFDLHGGQVpLQWVHPATAVaaEVPVHDLCGLDGETRRLRLRAWIEEEQATPFDWS 1472
Cdd:PRK12467   82 GELDVSALRRAFDALVARHESLRTRFVQDEEGF-RQVIDASLSL--TIPLDDLANEQGRARESQIEAYINEEVARPFDLA 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1473 RPPLVRLAALALDERRFALGVAEHHSVLDGWSLQSLVDELLAVYADLLAGvvaREAEAPA--VGFRDYVALER---EAEA 1547
Cdd:PRK12467  159 NGPLLRVRLLRLADDEHVLVVTLHHIISDGWSMRVLVEELVQLYSAYSQG---REPSLPAlpIQYADYAIWQRswlEAGE 235

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1548 NAASALFWLDYLAGAryRPLPGLAEEGPR------RMAAVRVDVPADSLSRLRALAERSGLPLRSLLLAAHGRALCRFSD 1621
Cdd:PRK12467  236 RERQLAYWQEQLGGE--HTVLELPTDRPRpavpsyRGARLRVDLPQALSAGLKALAQREGVTLFMVLLASFQTLLHRYSG 313

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1622 ADEVVTGFVSHGRPEEPgADRLLGLFLNT--LPCRLSASVDLLDSARRAfdyERASLEHRRH------PLAAIRRRNREL 1693
Cdd:PRK12467  314 QSDIRIGVPNANRNRVE-TERLIGFFVNTqvLKAEVDPQASFLELLQQV---KRTALGAQAHqdlpfeQLVEALQPERSL 389

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1694 RLDSLFNFVDFHQDDAAPAGVRHGGILDQVVVDVDVPLAVD---------FEVAgERLEVGFQYAAGRFPAERAEALAGA 1764
Cdd:PRK12467  390 SHSPLFQVMFNHQNTATGGRDREGAQLPGLTVEELSWARHTaqfdlaldtYESA-QGLWAAFTYATDLFEATTIERLATH 468

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15597498  1765 YREALLALLGDPVQPPAAAQAEDSVELRRVLKVLSrvlgrplAADQGFASAGGHSLLGVQA 1825
Cdd:PRK12467  469 WRNLLEAIVAEPRRRLGELPLLDAEERARELVRWN-------APATEYAPDCVHQLIEAQA 522
FC-FACS_FadD_like cd05936
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ...
 450-901 2.59e-33

Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341259 [Multi-domain]  Cd Length: 468  Bit Score: 136.15  E-value: 2.59e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  450 LVAAFDLRAALQPQAPALLDAHGSLDFATLRARSEAVAEALLAAGVRPGQAVAVMTGRNREAIVALLGVMRAAAVYTPVN 529
Cdd:cd05936    1 LADLLEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  530 PEFPAARVERMREAGGIVFALADaecagrarEAFAGAcldLSTLPLAGSGMSLPAPggrDAAYMIFTSGTSGQPKGVVVE 609
Cdd:cd05936   81 PLYTPRELEHILNDSGAKALIVA--------VSFTDL---LAAGAPLGERVALTPE---DVAVLQYTSGTTGVPKGAMLT 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  610 HASAL-NLSQALArtvYANVVGEGLRVTVNA-PF--SFDSSIKQILQLLSGHCLVLVPqevRSDPQRMLGFLEERRIDVL 685
Cdd:cd05936  147 HRNLVaNALQIKA---WLEDLLEGDDVVLAAlPLfhVFGLTVALLLPLALGATIVLIP---RFRPIGVLKEIRKHRVTIF 220

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  686 DCTPSLFRLLLQAGlDDAHPALPG--RILVGGERFDEaswEVAAGWRR---CQVFNLYGPTEATVNASLARVAEHARP-T 759
Cdd:cd05936  221 PGVPTMYIALLNAP-EFKKRDFSSlrLCISGGAPLPV---EVAERFEEltgVPIVEGYGLTETSPVVAVNPLDGPRKPgS 296

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  760 IGRALANVDLHVVDGLGRRKTRGASGELWIGGAGVARGYAGDAGEAAGRFVeEGWpgsgrlYRSGDLVRWRADGCLEFLG 839
Cdd:cd05936  297 IGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFV-DGW------LRTGDIGYMDEDGYFFIVD 369

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15597498  840 RIDEQVKINGYRIELGEIRSALLEHPAVGEAAVLtdeadaAEPGADR--RIVAFVTAAEE---TADE 901
Cdd:cd05936  370 RKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVV------GVPDPYSgeAVKAFVVLKEGaslTEEE 430
PRK05691 PRK05691
peptide synthase; Validated
 1223-1795 3.44e-32

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 138.76  E-value: 3.44e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1223 LPLTAEGKLDRRALLAALAAEAAAQTLEAPANAT-------------EAALLEIWKSVLKRPAIGVSDNFFQVGGDSIRL 1289
Cdd:PRK05691  541 LPKTSSGKLQRSACRLRLADGSLDSYALFPALQAveaaqtaasgdelQARIAAIWCEQLKVEQVAADDHFFLLGGNSIAA 620

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1290 IQMQVMAREA-GLAFTLRDVFNhqsirelARLLAAPASPADALGTSAPQSLEPFALLSAAErkrlpeglddAYPMTSLQQ 1368
Cdd:PRK05691  621 TQVVARLRDElGIDLNLRQLFE-------APTLAAFSAAVARQLAGGGAAQAAIARLPRGQ----------ALPQSLAQN 683

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1369 GMLL------QSEASGDPRLLHnvvlheVHGRLDGELLARAWAILIGRHAILRTGFDLHGGQvPLQWVHPAtavaAEVPV 1442
Cdd:PRK05691  684 RLWLlwqldpQSAAYNIPGGLH------LRGELDEAALRASFQRLVERHESLRTRFYERDGV-ALQRIDAQ----GEFAL 752

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1443 H--DLCGLDGETRRLRLRAWIEEEQATPFDWSRPPLVRLAALALDERRFALGVAEHHSVLDGWSLQSLVDELLAVYADLL 1520
Cdd:PRK05691  753 QriDLSDLPEAEREARAAQIREEEARQPFDLEKGPLLRVTLVRLDDEEHQLLVTLHHIVADGWSLNILLDEFSRLYAAAC 832

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1521 AGVVAREAEaPAVGFRDYVALERE--AEANAASAL-FWLDYLAGAryRPLPGLAEEGPR----RMAAVR--VDVPADSLS 1591
Cdd:PRK05691  833 QGQTAELAP-LPLGYADYGAWQRQwlAQGEAARQLaYWKAQLGDE--QPVLELATDHPRsarqAHSAARysLRVDASLSE 909

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1592 RLRALAERSGLPLRSLLLAAHGRALCRFSDADEVVTGFVSHGRPeEPGADRLLGLFLNT------LPCRLSASvDLLDSA 1665
Cdd:PRK05691  910 ALRGLAQAHQATLFMVLLAAFQALLHRYSGQGDIRIGVPNANRP-RLETQGLVGFFINTqvlraqLDGRLPFT-ALLAQV 987

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1666 RRAFDYERAsleHRRHPLAAIRRRNRELRLDSLFNFVDFHQDDAAPAGVRHGGILDQVVVDVDVPLAVDFEVAGE----- 1740
Cdd:PRK05691  988 RQATLGAQA---HQDLPFEQLVEALPQAREQGLFQVMFNHQQRDLSALRRLPGLLAEELPWHSREAKFDLQLHSEedrng 1064

                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 15597498  1741 RLEVGFQYAAGRFPAERAEALAGAYREALLALLGDPVQPPAAAQAEDSVELRRVL 1795
Cdd:PRK05691 1065 RLTLSFDYAAELFDAATIERLAEHFLALLEQVCEDPQRALGDVQLLDAAERAQLA 1119
PRK05691 PRK05691
peptide synthase; Validated
 1192-1668 5.41e-32

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 137.99  E-value: 5.41e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1192 GGELSEQALRGFLEARLPAYMLPSRIARVERLPLTAEGKLDRRALLAALAAEAAAQTleaPANATEAALLEIWKSVLKRP 1271
Cdd:PRK05691 1578 GQEAEAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRALPEPVWQQREHVE---PRTELQQQIAAIWREVLGLP 1654

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1272 AIGVSDNFFQVGGDSIRLIQMQVMAREA-GLAFTLRDVFNHQSIRELARLLAApaspadalgtsapqslepfaLLSAAER 1350
Cdd:PRK05691 1655 RVGLRDDFFALGGHSLLATQIVSRTRQAcDVELPLRALFEASELGAFAEQVAR--------------------IQAAGER 1714

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1351 KRLP--EGLD--DAYPMTSLQQGM--LLQSEASGDPrllHNVV-LHEVHGRLDGELLARAWAILIGRHAILRTGFDLHGG 1423
Cdd:PRK05691 1715 NSQGaiARVDrsQPVPLSYSQQRMwfLWQMEPDSPA---YNVGgMARLSGVLDVDRFEAALQALILRHETLRTTFPSVDG 1791

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1424 qVPLQWVHPATAVaaEVPVHDLCGLDGETRRLRLRAWIEEEQATPFDWSRPPLVRLAALALDERRFALGVAEHHSVLDGW 1503
Cdd:PRK05691 1792 -VPVQQVAEDSGL--RMDWQDFSALPADARQQRLQQLADSEAHQPFDLERGPLLRACLVKAAEREHYFVLTLHHIVTEGW 1868

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1504 SLQSLVDELLAVYADLLAGvvaREA--EAPAVGFRDYVALER---EAEANAASALFWLDYLagARYRPLPGLAEEGPR-- 1576
Cdd:PRK05691 1869 AMDIFARELGALYEAFLDD---RESplEPLPVQYLDYSVWQRqwlESGERQRQLDYWKAQL--GNEHPLLELPADRPRpp 1943

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1577 ----RMAAVRVDVPADSLSRLRALAERSGLPLRSLLLAAHGRALCRFSDADEVVTG--FVSHGRPEEPGadrLLGLFLNT 1650
Cdd:PRK05691 1944 vqshRGELYRFDLSPELAARVRAFNAQRGLTLFMTMTATLAALLYRYSGQRDLRIGapVANRIRPESEG---LIGAFLNT 2020

                         490       500
                  ....*....|....*....|...
gi 15597498  1651 --LPCRLSASV---DLLDSARRA 1668
Cdd:PRK05691 2021 qvLRCQLDGQMsvsELLEQVRQT 2043
BCL_4HBCL cd05959
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ...
 452-908 6.61e-32

Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.


Pssm-ID: 341269 [Multi-domain]  Cd Length: 508  Bit Score: 132.88  E-value: 6.61e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  452 AAFDLRAALQPQAPALLDAHGSLDFATLRARSEAVAEALLAAGVRPGQAVAVMTGRNREAIVALLGVMRAAAVYTPVNPE 531
Cdd:cd05959    8 LVDLNLNEGRGDKTAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  532 FPAARVERMREAGGIVFALADAECAGRAREAFAGACLDLSTLPLAGSGMSL------------------PAPGGRDA-AY 592
Cdd:cd05959   88 LTPDDYAYYLEDSRARVVVVSGELAPVLAAALTKSEHTLVVLIVSGGAGPEagalllaelvaaeaeqlkPAATHADDpAF 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  593 MIFTSGTSGQPKGVVVEHASALNLSQALARTVYA----NVV--------GEGLRVTVNAPFSFdssikqilqllsGHCLV 660
Cdd:cd05959  168 WLYSSGSTGRPKGVVHLHADIYWTAELYARNVLGiredDVCfsaaklffAYGLGNSLTFPLSV------------GATTV 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  661 LVPQevRSDPQRMLGFLEERRIDVLDCTPSLFRLLLqaglddAHPALPGRILV-------GGERFDEASWEvaaGWRR-- 731
Cdd:cd05959  236 LMPE--RPTPAAVFKRIRRYRPTVFFGVPTLYAAML------AAPNLPSRDLSslrlcvsAGEALPAEVGE---RWKArf 304

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  732 -CQVFNLYGPTEAtVNASLARVAEHARP-TIGRALANVDLHVVDGLGRRKTRGASGELWIGGAGVARGYAGDAGEAAGRF 809
Cdd:cd05959  305 gLDILDGIGSTEM-LHIFLSNRPGRVRYgTTGKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTF 383

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  810 vEEGWpgsgrlYRSGDLVRWRADGCLEFLGRIDEQVKINGYRIELGEIRSALLEHPAVGEAAVLtdeadaAEPGADRRI- 888
Cdd:cd05959  384 -QGEW------TRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVV------GVEDEDGLTk 450

                        490       500
                 ....*....|....*....|.
gi 15597498  889 -VAFVTAAEETADESWLEVDL 908
Cdd:cd05959  451 pKAFVVLRPGYEDSEALEEEL 471
Thioesterase pfam00975
Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of ...
 1886-2110 4.32e-31

Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of peptide antibiotics. Next to the operons encoding these enzymes, in almost all cases, are genes that encode proteins that have similarity to the type II fatty acid thioesterases of vertebrates. There are also modules within the peptide synthetases that also share this similarity. With respect to antibiotic production, thioesterases are required for the addition of the last amino acid to the peptide antibiotic, thereby forming a cyclic antibiotic. Thioesterases (non-integrated) have molecular masses of 25-29 kDa.


Pssm-ID: 395776 [Multi-domain]  Cd Length: 223  Bit Score: 122.88  E-value: 4.32e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   1886 RLIALPPAGGNAGTFRGWDARLPADVELLAIQYPGRQErqDEPFVTDVEAMLCAIDDALLPLLDR-PFALIGASLGGMLA 1964
Cdd:pfam00975    2 PLFCFPPAGGSASSFRSLARRLPPPAEVLAVQYPGRGR--GEPPLNSIEALADEYAEALRQIQPEgPYALFGHSMGGMLA 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   1965 YELAARLESLhGLRARQLFVISSRAPGPDlEYPRFHAMGDAELLRTLREYDVLPLEVLDDPELREISLATLRADSRLAAD 2044
Cdd:pfam00975   80 FEVARRLERQ-GEAVRSLFLSDASAPHTV-RYEASRAPDDDEVVAEFTDEGGTPEELLEDEELLSMLLPALRADYRALES 157

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15597498   2045 YRYRPREplAIPITAILGEQDPGVSRVAIDGWRRHASRYE--LETLAGGHGLVVTAAEEVCAILRQRL 2110
Cdd:pfam00975  158 YSCPPLD--AQSATLFYGSDDPLHDADDLAEWVRDHTPGEfdVHVFDGDHFYLIEHLEAVLEIIEAKL 223
FACL_like_6 cd05922
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 494-897 6.38e-31

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: 128.71  E-value: 6.38e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  494 GVRPGQAVAVMTGRNREAIVALLGVMRAAA----VYTPVNPEFPAARVERMREAGGIVFALADAECAGRAREAfAGACLD 569
Cdd:cd05922   14 GGVRGERVVLILPNRFTYIELSFAVAYAGGrlglVFVPLNPTLKESVLRYLVADAGGRIVLADAGAADRLRDA-LPASPD 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  570 LSTL----PLAGSGMSLPA--PGGRDAAYMIFTSGTSGQPKGVVVEHASALNLSQALARtvYANVVGEGlRVTVNAPFSF 643
Cdd:cd05922   93 PGTVldadGIRAARASAPAheVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAE--YLGITADD-RALTVLPLSY 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  644 DSSIKQIL-QLLSGHCLVLVPQEVRsdPQRMLGFLEERRIDVLDCTPSLFRLLLQAGLDDAH-PALPGRILVGGERFDEA 721
Cdd:cd05922  170 DYGLSVLNtHLLRGATLVLTNDGVL--DDAFWEDLREHGATGLAGVPSTYAMLTRLGFDPAKlPSLRYLTQAGGRLPQET 247

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  722 SWEVAAGWRRCQVFNLYGPTEATVNAS-LARVAEHARPT-IGRALANVDLHVVDGLGRRKTRGASGELWIGGAGVARGYA 799
Cdd:cd05922  248 IARLRELLPGAQVYVMYGQTEATRRMTyLPPERILEKPGsIGLAIPGGEFEILDDDGTPTPPGEPGEIVHRGPNVMKGYW 327

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  800 GD-AGEAAGRfveegwPGSGRLYrSGDLVRWRADGCLEFLGRIDEQVKINGYRIELGEIRSALLEHPAVGEAAVLtdead 878
Cdd:cd05922  328 NDpPYRRKEG------RGGGVLH-TGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAV----- 395

                        410
                 ....*....|....*....
gi 15597498  879 AAEPGADRRIVAFVTAAEE 897
Cdd:cd05922  396 GLPDPLGEKLALFVTAPDK 414
FACL_fum10p_like cd05926
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ...
 462-872 4.48e-30

Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.


Pssm-ID: 341249 [Multi-domain]  Cd Length: 493  Bit Score: 127.04  E-value: 4.48e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  462 PQAPALL--DAHGSLDFATLRARSEAVAEALLAAGVRPGQAVAVMTGRNREAIVALLGVMRAAAVYTPVNPEFPAARVER 539
Cdd:cd05926    1 PDAPALVvpGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  540 MREAGGIVFALADAEC---AGRAREAFAGACLDL----STLPLAGSGMSLPA-------------PGGRDAAYMIFTSGT 599
Cdd:cd05926   81 YLADLGSKLVLTPKGElgpASRAASKLGLAILELaldvGVLIRAPSAESLSNlladkknaksegvPLPDDLALILHTSGT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  600 SGQPKGVVVEH----ASALNLSQALARTVYANVV-------GEGLRVTVNAPfsfdssikqilqLLSGHCLVLVPqevRS 668
Cdd:cd05926  161 TGRPKGVPLTHrnlaASATNITNTYKLTPDDRTLvvmplfhVHGLVASLLST------------LAAGGSVVLPP---RF 225

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  669 DPQRMLGFLEERRIDVLDCTPSLFRLLLqagldDAHPALPGRILvGGERF--------DEASWEVAAGWRRCQVFNLYGP 740
Cdd:cd05926  226 SASTFWPDVRDYNATWYTAVPTIHQILL-----NRPEPNPESPP-PKLRFirscsaslPPAVLEALEATFGAPVLEAYGM 299

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  741 TEATVNASLARVAEHARP--TIGRAlANVDLHVVDGLGRRKTRGASGELWIGGAGVARGYAGDAGEAAGRFVEEGWpgsg 818
Cdd:cd05926  300 TEAAHQMTSNPLPPGPRKpgSVGKP-VGVEVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGW---- 374

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....
gi 15597498  819 rlYRSGDLVRWRADGCLEFLGRIDEQVKINGYRIELGEIRSALLEHPAVGEAAV 872
Cdd:cd05926  375 --FRTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVA 426
MACS_like_4 cd05969
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ...
 476-892 8.92e-30

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: 124.92  E-value: 8.92e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  476 FATLRARSEAVAEALLAAGVRPGQAVAVMTGRNREAIVALLGVMRAAAVYTPVNPEF-PAARVERMREAGGIVfALADAE 554
Cdd:cd05969    3 FAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFgPEAIRDRLENSEAKV-LITTEE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  555 CAGRareafagacldlstlplagsgMSLpapggRDAAYMIFTSGTSGQPKGVVveHASALNLSQAL-ARTVYANVVGEGL 633
Cdd:cd05969   82 LYER---------------------TDP-----EDPTLLHYTSGTTGTPKGVL--HVHDAMIFYYFtGKYVLDLHPDDIY 133

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  634 RVTVNAPFSFDSSIKQILQLLSGHCLVLVpqEVRSDPQRMLGFLEERRIDVLDCTPSLFRLLLQAGLDDAhpalpgrilv 713
Cdd:cd05969  134 WCTADPGWVTGTVYGIWAPWLNGVTNVVY--EGRFDAESWYGIIERVKVTVWYTAPTAIRMLMKEGDELA---------- 201

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  714 ggERFDEASWEVAAG-----------WRRcQVFNL-----YGPTEATVNASLARVAEHARP-TIGRALANVDLHVVDGLG 776
Cdd:cd05969  202 --RKYDLSSLRFIHSvgeplnpeairWGM-EVFGVpihdtWWQTETGSIMIANYPCMPIKPgSMGKPLPGVKAAVVDENG 278

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  777 RRKTRGASGELWI--GGAGVARGYAGDAGEAAGRFVEeGWpgsgrlYRSGDLVRWRADGCLEFLGRIDEQVKINGYRIEL 854
Cdd:cd05969  279 NELPPGTKGILALkpGWPSMFRGIWNDEERYKNSFID-GW------YLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGP 351

                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 15597498  855 GEIRSALLEHPAVGEAAVLTDEadaaEPGADRRIVAFV 892
Cdd:cd05969  352 FEVESALMEHPAVAEAGVIGKP----DPLRGEIIKAFI 385
BCL_like cd05919
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ...
 465-899 9.69e-30

Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.


Pssm-ID: 341243 [Multi-domain]  Cd Length: 436  Bit Score: 124.88  E-value: 9.69e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  465 PALLDAHGSLDFATLRARSEAVAEALLAAGVRPGQAVAVMTGRNREAIVALLGVMRAAAVYTPVNPEFPAARVErmreag 544
Cdd:cd05919    2 TAFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYA------ 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  545 givFALADAECAGRAREAfagacldlstlplagsgmslpapggRDAAYMIFTSGTSGQPKGVVVEHASALNLSQALARTV 624
Cdd:cd05919   76 ---YIARDCEARLVVTSA-------------------------DDIAYLLYSSGTTGPPKGVMHAHRDPLLFADAMAREA 127

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  625 YANVVGEGLRVTVNAPFSFDSSIKQILQLLSGHCLVLVPQevRSDPQRMLGFLEERRIDVLDCTPSLFRLLLQAGLDDAH 704
Cdd:cd05919  128 LGLTPGDRVFSSAKMFFGYGLGNSLWFPLAVGASAVLNPG--WPTAERVLATLARFRPTVLYGVPTFYANLLDSCAGSPD 205

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  705 PALPGRILV-GGERFDEASWEVAAGWRRCQVFNLYGPTEaTVNASLARVAEHARP-TIGRALANVDLHVVDGLGRRKTRG 782
Cdd:cd05919  206 ALRSLRLCVsAGEALPRGLGERWMEHFGGPILDGIGATE-VGHIFLSNRPGAWRLgSTGRPVPGYEIRLVDEEGHTIPPG 284

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  783 ASGELWIGGAGVARGYAGDAGEAAGRFvEEGWpgsgrlYRSGDLVRWRADGCLEFLGRIDEQVKINGYRIELGEIRSALL 862
Cdd:cd05919  285 EEGDLLVRGPSAAVGYWNNPEKSRATF-NGGW------YRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLII 357

                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 15597498  863 EHPAVGEAAVL-TDEADAAEpgadrRIVAFVTAAEETA 899
Cdd:cd05919  358 QHPAVAEAAVVaVPESTGLS-----RLTAFVVLKSPAA 390
MCS cd05941
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ...
 463-899 1.01e-29

Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.


Pssm-ID: 341264 [Multi-domain]  Cd Length: 442  Bit Score: 124.71  E-value: 1.01e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  463 QAPALLDAHGSLDFATLRARSEAVAEA-LLAAGVRPGQAVAVMTGRNREAIVALLGVMRAAAVYTPVNPEFPAARVERMr 541
Cdd:cd05941    1 DRIAIVDDGDSITYADLVARAARLANRlLALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYV- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  542 eaggivfaLADAEcagrareafagacldlSTLPLagsgmslpapggrDAAYMIFTSGTSGQPKGVVVEHASALNLSQALa 621
Cdd:cd05941   80 --------ITDSE----------------PSLVL-------------DPALILYTSGTTGRPKGVVLTHANLAANVRAL- 121

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  622 rtvyanvvgeglrvtVNA-PFSFDSSIKQILQLLSGHCLV---LVPQEVRS--------DPQRMLGFLEERRIDVLDCTP 689
Cdd:cd05941  122 ---------------VDAwRWTEDDVLLHVLPLHHVHGLVnalLCPLFAGAsveflpkfDPKEVAISRLMPSITVFMGVP 186

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  690 SLF-RLLLQAGLDDAHPALPG-------RILVGG------ERFDEasWEVAAGWRrcqVFNLYGPTEATVNASlARVAEH 755
Cdd:cd05941  187 TIYtRLLQYYEAHFTDPQFARaaaaerlRLMVSGsaalpvPTLEE--WEAITGHT---LLERYGMTEIGMALS-NPLDGE 260

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  756 ARP-TIGRALANVDLHVVDGLGRRKT-RGASGELWIGGAGVARGYAGDAGEAAGRFVEEGWpgsgrlYRSGDLVRWRADG 833
Cdd:cd05941  261 RRPgTVGMPLPGVQARIVDEETGEPLpRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGW------FKTGDLGVVDEDG 334

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15597498  834 CLEFLGRI-DEQVKINGYRIELGEIRSALLEHPAVGEAAVLtdeadaAEPGAD--RRIVAFVTAAEETA 899
Cdd:cd05941  335 YYWILGRSsVDIIKSGGYKVSALEIERVLLAHPGVSECAVI------GVPDPDwgERVVAVVVLRAGAA 397
fkbM_fam TIGR01444
methyltransferase, FkbM family; Members of this family are characterized by two well-conserved ...
 947-1122 1.42e-29

methyltransferase, FkbM family; Members of this family are characterized by two well-conserved short regions separated by a variable in both sequence and length. The first of the two regions is found in a large number of proteins outside this subfamily, a number of which have been characterized as methyltransferases. One member of the present family, FkbM, was shown to be required for a specific methylation in the biosynthesis of the immunosuppressant FK506 in Streptomyces strain MA6548.


Pssm-ID: 273628  Cd Length: 143  Bit Score: 115.87  E-value: 1.42e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498    947 VVLDVGANIGLFSLYIASRAPRARVVAFEPLAPIRRRLEANLGRYA-PQVEVFGIGLSDAEREETFTYYPGYSTFSGIAE 1025
Cdd:TIGR01444    1 VVIDVGANIGDTSLYFARKGAEGRVIAFEPLPDAYEILEENVKLNNlPNVVLLNAAVGDRDGELEFNVSDDDTGNSSLLP 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   1026 YADASGERDVirrylsnqgeegganllldnideilddrlraeahRCRLRRLDQVIGELGLERIDLLKIDVQRAEMDVLLG 1105
Cdd:TIGR01444   81 TPDADRESEI----------------------------------EVEVVTLDDLVEEFGLDKVDLLKIDVEGAELEVLRG 126

                          170
                   ....*....|....*..
gi 15597498   1106 LDDAALAKVRQIVLEVH 1122
Cdd:TIGR01444  127 AAETLLEKRPVIVLEVH 143
PRK06187 PRK06187
long-chain-fatty-acid--CoA ligase; Validated
 458-901 7.64e-29

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235730 [Multi-domain]  Cd Length: 521  Bit Score: 123.76  E-value: 7.64e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   458 AALQPQAPALLDAHGSLDFATLRARSEAVAEALLAAGVRPGQAVAVMTGRNREAIVALLGVMRAAAVYTPVNPEFPAARV 537
Cdd:PRK06187   16 ARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPINIRLKPEEI 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   538 ER-MREAGGIVFaLADAECAG---RAREAF--------AGACLDLSTLPLAGSGMSL----------PAPGGRDAAYMIF 595
Cdd:PRK06187   96 AYiLNDAEDRVV-LVDSEFVPllaAILPQLptvrtvivEGDGPAAPLAPEVGEYEELlaaasdtfdfPDIDENDAAAMLY 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   596 TSGTSGQPKGVVVEHASALNLSQALARtvyANVVGEGLRVTVNAP-F-SFDSSIKqILQLLSGHCLVLVPqevRSDPQRM 673
Cdd:PRK06187  175 TSGTTGHPKGVVLSHRNLFLHSLAVCA---WLKLSRDDVYLVIVPmFhVHAWGLP-YLALMAGAKQVIPR---RFDPENL 247

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   674 LGFLEERRIDVLDCTPSLFRLLLQAglDDAHPA-LPGR--ILVGG--------ERFDEASwevaagwrRCQVFNLYGPTE 742
Cdd:PRK06187  248 LDLIETERVTFFFAVPTIWQMLLKA--PRAYFVdFSSLrlVIYGGaalppallREFKEKF--------GIDLVQGYGMTE 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   743 ATVNASLARVAEHA------RPTIGRALANVDLHVVDGLGRR--KTRGASGELWIGGAGVARGYAGDAgEAAGRFVEEGW 814
Cdd:PRK06187  318 TSPVVSVLPPEDQLpgqwtkRRSAGRPLPGVEARIVDDDGDElpPDGGEVGEIIVRGPWLMQGYWNRP-EATAETIDGGW 396

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   815 pgsgrlYRSGDLVRWRADGCLEFLGRIDEQVKINGYRIELGEIRSALLEHPAVGEAAVL--TDEAdaaepgADRRIVAFV 892
Cdd:PRK06187  397 ------LHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIgvPDEK------WGERPVAVV 464

                         490
                  ....*....|
gi 15597498   893 TAAE-ETADE 901
Cdd:PRK06187  465 VLKPgATLDA 474
4CL cd05904
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ...
 446-901 1.21e-28

4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.


Pssm-ID: 341230 [Multi-domain]  Cd Length: 505  Bit Score: 122.73  E-value: 1.21e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  446 PVESLVAAFDLRAALQ-PQAPALLDAHG--SLDFATLRARSEAVAEALLAAGVRPGQAVAVMTGRNREAIVALLGVMRAA 522
Cdd:cd05904    2 PTDLPLDSVSFLFASAhPSRPALIDAATgrALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  523 AVYTPVNPEFPAARVERMREAGGIVFALADAECAGRAR----------EAFAGACLDLSTLPLAGSGMSLPAPGGR-DAA 591
Cdd:cd05904   82 AVVTTANPLSTPAEIAKQVKDSGAKLAFTTAELAEKLAslalpvvlldSAEFDSLSFSDLLFEADEAEPPVVVIKQdDVA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  592 YMIFTSGTSGQPKGVVVEHAsalNLSQALARTV-YANVVGEGLRVTVNA-P----FSFDSSIKQILQLlsGHCLVLVPqe 665
Cdd:cd05904  162 ALLYSSGTTGRSKGVMLTHR---NLIAMVAQFVaGEGSNSDSEDVFLCVlPmfhiYGLSSFALGLLRL--GATVVVMP-- 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  666 vRSDPQRMLGFLEERRIDVLDCTPSLFRLLLQAGLDDAHPALPGR-ILVGGERFDEaswEVAAGWRR----CQVFNLYGP 740
Cdd:cd05904  235 -RFDLEELLAAIERYKVTHLPVVPPIVLALVKSPIVDKYDLSSLRqIMSGAAPLGK---ELIEAFRAkfpnVDLGQGYGM 310

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  741 TEAT-VNASLARVAEHARP--TIGRALANVDLHVVD-GLGRRKTRGASGELWIGGAGVARGYAGDAGEAAGRFVEEGWpg 816
Cdd:cd05904  311 TESTgVVAMCFAPEKDRAKygSVGRLVPNVEAKIVDpETGESLPPNQTGELWIRGPSIMKGYLNNPEATAATIDKEGW-- 388

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  817 sgrlYRSGDLVRWRADGCLEFLGRIDEQVKINGYRIELGEIRSALLEHPAVGEAAV--LTDEaDAAE-PgadrriVAFV- 892
Cdd:cd05904  389 ----LHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVipYPDE-EAGEvP------MAFVv 457

                        490
                 ....*....|.
gi 15597498  893 --TAAEETADE 901
Cdd:cd05904  458 rkPGSSLTEDE 468
A_NRPS_alphaAR cd17647
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ...
 494-909 1.58e-28

Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.


Pssm-ID: 341302 [Multi-domain]  Cd Length: 520  Bit Score: 122.63  E-value: 1.58e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  494 GVRPGQAVAVMTGRNREAIVALLGVMRAAAVYTPVNPEFPAARvermreagGIVFaLADAECAGRAREAFAGACLDLSTL 573
Cdd:cd17647   41 GIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPAR--------QNIY-LGVAKPRGLIVIRAAGVVVGPDSN 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  574 PLagsgmslpapggrdaayMIFTSGTSGQPKGVVVEHASAlnlsqalarTVYANVVGEGLRVTVNAPFSFDSSIKQ---- 649
Cdd:cd17647  112 PT-----------------LSFTSGSEGIPKGVLGRHFSL---------AYYFPWMAKRFNLSENDKFTMLSGIAHdpiq 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  650 ---ILQLLSGHCLVLVPQEVRSDPQRMLGFLEERRIDVLDCTPSLFRLLlQAGLDDAHPALPGRILVGG--ERFDEASWE 724
Cdd:cd17647  166 rdmFTPLFLGAQLLVPTQDDIGTPGRLAEWMAKYGATVTHLTPAMGQLL-TAQATTPFPKLHHAFFVGDilTKRDCLRLQ 244

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  725 VAAgwRRCQVFNLYGPTEATVNASLARV-AEHARPTI----------GRALANVDLHVVDGLGRRKTRGAS--GELWIGG 791
Cdd:cd17647  245 TLA--ENVRIVNMYGTTETQRAVSYFEVpSRSSDPTFlknlkdvmpaGRGMLNVQLLVVNRNDRTQICGIGevGEIYVRA 322

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  792 AGVARGYAGDAGEAAGRF-----VEEG----------------WPG-SGRLYRSGDLVRWRADGCLEFLGRIDEQVKING 849
Cdd:cd17647  323 GGLAEGYRGLPELNKEKFvnnwfVEPDhwnyldkdnnepwrqfWLGpRDRLYRTGDLGRYLPNGDCECCGRADDQVKIRG 402

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  850 YRIELGEIRSALLEHPAVGEAAVLTDEADAAEPGAdrrIVAFVTAAEETADESWLEVDLP 909
Cdd:cd17647  403 FRIELGEIDTHISQHPLVRENITLVRRDKDEEPTL---VSYIVPRFDKPDDESFAQEDVP 459
MACS_AAE_MA_like cd05970
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ...
 455-872 1.70e-27

Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.


Pssm-ID: 341274 [Multi-domain]  Cd Length: 537  Bit Score: 119.52  E-value: 1.70e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  455 DLRAALQPQAPALL--DAHGS---LDFATLRARSEAVAEALLAAGVRPGQAVAVMTGRNREAIVALLGVMRAAAVYTPVN 529
Cdd:cd05970   24 DAMAKEYPDKLALVwcDDAGEeriFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPAT 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  530 PEFPAARVERMREAGGIVFALADAEcaGRAREAFAGACLDLSTLP-LAGSGMSLP------------------------A 584
Cdd:cd05970  104 HQLTAKDIVYRIESADIKMIVAIAE--DNIPEEIEKAAPECPSKPkLVWVGDPVPegwidfrkliknaspdferptansY 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  585 PGGRDAAYMIFTSGTSGQPKgvVVEHASALNLSQALARTVYANVVGEGLRVTVnAPFSFDSSI--KQILQLLSGhCLVLV 662
Cdd:cd05970  182 PCGEDILLVYFSSGTTGMPK--MVEHDFTYPLGHIVTAKYWQNVREGGLHLTV-ADTGWGKAVwgKIYGQWIAG-AAVFV 257

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  663 PQEVRSDPQRMLGFLEERRIDVLDCTPSLFRLLLQAGLDDAHPALPGRILVGGERFDEaswEVAAGWRR---CQVFNLYG 739
Cdd:cd05970  258 YDYDKFDPKALLEKLSKYGVTTFCAPPTIYRFLIREDLSRYDLSSLRYCTTAGEALNP---EVFNTFKEktgIKLMEGFG 334

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  740 PTEATVNASLARVAEHARPTIGRALANVDLHVVDGLGRRKTRGASGELWIGGA-----GVARGYAGDAGEAAgrfveEGW 814
Cdd:cd05970  335 QTETTLTIATFPWMEPKPGSMGKPAPGYEIDLIDREGRSCEAGEEGEIVIRTSkgkpvGLFGGYYKDAEKTA-----EVW 409

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 15597498  815 PGSgrLYRSGDlVRWR-ADGCLEFLGRIDEQVKINGYRIELGEIRSALLEHPAVGEAAV 872
Cdd:cd05970  410 HDG--YYHTGD-AAWMdEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAV 465
E-C_NRPS cd19544
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); ...
 1361-1688 4.04e-27

Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); Dual function Epimerization/Condensation (E/C) domains have both an epimerization and a DCL condensation activity. Dual E/C domains first epimerize the substrate amino acid to produce a D-configuration, then catalyze the condensation between the D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. They are D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. These Dual E/C domains contain an extended His-motif (HHx(N)GD) near the N-terminus of the domain in addition to the standard Condensation (C) domain active site motif (HHxxxD). C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains, these include the DCL-type, LCL-type, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C domains, and the X-domain.


Pssm-ID: 380466 [Multi-domain]  Cd Length: 413  Bit Score: 116.38  E-value: 4.04e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1361 YPMTSLQQGML----LQSEasGDPRLLHNVVLHEVHGRLDGelLARAWAILIGRHAILRTGFDLHGGQVPLQWVHPAtav 1436
Cdd:cd19544    2 YPLAPLQEGILfhhlLAEE--GDPYLLRSLLAFDSRARLDA--FLAALQQVIDRHDILRTAILWEGLSEPVQVVWRQ--- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1437 aAEVPVHDLCGLDGETRRLRLRAWIEEEQaTPFDWSRPPLVRLAAlALDER--RFALGVAEHHSVLDGWSLQSLVDELLA 1514
Cdd:cd19544   75 -AELPVEELTLDPGDDALAQLRARFDPRR-YRLDLRQAPLLRAHV-AEDPAngRWLLLLLFHHLISDHTSLELLLEEIQA 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1515 vyadLLAGvvaREAE-APAVGFRDYVALEREAEANAASALFWLDYLAGARYRPLP-GLAE--EGPRRMAAVRVDVPADSL 1590
Cdd:cd19544  152 ----ILAG---RAAAlPPPVPYRNFVAQARLGASQAEHEAFFREMLGDVDEPTAPfGLLDvqGDGSDITEARLALDAELA 224

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1591 SRLRALAERSGLPLRSLLLAAHGRALCRFSDADEVVTGFVSHGR-PEEPGADRLLGLFLNTLPCRLS-ASVDLLDSARRA 1668
Cdd:cd19544  225 QRLRAQARRLGVSPASLFHLAWALVLARCSGRDDVVFGTVLSGRmQGGAGADRALGMFINTLPLRVRlGGRSVREAVRQT 304

                        330       340
                 ....*....|....*....|
gi 15597498 1669 FDYERASLEHRRHPLAAIRR 1688
Cdd:cd19544  305 HARLAELLRHEHASLALAQR 324
CHC_CoA_lg cd05903
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ...
 473-876 4.31e-27

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: 116.71  E-value: 4.31e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  473 SLDFATLRARSEAVAEALLAAGVRPGQAVAVMTGRNREAIVALLGVMRAAAVYTPVNPEFpaarveRMREAGgivFALAD 552
Cdd:cd05903    1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFF------REHELA---FILRR 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  553 AecagRAREAFAgacldlstlPLAGSGMSlPAPGGRDAAYMIFTSGTSGQPKGVVVEHASALNLSQALARTVyanVVGEG 632
Cdd:cd05903   72 A----KAKVFVV---------PERFRQFD-PAAMPDAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERL---GLGPG 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  633 LRVTVNAPfsfdssIKQILQLLSGHCLVLV---PQEVRS--DPQRMLGFLEERRID-VLDCTPSLFRLLLQAGLDDAHPA 706
Cdd:cd05903  135 DVFLVASP------MAHQTGFVYGFTLPLLlgaPVVLQDiwDPDKALALMREHGVTfMMGATPFLTDLLNAVEEAGEPLS 208

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  707 LPGRILVGGERFDEASWEVAAGWRRCQVFNLYGPTE---ATVNASLARVaEHARPTIGRALANVDLHVVDGLGRRKTRGA 783
Cdd:cd05903  209 RLRTFVCGGATVPRSLARRAAELLGAKVCSAYGSTEcpgAVTSITPAPE-DRRLYTDGRPLPGVEIKVVDDTGATLAPGV 287

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  784 SGELWIGGAGVARGYAgDAGEAAGRFVEEGWpgsgrlYRSGDLVRWRADGCLEFLGRIDEQVKINGYRIELGEIRSALLE 863
Cdd:cd05903  288 EGELLSRGPSVFLGYL-DRPDLTADAAPEGW------FRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLG 360

                        410
                 ....*....|....*
gi 15597498  864 HPAVGEAAV--LTDE 876
Cdd:cd05903  361 HPGVIEAAVvaLPDE 375
beta-lac_NRPS cd19547
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ...
 1361-1708 6.87e-27

Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis NocB which exhibits an unusual cyclization to form beta-lactam rings in pro-nocardicin G synthesis; Nocardia uniformis NRPS NocB acts centrally in the biosynthesis of the nocardicin monocyclic beta-lactam antibiotics. Along with another NRPS NocA, it mediates an unusual cyclization to form beta-lactam rings in the synthesis of the beta-lactam-containing pentapeptide pro-nocardicin G. This small subfamily is related to DCL-type Condensation (C) domains, which catalyze condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; domains belonging to this subfamily have an HHHxxxD motif at the active site.


Pssm-ID: 380469 [Multi-domain]  Cd Length: 422  Bit Score: 115.87  E-value: 6.87e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1361 YPMTSLQQGMLLQSEASGDPRLLHNVVLHEVHGRLDGELLARAWAILIGRHAILRTGFDLHGGQVPLQWVHpaTAVAAEV 1440
Cdd:cd19547    2 YPLAPMQEGMLFRGLFWPDSDAYFNQNVLELVGGTDEDVLREAWRRVADRYEILRTGFTWRDRAEPLQYVR--DDLAPPW 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1441 PVHDLCGLDGETRRLRLRAWIEEEQATPFDWSRPPLVRLAALALDERRFALGVAEHHSVLDGWSLQSLVDELLAVYADLL 1520
Cdd:cd19547   80 ALLDWSGEDPDRRAELLERLLADDRAAGLSLADCPLYRLTLVRLGGGRHYLLWSHHHILLDGWCLSLIWGDVFRVYEELA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1521 AGvvaREAE-APAVGFRDYVALEREAEANA-ASALFWLDYLAGARYRPLPGLAEEGPRRMAAVRVDVPaDSLSRLRALAE 1598
Cdd:cd19547  160 HG---REPQlSPCRPYRDYVRWIRARTAQSeESERFWREYLRDLTPSPFSTAPADREGEFDTVVHEFP-EQLTRLVNEAA 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1599 RS-GLPLRSLLLAAHGRALCRFSDADEVVTGFVSHGRPEE-PGADRLLGLFLNTLPCRLSASVD-----LLDSARRAFDY 1671
Cdd:cd19547  236 RGyGVTTNAISQAAWSMLLALQTGARDVVHGLTIAGRPPElEGSEHMVGIFINTIPLRIRLDPDqtvtgLLETIHRDLAT 315

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 15597498 1672 ERAsleHRRHPLAAIRRRNRELRL------DSLFNFVDFHQDD 1708
Cdd:cd19547  316 TAA---HGHVPLAQIKSWASGERLsggrvfDNLVAFENYPEDN 355
FUM14_C_NRPS-like cd19545
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ...
 1360-1776 1.92e-26

Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond forming Fusarium verticillioides FUM14 protein; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) typically catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. However, some C-domains have ester-bond forming activity. This subfamily includes Fusarium verticillioides FUM14 (also known as NRPS8), a bi-domain protein with an ester-bond forming NRPS C-domain, which catalyzes linkages between an aminoacyl/peptidyl-PCP donor and a hydroxyl-containing acceptor. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. FUM14 has an altered active site motif DHTHCD instead of the typical HHxxxD motif seen in other subfamily members. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380467 [Multi-domain]  Cd Length: 395  Bit Score: 113.93  E-value: 1.92e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1360 AYPMTSLQQGMLLQSEASGDPRLLHNVVlhEVHGRLDGELLARAWAILIGRHAILRTGFDLHGGQVPLQwvhpatAVAAE 1439
Cdd:cd19545    1 IYPCTPLQEGLMALTARQPGAYVGQRVF--ELPPDIDLARLQAAWEQVVQANPILRTRIVQSDSGGLLQ------VVVKE 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1440 VPVHDLCGLDgetrrlrLRAWIEEEQATPFDWSrPPLVRLAAL--ALDERRFALGVaeHHSVLDGWSLQSLVDELLAVYA 1517
Cdd:cd19545   73 SPISWTESTS-------LDEYLEEDRAAPMGLG-GPLVRLALVedPDTERYFVWTI--HHALYDGWSLPLILRQVLAAYQ 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1518 DllagvvarEAEAPAVGFRDYVALEREAEAnAASALFWLDYLAGAR---YRPLPGLAEEgPRRMAAVRVDVPADSLSrlr 1594
Cdd:cd19545  143 G--------EPVPQPPPFSRFVKYLRQLDD-EAAAEFWRSYLAGLDpavFPPLPSSRYQ-PRPDATLEHSISLPSSA--- 209

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1595 alaeRSGLPLRSLLLAAHGRALCRFSDADEVVTGFVSHGR--PeEPGADRLLGLFLNTLPCRLS----ASV-DLLDSARR 1667
Cdd:cd19545  210 ----SSGVTLATVLRAAWALVLSRYTGSDDVVFGVTLSGRnaP-VPGIEQIVGPTIATVPLRVRidpeQSVeDFLQTVQK 284

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1668 AfDYERASLEHRrhPLAAIRRRNRELR----LDSLFNFVdfHQDDAAPAGVRHGGILDQVVVDVDVPLAV---DFEVAGE 1740
Cdd:cd19545  285 D-LLDMIPFEHT--GLQNIRRLGPDARaacnFQTLLVVQ--PALPSSTSESLELGIEEESEDLEDFSSYGltlECQLSGS 359

                        410       420       430
                 ....*....|....*....|....*....|....*.
gi 15597498 1741 RLEVGFQYAAGRFPAERAEALAGAYREALLALLGDP 1776
Cdd:cd19545  360 GLRVRARYDSSVISEEQVERLLDQFEHVLQQLASAP 395
EntE COG1021
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ...
 432-898 2.50e-26

EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440644 [Multi-domain]  Cd Length: 533  Bit Score: 116.01  E-value: 2.50e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  432 ERYQA---WQGErvepapveSLVAAFDLRAALQPQAPALLDAHGSLDFATLRARSEAVAEALLAAGVRPGQAVAVMTGRN 508
Cdd:COG1021   14 ARYREagyWRGE--------TLGDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNV 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  509 REAIVALLGVMRAAAVytPVNPEFPAARVE-----RMREAGGIVFA-----LADAECAGRAREAF-----------AGAC 567
Cdd:COG1021   86 AEFVIVFFALFRAGAI--PVFALPAHRRAEishfaEQSEAVAYIIPdrhrgFDYRALARELQAEVpslrhvlvvgdAGEF 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  568 LDLSTLPLAGSGMSLPAPGGRDAAYMIFTSGTSGQPKGVVVEHASALNLSQALAR-------TVYAnvvgeglrVTVNAP 640
Cdd:COG1021  164 TSLDALLAAPADLSEPRPDPDDVAFFQLSGGTTGLPKLIPRTHDDYLYSVRASAEicgldadTVYL--------AALPAA 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  641 FSFDSSIKQIL-QLLSGHCLVLVPqevRSDPQRMLGFLEERRIDVLDCTPSLFRLLLQAgLDDAHPALPG--RILVGGER 717
Cdd:COG1021  236 HNFPLSSPGVLgVLYAGGTVVLAP---DPSPDTAFPLIERERVTVTALVPPLALLWLDA-AERSRYDLSSlrVLQVGGAK 311

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  718 FDEaswEVAA------GWRRCQVFnlyGPTEATVN-----ASLARVAEharpTIGRALANVD-LHVVDGLGRRKTRGASG 785
Cdd:COG1021  312 LSP---ELARrvrpalGCTLQQVF---GMAEGLVNytrldDPEEVILT----TQGRPISPDDeVRIVDEDGNPVPPGEVG 381

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  786 ELWIGGAGVARGYAGDAGEAAGRFVEEGWpgsgrlYRSGDLVRWRADGCLEFLGRIDEQvkIN--GYRIELGEIRSALLE 863
Cdd:COG1021  382 ELLTRGPYTIRGYYRAPEHNARAFTPDGF------YRTGDLVRRTPDGYLVVEGRAKDQ--INrgGEKIAAEEVENLLLA 453

                        490       500       510
                 ....*....|....*....|....*....|....*....
gi 15597498  864 HPAVGEAAVLtdeadaAEPgaDR----RIVAFVTAAEET 898
Cdd:COG1021  454 HPAVHDAAVV------AMP--DEylgeRSCAFVVPRGEP 484
starter-C_NRPS cd19533
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ...
 1361-1716 3.03e-26

Starter Condensation domains, found in the first module of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. While standard C-domains catalyze peptide bond formation between two amino acids, an initial, ('starter') C-domain may instead acylate an amino acid with a fatty acid. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380456 [Multi-domain]  Cd Length: 419  Bit Score: 114.00  E-value: 3.03e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1361 YPMTSLQQGMLLQSEASGDPRLLHNVVLHEVHGRLDGELLARAWAILIGRHAILRTGFDLHGGqVPLQWVHPATAVAAEV 1440
Cdd:cd19533    2 LPLTSAQRGVWFAEQLDPEGSIYNLAEYLEITGPVDLAVLERALRQVIAEAETLRLRFTEEEG-EPYQWIDPYTPVPIRH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1441 PvhDLCGldGETRRLRLRAWIEEEQATPFDWSRPPLVRLAALALDERRFALGVAEHHSVLDGWSLQSLVDELLAVYADLL 1520
Cdd:cd19533   81 I--DLSG--DPDPEGAAQQWMQEDLRKPLPLDNDPLFRHALFTLGDNRHFWYQRVHHIVMDGFSFALFGQRVAEIYTALL 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1521 AGVVAREAEAPAvgFRDYVALE---REAEANAASALFWLDYLAGAryRPLPGLAEEGPRRMAAVRV---DVPADSLSRLR 1594
Cdd:cd19533  157 KGRPAPPAPFGS--FLDLVEEEqayRQSERFERDRAFWTEQFEDL--PEPVSLARRAPGRSLAFLRrtaELPPELTRTLL 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1595 ALAERSGLPLRSLLLAAHGRALCRFSDADEVVTGFVSHGRPEEpGADRLLGLFLNTLPCRL--SASVDLLDSARRAFDYE 1672
Cdd:cd19533  233 EAAEAHGASWPSFFIALVAAYLHRLTGANDVVLGVPVMGRLGA-AARQTPGMVANTLPLRLtvDPQQTFAELVAQVSREL 311

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 15597498 1673 RASLEHRRHPLAAIRRRNRELR-LDSLFNFV------DFHQDDAAPAGVRH 1716
Cdd:cd19533  312 RSLLRHQRYRYEDLRRDLGLTGeLHPLFGPTvnympfDYGLDFGGVVGLTH 362
CBAL cd05923
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ...
 458-905 6.55e-26

4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.


Pssm-ID: 341247 [Multi-domain]  Cd Length: 493  Bit Score: 114.14  E-value: 6.55e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  458 AALQPQAPALLDAHGSLD--FATLRARSEAVAEALLAAGVRPGQAVAVMTGRNREAIVALLGVMRAAAVYTPVNPEFPAA 535
Cdd:cd05923   11 ASRAPDACAIADPARGLRltYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAA 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  536 RVERMREAGGIVFAL-------ADAECAGRAREAFAGACLDLSTLPLAGSGMSLPAPGGRDAAYMIFTSGTSGQPKGVVV 608
Cdd:cd05923   91 ELAELIERGEMTAAViavdaqvMDAIFQSGVRVLALSDLVGLGEPESAGPLIEDPPREPEQPAFVFYTSGTTGLPKGAVI 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  609 EHASALNLSQALArTVYANVVGEGLRVTVNAPFSFDSSIKQILQL-LSGHCLVLVPQEVrsDPQRMLGFLEERRIDVLDC 687
Cdd:cd05923  171 PQRAAESRVLFMS-TQAGLRHGRHNVVLGLMPLYHVIGFFAVLVAaLALDGTYVVVEEF--DPADALKLIEQERVTSLFA 247

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  688 TPSLFRLLL----QAGLDD--------AHPALPGRILvggERFDEAswevaagwRRCQVFNLYGPTEAtVNASLARVAeh 755
Cdd:cd05923  248 TPTHLDALAaaaeFAGLKLsslrhvtfAGATMPDAVL---ERVNQH--------LPGEKVNIYGTTEA-MNSLYMRDA-- 313

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  756 ARPTIGRALANVDLHVVDGLGRRKTR---GASGELWIGGAGVA--RGYAGDAgEAAGRFVEEGWpgsgrlYRSGDLVRWR 830
Cdd:cd05923  314 RTGTEMRPGFFSEVRIVRIGGSPDEAlanGEEGELIVAAAADAafTGYLNQP-EATAKKLQDGW------YRTGDVGYVD 386

                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15597498  831 ADGCLEFLGRIDEQVKINGYRIELGEIRSALLEHPAVGEAAVLtdeaDAAEPGADRRIVAFVTAAEETADESWLE 905
Cdd:cd05923  387 PSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVI----GVADERWGQSVTACVVPREGTLSADELD 457
PRK05691 PRK05691
peptide synthase; Validated
 1290-1713 8.29e-26

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 117.58  E-value: 8.29e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1290 IQMQVMAREAGLAFTL-RDVFNHQSIRELA-----RLLAAPASP-ADALGTSAPQSLePFALLSAAERKRLP---EGLDD 1359
Cdd:PRK05691 3178 VDGQVYGGELVLRWTYsAERYDEQTIAELAeaylaELQALIAHClADGAGGLTPSDF-PLAQLTQAQLDALPvpaAEIED 3256

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1360 AYPMTSLQQGMLLQSEASGDPRLLHNVVLHEVHGRLDGELLARAWAILIGRHAILRTGFDLHGGQVPLQWVHPATAVAAE 1439
Cdd:PRK05691 3257 VYPLTPMQEGLLLHTLLEPGTGLYYMQDRYRINSALDPERFAQAWQAVVARHEALRASFSWNAGETMLQVIHKPGRTPID 3336

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1440 VpvHDLCGLDGETRRLRLRAWIEEEQATPFDWSRPPLVRLAALALDERRFALGVAEHHSVLDGWSLQSLVDELLAVYADL 1519
Cdd:PRK05691 3337 Y--LDWRGLPEDGQEQRLQALHKQEREAGFDLLNQPPFHLRLIRVDEARYWFMMSNHHILIDAWCRSLLMNDFFEIYTAL 3414

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1520 LAGVVAREAEAPAvgFRDYVA-LEREAEANAASalFWLDYLAG-ARYRPLPG----LAEEGPRRMAAV------RVDVpA 1587
Cdd:PRK05691 3415 GEGREAQLPVPPR--YRDYIGwLQRQDLAQARQ--WWQDNLRGfERPTPIPSdrpfLREHAGDSGGMVvgdcytRLDA-A 3489

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1588 DSlSRLRALAERSGLPLRSLLLAAHGRALCRFSDADEVVTGFVSHGRP-EEPGADRLLGLFLNTLPCRLSASVdlldsar 1666
Cdd:PRK05691 3490 DG-ARLRELAQAHQLTVNTFAQAAWALVLRRYSGDRDVLFGVTVAGRPvSMPQMQRTVGLFINSIALRVQLPA------- 3561

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*..
gi 15597498  1667 rafDYERASLehrRHPLAAIRRRNRELRLDSLFNFVDFHQDDAAPAG 1713
Cdd:PRK05691 3562 ---AGQRCSV---RQWLQGLLDSNMELREYEYLPLVAIQECSELPKG 3602
VL_LC_FACS_like cd05907
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ...
 494-917 1.31e-25

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: 112.69  E-value: 1.31e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  494 GVRPGQAVAVMtGRNR-EAIVALLGVMRAAAVYTPVNPEFPAARVERMreaggivfaLADAEcagrAREAFAGACLDLST 572
Cdd:cd05907   26 GVEPGDRVAIL-SRNRpEWTIADLAILAIGAVPVPIYPTSSAEQIAYI---------LNDSE----AKALFVEDPDDLAT 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  573 LplagsgmslpapggrdaaymIFTSGTSGQPKGVVVEHASALNLSQALARTVYAnvvGEGLRVTVNAPFS--FDSSIKQI 650
Cdd:cd05907   92 I--------------------IYTSGTTGRPKGVMLSHRNILSNALALAERLPA---TEGDRHLSFLPLAhvFERRAGLY 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  651 LQLLSGHCLVLVPqevrsDPQRMLGFLEERRIDVLDCTPSLFRLLLQAGLDDAHPALPGRIL------------VGGERF 718
Cdd:cd05907  149 VPLLAGARIYFAS-----SAETLLDDLSEVRPTVFLAVPRVWEKVYAAIKVKAVPGLKRKLFdlavggrlrfaaSGGAPL 223

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  719 DE--ASWEVAAGwrrCQVFNLYGPTEATVNASLARVAEHARPTIGRALANVDLHVVDglgrrktrgaSGELWIGGAGVAR 796
Cdd:cd05907  224 PAelLHFFRALG---IPVYEGYGLTETSAVVTLNPPGDNRIGTVGKPLPGVEVRIAD----------DGEILVRGPNVML 290

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  797 GYAGDAGEAAGRFVEEGWpgsgrlYRSGDLVRWRADGCLEFLGRI-DEQVKINGYRIELGEIRSALLEHPAVGEAAVLTD 875
Cdd:cd05907  291 GYYKNPEATAEALDADGW------LHTGDLGEIDEDGFLHITGRKkDLIITSGGKNISPEPIENALKASPLISQAVVIGD 364

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|..
gi 15597498  876 eadaaepgADRRIVAFVTAAEETAdESWLEVDLPSGHRVAGL 917
Cdd:cd05907  365 --------GRPFLVALIVPDPEAL-EAWAEEHGIAYTDVAEL 397
ttLC_FACS_AlkK_like cd12119
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ...
 475-901 3.03e-25

Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family catalyzes the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified from Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes uncharacterized FACS proteins.


Pssm-ID: 341284 [Multi-domain]  Cd Length: 518  Bit Score: 112.34  E-value: 3.03e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  475 DFATLRARSEAVAEALLAAGVRPGQAVAVMTGRNREAIVALLGVMRAAAVYTPVNPEFPAARVER-MREAG-GIVFAlaD 552
Cdd:cd12119   27 TYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYiINHAEdRVVFV--D 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  553 AECAGRArEAFAGACLDLSTLPLAGSGMSLPAPGG------------------------RDAAYMIFTSGTSGQPKGVV- 607
Cdd:cd12119  105 RDFLPLL-EAIAPRLPTVEHVVVMTDDAAMPEPAGvgvlayeellaaespeydwpdfdeNTAAAICYTSGTTGNPKGVVy 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  608 -----VEHASALNLSQALA---RTVYanvvgegLRVT----VNA---PFSfdssikqilQLLSGHCLVLvPQeVRSDPQR 672
Cdd:cd12119  184 shrslVLHAMAALLTDGLGlseSDVV-------LPVVpmfhVNAwglPYA---------AAMVGAKLVL-PG-PYLDPAS 245

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  673 MLGFLEERRIDVLDCTPSLFRLLLQAGLDDAHPALPGR-ILVGG--------ERFDEASWEVAAGWrrcqvfnlyGPTE- 742
Cdd:cd12119  246 LAELIEREGVTFAAGVPTVWQGLLDHLEANGRDLSSLRrVVIGGsavprsliEAFEERGVRVIHAW---------GMTEt 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  743 ---ATVNASLARVAE-------HARPTIGRALANVDLHVVDGLGRRKTR--GASGELWIGGAGVARGYAGDAGEAAGRFv 810
Cdd:cd12119  317 splGTVARPPSEHSNlsedeqlALRAKQGRPVPGVELRIVDDDGRELPWdgKAVGELQVRGPWVTKSYYKNDEESEALT- 395

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  811 EEGWpgsgrlYRSGDLVRWRADGCLEFLGRIDEQVKINGYRIELGEIRSALLEHPAVGEAAVLTdeadAAEPGADRRIVA 890
Cdd:cd12119  396 EDGW------LRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIG----VPHPKWGERPLA 465

                        490
                 ....*....|....
gi 15597498  891 FVTAAEE---TADE 901
Cdd:cd12119  466 VVVLKEGatvTAEE 479
C_PKS-NRPS cd20483
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
 1362-1686 4.16e-25

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHXXXD motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380471 [Multi-domain]  Cd Length: 430  Bit Score: 110.81  E-value: 4.16e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1362 PMTSLQQGMLLQSEASGDPRLLHNVVLHEVHGRLDGELLARAWAILIGRHAILRTGFdLHGGQVPLQwvHPATAVAAEVP 1441
Cdd:cd20483    3 PMSTFQRRLWFLHNFLEDKTFLNLLLVCHIKGKPDVNLLQKALSELVRRHEVLRTAY-FEGDDFGEQ--QVLDDPSFHLI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1442 VHDLCglDGETRRLRLRAWIEEEQATPFDWSRPPLVRLAALALDERRFALGVAEHHSVLDGWSLQSLVDELLAVYADLLA 1521
Cdd:cd20483   80 VIDLS--EAADPEAALDQLVRNLRRQELDIEEGEVIRGWLVKLPDEEFALVLASHHIAWDRGSSKSIFEQFTALYDALRA 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1522 GVVAREAEAPAVGFRDYVALERE---AEANAASALFWLDYLAGAryrP-----LPGLAEEGPRRM----AAVRVDVPADS 1589
Cdd:cd20483  158 GRDLATVPPPPVQYIDFTLWHNAllqSPLVQPLLDFWKEKLEGI---PdasklLPFAKAERPPVKdyerSTVEATLDKEL 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1590 LSRLRALAERSGLPLRSLLLAAHGRALCRFSDADEVVTGFVSHGRPeEPGADRLLGLFLNTLPCRLSAS-----VDLLDS 1664
Cdd:cd20483  235 LARMKRICAQHAVTPFMFLLAAFRAFLYRYTEDEDLTIGMVDGDRP-HPDFDDLVGFFVNMLPIRCRMDcdmsfDDLLES 313

                        330       340
                 ....*....|....*....|...
gi 15597498 1665 AR-RAFDyeraSLEHRRHPLAAI 1686
Cdd:cd20483  314 TKtTCLE----AYEHSAVPFDYI 332
MACS_like_2 cd05973
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
 474-873 1.67e-24

Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.


Pssm-ID: 341277 [Multi-domain]  Cd Length: 437  Bit Score: 109.14  E-value: 1.67e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  474 LDFATLRARSEAVAEALLAAGVRPGQAVAVMTGRNREAIVALLGVMRAAAVYTPVNPEF-PAARVERMREAGGIVFaLAD 552
Cdd:cd05973    1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFgPKAIEHRLRTSGARLV-VTD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  553 AecAGRAReafagacldLSTLPLAgsgmslpapggrdaayMIFTSGTSGQPKGVVVEhASALNLSQALAR--------TV 624
Cdd:cd05973   80 A--ANRHK---------LDSDPFV----------------MMFTSGTTGLPKGVPVP-LRALAAFGAYLRdavdlrpeDS 131

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  625 YANVV----GEGLRVTVNAPfsfdssikqilqLLSGHCLVLVpqEVRSDPQRMLGFLEERRIDVLDCTPSLFRLLLQAGL 700
Cdd:cd05973  132 FWNAAdpgwAYGLYYAITGP------------LALGHPTILL--EGGFSVESTWRVIERLGVTNLAGSPTAYRLLMAAGA 197

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  701 DdAHPALPGRILVGGERFDEASWEVAAGWRRC---QVFNLYGPTEatVNASLARVAEHARP----TIGRALANVDLHVVD 773
Cdd:cd05973  198 E-VPARPKGRLRRVSSAGEPLTPEVIRWFDAAlgvPIHDHYGQTE--LGMVLANHHALEHPvhagSAGRAMPGWRVAVLD 274

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  774 GLGRRKTRGASGELWIGGAGVA----RGYAGDAGEAAgrfveegwpgSGRLYRSGDLVRWRADGCLEFLGRIDEQVKING 849
Cdd:cd05973  275 DDGDELGPGEPGRLAIDIANSPlmwfRGYQLPDTPAI----------DGGYYLTGDTVEFDPDGSFSFIGRADDVITMSG 344

                        410       420
                 ....*....|....*....|....
gi 15597498  850 YRIELGEIRSALLEHPAVGEAAVL 873
Cdd:cd05973  345 YRIGPFDVESALIEHPAVAEAAVI 368
FACL_DitJ_like cd05934
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 476-872 8.67e-24

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.


Pssm-ID: 341257 [Multi-domain]  Cd Length: 422  Bit Score: 106.61  E-value: 8.67e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  476 FATLRARSEAVAEALLAAGVRPGQAVAVMTGRNREAIVALLGVMRAAAVYTPVNPefpaarvermreaggivfALADAEC 555
Cdd:cd05934    6 YAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINT------------------ALRGDEL 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  556 AGRAREAfaGACLDLStlplagsgmslpapggrDAAYMIFTSGTSGQPKGVVVEHASALNLSQALARtvyANVVGEGLRV 635
Cdd:cd05934   68 AYIIDHS--GAQLVVV-----------------DPASILYTSGTTGPPKGVVITHANLTFAGYYSAR---RFGLGEDDVY 125

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  636 TVNAP-FSFDSSIKQILQ-LLSGHCLVLVPqevRSDPQRMLGFLEERRIDVLDCTPSLFRLLLQA--GLDDAH------- 704
Cdd:cd05934  126 LTVLPlFHINAQAVSVLAaLSVGATLVLLP---RFSASRFWSDVRRYGATVTNYLGAMLSYLLAQppSPDDRAhrlraay 202

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  705 --PALPGRILVGGERFDeaswevaagwrrCQVFNLYGPTEATVNASLARVAEHARPTIGRALANVDLHVVDGLGRRKTRG 782
Cdd:cd05934  203 gaPNPPELHEEFEERFG------------VRLLEGYGMTETIVGVIGPRDEPRRPGSIGRPAPGYEVRIVDDDGQELPAG 270

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  783 ASGELWI---GGAGVARGYAGDAGEAAGRFvEEGWpgsgrlYRSGDLVRWRADGCLEFLGRIDEQVKINGYRIELGEIRS 859
Cdd:cd05934  271 EPGELVIrglRGWGFFKGYYNMPEATAEAM-RNGW------FHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVER 343

                        410
                 ....*....|...
gi 15597498  860 ALLEHPAVGEAAV 872
Cdd:cd05934  344 AILRHPAVREAAV 356
PRK12316 PRK12316
peptide synthase; Provisional
 1391-1778 9.61e-24

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 110.82  E-value: 9.61e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1391 VHGRLDGELLARAWAILIGRHAILRTGFDLHGGQVpLQWVHPATAVaaEVPVHDLCGLDGETRRLRLRAWIEEEQATPFD 1470
Cdd:PRK12316   80 LNGPLDRQALERAFASLVQRHETLRTVFPRGADDS-LAQVPLDRPL--EVEFEDCSGLPEAEQEARLRDEAQRESLQPFD 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1471 WSRPPLVRLAALALDERRFALGVAEHHSVLDGWSLQSLVDELLAVYADLLAGvvaREAEAPA--VGFRDYVALER---EA 1545
Cdd:PRK12316  157 LCEGPLLRVRLLRLGEEEHVLLLTLHHIVSDGWSMNVLIEEFSRFYSAYATG---AEPGLPAlpIQYADYALWQRswlEA 233

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1546 EANAASALFWLDYLAGAryRPLPGLAEEGPR------RMAAVRVDVPADSLSRLRALAERSGLPLRSLLLAAHGRALCRF 1619
Cdd:PRK12316  234 GEQERQLEYWRAQLGEE--HPVLELPTDHPRpavpsyRGSRYEFSIDPALAEALRGTARRQGLTLFMLLLGAFNVLLHRY 311

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1620 SDADEVVTGFVSHGRpEEPGADRLLGLFLNTLPCR----LSASV-DLLDSARRAFDYERASLEHRRHPLAAIRRRNRELR 1694
Cdd:PRK12316  312 SGQTDIRVGVPIANR-NRAEVEGLIGFFVNTQVLRsvfdGRTRVaTLLAGVKDTVLGAQAHQDLPFERLVEALKVERSLS 390

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1695 LDSLFNFVDFHQDDAAPAGVRHGGILDQVVVDVDVPLAVDFEVA------GERLEVGFQYAAGRFPAERAEALAGAYREA 1768
Cdd:PRK12316  391 HSPLFQVMYNHQPLVADIEALDTVAGLEFGQLEWKSRTTQFDLTldtyekGGRLHAALTYATDLFEARTVERMARHWQNL 470

                         410
                  ....*....|
gi 15597498  1769 LLALLGDPVQ 1778
Cdd:PRK12316  471 LRGMVENPQA 480
MACS_like_1 cd05974
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
 474-873 1.17e-23

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: 341278 [Multi-domain]  Cd Length: 432  Bit Score: 106.50  E-value: 1.17e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  474 LDFATLRARSEAVAEALLAAGVRPGQAVAVMTGRNREAIVALLGVMRAAAVYTPVNPEFPAARVERMREAGGIVFALADA 553
Cdd:cd05974    1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDLRDRVDRGGAVYAAVDE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  554 ECAGRareafagacldlstlplagsgmslpapggrDAAYMIFTSGTSGQPKgvVVEHASALNLSQALARTVYANVVGEGL 633
Cdd:cd05974   81 NTHAD------------------------------DPMLLYFTSGTTSKPK--LVEHTHRSYPVGHLSTMYWIGLKPGDV 128

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  634 RVTVNAPFSFDSSIKQILQLLSGHCLVLVPQEVRSDPQRMLGFLEERRIDVLDCTPSLFRLLLQAGLddAHPALPGRILV 713
Cdd:cd05974  129 HWNISSPGWAKHAWSCFFAPWNAGATVFLFNYARFDAKRVLAALVRYGVTTLCAPPTVWRMLIQQDL--ASFDVKLREVV 206

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  714 G-GERFD-EASWEVAAGWRRcQVFNLYGPTEATVNASLARVAEHARPTIGRALANVDLHVVDGLGRRKTRGASGeLWIGG 791
Cdd:cd05974  207 GaGEPLNpEVIEQVRRAWGL-TIRDGYGQTETTALVGNSPGQPVKAGSMGRPLPGYRVALLDPDGAPATEGEVA-LDLGD 284

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  792 ---AGVARGYAGDAGEAAGRFveegwpgSGRLYRSGDLVRWRADGCLEFLGRIDEQVKINGYRIELGEIRSALLEHPAVG 868
Cdd:cd05974  285 trpVGLMKGYAGDPDKTAHAM-------RGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAVA 357


                 ....*
gi 15597498  869 EAAVL 873
Cdd:cd05974  358 EAAVV 362
LCL_NRPS-like cd19540
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ...
 1392-1668 3.24e-23

LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380463 [Multi-domain]  Cd Length: 433  Bit Score: 105.20  E-value: 3.24e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1392 HGRLDGELLARAWAILIGRHAILRTGFDLHGGqVPLQWVHPATAVAAEVPVHDLcgldGETRrlrLRAWIEEEQATPFDW 1471
Cdd:cd19540   33 TGALDVDALRAALADVVARHESLRTVFPEDDG-GPYQVVLPAAEARPDLTVVDV----TEDE---LAARLAEAARRGFDL 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1472 SRPPLVRLAALALDERRFALGVAEHHSVLDGWSLQSLVDELLAVYADLLAGvVAREAEAPAVGFRDYVALERE---AEAN 1548
Cdd:cd19540  105 TAELPLRARLFRLGPDEHVLVLVVHHIAADGWSMAPLARDLATAYAARRAG-RAPDWAPLPVQYADYALWQREllgDEDD 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1549 AASAL-----FWLDYLAGARY-------RPLPGLAEegpRRMAAVRVDVPADSLSRLRALAERSGLPLRSLLLAAHGRAL 1616
Cdd:cd19540  184 PDSLAarqlaYWRETLAGLPEelelptdRPRPAVAS---YRGGTVEFTIDAELHARLAALAREHGATLFMVLHAALAVLL 260

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 15597498 1617 CRFSDADEVVTGFVSHGRPEEpGADRLLGLFLNTLPCRLSAS-----VDLLDSARRA 1668
Cdd:cd19540  261 SRLGAGDDIPIGTPVAGRGDE-ALDDLVGMFVNTLVLRTDVSgdptfAELLARVRET 316
alpha_am_amid TIGR03443
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ...
 494-869 3.93e-23

L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.


Pssm-ID: 274582 [Multi-domain]  Cd Length: 1389  Bit Score: 108.23  E-value: 3.93e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498    494 GVRPGQAVAVMTGRNREAIVALLGVMRAAAVYTPVNPEFPAAR------VERMReaggivfALADAECAGRAR---EAFA 564
Cdd:TIGR03443  291 GIKRGDVVMIYAYRGVDLVVAVMGVLKAGATFSVIDPAYPPARqtiylsVAKPR-------ALIVIEKAGTLDqlvRDYI 363

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498    565 GACLDLST----LPLAGSGM---SLPAPGGRD--AAY-------------------MIFTSGTSGQPKGVVVEHASAlnl 616
Cdd:TIGR03443  364 DKELELRTeipaLALQDDGSlvgGSLEGGETDvlAPYqalkdtptgvvvgpdsnptLSFTSGSEGIPKGVLGRHFSL--- 440

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498    617 sqalarTVYANVVGEGLRVTVNAPFSFDSSI------KQILQLLSGHCLVLVP-QEVRSDPQRMLGFLEERRIDVLDCTP 689
Cdd:TIGR03443  441 ------AYYFPWMAKRFGLSENDKFTMLSGIahdpiqRDMFTPLFLGAQLLVPtADDIGTPGRLAEWMAKYGATVTHLTP 514

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498    690 SLFRLLlQAGLDDAHPALPGRILVGG--ERFDEASWEVAAgwRRCQVFNLYGPTEATVNASLARVAEHAR-PTI------ 760
Cdd:TIGR03443  515 AMGQLL-SAQATTPIPSLHHAFFVGDilTKRDCLRLQTLA--ENVCIVNMYGTTETQRAVSYFEIPSRSSdSTFlknlkd 591

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498    761 ----GRALANVDLHVVDGLGRRKT--RGASGELWIGGAGVARGYAGDAGEAAGRFV---------------------EEG 813
Cdd:TIGR03443  592 vmpaGKGMKNVQLLVVNRNDRTQTcgVGEVGEIYVRAGGLAEGYLGLPELNAEKFVnnwfvdpshwidldkennkpeREF 671

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 15597498    814 WPG-SGRLYRSGDLVRWRADGCLEFLGRIDEQVKINGYRIELGEIRSALLEHPAVGE 869
Cdd:TIGR03443  672 WLGpRDRLYRTGDLGRYLPDGNVECCGRADDQVKIRGFRIELGEIDTHLSQHPLVRE 728
ACS-like cd17634
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ...
 494-906 9.58e-23

acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.


Pssm-ID: 341289 [Multi-domain]  Cd Length: 587  Bit Score: 105.35  E-value: 9.58e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  494 GVRPGQAVAVMTGRNREAIVALLGVMRAAAVYTPVNPEF-PAARVERMREAGGIVFALADAEC-AGRA------------ 559
Cdd:cd17634  105 GVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFaPEAVAGRIIDSSSRLLITADGGVrAGRSvplkknvddaln 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  560 -------------REAFA-----GACLDLSTLPLAGSGMSLPAP-GGRDAAYMIFTSGTSGQPKGVVVEHAS-ALNLSQA 619
Cdd:cd17634  185 pnvtsvehvivlkRTGSDidwqeGRDLWWRDLIAKASPEHQPEAmNAEDPLFILYTSGTTGKPKGVLHTTGGyLVYAATT 264

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  620 LaRTVYANVVGEGLRVTVNAPFSFDSSIKQILQLLSGHCLVL---VPqeVRSDPQRMLGFLEERRIDVLDCTPSLFRLLL 696
Cdd:cd17634  265 M-KYVFDYGPGDIYWCTADVGWVTGHSYLLYGPLACGATTLLyegVP--NWPTPARMWQVVDKHGVNILYTAPTAIRALM 341

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  697 QAGLD--DAHPALPGRILVG-GERFDEASWEVAA---GWRRCQVFNLYGPTEAT----VNASLARVAEHARPTigRALAN 766
Cdd:cd17634  342 AAGDDaiEGTDRSSLRILGSvGEPINPEAYEWYWkkiGKEKCPVVDTWWQTETGgfmiTPLPGAIELKAGSAT--RPVFG 419

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  767 VDLHVVDGLGRRKTRGASGELWIGGA--GVARGYAGDAGeaagRFVEEGWPGSGRLYRSGDLVRWRADGCLEFLGRIDEQ 844
Cdd:cd17634  420 VQPAVVDNEGHPQPGGTEGNLVITDPwpGQTRTLFGDHE----RFEQTYFSTFKGMYFSGDGARRDEDGYYWITGRSDDV 495

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15597498  845 VKINGYRIELGEIRSALLEHPAVGEAAVLtdeaDAAEPGADRRIVAFVT--AAEETADESWLEV 906
Cdd:cd17634  496 INVAGHRLGTAEIESVLVAHPKVAEAAVV----GIPHAIKGQAPYAYVVlnHGVEPSPELYAEL 555
FAA1 COG1022
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
440-905 9.08e-22

Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];


Pssm-ID: 440645 [Multi-domain]  Cd Length: 603  Bit Score: 102.49  E-value: 9.08e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  440 ERVEPAPVESLVAAFDLRAALQPQAPALLDAHG----SLDFATLRARSEAVAEALLAAGVRPGQAVAVMtGRNR-EAIVA 514
Cdd:COG1022    3 EFSDVPPADTLPDLLRRRAARFPDRVALREKEDgiwqSLTWAEFAERVRALAAGLLALGVKPGDRVAIL-SDNRpEWVIA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  515 LLGVMRAAAVYTPVNPEFPAARVERMREAGGIVFALA-DAECAGRAREAFAGA-------------------CLDLSTLP 574
Cdd:COG1022   82 DLAILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFVeDQEQLDKLLEVRDELpslrhivvldprglrddprLLSLDELL 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  575 LAGSGMSLP--------APGGRDAAYMIFTSGTSGQPKGVVVEHAS----ALNLSQALART-------------VYANVV 629
Cdd:COG1022  162 ALGREVADPaelearraAVKPDDLATIIYTSGTTGRPKGVMLTHRNllsnARALLERLPLGpgdrtlsflplahVFERTV 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  630 GEGL---RVTVNapfsFDSSIKQILQLLsghclvlvpQEVRsdPQRMLG---FLE------ERRIDvlDCTP---SLFRL 694
Cdd:COG1022  242 SYYAlaaGATVA----FAESPDTLAEDL---------REVK--PTFMLAvprVWEkvyagiQAKAE--EAGGlkrKLFRW 304

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  695 LLQAGLDDAHPALPGRILVGGER--FDEASWEVAAGWR-----RCQ-----------------------VFNLYGPTEAT 744
Cdd:COG1022  305 ALAVGRRYARARLAGKSPSLLLRlkHALADKLVFSKLRealggRLRfavsggaalgpelarffralgipVLEGYGLTETS 384

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  745 VNASlARVAEHARP-TIGRALANVDLHVvdglgrrktrGASGELWIGGAGVARGYAGDAGEAAGRFVEEGWpgsgrlYRS 823
Cdd:COG1022  385 PVIT-VNRPGDNRIgTVGPPLPGVEVKI----------AEDGEILVRGPNVMKGYYKNPEATAEAFDADGW------LHT 447

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  824 GDLVRWRADGCLEFLGRIDEQVKI-NGYRIELGEIRSALLEHPAVGEAAVLtdeadaaepGADRR-IVAFVTAAEETAdE 901
Cdd:COG1022  448 GDIGELDEDGFLRITGRKKDLIVTsGGKNVAPQPIENALKASPLIEQAVVV---------GDGRPfLAALIVPDFEAL-G 517


                 ....
gi 15597498  902 SWLE 905
Cdd:COG1022  518 EWAE 521
PRK07788 PRK07788
acyl-CoA synthetase; Validated
 458-899 9.40e-22

acyl-CoA synthetase; Validated


Pssm-ID: 236097 [Multi-domain]  Cd Length: 549  Bit Score: 101.93  E-value: 9.40e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   458 AALQPQAPALLDAHGSLDFATLRARSEAVAEALLAAGVRPGQAVAVMTGRNREAIVALLGVMRAAAVYTPVNPEFPAARV 537
Cdd:PRK07788   59 ARRAPDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGPQL 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   538 ERMREAGGIVFALADAECAGRAR-------------------EAFAGACLDLSTLPLAGSGMSLPAPgGRDAAYMIFTSG 598
Cdd:PRK07788  139 AEVAAREGVKALVYDDEFTDLLSalppdlgrlrawggnpdddEPSGSTDETLDDLIAGSSTAPLPKP-PKPGGIVILTSG 217

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   599 TSGQPKGVVVEHASALN-LSQALAR------------------TVYAN-VVGEGLRVTVNAPFSFDSsiKQILQLLSGH- 657
Cdd:PRK07788  218 TTGTPKGAPRPEPSPLApLAGLLSRvpfragettllpapmfhaTGWAHlTLAMALGSTVVLRRRFDP--EATLEDIAKHk 295

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   658 --CLVLVPQEVrsdpQRMLGFLEERRIDVlDCtpSLFRLLLQAGlddahPALPGRIlvgGERFDEASWEVaagwrrcqVF 735
Cdd:PRK07788  296 atALVVVPVML----SRILDLGPEVLAKY-DT--SSLKIIFVSG-----SALSPEL---ATRALEAFGPV--------LY 352

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   736 NLYGPTEATVnASLARVAEHARP--TIGRALANVDLHVVDGLGRRKTRGASGELWIGGAGVARGYAGDAGEAagrfVEEG 813
Cdd:PRK07788  353 NLYGSTEVAF-ATIATPEDLAEApgTVGRPPKGVTVKILDENGNEVPRGVVGRIFVGNGFPFEGYTDGRDKQ----IIDG 427

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   814 wpgsgrLYRSGDLVRWRADGCLEFLGRIDEQVKINGYRIELGEIRSALLEHPAVGEAAVLTDEADaaEPGAdrRIVAFVT 893
Cdd:PRK07788  428 ------LLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDE--EFGQ--RLRAFVV 497


                  ....*.
gi 15597498   894 AAEETA 899
Cdd:PRK07788  498 KAPGAA 503
MACS_like_3 cd05971
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
 476-873 1.40e-21

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: 100.20  E-value: 1.40e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  476 FATLRARSEAVAEALLAAGVRPGQAVAVMTGRNREAIVALLGVMRAAAVYTPVNPEFPAARVErmreaggivFALADAEc 555
Cdd:cd05971    9 FKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALE---------YRLSNSG- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  556 agrareafaGACL--DLSTlplagsgmslpapggrDAAYMIFTSGTSGQPKG------VVVEHASALNLSQALARTvyan 627
Cdd:cd05971   79 ---------ASALvtDGSD----------------DPALIIYTSGTTGPPKGalhahrVLLGHLPGVQFPFNLFPR---- 129

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  628 vvgEGLRVTVNAPFSFDSSIKQILQLLSGHCLVLVPQEVRS-DPQRMLGFLEERRIDVLDCTPSLFRLLLQAGLDDAHPA 706
Cdd:cd05971  130 ---DGDLYWTPADWAWIGGLLDVLLPSLYFGVPVLAHRMTKfDPKAALDLMSRYGVTTAFLPPTALKMMRQQGEQLKHAQ 206

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  707 LPGRILVGGerfDEASWEVAAGWRRCQ----VFNLYGPTEATVNASLARVAEHARP-TIGRALANVDLHVVDGLGRRKTR 781
Cdd:cd05971  207 VKLRAIATG---GESLGEELLGWAREQfgveVNEFYGQTECNLVIGNCSALFPIKPgSMGKPIPGHRVAIVDDNGTPLPP 283

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  782 GASGELwiggaGVAR-------GYAGDAGEAAGRFVeegwpgsGRLYRSGDLVRWRADGCLEFLGRIDEQVKINGYRIEL 854
Cdd:cd05971  284 GEVGEI-----AVELpdpvaflGYWNNPSATEKKMA-------GDWLLTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGP 351

                        410
                 ....*....|....*....
gi 15597498  855 GEIRSALLEHPAVGEAAVL 873
Cdd:cd05971  352 AEIEECLLKHPAVLMAAVV 370
PRK07470 PRK07470
acyl-CoA synthetase; Validated
 458-873 2.06e-21

acyl-CoA synthetase; Validated


Pssm-ID: 180988 [Multi-domain]  Cd Length: 528  Bit Score: 100.50  E-value: 2.06e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   458 AALQPQAPALLDAHGSLDFATLRARSEAVAEALLAAGVRPGQAVAVMTGRNREAIVALLGVMRAAAVYTPVNPEFPAARV 537
Cdd:PRK07470   17 ARRFPDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQTPDEV 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   538 ERMREAGGIVFALADAECAGRAREAFAGACLDLSTLPLAGSGMSLP-------APGGR---------DAAYMIFTSGTSG 601
Cdd:PRK07470   97 AYLAEASGARAMICHADFPEHAAAVRAASPDLTHVVAIGGARAGLDyealvarHLGARvanaavdhdDPCWFFFTSGTTG 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   602 QPKGVVVEHAS-ALNLSQALARTVYAnvVGEGLRVTVNAPFSFDSSIKQILQLLSGHCLVLVPQEvRSDPQRMLGFLEER 680
Cdd:PRK07470  177 RPKAAVLTHGQmAFVITNHLADLMPG--TTEQDASLVVAPLSHGAGIHQLCQVARGAATVLLPSE-RFDPAEVWALVERH 253

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   681 RIDVLDCTPSLFRLLLQaglddaHPALpgrilvggERFDEAS--WEVAAG---WRRCQVFNL----------YGPTEATV 745
Cdd:PRK07470  254 RVTNLFTVPTILKMLVE------HPAV--------DRYDHSSlrYVIYAGapmYRADQKRALaklgkvlvqyFGLGEVTG 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   746 NASLARVAEHARP--------TIGRALANVDLHVVDGLGRRKTRGASGELWIGGAGVARGYAGDAgEAAGRFVEEGWpgs 817
Cdd:PRK07470  320 NITVLPPALHDAEdgpdarigTCGFERTGMEVQIQDDEGRELPPGETGEICVIGPAVFAGYYNNP-EANAKAFRDGW--- 395

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 15597498   818 grlYRSGDLVRWRADGCLEFLGRIDEQVKINGYRIELGEIRSALLEHPAVGEAAVL 873
Cdd:PRK07470  396 ---FRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVL 448
23DHB-AMP_lg cd05920
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ...
 428-897 2.12e-21

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: 100.09  E-value: 2.12e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  428 AAERERYQAWQGErvepaPVESLVAAfdlRAALQPQAPALLDAHGSLDFATLRARSEAVAEALLAAGVRPGQAVAVMTGR 507
Cdd:cd05920    3 ARRYRAAGYWQDE-----PLGDLLAR---SAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPN 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  508 NREAIVALLGVMRAAAVytPVNpefpAARVERMREAGGIV-FALADAECAGRAREAFAGACLdlstlplagsgMSLPAPG 586
Cdd:cd05920   75 VAEFVVLFFALLRLGAV--PVL----ALPSHRRSELSAFCaHAEAVAYIVPDRHAGFDHRAL-----------ARELAES 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  587 GRDAAYMIFTSGTSGQPKGVVVEH--------ASAlNLSQALARTVYANVVGEGLRVTVNAPFSFDSsikqilqLLSGHC 658
Cdd:cd05920  138 IPEVALFLLSGGTTGTPKLIPRTHndyaynvrASA-EVCGLDQDTVYLAVLPAAHNFPLACPGVLGT-------LLAGGR 209

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  659 LVLVPqevRSDPQRMLGFLEERRIDVLDCTPSLFRLLLQAGLDDAHPALPGRIL-VGGERFDEASWEVAAGWRRCQVFNL 737
Cdd:cd05920  210 VVLAP---DPSPDAAFPLIEREGVTVTALVPALVSLWLDAAASRRADLSSLRLLqVGGARLSPALARRVPPVLGCTLQQV 286

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  738 YGPTEATVNAS-LARVAEHARPTIGRALANVD-LHVVDGLGRRKTRGASGELWIGGAGVARGYAGDAGEAAGRFVEEGWp 815
Cdd:cd05920  287 FGMAEGLLNYTrLDDPDEVIIHTQGRPMSPDDeIRVVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPDGF- 365

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  816 gsgrlYRSGDLVRWRADGCLEFLGRIDEQVKINGYRIELGEIRSALLEHPAVGEAAVLTdeadAAEPGADRRIVAFVTAA 895
Cdd:cd05920  366 -----YRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVA----MPDELLGERSCAFVVLR 436


                 ..
gi 15597498  896 EE 897
Cdd:cd05920  437 DP 438
PRK12467 PRK12467
peptide synthase; Provisional
 1198-1372 5.54e-21

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 101.39  E-value: 5.54e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1198 QALRGFLEARLPAYMLPSRIARVERLPLTAEGKLDRRALLAALAAEAAAQTLeaPANATEAALLEIWKSVLKRPAIGVSD 1277
Cdd:PRK12467 3550 ETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDRKALPDPDAKGSREYVA--PRSEVEQQLAAIWADVLGVEQVGVTD 3627

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1278 NFFQVGGDSIRLIQMQVMAREA-GLAFTLRDVFNHQSIRELA------RLLAAPASPADALGTSAPQSLEPFALL-SAAE 1349
Cdd:PRK12467 3628 NFFELGGDSLLALQVLSRIRQSlGLKLSLRDLMSAPTIAELAgysplgDVPVNLLLDLNRLETGFPALFCRHEGLgTVFD 3707

                         170       180
                  ....*....|....*....|...
gi 15597498  1350 RKRLPEGLDDAYPMTSLQQGMLL 1372
Cdd:PRK12467 3708 YEPLAVILEGDRHVLGLTCRHLL 3730
OSB_MenE-like cd17630
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ...
 591-905 8.47e-21

O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.


Pssm-ID: 341285 [Multi-domain]  Cd Length: 325  Bit Score: 95.86  E-value: 8.47e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  591 AYMIFTSGTSGQPKGVVVEHAsalnlsqalarTVYANVVGeglrvtVNAPFSFDSSIKQILQLLSGH---------CL-- 659
Cdd:cd17630    3 ATVILTSGSTGTPKAVVHTAA-----------NLLASAAG------LHSRLGFGGGDSWLLSLPLYHvgglailvrSLla 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  660 --VLVPQEVRSDPQRMLgflEERRIDVLDCTPSLFRLLLQAGLDDAHPALPGRILVGG--------ERFDEASWEVAAGw 729
Cdd:cd17630   66 gaELVLLERNQALAEDL---APPGVTHVSLVPTQLQRLLDSGQGPAALKSLRAVLLGGapippellERAADRGIPLYTT- 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  730 rrcqvfnlYGPTEATVNASLARVAEHARPTIGRALANVDLHVVDGlgrrktrgasGELWIGGAGVARGYAgdAGEAAGRF 809
Cdd:cd17630  142 --------YGMTETASQVATKRPDGFGRGGVGVLLPGRELRIVED----------GEIWVGGASLAMGYL--RGQLVPEF 201

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  810 VEEGWpgsgrlYRSGDLVRWRADGCLEFLGRIDEQVKINGYRIELGEIRSALLEHPAVGEAAVLtDEADaAEPGAdrRIV 889
Cdd:cd17630  202 NEDGW------FTTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVV-GVPD-EELGQ--RPV 271

                        330
                 ....*....|....*.
gi 15597498  890 AFVTAAEETADESWLE 905
Cdd:cd17630  272 AVIVGRGPADPAELRA 287
PRK05852 PRK05852
fatty acid--CoA ligase family protein;
449-875 1.27e-20

fatty acid--CoA ligase family protein;


Pssm-ID: 235625 [Multi-domain]  Cd Length: 534  Bit Score: 98.42  E-value: 1.27e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   449 SLVAAFDLRAALQPQAPALL--DAHGSLDFATLRARSEAVAEALLAAGVRPGQAVAVMTGRNREAIVALLGVMRAAAVYT 526
Cdd:PRK05852   17 RIADLVEVAATRLPEAPALVvtADRIAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVV 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   527 PVNPEFPAA-RVERMREAGG-IVFALADAEC---------------AGRAREAFAGAC---LDLSTLPLAGSgmSLPAPG 586
Cdd:PRK05852   97 PLDPALPIAeQRVRSQAAGArVVLIDADGPHdraepttrwwpltvnVGGDSGPSGGTLsvhLDAATEPTPAT--STPEGL 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   587 GRDAAYMIFTSGTSGQPKGVVVEHASalnlsqaLARTVYANVVGEGL-----RVTVNAPFSFDSSIKQILQLLSGHCLVL 661
Cdd:PRK05852  175 RPDDAMIMFTGGTTGLPKMVPWTHAN-------IASSVRAIITGYRLsprdaTVAVMPLYHGHGLIAALLATLASGGAVL 247

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   662 VPQEVRSDPQRmlgFLEErrIDVLDCT-----PSLFRLLLQAGLDDAHPALPGRIlvggeRF--------DEASWEVAAG 728
Cdd:PRK05852  248 LPARGRFSAHT---FWDD--IKAVGATwytavPTIHQILLERAATEPSGRKPAAL-----RFirscsaplTAETAQALQT 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   729 WRRCQVFNLYGPTEATVNASLARVAEHAR---PTIGRALAN----VDLHVVDGLGRRKTRGASGELWIGGAGVARGYAGD 801
Cdd:PRK05852  318 EFAAPVVCAFGMTEATHQVTTTQIEGIGQtenPVVSTGLVGrstgAQIRIVGSDGLPLPAGAVGEVWLRGTTVVRGYLGD 397

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15597498   802 AGEAAGRFVeEGWpgsgrlYRSGDLVRWRADGCLEFLGRIDEQVKINGYRIELGEIRSALLEHPAVGEAAVLTD 875
Cdd:PRK05852  398 PTITAANFT-DGW------LRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGV 464
ABCL cd05958
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ...
 464-899 1.94e-20

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: 96.78  E-value: 1.94e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  464 APALLDAHGSLDFATLRARS-EAVAEALLAAGVRPGQAVAVMTGRNREAIVALLGVMRAAAVYTPVNPEFPAARVERMRE 542
Cdd:cd05958    1 RTCLRSPEREWTYRDLLALAnRIANVLVGELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  543 AGGIVFALadaeCAGRAREAfagacldlstlplagsgmslpapggRDAAYMIFTSGTSGQPKGVVVEHASALNLSQALAR 622
Cdd:cd05958   81 KARITVAL----CAHALTAS-------------------------DDICILAFTSGTTGAPKATMHFHRDPLASADRYAV 131

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  623 tvyaNVVG--EGLRVTVNAP--FSFDSSIKQILQLLSGHCLVLVPQEVrsdPQRMLGFLEERRIDVLDCTPSLFRLLLqA 698
Cdd:cd05958  132 ----NVLRlrEDDRFVGSPPlaFTFGLGGVLLFPFGVGASGVLLEEAT---PDLLLSAIARYKPTVLFTAPTAYRAML-A 203

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  699 GLDDAHPALPG--RILVGGERFDEASWEVaagWRRC---QVFNLYGPTEAtVNASLARVAEHARP-TIGRALANVDLHVV 772
Cdd:cd05958  204 HPDAAGPDLSSlrKCVSAGEALPAALHRA---WKEAtgiPIIDGIGSTEM-FHIFISARPGDARPgATGKPVPGYEAKVV 279

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  773 DGLGRRKTRGASGELWIGGAgvaRGYAGDAGEAAGRFVEEGWPGSGRLYRSGdlvrwrADGCLEFLGRIDEQVKINGYRI 852
Cdd:cd05958  280 DDEGNPVPDGTIGRLAVRGP---TGCRYLADKRQRTYVQGGWNITGDTYSRD------PDGYFRHQGRSDDMIVSGGYNI 350

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*....
gi 15597498  853 ELGEIRSALLEHPAVGEAAVLtdeadaAEPGADRRIV--AFVTAAEETA 899
Cdd:cd05958  351 APPEVEDVLLQHPAVAECAVV------GHPDESRGVVvkAFVVLRPGVI 393
PRK08316 PRK08316
acyl-CoA synthetase; Validated
 458-872 2.08e-20

acyl-CoA synthetase; Validated


Pssm-ID: 181381 [Multi-domain]  Cd Length: 523  Bit Score: 97.31  E-value: 2.08e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   458 AALQPQAPALLDAHGSLDFATLRARSEAVAEALLAAGVRPGQAVAVMtGRNREAIVAL-LGVMRAAAVYTPVNPEFPAAR 536
Cdd:PRK08316   21 ARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAAL-GHNSDAYALLwLACARAGAVHVPVNFMLTGEE 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   537 VERMREAGGIVFALADAECAGRAREAFAGACLDLSTLPLAGSG--------------------MSLPAPGGRDAAYMIFT 596
Cdd:PRK08316  100 LAYILDHSGARAFLVDPALAPTAEAALALLPVDTLILSLVLGGreapggwldfadwaeagsvaEPDVELADDDLAQILYT 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   597 SGTSGQPKGVVVEHasalnlsQALARTVYANVVGEGLR---VTVNAPFSFDSSIKQIL---QLLSGHCLVLVPqevRSDP 670
Cdd:PRK08316  180 SGTESLPKGAMLTH-------RALIAEYVSCIVAGDMSaddIPLHALPLYHCAQLDVFlgpYLYVGATNVILD---APDP 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   671 QRMLGFLEERRIDVLDCTPSLFRLLLQaglddaHPALPGRILVGGER-FDEASW---EVAAGWRRC----QVFNLYGPTE 742
Cdd:PRK08316  250 ELILRTIEAERITSFFAPPTVWISLLR------HPDFDTRDLSSLRKgYYGASImpvEVLKELRERlpglRFYNCYGQTE 323

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   743 ATVNASLARVAEHAR--PTIGRALANVDLHVVDGLGRRKTRGASGELWIGGAGVARGYAGDAGEAAGRFvEEGWpgsgrl 820
Cdd:PRK08316  324 IAPLATVLGPEEHLRrpGSAGRPVLNVETRVVDDDGNDVAPGEVGEIVHRSPQLMLGYWDDPEKTAEAF-RGGW------ 396

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 15597498   821 YRSGDLVRWRADGCLEFLGRIDEQVKINGYRIELGEIRSALLEHPAVGEAAV 872
Cdd:PRK08316  397 FHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAV 448
LC_FACS_like cd05935
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ...
 473-884 3.37e-20

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: 96.01  E-value: 3.37e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  473 SLDFATLRARSEAVAEALLAAGVRPGQAVAVMTGRNREAIVALLGVMRAAAVYTPVNPEFPAARVErmreaggivFALAD 552
Cdd:cd05935    1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELE---------YILND 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  553 AEcagrAREAFAGACLDlstlplagsgmslpapggrDAAYMIFTSGTSGQPKGVVVEHASAlnLSQALARTVYANVVGEG 632
Cdd:cd05935   72 SG----AKVAVVGSELD-------------------DLALIPYTSGTTGLPKGCMHTHFSA--AANALQSAVWTGLTPSD 126

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  633 LRVTVNAPF---SFDSSIKqiLQLLSGHCLVLVpqeVRSDPQRMLGFLEERRIDVLDCTPSLFRLLLQAGLDDAHPALPG 709
Cdd:cd05935  127 VILACLPLFhvtGFVGSLN--TAVYVGGTYVLM---ARWDRETALELIEKYKVTFWTNIPTMLVDLLATPEFKTRDLSSL 201

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  710 RILVGGerfdEASWEVAAGWRRCQVFNL-----YGPTEATvnaSLARVAEHARP---TIGRALANVDLHVVD-GLGRRKT 780
Cdd:cd05935  202 KVLTGG----GAPMPPAVAEKLLKLTGLrfvegYGLTETM---SQTHTNPPLRPklqCLGIP*FGVDARVIDiETGRELP 274

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  781 RGASGELWIGGAGVARGYAGDAGEAAGRFVEEgwpGSGRLYRSGDLVRWRADGCLEFLGRIDEQVKINGYRIELGEIRSA 860
Cdd:cd05935  275 PNEVGEIVVRGPQIFKGYWNRPEETEESFIEI---KGRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAK 351

                        410       420
                 ....*....|....*....|....*.
gi 15597498  861 LLEHPAVGEAAVLT--DEADAAEPGA 884
Cdd:cd05935  352 LYKHPAI*EVCVISvpDERVGEEVKA 377
PRK09088 PRK09088
acyl-CoA synthetase; Validated
 456-873 4.41e-20

acyl-CoA synthetase; Validated


Pssm-ID: 181644 [Multi-domain]  Cd Length: 488  Bit Score: 96.03  E-value: 4.41e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   456 LRAALQPQAPALLDAHGSLD--FATLRARSEAVAEALLAAGVRPGQAVAVMtGRNREAIVAL-LGVMRAAAVYTPVNPEF 532
Cdd:PRK09088    3 FHARLQPQRLAAVDLALGRRwtYAELDALVGRLAAVLRRRGCVDGERLAVL-ARNSVWLVALhFACARVGAIYVPLNWRL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   533 PAARVERMREAGGIVFALADAECAgrareafAGACLDLSTLPLAGS----GMSLPAPGGRDAAYMI-FTSGTSGQPKGVV 607
Cdd:PRK09088   82 SASELDALLQDAEPRLLLGDDAVA-------AGRTDVEDLAAFIASadalEPADTPSIPPERVSLIlFTSGTSGQPKGVM 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   608 VehaSALNLSQALARTVYANVVGEGLRVTVNAP-FSFDSSIKQILQLLSGHCLVLVPQEVrsDPQRMLGFLEERRIDVLD 686
Cdd:PRK09088  155 L---SERNLQQTAHNFGVLGRVDAHSSFLCDAPmFHIIGLITSVRPVLAVGGSILVSNGF--EPKRTLGRLGDPALGITH 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   687 --CTPSLFRLLL-QAGLDDAHPALPGRILVGGERFDEAS--WEVAAGWRrcqVFNLYGPTEATVNASLARVAEHARPTIG 761
Cdd:PRK09088  230 yfCVPQMAQAFRaQPGFDAAALRHLTALFTGGAPHAAEDilGWLDDGIP---MVDGFGMSEAGTVFGMSVDCDVIRAKAG 306

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   762 RA---LANVDLHVVDGLGRRKTRGASGELWIGGAGVARGYAGDAGEAAGRFVEEGWpgsgrlYRSGDLVRWRADGCLEFL 838
Cdd:PRK09088  307 AAgipTPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFTGDGW------FRTGDIARRDADGFFWVV 380

                         410       420       430
                  ....*....|....*....|....*....|....*
gi 15597498   839 GRIDEQVKINGYRIELGEIRSALLEHPAVGEAAVL 873
Cdd:PRK09088  381 DRKKDMFISGGENVYPAEIEAVLADHPGIRECAVV 415
PRK13383 PRK13383
acyl-CoA synthetase; Provisional
 458-894 4.89e-20

acyl-CoA synthetase; Provisional


Pssm-ID: 139531 [Multi-domain]  Cd Length: 516  Bit Score: 96.22  E-value: 4.89e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   458 AALQPQAPALLDAHGSLDFATLRARSEAVAEALLAAGVRPGQAVAVMTGRNREAIVALLGVMRAAAVYTPVNPEFPAARV 537
Cdd:PRK13383   45 AARWPGRTAIIDDDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDAL 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   538 ERMREAGGIVFALADAECAGR-AREAFAGACLDLSTLPLAGSGMSLP-APGGRdaaYMIFTSGTSGQPKGV--VVEHASA 613
Cdd:PRK13383  125 AAALRAHHISTVVADNEFAERiAGADDAVAVIDPATAGAEESGGRPAvAAPGR---IVLLTSGTTGKPKGVprAPQLRSA 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   614 LNLSQALARTVYANVvgeGLRVTVNAPFSFDSSIKQILQLLSGHCLVLVPQEVrsDPQRMLGFLEERRIDVLDCTP-SLF 692
Cdd:PRK13383  202 VGVWVTILDRTRLRT---GSRISVAMPMFHGLGLGMLMLTIALGGTVLTHRHF--DAEAALAQASLHRADAFTAVPvVLA 276

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   693 RLLLQAGLDDAHPALPG-RILVG---------GERFDEASWEVaagwrrcqVFNLYGPTEATVNAsLARVAE--HARPTI 760
Cdd:PRK13383  277 RILELPPRVRARNPLPQlRVVMSsgdrldptlGQRFMDTYGDI--------LYNGYGSTEVGIGA-LATPADlrDAPETV 347

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   761 GRALANVDLHVVDGLGRRKTRGASGELWIGGAGVARGYAGDAGEAagrfVEEGwpgsgrLYRSGDLVRWRADGCLEFLGR 840
Cdd:PRK13383  348 GKPVAGCPVRILDRNNRPVGPRVTGRIFVGGELAGTRYTDGGGKA----VVDG------MTSTGDMGYLDNAGRLFIVGR 417

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 15597498   841 IDEQVKINGYRIELGEIRSALLEHPAVGEAAVLtdeaDAAEPGADRRIVAFVTA 894
Cdd:PRK13383  418 EDDMIISGGENVYPRAVENALAAHPAVADNAVI----GVPDERFGHRLAAFVVL 467
PRK06164 PRK06164
acyl-CoA synthetase; Validated
 448-904 2.29e-19

acyl-CoA synthetase; Validated


Pssm-ID: 235722 [Multi-domain]  Cd Length: 540  Bit Score: 94.42  E-value: 2.29e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   448 ESLVAAFDLRAALQPQAPALLDAHGSLDFATLRARSEAVAEALLAAGVRPGQAVAVMTGRNREAIVALLGVMRAAAVYTP 527
Cdd:PRK06164   10 DTLASLLDAHARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIA 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   528 VNPEFPAARVERMREAG------------GIVFA--LADAECAGRAR-EAFAGACLDLSTLP----------LAGSGMSL 582
Cdd:PRK06164   90 VNTRYRSHEVAHILGRGrarwlvvwpgfkGIDFAaiLAAVPPDALPPlRAIAVVDDAADATPapapgarvqlFALPDPAP 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   583 PAPGGRDA------AYMIFTSGTSGQPKGVVVEHASALNLSQALARtVYAnvVGEGLRVTVNAPFSFDSSIKQILQLLSG 656
Cdd:PRK06164  170 PAAAGERAadpdagALLFTTSGTTSGPKLVLHRQATLLRHARAIAR-AYG--YDPGAVLLAALPFCGVFGFSTLLGALAG 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   657 HCLVLVpqEVRSDPQRMLGFLEERRIDVLDCTPSLFRLLLQAGldDAHPALPGRILVGGERFDEASWEVAAgWRRCQ--- 733
Cdd:PRK06164  247 GAPLVC--EPVFDAARTARALRRHRVTHTFGNDEMLRRILDTA--GERADFPSARLFGFASFAPALGELAA-LARARgvp 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   734 VFNLYGPTE--ATVNASLARVAEHARPTIGRALAN--VDLHVVDGL-GRRKTRGASGELWIGGAGVARGYAGDAGEAAGR 808
Cdd:PRK06164  322 LTGLYGSSEvqALVALQPATDPVSVRIEGGGRPASpeARVRARDPQdGALLPDGESGEIEIRAPSLMRGYLDNPDATARA 401

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   809 FVEEGWpgsgrlYRSGDLVRWRADGCLEFLGRIDEQVKINGYRIELGEIRSALLEHPAVGEAAVLtdeadAAEPGADRRI 888
Cdd:PRK06164  402 LTDDGY------FRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVV-----GATRDGKTVP 470

                         490
                  ....*....|....*...
gi 15597498   889 VAFV--TAAEETADESWL 904
Cdd:PRK06164  471 VAFVipTDGASPDEAGLM 488
PRK06188 PRK06188
acyl-CoA synthetase; Validated
 462-872 5.30e-19

acyl-CoA synthetase; Validated


Pssm-ID: 235731 [Multi-domain]  Cd Length: 524  Bit Score: 93.13  E-value: 5.30e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   462 PQAPALLDAHGSLDFATLRARSEAVAEALLAAGVRPGQAVAVMTGRNREAIVALLGVMRAAAVYTPVNP-------EF-- 532
Cdd:PRK06188   26 PDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALHPlgslddhAYvl 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   533 -----------PAARVERMREAGGIVFALADAECAGRAREAfagacLDLSTLPLAGSGMSL-PAPGGRDAAYMIFTSGTS 600
Cdd:PRK06188  106 edagistlivdPAPFVERALALLARVPSLKHVLTLGPVPDG-----VDLLAAAAKFGPAPLvAAALPPDIAGLAYTGGTT 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   601 GQPKGVVVEHASALNLSQALARTVYanvVGEGLRVTVNAPFSFDSSIKQILQLLSGHCLVLVPqevRSDPQRMLGFLEER 680
Cdd:PRK06188  181 GKPKGVMGTHRSIATMAQIQLAEWE---WPADPRFLMCTPLSHAGGAFFLPTLLRGGTVIVLA---KFDPAEVLRAIEEQ 254

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   681 RIDVLDCTPS-LFRLLLQAGLDD------------AHPALPGRILVGGERFDeaswevaagwrrcQVF-NLYGPTEATVN 746
Cdd:PRK06188  255 RITATFLVPTmIYALLDHPDLRTrdlssletvyygASPMSPVRLAEAIERFG-------------PIFaQYYGQTEAPMV 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   747 ASLARVAEHARP------TIGRALANVDLHVVDGLGRRKTRGASGELWIGGAGVARGYAGDAGEAAGRFvEEGWpgsgrl 820
Cdd:PRK06188  322 ITYLRKRDHDPDdpkrltSCGRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAF-RDGW------ 394

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 15597498   821 YRSGDLVRWRADGCLEFLGRIDEQVKINGYRIELGEIRSALLEHPAVGEAAV 872
Cdd:PRK06188  395 LHTGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAV 446
FadD3 cd17638
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ...
 589-873 1.31e-18

acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.


Pssm-ID: 341293 [Multi-domain]  Cd Length: 330  Bit Score: 89.48  E-value: 1.31e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  589 DAAYMIFTSGTSGQPKGVVVEHASALNLSQALARTVYanvVGEGLRVTVNAPF--SFDSSIKQILQLLSGHclVLVPQEV 666
Cdd:cd17638    1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWADCAD---LTEDDRYLIINPFfhTFGYKAGIVACLLTGA--TVVPVAV 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  667 rSDPQRMLGFLEERRIDVLDCTPSLFRLLLqaglddAHPALPgrilvggeRFDEASWEVA---------AGWRRCQ---- 733
Cdd:cd17638   76 -FDVDAILEAIERERITVLPGPPTLFQSLL------DHPGRK--------KFDLSSLRAAvtgaatvpvELVRRMRselg 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  734 ---VFNLYGPTEATVnASLARV---AEHARPTIGRALANVDLHVVDglgrrktrgaSGELWIGGAGVARGYAGDAGEAAG 807
Cdd:cd17638  141 fetVLTAYGLTEAGV-ATMCRPgddAETVATTCGRACPGFEVRIAD----------DGEVLVRGYNVMQGYLDDPEATAE 209

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15597498  808 RFVEEGWpgsgrlYRSGDLVRWRADGCLEFLGRIDEQVKINGYRIELGEIRSALLEHPAVGEAAVL 873
Cdd:cd17638  210 AIDADGW------LHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVI 269
C_PKS-NRPS cd19532
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
 1362-1686 2.54e-18

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHxxxD motif, a few such as Monascus pilosus lovastatin nonaketide synthase MokA have a non-canonical HRxxxD motif in the C-domain and are unable to catalyze amide-bond formation. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380455 [Multi-domain]  Cd Length: 421  Bit Score: 89.82  E-value: 2.54e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1362 PMTSLQQGMLLQSEASGDPRLLHNVVLHEVHGRLDGELLARAWAILIGRHAILRTGF--DLHGGQvPLQWVHPATAVAAE 1439
Cdd:cd19532    3 PMSFGQSRFWFLQQYLEDPTTFNVTFSYRLTGPLDVARLERAVRAVGQRHEALRTCFftDPEDGE-PMQGVLASSPLRLE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1440 -VPVHDLCGLDGETRRLRLRAWieeeqatpfDWSRPPLVRLAALALDERRFALGVAEHHSVLDGWSLQSLVDELLAVYAD 1518
Cdd:cd19532   82 hVQISDEAEVEEEFERLKNHVY---------DLESGETMRIVLLSLSPTEHYLIFGYHHIAMDGVSFQIFLRDLERAYNG 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1519 llagvvaREAEAPAVGFRDYVALEREAEAN---AASALFWldylaGARYRPLPG------LAEEGPR------RMAAVRV 1583
Cdd:cd19532  153 -------QPLLPPPLQYLDFAARQRQDYESgalDEDLAYW-----KSEFSTLPEplpllpFAKVKSRppltryDTHTAER 220

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1584 DVPADSLSRLRALAERsglpLRS----LLLAAHGRALCRFSDADEVVTGFVSHGRPEEpGADRLLGLFLNTLPCRLSAS- 1658
Cdd:cd19532  221 RLDAALAARIKEASRK----LRVtpfhFYLAALQVLLARLLDVDDICIGIADANRTDE-DFMETIGFFLNLLPLRFRRDp 295

                        330       340       350
                 ....*....|....*....|....*....|..
gi 15597498 1659 ----VDLLDSARRAFdyeRASLEHRRHPLAAI 1686
Cdd:cd19532  296 sqtfADVLKETRDKA---YAALAHSRVPFDVL 324
LC_FACS_like cd17640
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ...
 494-939 5.36e-18

Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341295 [Multi-domain]  Cd Length: 468  Bit Score: 89.34  E-value: 5.36e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  494 GVRPGQAVAVMTGRNREAIVALLGVMRAAAVYTPVNPEfpaARVERMReaggivFALADAECAGRAREAfagacldlstl 573
Cdd:cd17640   26 GVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSD---SSVEELL------YILNHSESVALVVEN----------- 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  574 plagsgmslpapGGRDAAYMIFTSGTSGQPKGVVVEHASAL----NLSQ------------------ALARTVYANVVGE 631
Cdd:cd17640   86 ------------DSDDLATIIYTSGTTGNPKGVMLTHANLLhqirSLSDivppqpgdrflsilpiwhSYERSAEYFIFAC 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  632 GlrvtVNAPFSFDSSIKQILQLLSGHCLVLVP-----------QEVRSDP---QRMLGFLeerridvldctpsLFRLLLQ 697
Cdd:cd17640  154 G----CSQAYTSIRTLKDDLKRVKPHYIVSVPrlweslysgiqKQVSKSSpikQFLFLFF-------------LSGGIFK 216

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  698 AGLDDAHpALPGRIlvggERFDEAswevaAGWRrcqVFNLYGPTEATVNASLARVAEHARPTIGRALANVDLHVVDGLGR 777
Cdd:cd17640  217 FGISGGG-ALPPHV----DTFFEA-----IGIE---VLNGYGLTETSPVVSARRLKCNVRGSVGRPLPGTEIKIVDPEGN 283

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  778 RKTR-GASGELWIGGAGVARGYAGDAGEAAGRFVEEGWpgsgrlYRSGDLVRWRADGCLEFLGRI-DEQVKINGYRIELG 855
Cdd:cd17640  284 VVLPpGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDGW------FNTGDLGWLTCGGELVLTGRAkDTIVLSNGENVEPQ 357

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  856 EIRSALLEHPAVGEAAVLtdeadaaepGADRR-----IVAFVTAAEETADESwlEVDLPSGHRVAGLNLNETEYVYQEIf 930
Cdd:cd17640  358 PIEEALMRSPFIEQIMVV---------GQDQKrlgalIVPNFEELEKWAKES--GVKLANDRSQLLASKKVLKLYKNEI- 425


                 ....*....
gi 15597498  931 VDEVYSRDG 939
Cdd:cd17640  426 KDEISNRPG 434
Cyc_NRPS cd19535
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
 1395-1680 5.95e-18

Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Cyc (heterocyclization) domains catalyze two separate reactions in the creation of heterocyclized peptide products in nonribosomal peptide synthesis: amide bond formation followed by intramolecular cyclodehydration between a Cys, Ser, or Thr side chain and a carbonyl carbon on the peptide backbone to form a thiazoline, oxazoline, or methyloxazoline ring. Cyc-domains are homologous to standard NRPS Condensation (C) domains. C-domains typically have a conserved HHxxxD motif at the active site; Cyc-domains have an alternative, conserved DxxxxD active site motif, mutation of the aspartate residues in this motif can abolish or diminish condensation activity. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and Cyc-domains. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380458 [Multi-domain]  Cd Length: 423  Bit Score: 88.70  E-value: 5.95e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1395 LDGELLARAWAILIGRHAILRTGFdLHGGQvplQWVHPATAvAAEVPVHDLCGLDGETRRLRLRAWIEEEQATPFDWSRP 1474
Cdd:cd19535   37 LDPDRLERAWNKLIARHPMLRAVF-LDDGT---QQILPEVP-WYGITVHDLRGLSEEEAEAALEELRERLSHRVLDVERG 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1475 PLVRLAALALDERRFALgvaeHHS----VLDGWSLQSLVDELLAVYADllagvvaREAEAPAVG--FRDYVA--LEREAE 1546
Cdd:cd19535  112 PLFDIRLSLLPEGRTRL----HLSidllVADALSLQILLRELAALYED-------PGEPLPPLElsFRDYLLaeQALRET 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1547 ANAASALFWLDYLAgaryrPLPG-----LAEEgPRRMAAVRVD-----VPADSLSRLRALAERSGLPLRSLLLAAHGRAL 1616
Cdd:cd19535  181 AYERARAYWQERLP-----TLPPapqlpLAKD-PEEIKEPRFTrrehrLSAEQWQRLKERARQHGVTPSMVLLTAYAEVL 254

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15597498 1617 CRFSDADEV---VTGFvsHGRPEEPGADRLLGLF--LNTLPCRLSASVDLLDSARRAFDYERASLEHRR 1680
Cdd:cd19535  255 ARWSGQPRFllnLTLF--NRLPLHPDVNDVVGDFtsLLLLEVDGSEGQSFLERARRLQQQLWEDLDHSS 321
PRK12583 PRK12583
acyl-CoA synthetase; Provisional
 438-873 6.86e-18

acyl-CoA synthetase; Provisional


Pssm-ID: 237145 [Multi-domain]  Cd Length: 558  Bit Score: 89.83  E-value: 6.86e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   438 QGERVEPAPVESLVAAFDLRAALQPQAPALLDAHGSLDF--ATLRARSEAVAEALLAAGVRPGQAVAVMTGRNREAIVAL 515
Cdd:PRK12583    8 QGGGDKPLLTQTIGDAFDATVARFPDREALVVRHQALRYtwRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQ 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   516 LGVMRAAAVYTPVNPEFPAARVE---RMREAGGIVFA------------------LADAECAGRAREAF----------- 563
Cdd:PRK12583   88 FATARIGAILVNINPAYRASELEyalGQSGVRWVICAdafktsdyhamlqellpgLAEGQPGALACERLpelrgvvslap 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   564 --AGACLDLSTLPLAGSGMSLPAPGGRDAAY-------MIFTSGTSGQPKGVVVEHASALNLSQALARTVYanvVGEGLR 634
Cdd:PRK12583  168 apPPGFLAWHELQARGETVSREALAERQASLdrddpinIQYTSGTTGFPKGATLSHHNILNNGYFVAESLG---LTEHDR 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   635 VTVNAPF--SFDSSIKQILQLLSGHCLVLvPQEVrSDPQRMLGFLEERRIDVLDCTPSLFrlllQAGLDdaHP------- 705
Cdd:PRK12583  245 LCVPVPLyhCFGMVLANLGCMTVGACLVY-PNEA-FDPLATLQAVEEERCTALYGVPTMF----IAELD--HPqrgnfdl 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   706 -ALPGRILVGGERFDEASWEVAAGWRRCQVFNLYGPTEA-------TVNASLARVAEharpTIGRALANVDLHVVDGLGR 777
Cdd:PRK12583  317 sSLRTGIMAGAPCPIEVMRRVMDEMHMAEVQIAYGMTETspvslqtTAADDLERRVE----TVGRTQPHLEVKVVDPDGA 392

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   778 RKTRGASGELWIGGAGVARGYAGDAGEAAGRFVEEGWpgsgrlYRSGDLVRWRADGCLEFLGRIDEQVKINGYRIELGEI 857
Cdd:PRK12583  393 TVPRGEIGELCTRGYSVMKGYWNNPEATAESIDEDGW------MHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREI 466

                         490
                  ....*....|....*.
gi 15597498   858 RSALLEHPAVGEAAVL 873
Cdd:PRK12583  467 EEFLFTHPAVADVQVF 482
E_NRPS cd19534
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
 1384-1773 1.05e-17

Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Epimerization (E) domains of nonribosomal peptide synthetases (NRPS) flip the chirality of the end amino acid of a peptide being manufactured by the NRPS. E-domains are homologous to the Condensation (C) domains. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Specialized tailoring NRPS domains such as E-domains greatly increase the range of possible peptide products created by the NRPS machinery. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the E-domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380457 [Multi-domain]  Cd Length: 428  Bit Score: 88.08  E-value: 1.05e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1384 HNVVLHeVHGRLDGELLARAWAILIGRHAILRTGFDLHGGQVpLQWVHPATAVAAEVPVHDLcglDGETRRLRLRAWIEE 1463
Cdd:cd19534   24 QSVLLR-VPQGLDPDALRQALRALVEHHDALRMRFRREDGGW-QQRIRGDVEELFRLEVVDL---SSLAQAAAIEALAAE 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1464 EQATpFDWSRPPLVRLAALALDERRFALGVAEHHSVLDGWSLQSLVDELLAVYADLLAGvvaREAEAPAVG-FRDYVALE 1542
Cdd:cd19534   99 AQSS-LDLEEGPLLAAALFDGTDGGDRLLLVIHHLVVDGVSWRILLEDLEAAYEQALAG---EPIPLPSKTsFQTWAELL 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1543 REA---EANAASALFWLDyLAGARYRPLPG--LAEEGPRRMAAVRVDVpadslSRLRALAERSGLPLRS----LLLAAHG 1613
Cdd:cd19534  175 AEYaqsPALLEELAYWRE-LPAADYWGLPKdpEQTYGDARTVSFTLDE-----EETEALLQEANAAYRTeindLLLAALA 248

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1614 RALCRFSDADEVVTGFVSHGR-PEEPGAD--RLLGLFLNTLPCRL--SASVDLLDS------ARRA-----FDY------ 1671
Cdd:cd19534  249 LAFQDWTGRAPPAIFLEGHGReEIDPGLDlsRTVGWFTSMYPVVLdlEASEDLGDTlkrvkeQLRRipnkgIGYgilryl 328

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1672 -ERASLEHRRHPLAAIrrrnrelrldsLFNFV-DFHQDDAAPAGVRHGGILDQVVVDVDVPLAVDFE----VAGERLEVG 1745
Cdd:cd19534  329 tPEGTKRLAFHPQPEI-----------SFNYLgQFDQGERDDALFVSAVGGGGSDIGPDTPRFALLDinavVEGGQLVIT 397

                        410       420
                 ....*....|....*....|....*...
gi 15597498 1746 FQYAAGRFPAERAEALAGAYREALLALL 1773
Cdd:cd19534  398 VSYSRNMYHEETIQQLADSYKEALEALI 425
OSB_CoA_lg cd05912
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ...
 473-901 1.59e-17

O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.


Pssm-ID: 341238 [Multi-domain]  Cd Length: 411  Bit Score: 87.40  E-value: 1.59e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  473 SLDFATLRARSEAVAEALLAAGVRPGQAVAVMTGRNREAIVALLGVMRAAAVYTPVNPEFPAARvermreaggIVFALAD 552
Cdd:cd05912    1 SYTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNE---------LAFQLKD 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  553 AECAgrareafagacLDlstlplagsgmslpapggrDAAYMIFTSGTSGQPKGVvvehasalnlsQALARTVYANVVGEG 632
Cdd:cd05912   72 SDVK-----------LD-------------------DIATIMYTSGTTGKPKGV-----------QQTFGNHWWSAIGSA 110

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  633 LRVTVNA--------PFSFDSSIKQIL-QLLSGHCLVLVPqevRSDPQRMLGFLEERRIDVLDCTPSLFRLLLQAGLDDA 703
Cdd:cd05912  111 LNLGLTEddnwlcalPLFHISGLSILMrSVIYGMTVYLVD---KFDAEQVLHLINSGKVTIISVVPTMLQRLLEILGEGY 187

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  704 HPALPGrILVGGERFDEASWEVAAGwRRCQVFNLYGPTE-----ATVNASLArvaeHARP-TIGRALANVDLHVVDGLGR 777
Cdd:cd05912  188 PNNLRC-ILLGGGPAPKPLLEQCKE-KGIPVYQSYGMTEtcsqiVTLSPEDA----LNKIgSAGKPLFPVELKIEDDGQP 261

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  778 RKTrgaSGELWIGGAGVARGYAGDAgEAAGRFVEEGWpgsgrlYRSGDLVRWRADGCLEFLGRIDEQVKINGYRIELGEI 857
Cdd:cd05912  262 PYE---VGEILLKGPNVTKGYLNRP-DATEESFENGW------FKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEI 331

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*.
gi 15597498  858 RSALLEHPAVGEAAV--LTDEADAAEPgadrriVAFVTAAEETADE 901
Cdd:cd05912  332 EEVLLSHPAIKEAGVvgIPDDKWGQVP------VAFVVSERPISEE 371
PRK05605 PRK05605
long-chain-fatty-acid--CoA ligase; Validated
 434-899 2.42e-17

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235531 [Multi-domain]  Cd Length: 573  Bit Score: 88.13  E-value: 2.42e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   434 YQAWQGERVEPaPVESLVAAFDLRAALQPQAPAL-----------LDAHGSLDFATLRArseavaeallaAGVRPGQAVA 502
Cdd:PRK05605   19 YAPWTPHDLDY-GDTTLVDLYDNAVARFGDRPALdffgatttyaeLGKQVRRAAAGLRA-----------LGVRPGDRVA 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   503 VMTGRNREAIVALLGVMRAAAV-------YTPVNPEFP---------------AARVERMREAGG---IV---------- 547
Cdd:PRK05605   87 IVLPNCPQHIVAFYAVLRLGAVvvehnplYTAHELEHPfedhgarvaivwdkvAPTVERLRRTTPletIVsvnmiaampl 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   548 ---FAL---------ADAECAGRAREAFAGACLDLSTLPLAGSGMSLPAPGGRDAAYMIFTSGTSGQPKGVVVEHASAL- 614
Cdd:PRK05605  167 lqrLALrlpipalrkARAALTGPAPGTVPWETLVDAAIGGDGSDVSHPRPTPDDVALILYTSGTTGKPKGAQLTHRNLFa 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   615 NLSQALA---------RTVYA-----NVVGeglrVTVNAPFSfdssikqilqLLSGHCLVLVPqevRSDPQRMLGFLEER 680
Cdd:PRK05605  247 NAAQGKAwvpglgdgpERVLAalpmfHAYG----LTLCLTLA----------VSIGGELVLLP---APDIDLILDAMKKH 309

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   681 RIDVLDCTPSLFRLLLQA----GLD--------DAHPALPGRILvggerfdeASWEVAAGWRrcqVFNLYGPTEATVNAS 748
Cdd:PRK05605  310 PPTWLPGVPPLYEKIAEAaeerGVDlsgvrnafSGAMALPVSTV--------ELWEKLTGGL---LVEGYGLTETSPIIV 378

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   749 LARVAEHARP-TIGRALANVDLHVVD--GLGRRKTRGASGELWIGGAGVARGYAGDAgEAAGRFVEEGWpgsgrlYRSGD 825
Cdd:PRK05605  379 GNPMSDDRRPgYVGVPFPDTEVRIVDpeDPDETMPDGEEGELLVRGPQVFKGYWNRP-EETAKSFLDGW------FRTGD 451

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15597498   826 LVRWRADGCLEFLGRIDEQVKINGYRIELGEIRSALLEHPAVGEAAVL-TDEADAAEpgadrRIVAFVTAAEETA 899
Cdd:PRK05605  452 VVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVgLPREDGSE-----EVVAAVVLEPGAA 521
PRK07787 PRK07787
acyl-CoA synthetase; Validated
 495-901 2.90e-17

acyl-CoA synthetase; Validated


Pssm-ID: 236096 [Multi-domain]  Cd Length: 471  Bit Score: 87.35  E-value: 2.90e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   495 VRPGQAVAVMTGRNREAIVALLGVMRAAAVYTPVNPEFPAARVERMREAGGIVFALADA--ECAGRAREAfagacLDLSt 572
Cdd:PRK07787   42 VAGARRVAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAERRHILADSGAQAWLGPApdDPAGLPHVP-----VRLH- 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   573 lplAGSGMSLPAPGGRDAAYMIFTSGTSGQPKGVVV-EHASALN---LSQALARTVyANVVGEGLrvtvnapfsfdssik 648
Cdd:PRK07787  116 ---ARSWHRYPEPDPDAPALIVYTSGTTGPPKGVVLsRRAIAADldaLAEAWQWTA-DDVLVHGL--------------- 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   649 qilQLLSGHCLVL-----------VPQEVRSDPQRMLGFLEeRRIDVLDCTPSLFRLLlqAGLDDAHPAL-PGRILVGGE 716
Cdd:PRK07787  177 ---PLFHVHGLVLgvlgplrignrFVHTGRPTPEAYAQALS-EGGTLYFGVPTVWSRI--AADPEAARALrGARLLVSGS 250

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   717 rfdeASWEVAAGWRRC-----QVFNLYGPTEATVNASlARVAEHARP-TIGRALANVDLHVVDGLGRRKTRGAS--GELW 788
Cdd:PRK07787  251 ----AALPVPVFDRLAaltghRPVERYGMTETLITLS-TRADGERRPgWVGLPLAGVETRLVDEDGGPVPHDGEtvGELQ 325

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   789 IGGAGVARGYAGDAGEAAGRFVEEGWpgsgrlYRSGDLVRWRADGCLEFLGRID-EQVKINGYRIELGEIRSALLEHPAV 867
Cdd:PRK07787  326 VRGPTLFDGYLNRPDATAAAFTADGW------FRTGDVAVVDPDGMHRIVGREStDLIKSGGYRIGAGEIETALLGHPGV 399

                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 15597498   868 GEAAVLtdeadaAEPGAD--RRIVAFVTAAEETADE 901
Cdd:PRK07787  400 REAAVV------GVPDDDlgQRIVAYVVGADDVAAD 429
PRK07514 PRK07514
malonyl-CoA synthase; Validated
 456-872 3.04e-17

malonyl-CoA synthase; Validated


Pssm-ID: 181011 [Multi-domain]  Cd Length: 504  Bit Score: 87.24  E-value: 3.04e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   456 LRAALQ-PQAPALLDAHGS-LDFATLRARSEAVAEALLAAGVRPGQAVAVMTGRNREAIVALLGVMRAAAVYTPVNPEFP 533
Cdd:PRK07514    9 LRAAFAdRDAPFIETPDGLrYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYT 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   534 AARVER-MREAGGIVFALADAECAGRAREAFAGACLDLSTLPLAGSGmSL------------PAP-GGRDAAYMIFTSGT 599
Cdd:PRK07514   89 LAELDYfIGDAEPALVVCDPANFAWLSKIAAAAGAPHVETLDADGTG-SLleaaaaapddfeTVPrGADDLAAILYTSGT 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   600 SGQPKGVVVEHAsalNL-SQALARTVYANVVGE-------------GLRVTVNapfsfdssikqiLQLLSGHCLVLVPqe 665
Cdd:PRK07514  168 TGRSKGAMLSHG---NLlSNALTLVDYWRFTPDdvlihalpifhthGLFVATN------------VALLAGASMIFLP-- 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   666 vRSDPQRMLGFLeeRRIDVLDCTPSLF-RLLLQAGLDDAHPAlPGRILVGG------ERFDEasWEVAAGWRrcqVFNLY 738
Cdd:PRK07514  231 -KFDPDAVLALM--PRATVMMGVPTFYtRLLQEPRLTREAAA-HMRLFISGsapllaETHRE--FQERTGHA---ILERY 301

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   739 GPTEATVNASLARVAEHARPTIGRALANVDLHVVD-GLGRRKTRGASGELWIGGAGVARGYAGDAGEAAGRFVEEGWpgs 817
Cdd:PRK07514  302 GMTETNMNTSNPYDGERRAGTVGFPLPGVSLRVTDpETGAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADGF--- 378

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 15597498   818 grlYRSGDLVRWRADGCLEFLGRIDEQVKINGYRIELGEIRSALLEHPAVGEAAV 872
Cdd:PRK07514  379 ---FITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAV 430
AAS_C cd05909
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ...
 589-901 9.97e-17

C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.


Pssm-ID: 341235 [Multi-domain]  Cd Length: 490  Bit Score: 85.85  E-value: 9.97e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  589 DAAYMIFTSGTSGQPKGVVVEHASALNLSQALARTVYAN---VVGEGLrvtvnaPF--SFDSSIKQILQLLSGHCLVLVP 663
Cdd:cd05909  148 DPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNpedVVFGAL------PFfhSFGLTGCLWLPLLSGIKVVFHP 221

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  664 QEVrsDPQRMLGFLEERRIDVLDCTPSLFRLLLQAglddAHPA-LPG-R-ILVGGERFDEASWEVAAGWRRCQVFNLYGP 740
Cdd:cd05909  222 NPL--DYKKIPELIYDKKATILLGTPTFLRGYARA----AHPEdFSSlRlVVAGAEKLKDTLRQEFQEKFGIRILEGYGT 295

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  741 TEATVNASLARVAEHARP-TIGRALANVDLHVVDGLGRRKTR-GASGELWIGGAGVARGYAGDAgEAAGRFVEEGWpgsg 818
Cdd:cd05909  296 TECSPVISVNTPQSPNKEgTVGRPLPGMEVKIVSVETHEEVPiGEGGLLLVRGPNVMLGYLNEP-ELTSFAFGDGW---- 370

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  819 rlYRSGDLVRWRADGCLEFLGRIDEQVKINGYRIELGEIRSALLEH--PAVGEAAVLTDEADAAEpgadrRIVAFVTAAE 896
Cdd:cd05909  371 --YDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEIlpEDNEVAVVSVPDGRKGE-----KIVLLTTTTD 443


                 ....*
gi 15597498  897 ETADE 901
Cdd:cd05909  444 TDPSS 448
MACS_euk cd05928
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ...
 494-874 1.79e-16

Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.


Pssm-ID: 341251 [Multi-domain]  Cd Length: 530  Bit Score: 85.21  E-value: 1.79e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  494 GVRPGQAVAVMTGRNREAIVALLGVMRAAAVYTPVNPEFPAARVE---RMREAGGIVfalADAECAGRArEAFAGACLDL 570
Cdd:cd05928   63 GLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILyrlQASKAKCIV---TSDELAPEV-DSVASECPSL 138

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  571 ST------------------LPLAGSGMSLPAPGGRDAAYMIFTSGTSGQPKgvVVEHasalnlSQALArtvyanvvgeG 632
Cdd:cd05928  139 KTkllvseksrdgwlnfkelLNEASTEHHCVETGSQEPMAIYFTSGTTGSPK--MAEH------SHSSL----------G 200

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  633 LRVTVNAPFSFDSSIKQILQLLS------------------GHClVLVPQEVRSDPQRMLGFLEERRIDVLDCTPSLFRL 694
Cdd:cd05928  201 LGLKVNGRYWLDLTASDIMWNTSdtgwiksawsslfepwiqGAC-VFVHHLPRFDPLVILKTLSSYPITTFCGAPTVYRM 279

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  695 LLQAGLDDAH-PALPgRILVGGERFDEaswEVAAGWRR---CQVFNLYGPTEATVNASLARVAEHARPTIGRALANVDLH 770
Cdd:cd05928  280 LVQQDLSSYKfPSLQ-HCVTGGEPLNP---EVLEKWKAqtgLDIYEGYGQTETGLICANFKGMKIKPGSMGKASPPYDVQ 355

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  771 VVDGLGRRKTRGASGELWI-----GGAGVARGYAGDAGEAAGRFveegwpgSGRLYRSGDLVRWRADGCLEFLGRIDEQV 845
Cdd:cd05928  356 IIDDNGNVLPPGTEGDIGIrvkpiRPFGLFSGYVDNPEKTAATI-------RGDFYLTGDRGIMDEDGYFWFMGRADDVI 428

                        410       420
                 ....*....|....*....|....*....
gi 15597498  846 KINGYRIELGEIRSALLEHPAVGEAAVLT 874
Cdd:cd05928  429 NSSGYRIGPFEVESALIEHPAVVESAVVS 457
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
 1192-1616 1.80e-16

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: 86.45  E-value: 1.80e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1192 GGELSEQALRGFLEARLPAYMLPSRIARVERLPLTAEGKLDRRALLAALAAEAAAQTLEAPANATEAALLEIWKSVLKRp 1271
Cdd:COG1020  924 GAAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLALPAPAAAAAAAAAAPPAEEEEEEAALALLLLLVVV- 1002

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1272 aIGVSDNFFQVGGDSIRLIQMQVMAREAGLAFTLRDVFNHQSIRELARLLAAPASPADALGTSAPQSLEPFALLSAAERK 1351
Cdd:COG1020 1003 -VGDDDFFFFGGGLGLLLLLALARAARLLLLLLLLLLLFLAAAAAAAAAAAAAAAAAAAAPLAAAAAPLPLPPLLLSLLA 1081

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1352 RLPEGLDDAYPMTSLQQGMLLQSEASGDPRLLHNVVLHEVHgrldgellarawailigRHAILRTGFDLHGGQVPLQWVH 1431
Cdd:COG1020 1082 LLLALLLLLALLALLALLLLLLLLLLLLALLLLLALLLALL-----------------AALRARRAVRQEGPRLRLLVAL 1144

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1432 PATAVAAEVPVHDLCGLDGETRRLRLRAWIEEEQATPFDWSRPPLVRLAALALDERRFALGVAEHHSVLDGWSLQSLVDE 1511
Cdd:COG1020 1145 AAALALAALLALLLAAAAAAAELLAAAALLLLLALLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLL 1224

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1512 LLAVYADLLAGVVAREAEAPAVGFRDYVALEREAEANAASALFWLDYLAGARYRPLPGLAEEGPRRMAAVRVDVPADSLS 1591
Cdd:COG1020 1225 AAAAAALLALALLLALLALAALLALAALAALAAALLALALALLALALLLLALALLLPALARARAARTARALALLLLLALL 1304

                        410       420
                 ....*....|....*....|....*
gi 15597498 1592 RLRALAERSGLPLRSLLLAAHGRAL 1616
Cdd:COG1020 1305 LLLALALALLLLLLLLLALLLLALL 1329
PRK06155 PRK06155
crotonobetaine/carnitine-CoA ligase; Provisional
 442-881 2.00e-16

crotonobetaine/carnitine-CoA ligase; Provisional


Pssm-ID: 235719 [Multi-domain]  Cd Length: 542  Bit Score: 85.20  E-value: 2.00e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   442 VEPAPV--ESLVAAFDLRAALQPQAPALLDAHGSLDFATLRARSEAVAEALLAAGVRPGQAVAVMTGRNREAIVALLGVM 519
Cdd:PRK06155   13 VDPLPPseRTLPAMLARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCA 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   520 RAAAVYTPVNPEFPAARVERMREAGGIVFALADAECAGRAREAFAGAC-----------------LDLSTLPLAGSGMSL 582
Cdd:PRK06155   93 WLGAIAVPINTALRGPQLEHILRNSGARLLVVEAALLAALEAADPGDLplpavwlldapasvsvpAGWSTAPLPPLDAPA 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   583 PA--PGGRDAAYMIFTSGTSGQPKGVVVEHASALNLSQALARTVYanvVGEGLRVTVNAPFSFDSSIKQILQ-LLSGHCL 659
Cdd:PRK06155  173 PAaaVQPGDTAAILYTSGTTGPSKGVCCPHAQFYWWGRNSAEDLE---IGADDVLYTTLPLFHTNALNAFFQaLLAGATY 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   660 VLVPQ--------EVRSDpQRMLGFLEERRIDVLDCTPSLFRlllqaglDDAH-------PALPGRILVG-GERFDeasw 723
Cdd:PRK06155  250 VLEPRfsasgfwpAVRRH-GATVTYLLGAMVSILLSQPARES-------DRAHrvrvalgPGVPAALHAAfRERFG---- 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   724 evaagwrrCQVFNLYGPTEAtvNASLARVAEHARP-TIGRALANVDLHVVDGLGRRKTRGASGELWIGGA---GVARGYA 799
Cdd:PRK06155  318 --------VDLLDGYGSTET--NFVIAVTHGSQRPgSMGRLAPGFEARVVDEHDQELPDGEPGELLLRADepfAFATGYF 387

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   800 GDAGEAAgrfveEGWpgSGRLYRSGDLVRWRADGCLEFLGRIDEQVKINGYRIELGEIRSALLEHPAVGEAAVLTDEADA 879
Cdd:PRK06155  388 GMPEKTV-----EAW--RNLWFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSEL 460


                  ..
gi 15597498   880 AE 881
Cdd:PRK06155  461 GE 462
X-Domain_NRPS cd19546
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ...
 1358-1682 2.20e-16

X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to the non-ribosomal peptide synthetase (NRPS); The X-domain is a catalytically inactive member of the Condensation (C) domain family of non-ribosomal peptide synthetase (NRPS). It has been shown to recruit oxygenases to the NRPS to perform side-chain crosslinking in the production of glycopeptide antibiotics. C-domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as this X-domain, the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, and dual E/C (epimerization and condensation) domains. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity; members of this X-domain subfamily lack the second H of this motif.


Pssm-ID: 380468 [Multi-domain]  Cd Length: 440  Bit Score: 84.07  E-value: 2.20e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1358 DDAYPMTSLQQGMLLQSEASGDPRLLHNVVLHEVHGRLDGELLARAWAILIGRHAILRTGFDLHGGQVpLQWVHPATAVA 1437
Cdd:cd19546    2 PDEVPATAGQLRTWLLARLDEETRGRHLSVALRLRGRLDRDALEAALGDVAARHEILRTTFPGDGGDV-HQRILDADAAR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1438 AEVPVhdlcgldGETRRLRLRAWIEEEQATPFDWSRPPLVRLAALALDERRFALGVAEHHSVLDGWSLQSLVDELLAVYA 1517
Cdd:cd19546   81 PELPV-------VPATEEELPALLADRAAHLFDLTRETPWRCTLFALSDTEHVLLLVVHRIAADDESLDVLVRDLAAAYG 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1518 DLLAGVVAREAEAPaVGFRDYVALERE--AEANAASAL------FWLDYLAGARY-------RPLPGLAEegpRRMAAVR 1582
Cdd:cd19546  154 ARREGRAPERAPLP-LQFADYALWEREllAGEDDRDSLigdqiaYWRDALAGAPDelelptdRPRPVLPS---RRAGAVP 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1583 VDVPADSLSRLRALAERSGLPLRSLLLAAHGRALCRFSDADEVVTGFVSHGRPEEPGADRLLGLFLNTLPCRLSASVD-- 1660
Cdd:cd19546  230 LRLDAEVHARLMEAAESAGATMFTVVQAALAMLLTRLGAGTDVTVGTVLPRDDEEGDLEGMVGPFARPLALRTDLSGDpt 309

                        330       340
                 ....*....|....*....|....*
gi 15597498 1661 ---LLDSARRAFdyerasLEHRRHP 1682
Cdd:cd19546  310 freLLGRVREAV------REARRHQ 328
AACS_like cd05968
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ...
 473-871 2.77e-16

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: 84.85  E-value: 2.77e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  473 SLDFATLRARSEAVAEALLAAGVRPGQAVAVMTGRNREAIVALLGVMRAAAVYTPVNPEF-PAARVERMREAGGIVFALA 551
Cdd:cd05968   91 TLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFgKEAAATRLQDAEAKALITA 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  552 DA--------ECAGRAREAFAGACLDLSTLPLAGSGMSLPAPGGRDAAY---------------------MIFTSGTSGQ 602
Cdd:cd05968  171 DGftrrgrevNLKEEADKACAQCPTVEKVVVVRHLGNDFTPAKGRDLSYdeeketagdgaertesedplmIIYTSGTTGK 250

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  603 PKGVVVEHAS-ALNLSQALArtvYANVVGEGLRVT-------VNAPFSFDSSikqilqLLSGHCLVL---VPQEvrSDPQ 671
Cdd:cd05968  251 PKGTVHVHAGfPLKAAQDMY---FQFDLKPGDLLTwftdlgwMMGPWLIFGG------LILGATMVLydgAPDH--PKAD 319

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  672 RMLGFLEERRIDVLDCTPSLFRLLLQAGLD--DAHPALPGRILVG-GERFDEASWE---VAAGWRRCQVFNLYGPTEATV 745
Cdd:cd05968  320 RLWRMVEDHEITHLGLSPTLIRALKPRGDApvNAHDLSSLRVLGStGEPWNPEPWNwlfETVGKGRNPIINYSGGTEISG 399

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  746 NASLARVAEHARP-TIGRALANVDLHVVDGLGRRkTRGASGEL-----WIGgagVARGYAGDAGeaagRFVEEGWPGSGR 819
Cdd:cd05968  400 GILGNVLIKPIKPsSFNGPVPGMKADVLDESGKP-ARPEVGELvllapWPG---MTRGFWRDED----RYLETYWSRFDN 471

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|..
gi 15597498  820 LYRSGDLVRWRADGCLEFLGRIDEQVKINGYRIELGEIRSALLEHPAVGEAA 871
Cdd:cd05968  472 VWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESA 523
PRK06839 PRK06839
o-succinylbenzoate--CoA ligase;
457-873 2.86e-16

o-succinylbenzoate--CoA ligase;


Pssm-ID: 168698 [Multi-domain]  Cd Length: 496  Bit Score: 84.14  E-value: 2.86e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   457 RAALQPQAPALLDAHGSLDFATLRAR-SEAVAEALLAAGVRPGQAVAVMTGRNREAIVALLGVMRAAAVYTPVNPEFPAA 535
Cdd:PRK06839   11 RAYLHPDRIAIITEEEEMTYKQLHEYvSKVAAYLIYELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTEN 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   536 RVERMREAGGIVFALADAECAGRAREAFAGACLD--LSTLPLAGSGMSLPA---PGGRDAAYMI-FTSGTSGQPKGVVVE 609
Cdd:PRK06839   91 ELIFQLKDSGTTVLFVEKTFQNMALSMQKVSYVQrvISITSLKEIEDRKIDnfvEKNESASFIIcYTSGTTGKPKGAVLT 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   610 HASAlnLSQALARTVYANVVGEGLRVTVNAPFSFDSSIKQILQLLSGHCLVLVPQevRSDPQRMLGFLEERRIDVLDCTP 689
Cdd:PRK06839  171 QENM--FWNALNNTFAIDLTMHDRSIVLLPLFHIGGIGLFAFPTLFAGGVIIVPR--KFEPTKALSMIEKHKVTVVMGVP 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   690 SLFRLLLQAgLDDAHPALPG-RILVGG---------ERFDEASWEVAAGwrrcqvfnlYGPTEA--TVNASLARVAEHAR 757
Cdd:PRK06839  247 TIHQALINC-SKFETTNLQSvRWFYNGgapcpeelmREFIDRGFLFGQG---------FGMTETspTVFMLSEEDARRKV 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   758 PTIGRALANVDLHVVDGLGRRKTRGASGELWIGGAGVARGYAGDAgEAAGRFVEEGWpgsgrlYRSGDLVRWRADGCLEF 837
Cdd:PRK06839  317 GSIGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRP-DATEETIQDGW------LCTGDLARVDEDGFVYI 389

                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 15597498   838 LGRIDEQVKINGYRIELGEIRSALLEHPAVGEAAVL 873
Cdd:PRK06839  390 VGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVV 425
Methyltransf_21 pfam05050
Methyltransferase FkbM domain; This family has members from bacteria to human, and appears to ...
 950-1147 5.48e-16

Methyltransferase FkbM domain; This family has members from bacteria to human, and appears to be a methyltransferase.


Pssm-ID: 428282  Cd Length: 170  Bit Score: 77.61  E-value: 5.48e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498    950 DVGANIGLFSLYIAS----RAPRARVVAFEPLAPIRRRLEANLGRYApqvevfgigLSDAEREETFtyYPGYSTFSGIAE 1025
Cdd:pfam05050    1 DVGANDGVWDSVALLfekkCGGGGEVLAIEPNPNKLEKLDCTLLNLA---------LGNDVGLYEF--YLGGKGGGGYLL 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   1026 YADasgerdvirryLSNQGEEGGANLLLDNIDEIlddrlraeahRCRLRRLDQVIGELGLERIDLLKIDVQRAEMDVLLG 1105
Cdd:pfam05050   70 FAV-----------GDPQGASTSSVLGGEEAKYI----------EVETVTLDSFLEEIKKSDIDLLKIDVEGAELEVLEG 128

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 15597498   1106 lDDAALAKVR--QIVLEVHdKRDGATAGRADALSDLLRRHGFEV 1147
Cdd:pfam05050  129 -AEKTLKRCQpnIIVIEVH-FFHYFGGPLFDEIRQFLRECGYRL 170
PRK09029 PRK09029
O-succinylbenzoic acid--CoA ligase; Provisional
 458-904 7.94e-16

O-succinylbenzoic acid--CoA ligase; Provisional


Pssm-ID: 236363 [Multi-domain]  Cd Length: 458  Bit Score: 82.61  E-value: 7.94e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   458 AALQPQAPALLDAHGSLDFATLRARSEAVAEALLAAGVRPGQAVAVMtGRNR-EAIVALLGVMRAAAVYTPVNPEFPAAR 536
Cdd:PRK09029   13 AQVRPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALR-GKNSpETLLAYLALLQCGARVLPLNPQLPQPL 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   537 VERMREAGGIVFALADAECagrareaFAGACLDLSTLPLAGSGMSLPAPGGRDAAyMIFTSGTSGQPKGVVVEHASALnl 616
Cdd:PRK09029   92 LEELLPSLTLDFALVLEGE-------NTFSALTSLHLQLVEGAHAVAWQPQRLAT-MTLTSGSTGLPKAAVHTAQAHL-- 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   617 sqalartvyANVVGeglrvtVNAPFSFDSSIKQILQ---------------LLSGHCLVLvpqevrsdpqRMLGFLEErr 681
Cdd:PRK09029  162 ---------ASAEG------VLSLMPFTAQDSWLLSlplfhvsgqgivwrwLYAGATLVV----------RDKQPLEQ-- 214

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   682 iDVLDCT-----PS-LFRLLLQagldDAHPALPGRILVGGERFDEASWEVAAGWR-RCqvFNLYGPTEA--TVNASLArv 752
Cdd:PRK09029  215 -ALAGCThaslvPTqLWRLLDN----RSEPLSLKAVLLGGAAIPVELTEQAEQQGiRC--WCGYGLTEMasTVCAKRA-- 285

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   753 aeHARPTIGRALANVDLHVVDglgrrktrgasGELWIGGAGVARGYAGDageaaGRFV----EEGWpgsgrlYRSGDLVR 828
Cdd:PRK09029  286 --DGLAGVGSPLPGREVKLVD-----------GEIWLRGASLALGYWRQ-----GQLVplvnDEGW------FATRDRGE 341

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15597498   829 WRaDGCLEFLGRIDEQVKINGYRIELGEIRSALLEHPAVGEAAVLtdEADAAEPGAdrRIVAFVTAAEETADES---WL 904
Cdd:PRK09029  342 WQ-NGELTILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFVV--PVADAEFGQ--RPVAVVESDSEAAVVNlaeWL 415
PRK12316 PRK12316
peptide synthase; Provisional
 1198-1329 1.07e-15

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 84.24  E-value: 1.07e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1198 QALRGFLEARLPAYMLPSRIARVERLPLTAEGKLDRRALLAALAAEAAAQTLEaPANATEAALLEIWKSVLKRPAIGVSD 1277
Cdd:PRK12316 5016 DELKAALRERLPEYMVPAHLVFLARMPLTPNGKLDRKALPQPDASLLQQAYVA-PRSELEQQVAAIWAEVLQLERVGLDD 5094

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 15597498  1278 NFFQVGGDSirLIQMQVMAR---EAGLAFTLRDVFNHQSIRELARLLAAPASPAD 1329
Cdd:PRK12316 5095 NFFELGGHS--LLAIQVTSRiqlELGLELPLRELFQTPTLAAFVELAAAAGSGDD 5147
PRK04319 PRK04319
acetyl-CoA synthetase; Provisional
 468-872 1.18e-15

acetyl-CoA synthetase; Provisional


Pssm-ID: 235279 [Multi-domain]  Cd Length: 570  Bit Score: 82.64  E-value: 1.18e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   468 LDAHGSLD--FATLRARSEAVAEALLAAGVRPGQAVAVMTGRNREAIVALLGVMRAAAVYTPVNPEF-PAARVERMREAG 544
Cdd:PRK04319   66 LDASRKEKytYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFmEEAVRDRLEDSE 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   545 GIVF----ALADAECAGR-----------AREAFAGACLDLSTLpLAGSGMSLPAPGGR--DAAYMIFTSGTSGQPKGVV 607
Cdd:PRK04319  146 AKVLittpALLERKPADDlpslkhvllvgEDVEEGPGTLDFNAL-MEQASDEFDIEWTDreDGAILHYTSGSTGKPKGVL 224

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   608 VEHASALnlsQALARTVYANVVGEGLR---------VT-----VNAPfsfdssikqilqLLSGHCLVLVpqEVRSDPQRM 673
Cdd:PRK04319  225 HVHNAML---QHYQTGKYVLDLHEDDVywctadpgwVTgtsygIFAP------------WLNGATNVID--GGRFSPERW 287

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   674 LGFLEERRIDVLDCTPSLFRLLLQAGLDDA----HPALpgR-ILVGGERFD-EASWevaagWRRcQVFNL-----YGPTE 742
Cdd:PRK04319  288 YRILEDYKVTVWYTAPTAIRMLMGAGDDLVkkydLSSL--RhILSVGEPLNpEVVR-----WGM-KVFGLpihdnWWMTE 359

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   743 --ATVNASLArvAEHARP-TIGRALANVDLHVVDGLGRRKTRGASGELWI--GGAGVARGYAGDAGEAAGRFVEeGWpgs 817
Cdd:PRK04319  360 tgGIMIANYP--AMDIKPgSMGKPLPGIEAAIVDDQGNELPPNRMGNLAIkkGWPSMMRGIWNNPEKYESYFAG-DW--- 433

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 15597498   818 grlYRSGDLVRWRADGCLEFLGRIDEQVKINGYRIELGEIRSALLEHPAVGEAAV 872
Cdd:PRK04319  434 ---YVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGV 485
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
1199-1332 1.37e-15

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 83.56  E-value: 1.37e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1199 ALRGFLEARLPAYMLPSRIARVERLPLTAEGKLDRRalLAALAAEAAAQTLEAPANATEAALLEIWKSVLKRPAIGVSDN 1278
Cdd:PRK10252  924 ALQAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRK--ALPLPELKAQVPGRAPKTGTETIIAAAFSSLLGCDVVDADAD 1001

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 15597498  1279 FFQVGGDSirLIQMQVMA---REAGLAFTLRDVFNHQSIRELARLLAAPASPADALG 1332
Cdd:PRK10252 1002 FFALGGHS--LLAMKLAAqlsRQFARQVTPGQVMVASTVAKLATLLDAEEDESRRLG 1056
PLN02574 PLN02574
4-coumarate--CoA ligase-like
 446-899 1.74e-15

4-coumarate--CoA ligase-like


Pssm-ID: 215312 [Multi-domain]  Cd Length: 560  Bit Score: 82.20  E-value: 1.74e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   446 PVESLVAAFDLRAAlQPQAPALLDAHG--SLDFATLRAR-SEAVAEALLAAGVRPGQAVAVMTGRNREAIVALLGVMRAA 522
Cdd:PLN02574   38 PNLDAVSFIFSHHN-HNGDTALIDSSTgfSISYSELQPLvKSMAAGLYHVMGVRQGDVVLLLLPNSVYFPVIFLAVLSLG 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   523 AVYTPVNPEFPAARV-ERMREAG-GIVFALADAECAGRA--------REAFAGACLDLSTLP----LAGSGMSLPAP--G 586
Cdd:PLN02574  117 GIVTTMNPSSSLGEIkKRVVDCSvGLAFTSPENVEKLSPlgvpvigvPENYDFDSKRIEFPKfyelIKEDFDFVPKPviK 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   587 GRDAAYMIFTSGTSGQPKGVVVEHASALNLSQALAR---TVYANVVGEGLRVTVNAPFSFDSSIKQILQLLSGHCLVLVP 663
Cdd:PLN02574  197 QDDVAAIMYSSGTTGASKGVVLTHRNLIAMVELFVRfeaSQYEYPGSDNVYLAALPMFHIYGLSLFVVGLLSLGSTIVVM 276

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   664 QevRSDPQRMLGFLEERRIDVLDCTPSLFRLLLQAGLDDAHPALPGRILV---GGERFDEASWEVAAGWRRCQVFNLYGP 740
Cdd:PLN02574  277 R--RFDASDMVKVIDRFKVTHFPVVPPILMALTKKAKGVCGEVLKSLKQVscgAAPLSGKFIQDFVQTLPHVDFIQGYGM 354

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   741 TEATVNASLARVAEHAR--PTIGRALANVDLHVVD-GLGRRKTRGASGELWIGGAGVARGYAGDAGEAAGRFVEEGWpgs 817
Cdd:PLN02574  355 TESTAVGTRGFNTEKLSkySSVGLLAPNMQAKVVDwSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGW--- 431

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   818 grlYRSGDLVRWRADGCLEFLGRIDEQVKINGYRIELGEIRSALLEHPAVGEAAVL-TDEADAAE-PgadrriVAFVTAA 895
Cdd:PLN02574  432 ---LRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTaVPDKECGEiP------VAFVVRR 502


                  ....
gi 15597498   896 EETA 899
Cdd:PLN02574  503 QGST 506
Firefly_Luc cd17642
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ...
 589-884 3.08e-15

insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.


Pssm-ID: 341297 [Multi-domain]  Cd Length: 532  Bit Score: 81.03  E-value: 3.08e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  589 DAAYMIFTSGTSGQPKGVVVEHASALNLSQALARTVYANVVGEGLRVTVNAPFSFDSSIKQIL-QLLSGHCLVLVPqevR 667
Cdd:cd17642  185 QVALIMNSSGSTGLPKGVQLTHKNIVARFSHARDPIFGNQIIPDTAILTVIPFHHGFGMFTTLgYLICGFRVVLMY---K 261

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  668 SDPQRMLGFLEERRIDVLDCTPSLFRLLLQAGLDDAHP-ALPGRILVGGERFDEASWEVAAgwRRcqvFNL------YGP 740
Cdd:cd17642  262 FEEELFLRSLQDYKVQSALLVPTLFAFFAKSTLVDKYDlSNLHEIASGGAPLSKEVGEAVA--KR---FKLpgirqgYGL 336

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  741 TEATvNASLARVAEHARP-TIGRALANVDLHVVDgLGRRKTRGAS--GELWIGGAGVARGYAGDAGEAAGRFVEEGWpgs 817
Cdd:cd17642  337 TETT-SAILITPEGDDKPgAVGKVVPFFYAKVVD-LDTGKTLGPNerGELCVKGPMIMKGYVNNPEATKALIDKDGW--- 411

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15597498  818 grlYRSGDLVRWRADGCLEFLGRIDEQVKINGYRIELGEIRSALLEHPAVGEAAV--LTDEADAAEPGA 884
Cdd:cd17642  412 ---LHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVagIPDEDAGELPAA 477
C_PKS-NRPS_PksJ-like cd20484
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
 1393-1654 3.11e-15

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs), similar to Bacillus subtilis PksJ; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily have the typical C-domain HHxxxD motif. PksJ is involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is important in secondary metabolism. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380472 [Multi-domain]  Cd Length: 430  Bit Score: 80.44  E-value: 3.11e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1393 GRLDGELLARAWAILIGRHAILRTGFDLHGGqVPLQWVHPATAVAaeVPVHDLCGLDGEtrrlRLRAWIEEEQATPFDWS 1472
Cdd:cd20484   34 SKLDVEKFKQACQFVLEQHPILKSVIEEEDG-VPFQKIEPSKPLS--FQEEDISSLKES----EIIAYLREKAKEPFVLE 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1473 RPPLVRLAALALDERRFALGVAEHHSVLDGWSLQSLVDELLAVYADLLAGVVAREAEAPAVgFRDYVALEREAEANAASA 1552
Cdd:cd20484  107 NGPLMRVHLFSRSEQEHFVLITIHHIIFDGSSSLTLIHSLLDAYQALLQGKQPTLASSPAS-YYDFVAWEQDMLAGAEGE 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1553 ---LFWLDYLAGAryrpLPGLAEEGPRRMAAVRVD--------VPADSLSRLRALAERSGLPLRSLLLAAHGRALCRFSD 1621
Cdd:cd20484  186 ehrAYWKQQLSGT----LPILELPADRPRSSAPSFegqtytrrLPSELSNQIKSFARSQSINLSTVFLGIFKLLLHRYTG 261

                        250       260       270
                 ....*....|....*....|....*....|...
gi 15597498 1622 ADEVVTGFVSHGRPEEpGADRLLGLFLNTLPCR 1654
Cdd:cd20484  262 QEDIIVGMPTMGRPEE-RFDSLIGYFINMLPIR 293
PRK13382 PRK13382
bile acid CoA ligase;
452-899 3.57e-15

bile acid CoA ligase;


Pssm-ID: 172019 [Multi-domain]  Cd Length: 537  Bit Score: 80.96  E-value: 3.57e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   452 AAFDLRAALQPQAPALLDAHGSLDFATLRARSEAVAEALLAAGVRPGQAVAVMTGRNREAIVALLGVMRAAAVYTPVNPE 531
Cdd:PRK13382   47 SGFAIAAQRCPDRPGLIDELGTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTS 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   532 F--PAARVERMREAGGIVF-----------ALADAECAGRArEAFAGACLDLSTLPL-AGSGMSLPAPGGRDAAYMIFTS 597
Cdd:PRK13382  127 FagPALAEVVTREGVDTVIydeefsatvdrALADCPQATRI-VAWTDEDHDLTVEVLiAAHAGQRPEPTGRKGRVILLTS 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   598 GTSGQPKGVV-VEHASALNLSQALARTVYanvvgEGLRVTV-NAPFSFDSSIKQILQLLSGHCLVLVPQevRSDPQRMLG 675
Cdd:PRK13382  206 GTTGTPKGARrSGPGGIGTLKAILDRTPW-----RAEEPTViVAPMFHAWGFSQLVLAASLACTIVTRR--RFDPEATLD 278

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   676 FLEERRIDVLDCTPSLFRLLLqagldDAHPALPGRILVGGERFDEASWE------VAAGWRRCQ--VFNLYGPTEATVNA 747
Cdd:PRK13382  279 LIDRHRATGLAVVPVMFDRIM-----DLPAEVRNRYSGRSLRFAAASGSrmrpdvVIAFMDQFGdvIYNNYNATEAGMIA 353

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   748 SLARVAEHARP-TIGRALANVDLHVVDGLGRRKTRGASGELWIGGAGVARGY-AGDAGEAAGRFVEegwpgsgrlyrSGD 825
Cdd:PRK13382  354 TATPADLRAAPdTAGRPAEGTEIRILDQDFREVPTGEVGTIFVRNDTQFDGYtSGSTKDFHDGFMA-----------SGD 422

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15597498   826 LVRWRADGCLEFLGRIDEQVKINGYRIELGEIRSALLEHPAVGEAAVLTdeADAAEPGadRRIVAFVTAAEETA 899
Cdd:PRK13382  423 VGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIG--VDDEQYG--QRLAAFVVLKPGAS 492
PRK06145 PRK06145
acyl-CoA synthetase; Validated
 449-896 4.23e-15

acyl-CoA synthetase; Validated


Pssm-ID: 102207 [Multi-domain]  Cd Length: 497  Bit Score: 80.70  E-value: 4.23e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   449 SLVAAFDLRAALQPQAPALLDAHGSLDFATLRARSEAVAEALLAAGVRPGQAVAVMTgRNREAIVAL-LGVMRAAAVYTP 527
Cdd:PRK06145    3 NLSASIAFHARRTPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLM-KNSAAFLELaFAASYLGAVFLP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   528 VNPEFPAARVERMREAGGIVFALADAE----CAGRAREAFAGACLDLSTLPLAGSGMSLPAPGGR---DAAYMIFTSGTS 600
Cdd:PRK06145   82 INYRLAADEVAYILGDAGAKLLLVDEEfdaiVALETPKIVIDAAAQADSRRLAQGGLEIPPQAAVaptDLVRLMYTSGTT 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   601 GQPKGVVVEHAsalNLSQALARTVYANVVGEGLRVTVNAPF----SFDssIKQILQLLSGHCLVLvpqEVRSDPQRMLGF 676
Cdd:PRK06145  162 DRPKGVMHSYG---NLHWKSIDHVIALGLTASERLLVVGPLyhvgAFD--LPGIAVLWVGGTLRI---HREFDPEAVLAA 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   677 LEERRIDVLDCTPSLFRLLLqaglddahpALPGRilvggERFDEAS--WEVAAG--------------WRRCQVFNLYGP 740
Cdd:PRK06145  234 IERHRLTCAWMAPVMLSRVL---------TVPDR-----DRFDLDSlaWCIGGGektpesrirdftrvFTRARYIDAYGL 299

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   741 TEATVNASL---ARVAEHARPTiGRALANVDLHVVDGLGRRKTRGASGELWIGGAGVARGYAGDAGEAAGRFVeEGWpgs 817
Cdd:PRK06145  300 TETCSGDTLmeaGREIEKIGST-GRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFY-GDW--- 374

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15597498   818 grlYRSGDLVRWRADGCLEFLGRIDEQVKINGYRIELGEIRSALLEHPAVGEAAVLtdeaDAAEPGADRRIVAFVTAAE 896
Cdd:PRK06145  375 ---FRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVI----GVHDDRWGERITAVVVLNP 446
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
1354-1688 4.77e-15

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 81.63  E-value: 4.77e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1354 PEGLDDAYPMTSLQQGMLLQSEASGDPRLLHNVVLHEVHGRLDGELLARAWAILIGRHAILRTGFDLHGGQvPLQWVHPA 1433
Cdd:PRK10252    1 AEPMSQHLPLVAAQPGIWMAEKLSPLPSAWSVAHYVELTGELDAPLLARAVVAGLAEADTLRMRFTEDNGE-VWQWVDPA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1434 tAVAAEVPVHDLCGLDGETRRLRlrAWIEEEQATPFDWSR-PPLVRLAALALDERRFALGVAEHHSVLDGWSLQSLVDEL 1512
Cdd:PRK10252   80 -LTFPLPEIIDLRTQPDPHAAAQ--ALMQADLQQDLRVDSgKPLVFHQLIQLGDNRWYWYQRYHHLLVDGFSFPAITRRI 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1513 LAVYADLLAGvvAREAEAPAVGFRDYVALE---REAEANAASALFWLdylagARYRPLPGLAEEGPRRMAA-------VR 1582
Cdd:PRK10252  157 AAIYCAWLRG--EPTPASPFTPFADVVEEYqryRASEAWQRDAAFWA-----EQRRQLPPPASLSPAPLPGrsasadiLR 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1583 VDVPADSLSRLRALAERSGLPLRSLLLAAHGRALCRFSDADEVVTGFVSHGRPEEPGAdRLLGLFLNTLPCRLS--ASVD 1660
Cdd:PRK10252  230 LKLEFTDGAFRQLAAQASGVQRPDLALALVALWLGRLCGRMDYAAGFIFMRRLGSAAL-TATGPVLNVLPLRVHiaAQET 308

                         330       340
                  ....*....|....*....|....*...
gi 15597498  1661 LLDSARRAFDYERASLEHRRHPLAAIRR 1688
Cdd:PRK10252  309 LPELATRLAAQLKKMRRHQRYDAEQIVR 336
PRK07529 PRK07529
AMP-binding domain protein; Validated
 446-872 4.89e-15

AMP-binding domain protein; Validated


Pssm-ID: 236043 [Multi-domain]  Cd Length: 632  Bit Score: 80.77  E-value: 4.89e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   446 PVESLVAAFDLRAALQPQAPAL--------LDAHGSLDFATLRARSEAVAEALLAAGVRPGQAVAVMTGRNREAIVALLG 517
Cdd:PRK07529   23 LPASTYELLSRAAARHPDAPALsflldadpLDRPETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWG 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   518 VMrAAAVYTPVNPEF-PAARVERMREAGG-IVFALA---DAECAGRAREAFAgACLDLSTLPLAGSGMSLPAP------- 585
Cdd:PRK07529  103 GE-AAGIANPINPLLePEQIAELLRAAGAkVLVTLGpfpGTDIWQKVAEVLA-ALPELRTVVEVDLARYLPGPkrlavpl 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   586 ------------------------------GGRDAAYMIFTSGTSGQPKGVVVEHA--------SALNLSQALARTVYAN 627
Cdd:PRK07529  181 irrkaharildfdaelarqpgdrlfsgrpiGPDDVAAYFHTGGTTGMPKLAQHTHGnevanawlGALLLGLGPGDTVFCG 260

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   628 V----VGeGLRVTVNAPFSfdssikqilqllSG-HCLVLVPQEVRsDPQRMLGF---LEERRIDVLDCTPSLFRLLLQAG 699
Cdd:PRK07529  261 LplfhVN-ALLVTGLAPLA------------RGaHVVLATPQGYR-GPGVIANFwkiVERYRINFLSGVPTVYAALLQVP 326

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   700 LDDAH-----------PALPGRIlvgGERFDEASwevaaGWRrcqVFNLYGPTEATVNASLARVAEHARP-TIGRAL--A 765
Cdd:PRK07529  327 VDGHDisslryalcgaAPLPVEV---FRRFEAAT-----GVR---IVEGYGLTEATCVSSVNPPDGERRIgSVGLRLpyQ 395

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   766 NVDLHVVDGLGRRK---TRGASGELWIGGAGVARGYAgDAGEAAGRFVEEGWpgsgrlYRSGDLVRWRADGCLEFLGRID 842
Cdd:PRK07529  396 RVRVVILDDAGRYLrdcAVDEVGVLCIAGPNVFSGYL-EAAHNKGLWLEDGW------LNTGDLGRIDADGYFWLTGRAK 468

                         490       500       510
                  ....*....|....*....|....*....|
gi 15597498   843 EQVKINGYRIELGEIRSALLEHPAVGEAAV 872
Cdd:PRK07529  469 DLIIRGGHNIDPAAIEEALLRHPAVALAAA 498
PRK06178 PRK06178
acyl-CoA synthetase; Validated
 458-901 8.25e-15

acyl-CoA synthetase; Validated


Pssm-ID: 235724 [Multi-domain]  Cd Length: 567  Bit Score: 80.09  E-value: 8.25e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   458 AALQPQAPALlDAHGS-LDFATLRARSEAVAEALLAAGVRPGQAVAVMTGRNREAIVALLGVMRAAAVYTPVNPEFPAAR 536
Cdd:PRK06178   43 ARERPQRPAI-IFYGHvITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHE 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   537 VE-RMREAGGIVF----ALAD------AECAGR-------------------------AREAFAGACLDLSTLPLAGSGM 580
Cdd:PRK06178  122 LSyELNDAGAEVLlaldQLAPvveqvrAETSLRhvivtsladvlpaeptlplpdslraPRLAAAGAIDLLPALRACTAPV 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   581 SLPAPGGRDAAYMIFTSGTSGQPKGVVVEH-------ASALNLSQALAR-TVYAN------VVGEGLRVtvnapfsfdss 646
Cdd:PRK06178  202 PLPPPALDALAALNYTGGTTGMPKGCEHTQrdmvytaAAAYAVAVVGGEdSVFLSflpefwIAGENFGL----------- 270

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   647 ikqILQLLSGHCLVLVpqeVRSDPQRMLGFLEERRIDVLDCTPSLFRLLLQaglddaHPALPGRILVGGERFDEAS---- 722
Cdd:PRK06178  271 ---LFPLFSGATLVLL---ARWDAVAFMAAVERYRVTRTVMLVDNAVELMD------HPRFAEYDLSSLRQVRVVSfvkk 338

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   723 --------WEVAAGwrrCQVFNL-YGPTEATVNASLARVAE------HARPT-IGRALANVDLHVVD-GLGRRKTRGASG 785
Cdd:PRK06178  339 lnpdyrqrWRALTG---SVLAEAaWGMTETHTCDTFTAGFQdddfdlLSQPVfVGLPVPGTEFKICDfETGELLPLGAEG 415

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   786 ELWIGGAGVARGYAGDAgEAAGRFVEEGWpgsgrlYRSGDLVRWRADGCLEFLGRIDEQVKINGYRIELGEIRSALLEHP 865
Cdd:PRK06178  416 EIVVRTPSLLKGYWNKP-EATAEALRDGW------LHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHP 488

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|.
gi 15597498   866 AVGEAAVL--TDEADAAEPgadrriVAFVT---AAEETADE 901
Cdd:PRK06178  489 AVLGSAVVgrPDPDKGQVP------VAFVQlkpGADLTAAA 523
FADD10 cd17635
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ...
 588-876 9.56e-15

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: 78.07  E-value: 9.56e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  588 RDAAYMIFTSGTSGQPKGVVVEHASALNLSQALARTVYANVVGEGLRVTVNAPFSFDSSIKQILQLLSGHCLVLVPqevR 667
Cdd:cd17635    1 EDPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGE---N 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  668 SDPQRMLGFLEERRIDVLDCTPSLFRLLLQAgLDDAHPALPGR--ILVGGERFDEASWEVAAGWRRCQVFNLYGPTEATV 745
Cdd:cd17635   78 TTYKSLFKILTTNAVTTTCLVPTLLSKLVSE-LKSANATVPSLrlIGYGGSRAIAADVRFIEATGLTNTAQVYGLSETGT 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  746 NASL--ARVAEHARpTIGRALANVDLHVVDGLGRRKTRGASGELWIGGAGVARGYAGDAGEAAGRFVeEGWpgsgrlYRS 823
Cdd:cd17635  157 ALCLptDDDSIEIN-AVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLI-DGW------VNT 228

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 15597498  824 GDLVRWRADGCLEFLGRIDEQVKINGYRIELGEIRSALLEHPAVGEAAV--LTDE 876
Cdd:cd17635  229 GDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACyeISDE 283
ACS cd05966
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ...
 589-893 9.92e-15

Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.


Pssm-ID: 341270 [Multi-domain]  Cd Length: 608  Bit Score: 79.91  E-value: 9.92e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  589 DAAYMIFTSGTSGQPKGVVveHASALNLSQALARTVYAnvvgeglrvtvnapfsFD----------SSIKQIlqllSGHC 658
Cdd:cd05966  232 DPLFILYTSGSTGKPKGVV--HTTGGYLLYAATTFKYV----------------FDyhpddiywctADIGWI----TGHS 289

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  659 LVL---------------VPqeVRSDPQRMLGFLEERRIDVLDCTPSLFRLLLQAGLD--DAHPALPGRIL--VGgERFD 719
Cdd:cd05966  290 YIVygplangattvmfegTP--TYPDPGRYWDIVEKHKVTIFYTAPTAIRALMKFGDEwvKKHDLSSLRVLgsVG-EPIN 366

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  720 EASW----EVAaGWRRCQVFNLYGPTE--ATVNASLARVAEhARP-TIGRALANVDLHVVDGLGRRKTRGASGELWIGGA 792
Cdd:cd05966  367 PEAWmwyyEVI-GKERCPIVDTWWQTEtgGIMITPLPGATP-LKPgSATRPFFGIEPAILDEEGNEVEGEVEGYLVIKRP 444

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  793 --GVARGYAGDAGeaagRFVEEGWPGSGRLYRSGDLVRWRADGCLEFLGRIDEQVKINGYRIELGEIRSALLEHPAVGEA 870
Cdd:cd05966  445 wpGMARTIYGDHE----RYEDTYFSKFPGYYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEA 520

                        330       340
                 ....*....|....*....|....*....
gi 15597498  871 AV------LTDEAdaaepgadrrIVAFVT 893
Cdd:cd05966  521 AVvgrphdIKGEA----------IYAFVT 539
A_NRPS_TubE_like cd05906
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ...
 476-867 1.23e-14

The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341232 [Multi-domain]  Cd Length: 540  Bit Score: 79.25  E-value: 1.23e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  476 FATLRARSEAVAEALLAAGVRPGQAVAVMTGRNREAIVALLGVMRAAAVYTPVNP----EFPAARVERMREA-----GGI 546
Cdd:cd05906   42 YQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPLTVpptyDEPNARLRKLRHIwqllgSPV 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  547 VFALADAECAGRAREAFAGAC----LDLSTLPLAGSGMSLPAPGGRDAAYMIFTSGTSGQPKGVVVEHAsalnlsQALAR 622
Cdd:cd05906  122 VLTDAELVAEFAGLETLSGLPgirvLSIEELLDTAADHDLPQSRPDDLALLMLTSGSTGFPKAVPLTHR------NILAR 195

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  623 TVYANVVGEGLR--VTVN-APFSFDSSIKQI-LQLLSGHCL-VLVP-QEVRSDPQRMLGFLEERRIDVLDCTPSLFRLLL 696
Cdd:cd05906  196 SAGKIQHNGLTPqdVFLNwVPLDHVGGLVELhLRAVYLGCQqVHVPtEEILADPLRWLDLIDRYRVTITWAPNFAFALLN 275

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  697 QA--GLDDAHPALPG--RILVGGE--------RFDE-------------ASW---EVAAGWRRCQVFNLYGPTEATVNAS 748
Cdd:cd05906  276 DLleEIEDGTWDLSSlrYLVNAGEavvaktirRLLRllepyglppdairPAFgmtETCSGVIYSRSFPTYDHSQALEFVS 355

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  749 LarvaeharptiGRALANVDLHVVDGLGRRKTRGASGELWIGGAGVARGYAGDAGEAAGRFVEEGWpgsgrlYRSGDLVr 828
Cdd:cd05906  356 L-----------GRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTEDGW------FRTGDLG- 417

                        410       420       430
                 ....*....|....*....|....*....|....*....
gi 15597498  829 WRADGCLEFLGRIDEQVKINGYRIELGEIRSALLEHPAV 867
Cdd:cd05906  418 FLDNGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGV 456
FACL_like_2 cd05917
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 589-872 6.73e-14

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341241 [Multi-domain]  Cd Length: 349  Bit Score: 75.39  E-value: 6.73e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  589 DAAYMIFTSGTSGQPKGVVVEHASALNlsqalartvYANVVGEGLRVTVN------APF--SFDSSIKQILQLLSGHCLV 660
Cdd:cd05917    3 DVINIQFTSGTTGSPKGATLTHHNIVN---------NGYFIGERLGLTEQdrlcipVPLfhCFGSVLGVLACLTHGATMV 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  661 LVpqEVRSDPQRMLGFLEERRIDVLDCTPSLFRLLLQaglddaHPALPgrilvggeRFDEASWE--VAAGW--------R 730
Cdd:cd05917   74 FP--SPSFDPLAVLEAIEKEKCTALHGVPTMFIAELE------HPDFD--------KFDLSSLRtgIMAGApcppelmkR 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  731 RCQVFNL------YGPTEAT-------VNASLARVAEharpTIGRALANVDLHVVDGLGRRK-TRGASGELWIGGAGVAR 796
Cdd:cd05917  138 VIEVMNMkdvtiaYGMTETSpvstqtrTDDSIEKRVN----TVGRIMPHTEAKIVDPEGGIVpPVGVPGELCIRGYSVMK 213

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15597498  797 GYAGDAGEAAGRFVEEGWpgsgrlYRSGDLVRWRADGCLEFLGRIDEQVKINGYRIELGEIRSALLEHPAVGEAAV 872
Cdd:cd05917  214 GYWNDPEKTAEAIDGDGW------LHTGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQV 283
FACL_like_1 cd05910
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 474-871 1.02e-13

Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341236 [Multi-domain]  Cd Length: 457  Bit Score: 75.96  E-value: 1.02e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  474 LDFATLRARSEAVAEALLAAGVRPGQAVAVMTGRNREAIVALLGVMRAAAVYTPVNPEFPAARVERmreaggivfALADA 553
Cdd:cd05910    3 LSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQ---------CLQEA 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  554 EcagraREAFAGacldlstLPLAGsgmslpapggrDAAYMIFTSGTSGQPKGVVVEHASALNLSQALaRTVYANVVGEGL 633
Cdd:cd05910   74 E-----PDAFIG-------IPKAD-----------EPAAILFTSGSTGTPKGVVYRHGTFAAQIDAL-RQLYGIRPGEVD 129

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  634 RVTVnAPFSfdssikqILQLLSGHCLVLVPQE----VRSDPQRMLGFLEERRIDVLDCTPSLFRLLLQAGLDDAHPaLPG 709
Cdd:cd05910  130 LATF-PLFA-------LFGPALGLTSVIPDMDptrpARADPQKLVGAIRQYGVSIVFGSPALLERVARYCAQHGIT-LPS 200

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  710 --RILVGGERFDEAsweVAAGWRR-----CQVFNLYGPTEA---TVNASLARVAEHARPT-------IGRALANVDLHVV 772
Cdd:cd05910  201 lrRVLSAGAPVPIA---LAARLRKmlsdeAEILTPYGATEAlpvSSIGSRELLATTTAATsggagtcVGRPIPGVRVRII 277

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  773 D---------GLGRRKTRGASGELWIGGAGVARGYAGDagEAAGRFVEEGWPGSGRLYRSGDLVRWRADGCLEFLGRIDE 843
Cdd:cd05910  278 EiddepiaewDDTLELPRGEIGEITVTGPTVTPTYVNR--PVATALAKIDDNSEGFWHRMGDLGYLDDEGRLWFCGRKAH 355

                        410       420
                 ....*....|....*....|....*...
gi 15597498  844 QVKINGYRIELGEIRSALLEHPAVGEAA 871
Cdd:cd05910  356 RVITTGGTLYTEPVERVFNTHPGVRRSA 383
PRK08314 PRK08314
long-chain-fatty-acid--CoA ligase; Validated
 446-872 2.00e-13

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236235 [Multi-domain]  Cd Length: 546  Bit Score: 75.38  E-value: 2.00e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   446 PVESLVAAFDLRAALQPQAPALLDAHGSLDFATLRARSEAVAE-ALLAAGVRPGQAVAVMTGRNREAIVALLGVMRAAAV 524
Cdd:PRK08314    8 PETSLFHNLEVSARRYPDKTAIVFYGRAISYRELLEEAERLAGyLQQECGVRKGDRVLLYMQNSPQFVIAYYAILRANAV 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   525 YTPVNPEFPAARVERMREAGGIVFALADAECAGRAREAFAGACLD-------LSTLPlAGSGMSLPA------------- 584
Cdd:PRK08314   88 VVPVNPMNREEELAHYVTDSGARVAIVGSELAPKVAPAVGNLRLRhvivaqySDYLP-AEPEIAVPAwlraepplqalap 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   585 --------------------PGGRDAAYMIFTSGTSGQPKGVVVEHasalnlsqalaRTVYANVVGEGLRVTVNA----- 639
Cdd:PRK08314  167 ggvvawkealaaglappphtAGPDDLAVLPYTSGTTGVPKGCMHTH-----------RTVMANAVGSVLWSNSTPesvvl 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   640 ---PF--------SFDSSIkqilqlLSGHCLVLVPqevRSDPQRMLGFLEERRIDVLDCTPS-LFRLLLQAGLDDAHpaL 707
Cdd:PRK08314  236 avlPLfhvtgmvhSMNAPI------YAGATVVLMP---RWDREAAARLIERYRVTHWTNIPTmVVDFLASPGLAERD--L 304

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   708 PGRILVGGerfDEASWEVAAGWRRCQVFNL-----YGPTEaTVNASLARVAEHARPT-IGRALANVDLHVVD-GLGRRKT 780
Cdd:PRK08314  305 SSLRYIGG---GGAAMPEAVAERLKELTGLdyvegYGLTE-TMAQTHSNPPDRPKLQcLGIPTFGVDARVIDpETLEELP 380

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   781 RGASGELWIGGAGVARGYAGDAGEAAGRFVE-EGwpgsGRLYRSGDLVRWRADGCLEFLGRIDEQVKINGYRIELGEIRS 859
Cdd:PRK08314  381 PGEVGEIVVHGPQVFKGYWNRPEATAEAFIEiDG----KRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVEN 456

                         490
                  ....*....|...
gi 15597498   860 ALLEHPAVGEAAV 872
Cdd:PRK08314  457 LLYKHPAIQEACV 469
LCL_NRPS cd19538
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ...
 1393-1683 2.33e-13

LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.


Pssm-ID: 380461 [Multi-domain]  Cd Length: 432  Bit Score: 74.61  E-value: 2.33e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1393 GRLDGELLARAWAILIGRHAILRTGFDLHGGqVPLQWVHPATAvaAEVPVHDLcgldgETRRLRLRAWIEEEQATPFDWS 1472
Cdd:cd19538   34 GKLDVQALQQALYDVVERHESLRTVFPEEDG-VPYQLILEEDE--ATPKLEIK-----EVDEEELESEINEAVRYPFDLS 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1473 RPPLVRLAALALDERRFALGVAEHHSVLDGWSLQSLVDELLAVYADLLAGVVAREAEAPaVGFRDYVALERE---AEANA 1549
Cdd:cd19538  106 EEPPFRATLFELGENEHVLLLLLHHIAADGWSLAPLTRDLSKAYRARCKGEAPELAPLP-VQYADYALWQQEllgDESDP 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1550 ASAL-----FWLDYLAGaryrpLPGLAE---EGPRRMAA------VRVDVPADSLSRLRALAERSGLPLRSLLLAAHGRA 1615
Cdd:cd19538  185 DSLIarqlaYWKKQLAG-----LPDEIElptDYPRPAESsyeggtLTFEIDSELHQQLLQLAKDNNVTLFMVLQAGFAAL 259

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1616 LCRFSDADEVVTGFVSHGRPEEpGADRLLGLFLNTLPCRLSASVD-----LLDSARR----AFDYERASLEH-------- 1678
Cdd:cd19538  260 LTRLGAGTDIPIGSPVAGRNDD-SLEDLVGFFVNTLVLRTDTSGNpsfreLLERVKEtnleAYEHQDIPFERlvealnpt 338


                 ....*...
gi 15597498 1679 ---RRHPL 1683
Cdd:cd19538  339 rsrSRHPL 346
PRK12406 PRK12406
long-chain-fatty-acid--CoA ligase; Provisional
 473-872 2.54e-13

long-chain-fatty-acid--CoA ligase; Provisional


Pssm-ID: 183506 [Multi-domain]  Cd Length: 509  Bit Score: 75.12  E-value: 2.54e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   473 SLDFATLRARSEAVAEALLAAGVRPGQAVAVMTgRNREA-IVALLGVMRAAAVYTPVNPEFPAARVERMREAGGIVFALA 551
Cdd:PRK12406   11 RRSFDELAQRAARAAGGLAALGVRPGDCVALLM-RNDFAfFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIA 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   552 DAECAGRAREAFAGAC--LDLSTLP-------LAGSGMSLPA-----------------PGGRDAAYMIFTSGTSGQPKG 605
Cdd:PRK12406   90 HADLLHGLASALPAGVtvLSVPTPPeiaaayrISPALLTPPAgaidwegwlaqqepydgPPVPQPQSMIYTSGTTGHPKG 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   606 V-----VVEHASAlnlSQALARTVYAnvVGEGLRVTVN------APFSFDssikqILQLLSGHCLVLVPqevRSDPQRML 674
Cdd:PRK12406  170 VrraapTPEQAAA---AEQMRALIYG--LKPGIRALLTgplyhsAPNAYG-----LRAGRLGGVLVLQP---RFDPEELL 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   675 GFLEERRIDVLDCTPSLFRLLLQaglddahpaLPGRIlvgGERFDEAS--WEVAAG-------------WRRCQVFNLYG 739
Cdd:PRK12406  237 QLIERHRITHMHMVPTMFIRLLK---------LPEEV---RAKYDVSSlrHVIHAAapcpadvkramieWWGPVIYEYYG 304

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   740 PTEATVNASLARVAEHARP-TIGRALANVDLHVVDGLGRRKTRGASGELWIGGAGVAR-GYAGDAGEAAGrfveegwPGS 817
Cdd:PRK12406  305 STESGAVTFATSEDALSHPgTVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAGNPDfTYHNKPEKRAE-------IDR 377

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 15597498   818 GRLYRSGDLVRWRADGCLEFLGRIDEQVKINGYRIELGEIRSALLEHPAVGEAAV 872
Cdd:PRK12406  378 GGFITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAV 432
ACLS-CaiC cd17637
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ...
 589-872 3.14e-13

acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341292 [Multi-domain]  Cd Length: 333  Bit Score: 73.07  E-value: 3.14e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  589 DAAYMIFTSGTSGQPKGVVVEHAsalNLSQALARTVYANVVGEGLRVTVNAPFSFDSSIKQILQLL-SGHCLVLVPqevR 667
Cdd:cd17637    1 DPFVIIHTAAVAGRPRGAVLSHG---NLIAANLQLIHAMGLTEADVYLNMLPLFHIAGLNLALATFhAGGANVVME---K 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  668 SDPQRMLGFLEERRIDVL-DCTPSLFRLLLQAgldDAHPALPG--RILVGGErfdeaSWEVAAGWRRC---QVFNLYGPT 741
Cdd:cd17637   75 FDPAEALELIEEEKVTLMgSFPPILSNLLDAA---EKSGVDLSslRHVLGLD-----APETIQRFEETtgaTFWSLYGQT 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  742 EATVNASLARVAEhaRP-TIGRALANVDLHVVDGLGRRKTRGASGELWIGGAGVARGYAGDAGEAAGRFvEEGWpgsgrl 820
Cdd:cd17637  147 ETSGLVTLSPYRE--RPgSAGRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTF-RNGW------ 217

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 15597498  821 YRSGDLVRWRADGCLEFLGRIDEQ--VKINGYRIELGEIRSALLEHPAVGEAAV 872
Cdd:cd17637  218 HHTGDLGRFDEDGYLWYAGRKPEKelIKPGGENVYPAEVEKVILEHPAIAEVCV 271
PrpE cd05967
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ...
 589-873 3.35e-13

Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.


Pssm-ID: 341271 [Multi-domain]  Cd Length: 617  Bit Score: 75.04  E-value: 3.35e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  589 DAAYMIFTSGTSGQPKGVVVE---HASALNLSQalaRTVYAN--------------VVGEGLrvTVNAPfsfdssikqil 651
Cdd:cd05967  231 DPLYILYTSGTTGKPKGVVRDnggHAVALNWSM---RNIYGIkpgdvwwaasdvgwVVGHSY--IVYGP----------- 294

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  652 qLLSGHCLVLVP-QEVRS-DPQRMLGFLEERRIDVLDCTPSLFRLLLQAGLDDAHpalpGR---------ILVGGERFDE 720
Cdd:cd05967  295 -LLHGATTVLYEgKPVGTpDPGAFWRVIEKYQVNALFTAPTAIRAIRKEDPDGKY----IKkydlsslrtLFLAGERLDP 369

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  721 ASWEVAAGWRRCQVFNLYGPTEA--TVNASLARVAEHARP--TIGRALANVDLHVVDGLGRRKTRGASGELWIGGA---G 793
Cdd:cd05967  370 PTLEWAENTLGVPVIDHWWQTETgwPITANPVGLEPLPIKagSPGKPVPGYQVQVLDEDGEPVGPNELGNIVIKLPlppG 449

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  794 VARGYAGDAGeaagRFVEEGWPGSGRLYRSGDLVRWRADGCLEFLGRIDEQVKINGYRIELGEIRSALLEHPAVGEAAVL 873
Cdd:cd05967  450 CLLTLWKNDE----RFKKLYLSKFPGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVV 525
PRK03640 PRK03640
o-succinylbenzoate--CoA ligase;
457-901 4.00e-13

o-succinylbenzoate--CoA ligase;


Pssm-ID: 235146 [Multi-domain]  Cd Length: 483  Bit Score: 74.23  E-value: 4.00e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   457 RAALQPQAPALLDAHGSLDFATLRARSEAVAEALLAAGVRPGQAVAVMTGRNRE---AIVAL--LGV------------- 518
Cdd:PRK03640   11 RAFLTPDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEmilVIHALqqLGAvavllntrlsree 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   519 -----MRAAAVYTPVNPEFPAarvermREAGGIVFALADAEcAGRAREAFAgacldLSTLPLagsgmslpapggRDAAYM 593
Cdd:PRK03640   91 llwqlDDAEVKCLITDDDFEA------KLIPGISVKFAELM-NGPKEEAEI-----QEEFDL------------DEVATI 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   594 IFTSGTSGQPKGVVV---EH-----ASALNLsqalartvyanvvgeGLR------VTVnaPFsFDSSIKQIL--QLLSGH 657
Cdd:PRK03640  147 MYTSGTTGKPKGVIQtygNHwwsavGSALNL---------------GLTeddcwlAAV--PI-FHISGLSILmrSVIYGM 208

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   658 CLVLVPqevRSDPQRMLGFLEERRIDVLDCTPS-LFRLLLQAGLDDAHPALPGrILVGGERFDEASWEVAAGwRRCQVFN 736
Cdd:PRK03640  209 RVVLVE---KFDAEKINKLLQTGGVTIISVVSTmLQRLLERLGEGTYPSSFRC-MLLGGGPAPKPLLEQCKE-KGIPVYQ 283

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   737 LYGPTE-ATVNASLArvAEHARPTIGRA---LANVDLHVVDGlGRRKTRGASGELWIGGAGVARGYAG--DAGEAAgrfV 810
Cdd:PRK03640  284 SYGMTEtASQIVTLS--PEDALTKLGSAgkpLFPCELKIEKD-GVVVPPFEEGEIVVKGPNVTKGYLNreDATRET---F 357

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   811 EEGWpgsgrlYRSGDLVRWRADGCLEFLGRIDEQVKINGYRIELGEIRSALLEHPAVGEAAV--LTDEADAAEPgadrri 888
Cdd:PRK03640  358 QDGW------FKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVvgVPDDKWGQVP------ 425

                         490
                  ....*....|....
gi 15597498   889 VAFVTAAEE-TADE 901
Cdd:PRK03640  426 VAFVVKSGEvTEEE 439
FAAL cd05931
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ...
 457-901 4.26e-13

Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.


Pssm-ID: 341254 [Multi-domain]  Cd Length: 547  Bit Score: 74.58  E-value: 4.26e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  457 RAALQPQAPAL--LDAHGSLD----FATLRARSEAVAEALLAAGvRPGQAVAVMTGRNREAIVALLGVMRAAAVYTPVNP 530
Cdd:cd05931    2 RAAARPDRPAYtfLDDEGGREetltYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  531 EFPAARVERMREA---GGIVFALADAECAGRAREAFAGAC-------LDLSTLPLAGSGMSL-PAPGGRDAAYMIFTSGT 599
Cdd:cd05931   81 PTPGRHAERLAAIladAGPRVVLTTAAALAAVRAFAASRPaagtprlLVVDLLPDTSAADWPpPSPDPDDIAYLQYTSGS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  600 SGQPKGVVVEHASALNLSQALARTVYANvvgEGLRVTVNAPFSFDSSIKQ-ILQ-LLSGHCLVLV-PQEVRSDPQRMLGF 676
Cdd:cd05931  161 TGTPKGVVVTHRNLLANVRQIRRAYGLD---PGDVVVSWLPLYHDMGLIGgLLTpLYSGGPSVLMsPAAFLRRPLRWLRL 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  677 LEERRIdvlDCTPS---LFRLLLQAGLDDAHPALP----GRILVGGERFDEASWEV------AAGWRRCQVFNLYGPTEA 743
Cdd:cd05931  238 ISRYRA---TISAApnfAYDLCVRRVRDEDLEGLDlsswRVALNGAEPVRPATLRRfaeafaPFGFRPEAFRPSYGLAEA 314

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  744 TVNASLAR---------------------VAEHARPTI-----GRALANVDLHVVDGLGRRKTR-GASGELWIGGAGVAR 796
Cdd:cd05931  315 TLFVSGGPpgtgpvvlrvdrdalagravaVAADDPAARelvscGRPLPDQEVRIVDPETGRELPdGEVGEIWVRGPSVAS 394

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  797 GYAGDAGEAAGRFVEEGWPGSGRLYRSGDLvRWRADGCLEFLGRIDEQVKING-----YRIElgeiRSALLEHPAVGEAA 871
Cdd:cd05931  395 GYWGRPEATAETFGALAATDEGGWLRTGDL-GFLHDGELYITGRLKDLIIVRGrnhypQDIE----ATAEEAHPALRPGC 469

                        490       500       510
                 ....*....|....*....|....*....|
gi 15597498  872 VltdeADAAEPGADRRIVAFVTAAEETADE 901
Cdd:cd05931  470 V----AAFSVPDDGEERLVVVAEVERGADP 495
PRK05677 PRK05677
long-chain-fatty-acid--CoA ligase; Validated
 584-871 6.48e-13

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 168170 [Multi-domain]  Cd Length: 562  Bit Score: 74.03  E-value: 6.48e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   584 APGGRDAAYMIFTSGTSGQPKGVVVEHASAL-NLSQAlaRTVYANVVGEGLRVTVnAP------FSFdsSIKQILQLLSG 656
Cdd:PRK05677  203 NPQADDVAVLQYTGGTTGVAKGAMLTHRNLVaNMLQC--RALMGSNLNEGCEILI-APlplyhiYAF--TFHCMAMMLIG 277

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   657 HCLVLVPqevrsDPQRMLGFLEERR------------IDVLDCTPSLFRLLLQAGLDdahpalpgRILVGGERFDEAswe 724
Cdd:PRK05677  278 NHNILIS-----NPRDLPAMVKELGkwkfsgfvglntLFVALCNNEAFRKLDFSALK--------LTLSGGMALQLA--- 341

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   725 VAAGWRR---CQVFNLYGPTE----ATVNAslarvAEHARP-TIGRALANVDLHVVDGLGRRKTRGASGELWIGGAGVAR 796
Cdd:PRK05677  342 TAERWKEvtgCAICEGYGMTEtspvVSVNP-----SQAIQVgTIGIPVPSTLCKVIDDDGNELPLGEVGELCVKGPQVMK 416

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15597498   797 GYAGDAGEAAGRFVEEGWpgsgrlYRSGDLVRWRADGCLEFLGRIDEQVKINGYRIELGEIRSALLEHPAVGEAA 871
Cdd:PRK05677  417 GYWQRPEATDEILDSDGW------LKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCA 485
FACL_like_5 cd05924
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 589-901 6.88e-13

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: 341248 [Multi-domain]  Cd Length: 364  Bit Score: 72.41  E-value: 6.88e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  589 DAAYMIFTSGTSGQPKGVVVEHA---SALNLSQALARTVYANVVGEGLRVTVNAPFSF---------DSSIKQILQLLSG 656
Cdd:cd05924    4 DDLYILYTGGTTGMPKGVMWRQEdifRMLMGGADFGTGEFTPSEDAHKAAAAAAGTVMfpapplmhgTGSWTAFGGLLGG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  657 HCLVLVpqEVRSDPQRMLGFLEERRIDVLDCTPSLF-RLLLQAgLDDAHPA-LPGRILV--GGERFdeaSWEVAAGWRRC 732
Cdd:cd05924   84 QTVVLP--DDRFDPEEVWRTIEKHKVTSMTIVGDAMaRPLIDA-LRDAGPYdLSSLFAIssGGALL---SPEVKQGLLEL 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  733 Q----VFNLYGPTEATVNASlARVAEHARPTIGRALANVDLHVVDGLGRRKTRGASGELWIGGAG-VARGYAGDAGEAAG 807
Cdd:cd05924  158 VpnitLVDAFGSSETGFTGS-GHSAGSGPETGPFTRANPDTVVLDDDGRVVPPGSGGVGWIARRGhIPLGYYGDEAKTAE 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  808 RFVEEGwpgSGRLYRSGDLVRWRADGCLEFLGRIDEQVKINGYRIELGEIRSALLEHPAVGEAAV--LTDEADAAEPGAd 885
Cdd:cd05924  237 TFPEVD---GVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVvgRPDERWGQEVVA- 312

                        330
                 ....*....|....*.
gi 15597498  886 rrIVAFVTAAEETADE 901
Cdd:cd05924  313 --VVQLREGAGVDLEE 326
PLN02330 PLN02330
4-coumarate--CoA ligase-like 1
 494-897 1.21e-12

4-coumarate--CoA ligase-like 1


Pssm-ID: 215189 [Multi-domain]  Cd Length: 546  Bit Score: 73.09  E-value: 1.21e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   494 GVRPGQAVAVMTGRNREAIVALLGVMRAAAVYTPVNPEFPAARVERMREAGGIVFALADAECAGRAR-----------EA 562
Cdd:PLN02330   76 GLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVTNDTNYGKVKglglpvivlgeEK 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   563 FAGAC---LDLSTLPLAGSGMSLPAPGGRDAAYMIFTSGTSGQPKGVVVEHASAL-NLSQALArTVYANVVGEGLRVTVn 638
Cdd:PLN02330  156 IEGAVnwkELLEAADRAGDTSDNEEILQTDLCALPFSSGTTGISKGVMLTHRNLVaNLCSSLF-SVGPEMIGQVVTLGL- 233

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   639 APFSFDSSIKQILQLL---SGHCLV------------LVPQEVRSDP---QRMLGFLEERRIDVLDctpsLFRLLLQAGL 700
Cdd:PLN02330  234 IPFFHIYGITGICCATlrnKGKVVVmsrfelrtflnaLITQEVSFAPivpPIILNLVKNPIVEEFD----LSKLKLQAIM 309

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   701 DDAHPALPGRILVGGERFDEAswevaagwrrcQVFNLYGPTEATvnaslARVAEHARPTIGRALA----------NVDLH 770
Cdd:PLN02330  310 TAAAPLAPELLTAFEAKFPGV-----------QVQEAYGLTEHS-----CITLTHGDPEKGHGIAkknsvgfilpNLEVK 373

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   771 VVD-GLGRRKTRGASGELWIGGAGVARGYAGDAGEAAGRFVEEGWpgsgrlYRSGDLVRWRADGCLEFLGRIDEQVKING 849
Cdd:PLN02330  374 FIDpDTGRSLPKNTPGELCVRSQCVMQGYYNNKEETDRTIDEDGW------LHTGDIGYIDDDGDIFIVDRIKELIKYKG 447

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 15597498   850 YRIELGEIRSALLEHPAVGEAAV--LTDEADAAEPGADRRIVAFVTAAEE 897
Cdd:PLN02330  448 FQVAPAELEAILLTHPSVEDAAVvpLPDEEAGEIPAACVVINPKAKESEE 497
PRK13390 PRK13390
acyl-CoA synthetase; Provisional
 458-901 1.57e-12

acyl-CoA synthetase; Provisional


Pssm-ID: 139538 [Multi-domain]  Cd Length: 501  Bit Score: 72.35  E-value: 1.57e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   458 AALQPQAPALLDAHG--SLDFATLRARSEAVAEALLAAGVRPGQAVAVMTGRNREAIVALLGVMRAAAVYTPVNPEFPAA 535
Cdd:PRK13390    7 AQIAPDRPAVIVAETgeQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAP 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   536 RVERMREAGGIVFALADAECAGRAREAFAGACLDLS-----------TLPLAGSGMSLP-APGGrdaAYMIFTSGTSGQP 603
Cdd:PRK13390   87 EADYIVGDSGARVLVASAALDGLAAKVGADLPLRLSfggeidgfgsfEAALAGAGPRLTeQPCG---AVMLYSSGTTGFP 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   604 KGVVVEhASALNLSQ------ALARTVY----ANVVGEGLRVTVNAPFSFDSSIKQIlqllsGHCLVLVPqevRSDPQRM 673
Cdd:PRK13390  164 KGIQPD-LPGRDVDApgdpivAIARAFYdiseSDIYYSSAPIYHAAPLRWCSMVHAL-----GGTVVLAK---RFDAQAT 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   674 LGFLEERRIDVLDCTPSLFRLLLQagLDDA--------------HPALPGRILVGGERFDeaswevaagWRRCQVFNLYG 739
Cdd:PRK13390  235 LGHVERYRITVTQMVPTMFVRLLK--LDADvrtrydvsslraviHAAAPCPVDVKHAMID---------WLGPIVYEYYS 303

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   740 PTEA---TVNASLARVAEHArpTIGRALANvDLHVVDGLGRRKTRGASGELWIGGAGVARGYAGDAGEAAgrfvEEGWPG 816
Cdd:PRK13390  304 STEAhgmTFIDSPDWLAHPG--SVGRSVLG-DLHICDDDGNELPAGRIGTVYFERDRLPFRYLNDPEKTA----AAQHPA 376

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   817 SGRLYRSGDLVRWRADGCLEFLGRIDEQVKINGYRIELGEIRSALLEHPAVGEAAVL--TDEADAAEPGADRRIVAFVTA 894
Cdd:PRK13390  377 HPFWTTVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIgvPDPEMGEQVKAVIQLVEGIRG 456


                  ....*..
gi 15597498   895 AEETADE 901
Cdd:PRK13390  457 SDELARE 463
caiC PRK08008
putative crotonobetaine/carnitine-CoA ligase; Validated
 589-896 3.99e-12

putative crotonobetaine/carnitine-CoA ligase; Validated


Pssm-ID: 181195 [Multi-domain]  Cd Length: 517  Bit Score: 71.25  E-value: 3.99e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   589 DAAYMIFTSGTSGQPKGVVVEHAsalNLSQALARTVYANVVGEGLR-VTVNAPFSFDSSIKQILQLLS-GHCLVLVpqEV 666
Cdd:PRK08008  174 DTAEILFTSGTTSRPKGVVITHY---NLRFAGYYSAWQCALRDDDVyLTVMPAFHIDCQCTAAMAAFSaGATFVLL--EK 248

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   667 RSdPQRMLGFLEERRIDVLDCTPSLFR-LLLQaglddahPALPGrilvggER----------FDEASWEVAAGWRRCQV- 734
Cdd:PRK08008  249 YS-ARAFWGQVCKYRATITECIPMMIRtLMVQ-------PPSAN------DRqhclrevmfyLNLSDQEKDAFEERFGVr 314

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   735 -FNLYGPTEATVNASLARVAEHAR-PTIGRALANVDLHVVDGLGRRKTRGASGELWIGG-AG--VARGYAGDAGEAAGRF 809
Cdd:PRK08008  315 lLTSYGMTETIVGIIGDRPGDKRRwPSIGRPGFCYEAEIRDDHNRPLPAGEIGEICIKGvPGktIFKEYYLDPKATAKVL 394

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   810 VEEGWpgsgrLYrSGDLVRWRADGCLEFLGRIDEQVKINGYRIELGEIRSALLEHPAVGEAAVLtdeaDAAEPGADRRIV 889
Cdd:PRK08008  395 EADGW-----LH-TGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVV----GIKDSIRDEAIK 464


                  ....*..
gi 15597498   890 AFVTAAE 896
Cdd:PRK08008  465 AFVVLNE 471
PRK05691 PRK05691
peptide synthase; Validated
 1193-1318 7.98e-12

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 71.35  E-value: 7.98e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1193 GELSEQaLRGFLEARLPAYMLPSRIARVERLPLTAEGKLDRRALLAALAAEAAAQTLEAPANATEAALLEIWKSVLKRPA 1272
Cdd:PRK05691 4180 GALLER-IKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKALPALDIGQLQSQAYLAPRNELEQTLATIWADVLKVER 4258

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 15597498  1273 IGVSDNFFQVGGDSIRLIQMQVMAREA-GLAFTLRDVFNHQSIRELA 1318
Cdd:PRK05691 4259 VGVHDNFFELGGHSLLATQIASRVQKAlQRNVPLRAMFECSTVEELA 4305
LC_FACS_euk1 cd17639
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ...
 732-892 1.48e-11

Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.


Pssm-ID: 341294 [Multi-domain]  Cd Length: 507  Bit Score: 69.17  E-value: 1.48e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  732 CQVFNLYGPTEATVNASLARVAEHARPTIGRALANVDLHVVD---GLGRRKTRGASGELWIGGAGVARGYAGDAGEAAGR 808
Cdd:cd17639  275 CPVIQGYGLTETCAGGTVQDPGDLETGRVGPPLPCCEIKLVDweeGGYSTDKPPPRGEILIRGPNVFKGYYKNPEKTKEA 354

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  809 FVEEGWpgsgrlYRSGDLVRWRADGCLEFLGRIDEQVKI-NGYRIELGEIRSALLEHPAVGEAAVLtdeADAAEPgadrR 887
Cdd:cd17639  355 FDGDGW------FHTGDIGEFHPDGTLKIIDRKKDLVKLqNGEYIALEKLESIYRSNPLVNNICVY---ADPDKS----Y 421


                 ....*
gi 15597498  888 IVAFV 892
Cdd:cd17639  422 PVAIV 426
MenH COG0596
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ...
 1873-2111 1.57e-11

2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold [Coenzyme transport and metabolism, General function prediction only]; 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440361 [Multi-domain]  Cd Length: 221  Bit Score: 66.18  E-value: 1.57e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1873 LWLQRSGSAQPRLrlIALPPAGGNAGTFRGWDARLPADVELLAIQYPGRQERQDEPFVTDVEAMLCAIDDALLPLLDRPF 1952
Cdd:COG0596   14 LHYREAGPDGPPV--VLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKPAGGYTLDDLADDLAALLDALGLERV 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1953 ALIGASLGGMLAYELAARleslHGLRARQLFVISsrapgpdleyprfhamgdaELLRTLREYDVLPlevlddpelrEISL 2032
Cdd:COG0596   92 VLVGHSMGGMVALELAAR----HPERVAGLVLVD-------------------EVLAALAEPLRRP----------GLAP 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 2033 ATLRADSRLAADYRYRPR-EPLAIPITAILGEQDPGVSRVAIDGWRRHASRYELETLAG-GHGLVVTAAEEVCAILRQRL 2110
Cdd:COG0596  139 EALAALLRALARTDLRERlARITVPTLVIWGEKDPIVPPALARRLAELLPNAELVVLPGaGHFPPLEQPEAFAAALRDFL 218


                 .
gi 15597498 2111 A 2111
Cdd:COG0596  219 A 219
PRK07798 PRK07798
acyl-CoA synthetase; Validated
 454-872 2.67e-11

acyl-CoA synthetase; Validated


Pssm-ID: 236100 [Multi-domain]  Cd Length: 533  Bit Score: 68.76  E-value: 2.67e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   454 FDLRAALQPQAPALLDAHGSLDFATLRARSEAVAEALLAAGVRPGQAVAVMtGRNR-EAIVALLGVMRAAAVYTPVN--- 529
Cdd:PRK07798    9 FEAVADAVPDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIY-ARNRiEYVEAMLGAFKARAVPVNVNyry 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   530 --------------------PEFpAARVERMR-EAGGI--VFALADaecaGRAREAFAGAcLDLSTLPLAGSGMSLPAPG 586
Cdd:PRK07798   88 vedelryllddsdavalvyeREF-APRVAEVLpRLPKLrtLVVVED----GSGNDLLPGA-VDYEDALAAGSPERDFGER 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   587 GRDAAYMIFTSGTSGQPKGVVVEH---------------ASALNLSQALARTVYAnvvGEGLRVTVNAPFSFDSSIKQIL 651
Cdd:PRK07798  162 SPDDLYLLYTGGTTGMPKGVMWRQedifrvllggrdfatGEPIEDEEELAKRAAA---GPGMRRFPAPPLMHGAGQWAAF 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   652 Q-LLSGHCLVLVPqEVRSDPQRMLGFLEERRIDVLDCTPSLF-RLLLQAgLDDAHPA-LPGRILV--GGERFdeaSWEVA 726
Cdd:PRK07798  239 AaLFSGQTVVLLP-DVRFDADEVWRTIEREKVNVITIVGDAMaRPLLDA-LEARGPYdLSSLFAIasGGALF---SPSVK 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   727 AGWRR----CQVFNLYGPTEATVNASlARVAEHARPTIG-RALANVDLHVVDGLGRRKTRGASGELWIGGAG-VARGYAG 800
Cdd:PRK07798  314 EALLEllpnVVLTDSIGSSETGFGGS-GTVAKGAVHTGGpRFTIGPRTVVLDEDGNPVEPGSGEIGWIARRGhIPLGYYK 392

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15597498   801 DAGEAAGRFVEEGwpgsGRLYR-SGDLVRWRADGCLEFLGRiDEQVkIN--GYRIELGEIRSALLEHPAVGEAAV 872
Cdd:PRK07798  393 DPEKTAETFPTID----GVRYAiPGDRARVEADGTITLLGR-GSVC-INtgGEKVFPEEVEEALKAHPDVADALV 461
PRK08276 PRK08276
long-chain-fatty-acid--CoA ligase; Validated
 473-872 2.76e-11

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 236215 [Multi-domain]  Cd Length: 502  Bit Score: 68.39  E-value: 2.76e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   473 SLDFATLRARSEAVAEALLAAGVRPGQAVAVMTGRNREAIVALLGVMRAAAVYTPVNPEFPAARVERM-REAGGIVFaLA 551
Cdd:PRK08276   11 VVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIvDDSGAKVL-IV 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   552 DAECAGRAREAFAGACLDLSTLPLAGSG----MSLPAPGGRDAAY----------MIFTSGTSGQPKGVVVE------HA 611
Cdd:PRK08276   90 SAALADTAAELAAELPAGVPLLLVVAGPvpgfRSYEEALAAQPDTpiadetagadMLYSSGTTGRPKGIKRPlpgldpDE 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   612 SALNLSQALARTVYAnvvGEGLRVTVNAPF------SFDSSIKQIlqllsGHCLVLVPqevRSDPQRMLGFLEERRIDVL 685
Cdd:PRK08276  170 APGMMLALLGFGMYG---GPDSVYLSPAPLyhtaplRFGMSALAL-----GGTVVVME---KFDAEEALALIERYRVTHS 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   686 DCTPSLFRLLLqaglddahpALPGRILvggERFDEASWEVAA---------------GWRRCQVFNLYGPTEA---TVnA 747
Cdd:PRK08276  239 QLVPTMFVRML---------KLPEEVR---ARYDVSSLRVAIhaaapcpvevkramiDWWGPIIHEYYASSEGggvTV-I 305

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   748 SLARVAEHaRPTIGRALANVdLHVVDGLGRRKTRGASGELWIGGAGVARGYAGDAGEAAGRFVEEGWpgsgrlYRSGDLV 827
Cdd:PRK08276  306 TSEDWLAH-PGSVGKAVLGE-VRILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAARNPHGW------VTVGDVG 377

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*
gi 15597498   828 RWRADGCLEFLGRIDEQVKINGYRIELGEIRSALLEHPAVGEAAV 872
Cdd:PRK08276  378 YLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAV 422
PRK13295 PRK13295
cyclohexanecarboxylate-CoA ligase; Reviewed
 454-872 2.76e-11

cyclohexanecarboxylate-CoA ligase; Reviewed


Pssm-ID: 171961 [Multi-domain]  Cd Length: 547  Bit Score: 68.54  E-value: 2.76e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   454 FDLRAALQPQAPALLDA---HGS---LDFATLRARSEAVAEALLAAGVRPGQAVAVMTGRNREAIVALLGVMRAAAVYTP 527
Cdd:PRK13295   30 LDACVASCPDKTAVTAVrlgTGAprrFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNP 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   528 VNPEFpaarveRMREAGgivFALADAEC--------------AGRARE-----------AFAGACLDLS----------- 571
Cdd:PRK13295  110 LMPIF------RERELS---FMLKHAESkvlvvpktfrgfdhAAMARRlrpelpalrhvVVVGGDGADSfeallitpawe 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   572 TLPLAGSGMSLPAPGGRDAAYMIFTSGTSGQPKGVVveHAsalnlsqalARTVYANVV--------GEGLRVTVNAPFSF 643
Cdd:PRK13295  181 QEPDAPAILARLRPGPDDVTQLIYTSGTTGEPKGVM--HT---------ANTLMANIVpyaerlglGADDVILMASPMAH 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   644 DSS--IKQILQLLSGHCLVLvpQEVRsDPQRMLGFLEERRID-VLDCTPSLFRLLlQAGLDDAHPALPGRI-LVGGERFD 719
Cdd:PRK13295  250 QTGfmYGLMMPVMLGATAVL--QDIW-DPARAAELIRTEGVTfTMASTPFLTDLT-RAVKESGRPVSSLRTfLCAGAPIP 325

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   720 EASWEVAAGWRRCQVFNLYGPTE--ATVNASLARVAEHARPTIGRALANVDLHVVDGLGRRKTRGASGELWIGGAGVARG 797
Cdd:PRK13295  326 GALVERARAALGAKIVSAWGMTEngAVTLTKLDDPDERASTTDGCPLPGVEVRVVDADGAPLPAGQIGRLQVRGCSNFGG 405

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   798 YAG-------DAgeaagrfveEGWpgsgrlYRSGDLVRWRADGCLEFLGRIDEQVKINGYRIELGEIRSALLEHPAVGEA 870
Cdd:PRK13295  406 YLKrpqlngtDA---------DGW------FDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQV 470


                  ..
gi 15597498   871 AV 872
Cdd:PRK13295  471 AI 472
PRK06087 PRK06087
medium-chain fatty-acid--CoA ligase;
457-906 3.92e-11

medium-chain fatty-acid--CoA ligase;


Pssm-ID: 180393 [Multi-domain]  Cd Length: 547  Bit Score: 68.24  E-value: 3.92e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   457 RAALQPQAPALLDAHG-SLDFATLRARSEAVAEALLAAGVRPGQAVAVMTGRNREAIVALLGVMRAAAVYTPVNPEFPAA 535
Cdd:PRK06087   32 TARAMPDKIAVVDNHGaSYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREA 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   536 R-VERMREAGGIVF--------------ALADAE-------CAGRAREAFAGACLDLSTLPLAGSGMSLPAP-GGRDAAY 592
Cdd:PRK06087  112 ElVWVLNKCQAKMFfaptlfkqtrpvdlILPLQNqlpqlqqIVGVDKLAPATSSLSLSQIIADYEPLTTAITtHGDELAA 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   593 MIFTSGTSGQPKGVVVEHASALNLSQALARtvyanvvgeGLRVTVNAPFSFDSSIKQ--------ILQLLSGHCLVLvpq 664
Cdd:PRK06087  192 VLFTSGTEGLPKGVMLTHNNILASERAYCA---------RLNLTWQDVFMMPAPLGHatgflhgvTAPFLIGARSVL--- 259

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   665 EVRSDPQRMLGFLEERRID-VLDCTPSLFRLLLQagLDDAHPALPGR--ILVGG----ERFDEASWEvaAGWRRCQVfnl 737
Cdd:PRK06087  260 LDIFTPDACLALLEQQRCTcMLGATPFIYDLLNL--LEKQPADLSALrfFLCGGttipKKVARECQQ--RGIKLLSV--- 332

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   738 YGPTEATVNA--SLARVAEHARPTIGRALANVDLHVVDGlgRRKT--RGASGELWIGGAGVARGYAGDAGEAAGRFVEEG 813
Cdd:PRK06087  333 YGSTESSPHAvvNLDDPLSRFMHTDGYAAAGVEIKVVDE--ARKTlpPGCEGEEASRGPNVFMGYLDEPELTARALDEEG 410

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   814 WPGSgrlyrsGDLVRWRADGCLEFLGRIDEQVKINGYRIELGEIRSALLEHPAVGEAAVLtdeadaAEPGaDR---RIVA 890
Cdd:PRK06087  411 WYYS------GDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVV------AMPD-ERlgeRSCA 477

                         490
                  ....*....|....*.
gi 15597498   891 FVTAAEETADESWLEV 906
Cdd:PRK06087  478 YVVLKAPHHSLTLEEV 493
PRK12492 PRK12492
long-chain-fatty-acid--CoA ligase; Provisional
 576-873 4.07e-11

long-chain-fatty-acid--CoA ligase; Provisional


Pssm-ID: 171539 [Multi-domain]  Cd Length: 562  Bit Score: 67.92  E-value: 4.07e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   576 AGSGMSLPAPGGRDAAYMIFTSGTSGQPKGVVVEHASAL-NLSQALA-----RTVYANVVGEGLRVTVnAP------FSF 643
Cdd:PRK12492  195 RGLSLKPVPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVaNMLQVRAclsqlGPDGQPLMKEGQEVMI-APlplyhiYAF 273

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   644 DSSIkqILQLLSGHCLVLVpqevrSDPQRMLGFLEER---RIDVLDCTPSLFRLLLQ----AGLDDAHPALPGRilvGGE 716
Cdd:PRK12492  274 TANC--MCMMVSGNHNVLI-----TNPRDIPGFIKELgkwRFSALLGLNTLFVALMDhpgfKDLDFSALKLTNS---GGT 343

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   717 RFDEASWEVAAGWRRCQVFNLYGPTEATVNASLARVAEHAR-PTIGRALANVDLHVVDGLGRRKTRGASGELWIGGAGVA 795
Cdd:PRK12492  344 ALVKATAERWEQLTGCTIVEGYGLTETSPVASTNPYGELARlGTVGIPVPGTALKVIDDDGNELPLGERGELCIKGPQVM 423

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15597498   796 RGYAGDAGEAAGRFVEEGWpgsgrlYRSGDLVRWRADGCLEFLGRIDEQVKINGYRIELGEIRSALLEHPAVGEAAVL 873
Cdd:PRK12492  424 KGYWQQPEATAEALDAEGW------FKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAI 495
entE PRK10946
(2,3-dihydroxybenzoyl)adenylate synthase;
461-871 4.65e-11

(2,3-dihydroxybenzoyl)adenylate synthase;


Pssm-ID: 236803 [Multi-domain]  Cd Length: 536  Bit Score: 67.71  E-value: 4.65e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   461 QPQAPALLDAHGSLDFATLRARSEAVAEALLAAGVRPGQAVAVMTGRNREAIVALLGVMRAAAVytPVNPEFPAARVERM 540
Cdd:PRK10946   36 ASDAIAVICGERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLGVA--PVNALFSHQRSELN 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   541 REAGGIVFAL--ADAECAGRAREAFA------------------GACLDLSTLPLAGSGMSLPAPGGRD-AAYMIFTSGT 599
Cdd:PRK10946  114 AYASQIEPALliADRQHALFSDDDFLntlvaehsslrvvlllndDGEHSLDDAINHPAEDFTATPSPADeVAFFQLSGGS 193

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   600 SGQPKGVVVEH--------ASAlNLSQALARTVYANvvgeGLRVTVNAPFSfdsSIKQILQLLSGHCLVLVPqevrsDPQ 671
Cdd:PRK10946  194 TGTPKLIPRTHndyyysvrRSV-EICGFTPQTRYLC----ALPAAHNYPMS---SPGALGVFLAGGTVVLAP-----DPS 260

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   672 RMLGF--LEERRIDVLDCTPSLFRLLLQAGLDDAHPALPGR---ILVGGERFDEAsweVAagwRR------CQVFNLYGP 740
Cdd:PRK10946  261 ATLCFplIEKHQVNVTALVPPAVSLWLQAIAEGGSRAQLASlklLQVGGARLSET---LA---RRipaelgCQLQQVFGM 334

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   741 TEATVNAS-LARVAEHARPTIGRALANVD-LHVVDGLGRRKTRGASGELWIGGAGVARGYAGDAGEAAGRFVEEGWpgsg 818
Cdd:PRK10946  335 AEGLVNYTrLDDSDERIFTTQGRPMSPDDeVWVADADGNPLPQGEVGRLMTRGPYTFRGYYKSPQHNASAFDANGF---- 410

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 15597498   819 rlYRSGDLVRWRADGCLEFLGRIDEQVKINGYRIELGEIRSALLEHPAVGEAA 871
Cdd:PRK10946  411 --YCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAA 461
PRK05857 PRK05857
fatty acid--CoA ligase;
457-902 7.11e-11

fatty acid--CoA ligase;


Pssm-ID: 180293 [Multi-domain]  Cd Length: 540  Bit Score: 67.34  E-value: 7.11e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   457 RAALQPQAPAL--LDAHGSLDFATLRARSEAVAEALLAAGVRPGQAVAVMTGRNREAIVALLGVMRAAAVYTPVNPEFPA 534
Cdd:PRK05857   23 QARQQPEAIALrrCDGTSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLPI 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   535 ARVERMREAGGIVFALADAECAGRAREAFAGACLDLSTLPLAGSGMSL-------------PAPGGRDAAYMIFTSGTSG 601
Cdd:PRK05857  103 AAIERFCQITDPAAALVAPGSKMASSAVPEALHSIPVIAVDIAAVTREsehsldaaslagnADQGSEDPLAMIFTSGTTG 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   602 QPKGVVVEHASALNLSQALARTVYA---NVVGEglrvTVNAPFSFD--SSIKQILQLL--SGHCL-----------VLVP 663
Cdd:PRK05857  183 EPKAVLLANRTFFAVPDILQKEGLNwvtWVVGE----TTYSPLPAThiGGLWWILTCLmhGGLCVtggenttslleILTT 258

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   664 QEVRSD---PQRMLGFLEERRIDVLDcTPSLfRLLLQAGlddahpalpGRILVGGERFDEaswevAAGWRRCQVfnlYGP 740
Cdd:PRK05857  259 NAVATTclvPTLLSKLVSELKSANAT-VPSL-RLVGYGG---------SRAIAADVRFIE-----ATGVRTAQV---YGL 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   741 TEA--------TVNASLARVAEHArptIGRALANVDLHVV--DGLGRRKTRGAS----GELWIGGAGVARGYAGDAgEAA 806
Cdd:PRK05857  320 SETgctalclpTDDGSIVKIEAGA---VGRPYPGVDVYLAatDGIGPTAPGAGPsasfGTLWIKSPANMLGYWNNP-ERT 395

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   807 GRFVEEGWpgsgrlYRSGDLVRWRADGCLEFLGRIDEQVKINGYRIELGEIRSALLEHPAVGEAAVLtdEADAAEPGAdr 886
Cdd:PRK05857  396 AEVLIDGW------VNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACY--EIPDEEFGA-- 465

                         490
                  ....*....|....*.
gi 15597498   887 rIVAFVTAAEETADES 902
Cdd:PRK05857  466 -LVGLAVVASAELDES 480
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
1793-1971 1.37e-10

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 66.99  E-value: 1.37e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1793 RVLKVLSRVLGR-PLAADQGFASAGGHSLLGVQAIAELRRLTGRQLSLGLLQGDPDAREVVRRCHAADAPPLPPATERAR 1871
Cdd:PRK10252  982 IIAAAFSSLLGCdVVDADADFFALGGHSLLAMKLAAQLSRQFARQVTPGQVMVASTVAKLATLLDAEEDESRRLGFGTIL 1061

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1872 ALwlqRSGSAQPrlrLIALPPAGGNAGTFRGWDARLPADVELLAIQYPGRQERQDEPfvTDVEAMlcaIDDALLPLLDR- 1950
Cdd:PRK10252 1062 PL---REGDGPT---LFCFHPASGFAWQFSVLSRYLDPQWSIYGIQSPRPDGPMQTA--TSLDEV---CEAHLATLLEQq 1130

                         170       180
                  ....*....|....*....|....
gi 15597498  1951 ---PFALIGASLGGMLAYELAARL 1971
Cdd:PRK10252 1131 phgPYHLLGYSLGGTLAQGIAARL 1154
PRK07786 PRK07786
long-chain-fatty-acid--CoA ligase; Validated
 458-873 1.44e-10

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 169098 [Multi-domain]  Cd Length: 542  Bit Score: 66.34  E-value: 1.44e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   458 AALQPQAPALLDAHGSLDFATLRARSEAVAEALLAAGVRPGQAVAVMTGRNREAIVALLGVMRAAAVYTPVNPEFPAARV 537
Cdd:PRK07786   27 ALMQPDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEI 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   538 E---RMREAGGIVFALADAECAGRARE-------------AFAGACLDLSTLPLAGSGMSLPAPGGRDAAYMI-FTSGTS 600
Cdd:PRK07786  107 AflvSDCGAHVVVTEAALAPVATAVRDivpllstvvvaggSSDDSVLGYEDLLAEAGPAHAPVDIPNDSPALImYTSGTT 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   601 GQPKGVVVEHAsalNLSQALARTVYANVVGEGLRVT-VNAPFSFDSSIKQILQ-LLSGHCLVLVPQEVrSDPQRMLGFLE 678
Cdd:PRK07786  187 GRPKGAVLTHA---NLTGQAMTCLRTNGADINSDVGfVGVPLFHIAGIGSMLPgLLLGAPTVIYPLGA-FDPGQLLDVLE 262

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   679 ERRIDVLDCTPSLFrlllQAGLDDAHP---ALPGRILVGGE--RFDEASWEVAAGWRRCQVFNLYGPTEAT-VNASL-AR 751
Cdd:PRK07786  263 AEKVTGIFLVPAQW----QAVCAEQQArprDLALRVLSWGAapASDTLLRQMAATFPEAQILAAFGQTEMSpVTCMLlGE 338

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   752 VAEHARPTIGRALANVDLHVVDGLGRRKTRGASGELWIGGAGVARGYAGDAGEAAGRFvEEGWpgsgrlYRSGDLVRWRA 831
Cdd:PRK07786  339 DAIRKLGSVGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAF-AGGW------FHSGDLVRQDE 411

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 15597498   832 DGCLEFLGRIDEQVKINGYRIELGEIRSALLEHPAVGEAAVL 873
Cdd:PRK07786  412 EGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVI 453
FACL_like_4 cd05944
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 586-873 2.04e-10

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: 64.81  E-value: 2.04e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  586 GGRDAAYMiFTSGTSGQPKGVVVEHASALNLSQALARTVyanVVGEGLRVTVNAP-FSFDSSIKQILQLLS--GHCLVLV 662
Cdd:cd05944    1 SDDVAAYF-HTGGTTGTPKLAQHTHSNEVYNAWMLALNS---LFDPDDVLLCGLPlFHVNGSVVTLLTPLAsgAHVVLAG 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  663 PQEVRsDP---QRMLGFLEERRIDVLDCTPSLFRLLLQ----AGLDDAHPALPGRILVGGERFdeASWEVAAGWRRCQVf 735
Cdd:cd05944   77 PAGYR-NPglfDNFWKLVERYRITSLSTVPTVYAALLQvpvnADISSLRFAMSGAAPLPVELR--ARFEDATGLPVVEG- 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  736 nlYGPTEATVNASLARVAEHARP-TIGRAL--ANVDLHVVDGLGRRKTRGAS---GELWIGGAGVARGYAGDAGeAAGRF 809
Cdd:cd05944  153 --YGLTEATCLVAVNPPDGPKRPgSVGLRLpyARVRIKVLDGVGRLLRDCAPdevGEICVAGPGVFGGYLYTEG-NKNAF 229

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15597498  810 VEEGWpgsgrlYRSGDLVRWRADGCLEFLGRIDEQVKINGYRIELGEIRSALLEHPAVGEAAVL 873
Cdd:cd05944  230 VADGW------LNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAV 287
C_NRPS-like cd19537
Condensation family domain with an atypical active site motif; Condensation (C) domains of ...
 1385-1678 2.19e-10

Condensation family domain with an atypical active site motif; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily typically have a non-canonical conserved SHXXXDX(14)Y motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.


Pssm-ID: 380460 [Multi-domain]  Cd Length: 395  Bit Score: 64.90  E-value: 2.19e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1385 NV-VLHEVHGRLDGELLARAWAILIGRHAILRTGFDLHGGQvplqwvhPATAVAAEVP-VHDLCGLDgetrrlrlrawIE 1462
Cdd:cd19537   25 NVsFACRLSGDVDRDRLASAWNTVLARHRILRSRYVPRDGG-------LRRSYSSSPPrVQRVDTLD-----------VW 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1463 EEQATPFDWSRPPLVRlaalALDERRFALGVAeHHSVLDGWSLQSLVDELLAVYA-DLLAGVVAREAEAPavgfrdyvAL 1541
Cdd:cd19537   87 KEINRPFDLEREDPIR----VFISPDTLLVVM-SHIICDLTTLQLLLREVSAAYNgKLLPPVRREYLDST--------AW 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1542 EREAEANAASalFWLDYLAGARYRPLPGLAEEGPRRMAAVRVDVPADSLSRLRALAERSGLPLRSLLLAAHGRALCRFSD 1621
Cdd:cd19537  154 SRPASPEDLD--FWSEYLSGLPLLNLPRRTSSKSYRGTSRVFQLPGSLYRSLLQFSTSSGITLHQLALAAVALALQDLSD 231

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15597498 1622 ADEVVTGFVSHGRPEEpGADRLLGLFLNTLPCRL-------SASVDLLDSARRAFdyeRASLEH 1678
Cdd:cd19537  232 RTDIVLGAPYLNRTSE-EDMETVGLFLEPLPIRIrfpsssdASAADFLRAVRRSS---QAALAH 291
PRK08751 PRK08751
long-chain fatty acid--CoA ligase;
589-871 3.14e-10

long-chain fatty acid--CoA ligase;


Pssm-ID: 181546 [Multi-domain]  Cd Length: 560  Bit Score: 65.28  E-value: 3.14e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   589 DAAYMIFTSGTSGQPKGVVVEHASAL-NLSQALARTVYANVVGEGLRVTVNA-PFS--FDSSIKQILQLLSGHCLVLVpq 664
Cdd:PRK08751  209 DIAFLQYTGGTTGVAKGAMLTHRNLVaNMQQAHQWLAGTGKLEEGCEVVITAlPLYhiFALTANGLVFMKIGGCNHLI-- 286

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   665 evrSDPQRMLGFLEE---RRIDVLDCTPSLFRLLLQA-GLDDAHPALPGRILVGGERFDEAsweVAAGWRRCQVFNL--- 737
Cdd:PRK08751  287 ---SNPRDMPGFVKElkkTRFTAFTGVNTLFNGLLNTpGFDQIDFSSLKMTLGGGMAVQRS---VAERWKQVTGLTLvea 360

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   738 YGPTEATVNASL--ARVAEHaRPTIGRALANVDLHVVDGLGRRKTRGASGELWIGGAGVARGYAGDAGEAAGRFVEEGWP 815
Cdd:PRK08751  361 YGLTETSPAACInpLTLKEY-NGSIGLPIPSTDACIKDDAGTVLAIGEIGELCIKGPQVMKGYWKRPEETAKVMDADGWL 439

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 15597498   816 GSgrlyrsGDLVRWRADGCLEFLGRIDEQVKINGYRIELGEIRSALLEHPAVGEAA 871
Cdd:PRK08751  440 HT------GDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVA 489
A_NRPS cd05930
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ...
 1192-1234 3.76e-10

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: 64.47  E-value: 3.76e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 15597498 1192 GGELSEQALRGFLEARLPAYMLPSRIARVERLPLTAEGKLDRR 1234
Cdd:cd05930  400 GGELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRK 442
PRK08974 PRK08974
long-chain-fatty-acid--CoA ligase FadD;
587-873 1.05e-09

long-chain-fatty-acid--CoA ligase FadD;


Pssm-ID: 236359 [Multi-domain]  Cd Length: 560  Bit Score: 63.53  E-value: 1.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   587 GRDAAYMIFTSGTSGQPKGVVVEHASAL-NLSQALArtVYANVVGEGLRVTVNApfsfdssikqiLQL-----LSGHCLV 660
Cdd:PRK08974  205 PEDLAFLQYTGGTTGVAKGAMLTHRNMLaNLEQAKA--AYGPLLHPGKELVVTA-----------LPLyhifaLTVNCLL 271

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   661 LVPQEVRS----DPQRMLGFLEE---RRIDVLDCTPSLFRLLLQ----AGLDDAHPalpgRILVGG----ERFDEASWEV 725
Cdd:PRK08974  272 FIELGGQNllitNPRDIPGFVKElkkYPFTAITGVNTLFNALLNneefQELDFSSL----KLSVGGgmavQQAVAERWVK 347

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   726 AAGwrrCQVFNLYGPTEAT--VNASLARVAEHArPTIGRALANVDLHVVDGLGRRKTRGASGELWIGGAGVARGYAGDAg 803
Cdd:PRK08974  348 LTG---QYLLEGYGLTECSplVSVNPYDLDYYS-GSIGLPVPSTEIKLVDDDGNEVPPGEPGELWVKGPQVMLGYWQRP- 422

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   804 EAAGRFVEEGWpgsgrlYRSGDLVRWRADGCLEFLGRIDEQVKINGYRIELGEIRSALLEHPAVGEAAVL 873
Cdd:PRK08974  423 EATDEVIKDGW------LATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAV 486
ttLC_FACS_AEE21_like cd12118
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ...
 458-872 1.06e-09

Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.


Pssm-ID: 341283 [Multi-domain]  Cd Length: 486  Bit Score: 63.47  E-value: 1.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  458 AALQPQAPALLDAHGSLDFATLRARSEAVAEALLAAGVRPGQAVAVMtGRNREAIVAL-LGVMRAAAVYTPVNPEFPAAR 536
Cdd:cd12118   14 AAVYPDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVL-APNTPAMYELhFGVPMAGAVLNALNTRLDAEE 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  537 VERMREAGGIVFALADAEcagrareaFAGACLDLSTLPLAGSgmsLPAPGGRDAAYMIFTSGTSGQPKGVVVEHASA-LN 615
Cdd:cd12118   93 IAFILRHSEAKVLFVDRE--------FEYEDLLAEGDPDFEW---IPPADEWDPIALNYTSGTTGRPKGVVYHHRGAyLN 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  616 -LSQALA-----RTVY--------AN-------VVGEG-----LRvTVNAPfsfdssikQILQLLSGHclvlvpqevrsd 669
Cdd:cd12118  162 aLANILEwemkqHPVYlwtlpmfhCNgwcfpwtVAAVGgtnvcLR-KVDAK--------AIYDLIEKH------------ 220

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  670 pqrmlgfleerRIDVLDCTPSLFRLLLQAGLDDAHPaLPGRI--LVGGERFDEASWEVAA--GWRRCQVFNL---YGPte 742
Cdd:cd12118  221 -----------KVTHFCGAPTVLNMLANAPPSDARP-LPHRVhvMTAGAPPPAAVLAKMEelGFDVTHVYGLtetYGP-- 286

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  743 ATVNASLArvAEHARPTIGRALAN----VDLHVVDGLGRRKTRGAS---------GELWIGGAGVARGYAGDAgEAAGRF 809
Cdd:cd12118  287 ATVCAWKP--EWDELPTEERARLKarqgVRYVGLEEVDVLDPETMKpvprdgktiGEIVFRGNIVMKGYLKNP-EATAEA 363

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15597498  810 VEEGWpgsgrlYRSGDLVRWRADGCLEFLGRIDEQVKINGYRIELGEIRSALLEHPAVGEAAV 872
Cdd:cd12118  364 FRGGW------FHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAV 420
AFD_YhfT-like cd17633
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ...
 592-873 1.22e-09

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: 62.04  E-value: 1.22e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  592 YMIFTSGTSGQPKGVVVEHASALNlSQALARTVYaNVVGEGlRVTVNAPFSFDSSIKQILQLL-SGHCLVLVPQevrSDP 670
Cdd:cd17633    4 YIGFTSGTTGLPKAYYRSERSWIE-SFVCNEDLF-NISGED-AILAPGPLSHSLFLYGAISALyLGGTFIGQRK---FNP 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  671 QRMLGFLEERRIDVLDCTPSLFRLLLQAGLDDAHPALpgrILVGGERFDEASWE-VAAGWRRCQVFNLYGPTEATVNASL 749
Cdd:cd17633   78 KSWIRKINQYNATVIYLVPTMLQALARTLEPESKIKS---IFSSGQKLFESTKKkLKNIFPKANLIEFYGTSELSFITYN 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  750 ARVAEHARPTIGRALANVDLHVVDGLGrrktrGASGELWIGGAGVARGYAgdageAAGRFVEEGWpgsgrlYRSGDLVRW 829
Cdd:cd17633  155 FNQESRPPNSVGRPFPNVEIEIRNADG-----GEIGKIFVKSEMVFSGYV-----RGGFSNPDGW------MSVGDIGYV 218

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 15597498  830 RADGCLEFLGRIDEQVKINGYRIELGEIRSALLEHPAVGEAAVL 873
Cdd:cd17633  219 DEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVV 262
EntF2 COG3319
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase ...
 1288-2002 1.43e-09

Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442548 [Multi-domain]  Cd Length: 855  Bit Score: 63.57  E-value: 1.43e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1288 RLIQMQVMAREAGLAFTLRDVFNHQSIRELARLLAAPASPADALGTSAPQSLEPFALLSAAERKRLPEGLDDAYPMTSLQ 1367
Cdd:COG3319   12 AAAAAAAAAAAAAAALAAAAAAAAAAALLLLAAALLVALAALALAALALAALLAVALLAAALALAALAALAALALALAAA 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1368 QGMLLQSEASGDPRLLHNVVLHEVHGRLDGELLARAWAILIGRHAILRTGFDLHGGQVPLQWVHPATAVAAEVPVHDLCG 1447
Cdd:COG3319   92 AAALLLAALALLLALLAALALALLALLLAALLLALAALAAAAAAAALAAAAAAAAALAAAAGLGGGGGGAGVLVLVLAAL 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1448 LDGETRRLRLRAWIEEEQATPFDWSRPPLVRLAALALDERRFALGVAEHHSVLDGWSLQSLVDELLAVYADLLAGVVARE 1527
Cdd:COG3319  172 LALLLAALLALALALAALLLLALAAALALALLLLLALLLLLLLLLALLLLLLLALLAAAALLALLLALLLLLLAALLLLL 251

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1528 AEAPAVGFRDYVALEREAEANAASALFWLDYLAGARYRPLPGLAEEGPRRMAAVRVDVPADSLSRLRALAERSGLPLRSL 1607
Cdd:COG3319  252 ALALLLLLALLLLLGLLALLLALLLLLALLLLAAAAALAAGGTATTAAVTTTAAAAAPGVAGALGPIGGGPGLLVLLVLL 331

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1608 LLAAHGRALCRFSDADEVVTGFVSHGRPEEPGADRLLGLFLNTLPCRLSASVDLLDSARRAFDYERASLEHRRHPLAAIR 1687
Cdd:COG3319  332 VLLLPLLLGVGGGGGGGGGGGGAGGLAGRGLRAAAALRDPAGAGARGRLRRGGDRGRRLGGGLLLGLGRLRLQRLRRGLR 411

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1688 RRNRELRLDSLFNFVDFHQDDAAPAGVRHGGILDQVVVDVDVPLAVDFEVAGERLEVGFQYAAGRFPAERAEALAGAYRE 1767
Cdd:COG3319  412 EELEEAEAALAEAAAVAAAVAAAAAAAAAAAALAAAVVAAAALAAAALLLLLLLLLLPPPLPPALLLLLLLLLLLLLAAL 491

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1768 ALLALLGDPVQPPAAAQAEDSVELRRVLKVLSRVLGRPLAADQGFASAGGHSLLGVQAIAELRRLTGRQLSLGLLQGDPD 1847
Cdd:COG3319  492 LLAAAAPAAAAAAAAAPAPAAALELALALLLLLLLGLGLVGDDDDFFGGGGGSLLALLLLLLLLALLLRLLLLLALLLAP 571

                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1848 AREVVRRchaaDAPPLPPATERARALWLQRSGSAQPrlrLIALPPAGGNAGTFRGWDARLPADVELLAIQYPGRQERQDE 1927
Cdd:COG3319  572 TLAALAA----ALAAAAAAAALSPLVPLRAGGSGPP---LFCVHPAGGNVLCYRPLARALGPDRPVYGLQAPGLDGGEPP 644

                        650       660       670       680       690       700       710
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15597498 1928 PfvTDVEAMLCAIDDALLPLL-DRPFALIGASLGGMLAYELAARLESLhGLRARQLFVISSRAPGPDLEYPRFHAM 2002
Cdd:COG3319  645 P--ASVEEMAARYVEAIRAVQpEGPYHLLGWSFGGLVAYEMARQLEAQ-GEEVALLVLLDSYAPGALARLDEAELL 717
PRK00174 PRK00174
acetyl-CoA synthetase; Provisional
 761-901 1.59e-09

acetyl-CoA synthetase; Provisional


Pssm-ID: 234677 [Multi-domain]  Cd Length: 637  Bit Score: 63.24  E-value: 1.59e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   761 GRALANVDLHVVDGLGRRKTRGASGEL-----WiggAGVARGYAGDAGeaagRFVEEGWPGSGRLYRSGDLVRWRADGCL 835
Cdd:PRK00174  427 TRPLPGIQPAVVDEEGNPLEGGEGGNLvikdpW---PGMMRTIYGDHE----RFVKTYFSTFKGMYFTGDGARRDEDGYY 499

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15597498   836 EFLGRIDEQVKINGYRIELGEIRSALLEHPAVGEAAV------LTDEAdaaepgadrrIVAFVT--AAEETADE 901
Cdd:PRK00174  500 WITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVvgrpddIKGQG----------IYAFVTlkGGEEPSDE 563
alpha_am_amid TIGR03443
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ...
 1200-1362 1.67e-09

L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.


Pssm-ID: 274582 [Multi-domain]  Cd Length: 1389  Bit Score: 63.55  E-value: 1.67e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   1200 LRGFLEARLPAYMLPSRIARVERLPLTAEGKLDR-------RALLAALAAEAAAQTLEAPANATEAALLEIWKSVL-KRP 1271
Cdd:TIGR03443  786 IREYLKKKLPSYAIPTVIVPLKKLPLNPNGKVDKpalpfpdTAQLAAVAKNRSASAADEEFTETEREIRDLWLELLpNRP 865

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   1272 A-IGVSDNFFQVGGDSIRLIQMqvmareaglAFTLRD----------VFNHQSIRELAR---LLAAPASPADALGTSAPQ 1337
Cdd:TIGR03443  866 AtISPDDSFFDLGGHSILATRM---------IFELRKklnvelplglIFKSPTIKGFAKevdRLKKGEELADEGDSEIEE 936

                          170       180
                   ....*....|....*....|....*
gi 15597498   1338 SLEPFALLSAAERKRLPEGLDDAYP 1362
Cdd:TIGR03443  937 EETVLELDYAKDAKTLVDSLPKSYP 961
PRK13391 PRK13391
acyl-CoA synthetase; Provisional
 455-892 2.00e-09

acyl-CoA synthetase; Provisional


Pssm-ID: 184022 [Multi-domain]  Cd Length: 511  Bit Score: 62.40  E-value: 2.00e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   455 DLRAALQPQAPALLDAHG--SLDFATLRARSEAVAEALLAAGVRPGQAVAVMTGRNREAIVALLGVMRAAAVYTPVN--- 529
Cdd:PRK13391    4 GIHAQTTPDKPAVIMASTgeVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNshl 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   530 --PEfpAARVERMREAGGIVFALADAECAGRAREAFAG--ACLDL---STLP----LAGSGMSLPAPGGRD---AAYMIF 595
Cdd:PRK13391   84 tpAE--AAYIVDDSGARALITSAAKLDVARALLKQCPGvrHRLVLdgdGELEgfvgYAEAVAGLPATPIADeslGTDMLY 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   596 TSGTSGQPKGVVVEHASaLNLSQALART-VYANVVG--EGLRVTVNAPF--SFDSSIKQILQLLSGHCLVLvpqeVRSDP 670
Cdd:PRK13391  162 SSGTTGRPKGIKRPLPE-QPPDTPLPLTaFLQRLWGfrSDMVYLSPAPLyhSAPQRAVMLVIRLGGTVIVM----EHFDA 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   671 QRMLGFLEERRIDVLDCTPSLFRLLLQaglddahpaLPGRILvggERFDEASWEVAA---------------GWRRCQVF 735
Cdd:PRK13391  237 EQYLALIEEYGVTHTQLVPTMFSRMLK---------LPEEVR---DKYDLSSLEVAIhaaapcppqvkeqmiDWWGPIIH 304

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   736 NLYGPTEAtVNASLARVAEH-ARP-TIGRALANvDLHVVDGLGRRKTRGASGELWIGGAGVARGYAGDAGEAAGRFVEEG 813
Cdd:PRK13391  305 EYYAATEG-LGFTACDSEEWlAHPgTVGRAMFG-DLHILDDDGAELPPGEPGTIWFEGGRPFEYLNDPAKTAEARHPDGT 382

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   814 WPgsgrlyRSGDLVRWRADGCLEFLGRIDEQVKINGYRIELGEIRSALLEHPAVGEAAV--LTDE------------ADA 879
Cdd:PRK13391  383 WS------TVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVfgVPNEdlgeevkavvqpVDG 456

                         490
                  ....*....|....*
gi 15597498   880 AEPGAD--RRIVAFV 892
Cdd:PRK13391  457 VDPGPAlaAELIAFC 471
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
 1258-1316 2.61e-09

Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.


Pssm-ID: 425746 [Multi-domain]  Cd Length: 62  Bit Score: 54.88  E-value: 2.61e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15597498   1258 AALLEIWKSVLKRPA--IGVSDNFFQVGGDSIRLIQMQVMAREA-GLAFTLRDVFNHQSIRE 1316
Cdd:pfam00550    1 ERLRELLAEVLGVPAeeIDPDTDLFDLGLDSLLAVELIARLEEEfGVEIPPSDLFEHPTLAE 62
PtmA cd17636
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ...
 738-873 3.50e-09

long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.


Pssm-ID: 341291 [Multi-domain]  Cd Length: 331  Bit Score: 60.78  E-value: 3.50e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  738 YGPTEATVNASLARVAEHARPTIGRALANVDLHVVDGLGRRKTRGASGELWIGGAGVARGYAGDAGEAAGRFVeEGWpgs 817
Cdd:cd17636  143 YGQTEVMGLATFAALGGGAIGGAGRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRTR-GGW--- 218

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 15597498  818 grlYRSGDLVRWRADGCLEFLGRIDEQVKINGYRIELGEIRSALLEHPAVGEAAVL 873
Cdd:cd17636  219 ---HHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVI 271
PRK06710 PRK06710
long-chain-fatty-acid--CoA ligase; Validated
 458-898 1.11e-08

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 180666 [Multi-domain]  Cd Length: 563  Bit Score: 60.05  E-value: 1.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   458 AALQPQAPALLDAHGSLDFATLRARSEAVAEALLAAGVRPGQAVAVMTGRNREAIVALLGVMRAAAVYTPVNPEFPAARV 537
Cdd:PRK06710   34 ASRYPEKKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTEREL 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   538 E-RMREAGG-------IVFA-LADAECAGRAREAFAGACLDLSTLPL--------------------------------- 575
Cdd:PRK06710  114 EyQLHDSGAkvilcldLVFPrVTNVQSATKIEHVIVTRIADFLPFPKnllypfvqkkqsnlvvkvsesetihlwnsveke 193

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   576 AGSGMSLPAPGGRDAAYMIFTSGTSGQPKGVVVEHASALNLSQALARTVYANVVGEGLRVTVnAPFSFDSSIKQILQL-- 653
Cdd:PRK06710  194 VNTGVEVPCDPENDLALLQYTGGTTGFPKGVMLTHKNLVSNTLMGVQWLYNCKEGEEVVLGV-LPFFHVYGMTAVMNLsi 272

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   654 LSGHCLVLVPqevRSDPQRMLGFLEERRIDVLDCTPSLFRLLLQAGLDDAHPALPGRILVGG---------ERFDeaswE 724
Cdd:PRK06710  273 MQGYKMVLIP---KFDMKMVFEAIKKHKVTLFPGAPTIYIALLNSPLLKEYDISSIRACISGsaplpvevqEKFE----T 345

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   725 VAAGwrrcQVFNLYGPTEATVNASLARVAEHARP-TIGRALANVDLHVVD-GLGRRKTRGASGELWIGGAGVARGYAGDA 802
Cdd:PRK06710  346 VTGG----KLVEGYGLTESSPVTHSNFLWEKRVPgSIGVPWPDTEAMIMSlETGEALPPGEIGEIVVKGPQIMKGYWNKP 421

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   803 GEAAGrFVEEGWpgsgrlYRSGDLVRWRADGCLEFLGRIDEQVKINGYRIELGEIRSALLEHPAVGEAAVLtdeaDAAEP 882
Cdd:PRK06710  422 EETAA-VLQDGW------LHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTI----GVPDP 490

                         490
                  ....*....|....*.
gi 15597498   883 GADRRIVAFVTAAEET 898
Cdd:PRK06710  491 YRGETVKAFVVLKEGT 506
A_NRPS_Srf_like cd12117
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ...
 1192-1234 1.25e-08

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: 59.91  E-value: 1.25e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 15597498 1192 GGELSEQALRGFLEARLPAYMLPSRIARVERLPLTAEGKLDRR 1234
Cdd:cd12117  439 EGALDAAELRAFLRERLPAYMVPAAFVVLDELPLTANGKVDRR 481
PRK06060 PRK06060
p-hydroxybenzoic acid--AMP ligase FadD22;
586-902 1.82e-08

p-hydroxybenzoic acid--AMP ligase FadD22;


Pssm-ID: 180374 [Multi-domain]  Cd Length: 705  Bit Score: 59.66  E-value: 1.82e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   586 GGRDAAYMIFTSGTSGQPKGVVVEHASALNLSQALARtvyanvvgEGLRVT--------VNAPFSFDSSIKQILQLLSGH 657
Cdd:PRK06060  143 GGDALAYATYTSGTTGPPKAAIHRHADPLTFVDAMCR--------KALRLTpedtglcsARMYFAYGLGNSVWFPLATGG 214

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   658 CLVLVPQEVRSDPQRMLGFLEERriDVLDCTPSLFRLLLQAGLDDAHPALpgRILV-GGErfdeaSWEVAAGWRRCQVFN 736
Cdd:PRK06060  215 SAVINSAPVTPEAAAILSARFGP--SVLYGVPNFFARVIDSCSPDSFRSL--RCVVsAGE-----ALELGLAERLMEFFG 285

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   737 ----LYGPTEATVNAS-LARVAEHARP-TIGRALANVDLHVVDGLGRRKTRGASGELWIGGAGVARGYagdAGEAAGRFV 810
Cdd:PRK06060  286 gipiLDGIGSTEVGQTfVSNRVDEWRLgTLGRVLPPYEIRVVAPDGTTAGPGVEGDLWVRGPAIAKGY---WNRPDSPVA 362

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   811 EEGWpgsgrlYRSGDLVRWRADGCLEFLGRIDEQVKINGYRIELGEIRSALLEHPAVGEAAVL-TDEADaaepGADRRIV 889
Cdd:PRK06060  363 NEGW------LDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVaVREST----GASTLQA 432

                         330
                  ....*....|...
gi 15597498   890 AFVTAAEETADES 902
Cdd:PRK06060  433 FLVATSGATIDGS 445
A_NRPS_ACVS-like cd17648
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ...
 1193-1234 3.05e-08

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: 58.57  E-value: 3.05e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 15597498 1193 GELSEQALRGFLEARLPAYMLPSRIARVERLPLTAEGKLDRR 1234
Cdd:cd17648  409 GHVPESDLLSFLRAKLPRYMVPARLVRLEGIPVTINGKLDVR 450
PRK06018 PRK06018
putative acyl-CoA synthetase; Provisional
 476-873 4.27e-08

putative acyl-CoA synthetase; Provisional


Pssm-ID: 235673 [Multi-domain]  Cd Length: 542  Bit Score: 58.22  E-value: 4.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   476 FATLRARSEAVAEALLAAGVRPGQAVAVM---TGRNREaivALLGVMRAAAVYTPVNPE-FPAARVERMREAGG------ 545
Cdd:PRK06018   42 YAQIHDRALKVSQALDRDGIKLGDRVATIawnTWRHLE---AWYGIMGIGAICHTVNPRlFPEQIAWIINHAEDrvvitd 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   546 -----IVFALADAECAGRAREAFAG-ACLDLSTLPLAGSGMSLPAPGGRD----------AAYMIFTSGTSGQPKGVVVE 609
Cdd:PRK06018  119 ltfvpILEKIADKLPSVERYVVLTDaAHMPQTTLKNAVAYEEWIAEADGDfawktfdentAAGMCYTSGTTGDPKGVLYS 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   610 HASalNLSQALArTVYANVVGEGLRVTV---------NA---PFSFDSSIKQilqllsghclvLVPQEVRSDPQRMLGFL 677
Cdd:PRK06018  199 HRS--NVLHALM-ANNGDALGTSAADTMlpvvplfhaNSwgiAFSAPSMGTK-----------LVMPGAKLDGASVYELL 264

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   678 EERRIDVLDCTPSLFRLLLQAgLDDAHPALP--GRILVGG--------ERFDEASWEVAAGWrrcqvfnlyGPTE----- 742
Cdd:PRK06018  265 DTEKVTFTAGVPTVWLMLLQY-MEKEGLKLPhlKMVVCGGsamprsmiKAFEDMGVEVRHAW---------GMTEmsplg 334

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   743 --ATVNASLARVAEHARPTI----GRALANVDLHVVDGLGRRKTRG--ASGELWIGGAGVARGYAGDAGEAagrFVEEGW 814
Cdd:PRK06018  335 tlAALKPPFSKLPGDARLDVlqkqGYPPFGVEMKITDDAGKELPWDgkTFGRLKVRGPAVAAAYYRVDGEI---LDDDGF 411

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 15597498   815 pgsgrlYRSGDLVRWRADGCLEFLGRIDEQVKINGYRIELGEIRSALLEHPAVGEAAVL 873
Cdd:PRK06018  412 ------FDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVI 464
PRK08279 PRK08279
long-chain-acyl-CoA synthetase; Validated
 438-627 5.06e-08

long-chain-acyl-CoA synthetase; Validated


Pssm-ID: 236217 [Multi-domain]  Cd Length: 600  Bit Score: 57.96  E-value: 5.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   438 QGERVEPAPVESLVAAFDLRAALQPQAPALLDAHGSLDFATLRARSEAVAEALLAAGVRPGQAVAVMTgRNR-EAIVALL 516
Cdd:PRK08279   27 RTALITPDSKRSLGDVFEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLM-ENRpEYLAAWL 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   517 GVMRAAAVYTPVN-----------------------PEFpAARVERMRE----AGGIVFALADAECAGRAREAFAGACLD 569
Cdd:PRK08279  106 GLAKLGAVVALLNtqqrgavlahslnlvdakhlivgEEL-VEAFEEARAdlarPPRLWVAGGDTLDDPEGYEDLAAAAAG 184

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 15597498   570 LSTLPLAGSGmslpAPGGRDAAYMIFTSGTSGQPKGVVVEHASALNLSQALARTVYAN 627
Cdd:PRK08279  185 APTTNPASRS----GVTAKDTAFYIYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLRLT 238
PRK07638 PRK07638
acyl-CoA synthetase; Validated
 592-873 5.07e-08

acyl-CoA synthetase; Validated


Pssm-ID: 236071 [Multi-domain]  Cd Length: 487  Bit Score: 57.87  E-value: 5.07e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   592 YMIFTSGTSGQPKGVVVEHASALNLSQALARTVYanvVGEGLRVTVnaPFSFDSSI---KQILQLLSGHCLVLVPQEVrs 668
Cdd:PRK07638  147 YMGFTSGSTGKPKAFLRAQQSWLHSFDCNVHDFH---MKREDSVLI--AGTLVHSLflyGAISTLYVGQTVHLMRKFI-- 219

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   669 dPQRMLGFLEERRIDVLDCTPSLFRLLLQAgldDAHPALPGRILVGGerfdeASWE------VAAGWRRCQVFNLYGPTE 742
Cdd:PRK07638  220 -PNQVLDKLETENISVMYTVPTMLESLYKE---NRVIENKMKIISSG-----AKWEaeakekIKNIFPYAKLYEFYGASE 290

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   743 ATVNASLARVAEHARPT-IGRALANVDLHVVDGLGRRKTRGASGELWIGGAGVARGYAGDaGEAAGRFVEEGWpgsgrlY 821
Cdd:PRK07638  291 LSFVTALVDEESERRPNsVGRPFHNVQVRICNEAGEEVQKGEIGTVYVKSPQFFMGYIIG-GVLARELNADGW------M 363

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 15597498   822 RSGDLVRWRADGCLEFLGRIDEQVKINGYRIELGEIRSALLEHPAVGEAAVL 873
Cdd:PRK07638  364 TVRDVGYEDEEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVI 415
PLN02246 PLN02246
4-coumarate--CoA ligase
 494-896 5.23e-08

4-coumarate--CoA ligase


Pssm-ID: 215137 [Multi-domain]  Cd Length: 537  Bit Score: 58.07  E-value: 5.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   494 GVRPGQAVAVMTGRNREAIVALLGVMRAAAVYTPVNPEFPAARVERMREAGGIVFALADAECAGRAREAFAG-------- 565
Cdd:PLN02246   71 GIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAKQAKASGAKLIITQSCYVDKLKGLAEDdgvtvvti 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   566 -----ACLDLSTLPLAGSGmSLPAP--GGRDAAYMIFTSGTSGQPKGVVVEHASalnlsqaLARTVYANVVGEglrvtvN 638
Cdd:PLN02246  151 ddppeGCLHFSELTQADEN-ELPEVeiSPDDVVALPYSSGTTGLPKGVMLTHKG-------LVTSVAQQVDGE------N 216

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   639 APFSFDS--------------SIKQIL--QLLSGHCLVLVPqevRSDPQRMLGFLEERRIDVLDCTP------------- 689
Cdd:PLN02246  217 PNLYFHSddvilcvlpmfhiySLNSVLlcGLRVGAAILIMP---KFEIGALLELIQRHKVTIAPFVPpivlaiakspvve 293

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   690 ----SLFRLLLQAG------LDDAHPA-LPGRILVGGerfdeaswevaagwrrcqvfnlYGPTEA-TVNA-SLArVAEHA 756
Cdd:PLN02246  294 kydlSSIRMVLSGAaplgkeLEDAFRAkLPNAVLGQG----------------------YGMTEAgPVLAmCLA-FAKEP 350

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   757 RPT----IGRALANVDLHVVD-GLGRRKTRGASGELWIGGAGVARGYAGDAgEAAGRFV-EEGWpgsgrlYRSGDLVRWR 830
Cdd:PLN02246  351 FPVksgsCGTVVRNAELKIVDpETGASLPRNQPGEICIRGPQIMKGYLNDP-EATANTIdKDGW------LHTGDIGYID 423

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15597498   831 ADGCLEFLGRIDEQVKINGYRIELGEIRSALLEHPAVGEAAVLT--DEADAAEPgadrriVAFVTAAE 896
Cdd:PLN02246  424 DDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPmkDEVAGEVP------VAFVVRSN 485
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
 1252-1323 5.76e-08

Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis


Pssm-ID: 440006 [Multi-domain]  Cd Length: 80  Bit Score: 51.78  E-value: 5.76e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15597498 1252 PANATEAALLEIWKSVLKRPA--IGVSDNFFQV-GGDSIRLIQMQVMAREA-GLAFTLRDVFNHQSIRELARLLAA 1323
Cdd:COG0236    2 PREELEERLAEIIAEVLGVDPeeITPDDSFFEDlGLDSLDAVELIAALEEEfGIELPDTELFEYPTVADLADYLEE 77
PRK08633 PRK08633
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
 589-910 7.05e-08

2-acyl-glycerophospho-ethanolamine acyltransferase; Validated


Pssm-ID: 236315 [Multi-domain]  Cd Length: 1146  Bit Score: 58.01  E-value: 7.05e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   589 DAAYMIFTSGTSGQPKGVVVEHASALNLSQALARTVYANvvgEGLRVTVNAPF--SFDSSIKQILQLLSGHCLVLVPqev 666
Cdd:PRK08633  783 DTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLR---NDDVILSSLPFfhSFGLTVTLWLPLLEGIKVVYHP--- 856

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   667 rsDPQ--RMLGFL-EERRIDVLDCTPSLFRLLLQAglDDAHPALPG--RILV-GGERFDEaswEVAAGWRrcQVFNL--- 737
Cdd:PRK08633  857 --DPTdaLGIAKLvAKHRATILLGTPTFLRLYLRN--KKLHPLMFAslRLVVaGAEKLKP---EVADAFE--EKFGIril 927

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   738 --YGPTE----ATVNASLARVAE------HARPTIGRALANVDLHVVD--GLGRRKTrGASGELWIGGAGVARGYAGDAG 803
Cdd:PRK08633  928 egYGATEtspvASVNLPDVLAADfkrqtgSKEGSVGMPLPGVAVRIVDpeTFEELPP-GEDGLILIGGPQVMKGYLGDPE 1006

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   804 EAAGRFVE---EGWpgsgrlYRSGDLVRWRADGCLEFLGRIDEQVKINGYRIELGEIRSALLEhpAVGEAAVLTdeADAA 880
Cdd:PRK08633 1007 KTAEVIKDidgIGW------YVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAK--ALGGEEVVF--AVTA 1076

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 15597498   881 EPGADR--RIVAFVTAAEETADESW---LEVDLPS 910
Cdd:PRK08633 1077 VPDEKKgeKLVVLHTCGAEDVEELKraiKESGLPN 1111
PLN02860 PLN02860
o-succinylbenzoate-CoA ligase
 589-873 1.59e-07

o-succinylbenzoate-CoA ligase


Pssm-ID: 215464 [Multi-domain]  Cd Length: 563  Bit Score: 56.35  E-value: 1.59e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   589 DAAYMIFTSGTSGQPKGVVVEHaSALnLSQALARTVyanVVGEG-----LRVtvnAPFSFDSSIKQIL-QLLSGHCLVLV 662
Cdd:PLN02860  173 DAVLICFTSGTTGRPKGVTISH-SAL-IVQSLAKIA---IVGYGeddvyLHT---APLCHIGGLSSALaMLMVGACHVLL 244

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   663 PqevRSDPQRMLGFLEERRIDVLDCTPSLFRLLLQ----AGLDDAHPALPgRILVGG-----ERFDEASwevaAGWRRCQ 733
Cdd:PLN02860  245 P---KFDAKAALQAIKQHNVTSMITVPAMMADLISltrkSMTWKVFPSVR-KILNGGgslssRLLPDAK----KLFPNAK 316

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   734 VFNLYGPTEATVNASLARVAEHARPTIGRALANVDL-------------------HVVDGLGRRKTrGASGELWIGGAGV 794
Cdd:PLN02860  317 LFSAYGMTEACSSLTFMTLHDPTLESPKQTLQTVNQtksssvhqpqgvcvgkpapHVELKIGLDES-SRVGRILTRGPHV 395

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15597498   795 ARGYAGDAGEAAGRFVEEGWpgsgrlYRSGDLVRWRADGCLEFLGRIDEQVKINGYRIELGEIRSALLEHPAVGEAAVL 873
Cdd:PLN02860  396 MLGYWGQNSETASVLSNDGW------LDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVV 468
PRK07867 PRK07867
acyl-CoA synthetase; Validated
 574-872 1.75e-07

acyl-CoA synthetase; Validated


Pssm-ID: 236120 [Multi-domain]  Cd Length: 529  Bit Score: 56.23  E-value: 1.75e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   574 PLAGSGMSLPAPGGRDAAYMIFTSGTSGQPKGVVVEHASALNLSQALAR--------TVY-------ANVVGEGLRVTVN 638
Cdd:PRK07867  138 AHRDAEPPFRVADPDDLFMLIFTSGTSGDPKAVRCTHRKVASAGVMLAQrfglgpddVCYvsmplfhSNAVMAGWAVALA 217

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   639 ApfsfdssikqilqllsGHCLVLVPQEVRSdpqrmlGFLEE-RRIDVLDCT----PSLFRLLLQAGLDDAHPALpgRILV 713
Cdd:PRK07867  218 A----------------GASIALRRKFSAS------GFLPDvRRYGATYANyvgkPLSYVLATPERPDDADNPL--RIVY 273

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   714 GGErfdEASWEVAAGWRR--CQVFNLYGPTEATVnaSLARVAEHARPTIGRALANVDLH-----------VVDGLGRRKT 780
Cdd:PRK07867  274 GNE---GAPGDIARFARRfgCVVVDGFGSTEGGV--AITRTPDTPPGALGPLPPGVAIVdpdtgtecppaEDADGRLLNA 348

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   781 RGASGELW-IGGAGVARGYAGDAgEAAGRFVEEGWpgsgrlYRSGDLVRWRADGCLEFLGRIDEQVKINGYRIELGEIRS 859
Cdd:PRK07867  349 DEAIGELVnTAGPGGFEGYYNDP-EADAERMRGGV------YWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIER 421

                         330
                  ....*....|...
gi 15597498   860 ALLEHPAVGEAAV 872
Cdd:PRK07867  422 ILLRYPDATEVAV 434
LC-FACS_euk cd05927
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ...
 589-840 2.78e-07

Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.


Pssm-ID: 341250 [Multi-domain]  Cd Length: 545  Bit Score: 55.68  E-value: 2.78e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  589 DAAYMIFTSGTSGQPKGVVVEHASALNLSQALARTV-YANVVGEGL-------------RVTVNAPFSFDSSI------- 647
Cdd:cd05927  115 DLATICYTSGTTGNPKGVMLTHGNIVSNVAGVFKILeILNKINPTDvyisylplahifeRVVEALFLYHGAKIgfysgdi 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  648 KQI---LQLLSGHCLVLVPqevrsdpqRMLGFLEERRIDVLDCTPSLFRLL-----------LQAGLDDAHP-------- 705
Cdd:cd05927  195 RLLlddIKALKPTVFPGVP--------RVLNRIYDKIFNKVQAKGPLKRKLfnfalnyklaeLRSGVVRASPfwdklvfn 266

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  706 ----ALPGR---ILVGG-------ERFdeasWEVAAGwrrCQVFNLYGPTEATVNASLARVAEHARPTIGRALANVDLHV 771
Cdd:cd05927  267 kikqALGGNvrlMLTGSaplspevLEF----LRVALG---CPVLEGYGQTECTAGATLTLPGDTSVGHVGGPLPCAEVKL 339

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15597498  772 VD----GLGRRKTRGAsGELWIGGAGVARGYAGDAGEAAGRFVEEGWpgsgrlYRSGDLVRWRADGCLEFLGR 840
Cdd:cd05927  340 VDvpemNYDAKDPNPR-GEVCIRGPNVFSGYYKDPEKTAEALDEDGW------LHTGDIGEWLPNGTLKIIDR 405
A_NRPS_Ta1_like cd12116
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ...
 1195-1234 3.39e-07

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: 55.38  E-value: 3.39e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 15597498 1195 LSEQALRGFLEARLPAYMLPSRIARVERLPLTAEGKLDRR 1234
Cdd:cd12116  429 PDAAALRAHLRATLPAYMVPSAFVRLDALPLTANGKLDRK 468
LC_FACS_bac cd05932
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ...
 583-876 3.87e-07

Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341255 [Multi-domain]  Cd Length: 508  Bit Score: 55.17  E-value: 3.87e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  583 PAPGGRDAAYMIFTSGTSGQPKGVVVEHASALNLSQALARTVYanvVGEGLRVTVNAP--------FSFDSSIKQILQLL 654
Cdd:cd05932  132 PTRFPEQLATLIYTSGTTGQPKGVMLTFGSFAWAAQAGIEHIG---TEENDRMLSYLPlahvtervFVEGGSLYGGVLVA 208

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  655 SGHCLVLVPQEV-RSDP--------------QRMLGFLEERRIDVLDCTPSLFRL----LLQA-GLDDAhpalpgRILVG 714
Cdd:cd05932  209 FAESLDTFVEDVqRARPtlffsvprlwtkfqQGVQDKIPQQKLNLLLKIPVVNSLvkrkVLKGlGLDQC------RLAGC 282

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  715 GER---FDEASWEVAAGWRRCQVfnlYGPTEATVNASLARVAEHARPTIGRALANVDLHVVDglgrrktrgaSGELWIGG 791
Cdd:cd05932  283 GSApvpPALLEWYRSLGLNILEA---YGMTENFAYSHLNYPGRDKIGTVGNAGPGVEVRISE----------DGEILVRS 349

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  792 AGVARGYAGDAGEAAGRFVEEGWpgsgrlYRSGDLVRWRADGCLEFLGRIDEQVKIN-GYRIELGEIRSALLEHPAVgEA 870
Cdd:cd05932  350 PALMMGYYKDPEATAEAFTADGF------LRTGDKGELDADGNLTITGRVKDIFKTSkGKYVAPAPIENKLAEHDRV-EM 422


                 ....*.
gi 15597498  871 AVLTDE 876
Cdd:cd05932  423 VCVIGS 428
PRK09274 PRK09274
peptide synthase; Provisional
 458-870 4.08e-07

peptide synthase; Provisional


Pssm-ID: 236443 [Multi-domain]  Cd Length: 552  Bit Score: 55.29  E-value: 4.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   458 AALQPQAPALLDAHG----------SLDFATLRARSEAVAEALLAAGVRPGQAVAVMTGRNREAIVALLGVMRAAAVytP 527
Cdd:PRK09274   16 AQERPDQLAVAVPGGrgadgklaydELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKAGAV--P 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   528 V------------------NPE----FPAARVERmreaggIVFALADAE-----CAGRaREAFAGACLDLSTLPLAGSGM 580
Cdd:PRK09274   94 VlvdpgmgiknlkqclaeaQPDafigIPKAHLAR------RLFGWGKPSvrrlvTVGG-RLLWGGTTLATLLRDGAAAPF 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   581 SLPAPGGRDAAYMIFTSGTSGQPKGVVVEHASALNLSQALaRTVYANVVGEglrvtvnapfsFDSSIKQILQLLS---GH 657
Cdd:PRK09274  167 PMADLAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEAL-REDYGIEPGE-----------IDLPTFPLFALFGpalGM 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   658 CLVLVPQE----VRSDPQRMLGFLEERRIDVLDCTPSLFRLLLQAGLDDAHPaLPG--RILVGG--------ERFDEASW 723
Cdd:PRK09274  235 TSVIPDMDptrpATVDPAKLFAAIERYGVTNLFGSPALLERLGRYGEANGIK-LPSlrRVISAGapvpiaviERFRAMLP 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   724 EVAagwrrcQVFNLYGPTEA------TVNASLARVAEHARP----TIGRALANVDLHVV---DGLG------RRKTRGAS 784
Cdd:PRK09274  314 PDA------EILTPYGATEAlpissiESREILFATRAATDNgagiCVGRPVDGVEVRIIaisDAPIpewddaLRLATGEI 387

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   785 GELWIGGAGVARGYAGDAGEAAGRFVEEgwPGSGRLYRSGDLVRWRADGCLEFLGRIDEQVKING---YRIELGEI---- 857
Cdd:PRK09274  388 GEIVVAGPMVTRSYYNRPEATRLAKIPD--GQGDVWHRMGDLGYLDAQGRLWFCGRKAHRVETAGgtlYTIPCERIfnth 465

                         490
                  ....*....|....*..
gi 15597498   858 ----RSALLEHPAVGEA 870
Cdd:PRK09274  466 pgvkRSALVGVGVPGAQ 482
PLN02654 PLN02654
acetate-CoA ligase
 803-896 5.00e-07

acetate-CoA ligase


Pssm-ID: 215353 [Multi-domain]  Cd Length: 666  Bit Score: 54.90  E-value: 5.00e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   803 GEAAGRF-VEEGWPGSGR-------------------LYRSGDLVRWRADGCLEFLGRIDEQVKINGYRIELGEIRSALL 862
Cdd:PLN02654  477 GECSGYLcVKKSWPGAFRtlygdheryettyfkpfagYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALV 556

                          90       100       110
                  ....*....|....*....|....*....|....
gi 15597498   863 EHPAVGEAAVLTDEADAAEPGadrrIVAFVTAAE 896
Cdd:PLN02654  557 SHPQCAEAAVVGIEHEVKGQG----IYAFVTLVE 586
AcpA COG3433
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ...
 1192-1323 6.07e-07

Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442659 [Multi-domain]  Cd Length: 295  Bit Score: 53.60  E-value: 6.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1192 GGELSEQALRGFLEARLPAYMLPSRIARVERLPLTAEGKLDRRALLAALAAEAAAQTLEAPA---NATEAALLEIWKSVL 1268
Cdd:COG3433  153 LDGLAAAAALAALDKVPPDVVAASAVVALDALLLLALKVVARAAPALAAAEALLAAASPAPAletALTEEELRADVAELL 232

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 15597498 1269 KRPA--IGVSDNFFQVGGDSIRLIQMQVMAREAGLAFTLRDVFNHQSIRELARLLAA 1323
Cdd:COG3433  233 GVDPeeIDPDDNLFDLGLDSIRLMQLVERWRKAGLDVSFADLAEHPTLAAWWALLAA 289
PRK06334 PRK06334
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
 589-864 7.28e-07

long chain fatty acid--[acyl-carrier-protein] ligase; Validated


Pssm-ID: 180533 [Multi-domain]  Cd Length: 539  Bit Score: 54.44  E-value: 7.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   589 DAAYMIFTSGTSGQPKGVVVEHASALNLSQALARtvYANVVGEGLRVTVNAPF---SFDSSikQILQLLSGHCLVLVPQE 665
Cdd:PRK06334  184 DVAVILFTSGTEKLPKGVPLTHANLLANQRACLK--FFSPKEDDVMMSFLPPFhayGFNSC--TLFPLLSGVPVVFAYNP 259

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   666 VRsdPQRMLGFLEERRIDVLDCTPSLFRLLLQAGlDDAHPALPGR--ILVGGERF-DEASWEVAAGWRRCQVFNLYGPTE 742
Cdd:PRK06334  260 LY--PKKIVEMIDEAKVTFLGSTPVFFDYILKTA-KKQESCLPSLrfVVIGGDAFkDSLYQEALKTFPHIQLRQGYGTTE 336

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   743 A----TVNASLARVAEHArptIGRALANVDLHVVDglgrRKTR-----GASGELWIGGAGVARGYAG-DAGEAAGRFVEE 812
Cdd:PRK06334  337 CspviTINTVNSPKHESC---VGMPIRGMDVLIVS----EETKvpvssGETGLVLTRGTSLFSGYLGeDFGQGFVELGGE 409

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 15597498   813 GWpgsgrlYRSGDLVRWRADGCLEFLGRIDEQVKINGYRIELGEIRSALLEH 864
Cdd:PRK06334  410 TW------YVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMEG 455
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
 1560-2096 9.20e-07

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 54.49  E-value: 9.20e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1560 AGARYRPLPGLAEEgpRRMAAVRVDVPAdslsrLRALAERSGLPLRSLLLAAHGRALCRFSDADEVVTGFVSHGRPEEPG 1639
Cdd:COG3321  856 RGRRRVPLPTYPFQ--REDAAAALLAAA-----LAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAA 928

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1640 ADRLLGLFLNTLPCRLSASVDLLDSARRAFDYERASLEHRRHPLAAIRRRNRELRLDSLFNFVDFHQDDAAPAGVRHGGI 1719
Cdd:COG3321  929 LLALVALAAAAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAA 1008

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1720 LDQVVVDVDVPLAVDFEVAGERLEVGFQYAAGRFPAERAEALAGAYREALLALLGDPVQPPAAAQAEDSVELRRVLKVLS 1799
Cdd:COG3321 1009 ALLLAAAAAAAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAA 1088

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1800 RVLGRPLAADQGFASAGGHSLLGVQAIAELRRLTGRQLSLGLLQGDPDAREVVRRCHAADAPPLPPATERARALWLQRSG 1879
Cdd:COG3321 1089 ALAAAALALALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALL 1168

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1880 SAQPRLRLIALPPAGGNAGTFRGWDARLPADVELLAIQYPGRQERQDEPFVTDVEAMLCAIDDALLPLLDRPFALIGASL 1959
Cdd:COG3321 1169 AAAALLLALALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAAL 1248

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498 1960 GGMLAYELAARLESLHGLRARQLFVISSRAPGPDLEYPRFHAMGDAELLRTLREYDVLPLEVLDDPELREISLATLRADS 2039
Cdd:COG3321 1249 AAAAAALLAALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAA 1328

                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 15597498 2040 RLAADYRYRPREPLAIPITAILGEQDPGVSRVAIDGWRRHASRYELETLAGGHGLVV 2096
Cdd:COG3321 1329 ALAALAAAVAAALALAAAAAAAAAAAAAAAAAAALAAAAGAAAAAAALALAALAAAV 1385
A_NRPS_VisG_like cd17651
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ...
 1199-1234 1.09e-06

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: 53.50  E-value: 1.09e-06
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 15597498 1199 ALRGFLEARLPAYMLPSRIARVERLPLTAEGKLDRR 1234
Cdd:cd17651  453 ELRAALATHLPEYMVPSAFVLLDALPLTPNGKLDRR 488
PRK08315 PRK08315
AMP-binding domain protein; Validated
 589-872 1.30e-06

AMP-binding domain protein; Validated


Pssm-ID: 236236 [Multi-domain]  Cd Length: 559  Bit Score: 53.66  E-value: 1.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   589 DAAYMIFTSGTSGQPKGVVVEHASALNlsqalartvYANVVGEGLRVTVN------APF--SFDSSIKQILQLLSGHCLV 660
Cdd:PRK08315  200 DPINIQYTSGTTGFPKGATLTHRNILN---------NGYFIGEAMKLTEEdrlcipVPLyhCFGMVLGNLACVTHGATMV 270

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   661 lVPQEvRSDPQRMLGFLEERRidvldCT-----PSLFrlllQAGLDdaHPALPgrilvggeRFDEASWE--VAAG----- 728
Cdd:PRK08315  271 -YPGE-GFDPLATLAAVEEER-----CTalygvPTMF----IAELD--HPDFA--------RFDLSSLRtgIMAGspcpi 329

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   729 --WRRCQ-------VFNLYGPTEAT-------VNASLA-RVAeharpTIGRALANVDLHVVD-GLGRRKTRGASGELWIG 790
Cdd:PRK08315  330 evMKRVIdkmhmseVTIAYGMTETSpvstqtrTDDPLEkRVT-----TVGRALPHLEVKIVDpETGETVPRGEQGELCTR 404

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   791 GAGVARGYAGDAGEAAGRFVEEGWpgsgrlYRSGDLVRWRADGCLEFLGRIDEQVKINGYRIELGEIRSALLEHPAVGEA 870
Cdd:PRK08315  405 GYSVMKGYWNDPEKTAEAIDADGW------MHTGDLAVMDEEGYVNIVGRIKDMIIRGGENIYPREIEEFLYTHPKIQDV 478


                  ..
gi 15597498   871 AV 872
Cdd:PRK08315  479 QV 480
PRK06814 PRK06814
acyl-[ACP]--phospholipid O-acyltransferase;
579-901 2.05e-06

acyl-[ACP]--phospholipid O-acyltransferase;


Pssm-ID: 235865 [Multi-domain]  Cd Length: 1140  Bit Score: 53.43  E-value: 2.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   579 GMSLPAPGGRDAAYMIFTSGTSGQPKGVVVEHASAL-NLSQALARTVY--ANVVGEGLRVtvnapF-SFDSSIKQILQLL 654
Cdd:PRK06814  784 LVYFCNRDPDDPAVILFTSGSEGTPKGVVLSHRNLLaNRAQVAARIDFspEDKVFNALPV-----FhSFGLTGGLVLPLL 858

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   655 SGHCLVLVPQ--EVRSDPQR--------MLG---FLE--ERRIDVLDctpslFRLLLqaglddahpalpgRILVGGERFD 719
Cdd:PRK06814  859 SGVKVFLYPSplHYRIIPELiydtnatiLFGtdtFLNgyARYAHPYD-----FRSLR-------------YVFAGAEKVK 920

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   720 EASWEVAAGWRRCQVFNLYGPTEAT----VNASLarvaeHARP-TIGRALANVD--LHVVDGLgrrktrGASGELWIGGA 792
Cdd:PRK06814  921 EETRQTWMEKFGIRILEGYGVTETApviaLNTPM-----HNKAgTVGRLLPGIEyrLEPVPGI------DEGGRLFVRGP 989

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   793 GVARGYAGDAGEAAGRFVEEGWpgsgrlYRSGDLVRWRADGCLEFLGRIDEQVKINGYRIELGEIRSALLE-HPAVGEAA 871
Cdd:PRK06814  990 NVMLGYLRAENPGVLEPPADGW------YDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAElWPDALHAA 1063

                         330       340       350
                  ....*....|....*....|....*....|
gi 15597498   872 VLTDEADAAEpgadrRIVAFVTAAEETADE 901
Cdd:PRK06814 1064 VSIPDARKGE-----RIILLTTASDATRAA 1088
A_NRPS_Bac cd17655
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ...
 1194-1234 2.23e-06

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: 52.72  E-value: 2.23e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 15597498 1194 ELSEQALRGFLEARLPAYMLPSRIARVERLPLTAEGKLDRR 1234
Cdd:cd17655  444 ELPVAQLREFLARELPDYMIPSYFIKLDEIPLTPNGKVDRK 484
PRK07824 PRK07824
o-succinylbenzoate--CoA ligase;
761-900 2.28e-06

o-succinylbenzoate--CoA ligase;


Pssm-ID: 236108 [Multi-domain]  Cd Length: 358  Bit Score: 51.97  E-value: 2.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   761 GRALANVDLHVVDGlgrrktrgasgELWIGGAGVARGYAGdaGEAAGRFVEEGWpgsgrlYRSGDLVRWrADGCLEFLGR 840
Cdd:PRK07824  195 GVPLDGVRVRVEDG-----------RIALGGPTLAKGYRN--PVDPDPFAEPGW------FRTDDLGAL-DDGVLTVLGR 254

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   841 IDEQVKINGYRIELGEIRSALLEHPAVGEAAVLtdeaDAAEPGADRRIVAFVTAAEETAD 900
Cdd:PRK07824  255 ADDAISTGGLTVLPQVVEAALATHPAVADCAVF----GLPDDRLGQRVVAAVVGDGGPAP 310
A_NRPS_AB3403-like cd17646
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ...
 1192-1234 3.28e-06

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: 51.89  E-value: 3.28e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 15597498 1192 GGELSEQALRGFLEARLPAYMLPSRIARVERLPLTAEGKLDRR 1234
Cdd:cd17646  444 AAGPDTAALRAHLAERLPEYMVPAAFVVLDALPLTANGKLDRA 486
A_NRPS_Cytc1-like cd17643
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ...
 1199-1234 3.36e-06

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: 51.92  E-value: 3.36e-06
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 15597498 1199 ALRGFLEARLPAYMLPSRIARVERLPLTAEGKLDRR 1234
Cdd:cd17643  413 ELRALLKELLPDYMVPARYVPLDALPLTVNGKLDRA 448
A_NRPS_PvdJ-like cd17649
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ...
 1198-1234 3.76e-06

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: 51.60  E-value: 3.76e-06
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 15597498 1198 QALRGFLEARLPAYMLPSRIARVERLPLTAEGKLDRR 1234
Cdd:cd17649  411 AQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLDRK 447
MenE/FadK COG0318
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ...
 1192-1234 3.98e-06

O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440087 [Multi-domain]  Cd Length: 452  Bit Score: 51.73  E-value: 3.98e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 15597498 1192 GGELSEQALRGFLEARLPAYMLPSRIARVERLPLTAEGKLDRR 1234
Cdd:COG0318  397 GAELDAEELRAFLRERLARYKVPRRVEFVDELPRTASGKIDRR 439
C_NRPS-like cd19066
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ...
 22-415 4.40e-06

Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long, with various activities such as antibiotic, antifungal, antitumor and immunosuppression. There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.


Pssm-ID: 380453 [Multi-domain]  Cd Length: 427  Bit Score: 51.64  E-value: 4.40e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   22 FPLSPLQTRAWRRHAERPENTV----VGVRLHAPADpvatLERLRRALDGEAQLRVAYRT--MPGMSLPVQVLDGRAADL 95
Cdd:cd19066    2 IPLSPMQRGMWFLKKLATDPSAfnvaIEMFLTGSLD----LARLKQALDAVMERHDVLRTrfCEEAGRYEQVVLDKTVRF 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   96 LVE--RLPGDGDWAGRFARESARLAASPLGGEGQPVLALGLLLDAAGETLqgLLLAAPAFVVDAASLVALLRRGLGPAGQ 173
Cdd:cd19066   78 RIEiiDLRNLADPEARLLELIDQIQQTIYDLERGPLVRVALFRLADERDV--LVVAIHHIIVDGGSFQILFEDISSVYDA 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  174 ASADEGDEALLFQHFSEWA---NEALAGEDGESASGYWREQ----------------AAVAAESPLALADDLGEGEWtar 234
Cdd:cd19066  156 AERQKPTLPPPVGSYADYAawlEKQLESEAAQADLAYWTSYlhglppplplpkakrpSQVASYEVLTLEFFLRSEET--- 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  235 rllpRALLERLAANGL-PEAAALLAWTQVAGQFQGDEGLPLEMArlVSGRLFNEFAELAGPFAGVAPLCLENVRAGSVGE 313
Cdd:cd19066  233 ----KRLREVARESGTtPTQLLLAAFALALKRLTASIDVVIGLT--FLNRPDEAVEDTIGLFLNLLPLRIDTSPDATFPE 306

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  314 RLDALQAAILAQEEAAAL----------RDPFAPDWPLAELGFAWLA-----GELDGAGVAELDCR---QPPLGGFLELQ 375
Cdd:cd19066  307 LLKRTKEQSREAIEHQRVpfielvrhlgVVPEAPKHPLFEPVFTFKNnqqqlGKTGGFIFTTPVYTsseGTVFDLDLEAS 386

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|
gi 15597498  376 VLPHGEGRLASLRVRRDHDGTLAGRLLDAWVECLESIAAD 415
Cdd:cd19066  387 EDPDGDLLLRLEYSRGVYDERTIDRFAERYMTALRQLIEN 426
PRK07008 PRK07008
long-chain-fatty-acid--CoA ligase; Validated
 588-901 5.29e-06

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235908 [Multi-domain]  Cd Length: 539  Bit Score: 51.63  E-value: 5.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   588 RDAAYMIFTSGTSGQPKGVVVEHAS------------ALNLSqalARTVYANVVGeglRVTVNA---PFSFDssikqilq 652
Cdd:PRK07008  176 NQASSLCYTSGTTGNPKGALYSHRStvlhaygaalpdAMGLS---ARDAVLPVVP---MFHVNAwglPYSAP-------- 241

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   653 lLSGHCLVLVPQEVrsDPQRMLGFLEERRIDVLDCTPSLFRLLLQ----AGLDDAHPAlpgRILVGGERFDEASWEVAAG 728
Cdd:PRK07008  242 -LTGAKLVLPGPDL--DGKSLYELIEAERVTFSAGVPTVWLGLLNhmreAGLRFSTLR---RTVIGGSACPPAMIRTFED 315

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   729 WRRCQVFNLYGPTEATVNASLARV--AEHARP---------TIGRALANVDLHVVDGLGRRKTRG--ASGELWIGGAGVA 795
Cdd:PRK07008  316 EYGVEVIHAWGMTEMSPLGTLCKLkwKHSQLPldeqrklleKQGRVIYGVDMKIVGDDGRELPWDgkAFGDLQVRGPWVI 395

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   796 RGYagdageaagrFVEEGWPGSGRLYRSGDLVRWRADGCLEFLGRIDEQVKINGYRIELGEIRSALLEHPAVGEAAVLTd 875
Cdd:PRK07008  396 DRY----------FRGDASPLVDGWFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIA- 464

                         330       340
                  ....*....|....*....|....*....
gi 15597498   876 eadAAEPGADRR-IVAFVT--AAEETADE 901
Cdd:PRK07008  465 ---CAHPKWDERpLLVVVKrpGAEVTREE 490
A_NRPS_ApnA-like cd17644
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ...
 1194-1234 5.53e-06

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: 51.28  E-value: 5.53e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 15597498 1194 ELSEQALRGFLEARLPAYMLPSRIARVERLPLTAEGKLDRR 1234
Cdd:cd17644  422 SPSTVELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDRR 462
BACL_like cd05929
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ...
 546-872 7.67e-06

Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.


Pssm-ID: 341252 [Multi-domain]  Cd Length: 473  Bit Score: 50.84  E-value: 7.67e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  546 IVFALADAECAGRA--REAFAGACLDLSTLPLAGSGMSLPAPGGRD---------AAYMIFTSGTSGQPKGVVVEH---- 610
Cdd:cd05929   72 KSSRAPRAEACAIIeiKAAALVCGLFTGGGALDGLEDYEAAEGGSPetpiedeaaGWKMLYSGGTTGRPKGIKRGLpggp 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  611 ------ASALNLSQALARTVYANVVgeglRVTVNAPFSFDSSIkqilqLLSGHCLVLVPqevRSDPQRMLGFLEERRIDV 684
Cdd:cd05929  152 pdndtlMAAALGFGPGADSVYLSPA----PLYHAAPFRWSMTA-----LFMGGTLVLME---KFDPEEFLRLIERYRVTF 219

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  685 LDCTPSLFRLLLqaglddahpALPGrilVGGERFDEAS----WEVAA-----------GWRRCQVFNLYGPTEAtvNASL 749
Cdd:cd05929  220 AQFVPTMFVRLL---------KLPE---AVRNAYDLSSlkrvIHAAApcppwvkeqwiDWGGPIIWEYYGGTEG--QGLT 285

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  750 ARVAE----HaRPTIGRALANvDLHVVDGLGRRKTRGASGELWIGGAGvARGYAGDAGEAAGRFVEEGWpgsgrlyRS-G 824
Cdd:cd05929  286 IINGEewltH-PGSVGRAVLG-KVHILDEDGNEVPPGEIGEVYFANGP-GFEYTNDPEKTAAARNEGGW-------STlG 355

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 15597498  825 DLVRWRADGCLEFLGRIDEQVKINGYRIELGEIRSALLEHPAVGEAAV 872
Cdd:cd05929  356 DVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAV 403
PRK09192 PRK09192
fatty acyl-AMP ligase;
448-622 8.24e-06

fatty acyl-AMP ligase;


Pssm-ID: 236403 [Multi-domain]  Cd Length: 579  Bit Score: 50.77  E-value: 8.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   448 ESLVAAFDLrAALQPQAPALLDAHGSL----DFATLRARSEAVAEALLAAGVRPGQAVAVMTGRNREAIVALLGVMRAAA 523
Cdd:PRK09192   21 PTLVEALDY-AALGEAGMNFYDRRGQLeealPYQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGL 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   524 VytPVNPEFPAA---------RVERMREAGGIVFALADAECAGRAREA-------FAGACLDLSTLPLAgsGMSLPAPGG 587
Cdd:PRK09192  100 V--PVPLPLPMGfggresyiaQLRGMLASAQPAAIITPDELLPWVNEAthgnpllHVLSHAWFKALPEA--DVALPRPTP 175

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 15597498   588 RDAAYMIFTSGTSGQPKGVVVEHASALNLSQALAR 622
Cdd:PRK09192  176 DDIAYLQYSSGSTRFPRGVIITHRALMANLRAISH 210
A_NRPS_Sfm_like cd12115
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ...
 1192-1234 1.03e-05

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: 50.39  E-value: 1.03e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 15597498 1192 GGELSEQALRGFLEARLPAYMLPSRIARVERLPLTAEGKLDRR 1234
Cdd:cd12115  403 GAAGLVEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRS 445
DltA cd05945
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ...
 1199-1234 1.06e-05

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: 50.32  E-value: 1.06e-05
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 15597498 1199 ALRGFLEARLPAYMLPSRIARVERLPLTAEGKLDRR 1234
Cdd:cd05945  412 AIKAELAERLPPYMIPRRFVYLDELPLNANGKIDRK 447
PLN03102 PLN03102
acyl-activating enzyme; Provisional
 595-873 1.21e-05

acyl-activating enzyme; Provisional


Pssm-ID: 215576 [Multi-domain]  Cd Length: 579  Bit Score: 50.40  E-value: 1.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   595 FTSGTSGQPKGVVVEHA----SALNLSQALARTVYANVVGEGLRVTVNA-PFSFDSSIKQILQLLSGHclVLVPQEVRSd 669
Cdd:PLN03102  193 YTSGTTADPKGVVISHRgaylSTLSAIIGWEMGTCPVYLWTLPMFHCNGwTFTWGTAARGGTSVCMRH--VTAPEIYKN- 269

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   670 pqrmlgfLEERRIDVLDCTPSLFRLLLQAG-LDDAHPALPGRILVGGerfdeaSWEVAAGWRRC-----QVFNLYGPTEA 743
Cdd:PLN03102  270 -------IEMHNVTHMCCVPTVFNILLKGNsLDLSPRSGPVHVLTGG------SPPPAALVKKVqrlgfQVMHAYGLTEA 336

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   744 T-------VNASLARVAEH------ARPTIGR-ALANVDLHVVDGLGRRKTRGAS-GELWIGGAGVARGYAGDAgEAAGR 808
Cdd:PLN03102  337 TgpvlfceWQDEWNRLPENqqmelkARQGVSIlGLADVDVKNKETQESVPRDGKTmGEIVIKGSSIMKGYLKNP-KATSE 415

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15597498   809 FVEEGWpgsgrlYRSGDLVRWRADGCLEFLGRIDEQVKINGYRIELGEIRSALLEHPAVGEAAVL 873
Cdd:PLN03102  416 AFKHGW------LNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVV 474
Abhydrolase_6 pfam12697
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ...
 1895-2100 1.36e-05

Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse specificity.


Pssm-ID: 463673 [Multi-domain]  Cd Length: 211  Bit Score: 48.24  E-value: 1.36e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   1895 GNAGTFRGWDARLPADVELLAIQYPGRQERQDEPF----VTDVEAMLCAIDDAllplldRPFALIGASLGGMLAYELAar 1970
Cdd:pfam12697    6 GAGLSAAPLAALLAAGVAVLAPDLPGHGSSSPPPLdladLADLAALLDELGAA------RPVVLVGHSLGGAVALAAA-- 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   1971 leslHGLRARQLFVISSRAPGPDL--EYPRFHAMGDAELLRTLREYDVLPLEVLDDPELREISLATLRADSRLAADYRYR 2048
Cdd:pfam12697   78 ----AAALVVGVLVAPLAAPPGLLaaLLALLARLGAALAAPAWLAAESLARGFLDDLPADAEWAAALARLAALLAALALL 153

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 15597498   2049 PREPLA--IPITAILGEQDPGVSRVAIDGWRRHASRYELETLAGGHGLVVTAAE 2100
Cdd:pfam12697  154 PLAAWRdlPVPVLVLAEEDRLVPELAQRLLAALAGARLVVLPGAGHLPLDDPEE 207
A_NRPS_SidN3_like cd05918
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ...
 1198-1234 1.40e-05

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: 49.85  E-value: 1.40e-05
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 15597498 1198 QALRGFLEARLPAYMLPSRIARVERLPLTAEGKLDRR 1234
Cdd:cd05918  435 AELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRR 471
A_NRPS_CmdD_like cd17652
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ...
 1192-1234 2.26e-05

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: 49.17  E-value: 2.26e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 15597498 1192 GGELSEQALRGFLEARLPAYMLPSRIARVERLPLTAEGKLDRR 1234
Cdd:cd17652  391 GAAPTAAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRR 433
PRK13388 PRK13388
acyl-CoA synthetase; Provisional
 572-872 2.41e-05

acyl-CoA synthetase; Provisional


Pssm-ID: 237374 [Multi-domain]  Cd Length: 540  Bit Score: 49.25  E-value: 2.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   572 TLPLAGSGMSLPAPGGRDAAYMIFTSGTSGQPKGVVVEHASALNLSQALAR--------TVY-------ANVVGEGLRVT 636
Cdd:PRK13388  134 LVAAAGALTPHREVDAMDPFMLIFTSGTTGAPKAVRCSHGRLAFAGRALTErfgltrddVCYvsmplfhSNAVMAGWAPA 213

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   637 VNApfsfdssikqilqllsGHCLVLVPQEVRSdpqrmlGFLEE-RRIDVLDCT---PSLFRLLLQAGLDDAHpALPGRIL 712
Cdd:PRK13388  214 VAS----------------GAAVALPAKFSAS------GFLDDvRRYGATYFNyvgKPLAYILATPERPDDA-DNPLRVA 270

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   713 VGGERFDEaswEVAAGWRR--CQVFNLYGPTEATVNASLARVAEH---ARPTIGRALANVDLHVVDGLGRRKTRG----- 782
Cdd:PRK13388  271 FGNEASPR---DIAEFSRRfgCQVEDGYGSSEGAVIVVREPGTPPgsiGRGAPGVAIYNPETLTECAVARFDAHGallna 347

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   783 --ASGELW-IGGAGVARGYAGDAGEAAGRfVEEGWpgsgrlYRSGDLVRWRADGCLEFLGRIDEQVKINGYRIELGEIRS 859
Cdd:PRK13388  348 deAIGELVnTAGAGFFEGYYNNPEATAER-MRHGM------YWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIER 420

                         330
                  ....*....|...
gi 15597498   860 ALLEHPAVGEAAV 872
Cdd:PRK13388  421 ILLRHPAINRVAV 433
A_NRPS_TlmIV_like cd12114
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ...
 1192-1234 3.46e-05

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: 48.81  E-value: 3.46e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 15597498 1192 GGELSEQALRGFLEARLPAYMLPSRIARVERLPLTAEGKLDRR 1234
Cdd:cd12114  433 GTPIAPDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDRA 475
A_NRPS_GliP_like cd17653
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ...
 1199-1234 4.38e-05

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: 48.46  E-value: 4.38e-05
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 15597498 1199 ALRGFLEARLPAYMLPSRIARVERLPLTAEGKLDRR 1234
Cdd:cd17653  394 GLRSELAKHLPSYAVPDRIIALDSFPLTANGKVDRK 429
A_NRPS_ProA cd17656
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ...
 1194-1234 7.60e-05

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: 47.47  E-value: 7.60e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 15597498 1194 ELSEQALRGFLEARLPAYMLPSRIARVERLPLTAEGKLDRR 1234
Cdd:cd17656  436 ELNISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRK 476
PRK09294 PRK09294
phthiocerol/phthiodiolone dimycocerosyl transferase;
1391-1631 8.50e-05

phthiocerol/phthiodiolone dimycocerosyl transferase;


Pssm-ID: 181765 [Multi-domain]  Cd Length: 416  Bit Score: 47.40  E-value: 8.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1391 VHGRLDGELLARAWAILIGRHAILRTGFDLHGGQVPLqwvhpatAVAAEVPVHDLCGLDGETRRlrlrawieEEQATPFD 1470
Cdd:PRK09294   30 LRGVLDIDALSDAFDALLRAHPVLAAHLEQDSDGGWE-------LVADDLLHPGIVVVDGDAAR--------PLPELQLD 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1471 WSRPpLVRLAaLALDERRFALGVAEHHSVLDGWSLQSLVDELLAVYADLL-AGVVAREAEAPAVGFRDYVALEREAEANA 1549
Cdd:PRK09294   95 QGVS-LLALD-VVPDDGGARVTLYIHHSIADAHHSASLLDELWSRYTDVVtTGDPGPIRPQPAPQSLEAVLAQRGIRRQA 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  1550 ASALFWLD-----YLAGARYRPLPGLAEEGPRRMAAVRVDVPADSLSRLRALAERSGLPLRSLLLAAHGRALCRFSDADE 1624
Cdd:PRK09294  173 LSGAERFMpamyaYELPPTPTAAVLAKPGLPQAVPVTRCRLSKAQTSSLAAFGRRHRLTVNALVSAAILLAEWQLRRTPH 252


                  ....*..
gi 15597498  1625 VVTGFVS 1631
Cdd:PRK09294  253 VPLPYVY 259
PRK06187 PRK06187
long-chain-fatty-acid--CoA ligase; Validated
 1192-1234 8.83e-05

long-chain-fatty-acid--CoA ligase; Validated


Pssm-ID: 235730 [Multi-domain]  Cd Length: 521  Bit Score: 47.49  E-value: 8.83e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 15597498  1192 GGELSEQALRGFLEARLPAYMLPSRIARVERLPLTAEGKLDRR 1234
Cdd:PRK06187  469 GATLDAKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKR 511
PRK03640 PRK03640
o-succinylbenzoate--CoA ligase;
1192-1234 1.31e-04

o-succinylbenzoate--CoA ligase;


Pssm-ID: 235146 [Multi-domain]  Cd Length: 483  Bit Score: 46.88  E-value: 1.31e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 15597498  1192 GGELSEQALRGFLEARLPAYMLPSRIARVERLPLTAEGKLDRR 1234
Cdd:PRK03640  432 SGEVTEEELRHFCEEKLAKYKVPKRFYFVEELPRNASGKLLRH 474
PksD COG3321
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ...
 384-917 1.54e-04

Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442550 [Multi-domain]  Cd Length: 1386  Bit Score: 47.17  E-value: 1.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  384 LASLRVRRDHDGTLAGRLLDAWVECLE----SIAADRQLPLAGLPLigaaereryQAWQGERVEPAPVESLVAAFDLRAA 459
Cdd:COG3321  820 LPSLRRGEDELAQLLTALAQLWVAGVPvdwsALYPGRGRRRVPLPT---------YPFQREDAAAALLAAALAAALAAAA 890

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  460 LQPQAPALLDAHGSLDFATLRARSEAVAEALLAAGVRPGQAVAVMTGRNREAIVALLGVMRAAAVYTPVNPEFPAARVER 539
Cdd:COG3321  891 ALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVALAAAAAALLALAAAAAAAAAALAAAEAGALLLLAAA 970

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  540 MREAGGIVFALADAECAGRAREAFAGACLDLSTLPLAGSGMSLPAPGGRDAAYMIFTSGTSGQPKGVVVEHASALNLSQA 619
Cdd:COG3321  971 AAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAAAAAAALLALAALLAAAAAALAAAAAAAAAAAALAA 1050

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  620 LARTVYANVVGEGLRVTVNAPFSFDSsikqiLQLLSGHCLVLVPQEVRSDPQRMLGFLEERRIDVLDCTPSLFRLLLQAG 699
Cdd:COG3321 1051 LAAAAAAAAALALALAALLLLAALAE-----LALAAAALALAAALAAAALALALAALAAALLLLALLAALALAAAAAALL 1125

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  700 LDDAHPALPGRILVGGERFDEASWEVAAGWRRCQVFNLYGPTEATVNASLARVAEHARPTIGRALANVDLHVVDGLGRRK 779
Cdd:COG3321 1126 ALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLLALALALAAALAAALAGLAALLLAALLAALL 1205

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  780 TRGASGELWIGGAGVARGYAGDAGEAAGRFVEEGWPGSGRLYRSGDLVRWRADGCLEFLGRIDEQVKINGYRIELGEIRS 859
Cdd:COG3321 1206 AALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAAAALLAALAALALLAAAAGLAALAAAAAAAAAAL 1285

                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 15597498  860 ALLEHPAVGEAAVLTDEADAAEPGADRRIVAFVTAAEETADESWLEVDLPSGHRVAGL 917
Cdd:COG3321 1286 ALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAAALAALAAAVAAALAL 1343
PTZ00237 PTZ00237
acetyl-CoA synthetase; Provisional
 821-869 1.67e-04

acetyl-CoA synthetase; Provisional


Pssm-ID: 240325 [Multi-domain]  Cd Length: 647  Bit Score: 46.66  E-value: 1.67e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 15597498   821 YRSGDLVRWRADGCLEFLGRIDEQVKINGYRIELGEIRSALLEHPAVGE 869
Cdd:PTZ00237  494 YNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLE 542
PRK04813 PRK04813
D-alanine--poly(phosphoribitol) ligase subunit DltA;
1198-1233 1.71e-04

D-alanine--poly(phosphoribitol) ligase subunit DltA;


Pssm-ID: 235313 [Multi-domain]  Cd Length: 503  Bit Score: 46.43  E-value: 1.71e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 15597498  1198 QALRGFLEARLPAYMLPSRIARVERLPLTAEGKLDR 1233
Cdd:PRK04813  459 KAIKKELKERLMEYMIPRKFIYRDSLPLTPNGKIDR 494
FCS cd05921
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ...
 494-861 1.98e-04

Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.


Pssm-ID: 341245 [Multi-domain]  Cd Length: 561  Bit Score: 46.27  E-value: 1.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  494 GVRPGQAVAVMTGRNREAIVALLGVMRAAAVYTPVNPEFPA-----ARVERMRE--AGGIVFA-----LADA-------- 553
Cdd:cd05921   46 GLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVSPAYSLmsqdlAKLKHLFEllKPGLVFAqdaapFARAlaaifplg 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  554 --------ECAGRAREAFAGaclDLSTLPLAGSGMSLPAPGGRDAAYMIFTSGTSGQPKGVVVEHAsALNLSQALARTVY 625
Cdd:cd05921  126 tplvvsrnAVAGRGAISFAE---LAATPPTAAVDAAFAAVGPDTVAKFLFTSGSTGLPKAVINTQR-MLCANQAMLEQTY 201

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  626 ANVVGEGLRVTVNAPFS--FDSSIKQILQLLSGHCLVLvpQEVRSDPQRM---LGFLEERRIDVLDCTPSLFRLLLQAGL 700
Cdd:cd05921  202 PFFGEEPPVLVDWLPWNhtFGGNHNFNLVLYNGGTLYI--DDGKPMPGGFeetLRNLREISPTVYFNVPAGWEMLVAALE 279

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  701 DDahPALPGR-------ILVGGERFDEASWE------VAAGWRRCQVFNLYGPTEaTVNASLARVAEHARP-TIGRALAN 766
Cdd:cd05921  280 KD--EALRRRffkrlklMFYAGAGLSQDVWDrlqalaVATVGERIPMMAGLGATE-TAPTATFTHWPTERSgLIGLPAPG 356

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  767 VDLHVVdglgrrkTRGASGELWIGGAGVARGYAGDAGEAAGRFVEEGWpgsgrlYRSGDLVRWrADGC-----LEFLGRI 841
Cdd:cd05921  357 TELKLV-------PSGGKYEVRVKGPNVTPGYWRQPELTAQAFDEEGF------YCLGDAAKL-ADPDdpakgLVFDGRV 422

                        410       420
                 ....*....|....*....|.
gi 15597498  842 DEQVKIN-GYRIELGEIRSAL 861
Cdd:cd05921  423 AEDFKLAsGTWVSVGPLRARA 443
AMP-binding_C pfam13193
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ...
 1192-1230 2.13e-04

AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.


Pssm-ID: 463804 [Multi-domain]  Cd Length: 76  Bit Score: 41.76  E-value: 2.13e-04
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 15597498   1192 GGELSEQALRGFLEARLPAYMLPSRIARVERLPLTAEGK 1230
Cdd:pfam13193   38 GVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
 1792-1850 2.14e-04

Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.


Pssm-ID: 425746 [Multi-domain]  Cd Length: 62  Bit Score: 41.01  E-value: 2.14e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15597498   1792 RRVLKVLSRVLGRP---LAADQGFASAGGHSLLGVQAIAELRRLTGRQLSLGLLQGDPDARE 1850
Cdd:pfam00550    1 ERLRELLAEVLGVPaeeIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLAE 62
PKS_TE smart00824
Thioesterase; Peptide synthetases are involved in the non-ribosomal synthesis of peptide ...
 1926-1991 2.22e-04

Thioesterase; Peptide synthetases are involved in the non-ribosomal synthesis of peptide antibiotics. Next to the operons encoding these enzymes, in almost all cases, are genes that encode proteins that have similarity to the type II fatty acid thioesterases of vertebrates. There are also modules within the peptide synthetases that also share this similarity. With respect to antibiotic production, thioesterases are required for the addition of the last amino acid to the peptide antibiotic, thereby forming a cyclic antibiotic. Thioesterases (non-integrated) have molecular masses of 25-29 kDa.


Pssm-ID: 214835 [Multi-domain]  Cd Length: 212  Bit Score: 44.52  E-value: 2.22e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15597498    1926 DEPFVTDVEAMLCAIDDALLPLL-DRPFALIGASLGGMLAYELAARLESlHGLRARQLFVISSRAPG 1991
Cdd:smart00824   39 GEPLPASADALVEAQAEAVLRAAgGRPFVLVGHSSGGLLAHAVAARLEA-RGIPPAAVVLLDTYPPG 104
A_NRPS_PpsD_like cd17650
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ...
 1199-1234 2.58e-04

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: 45.92  E-value: 2.58e-04
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 15597498 1199 ALRGFLEARLPAYMLPSRIARVERLPLTAEGKLDRR 1234
Cdd:cd17650  410 ELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRR 445
PRK12582 PRK12582
acyl-CoA synthetase; Provisional
 490-894 2.64e-04

acyl-CoA synthetase; Provisional


Pssm-ID: 237144 [Multi-domain]  Cd Length: 624  Bit Score: 46.19  E-value: 2.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   490 LLAAGVRPGQAVAVMTGRNREAIVALLGVMRAAAVYTPVNPEF----------------------------PAARVERMR 541
Cdd:PRK12582   97 LLDLGLDPGRPVMILSGNSIEHALMTLAAMQAGVPAAPVSPAYslmshdhaklkhlfdlvkprvvfaqsgaPFARALAAL 176

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   542 EAGGIVFALADAECAGRAREAFAGAcldLSTLPLAGSGMSLPAPGGRDAAYMIFTSGTSGQPKGVVVEHasalnlsqala 621
Cdd:PRK12582  177 DLLDVTVVHVTGPGEGIASIAFADL---AATPPTAAVAAAIAAITPDTVAKYLFTSGSTGMPKAVINTQ----------- 242

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   622 RTVYANVVG-EGLRvtvnaPFSFDSSIKQILQ-----------------LLSGHCLVLvpqevrsDPQR-MLGFLEERRI 682
Cdd:PRK12582  243 RMMCANIAMqEQLR-----PREPDPPPPVSLDwmpwnhtmggnanfnglLWGGGTLYI-------DDGKpLPGMFEETIR 310

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   683 DVLDCTPSLF-----RLLLQAGLDDAHPALP-------GRILVGGERFDEASWE------VAAGWRRCQVFNLYGPTEAT 744
Cdd:PRK12582  311 NLREISPTVYgnvpaGYAMLAEAMEKDDALRrsffknlRLMAYGGATLSDDLYErmqalaVRTTGHRIPFYTGYGATETA 390

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   745 VNASLARVAEHARPTIGRALANVDLHVVdglgrrkTRGASGELWIGGAGVARGYAGDAGEAAGRFVEEGWpgsgrlYRSG 824
Cdd:PRK12582  391 PTTTGTHWDTERVGLIGLPLPGVELKLA-------PVGDKYEVRVKGPNVTPGYHKDPELTAAAFDEEGF------YRLG 457

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15597498   825 DLVRW----RADGCLEFLGRIDEQVKI-NGYRIELGEIRSALLehpavgeAAVLTDEADAAEPGADRrivAFVTA 894
Cdd:PRK12582  458 DAARFvdpdDPEKGLIFDGRVAEDFKLsTGTWVSVGTLRPDAV-------AACSPVIHDAVVAGQDR---AFIGL 522
ttLC_FACS_AlkK_like cd12119
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ...
 1192-1234 2.89e-04

Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family catalyzes the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified from Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes uncharacterized FACS proteins.


Pssm-ID: 341284 [Multi-domain]  Cd Length: 518  Bit Score: 45.70  E-value: 2.89e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 15597498 1192 GGELSEQALRGFLEARLPAYMLPSRIARVERLPLTAEGKLDRR 1234
Cdd:cd12119  472 GATVTAEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKK 514
FATP_chFAT1_like cd05937
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ...
 589-872 3.04e-04

Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.


Pssm-ID: 341260 [Multi-domain]  Cd Length: 468  Bit Score: 45.50  E-value: 3.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  589 DAAYMIFTSGTSGQPKGVVVEHASALNLSQALARTVyanVVGEGLRVTVNAPF--SFDSSIKQILQLLSGHCLVLVPQ-- 664
Cdd:cd05937   88 DPAILIYTSGTTGLPKAAAISWRRTLVTSNLLSHDL---NLKNGDRTYTCMPLyhGTAAFLGACNCLMSGGTLALSRKfs 164

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  665 ------EVRSDPQRMLGFLEErridvldctpsLFRLLLQAGL---DDAHPAlpgRILVG-GERFDeaSWEvaagwRRCQV 734
Cdd:cd05937  165 asqfwkDVRDSGATIIQYVGE-----------LCRYLLSTPPspyDRDHKV---RVAWGnGLRPD--IWE-----RFRER 223

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  735 FN------LYGPTEAT-------VNASLARVAEHARPTIGRALAN------VDLHVVDGLGRRKT-------RGASGE-- 786
Cdd:cd05937  224 FNvpeigeFYAATEGVfaltnhnVGDFGAGAIGHHGLIRRWKFENqvvlvkMDPETDDPIRDPKTgfcvrapVGEPGEml 303

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  787 --LWIGGAGVARGYAGDAGEAAGRFVEEGWPGSGRLYRSGDLVRWRADGCLEFLGRIDEQVKINGYRIELGEIRSALLEH 864
Cdd:cd05937  304 grVPFKNREAFQGYLHNEDATESKLVRDVFRKGDIYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAH 383


                 ....*...
gi 15597498  865 PAVGEAAV 872
Cdd:cd05937  384 PDIAEANV 391
PRK08043 PRK08043
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
589-900 3.32e-04

bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;


Pssm-ID: 181207 [Multi-domain]  Cd Length: 718  Bit Score: 45.86  E-value: 3.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   589 DAAYMIFTSGTSGQPKGVVVEHASALnlsqalartvyANVvgEGLRV----TVNAPF--------SFDSSIKQILQLLSG 656
Cdd:PRK08043  366 DAALILFTSGSEGHPKGVVHSHKSLL-----------ANV--EQIKTiadfTPNDRFmsalplfhSFGLTVGLFTPLLTG 432

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   657 HCLVLVPQEV--RSDPQrmlgFLEERRIDVLDCTpSLFrllLQAGLDDAHPALPGR---ILVGGERFDEAS---WEVAAG 728
Cdd:PRK08043  433 AEVFLYPSPLhyRIVPE----LVYDRNCTVLFGT-STF---LGNYARFANPYDFARlryVVAGAEKLQESTkqlWQDKFG 504

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   729 WRrcqVFNLYGPTE----ATVNASLArvaehARP-TIGRALANVD--LHVVDGL---GRRKTRGAS---GELWIGGAGVA 795
Cdd:PRK08043  505 LR---ILEGYGVTEcapvVSINVPMA-----AKPgTVGRILPGMDarLLSVPGIeqgGRLQLKGPNimnGYLRVEKPGVL 576

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   796 RGYAGDAGEAAgrfVEEGWpgsgrlYRSGDLVRWRADGCLEFLGRIDEQVKINGYRIELGEIRS-ALLEHPAVGEAAVLT 874
Cdd:PRK08043  577 EVPTAENARGE---MERGW------YDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQlALGVSPDKQHATAIK 647

                         330       340
                  ....*....|....*....|....*.
gi 15597498   875 DEADAAEPgadrrIVAFVTAAEETAD 900
Cdd:PRK08043  648 SDASKGEA-----LVLFTTDSELTRE 668
EntE COG1021
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ...
 1192-1234 4.10e-04

EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440644 [Multi-domain]  Cd Length: 533  Bit Score: 45.52  E-value: 4.10e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 15597498 1192 GGELSEQALRGFLEAR-LPAYMLPSRIARVERLPLTAEGKLDRR 1234
Cdd:COG1021  482 GEPLTLAELRRFLRERgLAAFKLPDRLEFVDALPLTAVGKIDKK 525
PRK05850 PRK05850
acyl-CoA synthetase; Validated
 449-610 7.55e-04

acyl-CoA synthetase; Validated


Pssm-ID: 235624 [Multi-domain]  Cd Length: 578  Bit Score: 44.55  E-value: 7.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   449 SLVAAFDLRAALQPQAPALL---------DAHGSLDFATLRARSEAVAEALLAAGVrPGQAVAVMTGRNREAIVALLGVM 519
Cdd:PRK05850    2 SVPSLLRERASLQPDDAAFTfidyeqdpaGVAETLTWSQLYRRTLNVAEELRRHGS-TGDRAVILAPQGLEYIVAFLGAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   520 RAAAVYTPVNPEFPAARVER----MREAGGIVF----ALAD--AECAGRAREAFAGACLDLSTLPL-AGSGMSLPAPGGR 588
Cdd:PRK05850   81 QAGLIAVPLSVPQGGAHDERvsavLRDTSPSVVlttsAVVDdvTEYVAPQPGQSAPPVIEVDLLDLdSPRGSDARPRDLP 160

                         170       180
                  ....*....|....*....|..
gi 15597498   589 DAAYMIFTSGTSGQPKGVVVEH 610
Cdd:PRK05850  161 STAYLQYTSGSTRTPAGVMVSH 182
A_NRPS_LgrA-like cd17645
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ...
 1194-1234 9.18e-04

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: 44.08  E-value: 9.18e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 15597498 1194 ELSEQALRGFLEARLPAYMLPSRIARVERLPLTAEGKLDRR 1234
Cdd:cd17645  397 EIPHEELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRK 437
PRK08308 PRK08308
acyl-CoA synthetase; Validated
 817-914 1.19e-03

acyl-CoA synthetase; Validated


Pssm-ID: 236231 [Multi-domain]  Cd Length: 414  Bit Score: 43.49  E-value: 1.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   817 SGRLYRSGDLVRWRADGCLEFLGRIDEQVKINGYRIELGEIRSALLEHPAVGEAAVLTdeadAAEPGADRRIVAFVTAAE 896
Cdd:PRK08308  289 GDKEIFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYR----GKDPVAGERVKAKVISHE 364

                          90       100
                  ....*....|....*....|.
gi 15597498   897 ETADES---WLEVDLPSgHRV 914
Cdd:PRK08308  365 EIDPVQlreWCIQHLAP-YQV 384
V_cholerae_RfbT pfam05575
Vibrio cholerae RfbT protein; This family consists of several RfbT proteins from Vibrio ...
 945-1042 1.21e-03

Vibrio cholerae RfbT protein; This family consists of several RfbT proteins from Vibrio cholerae. It has been found that genetic alteration of the rfbT gene is responsible for serotype conversion of Vibrio cholerae O1 and determines the difference between the Ogawa and Inaba serotypes, in that the presence of rfbT is sufficient for Inaba-to-Ogawa serotype conversion.


Pssm-ID: 114305  Cd Length: 286  Bit Score: 43.13  E-value: 1.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498    945 DAVVLDVGANIGLFSLYIASRAPRARVVAFEPLAPIRRRLEANLGRYAPQVEV--FGIGLSDAEREETFTYYPGYSTFSG 1022
Cdd:pfam05575   80 DTTYIDIGANVGTFCGIAARHITQGKIIAIEPLTEMENSIRMNVQLNNPLVEFhhFGCAIGENEGENIFEVYEFDNRVSS 159

                           90       100
                   ....*....|....*....|....*
gi 15597498   1023 I-----AEYADASGERDVIRRYLSN 1042
Cdd:pfam05575  160 LyfkknTDIADKVKNSQVLVRKLSS 184
PRK08162 PRK08162
acyl-CoA synthetase; Validated
 458-621 1.43e-03

acyl-CoA synthetase; Validated


Pssm-ID: 236169 [Multi-domain]  Cd Length: 545  Bit Score: 43.78  E-value: 1.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   458 AALQPQAPALLdaHGSL--DFATLRARSEAVAEALLAAGVRPGQAVAVMTGRNREAIVALLGVMRAAAVYTPVNPEFPAA 535
Cdd:PRK08162   28 AEVYPDRPAVI--HGDRrrTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDAA 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   536 RVERMREAGGIVFALADAECAGRAREAFagACLDLSTLPLAGSGMSlPAPGGR--------------------------- 588
Cdd:PRK08162  106 SIAFMLRHGEAKVLIVDTEFAEVAREAL--ALLPGPKPLVIDVDDP-EYPGGRfigaldyeaflasgdpdfawtlpadew 182

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 15597498   589 DAAYMIFTSGTSGQPKGVVVEHASA-LN-LSQALA 621
Cdd:PRK08162  183 DAIALNYTSGTTGNPKGVVYHHRGAyLNaLSNILA 217
AFD_YhfT-like cd17633
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ...
 1192-1233 1.92e-03

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: 42.78  E-value: 1.92e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 15597498 1192 GGELSEQALRGFLEARLPAYMLPSRIARVERLPLTAEGKLDR 1233
Cdd:cd17633  279 GDKLTYKQLKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
PLN02387 PLN02387
long-chain-fatty-acid-CoA ligase family protein
 785-867 2.72e-03

long-chain-fatty-acid-CoA ligase family protein


Pssm-ID: 215217 [Multi-domain]  Cd Length: 696  Bit Score: 42.80  E-value: 2.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   785 GELWIGGAGVARGYAGDagEAAGRFV----EEGWpgsgRLYRSGDLVRWRADGCLEFLGRIDEQVKI-NGYRIELGEIRS 859
Cdd:PLN02387  503 GEIVIGGPSVTLGYFKN--QEKTDEVykvdERGM----RWFYTGDIGQFHPDGCLEIIDRKKDIVKLqHGEYVSLGKVEA 576


                  ....*...
gi 15597498   860 ALLEHPAV 867
Cdd:PLN02387  577 ALSVSPYV 584
OSB_CoA_lg cd05912
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ...
 1193-1234 3.24e-03

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: 42.33  E-value: 3.24e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 15597498 1193 GELSEQALRGFLEARLPAYMLPSRIARVERLPLTAEGKLDRR 1234
Cdd:cd05912  366 RPISEEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRH 407
A_NRPS_alphaAR cd17647
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ...
 1200-1233 3.47e-03

Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.


Pssm-ID: 341302 [Multi-domain]  Cd Length: 520  Bit Score: 42.50  E-value: 3.47e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 15597498 1200 LRGFLEARLPAYMLPSRIARVERLPLTAEGKLDR 1233
Cdd:cd17647  481 IREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDK 514
AFD_class_I cd04433
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ...
 1192-1232 4.07e-03

Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.


Pssm-ID: 341228 [Multi-domain]  Cd Length: 336  Bit Score: 41.89  E-value: 4.07e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 15597498 1192 GGELSEQALRGFLEARLPAYMLPSRIARVERLPLTAEGKLD 1232
Cdd:cd04433  296 GADLDAEELRAHVRERLAPYKVPRRVVFVDALPRTASGKID 336
COG3903 COG3903
Predicted ATPase [General function prediction only];
52-465 4.57e-03

Predicted ATPase [General function prediction only];


Pssm-ID: 443109 [Multi-domain]  Cd Length: 933  Bit Score: 42.31  E-value: 4.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   52 ADPVATLERLRRALDGEAQLRVAYRTMPGMSLPVQVLDGRAADLLVERLPGDGDWAGRFARESARLAAsplggeGQPVLA 131
Cdd:COG3903  526 DNLRAALRWALAHGDAELALRLAAALAPFWFLRGLLREGRRWLERALAAAGEAAAALAAAAALAAAAA------AARAAA 599

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  132 LGLLLDAAGETLQGLLLAAPAFVVDAASLVALLRRGLGPAGQASADEGDEALLFQHFSEWANEALAGEDGESASGYWREQ 211
Cdd:COG3903  600 AAAAAAAAAAAAAAAAAAAAAAALLLLAALAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAA 679

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  212 AAVAAESPLALADDLGEGEWTARRLLPRALLERLAANGLPEAAALLAWTQVAGQFQGDEGLPLEMARLVSGRLFNEFAEL 291
Cdd:COG3903  680 AAAAAAALAAAAAALAAAAAAAALAAAAAAALAAAAAAAAAAAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAA 759

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  292 AGPFAGVAPLCLENVRAGSVGERLDALQAAILAQEEAAALRDPFAPDWPLAELGFAWLAGELDGAGVAELDCRQPPLGGF 371
Cdd:COG3903  760 AAALAAAAAAAALAALLLALAAAAAALAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAA 839

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498  372 LELQVLPHGEGRLASLRVRRDHDGTLAGRLLDAWVECLESIAADRQLPLAGLPLIGAAERERYQAWQGERVEPAPVESLV 451
Cdd:COG3903  840 AAAAAAAAAAAAAALAAALAAAAAAAAAAALAAAAAAAAAAAAALLAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALAA 919

                        410
                 ....*....|....
gi 15597498  452 AAFDLRAALQPQAP 465
Cdd:COG3903  920 AAAAAAAAAAAAAA 933
PRK12476 PRK12476
putative fatty-acid--CoA ligase; Provisional
 495-849 6.11e-03

putative fatty-acid--CoA ligase; Provisional


Pssm-ID: 171527 [Multi-domain]  Cd Length: 612  Bit Score: 41.65  E-value: 6.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   495 VRPGQAVAVMTGRNREAIVALLGVMRAAAVYTPV-NPEFPaARVERMREaggivfALADAECA-----GRAREAFAGACL 568
Cdd:PRK12476   89 AGPGDRVAILAPQGIDYVAGFFAAIKAGTIAVPLfAPELP-GHAERLDT------ALRDAEPTvvlttTAAAEAVEGFLR 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   569 DLSTL--PL----------AGSGMSLPAPGGRDAAYMIFTSGTSGQPKGVVVEH-ASALNLSQALartVYANVVGEGLRV 635
Cdd:PRK12476  162 NLPRLrrPRviaidaipdsAGESFVPVELDTDDVSHLQYTSGSTRPPVGVEITHrAVGTNLVQMI---LSIDLLDRNTHG 238

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   636 TVNAPFSFDSSIKQIL--QLLSGHCLVLVPQEVRSDPQRMLGFLEE--RRIDVLDCTPSL-FRLLLQAGLDDAHPALPGR 710
Cdd:PRK12476  239 VSWLPLYHDMGLSMIGfpAVYGGHSTLMSPTAFVRRPQRWIKALSEgsRTGRVVTAAPNFaYEWAAQRGLPAEGDDIDLS 318

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   711 ---ILVGGERFDEASWEV--AA----GWRRCQVFNLYGPTEATVnaSLARVAEHARPTI----------GRALA------ 765
Cdd:PRK12476  319 nvvLIIGSEPVSIDAVTTfnKAfapyGLPRTAFKPSYGIAEATL--FVATIAPDAEPSVvyldreqlgaGRAVRvaadap 396

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597498   766 NVDLHV-------------VD-GLGRRKTRGASGELWIGGAGVARGYAGDAGEAAGRFVE------------EGWPGSGR 819
Cdd:PRK12476  397 NAVAHVscgqvarsqwaviVDpDTGAELPDGEVGEIWLHGDNIGRGYWGRPEETERTFGAklqsrlaegshaDGAADDGT 476

                         410       420       430
                  ....*....|....*....|....*....|
gi 15597498   820 LYRSGDLVRWRaDGCLEFLGRIDEQVKING 849
Cdd:PRK12476  477 WLRTGDLGVYL-DGELYITGRIADLIVIDG 505
prpE PRK10524
propionyl-CoA synthetase; Provisional
 808-872 6.35e-03

propionyl-CoA synthetase; Provisional


Pssm-ID: 182517 [Multi-domain]  Cd Length: 629  Bit Score: 41.47  E-value: 6.35e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15597498   808 RFVEEGWPGSGRL-YRSGDLVRWRADGCLEFLGRIDEQVKINGYRIELGEIRSALLEHPAVGEAAV 872
Cdd:PRK10524  461 RFVKTYWSLFGRQvYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAVAEVAV 526
BCL_like cd05919
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ...
 1198-1233 6.44e-03

Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.


Pssm-ID: 341243 [Multi-domain]  Cd Length: 436  Bit Score: 41.29  E-value: 6.44e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 15597498 1198 QALRGFLEARLPAYMLPSRIARVERLPLTAEGKLDR 1233
Cdd:cd05919  397 RDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQR 432
 
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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