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Conserved domains on  [gi|992230864|ref|XP_015412020|]
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nonribosomal peptide synthase [Aspergillus nomiae NRRL 13137]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
A_NRPS_SidN3_like cd05918
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ...
 234-739 0e+00

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: 654.23  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  234 IHTLFRLQCILQPDAQAICAWDGTITYRQLDRLSSTVQGLLQQYDLGPGSVVPIIFKKSKWAIVAMLGVLKAGAAFCMLD 313
Cdd:cd05918     1 VHDLIEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  314 QSYPTKRLVNICKDVDAKVIVCSQelsigvsgstlsigdhntetatysaiqavntaSHDAAYVVYTSGSTGAPKGIVIEH 393
Cdd:cd05918    81 PSHPLQRLQEILQDTGAKVVLTSS--------------------------------PSDAAYVIFTSGSTGKPKGVVIEH 128

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  394 GSFCTNAIASSQAQNLDRSSRVLQFASYAFDVSVHESLTPLLLGGCVCIPSEAQRVNSLKEAVSTLRVNWVELTPTVARL 473
Cdd:cd05918   129 RALSTSALAHGRALGLTSESRVLQFASYTFDVSILEIFTTLAAGGCLCIPSEEDRLNDLAGFINRLRVTWAFLTPSVARL 208

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  474 WCPADIPTVKTLVMGGEPMLPNDISLWKDKLRLVCAYGPAECTVVSTVQSCV--QELGNIGRSPCGTCWIVSKDNHHRLM 551
Cdd:cd05918   209 LDPEDVPSLRTLVLGGEALTQSDVDTWADRVRLINAYGPAECTIAATVSPVVpsTDPRNIGRPLGATCWVVDPDNHDRLV 288

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  552 PVGCIGELIIGGPIVGRGYLKQPCLTANAFITNPEWASLFHLNGSYRFYKTGDLVRYNADGTIAYIGRKDTQVKLNGQRV 631
Cdd:cd05918   289 PIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPAWLKQEGSGRGRRLYRTGDLVRYNPDGSLEYVGRKDTQVKIRGQRV 368

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  632 ELGEIEHQAQPYFRDA-VIAAEVAAPAGR--KPILILFIARKYEYSVNMDCTMLLRPPSILFQEKAQGTNTLLQEVLPRH 708
Cdd:cd05918   369 ELGEIEHHLRQSLPGAkEVVVEVVKPKDGssSPQLVAFVVLDGSSSGSGDGDSLFLEPSDEFRALVAELRSKLRQRLPSY 448

                         490       500       510
                  ....*....|....*....|....*....|.
gi 992230864  709 MIPAAYIELLAMPISRTGKVNRKLLREAVEQ 739
Cdd:cd05918   449 MVPSVFLPLSHLPLTASGKIDRRALRELAES 479
FUM14_C_NRPS-like cd19545
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ...
 874-1258 4.35e-110

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: 356.61  E-value: 4.35e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  874 IYPCTPLQEALMAYTSKRPGAFQAQFRFQLPHQLDMLRLKEAWRIVIAANPILRTRIVFCHT-GALQVVLRPgEQLQWdl 952
Cdd:cd19545     1 IYPCTPLQEGLMALTARQPGAYVGQRVFELPPDIDLARLQAAWEQVVQANPILRTRIVQSDSgGLLQVVVKE-SPISW-- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  953 inGVHTSPGSL--------MSYGVPLVDMAITNDTAGKlsRTFCLTMHHAIFDGWSYGLILGAVEDAYKHTNAVQR-PFA 1023
Cdd:cd19545    78 --TESTSLDEYleedraapMGLGGPLVRLALVEDPDTE--RYFVWTIHHALYDGWSLPLILRQVLAAYQGEPVPQPpPFS 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1024 PFIKYILHCNYESAKHFWCSEFKDMQALPFPVPPLSRgHMANSSTTTHRQIHVSEWLSSYCTPSTIIQLAFTLLIAWRTE 1103
Cdd:cd19545   154 RFVKYLRQLDDEAAAEFWRSYLAGLDPAVFPPLPSSR-YQPRPDATLEHSISLPSSASSGVTLATVLRAAWALVLSRYTG 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1104 SMDVLFGLTVTGRNAPVAGIHRTTGPTIATFPLRTILYGTMNITDALLCMQNHIATLIPFEHTGLRRIKSFGTETARACQ 1183
Cdd:cd19545   233 SDDVVFGVTLSGRNAPVPGIEQIVGPTIATVPLRVRIDPEQSVEDFLQTVQKDLLDMIPFEHTGLQNIRRLGPDARAACN 312

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 992230864 1184 FQSLLIIQPVTYRESSEIFFELESNEHEQSK-FSTCPLTLVCELRTHSVSVKAISDNAVVISGDMERLLDQLEYLI 1258
Cdd:cd19545   313 FQTLLVVQPALPSSTSESLELGIEEESEDLEdFSSYGLTLECQLSGSGLRVRARYDSSVISEEQVERLLDQFEHVL 388
CT_NRPS-like cd19542
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ...
 1546-1951 5.39e-80

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: 270.33  E-value: 5.39e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1546 YPCSESHQGLLQTQMLRPFYYQSYTIWEVttrskSSPVSPVRLCNAWFTLARRHPALRTHLIDIPLCDGMsskIHVVHKD 1625
Cdd:cd19542     2 YPCTPMQEGMLLSQLRSPGLYFNHFVFDL-----DSSVDVERLRNAWRQLVQRHDILRTVFVESSAEGTF---LQVVLKS 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1626 YMADAAILSCEDEhVITELRKPFLPSDTGLYYP-HAFRICQTVSGRVFCKLEGGHAFLDATSVLIILRELAQAYDGQLSS 1704
Cdd:cd19542    74 LDPPIEEVETDED-SLDALTRDLLDDPTLFGQPpHRLTLLETSSGEVYLVLRISHALYDGVSLPIILRDLAAAYNGQLLP 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1705 vPGPSYSSAVAWLQSLpNGDNRMDYWRRQLKDASPCIFPRLRDQDSPSDTLVVTEqlASTATLTPVCTRHGLTVSNVLQV 1784
Cdd:cd19542   153 -PAPPFSDYISYLQSQ-SQEESLQYWRKYLQGASPCAFPSLSPKRPAERSLSSTR--RSLAKLEAFCASLGVTLASLFQA 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1785 AWGLMLRRYTESDDVCFGALISGRDSRIPDVDKMVGPFFNVLVCQLRFGREDSLWDVLRRNQTEIGNRLLNQHCSLIEVL 1864
Cdd:cd19542   229 AWALVLARYTGSRDVVFGYVVSGRDLPVPGIDDIVGPCINTLPVRVKLDPDWTVLDLLRQLQQQYLRSLPHQHLSLREIQ 308

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1865 RFST-YFGQPLFNTCISVEQ--PLSMDTPDASLCFKELETLEPTEYGIIATITIGTTDVGLGLTYKSDLLTEDQALAVAD 1941
Cdd:cd19542   309 RALGlWPSGTLFNTLVSYQNfeASPESELSGSSVFELSAAEDPTEYPVAVEVEPSGDSLKVSLAYSTSVLSEEQAEELLE 388

                         410
                  ....*....|
gi 992230864 1942 RFKMSITEIM 1951
Cdd:cd19542   389 QFDDILEALL 398
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
 1425-1484 3.39e-11

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: 60.27  E-value: 3.39e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 992230864  1425 ARLRGIVAHVLSIDPQNISPKDDFFTLGGDSISAMQVVS-LCRKHQLSLTALDIFNGRTIE 1484
Cdd:pfam00550    1 ERLRELLAEVLGVPAEEIDPDTDLFDLGLDSLLAVELIArLEEEFGVEIPPSDLFEHPTLA 61
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
 760-829 3.56e-11

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: 60.64  E-value: 3.56e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 992230864  760 PSTPVLDQLRLLFSAALRIPEEKIKPNDSFFH-LGGDSVSAIRLVGDARDQ-GLHITVESLFKRQTISKLAE 829
Cdd:COG0236     2 PREELEERLAEIIAEVLGVDPEEITPDDSFFEdLGLDSLDAVELIAALEEEfGIELPDTELFEYPTVADLAD 73
AFD_class_I super family cl17068
Adenylate forming domain, Class I superfamily; This family includes acyl- and aryl-CoA ligases, ...
 1294-1401 1.09e-08

Adenylate forming domain, Class I superfamily; 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.


The actual alignment was detected with superfamily member cd05918:

Pssm-ID: 473059 [Multi-domain]  Cd Length: 481  Bit Score: 59.86  E-value: 1.09e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1294 IEKKVYDYFGGDVFVLVDAIVPNGSSNRST-AMFVCETKRRREPTETSGLFTRPTDNIRWQLQQLISSLGQSLPRSAVPS 1372
Cdd:cd05918   373 IEHHLRQSLPGAKEVVVEVVKPKDGSSSPQlVAFVVLDGSSSGSGDGDSLFLEPSDEFRALVAELRSKLRQRLPSYMVPS 452

                          90       100
                  ....*....|....*....|....*....
gi 992230864 1373 LCLPVSFIPVDPLGQPDRIYLCEAASSMT 1401
Cdd:cd05918   453 VFLPLSHLPLTASGKIDRRALRELAESLS 481
 
Name Accession Description Interval E-value
A_NRPS_SidN3_like cd05918
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ...
 234-739 0e+00

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: 654.23  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  234 IHTLFRLQCILQPDAQAICAWDGTITYRQLDRLSSTVQGLLQQYDLGPGSVVPIIFKKSKWAIVAMLGVLKAGAAFCMLD 313
Cdd:cd05918     1 VHDLIEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  314 QSYPTKRLVNICKDVDAKVIVCSQelsigvsgstlsigdhntetatysaiqavntaSHDAAYVVYTSGSTGAPKGIVIEH 393
Cdd:cd05918    81 PSHPLQRLQEILQDTGAKVVLTSS--------------------------------PSDAAYVIFTSGSTGKPKGVVIEH 128

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  394 GSFCTNAIASSQAQNLDRSSRVLQFASYAFDVSVHESLTPLLLGGCVCIPSEAQRVNSLKEAVSTLRVNWVELTPTVARL 473
Cdd:cd05918   129 RALSTSALAHGRALGLTSESRVLQFASYTFDVSILEIFTTLAAGGCLCIPSEEDRLNDLAGFINRLRVTWAFLTPSVARL 208

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  474 WCPADIPTVKTLVMGGEPMLPNDISLWKDKLRLVCAYGPAECTVVSTVQSCV--QELGNIGRSPCGTCWIVSKDNHHRLM 551
Cdd:cd05918   209 LDPEDVPSLRTLVLGGEALTQSDVDTWADRVRLINAYGPAECTIAATVSPVVpsTDPRNIGRPLGATCWVVDPDNHDRLV 288

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  552 PVGCIGELIIGGPIVGRGYLKQPCLTANAFITNPEWASLFHLNGSYRFYKTGDLVRYNADGTIAYIGRKDTQVKLNGQRV 631
Cdd:cd05918   289 PIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPAWLKQEGSGRGRRLYRTGDLVRYNPDGSLEYVGRKDTQVKIRGQRV 368

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  632 ELGEIEHQAQPYFRDA-VIAAEVAAPAGR--KPILILFIARKYEYSVNMDCTMLLRPPSILFQEKAQGTNTLLQEVLPRH 708
Cdd:cd05918   369 ELGEIEHHLRQSLPGAkEVVVEVVKPKDGssSPQLVAFVVLDGSSSGSGDGDSLFLEPSDEFRALVAELRSKLRQRLPSY 448

                         490       500       510
                  ....*....|....*....|....*....|.
gi 992230864  709 MIPAAYIELLAMPISRTGKVNRKLLREAVEQ 739
Cdd:cd05918   449 MVPSVFLPLSHLPLTASGKIDRRALRELAES 479
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
 52-953 9.50e-122

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: 418.88  E-value: 9.50e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864   52 TSLYQTLLVAWSILLAEYTDSNNVSFGVfPCEGSDissvqqwEAAIEPQ-------LPI----SDGVT----LRHTRRWL 116
Cdd:COG1020   262 VTLFMVLLAAFALLLARYSGQDDVVVGT-PVAGRP-------RPELEGLvgffvntLPLrvdlSGDPSfaelLARVRETL 333

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  117 LE--------------------DSARHELFNTCIVLStNASPEASQFKSLQsIEKLG--------DIILLVDLLSPLLKL 168
Cdd:COG1020   334 LAayahqdlpferlveelqperDLSRNPLFQVMFVLQ-NAPADELELPGLT-LEPLEldsgtakfDLTLTVVETGDGLRL 411

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  169 SLQYVPSALHNAHANNIISTLEQIIHCVIHSPGRPFADSCLLSKHHQDQI-AEWNRNAPIHPFDSCIHTLFRLQCILQPD 247
Cdd:COG1020   412 TLEYNTDLFDAATIERMAGHLVTLLEALAADPDQPLGDLPLLTAAERQQLlAEWNATAAPYPADATLHELFEAQAARTPD 491

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  248 AQAICAWDGTITYRQLDRLSSTVQGLLQQYDLGPGSVVPIIFKKSKWAIVAMLGVLKAGAAFCMLDQSYPTKRLVNICKD 327
Cdd:COG1020   492 AVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAERLAYMLED 571

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  328 VDAKVIVCSQELSIGVSGS---TLSIgDHNTETATYSAIQAVNTASHDAAYVVYTSGSTGAPKGIVIEHGSFCTNAIASS 404
Cdd:COG1020   572 AGARLVLTQSALAARLPELgvpVLAL-DALALAAEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQ 650

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  405 QAQNLDRSSRVLQFASYAFDVSVHESLTPLLLGGCVCIPSEAQRVN--SLKEAVSTLRVNWVELTPTVARLW---CPADI 479
Cdd:COG1020   651 RRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDpaALAELLARHRVTVLNLTPSLLRALldaAPEAL 730

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  480 PTVKTLVMGGEPMLPNDISLWKDKL---RLVCAYGPAECTVVSTVQSCVQELGNIGRSPCG------TCWIVskDNHHRL 550
Cdd:COG1020   731 PSLRLVLVGGEALPPELVRRWRARLpgaRLVNLYGPTETTVDSTYYEVTPPDADGGSVPIGrpiantRVYVL--DAHLQP 808

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  551 MPVGCIGELIIGGPIVGRGYLKQPCLTANAFITNPewaslFHLNGSyRFYKTGDLVRYNADGTIAYIGRKDTQVKLNGQR 630
Cdd:COG1020   809 VPVGVPGELYIGGAGLARGYLNRPELTAERFVADP-----FGFPGA-RLYRTGDLARWLPDGNLEFLGRADDQVKIRGFR 882

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  631 VELGEIEHQ--AQPYFRDAVIAAEVAAPAGRkpILILFIArkyeysvnmdctmllrpPSILFQEKAQGTNTLLQEVLPRH 708
Cdd:COG1020   883 IELGEIEAAllQHPGVREAVVVAREDAPGDK--RLVAYVV-----------------PEAGAAAAAALLRLALALLLPPY 943

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  709 MIPAAYIELLAMPISRTGKVNRKLLREAVEQASEkdfrayypithndmIQLPSTPVLDQLRLLFSAALRIPEEKIKPNDS 788
Cdd:COG1020   944 MVPAAVVLLLPLPLTGNGKLDRLALPAPAAAAAA--------------AAAAPPAEEEEEEAALALLLLLVVVVGDDDFF 1009

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  789 FFHLGGDSVSAIRLVGDARDQGLHITVESLFKRQTISKLAECTHQMSNGIGSPIPPFSLLDPLGKGTYIAQAteqcsvFP 868
Cdd:COG1020  1010 FFGGGLGLLLLLALARAARLLLLLLLLLLLFLAAAAAAAAAAAAAAAAAAAAPLAAAAAPLPLPPLLLSLLA------LL 1083

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  869 EQIEDIYPCTPLQEALMAYTSKRPGAFQAQFRFQLPHQLDMLRLKEAWRIVIAANPILRTRIVFCHTGALQVVLRPGEQL 948
Cdd:COG1020  1084 LALLLLLALLALLALLLLLLLLLLLLALLLLLALLLALLAALRARRAVRQEGPRLRLLVALAAALALAALLALLLAAAAA 1163


                  ....*
gi 992230864  949 QWDLI 953
Cdd:COG1020  1164 AAELL 1168
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
 259-648 1.34e-120

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: 387.39  E-value: 1.34e-120
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864   259 TYRQLDRLSSTVQGLLQQYD-LGPGSVVPIIFKKSKWAIVAMLGVLKAGAAFCMLDQSYPTKRLVNICKDVDAKVIVCSQ 337
Cdd:TIGR01733    1 TYRELDERANRLARHLRAAGgVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864   338 ELSIGVSGSTLSIG----DHNTETATYSAIQAVNTASH--DAAYVVYTSGSTGAPKGIVIEHGSFCTNAIASSQAQNLDR 411
Cdd:TIGR01733   81 ALASRLAGLVLPVIlldpLELAALDDAPAPPPPDAPSGpdDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDP 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864   412 SSRVLQFASYAFDVSVHESLTPLLLGGCVCIPSEAQR---VNSLKEAVSTLRVNWVELTPTVARLWCPADIP---TVKTL 485
Cdd:TIGR01733  161 DDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEErddAALLAALIAEHPVTVLNLTPSLLALLAAALPPalaSLRLV 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864   486 VMGGEPMLPNDISLWKDK---LRLVCAYGPAECTVVSTVQSC------VQELGNIGRS-PCGTCWIVskDNHHRLMPVGC 555
Cdd:TIGR01733  241 ILGGEALTPALVDRWRARgpgARLINLYGPTETTVWSTATLVdpddapRESPVPIGRPlANTRLYVL--DDDLRPVPVGV 318

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864   556 IGELIIGGPIVGRGYLKQPCLTANAFITNPEWASLFHlngsyRFYKTGDLVRYNADGTIAYIGRKDTQVKLNGQRVELGE 635
Cdd:TIGR01733  319 VGELYIGGPGVARGYLNRPELTAERFVPDPFAGGDGA-----RLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGE 393

                          410
                   ....*....|....*
gi 992230864   636 IEH--QAQPYFRDAV 648
Cdd:TIGR01733  394 IEAalLRHPGVREAV 408
FUM14_C_NRPS-like cd19545
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ...
 874-1258 4.35e-110

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: 356.61  E-value: 4.35e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  874 IYPCTPLQEALMAYTSKRPGAFQAQFRFQLPHQLDMLRLKEAWRIVIAANPILRTRIVFCHT-GALQVVLRPgEQLQWdl 952
Cdd:cd19545     1 IYPCTPLQEGLMALTARQPGAYVGQRVFELPPDIDLARLQAAWEQVVQANPILRTRIVQSDSgGLLQVVVKE-SPISW-- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  953 inGVHTSPGSL--------MSYGVPLVDMAITNDTAGKlsRTFCLTMHHAIFDGWSYGLILGAVEDAYKHTNAVQR-PFA 1023
Cdd:cd19545    78 --TESTSLDEYleedraapMGLGGPLVRLALVEDPDTE--RYFVWTIHHALYDGWSLPLILRQVLAAYQGEPVPQPpPFS 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1024 PFIKYILHCNYESAKHFWCSEFKDMQALPFPVPPLSRgHMANSSTTTHRQIHVSEWLSSYCTPSTIIQLAFTLLIAWRTE 1103
Cdd:cd19545   154 RFVKYLRQLDDEAAAEFWRSYLAGLDPAVFPPLPSSR-YQPRPDATLEHSISLPSSASSGVTLATVLRAAWALVLSRYTG 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1104 SMDVLFGLTVTGRNAPVAGIHRTTGPTIATFPLRTILYGTMNITDALLCMQNHIATLIPFEHTGLRRIKSFGTETARACQ 1183
Cdd:cd19545   233 SDDVVFGVTLSGRNAPVPGIEQIVGPTIATVPLRVRIDPEQSVEDFLQTVQKDLLDMIPFEHTGLQNIRRLGPDARAACN 312

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 992230864 1184 FQSLLIIQPVTYRESSEIFFELESNEHEQSK-FSTCPLTLVCELRTHSVSVKAISDNAVVISGDMERLLDQLEYLI 1258
Cdd:cd19545   313 FQTLLVVQPALPSSTSESLELGIEEESEDLEdFSSYGLTLECQLSGSGLRVRARYDSSVISEEQVERLLDQFEHVL 388
PRK12316 PRK12316
peptide synthase; Provisional
 196-1907 3.21e-103

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 371.21  E-value: 3.21e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  196 VIHSPGRPFADSCLLSKHHQDQIAE-WNRNAPIHPFDSCIHTLFRLQCILQPDAQAICAWDGTITYRQLDRLSSTVQGLL 274
Cdd:PRK12316 3020 MVENPQRSVDELAMLDAEERGQLLEaWNATAAEYPLERGVHRLFEEQVERTPDAVALAFGEQRLSYAELNRRANRLAHRL 3099

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  275 QQYDLGPGSVVPIIFKKSKWAIVAMLGVLKAGAAFCMLDQSYPTKRLVNICKDVDAKVIVCSQELSIGVSGSTLSIGDHN 354
Cdd:PRK12316 3100 IERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLLSQSHLRLPLAQGVQVLDLDR 3179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  355 TETATYSAIQAVNTASHDAAYVVYTSGSTGAPKGIVIEHGSFCTNAIASSQAQNLDRSSRVLQFASYAFDVSVHESLTPL 434
Cdd:PRK12316 3180 GDENYAEANPAIRTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTFSFDVFVEELFWPL 3259

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  435 LLGGCVCI--PSEAQRVNSLKEAVSTLRVNWVELTPTVARLWC----PADIPTVKTLVMGGEPMLPNDISLWKDKLRLVC 508
Cdd:PRK12316 3260 MSGARVVLagPEDWRDPALLVELINSEGVDVLHAYPSMLQAFLeeedAHRCTSLKRIVCGGEALPADLQQQVFAGLPLYN 3339

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  509 AYGPAECTVVSTVQSCVQELGN---IGRsPCGTCWIVSKDNHHRLMPVGCIGELIIGGPIVGRGYLKQPCLTANAFITNP 585
Cdd:PRK12316 3340 LYGPTEATITVTHWQCVEEGKDavpIGR-PIANRACYILDGSLEPVPVGALGELYLGGEGLARGYHNRPGLTAERFVPDP 3418

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  586 EWAslfhlngSYRFYKTGDLVRYNADGTIAYIGRKDTQVKLNGQRVELGEIEH--QAQPYFRDAViaaeVAAPAGRKPIl 663
Cdd:PRK12316 3419 FVP-------GERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEArlLEHPWVREAV----VLAVDGRQLV- 3486

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  664 ilfiarkyEYSVNMDCTMLLRPpsilfQEKAQgtntlLQEVLPRHMIPAAYIELLAMPISRTGKVNRKLLREAVEQASEK 743
Cdd:PRK12316 3487 --------AYVVPEDEAGDLRE-----ALKAH-----LKASLPEYMVPAHLLFLERMPLTPNGKLDRKALPRPDAALLQQ 3548

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  744 DFRAyypithndmiqlPSTPVLDQLRLLFSAALRIPEekIKPNDSFFHLGGDSVSAIRLVGDARDQGLHITVESLFKRQT 823
Cdd:PRK12316 3549 DYVA------------PVNELERRLAAIWADVLKLEQ--VGLTDNFFELGGDSIISLQVVSRARQAGIRFTPKDLFQHQT 3614

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  824 ISKLAECTH-----QMSNGigsPIPPFSLLDPLgkgtyiaqateQCSVFPEQIediypctplqealmaytSKRPGAFQAQ 898
Cdd:PRK12316 3615 IQGLARVARvgggvAVDQG---PVSGETLLLPI-----------QQQFFEEPV-----------------PERHHWNQSL 3663

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  899 FrFQLPHQLDMLRLKEAWRIVIAANPILRTRIV--FCHTGALQVVLRPGEQLQWD-----------LINGVHTS----PG 961
Cdd:PRK12316 3664 L-LKPREALDAAALEAALQALVEHHDALRLRFVedAGGWTAEHLPVELGGALLWRaelddaeelerLGEEAQRSldlaDG 3742

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  962 SLMSygVPLVDMAitndtAGklSRTFCLTMHHAIFDGWSYGLILGAVEDAYKHTNAVQRPFAPfikyilhcnyesAKhfw 1041
Cdd:PRK12316 3743 PLLR--ALLATLA-----DG--SQRLLLVIHHLVVDGVSWRILLEDLQQAYQQLLQGEAPRLP------------AK--- 3798

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1042 CSEFKDMQAlpfpvpplsrghmanssttthrqiHVSEWLSSyctPSTIIQLAFtlliaWRTESMDVlfgltvtgrnapva 1121
Cdd:PRK12316 3799 TSSFKAWAE------------------------RLQEHARG---EALKAELAY-----WQEQLQGV-------------- 3832

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1122 gihrttgptiatfplrtilygtmniTDALLCMQNHIATLIPFEHTGLRRIKSFGTEtaracqfqSLLIIQPVTYRessei 1201
Cdd:PRK12316 3833 -------------------------SSELPCDHPQGALQNRHAASVQTRLDRELTR--------RLLQQAPAAYR----- 3874

                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1202 ffelesneheqskfstcplTLVCELRthsvsVKAISDNAVVISGDMERLLdQLEylidmitksptleiqniipspqdtys 1281
Cdd:PRK12316 3875 -------------------TQVNDLL-----LTALARVVCRWTGEASALV-QLE-------------------------- 3903

                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1282 yalqqsqywsSHIEKkvydyfggDVFVLVDAivpngssNRSTAMFVCETKRRREPTETSGLFTRPtdnIRWQLQQ----- 1356
Cdd:PRK12316 3904 ----------GHGRE--------DLFADIDL-------SRTVGWFTSLFPVRLSPVEDLGASIKA---IKEQLRAipnkg 3955

                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1357 ----LISSLGQSLPRSAVPslCLPVSFIPVDPLGQPDRiylceaassmTLDFLHSLTDPVNKYIDYHILPeEARLRGIVA 1432
Cdd:PRK12316 3956 igfgLLRYLGDEESRRTLA--GLPVPRITFNYLGQFDG----------SFDEEMALFVPAGESAGAEQSP-DAPLDNWLS 4022

                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1433 HVLSIDPQNISPKddfFTLGGDSISAMQVVSLCRKHQLSLTALDIFNGRtieliaTRLMPLTPytppstpaSDRSLdrrf 1512
Cdd:PRK12316 4023 LNGRVYGGELSLD---WTFSREMFEEATIQRLADDYAAELTALVEHCCD------AERHGVTP--------SDFPL---- 4081

                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1513 sllflnSDRDMERLESLLMATydigsmDSIEDAYPCSESHQGLLqtqmLRPFYYQSYTIWEVTTRSKSSPVSPVRLCNAW 1592
Cdd:PRK12316 4082 ------AGLDQARLDALPLPL------GEIEDIYPLSPMQQGML----FHSLYEQEAGDYINQMRVDVQGLDVERFRAAW 4145

                        1450      1460      1470      1480      1490      1500      1510      1520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1593 FTLARRHPALRTHLIDIplcDGMSSKIHVVHK---------DYMADAAILSCEDEHVITELRKPFLPSDTGLyyphaFRI 1663
Cdd:PRK12316 4146 QAALDRHDVLRSGFVWQ---GELGRPLQVVHKqvslpfaelDWRGRADLQAALDALAAAERERGFDLQRAPL-----LRL 4217

                        1530      1540      1550      1560      1570      1580      1590      1600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1664 CQTVSGRVFCKL--EGGHAFLDATSVLIILRELAQAYDGQLSSVPGPSYSSAVAWLQSlPNGDNRMDYWRRQLKD----- 1736
Cdd:PRK12316 4218 VLVRTAEGRHHLiyTNHHILMDGWSNSQLLGEVLERYSGRPPAQPGGRYRDYIAWLQR-QDAAASEAFWREQLAAldept 4296

                        1610      1620      1630      1640      1650      1660      1670      1680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1737 --ASPCIFPRLRDQDSPSDTLVVTeQLASTATLTPVCTRHGLTVSNVLQVAWGLMLRRYTESDDVCFGALISGRDSRIPD 1814
Cdd:PRK12316 4297 rlAQAIARADLRSANGYGEHVREL-DATATARLREFARTQRVTLNTLVQAAWLLLLQRYTGQDTVAFGATVAGRPAELPG 4375

                        1690      1700      1710      1720      1730      1740      1750      1760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1815 VDKMVGPFFNVLVCQLRFGREDSLWDVLRRNQTEIGNRLLNQHCSLIEVLRFSTYFGQPLFNTCI-----SVEQPLSMDT 1889
Cdd:PRK12316 4376 IEGQIGLFINTLPVIATPRAQQSVVEWLQQVQRQNLALREHEHTPLYEIQRWAGQGGEALFDSLLvfenyPVSEALQQGA 4455

                        1770
                  ....*....|....*...
gi 992230864 1890 PdASLCFKELETLEPTEY 1907
Cdd:PRK12316 4456 P-GGLRFGEVTNHEQTNY 4472
CT_NRPS-like cd19542
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ...
 1546-1951 5.39e-80

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: 270.33  E-value: 5.39e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1546 YPCSESHQGLLQTQMLRPFYYQSYTIWEVttrskSSPVSPVRLCNAWFTLARRHPALRTHLIDIPLCDGMsskIHVVHKD 1625
Cdd:cd19542     2 YPCTPMQEGMLLSQLRSPGLYFNHFVFDL-----DSSVDVERLRNAWRQLVQRHDILRTVFVESSAEGTF---LQVVLKS 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1626 YMADAAILSCEDEhVITELRKPFLPSDTGLYYP-HAFRICQTVSGRVFCKLEGGHAFLDATSVLIILRELAQAYDGQLSS 1704
Cdd:cd19542    74 LDPPIEEVETDED-SLDALTRDLLDDPTLFGQPpHRLTLLETSSGEVYLVLRISHALYDGVSLPIILRDLAAAYNGQLLP 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1705 vPGPSYSSAVAWLQSLpNGDNRMDYWRRQLKDASPCIFPRLRDQDSPSDTLVVTEqlASTATLTPVCTRHGLTVSNVLQV 1784
Cdd:cd19542   153 -PAPPFSDYISYLQSQ-SQEESLQYWRKYLQGASPCAFPSLSPKRPAERSLSSTR--RSLAKLEAFCASLGVTLASLFQA 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1785 AWGLMLRRYTESDDVCFGALISGRDSRIPDVDKMVGPFFNVLVCQLRFGREDSLWDVLRRNQTEIGNRLLNQHCSLIEVL 1864
Cdd:cd19542   229 AWALVLARYTGSRDVVFGYVVSGRDLPVPGIDDIVGPCINTLPVRVKLDPDWTVLDLLRQLQQQYLRSLPHQHLSLREIQ 308

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1865 RFST-YFGQPLFNTCISVEQ--PLSMDTPDASLCFKELETLEPTEYGIIATITIGTTDVGLGLTYKSDLLTEDQALAVAD 1941
Cdd:cd19542   309 RALGlWPSGTLFNTLVSYQNfeASPESELSGSSVFELSAAEDPTEYPVAVEVEPSGDSLKVSLAYSTSVLSEEQAEELLE 388

                         410
                  ....*....|
gi 992230864 1942 RFKMSITEIM 1951
Cdd:cd19542   389 QFDDILEALL 398
AMP-binding pfam00501
AMP-binding enzyme;
238-626 5.82e-71

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 244.91  E-value: 5.82e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864   238 FRLQCILQPDAQAICAWDG-TITYRQLDRLSSTVQGLLQQYDLGPGSVVPIIFKKSKWAIVAMLGVLKAGAAFCMLDQSY 316
Cdd:pfam00501    1 LERQAARTPDKTALEVGEGrRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864   317 PTKRLVNICKDVDAKVIVCSQELSIGVSGSTLSIGDHNTETATYSA--------------------IQAVNTASHDAAYV 376
Cdd:pfam00501   81 PAEELAYILEDSGAKVLITDDALKLEELLEALGKLEVVKLVLVLDRdpvlkeeplpeeakpadvppPPPPPPDPDDLAYI 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864   377 VYTSGSTGAPKGIVIEHGSFCTNAIASSQAQ----NLDRSSRVLQFASYAFDVSV-HESLTPLLLGGCVCIPSEAQR--V 449
Cdd:pfam00501  161 IYTSGTTGKPKGVMLTHRNLVANVLSIKRVRprgfGLGPDDRVLSTLPLFHDFGLsLGLLGPLLAGATVVLPPGFPAldP 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864   450 NSLKEAVSTLRVNWVELTPTVARLW------CPADIPTVKTLVMGGEPMLPNDISLWKDKLR--LVCAYGPAECTVVSTV 521
Cdd:pfam00501  241 AALLELIERYKVTVLYGVPTLLNMLleagapKRALLSSLRLVLSGGAPLPPELARRFRELFGgaLVNGYGLTETTGVVTT 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864   522 ----QSCVQELGNIGRSPCGTCWIVSKDNHHRLMPVGCIGELIIGGPIVGRGYLKQPCLTANAFITNpewaslfhlngsy 597
Cdd:pfam00501  321 plplDEDLRSLGSVGRPLPGTEVKIVDDETGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDED------------- 387

                          410       420
                   ....*....|....*....|....*....
gi 992230864   598 RFYKTGDLVRYNADGTIAYIGRKDTQVKL 626
Cdd:pfam00501  388 GWYRTGDLGRRDEDGYLEIVGRKKDQIKL 416
Condensation pfam00668
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ...
 1542-1849 7.97e-27

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: 116.28  E-value: 7.97e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  1542 IEDAYPCSESHQGLLQTQMLrpfyYQSYTIWEVTTRSKSSP-VSPVRLCNAWFTLARRHPALRTHLI-----DIPLC--D 1613
Cdd:pfam00668    1 VQDEYPLSPAQKRMWFLEKL----EPHSSAYNMPAVLKLTGeLDPERLEKALQELINRHDALRTVFIrqengEPVQVilE 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  1614 GMSSKIHVVHKDYMADAAILSCEDEHVITELRKPFLPSDTGLYYPHAFRIcqtVSGRVFCKLEGGHAFLDATSVLIILRE 1693
Cdd:pfam00668   77 ERPFELEIIDISDLSESEEEEAIEAFIQRDLQSPFDLEKGPLFRAGLFRI---AENRHHLLLSMHHIIVDGVSLGILLRD 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  1694 LAQAYDG-----QLSSVPGPSYSSAVAWLQSLPNGDNRMD---YWRRQLKDASPCI-----FPRLRDQDSPSDTLVVTEQ 1760
Cdd:pfam00668  154 LADLYQQllkgePLPLPPKTPYKDYAEWLQQYLQSEDYQKdaaYWLEQLEGELPVLqlpkdYARPADRSFKGDRLSFTLD 233

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  1761 LASTATLTPVCTRHGLTVSNVLQVAWGLMLRRYTESDDVCFGALISGRDSriPDVDKMVGPFFNVLVCQLRFGREDSLWD 1840
Cdd:pfam00668  234 EDTEELLRKLAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPS--PDIERMVGMFVNTLPLRIDPKGGKTFSE 311


                   ....*....
gi 992230864  1841 VLRRNQTEI 1849
Cdd:pfam00668  312 LIKRVQEDL 320
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
 1553-1943 1.44e-23

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: 109.56  E-value: 1.44e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1553 QGLLQTQMLRPFYYQSYTIWEVTTRSKSSPVSPVRLCNAWFTLARRHPALRTHLIDIPLCDGMSSKIHVVHKDYMADAAI 1632
Cdd:COG1020    28 WLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAGRPVQVIQPVVAAPLPVVVLLVDLEALA 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1633 LSCEDEHVITELRKPFLPSDTGLYYPHAFRICQTVSGRVfckLEGGHAFLDATSVLIILRELAQAYD----GQLSSVPGP 1708
Cdd:COG1020   108 EAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLL---LALHHIISDGLSDGLLLAELLRLYLaayaGAPLPLPPL 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1709 SYSSA------VAWLQSLPNGDNRmDYWRRQLKDA-----SPCIFPRLRDQDSPSDTLVVTEQLASTATLTPVCTRHGLT 1777
Cdd:COG1020   185 PIQYAdyalwqREWLQGEELARQL-AYWRQQLAGLpplleLPTDRPRPAVQSYRGARVSFRLPAELTAALRALARRHGVT 263

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1778 VSNVLQVAWGLMLRRYTESDDVCFGALISGRDSriPDVDKMVGPFFNVLVCQLRFGREDSLWDVLRRNQTEIGNRLLNQH 1857
Cdd:COG1020   264 LFMVLLAAFALLLARYSGQDDVVVGTPVAGRPR--PELEGLVGFFVNTLPLRVDLSGDPSFAELLARVRETLLAAYAHQD 341

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1858 CS---LIEVLRFSTYFG-QPLFNTCISVEQ--PLSMDTPDASLCFKELETlEPTEYGIIATITIGTTDVGLGLTYKSDLL 1931
Cdd:COG1020   342 LPferLVEELQPERDLSrNPLFQVMFVLQNapADELELPGLTLEPLELDS-GTAKFDLTLTVVETGDGLRLTLEYNTDLF 420

                         410
                  ....*....|..
gi 992230864 1932 TEDQALAVADRF 1943
Cdd:COG1020   421 DAATIERMAGHL 432
PRK12316 PRK12316
peptide synthase; Provisional
 1540-1907 2.17e-23

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 109.28  E-value: 2.17e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1540 DSIEDAYPCSESHQGLLqtqmLRPFYYQSYTIWEVTTRSKSSPVSPVRLCNAWFTLARRHPALRTHLIDIplcDGMSSKI 1619
Cdd:PRK12316 1551 GEIADIYPLSPMQQGML----FHSLYEQEAGDYINQLRVDVQGLDPDRFRAAWQATVDRHEILRSGFLWQ---DGLEQPL 1623

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1620 HVVHK---------DYMADAAILSCEDEHVITELRKPFLPSDTGLyyphaFRIC--QTVSGRVFCKLEGGHAFLDATSVL 1688
Cdd:PRK12316 1624 QVIHKqvelpfaelDWRGREDLGQALDALAQAERQKGFDLTRAPL-----LRLVlvRTGEGRHHLIYTNHHILMDGWSNA 1698

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1689 IILRELAQAYDGQLSSVPGPSYSSAVAWLQSlPNGDNRMDYWRRQLKD-ASPCIFPR-LRDQDSPSD--TLVVTEQLAST 1764
Cdd:PRK12316 1699 QLLGEVLQRYAGQPVAAPGGRYRDYIAWLQR-QDAAASEAFWKEQLAAlEEPTRLAQaARTEDGQVGygDHQQLLDPAQT 1777

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1765 ATLTPVCTRHGLTVSNVLQVAWGLMLRRYTESDDVCFGALISGRDSRIPDVDKMVGPFFNVLVCQLRFGREDSLWDVLRR 1844
Cdd:PRK12316 1778 RALAEFARAQKVTLNTLVQAAWLLLLQRYTGQETVAFGATVAGRPAELPGIEQQIGLFINTLPVIAAPRPDQSVADWLQE 1857

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1845 NQTEigNRLL--NQHCSLIEVLRFSTYFGQPLFNTCISVE-----QPLSMDTPdASLCFKELETLEPTEY 1907
Cdd:PRK12316 1858 VQAL--NLALreHEHTPLYDIQRWAGQGGEALFDSLLVFEnypvaEALKQGAP-AGLVFGRVSNHEQTNY 1924
PRK12316 PRK12316
peptide synthase; Provisional
 865-1295 5.69e-22

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 104.65  E-value: 5.69e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  865 SVFPEQIEDIYPCTPLQEALMAYTSKRP--GAFQAQFRFQLpHQLDMLRLKEAWRIVIAANPILRTRIVFcHTG---ALQ 939
Cdd:PRK12316 1547 PLPAGEIADIYPLSPMQQGMLFHSLYEQeaGDYINQLRVDV-QGLDPDRFRAAWQATVDRHEILRSGFLW-QDGleqPLQ 1624

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  940 VVLR----PGEQLQWDLINGVHTSPGSLMS---------YGVPLVDMAITNDTAGKLSRTFclTMHHAIFDGWSYGLILG 1006
Cdd:PRK12316 1625 VIHKqvelPFAELDWRGREDLGQALDALAQaerqkgfdlTRAPLLRLVLVRTGEGRHHLIY--TNHHILMDGWSNAQLLG 1702

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1007 AVEDAYkhtnAVQRPFAP------FIKYILHCNYESAKHFWCSEFKD-------MQALPFPVPPlsRGHMANSSTTTHRQ 1073
Cdd:PRK12316 1703 EVLQRY----AGQPVAAPggryrdYIAWLQRQDAAASEAFWKEQLAAleeptrlAQAARTEDGQ--VGYGDHQQLLDPAQ 1776

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1074 IHVsewLSSYC-----TPSTIIQLAFTLLIAWRTESMDVLFGLTVTGRNAPVAGIHRTTGPTIATFPLRTILYGTMNITD 1148
Cdd:PRK12316 1777 TRA---LAEFAraqkvTLNTLVQAAWLLLLQRYTGQETVAFGATVAGRPAELPGIEQQIGLFINTLPVIAAPRPDQSVAD 1853

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1149 ALLCMQNHIATLIPFEHTGLRRIKSFGTETARACqFQSLLIIQ--PVTyrESSE------IFFELESNeHEQSKFstcPL 1220
Cdd:PRK12316 1854 WLQEVQALNLALREHEHTPLYDIQRWAGQGGEAL-FDSLLVFEnyPVA--EALKqgapagLVFGRVSN-HEQTNY---PL 1926

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 992230864 1221 TLVCELrTHSVSVKAISDNAVVISGDMERLLDQLEYLIDMITKSPTLEIQNIipSPQDTYSYALQQSQyWSSHIE 1295
Cdd:PRK12316 1927 TLAVTL-GETLSLQYSYDRGHFDAAAIERLDRHLLHLLEQMAEDAQAALGEL--ALLDAGERQRILAD-WDRTPE 1997
Condensation pfam00668
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ...
 871-1269 1.41e-21

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: 100.10  E-value: 1.41e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864   871 IEDIYPCTPLQEAlMAYTSK---RPGAFQAQFRFQLPHQLDMLRLKEAWRIVIAANPILRTRIVFCHTGALQVVLRPGEQ 947
Cdd:pfam00668    1 VQDEYPLSPAQKR-MWFLEKlepHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIRQENGEPVQVILEERP 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864   948 LQWDLINGVHTSpgslMSYGVPLVDMAITNDTAGKL-----------------SRTFCL-TMHHAIFDGWSYGLILGAVE 1009
Cdd:pfam00668   80 FELEIIDISDLS----ESEEEEAIEAFIQRDLQSPFdlekgplfraglfriaeNRHHLLlSMHHIIVDGVSLGILLRDLA 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  1010 DAYKHT----NAVQRPFAPFIKYILHCN-------YESAKHFW---CSEFKDMQALPFPVPPLS-------------RGH 1062
Cdd:pfam00668  156 DLYQQLlkgePLPLPPKTPYKDYAEWLQqylqsedYQKDAAYWleqLEGELPVLQLPKDYARPAdrsfkgdrlsftlDED 235

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  1063 MANSSTTTHRQIHVsewlssycTPSTIIQLAFTLLIAWRTESMDVLFGLTVTGRNAPvaGIHRTTGPTIATFPLRTILYG 1142
Cdd:pfam00668  236 TEELLRKLAKAHGT--------TLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPSP--DIERMVGMFVNTLPLRIDPKG 305

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  1143 TMNITDALLCMQNHIATLIPFEHTGLRRIKSFGT---ETARACQFQSLLIIQPVTYRES-------SEIFFELESNEHEQ 1212
Cdd:pfam00668  306 GKTFSELIKRVQEDLLSAEPHQGYPFGDLVNDLRlprDLSRHPLFDPMFSFQNYLGQDSqeeefqlSELDLSVSSVIEEE 385

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 992230864  1213 SKFstcPLTLVCELRTHSVSVKAISDNAVVISGDMERLLDQLEYLIDMITKSPTLEI 1269
Cdd:pfam00668  386 AKY---DLSLTASERGGGLTIKIDYNTSLFDEETIERFAEHFKELLEQAIAHPSQPL 439
COG4908 COG4908
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ...
 878-1055 1.04e-11

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


Pssm-ID: 443936 [Multi-domain]  Cd Length: 243  Bit Score: 66.99  E-value: 1.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  878 TPLQEALMAYtSKRPGAFQAQFRFQLPHQLDMLRLKEAWRIVIAANPILRTRIVFCHTGALQVVLrPGEQLQWDLINGVH 957
Cdd:COG4908     2 SPAQKRFLFL-EPGSNAYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFVEEDGEPVQRID-PDADLPLEVVDLSA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  958 TSPGSLMSYGVPLVDMAITND---TAGKLSR-----------TFCLTMHHAIFDGWSYGLILGAVEDAYkhTNAVQ---- 1019
Cdd:COG4908    80 LPEPEREAELEELVAEEASRPfdlARGPLLRaalirlgedehVLLLTIHHIISDGWSLGILLRELAALY--AALLEgepp 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 992230864 1020 ------RPFAPFI----KYILHCNYESAKHFWCSEFKDM-QALPFPV 1055
Cdd:COG4908   158 plpelpIQYADYAawqrAWLQSEALEKQLEYWRQQLAGApPVLELPT 204
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
 1425-1484 3.39e-11

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: 60.27  E-value: 3.39e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 992230864  1425 ARLRGIVAHVLSIDPQNISPKDDFFTLGGDSISAMQVVS-LCRKHQLSLTALDIFNGRTIE 1484
Cdd:pfam00550    1 ERLRELLAEVLGVPAEEIDPDTDLFDLGLDSLLAVELIArLEEEFGVEIPPSDLFEHPTLA 61
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
 760-829 3.56e-11

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: 60.64  E-value: 3.56e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 992230864  760 PSTPVLDQLRLLFSAALRIPEEKIKPNDSFFH-LGGDSVSAIRLVGDARDQ-GLHITVESLFKRQTISKLAE 829
Cdd:COG0236     2 PREELEERLAEIIAEVLGVDPEEITPDDSFFEdLGLDSLDAVELIAALEEEfGIELPDTELFEYPTVADLAD 73
AcpA COG3433
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ...
 1424-1490 4.23e-11

Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442659 [Multi-domain]  Cd Length: 295  Bit Score: 65.93  E-value: 4.23e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 992230864 1424 EARLRGIVAHVLSIDPQNISPKDDFFTLGGDSISAMQVVSLCRKHQLSLTALDIFNGRTIELIATRL 1490
Cdd:COG3433   221 EEELRADVAELLGVDPEEIDPDDNLFDLGLDSIRLMQLVERWRKAGLDVSFADLAEHPTLAAWWALL 287
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
 766-825 1.27e-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: 55.65  E-value: 1.27e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 992230864   766 DQLRLLFSAALRIPEEKIKPNDSFFHLGGDSVSAIRLVGDARDQ-GLHITVESLFKRQTIS 825
Cdd:pfam00550    1 ERLRELLAEVLGVPAEEIDPDTDLFDLGLDSLLAVELIARLEEEfGVEIPPSDLFEHPTLA 61
A_NRPS_SidN3_like cd05918
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ...
 1294-1401 1.09e-08

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: 59.86  E-value: 1.09e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1294 IEKKVYDYFGGDVFVLVDAIVPNGSSNRST-AMFVCETKRRREPTETSGLFTRPTDNIRWQLQQLISSLGQSLPRSAVPS 1372
Cdd:cd05918   373 IEHHLRQSLPGAKEVVVEVVKPKDGSSSPQlVAFVVLDGSSSGSGDGDSLFLEPSDEFRALVAELRSKLRQRLPSYMVPS 452

                          90       100
                  ....*....|....*....|....*....
gi 992230864 1373 LCLPVSFIPVDPLGQPDRIYLCEAASSMT 1401
Cdd:cd05918   453 VFLPLSHLPLTASGKIDRRALRELAESLS 481
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
 764-829 5.81e-05

Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.


Pssm-ID: 214834 [Multi-domain]  Cd Length: 86  Bit Score: 43.39  E-value: 5.81e-05
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 992230864    764 VLDQLRLLFSAALRI-PEEKIKPNDSFFHLGGDSVSAIRLVGDARDQ-GLHITVESLFKRQTISKLAE 829
Cdd:smart00823   13 LLDLVREQVAAVLGHaAAEAIDPDRPFRDLGLDSLMAVELRNRLEAAtGLRLPATLVFDHPTPAALAE 80
 
Name Accession Description Interval E-value
A_NRPS_SidN3_like cd05918
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ...
 234-739 0e+00

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: 654.23  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  234 IHTLFRLQCILQPDAQAICAWDGTITYRQLDRLSSTVQGLLQQYDLGPGSVVPIIFKKSKWAIVAMLGVLKAGAAFCMLD 313
Cdd:cd05918     1 VHDLIEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  314 QSYPTKRLVNICKDVDAKVIVCSQelsigvsgstlsigdhntetatysaiqavntaSHDAAYVVYTSGSTGAPKGIVIEH 393
Cdd:cd05918    81 PSHPLQRLQEILQDTGAKVVLTSS--------------------------------PSDAAYVIFTSGSTGKPKGVVIEH 128

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  394 GSFCTNAIASSQAQNLDRSSRVLQFASYAFDVSVHESLTPLLLGGCVCIPSEAQRVNSLKEAVSTLRVNWVELTPTVARL 473
Cdd:cd05918   129 RALSTSALAHGRALGLTSESRVLQFASYTFDVSILEIFTTLAAGGCLCIPSEEDRLNDLAGFINRLRVTWAFLTPSVARL 208

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  474 WCPADIPTVKTLVMGGEPMLPNDISLWKDKLRLVCAYGPAECTVVSTVQSCV--QELGNIGRSPCGTCWIVSKDNHHRLM 551
Cdd:cd05918   209 LDPEDVPSLRTLVLGGEALTQSDVDTWADRVRLINAYGPAECTIAATVSPVVpsTDPRNIGRPLGATCWVVDPDNHDRLV 288

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  552 PVGCIGELIIGGPIVGRGYLKQPCLTANAFITNPEWASLFHLNGSYRFYKTGDLVRYNADGTIAYIGRKDTQVKLNGQRV 631
Cdd:cd05918   289 PIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPAWLKQEGSGRGRRLYRTGDLVRYNPDGSLEYVGRKDTQVKIRGQRV 368

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  632 ELGEIEHQAQPYFRDA-VIAAEVAAPAGR--KPILILFIARKYEYSVNMDCTMLLRPPSILFQEKAQGTNTLLQEVLPRH 708
Cdd:cd05918   369 ELGEIEHHLRQSLPGAkEVVVEVVKPKDGssSPQLVAFVVLDGSSSGSGDGDSLFLEPSDEFRALVAELRSKLRQRLPSY 448

                         490       500       510
                  ....*....|....*....|....*....|.
gi 992230864  709 MIPAAYIELLAMPISRTGKVNRKLLREAVEQ 739
Cdd:cd05918   449 MVPSVFLPLSHLPLTASGKIDRRALRELAES 479
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
 52-953 9.50e-122

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: 418.88  E-value: 9.50e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864   52 TSLYQTLLVAWSILLAEYTDSNNVSFGVfPCEGSDissvqqwEAAIEPQ-------LPI----SDGVT----LRHTRRWL 116
Cdd:COG1020   262 VTLFMVLLAAFALLLARYSGQDDVVVGT-PVAGRP-------RPELEGLvgffvntLPLrvdlSGDPSfaelLARVRETL 333

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  117 LE--------------------DSARHELFNTCIVLStNASPEASQFKSLQsIEKLG--------DIILLVDLLSPLLKL 168
Cdd:COG1020   334 LAayahqdlpferlveelqperDLSRNPLFQVMFVLQ-NAPADELELPGLT-LEPLEldsgtakfDLTLTVVETGDGLRL 411

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  169 SLQYVPSALHNAHANNIISTLEQIIHCVIHSPGRPFADSCLLSKHHQDQI-AEWNRNAPIHPFDSCIHTLFRLQCILQPD 247
Cdd:COG1020   412 TLEYNTDLFDAATIERMAGHLVTLLEALAADPDQPLGDLPLLTAAERQQLlAEWNATAAPYPADATLHELFEAQAARTPD 491

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  248 AQAICAWDGTITYRQLDRLSSTVQGLLQQYDLGPGSVVPIIFKKSKWAIVAMLGVLKAGAAFCMLDQSYPTKRLVNICKD 327
Cdd:COG1020   492 AVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAERLAYMLED 571

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  328 VDAKVIVCSQELSIGVSGS---TLSIgDHNTETATYSAIQAVNTASHDAAYVVYTSGSTGAPKGIVIEHGSFCTNAIASS 404
Cdd:COG1020   572 AGARLVLTQSALAARLPELgvpVLAL-DALALAAEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQ 650

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  405 QAQNLDRSSRVLQFASYAFDVSVHESLTPLLLGGCVCIPSEAQRVN--SLKEAVSTLRVNWVELTPTVARLW---CPADI 479
Cdd:COG1020   651 RRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDpaALAELLARHRVTVLNLTPSLLRALldaAPEAL 730

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  480 PTVKTLVMGGEPMLPNDISLWKDKL---RLVCAYGPAECTVVSTVQSCVQELGNIGRSPCG------TCWIVskDNHHRL 550
Cdd:COG1020   731 PSLRLVLVGGEALPPELVRRWRARLpgaRLVNLYGPTETTVDSTYYEVTPPDADGGSVPIGrpiantRVYVL--DAHLQP 808

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  551 MPVGCIGELIIGGPIVGRGYLKQPCLTANAFITNPewaslFHLNGSyRFYKTGDLVRYNADGTIAYIGRKDTQVKLNGQR 630
Cdd:COG1020   809 VPVGVPGELYIGGAGLARGYLNRPELTAERFVADP-----FGFPGA-RLYRTGDLARWLPDGNLEFLGRADDQVKIRGFR 882

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  631 VELGEIEHQ--AQPYFRDAVIAAEVAAPAGRkpILILFIArkyeysvnmdctmllrpPSILFQEKAQGTNTLLQEVLPRH 708
Cdd:COG1020   883 IELGEIEAAllQHPGVREAVVVAREDAPGDK--RLVAYVV-----------------PEAGAAAAAALLRLALALLLPPY 943

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  709 MIPAAYIELLAMPISRTGKVNRKLLREAVEQASEkdfrayypithndmIQLPSTPVLDQLRLLFSAALRIPEEKIKPNDS 788
Cdd:COG1020   944 MVPAAVVLLLPLPLTGNGKLDRLALPAPAAAAAA--------------AAAAPPAEEEEEEAALALLLLLVVVVGDDDFF 1009

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  789 FFHLGGDSVSAIRLVGDARDQGLHITVESLFKRQTISKLAECTHQMSNGIGSPIPPFSLLDPLGKGTYIAQAteqcsvFP 868
Cdd:COG1020  1010 FFGGGLGLLLLLALARAARLLLLLLLLLLLFLAAAAAAAAAAAAAAAAAAAAPLAAAAAPLPLPPLLLSLLA------LL 1083

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  869 EQIEDIYPCTPLQEALMAYTSKRPGAFQAQFRFQLPHQLDMLRLKEAWRIVIAANPILRTRIVFCHTGALQVVLRPGEQL 948
Cdd:COG1020  1084 LALLLLLALLALLALLLLLLLLLLLLALLLLLALLLALLAALRARRAVRQEGPRLRLLVALAAALALAALLALLLAAAAA 1163


                  ....*
gi 992230864  949 QWDLI 953
Cdd:COG1020  1164 AAELL 1168
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
 259-648 1.34e-120

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: 387.39  E-value: 1.34e-120
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864   259 TYRQLDRLSSTVQGLLQQYD-LGPGSVVPIIFKKSKWAIVAMLGVLKAGAAFCMLDQSYPTKRLVNICKDVDAKVIVCSQ 337
Cdd:TIGR01733    1 TYRELDERANRLARHLRAAGgVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864   338 ELSIGVSGSTLSIG----DHNTETATYSAIQAVNTASH--DAAYVVYTSGSTGAPKGIVIEHGSFCTNAIASSQAQNLDR 411
Cdd:TIGR01733   81 ALASRLAGLVLPVIlldpLELAALDDAPAPPPPDAPSGpdDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDP 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864   412 SSRVLQFASYAFDVSVHESLTPLLLGGCVCIPSEAQR---VNSLKEAVSTLRVNWVELTPTVARLWCPADIP---TVKTL 485
Cdd:TIGR01733  161 DDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEErddAALLAALIAEHPVTVLNLTPSLLALLAAALPPalaSLRLV 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864   486 VMGGEPMLPNDISLWKDK---LRLVCAYGPAECTVVSTVQSC------VQELGNIGRS-PCGTCWIVskDNHHRLMPVGC 555
Cdd:TIGR01733  241 ILGGEALTPALVDRWRARgpgARLINLYGPTETTVWSTATLVdpddapRESPVPIGRPlANTRLYVL--DDDLRPVPVGV 318

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864   556 IGELIIGGPIVGRGYLKQPCLTANAFITNPEWASLFHlngsyRFYKTGDLVRYNADGTIAYIGRKDTQVKLNGQRVELGE 635
Cdd:TIGR01733  319 VGELYIGGPGVARGYLNRPELTAERFVPDPFAGGDGA-----RLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGE 393

                          410
                   ....*....|....*
gi 992230864   636 IEH--QAQPYFRDAV 648
Cdd:TIGR01733  394 IEAalLRHPGVREAV 408
A_NRPS cd05930
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ...
 246-733 3.54e-118

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: 381.88  E-value: 3.54e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  246 PDAQAICAWDGTITYRQLDRLSSTVQGLLQQYDLGPGSVVPIIFKKSKWAIVAMLGVLKAGAAFCMLDQSYPTKRLVNIC 325
Cdd:cd05930     1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  326 KDVDAKVIVcsqelsigvsgstlsigdhntetatysaiqavnTASHDAAYVVYTSGSTGAPKGIVIEHGSFCTNAIASSQ 405
Cdd:cd05930    81 EDSGAKLVL---------------------------------TDPDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQE 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  406 AQNLDRSSRVLQFASYAFDVSVHESLTPLLLGGCVCIPSEAQRVN--SLKEAVSTLRVNWVELTPTVARLW----CPADI 479
Cdd:cd05930   128 AYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKDpeALADLLAEEGITVLHLTPSLLRLLlqelELAAL 207

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  480 PTVKTLVMGGEPMLPNDISLWKDKL---RLVCAYGPAECTVVSTVQSCVQELGNIGRSPCGT------CWIVskDNHHRL 550
Cdd:cd05930   208 PSLRLVLVGGEALPPDLVRRWRELLpgaRLVNLYGPTEATVDATYYRVPPDDEEDGRVPIGRpipntrVYVL--DENLRP 285

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  551 MPVGCIGELIIGGPIVGRGYLKQPCLTANAFITNPewaslFHLNGsyRFYKTGDLVRYNADGTIAYIGRKDTQVKLNGQR 630
Cdd:cd05930   286 VPPGVPGELYIGGAGLARGYLNRPELTAERFVPNP-----FGPGE--RMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYR 358

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  631 VELGEIEHQ--AQPYFRDAVIAAEVAAPAGrkPILILFIARKYEYSVNMDCtmlLRppsilfqekaqgtnTLLQEVLPRH 708
Cdd:cd05930   359 IELGEIEAAllAHPGVREAAVVAREDGDGE--KRLVAYVVPDEGGELDEEE---LR--------------AHLAERLPDY 419

                         490       500
                  ....*....|....*....|....*
gi 992230864  709 MIPAAYIELLAMPISRTGKVNRKLL 733
Cdd:cd05930   420 MVPSAFVVLDALPLTPNGKVDRKAL 444
FUM14_C_NRPS-like cd19545
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ...
 874-1258 4.35e-110

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: 356.61  E-value: 4.35e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  874 IYPCTPLQEALMAYTSKRPGAFQAQFRFQLPHQLDMLRLKEAWRIVIAANPILRTRIVFCHT-GALQVVLRPgEQLQWdl 952
Cdd:cd19545     1 IYPCTPLQEGLMALTARQPGAYVGQRVFELPPDIDLARLQAAWEQVVQANPILRTRIVQSDSgGLLQVVVKE-SPISW-- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  953 inGVHTSPGSL--------MSYGVPLVDMAITNDTAGKlsRTFCLTMHHAIFDGWSYGLILGAVEDAYKHTNAVQR-PFA 1023
Cdd:cd19545    78 --TESTSLDEYleedraapMGLGGPLVRLALVEDPDTE--RYFVWTIHHALYDGWSLPLILRQVLAAYQGEPVPQPpPFS 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1024 PFIKYILHCNYESAKHFWCSEFKDMQALPFPVPPLSRgHMANSSTTTHRQIHVSEWLSSYCTPSTIIQLAFTLLIAWRTE 1103
Cdd:cd19545   154 RFVKYLRQLDDEAAAEFWRSYLAGLDPAVFPPLPSSR-YQPRPDATLEHSISLPSSASSGVTLATVLRAAWALVLSRYTG 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1104 SMDVLFGLTVTGRNAPVAGIHRTTGPTIATFPLRTILYGTMNITDALLCMQNHIATLIPFEHTGLRRIKSFGTETARACQ 1183
Cdd:cd19545   233 SDDVVFGVTLSGRNAPVPGIEQIVGPTIATVPLRVRIDPEQSVEDFLQTVQKDLLDMIPFEHTGLQNIRRLGPDARAACN 312

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 992230864 1184 FQSLLIIQPVTYRESSEIFFELESNEHEQSK-FSTCPLTLVCELRTHSVSVKAISDNAVVISGDMERLLDQLEYLI 1258
Cdd:cd19545   313 FQTLLVVQPALPSSTSESLELGIEEESEDLEdFSSYGLTLECQLSGSGLRVRARYDSSVISEEQVERLLDQFEHVL 388
PRK12316 PRK12316
peptide synthase; Provisional
 196-1907 3.21e-103

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 371.21  E-value: 3.21e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  196 VIHSPGRPFADSCLLSKHHQDQIAE-WNRNAPIHPFDSCIHTLFRLQCILQPDAQAICAWDGTITYRQLDRLSSTVQGLL 274
Cdd:PRK12316 3020 MVENPQRSVDELAMLDAEERGQLLEaWNATAAEYPLERGVHRLFEEQVERTPDAVALAFGEQRLSYAELNRRANRLAHRL 3099

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  275 QQYDLGPGSVVPIIFKKSKWAIVAMLGVLKAGAAFCMLDQSYPTKRLVNICKDVDAKVIVCSQELSIGVSGSTLSIGDHN 354
Cdd:PRK12316 3100 IERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLLSQSHLRLPLAQGVQVLDLDR 3179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  355 TETATYSAIQAVNTASHDAAYVVYTSGSTGAPKGIVIEHGSFCTNAIASSQAQNLDRSSRVLQFASYAFDVSVHESLTPL 434
Cdd:PRK12316 3180 GDENYAEANPAIRTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTFSFDVFVEELFWPL 3259

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  435 LLGGCVCI--PSEAQRVNSLKEAVSTLRVNWVELTPTVARLWC----PADIPTVKTLVMGGEPMLPNDISLWKDKLRLVC 508
Cdd:PRK12316 3260 MSGARVVLagPEDWRDPALLVELINSEGVDVLHAYPSMLQAFLeeedAHRCTSLKRIVCGGEALPADLQQQVFAGLPLYN 3339

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  509 AYGPAECTVVSTVQSCVQELGN---IGRsPCGTCWIVSKDNHHRLMPVGCIGELIIGGPIVGRGYLKQPCLTANAFITNP 585
Cdd:PRK12316 3340 LYGPTEATITVTHWQCVEEGKDavpIGR-PIANRACYILDGSLEPVPVGALGELYLGGEGLARGYHNRPGLTAERFVPDP 3418

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  586 EWAslfhlngSYRFYKTGDLVRYNADGTIAYIGRKDTQVKLNGQRVELGEIEH--QAQPYFRDAViaaeVAAPAGRKPIl 663
Cdd:PRK12316 3419 FVP-------GERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEArlLEHPWVREAV----VLAVDGRQLV- 3486

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  664 ilfiarkyEYSVNMDCTMLLRPpsilfQEKAQgtntlLQEVLPRHMIPAAYIELLAMPISRTGKVNRKLLREAVEQASEK 743
Cdd:PRK12316 3487 --------AYVVPEDEAGDLRE-----ALKAH-----LKASLPEYMVPAHLLFLERMPLTPNGKLDRKALPRPDAALLQQ 3548

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  744 DFRAyypithndmiqlPSTPVLDQLRLLFSAALRIPEekIKPNDSFFHLGGDSVSAIRLVGDARDQGLHITVESLFKRQT 823
Cdd:PRK12316 3549 DYVA------------PVNELERRLAAIWADVLKLEQ--VGLTDNFFELGGDSIISLQVVSRARQAGIRFTPKDLFQHQT 3614

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  824 ISKLAECTH-----QMSNGigsPIPPFSLLDPLgkgtyiaqateQCSVFPEQIediypctplqealmaytSKRPGAFQAQ 898
Cdd:PRK12316 3615 IQGLARVARvgggvAVDQG---PVSGETLLLPI-----------QQQFFEEPV-----------------PERHHWNQSL 3663

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  899 FrFQLPHQLDMLRLKEAWRIVIAANPILRTRIV--FCHTGALQVVLRPGEQLQWD-----------LINGVHTS----PG 961
Cdd:PRK12316 3664 L-LKPREALDAAALEAALQALVEHHDALRLRFVedAGGWTAEHLPVELGGALLWRaelddaeelerLGEEAQRSldlaDG 3742

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  962 SLMSygVPLVDMAitndtAGklSRTFCLTMHHAIFDGWSYGLILGAVEDAYKHTNAVQRPFAPfikyilhcnyesAKhfw 1041
Cdd:PRK12316 3743 PLLR--ALLATLA-----DG--SQRLLLVIHHLVVDGVSWRILLEDLQQAYQQLLQGEAPRLP------------AK--- 3798

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1042 CSEFKDMQAlpfpvpplsrghmanssttthrqiHVSEWLSSyctPSTIIQLAFtlliaWRTESMDVlfgltvtgrnapva 1121
Cdd:PRK12316 3799 TSSFKAWAE------------------------RLQEHARG---EALKAELAY-----WQEQLQGV-------------- 3832

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1122 gihrttgptiatfplrtilygtmniTDALLCMQNHIATLIPFEHTGLRRIKSFGTEtaracqfqSLLIIQPVTYRessei 1201
Cdd:PRK12316 3833 -------------------------SSELPCDHPQGALQNRHAASVQTRLDRELTR--------RLLQQAPAAYR----- 3874

                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1202 ffelesneheqskfstcplTLVCELRthsvsVKAISDNAVVISGDMERLLdQLEylidmitksptleiqniipspqdtys 1281
Cdd:PRK12316 3875 -------------------TQVNDLL-----LTALARVVCRWTGEASALV-QLE-------------------------- 3903

                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1282 yalqqsqywsSHIEKkvydyfggDVFVLVDAivpngssNRSTAMFVCETKRRREPTETSGLFTRPtdnIRWQLQQ----- 1356
Cdd:PRK12316 3904 ----------GHGRE--------DLFADIDL-------SRTVGWFTSLFPVRLSPVEDLGASIKA---IKEQLRAipnkg 3955

                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1357 ----LISSLGQSLPRSAVPslCLPVSFIPVDPLGQPDRiylceaassmTLDFLHSLTDPVNKYIDYHILPeEARLRGIVA 1432
Cdd:PRK12316 3956 igfgLLRYLGDEESRRTLA--GLPVPRITFNYLGQFDG----------SFDEEMALFVPAGESAGAEQSP-DAPLDNWLS 4022

                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1433 HVLSIDPQNISPKddfFTLGGDSISAMQVVSLCRKHQLSLTALDIFNGRtieliaTRLMPLTPytppstpaSDRSLdrrf 1512
Cdd:PRK12316 4023 LNGRVYGGELSLD---WTFSREMFEEATIQRLADDYAAELTALVEHCCD------AERHGVTP--------SDFPL---- 4081

                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1513 sllflnSDRDMERLESLLMATydigsmDSIEDAYPCSESHQGLLqtqmLRPFYYQSYTIWEVTTRSKSSPVSPVRLCNAW 1592
Cdd:PRK12316 4082 ------AGLDQARLDALPLPL------GEIEDIYPLSPMQQGML----FHSLYEQEAGDYINQMRVDVQGLDVERFRAAW 4145

                        1450      1460      1470      1480      1490      1500      1510      1520
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1593 FTLARRHPALRTHLIDIplcDGMSSKIHVVHK---------DYMADAAILSCEDEHVITELRKPFLPSDTGLyyphaFRI 1663
Cdd:PRK12316 4146 QAALDRHDVLRSGFVWQ---GELGRPLQVVHKqvslpfaelDWRGRADLQAALDALAAAERERGFDLQRAPL-----LRL 4217

                        1530      1540      1550      1560      1570      1580      1590      1600
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1664 CQTVSGRVFCKL--EGGHAFLDATSVLIILRELAQAYDGQLSSVPGPSYSSAVAWLQSlPNGDNRMDYWRRQLKD----- 1736
Cdd:PRK12316 4218 VLVRTAEGRHHLiyTNHHILMDGWSNSQLLGEVLERYSGRPPAQPGGRYRDYIAWLQR-QDAAASEAFWREQLAAldept 4296

                        1610      1620      1630      1640      1650      1660      1670      1680
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1737 --ASPCIFPRLRDQDSPSDTLVVTeQLASTATLTPVCTRHGLTVSNVLQVAWGLMLRRYTESDDVCFGALISGRDSRIPD 1814
Cdd:PRK12316 4297 rlAQAIARADLRSANGYGEHVREL-DATATARLREFARTQRVTLNTLVQAAWLLLLQRYTGQDTVAFGATVAGRPAELPG 4375

                        1690      1700      1710      1720      1730      1740      1750      1760
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1815 VDKMVGPFFNVLVCQLRFGREDSLWDVLRRNQTEIGNRLLNQHCSLIEVLRFSTYFGQPLFNTCI-----SVEQPLSMDT 1889
Cdd:PRK12316 4376 IEGQIGLFINTLPVIATPRAQQSVVEWLQQVQRQNLALREHEHTPLYEIQRWAGQGGEALFDSLLvfenyPVSEALQQGA 4455

                        1770
                  ....*....|....*...
gi 992230864 1890 PdASLCFKELETLEPTEY 1907
Cdd:PRK12316 4456 P-GGLRFGEVTNHEQTNY 4472
PRK12316 PRK12316
peptide synthase; Provisional
 182-1168 1.78e-98

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 355.80  E-value: 1.78e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  182 ANNIISTLEQIIHcvihSPGRPFADSCLL-SKHHQDQIAEWNRNAPIHPFDSCIHTLFRLQCILQPDAQAICAWDGTITY 260
Cdd:PRK12316 1956 DRHLLHLLEQMAE----DAQAALGELALLdAGERQRILADWDRTPEAYPRGPGVHQRIAEQAARAPEAIAVVFGDQHLSY 2031

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  261 RQLDRLSSTVQGLLQQYDLGPGSVVPIIFKKSKWAIVAMLGVLKAGAAFCMLDQSYPTKRLVNICKDVDAKVIVC----S 336
Cdd:PRK12316 2032 AELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLTqrhlL 2111

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  337 QELSIGVSGSTLSIgDHNTETATY-SAIQAVNTASHDAAYVVYTSGSTGAPKGIVIEHGSFCTNAIASSQAQNLDRSSRV 415
Cdd:PRK12316 2112 ERLPLPAGVARLPL-DRDAEWADYpDTAPAVQLAGENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERYELSPADCE 2190

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  416 LQFASYAFDVSVHESLTPLLLGGCVCIPSEAQR-----VNSLKE-AVSTLR---VNWVELTPTVARLWCPadiPTVKTLV 486
Cdd:PRK12316 2191 LQFMSFSFDGAHEQWFHPLLNGARVLIRDDELWdpeqlYDEMERhGVTILDfppVYLQQLAEHAERDGRP---PAVRVYC 2267

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  487 MGGEPMLPNDISLWKDKLR---LVCAYGPAECTVVSTVQSC-VQELGNIGRSPCGT------CWIVSKDNHhrLMPVGCI 556
Cdd:PRK12316 2268 FGGEAVPAASLRLAWEALRpvyLFNGYGPTEAVVTPLLWKCrPQDPCGAAYVPIGRalgnrrAYILDADLN--LLAPGMA 2345

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  557 GELIIGGPIVGRGYLKQPCLTANAFITNPewaslFHLNGSyRFYKTGDLVRYNADGTIAYIGRKDTQVKLNGQRVELGEI 636
Cdd:PRK12316 2346 GELYLGGEGLARGYLNRPGLTAERFVPDP-----FSASGE-RLYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEI 2419

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  637 EH--QAQPYFRDAVIAAEvAAPAGRKPIlilfiarkyEYSVNMDCTMLLRppsilfqekaQGTNTLLQEVLPRHMIPAAY 714
Cdd:PRK12316 2420 EArlQAHPAVREAVVVAQ-DGASGKQLV---------AYVVPDDAAEDLL----------AELRAWLAARLPAYMVPAHW 2479

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  715 IELLAMPISRTGKVNRKLL-REAVEQASekdfRAYYPithndmiqlPSTPVLDQLRLLFSAALRIpeEKIKPNDSFFHLG 793
Cdd:PRK12316 2480 VVLERLPLNPNGKLDRKALpKPDVSQLR----QAYVA---------PQEGLEQRLAAIWQAVLKV--EQVGLDDHFFELG 2544

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  794 GDSVSAIRLVGDAR-DQGLHITVESLFKRQTISKLAECTHQMSNGIGSPIPPFSLLDPLgkgtyIAQATEQCSVFPEQIE 872
Cdd:PRK12316 2545 GHSLLATQVVSRVRqDLGLEVPLRILFERPTLAAFAASLESGQTSRAPVLQKVTRVQPL-----PLSHAQQRQWFLWQLE 2619

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  873 DIYPCTPLQEAL----MAYTSKRPGAFQAQFRFQLPHQLDMLRLKEAWRIVIAANPILRTRIVFCHTGALQVVLRPGE-- 946
Cdd:PRK12316 2620 PESAAYHLPSALhlrgVLDQAALEQAFDALVLRHETLRTRFVEVGEQTRQVILPNMSLRIVLEDCAGVADAAIRQRVAee 2699

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  947 -QLQWDLINGvhtspgslmsygvPLVDMAITNDTAGklSRTFCLTMHHAIFDGWSYGLILGAVEDAYKHTNAVQRPFAPF 1025
Cdd:PRK12316 2700 iQRPFDLARG-------------PLLRVRLLALDGQ--EHVLVITQHHIVSDGWSMQVMVDELVQAYAGARRGEQPTLPP 2764

                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1026 IKyILHCNYESAKHFWCSEFKDMQALPF---------PVPPLSRGHmANSSTTTHRQIHVSEWL-------------SSY 1083
Cdd:PRK12316 2765 LP-LQYADYAAWQRAWMDSGEGARQLDYwrerlggeqPVLELPLDR-PRPALQSHRGARLDVALdvalsrellalarREG 2842

                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1084 CTPSTIIQLAFTLLIAWRTESMDVLFGLTVTGRNAPvaGIHRTTGPTIATFPLRTILYGTMNITDALLCMQNHIATLIPF 1163
Cdd:PRK12316 2843 VTLFMLLLASFQVLLHRYSGQSDIRVGVPIANRNRA--ETERLIGFFVNTQVLRAQVDAQLAFRDLLGQVKEQALGAQAH 2920


                  ....*
gi 992230864 1164 EHTGL 1168
Cdd:PRK12316 2921 QDLPF 2925
PRK12467 PRK12467
peptide synthase; Provisional
 40-830 1.92e-98

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 355.62  E-value: 1.92e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864   40 EFSPEVKVEQDTtsLYQTllvAWSILLAEYTDSNNVSFGVF----PCEGSDIS--------------------SVQQWEA 95
Cdd:PRK12467 2874 EFARRHRVTLNT--LVQG---AWLLLLQRFTGQDTVCFGATvagrPAQLRGAEqqlglfintlpviaspraeqTVSDWLQ 2948

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864   96 AIEPQlpisdGVTLR---HT-----RRWllEDSARHELFNTCIVLST--------NASPEASQFKSLQSIEKLGDIILLV 159
Cdd:PRK12467 2949 QVQAQ-----NLALRefeHTpladiQRW--AGQGGEALFDSILVFENypisealkQGAPSGLRFGAVSSREQTNYPLTLA 3021

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  160 DLLSPLLKLSLQYVPSALHNAHANNIISTLEQIIHCVIHSPGRPFADSCLLSKHHQDQIAE-WNRNAPIHPFDSCIHTLF 238
Cdd:PRK12467 3022 VGLGDTLELEFSYDRQHFDAAAIERLAESFDRLLQAMLNNPAARLGELPTLAAHERRQVLHaWNATAAAYPSERLVHQLI 3101

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  239 RLQCILQPDAQAICAWDGTITYRQLDRLSSTVQGLLQQYDLGPGSVVPIIFKKSKWAIVAMLGVLKAGAAFCMLDQSYPT 318
Cdd:PRK12467 3102 EAQVARTPEAPALVFGDQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPR 3181

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  319 KRLVNICKDVDAKVIVCSQ----ELSIGVSGSTLSIgDHNTETATYSAIQAVNTASHDAAYVVYTSGSTGAPKGIVIEHG 394
Cdd:PRK12467 3182 ERLAYMIEDSGVKLLLTQAhlleQLPAPAGDTALTL-DRLDLNGYSENNPSTRVMGENLAYVIYTSGSTGKPKGVGVRHG 3260

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  395 SFCTNAIASSQAQNLDRSSRVLQFASYAFDVSVHESLTPLLLGGCVCI-PSEAQRVNSLKEAVSTLRVNWVELTPTVARL 473
Cdd:PRK12467 3261 ALANHLCWIAEAYELDANDRVLLFMSFSFDGAQERFLWTLICGGCLVVrDNDLWDPEELWQAIHAHRISIACFPPAYLQQ 3340

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  474 WC----PADIPTVKTLVMGGEPMLPNDISLWKDKLRLVC---AYGPAECTVVSTVQSCVQELGN------IGRSPCG-TC 539
Cdd:PRK12467 3341 FAedagGADCASLDIYVFGGEAVPPAAFEQVKRKLKPRGltnGYGPTEAVVTVTLWKCGGDAVCeapyapIGRPVAGrSI 3420

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  540 WIVskDNHHRLMPVGCIGELIIGGPIVGRGYLKQPCLTANAFITNPewaslFHLNGSyRFYKTGDLVRYNADGTIAYIGR 619
Cdd:PRK12467 3421 YVL--DGQLNPVPVGVAGELYIGGVGLARGYHQRPSLTAERFVADP-----FSGSGG-RLYRTGDLARYRADGVIEYLGR 3492

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  620 KDTQVKLNGQRVELGEIEH--QAQPYFRDAVIAAeVAAPAGRKPIlilfiarkyEYSVnmdctmllrpPSILFQEKAQGT 697
Cdd:PRK12467 3493 IDHQVKIRGFRIELGEIEArlLQHPSVREAVVLA-RDGAGGKQLV---------AYVV----------PADPQGDWRETL 3552

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  698 NTLLQEVLPRHMIPAAYIELLAMPISRTGKVNRKllreAVEQASEKDFRAYypithndmiQLPSTPVLDQLRLLFSAALR 777
Cdd:PRK12467 3553 RDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDRK----ALPDPDAKGSREY---------VAPRSEVEQQLAAIWADVLG 3619

                         810       820       830       840       850
                  ....*....|....*....|....*....|....*....|....*....|....
gi 992230864  778 IpeEKIKPNDSFFHLGGDSVSAIRLVGDARDQ-GLHITVESLFKRQTISKLAEC 830
Cdd:PRK12467 3620 V--EQVGVTDNFFELGGDSLLALQVLSRIRQSlGLKLSLRDLMSAPTIAELAGY 3671
PRK12467 PRK12467
peptide synthase; Provisional
 189-1028 2.93e-97

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 351.77  E-value: 2.93e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  189 LEQIIHCVIHSPGRPFAD-SCLLSKHHQDQIAEWNRNAPIHPFDsCIHTLFRLQCILQPDAQAICAWDGTITYRQLDRLS 267
Cdd:PRK12467  469 WRNLLEAIVAEPRRRLGElPLLDAEERARELVRWNAPATEYAPD-CVHQLIEAQARQHPERPALVFGEQVLSYAELNRQA 547

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  268 STVQGLLQQYDLGPGSVVPIIFKKSKWAIVAMLGVLKAGAAFCMLDQSYPTKRLVNICKDVDAKVIVCSQE----LSIGV 343
Cdd:PRK12467  548 NRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQSHllaqLPVPA 627

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  344 SGSTLSIGDHNTETATYSAIQ-AVNTASHDAAYVVYTSGSTGAPKGIVIEHGSFCTNAIASSQAQNLDRSSRVLQFASYA 422
Cdd:PRK12467  628 GLRSLCLDEPADLLCGYSGHNpEVALDPDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSMLMVSTFA 707

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  423 FDVSVHESLTPLLLGGCVCI--PSEAQRVNSLKEAVSTLRVNWVELTPTVARLW----CPADIPTVKTLVMGGEPMLPND 496
Cdd:PRK12467  708 FDLGVTELFGALASGATLHLlpPDCARDAEAFAALMADQGVTVLKIVPSHLQALlqasRVALPRPQRALVCGGEALQVDL 787

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  497 ISLWK---DKLRLVCAYGPAECTVVSTVQSCVQELGNIGRSPCG-----TCWIVSkDNHHRLMPVGCIGELIIGGPIVGR 568
Cdd:PRK12467  788 LARVRalgPGARLINHYGPTETTVGVSTYELSDEERDFGNVPIGqplanLGLYIL-DHYLNPVPVGVVGELYIGGAGLAR 866

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  569 GYLKQPCLTANAFITNPewaslFHLNGSyRFYKTGDLVRYNADGTIAYIGRKDTQVKLNGQRVELGEIEH--QAQPYFRD 646
Cdd:PRK12467  867 GYHRRPALTAERFVPDP-----FGADGG-RLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEArlLAQPGVRE 940

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  647 AVIaaeVAAPAGRKPILILFiarkyeysvnmdCTMLLRPPSILFQEKAQGTNTLLQEVLPRHMIPAAYIELLAMPISRTG 726
Cdd:PRK12467  941 AVV---LAQPGDAGLQLVAY------------LVPAAVADGAEHQATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNG 1005

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  727 KVNRKLLREAVEQASEKDFRAyypithndmiqlPSTPVLDQLRLLFSAALRIpeEKIKPNDSFFHLGGDSVSAIRLVGDA 806
Cdd:PRK12467 1006 KLDRKALPKPDASAVQATFVA------------PQTELEKRLAAIWADVLKV--ERVGLTDNFFELGGHSLLATQVISRV 1071

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  807 RDQ-GLHITVESLFKRQTISKLAECTHQMSNGIGSPIPPFSLLDPLgKGTYiAQATEQcsvFPEQIEdiypctplqealm 885
Cdd:PRK12467 1072 RQRlGIQVPLRTLFEHQTLAGFAQAVAAQQQGAQPALPDVDRDQPL-PLSY-AQERQW---FLWQLE------------- 1133

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  886 aytskrPG--AFQAQFRFQLPHQLDMLRLKEAWRIVIAANPILRTRIVFcHTGALQVVLRPGEQLQWDL-INGVHTSPGS 962
Cdd:PRK12467 1134 ------PGsaAYHIPQALRLKGPLDIEALERSFDALVARHESLRTTFVQ-EDGRTRQVIHPVGSLTLEEpLLLAADKDEA 1206

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  963 LMSYGVPLVDMAITNDTAGKLSR-----------TFCLTMHHAIFDGWSYGLI---LGAVEDAYKHTNAVQRPFAPfIKY 1028
Cdd:PRK12467 1207 QLKVYVEAEARQPFDLEQGPLLRvgllrlaadehVLVLTLHHIVSDGWSMQVLvdeLVALYAAYSQGQSLQLPALP-IQY 1285
A_NRPS_PvdJ-like cd17649
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ...
 246-734 2.60e-96

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: 319.31  E-value: 2.60e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  246 PDAQAICAWDGTITYRQLDRLSSTVQGLLQQYDLGPGSVVPIIFKKSKWAIVAMLGVLKAGAAFCMLDQSYPTKRLVNIC 325
Cdd:cd17649     1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  326 KDvdakvivcsqelsigvSGSTLSIGDHntetatysaiqavntaSHDAAYVVYTSGSTGAPKGIVIEHGSFCTNAIASSQ 405
Cdd:cd17649    81 ED----------------SGAGLLLTHH----------------PRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQATAE 128

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  406 AQNLDRSSRVLQFASYAFDVSVHESLTPLLLGGCVCIPSEAQ--RVNSLKEAVSTLRVNWVELTPTVARLW-------CP 476
Cdd:cd17649   129 RYGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDELwaSADELAEMVRELGVTVLDLPPAYLQQLaeeadrtGD 208

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  477 ADIPTVKTLVMGGEPMLPNDISLW-KDKLRLVCAYGPAECTVVSTVQSCVQELGNIG-RSPCGT------CWIVskDNHH 548
Cdd:cd17649   209 GRPPSLRLYIFGGEALSPELLRRWlKAPVRLFNAYGPTEATVTPLVWKCEAGAARAGaSMPIGRplggrsAYIL--DADL 286

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  549 RLMPVGCIGELIIGGPIVGRGYLKQPCLTANAFITNPewaslFHLNGSyRFYKTGDLVRYNADGTIAYIGRKDTQVKLNG 628
Cdd:cd17649   287 NPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDP-----FGAPGS-RLYRTGDLARWRDDGVIEYLGRVDHQVKIRG 360

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  629 QRVELGEIEH--QAQPYFRDAVIAAEVAAPAGRkpiLILFIArkyeysvnmdctmlLRPPSILfQEKAQGTNTLLQEVLP 706
Cdd:cd17649   361 FRIELGEIEAalLEHPGVREAAVVALDGAGGKQ---LVAYVV--------------LRAAAAQ-PELRAQLRTALRASLP 422

                         490       500
                  ....*....|....*....|....*...
gi 992230864  707 RHMIPAAYIELLAMPISRTGKVNRKLLR 734
Cdd:cd17649   423 DYMVPAHLVFLARLPLTPNGKLDRKALP 450
A_NRPS_CmdD_like cd17652
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ...
 246-733 4.86e-95

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: 314.96  E-value: 4.86e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  246 PDAQAICAWDGTITYRQLDRLSSTVQGLLQQYDLGPGSVVPIIFKKSKWAIVAMLGVLKAGAAFCMLDQSYPTKRLVNIC 325
Cdd:cd17652     1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  326 KDVDAKVIVcsqelsigvsgstlsigdhntetatysaiqavnTASHDAAYVVYTSGSTGAPKGIVIEHGSFCTNAIASSQ 405
Cdd:cd17652    81 ADARPALLL---------------------------------TTPDNLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQIA 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  406 AQNLDRSSRVLQFASYAFDVSVHESLTPLLLGGCVCIPSEAQRV--NSLKEAVSTLRVNWVELTPTVARLWCPADIPTVK 483
Cdd:cd17652   128 AFDVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELLpgEPLADLLREHRITHVTLPPAALAALPPDDLPDLR 207

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  484 TLVMGGEPMLPNDISLWKDKLRLVCAYGPAECTVVSTVQSCVQELGN--IGRSPCGT-CWIVskDNHHRLMPVGCIGELI 560
Cdd:cd17652   208 TLVVAGEACPAELVDRWAPGRRMINAYGPTETTVCATMAGPLPGGGVppIGRPVPGTrVYVL--DARLRPVPPGVPGELY 285

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  561 IGGPIVGRGYLKQPCLTANAFITNPewaslFHLNGSyRFYKTGDLVRYNADGTIAYIGRKDTQVKLNGQRVELGEIEH-- 638
Cdd:cd17652   286 IAGAGLARGYLNRPGLTAERFVADP-----FGAPGS-RMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAal 359

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  639 QAQPYFRDAVIAAEVAAPAGRkpililfiaRKYEYSVNMDCTmllRPPsilfqekAQGTNTLLQEVLPRHMIPAAYIELL 718
Cdd:cd17652   360 TEHPGVAEAVVVVRDDRPGDK---------RLVAYVVPAPGA---APT-------AAELRAHLAERLPGYMVPAAFVVLD 420

                         490
                  ....*....|....*
gi 992230864  719 AMPISRTGKVNRKLL 733
Cdd:cd17652   421 ALPLTPNGKLDRRAL 435
A_NRPS_VisG_like cd17651
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ...
 238-734 1.42e-94

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: 315.82  E-value: 1.42e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  238 FRLQCILQPDAQAICAWDGTITYRQLDRLSSTVQGLLQQYDLGPGSVVPIIFKKSKWAIVAMLGVLKAGAAFCMLDQSYP 317
Cdd:cd17651     1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  318 TKRLVNICKDVDAKVIVCSQELSIGVSGS--TLSIGDHNTETATYSAIQAVNTASHDAAYVVYTSGSTGAPKGIVIEHGS 395
Cdd:cd17651    81 AERLAFMLADAGPVLVLTHPALAGELAVElvAVTLLDQPGAAAGADAEPDPALDADDLAYVIYTSGSTGRPKGVVMPHRS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  396 FcTNAIA-SSQAQNLDRSSRVLQFASYAFDVSVHESLTPLLLGGCVCIPSEAQRVNS--LKEAVSTLRVNWVELTPTVAR 472
Cdd:cd17651   161 L-ANLVAwQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEVRTDPpaLAAWLDEQRISRVFLPTVALR 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  473 LWC------PADIPTVKTLVMGGEPmLPNDISL-----WKDKLRLVCAYGPAECTVVsTVQSCVQELGN------IGRsP 535
Cdd:cd17651   240 ALAehgrplGVRLAALRYLLTGGEQ-LVLTEDLrefcaGLPGLRLHNHYGPTETHVV-TALSLPGDPAAwpapppIGR-P 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  536 CGTCWIVSKDNHHRLMPVGCIGELIIGGPIVGRGYLKQPCLTANAFITNPEwaslfhlNGSYRFYKTGDLVRYNADGTIA 615
Cdd:cd17651   317 IDNTRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPF-------VPGARMYRTGDLARWLPDGELE 389

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  616 YIGRKDTQVKLNGQRVELGEIEHQ--AQPYFRDAVIAAEVAAPAGRKpiLILFIARKYEYSVnmdctmllrPPSILfqeK 693
Cdd:cd17651   390 FLGRADDQVKIRGFRIELGEIEAAlaRHPGVREAVVLAREDRPGEKR--LVAYVVGDPEAPV---------DAAEL---R 455

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|.
gi 992230864  694 AQgtntlLQEVLPRHMIPAAYIELLAMPISRTGKVNRKLLR 734
Cdd:cd17651   456 AA-----LATHLPEYMVPSAFVLLDALPLTPNGKLDRRALP 491
A_NRPS_Bac cd17655
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ...
 237-736 2.60e-91

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: 306.56  E-value: 2.60e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  237 LFRLQCILQPDAQAICAWDGTITYRQLDRLSSTVQGLLQQYDLGPGSVVPIIFKKSKWAIVAMLGVLKAGAAFCMLDQSY 316
Cdd:cd17655     2 LFEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  317 PTKRLVNICKDVDAKVIVCSQELSIGV--SGSTLSIGDHNTETATYSAIQAVNTAShDAAYVVYTSGSTGAPKGIVIEHG 394
Cdd:cd17655    82 PEERIQYILEDSGADILLTQSHLQPPIafIGLIDLLDEDTIYHEESENLEPVSKSD-DLAYVIYTSGSTGKPKGVMIEHR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  395 SFCTNAIASSQAQNLDRSSRVLQFASYAFDVSVHESLTPLLLGGCVCIPSEAQRVN--SLKEAVSTLRVNWVELTPTVAR 472
Cdd:cd17655   161 GVVNLVEWANKVIYQGEHLRVALFASISFDASVTEIFASLLSGNTLYIVRKETVLDgqALTQYIRQNRITIIDLTPAHLK 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  473 LWCPADI---PTVKTLVMGGEPMLPNDISLWKDKLRLVC----AYGPAECTVVSTVQSCVQELGNIGRSPCGT------C 539
Cdd:cd17655   241 LLDAADDsegLSLKHLIVGGEALSTELAKKIIELFGTNPtitnAYGPTETTVDASIYQYEPETDQQVSVPIGKplgntrI 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  540 WIVskDNHHRLMPVGCIGELIIGGPIVGRGYLKQPCLTANAFITNPewaslFHLNGsyRFYKTGDLVRYNADGTIAYIGR 619
Cdd:cd17655   321 YIL--DQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDP-----FVPGE--RMYRTGDLARWLPDGNIEFLGR 391

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  620 KDTQVKLNGQRVELGEIEHQAQ--PYFRDAVIaaevaapagrkpililfIARKYEYSVNMDCTMLLRPPSIlfqeKAQGT 697
Cdd:cd17655   392 IDHQVKIRGYRIELGEIEARLLqhPDIKEAVV-----------------IARKDEQGQNYLCAYIVSEKEL----PVAQL 450

                         490       500       510
                  ....*....|....*....|....*....|....*....
gi 992230864  698 NTLLQEVLPRHMIPAAYIELLAMPISRTGKVNRKLLREA 736
Cdd:cd17655   451 REFLARELPDYMIPSYFIKLDEIPLTPNGKVDRKALPEP 489
PRK12316 PRK12316
peptide synthase; Provisional
 200-829 3.22e-91

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 332.31  E-value: 3.22e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  200 PGRPFADSCLLSKHHQDQI-AEWNRNAPIHPFDSCIHTLFRLQCILQPDAQAICAWDGTITYRQLDRLSSTVQGLLQQYD 278
Cdd:PRK12316 4518 PQRRLGELQLLEKAEQQRIvALWNRTDAGYPATRCVHQLVAERARMTPDAVAVVFDEEKLTYAELNRRANRLAHALIARG 4597

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  279 LGPGSVVPIIFKKSKWAIVAMLGVLKAGAAFCMLDQSYPTKRLVNICKDVDAKVIVC----SQELSIGVSGSTLSIgDHN 354
Cdd:PRK12316 4598 VGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSGAALLLTqshlLQRLPIPDGLASLAL-DRD 4676

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  355 TETATYSAIQ-AVNTASHDAAYVVYTSGSTGAPKGIVIEHGSFCTNAIASSQAQNLDRSSRVLQFASYAFDVSVHESLTP 433
Cdd:PRK12316 4677 EDWEGFPAHDpAVRLHPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSFSFDGSHEGLYHP 4756

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  434 LLLGGCVCIPSEAQRV-NSLKEAVSTLRVNWVELTPTVARLWC-----PADIPTVKTLVMGGEPMLPNDISLWKDKL--- 504
Cdd:PRK12316 4757 LINGASVVIRDDSLWDpERLYAEIHEHRVTVLVFPPVYLQQLAehaerDGEPPSLRVYCFGGEAVAQASYDLAWRALkpv 4836

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  505 RLVCAYGPAECTVVSTVQS------CVQELGNIGRsPCGTCWIVSKDNHHRLMPVGCIGELIIGGPIVGRGYLKQPCLTA 578
Cdd:PRK12316 4837 YLFNGYGPTETTVTVLLWKardgdaCGAAYMPIGT-PLGNRSGYVLDGQLNPLPVGVAGELYLGGEGVARGYLERPALTA 4915

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  579 NAFITNPewaslFHLNGSyRFYKTGDLVRYNADGTIAYIGRKDTQVKLNGQRVELGEIEH--QAQPYFRDAVIAAeVAAP 656
Cdd:PRK12316 4916 ERFVPDP-----FGAPGG-RLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEArlREHPAVREAVVIA-QEGA 4988

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  657 AGRKPIlilfiarkyEYSVNMDCTMLlrPPSILFQEKAQGTNTLLQEVLPRHMIPAAYIELLAMPISRTGKVNRKLLREA 736
Cdd:PRK12316 4989 VGKQLV---------GYVVPQDPALA--DADEAQAELRDELKAALRERLPEYMVPAHLVFLARMPLTPNGKLDRKALPQP 5057

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  737 veQASEKDfRAYYPithndmiqlPSTPVLDQLRLLFSAALRIpeEKIKPNDSFFHLGGDSVSAIRLVGDARDQ-GLHITV 815
Cdd:PRK12316 5058 --DASLLQ-QAYVA---------PRSELEQQVAAIWAEVLQL--ERVGLDDNFFELGGHSLLAIQVTSRIQLElGLELPL 5123

                         650
                  ....*....|....
gi 992230864  816 ESLFKRQTISKLAE 829
Cdd:PRK12316 5124 RELFQTPTLAAFVE 5137
PRK12467 PRK12467
peptide synthase; Provisional
 191-1019 4.46e-91

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 331.74  E-value: 4.46e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  191 QIIHCVIHSPGRPFADSCLLSKHHQDQIAE-WNRNAPIHPFDSCIHTLFRLQCILQPDAQAICAWDGTITYRQLDRLSST 269
Cdd:PRK12467 1532 NLLQGLVADPERRLGELDLLDEAERRQILEgWNATHTGYPLARLVHQLIEDQAAATPEAVALVFGEQELTYGELNRRANR 1611

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  270 VQGLLQQYDLGPGSVVPIIFKKSKWAIVAMLGVLKAGAAFCMLDQSYPTKRLVNICKDVDAKVIVCS----QELSIGVSG 345
Cdd:PRK12467 1612 LAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLTQshlqARLPLPDGL 1691

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  346 STLSIGDHNTETATYSAIQ-AVNTASHDAAYVVYTSGSTGAPKGIVIEHGSFCTNAIASSQAQNLDRSSRVLQFASYAFD 424
Cdd:PRK12467 1692 RSLVLDQEDDWLEGYSDSNpAVNLAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAADVVLQFTSFAFD 1771

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  425 VSVHESLTPLLLGGCVCI--PSEAQRVNSLKEAVSTLRVNWVELTPTV--ARLWCPADI---PTVKTLVMGGEPMLPNDI 497
Cdd:PRK12467 1772 VSVWELFWPLINGARLVIapPGAHRDPEQLIQLIERQQVTTLHFVPSMlqQLLQMDEQVehpLSLRRVVCGGEALEVEAL 1851

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  498 SLWKDKLR---LVCAYGPAECTVVSTVQSC-VQELGNIGRSPCGT-----CWIVsKDNHHRLMPVGCIGELIIGGPIVGR 568
Cdd:PRK12467 1852 RPWLERLPdtgLFNLYGPTETAVDVTHWTCrRKDLEGRDSVPIGQpianlSTYI-LDASLNPVPIGVAGELYLGGVGLAR 1930

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  569 GYLKQPCLTANAFITNPewaslFHLNGSyRFYKTGDLVRYNADGTIAYIGRKDTQVKLNGQRVELGEIEH--QAQPYFRD 646
Cdd:PRK12467 1931 GYLNRPALTAERFVADP-----FGTVGS-RLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEArlREQGGVRE 2004

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  647 AVIAAeVAAPAGRkpiliLFIArkyeYSVNMDctmllrpPSILFQEKAQGT--NTL---LQEVLPRHMIPAAYIELLAMP 721
Cdd:PRK12467 2005 AVVIA-QDGANGK-----QLVA----YVVPTD-------PGLVDDDEAQVAlrAILknhLKASLPEYMVPAHLVFLARMP 2067

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  722 ISRTGKVNRKLLREAVEQASEKDFRAyypithndmiqlPSTPVLDQLRLLFSAALRIpeEKIKPNDSFFHLGGDSVSAIR 801
Cdd:PRK12467 2068 LTPNGKLDRKALPAPDASELQQAYVA------------PQSELEQRLAAIWQDVLGL--EQVGLHDNFFELGGDSIISIQ 2133

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  802 LVGDARDQGLHITVESLFKRQTISKLAECTHQMSNGIG---SPIPPFSLLDPLgKGTYIAQATEQ-----CSVFPEQIED 873
Cdd:PRK12467 2134 VVSRARQAGIRFTPKDLFQHQTVQSLAAVAQEGDGTVSidqGPVTGDLPLLPI-QQMFFADDIPErhhwnQSVLLEPREA 2212

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  874 IYPcTPLQEALMAYT----------SKRPGAFQAQFRFQLPHQLDMLrlkeaWRIVIAAnpilrtrivfchTGALQVVlr 943
Cdd:PRK12467 2213 LDA-ELLEAALQALLvhhdalrlgfVQEDGGWSAMHRAPEQERRPLL-----WQVVVAD------------KEELEAL-- 2272

                         810       820       830       840       850       860       870
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 992230864  944 pGEQLQ--WDLINGvhtspgslmsygvPLVDMAITNDTAGklSRTFCLTMHHAIFDGWSYGLILGAVEDAYKHTNAVQ 1019
Cdd:PRK12467 2273 -CEQAQrsLDLEEG-------------PLLRAVLATLPDG--SQRLLLVIHHLVVDGVSWRILLEDLQTAYRQLQGGQ 2334
A_NRPS_Srf_like cd12117
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ...
 237-733 7.59e-91

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: 304.89  E-value: 7.59e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  237 LFRLQCILQPDAQAICAWDGTITYRQLDRLSSTVQGLLQQYDLGPGSVVPIIFKKSKWAIVAMLGVLKAGAAFCMLDQSY 316
Cdd:cd12117     2 LFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPEL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  317 PTKRLVNICKDVDAKVIVCSQELSIGVSG-STLSIGDHNTETATYSAIQAVNTAsHDAAYVVYTSGSTGAPKGIVIEHGS 395
Cdd:cd12117    82 PAERLAFMLADAGAKVLLTDRSLAGRAGGlEVAVVIDEALDAGPAGNPAVPVSP-DDLAYVMYTSGSTGRPKGVAVTHRG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  396 -----FCTNAIAssqaqnLDRSSRVLQFASYAFDVSVHESLTPLLLGGCVCI--PSEAQRVNSLKEAVSTLRVNWVELTP 468
Cdd:cd12117   161 vvrlvKNTNYVT------LGPDDRVLQTSPLAFDASTFEIWGALLNGARLVLapKGTLLDPDALGALIAEEGVTVLWLTA 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  469 TVARLWC---PADIPTVKTLVMGGEPMLPNDISLWKDK---LRLVCAYGPAECTVVSTVQSCVQELGNIGRSPCG----- 537
Cdd:cd12117   235 ALFNQLAdedPECFAGLRELLTGGEVVSPPHVRRVLAAcpgLRLVNGYGPTENTTFTTSHVVTELDEVAGSIPIGrpian 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  538 -TCWIVskDNHHRLMPVGCIGELIIGGPIVGRGYLKQPCLTANAFITNPewaslfHLNGSyRFYKTGDLVRYNADGTIAY 616
Cdd:cd12117   315 tRVYVL--DEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADP------FGPGE-RLYRTGDLARWLPDGRLEF 385

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  617 IGRKDTQVKLNGQRVELGEIEHQ--AQPYFRDAVIAAEVAAPaGRKPILILFIARkyeysvnmdctmllRPPSilfqekA 694
Cdd:cd12117   386 LGRIDDQVKIRGFRIELGEIEAAlrAHPGVREAVVVVREDAG-GDKRLVAYVVAE--------------GALD------A 444

                         490       500       510
                  ....*....|....*....|....*....|....*....
gi 992230864  695 QGTNTLLQEVLPRHMIPAAYIELLAMPISRTGKVNRKLL 733
Cdd:cd12117   445 AELRAFLRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
A_NRPS_Ta1_like cd12116
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ...
 246-733 1.64e-89

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: 300.36  E-value: 1.64e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  246 PDAQAICAWDGTITYRQLDRLSSTVQGLLQQYDLGPGSVVPIIFKKSKWAIVAMLGVLKAGAAFCMLDQSYPTKRLVNIC 325
Cdd:cd12116     1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  326 KDVDAKVIVCSQELSIGVSGSTLSIGDHNtETATYSAIQAVNTAS-HDAAYVVYTSGSTGAPKGIVIEHGSFcTNAIASS 404
Cdd:cd12116    81 EDAEPALVLTDDALPDRLPAGLPVLLLAL-AAAAAAPAAPRTPVSpDDLAYVIYTSGSTGRPKGVVVSHRNL-VNFLHSM 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  405 QAQ-NLDRSSRVLQFASYAFDVSVHESLTPLLLGGCVCI-PSEAQR-VNSLKEAVSTLRVNWVELTPTVARL-----WCP 476
Cdd:cd12116   159 RERlGLGPGDRLLAVTTYAFDISLLELLLPLLAGARVVIaPRETQRdPEALARLIEAHSITVMQATPATWRMlldagWQG 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  477 AdiPTVKTLVmGGEPmLPNDIslwKDKL-----RLVCAYGPAECTVVSTVQSCVQELG--NIGRSPCGT-CWIVskDNHH 548
Cdd:cd12116   239 R--AGLTALC-GGEA-LPPDL---AARLlsrvgSLWNLYGPTETTIWSTAARVTAAAGpiPIGRPLANTqVYVL--DAAL 309

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  549 RLMPVGCIGELIIGGPIVGRGYLKQPCLTANAFITNPewaslFHLNGSyRFYKTGDLVRYNADGTIAYIGRKDTQVKLNG 628
Cdd:cd12116   310 RPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDP-----FAGPGS-RLYRTGDLVRRRADGRLEYLGRADGQVKIRG 383

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  629 QRVELGEIEH--QAQPYFRDAVIaaeVAAPAGRKPILILFIARKYEYSVNMDctmLLRppsilfqekaqgtnTLLQEVLP 706
Cdd:cd12116   384 HRIELGEIEAalAAHPGVAQAAV---VVREDGGDRRLVAYVVLKAGAAPDAA---ALR--------------AHLRATLP 443

                         490       500
                  ....*....|....*....|....*..
gi 992230864  707 RHMIPAAYIELLAMPISRTGKVNRKLL 733
Cdd:cd12116   444 AYMVPSAFVRLDALPLTANGKLDRKAL 470
PRK12316 PRK12316
peptide synthase; Provisional
 214-1017 8.84e-87

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 318.05  E-value: 8.84e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  214 HQDQIAEWNRNAPIHPFDSCIHTLFRLQCILQPDAQAICAWDGTITYRQLDRLSSTVQGLLQQYDLGPGSVVPIIFKKSK 293
Cdd:PRK12316  493 RGQLVEGWNATAAEYPLQRGVHRLFEEQVERTPEAPALAFGEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSI 572

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  294 WAIVAMLGVLKAGAAFCMLDQSYPTKRLVNICKDVDAKVIVCSQ----ELSIGVSGSTLSIGDHNTETATYSAiQAVNTA 369
Cdd:PRK12316  573 EMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLSQShlgrKLPLAAGVQVLDLDRPAAWLEGYSE-ENPGTE 651

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  370 SH--DAAYVVYTSGSTGAPKGIVIEHGSFCTNAIASSQAQNLDRSSRVLQFASYAFDVSVHESLTPLLLGG--CVCIPSE 445
Cdd:PRK12316  652 LNpeNLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGArlVVAAPGD 731

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  446 AQRVNSLKEAVSTLRVNWVELTPTVARLWC----PADIPTVKTLVMGGEPmLPNDISLW----KDKLRLVCAYGPAECTV 517
Cdd:PRK12316  732 HRDPAKLVELINREGVDTLHFVPSMLQAFLqdedVASCTSLRRIVCSGEA-LPADAQEQvfakLPQAGLYNLYGPTEAAI 810

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  518 VSTVQSCVQELGN---IGRSPCGT-CWIVskDNHHRLMPVGCIGELIIGGPIVGRGYLKQPCLTANAFITNPewaslfHL 593
Cdd:PRK12316  811 DVTHWTCVEEGGDsvpIGRPIANLaCYIL--DANLEPVPVGVLGELYLAGRGLARGYHGRPGLTAERFVPSP------FV 882

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  594 NGSyRFYKTGDLVRYNADGTIAYIGRKDTQVKLNGQRVELGEIEH--QAQPYFRDAVIAAevaapAGRKPILilfiarky 671
Cdd:PRK12316  883 AGE-RMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEArlLEHPWVREAAVLA-----VDGKQLV-------- 948

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  672 EYSVNMDCTMLLRppsilfQEKAQGtntlLQEVLPRHMIPAAYIELLAMPISRTGKVNRKLLREAVEQASEKDFRAyypi 751
Cdd:PRK12316  949 GYVVLESEGGDWR------EALKAH----LAASLPEYMVPAQWLALERLPLTPNGKLDRKALPAPEASVAQQGYVA---- 1014

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  752 thndmiqlPSTPVLDQLRLLFSAALRIpeEKIKPNDSFFHLGGDSVSAIRLVGDARDQGLHITVESLFKRQTISKLAECT 831
Cdd:PRK12316 1015 --------PRNALERTLAAIWQDVLGV--ERVGLDDNFFELGGDSIVSIQVVSRARQAGIQLSPRDLFQHQTIRSLALVA 1084

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  832 HQmsngigspippfslldplGKGTYIAQATEQCSVfpeqiediyPCTPLQEALMAYTSKRPGAFQAQFRFQLPHQLDMLR 911
Cdd:PRK12316 1085 KA------------------GQATAADQGPASGEV---------ALAPVQRWFFEQAIPQRQHWNQSLLLQARQPLDPDR 1137

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  912 LKEAWRIVIAANPILRTRIVfCHTGALQVVLRP--GEQLQW--------DLINGVHTSPGSL-MSYG----VPLVDMAit 976
Cdd:PRK12316 1138 LGRALERLVAHHDALRLRFR-EEDGGWQQAYAApqAGEVLWqrqaaseeELLALCEEAQRSLdLEQGpllrALLVDMA-- 1214

                         810       820       830       840
                  ....*....|....*....|....*....|....*....|.
gi 992230864  977 nDTAGKLsrtfCLTMHHAIFDGWSYGLILGAVEDAYKHTNA 1017
Cdd:PRK12316 1215 -DGSQRL----LLVIHHLVVDGVSWRILLEDLQRAYADLDA 1250
A_NRPS_ApnA-like cd17644
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ...
 233-733 2.96e-86

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: 290.88  E-value: 2.96e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  233 CIHTLFRLQCILQPDAQAICAWDGTITYRQLDRLSSTVQGLLQQYDLGPGSVVPIIFKKSKWAIVAMLGVLKAGAAFCML 312
Cdd:cd17644     1 CIHQLFEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  313 DQSYPTKRLVNICKDVDAKVIVcsqelsigvsgstlsigdhntetatysaiqavnTASHDAAYVVYTSGSTGAPKGIVIE 392
Cdd:cd17644    81 DPNYPQERLTYILEDAQISVLL---------------------------------TQPENLAYVIYTSGSTGKPKGVMIE 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  393 HGSFCTNAIASSQAQNLDRSSRVLQFASYAFDVSVHEsLTPLLLGGCVCIPSEAQRVNSLKEAVSTLRVNWVE---LTPT 469
Cdd:cd17644   128 HQSLVNLSHGLIKEYGITSSDRVLQFASIAFDVAAEE-IYVTLLSGATLVLRPEEMRSSLEDFVQYIQQWQLTvlsLPPA 206

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  470 VARLWCPA------DIP-TVKTLVMGGEPMLPNDISLW----KDKLRLVCAYGPAECTVVSTVQSCVQELGN------IG 532
Cdd:cd17644   207 YWHLLVLElllstiDLPsSLRLVIVGGEAVQPELVRQWqknvGNFIQLINVYGPTEATIAATVCRLTQLTERnitsvpIG 286

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  533 RsPCGTCWIVSKDNHHRLMPVGCIGELIIGGPIVGRGYLKQPCLTANAFITNPewaslFHLNGSYRFYKTGDLVRYNADG 612
Cdd:cd17644   287 R-PIANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHP-----FNSSESERLYKTGDLARYLPDG 360

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  613 TIAYIGRKDTQVKLNGQRVELGEIEH--QAQPYFRDAVIAAEVAAPAGRKpiLILFIARKYEYSVNmdctmllrpPSILF 690
Cdd:cd17644   361 NIEYLGRIDNQVKIRGFRIELGEIEAvlSQHNDVKTAVVIVREDQPGNKR--LVAYIVPHYEESPS---------TVELR 429

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|...
gi 992230864  691 QekaqgtntLLQEVLPRHMIPAAYIELLAMPISRTGKVNRKLL 733
Cdd:cd17644   430 Q--------FLKAKLPDYMIPSAFVVLEELPLTPNGKIDRRAL 464
A_NRPS_AB3403-like cd17646
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ...
 235-733 3.38e-86

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: 291.49  E-value: 3.38e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  235 HTLFRLQCILQPDAQAICAWDGTITYRQLDRLSSTVQGLLQQYDLGPGSVVPIIFKKSKWAIVAMLGVLKAGAAFCMLDQ 314
Cdd:cd17646     1 HALVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  315 SYPTKRLVNICKDVDAKVIVCSQELSIGVSGSTLSIGDHNTETATYSA-IQAVNTASHDAAYVVYTSGSTGAPKGIVIEH 393
Cdd:cd17646    81 GYPADRLAYMLADAGPAVVLTTADLAARLPAGGDVALLGDEALAAPPAtPPLVPPRPDNLAYVIYTSGSTGRPKGVMVTH 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  394 GSFcTNAIASSQAQ-NLDRSSRVLQFASYAFDVSVHESLTPLLLGGCVCI--PSEAQRVNSLKEAVSTLRVNWVELTPTV 470
Cdd:cd17646   161 AGI-VNRLLWMQDEyPLGPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVarPGGHRDPAYLAALIREHGVTTCHFVPSM 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  471 ARLWC----PADIPTVKTLVMGGEPMLPNDISLWKDKL--RLVCAYGPAECTVVSTVQSCVQELGN----IGRS-PCGTC 539
Cdd:cd17646   240 LRVFLaepaAGSCASLRRVFCSGEALPPELAARFLALPgaELHNLYGPTEAAIDVTHWPVRGPAETpsvpIGRPvPNTRL 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  540 WIVskDNHHRLMPVGCIGELIIGGPIVGRGYLKQPCLTANAFITNPewaslfHLNGSyRFYKTGDLVRYNADGTIAYIGR 619
Cdd:cd17646   320 YVL--DDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDP------FGPGS-RMYRTGDLARWRPDGALEFLGR 390

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  620 KDTQVKLNGQRVELGEIEH--QAQPYFRDAVIAAEvAAPAGRKPILILFIARKYEYSVNMDctmllrppsilfQEKAQgt 697
Cdd:cd17646   391 SDDQVKIRGFRVEPGEIEAalAAHPAVTHAVVVAR-AAPAGAARLVGYVVPAAGAAGPDTA------------ALRAH-- 455

                         490       500       510
                  ....*....|....*....|....*....|....*.
gi 992230864  698 ntlLQEVLPRHMIPAAYIELLAMPISRTGKVNRKLL 733
Cdd:cd17646   456 ---LAERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
A_NRPS_GliP_like cd17653
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ...
 237-735 4.94e-86

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: 289.21  E-value: 4.94e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  237 LFRLQCILQPDAQAICAWDGTITYRQLDRLSSTVQGLLQQYDLGPGSVVPIIFKKSKWAIVAMLGVLKAGAAFCMLDQSY 316
Cdd:cd17653     2 AFERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  317 PTKRLVNICKDVDAKVIVCsqelsigvsgstlsigdhntetatysaiqavNTASHDAAYVVYTSGSTGAPKGIVIEHGSF 396
Cdd:cd17653    82 PSARIQAILRTSGATLLLT-------------------------------TDSPDDLAYIIFTSGSTGIPKGVMVPHRGV 130

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  397 cTNAIASSQAqNLDR--SSRVLQFASYAFDVSVHESLTPLLLGGCVCIPSEAQRVNSLKEAVSTLrvnwvELTPTVARLW 474
Cdd:cd17653   131 -LNYVSQPPA-RLDVgpGSRVAQVLSIAFDACIGEIFSTLCNGGTLVLADPSDPFAHVARTVDAL-----MSTPSILSTL 203

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  475 CPADIPTVKTLVMGGEPMLPNDISLWKDKLRLVCAYGPAECTVVSTVQSCvqELGN---IGRS-PCGTCWIVSKDNhhRL 550
Cdd:cd17653   204 SPQDFPNLKTIFLGGEAVPPSLLDRWSPGRRLYNAYGPTECTISSTMTEL--LPGQpvtIGKPiPNSTCYILDADL--QP 279

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  551 MPVGCIGELIIGGPIVGRGYLKQPCLTANAFITNPEWaslfhlNGSyRFYKTGDLVRYNADGTIAYIGRKDTQVKLNGQR 630
Cdd:cd17653   280 VPEGVVGEICISGVQVARGYLGNPALTASKFVPDPFW------PGS-RMYRTGDYGRWTEDGGLEFLGREDNQVKVRGFR 352

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  631 VELGEIEH---QAQPYFRDAviAAEVAAPAgrkpiLILFIARKyeySVNMDctmllrppsiLFQEKaqgtntlLQEVLPR 707
Cdd:cd17653   353 INLEEIEEvvlQSQPEVTQA--AAIVVNGR-----LVAFVTPE---TVDVD----------GLRSE-------LAKHLPS 405

                         490       500
                  ....*....|....*....|....*...
gi 992230864  708 HMIPAAYIELLAMPISRTGKVNRKLLRE 735
Cdd:cd17653   406 YAVPDRIIALDSFPLTANGKVDRKALRE 433
A_NRPS_Sfm_like cd12115
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ...
 234-733 2.42e-85

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: 287.68  E-value: 2.42e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  234 IHTLFRLQCILQPDAQAICAWDGTITYRQLDRLSSTVQGLLQQYDLGPGSVVPIIFKKSKWAIVAMLGVLKAGAAFCMLD 313
Cdd:cd12115     1 LHDLVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  314 QSYPTKRLVNICKDVDAKVIVcsqelsigvsgstlsigdhntetatysaiqavnTASHDAAYVVYTSGSTGAPKGIVIEH 393
Cdd:cd12115    81 PAYPPERLRFILEDAQARLVL---------------------------------TDPDDLAYVIYTSGSTGRPKGVAIEH 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  394 GsfctNAIA----SSQAQNLDRSSRVLQFASYAFDVSVHESLTPLLLGGCVCIpseAQRVNSLKEAVSTLRVNWVELTPT 469
Cdd:cd12115   128 R----NAAAflqwAAAAFSAEELAGVLASTSICFDLSVFELFGPLATGGKVVL---ADNVLALPDLPAAAEVTLINTVPS 200

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  470 VARLWCPAD-IPT-VKTLVMGGEPmLPNDISlwkDKL-------RLVCAYGPAECTVVSTVqsCVQELGN-----IGRSP 535
Cdd:cd12115   201 AAAELLRHDaLPAsVRVVNLAGEP-LPRDLV---QRLyarlqveRVVNLYGPSEDTTYSTV--APVPPGAsgevsIGRPL 274

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  536 CGT-CWIVskDNHHRLMPVGCIGELIIGGPIVGRGYLKQPCLTANAFITNPEWASLfhlngsyRFYKTGDLVRYNADGTI 614
Cdd:cd12115   275 ANTqAYVL--DRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFGPGA-------RLYRTGDLVRWRPDGLL 345

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  615 AYIGRKDTQVKLNGQRVELGEIEHQ--AQPYFRDAVIAAEVAAPAGRKpiLILFIArkyeysvnmdctmlLRPPSILFQE 692
Cdd:cd12115   346 EFLGRADNQVKVRGFRIELGEIEAAlrSIPGVREAVVVAIGDAAGERR--LVAYIV--------------AEPGAAGLVE 409

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|.
gi 992230864  693 KAQGTntlLQEVLPRHMIPAAYIELLAMPISRTGKVNRKLL 733
Cdd:cd12115   410 DLRRH---LGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
CT_NRPS-like cd19542
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ...
 1546-1951 5.39e-80

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: 270.33  E-value: 5.39e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1546 YPCSESHQGLLQTQMLRPFYYQSYTIWEVttrskSSPVSPVRLCNAWFTLARRHPALRTHLIDIPLCDGMsskIHVVHKD 1625
Cdd:cd19542     2 YPCTPMQEGMLLSQLRSPGLYFNHFVFDL-----DSSVDVERLRNAWRQLVQRHDILRTVFVESSAEGTF---LQVVLKS 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1626 YMADAAILSCEDEhVITELRKPFLPSDTGLYYP-HAFRICQTVSGRVFCKLEGGHAFLDATSVLIILRELAQAYDGQLSS 1704
Cdd:cd19542    74 LDPPIEEVETDED-SLDALTRDLLDDPTLFGQPpHRLTLLETSSGEVYLVLRISHALYDGVSLPIILRDLAAAYNGQLLP 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1705 vPGPSYSSAVAWLQSLpNGDNRMDYWRRQLKDASPCIFPRLRDQDSPSDTLVVTEqlASTATLTPVCTRHGLTVSNVLQV 1784
Cdd:cd19542   153 -PAPPFSDYISYLQSQ-SQEESLQYWRKYLQGASPCAFPSLSPKRPAERSLSSTR--RSLAKLEAFCASLGVTLASLFQA 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1785 AWGLMLRRYTESDDVCFGALISGRDSRIPDVDKMVGPFFNVLVCQLRFGREDSLWDVLRRNQTEIGNRLLNQHCSLIEVL 1864
Cdd:cd19542   229 AWALVLARYTGSRDVVFGYVVSGRDLPVPGIDDIVGPCINTLPVRVKLDPDWTVLDLLRQLQQQYLRSLPHQHLSLREIQ 308

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1865 RFST-YFGQPLFNTCISVEQ--PLSMDTPDASLCFKELETLEPTEYGIIATITIGTTDVGLGLTYKSDLLTEDQALAVAD 1941
Cdd:cd19542   309 RALGlWPSGTLFNTLVSYQNfeASPESELSGSSVFELSAAEDPTEYPVAVEVEPSGDSLKVSLAYSTSVLSEEQAEELLE 388

                         410
                  ....*....|
gi 992230864 1942 RFKMSITEIM 1951
Cdd:cd19542   389 QFDDILEALL 398
A_NRPS_Cytc1-like cd17643
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ...
 246-733 4.18e-79

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: 269.56  E-value: 4.18e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  246 PDAQAICAWDGTITYRQLDRLSSTVQGLLQQYDLGPGSVVPIIFKKSKWAIVAMLGVLKAGAAFCMLDQSYPTKRLVNIC 325
Cdd:cd17643     1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  326 KDvdakvivcsqelsigvsgstlsigdhntetatySAIQAVNTASHDAAYVVYTSGSTGAPKGIVIEHGSFCTNAIASSQ 405
Cdd:cd17643    81 AD---------------------------------SGPSLLLTDPDDLAYVIYTSGSTGRPKGVVVSHANVLALFAATQR 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  406 AQNLDRSSRVLQFASYAFDVSVHESLTPLLLGGCVCIPSEAQRVN--SLKEAVSTLRVNWVELTPTVARLWCPAD----- 478
Cdd:cd17643   128 WFGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEVARSpeDFARLLRDEGVTVLNQTPSAFYQLVEAAdrdgr 207

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  479 -IPTVKTLVMGGEPMLPNDISLW-----KDKLRLVCAYGPAECTVVSTVQ------SCVQELGNIGRsPCGTCWIVSKDN 546
Cdd:cd17643   208 dPLALRYVIFGGEALEAAMLRPWagrfgLDRPQLVNMYGITETTVHVTFRpldaadLPAAAASPIGR-PLPGLRVYVLDA 286

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  547 HHRLMPVGCIGELIIGGPIVGRGYLKQPCLTANAFITNPewaslFHLNGSyRFYKTGDLVRYNADGTIAYIGRKDTQVKL 626
Cdd:cd17643   287 DGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANP-----FGGPGS-RMYRTGDLARRLPDGELEYLGRADEQVKI 360

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  627 NGQRVELGEIEH--QAQPYFRDAVIAAEVAAPAGrkpililfiARKYEYSVNMDCTMLLRPpsilfqekaqGTNTLLQEV 704
Cdd:cd17643   361 RGFRIELGEIEAalATHPSVRDAAVIVREDEPGD---------TRLVAYVVADDGAAADIA----------ELRALLKEL 421

                         490       500
                  ....*....|....*....|....*....
gi 992230864  705 LPRHMIPAAYIELLAMPISRTGKVNRKLL 733
Cdd:cd17643   422 LPDYMVPARYVPLDALPLTVNGKLDRAAL 450
DltA cd05945
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ...
 245-733 3.71e-77

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: 264.11  E-value: 3.71e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  245 QPDAQAICAWDGTITYRQLDRLSSTVQGLLQQYDLGPGSVVPIIFKKSKWAIVAMLGVLKAGAAFCMLDQSYPTKRLVNI 324
Cdd:cd05945     4 NPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERIREI 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  325 CKDVDAKVIVcsqelsigvsgstlsigdhntetatysaiqavnTASHDAAYVVYTSGSTGAPKGIVIEHG---SFcTNAI 401
Cdd:cd05945    84 LDAAKPALLI---------------------------------ADGDDNAYIIFTSGSTGRPKGVQISHDnlvSF-TNWM 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  402 ASsqAQNLDRSSRVLQFASYAFDVSVHESLTPLLLGGC-VCIPSEAQR-VNSLKEAVSTLRVN-WVElTPTVARL----- 473
Cdd:cd05945   130 LS--DFPLGPGDVFLNQAPFSFDLSVMDLYPALASGATlVPVPRDATAdPKQLFRFLAEHGITvWVS-TPSFAAMcllsp 206

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  474 -WCPADIPTVKTLVMGGEPMLPNDISLWKDKL---RLVCAYGPAECTVVSTVQSCVQELGN------IGRS-PCGTCWIV 542
Cdd:cd05945   207 tFTPESLPSLRHFLFCGEVLPHKTARALQQRFpdaRIYNTYGPTEATVAVTYIEVTPEVLDgydrlpIGYAkPGAKLVIL 286

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  543 skDNHHRLMPVGCIGELIIGGPIVGRGYLKQPCLTANAFitnpewaslFHLNGsYRFYKTGDLVRYNADGTIAYIGRKDT 622
Cdd:cd05945   287 --DEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAF---------FPDEG-QRAYRTGDLVRLEADGLLFYRGRLDF 354

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  623 QVKLNGQRVELGEIEH--QAQPYFRDAVIaaeVAAPAGRK-PILILFIarKYEYSVNMDCTMLLRppsilfQEkaqgtnt 699
Cdd:cd05945   355 QVKLNGYRIELEEIEAalRQVPGVKEAVV---VPKYKGEKvTELIAFV--VPKPGAEAGLTKAIK------AE------- 416

                         490       500       510
                  ....*....|....*....|....*....|....
gi 992230864  700 lLQEVLPRHMIPAAYIELLAMPISRTGKVNRKLL 733
Cdd:cd05945   417 -LAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
A_NRPS_ProA cd17656
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ...
 246-733 1.32e-76

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: 263.57  E-value: 1.32e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  246 PDAQAICAWDGTITYRQLDRLSSTVQGLLQQYDLGPGSVVPIIFKKSKWAIVAMLGVLKAGAAFCMLDQSYPTKRLVNIC 325
Cdd:cd17656     2 PDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIM 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  326 KDVDAKVIVCSQELSIGVS--GSTLSIGDHNTETATYSAIQAVNtASHDAAYVVYTSGSTGAPKGIVIEHGSFcTNAIAS 403
Cdd:cd17656    82 LDSGVRVVLTQRHLKSKLSfnKSTILLEDPSISQEDTSNIDYIN-NSDDLLYIIYTSGTTGKPKGVQLEHKNM-VNLLHF 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  404 SQAQ-NLDRSSRVLQFASYAFDVSVHESLTPLLLGGCV-CIPSEAQR-VNSLKEAVSTLRVNWVELTPTVARLWCPA--- 477
Cdd:cd17656   160 EREKtNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLyIIREETKRdVEQLFDLVKRHNIEVVFLPVAFLKFIFSEref 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  478 --DIPT-VKTLVMGGEPMLPNDisLWKDKLR-----LVCAYGPAECTVVSTV----QSCVQELGNIGRsPCGTCWIVSKD 545
Cdd:cd17656   240 inRFPTcVKHIITAGEQLVITN--EFKEMLHehnvhLHNHYGPSETHVVTTYtinpEAEIPELPPIGK-PISNTWIYILD 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  546 NHHRLMPVGCIGELIIGGPIVGRGYLKQPCLTANAFITNPewaslfhLNGSYRFYKTGDLVRYNADGTIAYIGRKDTQVK 625
Cdd:cd17656   317 QEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDP-------FDPNERMYRTGDLARYLPDGNIEFLGRADHQVK 389

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  626 LNGQRVELGEIEHQ--AQPYFRDAVIAAEvAAPAGRKPIlilfiarkYEYSVnmdctMLLRPPSILFQEKaqgtntlLQE 703
Cdd:cd17656   390 IRGYRIELGEIEAQllNHPGVSEAVVLDK-ADDKGEKYL--------CAYFV-----MEQELNISQLREY-------LAK 448

                         490       500       510
                  ....*....|....*....|....*....|
gi 992230864  704 VLPRHMIPAAYIELLAMPISRTGKVNRKLL 733
Cdd:cd17656   449 QLPEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
A_NRPS_PpsD_like cd17650
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ...
 246-733 3.10e-76

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: 261.25  E-value: 3.10e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  246 PDAQAICAWDGTITYRQLDRLSSTVQGLLQQYDLGPGSVVPIIFKKSKWAIVAMLGVLKAGAAFCMLDQSYPTKRLVNIC 325
Cdd:cd17650     1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  326 KDVDAKVIVcsqelsigvsgstlsigdhntetatysaiqavnTASHDAAYVVYTSGSTGAPKGIVIEHGSFCTNAIASSQ 405
Cdd:cd17650    81 EDSGAKLLL---------------------------------TQPEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAWRR 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  406 AQNLDRSS-RVLQFASYAFDVSVHESLTPLLLGGCVCI-PSEAQ-RVNSLKEAVSTLRVNWVELTPTVAR------LWCP 476
Cdd:cd17650   128 EYELDSFPvRLLQMASFSFDVFAGDFARSLLNGGTLVIcPDEVKlDPAALYDLILKSRITLMESTPALIRpvmayvYRNG 207

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  477 ADIPTVKTLVMGGEPMLPNDISLWKDKL----RLVCAYGPAECTVVSTV-QSCVQELGNIGRSPCG------TCWIVskD 545
Cdd:cd17650   208 LDLSAMRLLIVGSDGCKAQDFKTLAARFgqgmRIINSYGVTEATIDSTYyEEGRDPLGDSANVPIGrplpntAMYVL--D 285

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  546 NHHRLMPVGCIGELIIGGPIVGRGYLKQPCLTANAFITNPewaslfhLNGSYRFYKTGDLVRYNADGTIAYIGRKDTQVK 625
Cdd:cd17650   286 ERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENP-------FAPGERMYRTGDLARWRADGNVELLGRVDHQVK 358

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  626 LNGQRVELGEIEHQ--AQPYFRDAVIAAEVAApAGRKPILILFIARKyeySVNmdcTMLLRppsilfqekaqgtnTLLQE 703
Cdd:cd17650   359 IRGFRIELGEIESQlaRHPAIDEAVVAVREDK-GGEARLCAYVVAAA---TLN---TAELR--------------AFLAK 417

                         490       500       510
                  ....*....|....*....|....*....|
gi 992230864  704 VLPRHMIPAAYIELLAMPISRTGKVNRKLL 733
Cdd:cd17650   418 ELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
A_NRPS_TlmIV_like cd12114
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ...
 246-733 1.12e-75

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: 260.67  E-value: 1.12e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  246 PDAQAICAWDGTITYRQLDRLSSTVQGLLQQYDLGPGSVVPIIFKKSKWAIVAMLGVLKAGAAFCMLDQSYPTKRLVNIC 325
Cdd:cd12114     1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  326 KDVDAK-VIVCSQELSIGVSGSTLSIGDHNTETAtySAIQA-VNTASHDAAYVVYTSGSTGAPKGIVIEHGSfCTNAIAS 403
Cdd:cd12114    81 ADAGARlVLTDGPDAQLDVAVFDVLILDLDALAA--PAPPPpVDVAPDDLAYVIFTSGSTGTPKGVMISHRA-ALNTILD 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  404 SQAQ-NLDRSSRVLQFASYAFDVSVHESLTPLLLGGCVCIPSEAQR--VNSLKEAVSTLRVN-------WVELTPTVARL 473
Cdd:cd12114   158 INRRfAVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLPDEARRrdPAHWAELIERHGVTlwnsvpaLLEMLLDVLEA 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  474 wCPADIPTVKTLVMGGE---PMLPNDI-SLWKDkLRLVCAYGPAECTVVSTVQScVQELGNIGRS-PCG------TCWIV 542
Cdd:cd12114   238 -AQALLPSLRLVLLSGDwipLDLPARLrALAPD-ARLISLGGATEASIWSIYHP-IDEVPPDWRSiPYGrplanqRYRVL 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  543 skDNHHRLMPVGCIGELIIGGPIVGRGYLKQPCLTANAFITNPEWAslfhlngsyRFYKTGDLVRYNADGTIAYIGRKDT 622
Cdd:cd12114   315 --DPRGRDCPDWVPGELWIGGRGVALGYLGDPELTAARFVTHPDGE---------RLYRTGDLGRYRPDGTLEFLGRRDG 383

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  623 QVKLNGQRVELGEIEHQAQpyfRDAVIAAEVAAPAGRKPI--LILFIARKYEYSVNMDCTMLLRppsilfqekaqgtntl 700
Cdd:cd12114   384 QVKVRGYRIELGEIEAALQ---AHPGVARAVVVVLGDPGGkrLAAFVVPDNDGTPIAPDALRAF---------------- 444

                         490       500       510
                  ....*....|....*....|....*....|...
gi 992230864  701 LQEVLPRHMIPAAYIELLAMPISRTGKVNRKLL 733
Cdd:cd12114   445 LAQTLPAYMIPSRVIALEALPLTANGKVDRAAL 477
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
172-828 3.85e-74

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 273.07  E-value: 3.85e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  172 YVPSALHnAHANNIISTLEQIIHcvihSPGRPFADSCLLSKHHQDQIAEWNRNApiHPF-DSCIHTLFRLQCILQPDAQA 250
Cdd:PRK10252  404 YDEATLI-AHAERLKALIAQFAA----DPALLCGDVDILLPGEYAQLAQVNATA--VEIpETTLSALVAQQAAKTPDAPA 476

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  251 ICAWDGTITYRQLDRLSSTVQGLLQQYDLGPGSVVPIIFKKSKWAIVAMLGVLKAGAAFCMLDQSYPTKRLVNICKDVDA 330
Cdd:PRK10252  477 LADARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARP 556

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  331 KVIVCSQELSIGVSG-STLSIGDHNTETATYSAIQAVNTASHDAAYVVYTSGSTGAPKGIVIEHGSFcTNAIASSQAQ-N 408
Cdd:PRK10252  557 SLLITTADQLPRFADvPDLTSLCYNAPLAPQGAAPLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTAI-VNRLLWMQNHyP 635

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  409 LDRSSRVLQFASYAFDVSVHESLTPLLLGGC-VCIPSEAQR-------------VNSLKEAVSTLRVNWVELTPTVARLW 474
Cdd:PRK10252  636 LTADDVVLQKTPCSFDVSVWEFFWPFIAGAKlVMAEPEAHRdplamqqffaeygVTTTHFVPSMLAAFVASLTPEGARQS 715

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  475 CpadiPTVKTLVMGGEPMlpnDISLWKDKLRLVCA-----YGPAECTV-VSTVQSCVQELGNI-GRS-PCG-TCW---IV 542
Cdd:PRK10252  716 C----ASLRQVFCSGEAL---PADLCREWQQLTGAplhnlYGPTEAAVdVSWYPAFGEELAAVrGSSvPIGyPVWntgLR 788

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  543 SKDNHHRLMPVGCIGELIIGGPIVGRGYLKQPCLTANAFITNPewaslfHLNGSyRFYKTGDLVRYNADGTIAYIGRKDT 622
Cdd:PRK10252  789 ILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADP------FAPGE-RMYRTGDVARWLDDGAVEYLGRSDD 861

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  623 QVKLNGQRVELGEIEH--QAQPYFRDAVIAAEV----AAPAGRKPILILFIARkyEYSVNMDCTMLLrppsilfqekaqg 696
Cdd:PRK10252  862 QLKIRGQRIELGEIDRamQALPDVEQAVTHACVinqaAATGGDARQLVGYLVS--QSGLPLDTSALQ------------- 926

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  697 tnTLLQEVLPRHMIPAAYIELLAMPISRTGKVNRKLLrEAVEQASEKDFRAyypithndmiqlPSTPVLDQLRLLFSAAL 776
Cdd:PRK10252  927 --AQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKAL-PLPELKAQVPGRA------------PKTGTETIIAAAFSSLL 991

                         650       660       670       680       690
                  ....*....|....*....|....*....|....*....|....*....|...
gi 992230864  777 RIPEEKIkpNDSFFHLGGDSVSAIRLVGD-ARDQGLHITVESLFKRQTISKLA 828
Cdd:PRK10252  992 GCDVVDA--DADFFALGGHSLLAMKLAAQlSRQFARQVTPGQVMVASTVAKLA 1042
MenE/FadK COG0318
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ...
 234-741 2.05e-73

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: 253.19  E-value: 2.05e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  234 IHTLFRLQCILQPDAQAICAWDGTITYRQLDRLSSTVQGLLQQYDLGPGSVVPIIFKKSKWAIVAMLGVLKAGAAFCMLD 313
Cdd:COG0318     1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  314 QSYPTKRLVNICKDVDAKVIVCsqelsigvsgstlsigdhntetatysaiqavntashdaAYVVYTSGSTGAPKGIVIEH 393
Cdd:COG0318    81 PRLTAEELAYILEDSGARALVT--------------------------------------ALILYTSGTTGRPKGVMLTH 122

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  394 GSFCTNAIASSQAQNLDRSSRVLQ----FASYAFDVSVhesLTPLLLGGC-VCIPS-EAQRVNslkEAVSTLRVNWVELT 467
Cdd:COG0318   123 RNLLANAAAIAAALGLTPGDVVLValplFHVFGLTVGL---LAPLLAGATlVLLPRfDPERVL---ELIERERVTVLFGV 196

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  468 PTVARLWC------PADIPTVKTLVMGGEPMLPNDISLWKDKL--RLVCAYGPAECTVVSTV---QSCVQELGNIGRSPC 536
Cdd:COG0318   197 PTMLARLLrhpefaRYDLSSLRLVVSGGAPLPPELLERFEERFgvRIVEGYGLTETSPVVTVnpeDPGERRPGSVGRPLP 276

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  537 GT-CWIVskDNHHRLMPVGCIGELIIGGPIVGRGYLKQPCLTANAFItnpewaslfhlNGsyrFYKTGDLVRYNADGTIA 615
Cdd:COG0318   277 GVeVRIV--DEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAFR-----------DG---WLRTGDLGRLDEDGYLY 340

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  616 YIGRKDTQVKLNGQRVELGEIEH--QAQPYFRDAVIAAEVAAPAGRKPILILFiarkyeysvnmdctmlLRPPSILfqeK 693
Cdd:COG0318   341 IVGRKKDMIISGGENVYPAEVEEvlAAHPGVAEAAVVGVPDEKWGERVVAFVV----------------LRPGAEL---D 401

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*...
gi 992230864  694 AQGTNTLLQEVLPRHMIPAAYIELLAMPISRTGKVNRKLLREAVEQAS 741
Cdd:COG0318   402 AEELRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRERYAAGA 449
PRK05691 PRK05691
peptide synthase; Validated
 191-1024 2.97e-72

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 270.12  E-value: 2.97e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  191 QIIHCVIHSPGRPFADSCLLSKHHQDQI-AEWNRNAPIHPFDSCIHTLFRLQCILQPDAQAICAWDGTITYRQLDRLSST 269
Cdd:PRK05691 2146 NLLEALLGDPQQRLAELPLLAAAEQQQLlDSLAGEAGEARLDQTLHGLFAAQAARTPQAPALTFAGQTLSYAELDARANR 2225

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  270 VQGLLQQYDLGPGSVVPIIFKKSKWAIVAMLGVLKAGAAFCMLDQSYPTKRLVNICKDV-------DAKVIVCSQELSIG 342
Cdd:PRK05691 2226 LARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLHYMIEDSgiglllsDRALFEALGELPAG 2305

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  343 VSGSTLSigDHNTETATYSA--IQAVNTASHDAaYVVYTSGSTGAPKGIVIEHGSFCTNAIASSQAQNLDRSSRVLQFAS 420
Cdd:PRK05691 2306 VARWCLE--DDAAALAAYSDapLPFLSLPQHQA-YLIYTSGSTGKPKGVVVSHGEIAMHCQAVIERFGMRADDCELHFYS 2382

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  421 YAFDVSVHESLTPLLLGGCVCIPSEAQ-RVNSLKEAVSTLRVNWVELTPTVAR-----LWCPADIPTVKTLVMGGEPMLP 494
Cdd:PRK05691 2383 INFDAASERLLVPLLCGARVVLRAQGQwGAEEICQLIREQQVSILGFTPSYGSqlaqwLAGQGEQLPVRMCITGGEALTG 2462

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  495 NDISLWKDKLR---LVCAYGPAEcTVVSTVQSCVQEL--GNIGRSPCG------TCWIVSKDnhHRLMPVGCIGELIIGG 563
Cdd:PRK05691 2463 EHLQRIRQAFApqlFFNAYGPTE-TVVMPLACLAPEQleEGAASVPIGrvvgarVAYILDAD--LALVPQGATGELYVGG 2539

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  564 PIVGRGYLKQPCLTANAFITNPewaslFHLNGSyRFYKTGDLVRYNADGTIAYIGRKDTQVKLNGQRVELGEIEH--QAQ 641
Cdd:PRK05691 2540 AGLAQGYHDRPGLTAERFVADP-----FAADGG-RLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESrlLEH 2613

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  642 PYFRDAVIAAeVAAPAGRKpiLILFIARKyEYSVNMDCTMLLRppsilfqekaQGTNTLLQEVLPRHMIPAAYIELLAMP 721
Cdd:PRK05691 2614 PAVREAVVLA-LDTPSGKQ--LAGYLVSA-VAGQDDEAQAALR----------EALKAHLKQQLPDYMVPAHLILLDSLP 2679

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  722 ISRTGKVNRKLLREAVEQASEKDFRAyypithndmiqlPSTPVLDQLRLLFSAALRIpeEKIKPNDSFFHLGGDSVSAIR 801
Cdd:PRK05691 2680 LTANGKLDRRALPAPDPELNRQAYQA------------PRSELEQQLAQIWREVLNV--ERVGLGDNFFELGGDSILSIQ 2745

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  802 LVGDARDQGLHITVESLFKRQTISKLAEcthqmsngigspippfslldplgkgtyIAQATEQCSVFPEQIEDIYPCTPLQ 881
Cdd:PRK05691 2746 VVSRARQLGIHFSPRDLFQHQTVQTLAA---------------------------VATHSEAAQAEQGPLQGASGLTPIQ 2798

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  882 EALMAYTSKRPGAFQAQFRFQLPHQLDMLRLKEAWRIVIAANPILRTRIVfCHTGALQVVLRP--GEQLQW--------- 950
Cdd:PRK05691 2799 HWFFDSPVPQPQHWNQALLLEPRQALDPALLEQALQALVEHHDALRLRFS-QADGRWQAEYRAvtAQELLWqvtvadfae 2877

                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  951 ------------DLINGvhtspgslmsygvPLVDMAITNDTAGklSRTFCLTMHHAIFDGWSYGLILGAVEDAYKHTNAV 1018
Cdd:PRK05691 2878 caalfadaqrslDLQQG-------------PLLRALLVDGPQG--QQRLLLAIHHLVVDGVSWRVLLEDLQALYRQLSAG 2942


                  ....*.
gi 992230864 1019 QRPFAP 1024
Cdd:PRK05691 2943 AEPALP 2948
AMP-binding pfam00501
AMP-binding enzyme;
238-626 5.82e-71

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 244.91  E-value: 5.82e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864   238 FRLQCILQPDAQAICAWDG-TITYRQLDRLSSTVQGLLQQYDLGPGSVVPIIFKKSKWAIVAMLGVLKAGAAFCMLDQSY 316
Cdd:pfam00501    1 LERQAARTPDKTALEVGEGrRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864   317 PTKRLVNICKDVDAKVIVCSQELSIGVSGSTLSIGDHNTETATYSA--------------------IQAVNTASHDAAYV 376
Cdd:pfam00501   81 PAEELAYILEDSGAKVLITDDALKLEELLEALGKLEVVKLVLVLDRdpvlkeeplpeeakpadvppPPPPPPDPDDLAYI 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864   377 VYTSGSTGAPKGIVIEHGSFCTNAIASSQAQ----NLDRSSRVLQFASYAFDVSV-HESLTPLLLGGCVCIPSEAQR--V 449
Cdd:pfam00501  161 IYTSGTTGKPKGVMLTHRNLVANVLSIKRVRprgfGLGPDDRVLSTLPLFHDFGLsLGLLGPLLAGATVVLPPGFPAldP 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864   450 NSLKEAVSTLRVNWVELTPTVARLW------CPADIPTVKTLVMGGEPMLPNDISLWKDKLR--LVCAYGPAECTVVSTV 521
Cdd:pfam00501  241 AALLELIERYKVTVLYGVPTLLNMLleagapKRALLSSLRLVLSGGAPLPPELARRFRELFGgaLVNGYGLTETTGVVTT 320

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864   522 ----QSCVQELGNIGRSPCGTCWIVSKDNHHRLMPVGCIGELIIGGPIVGRGYLKQPCLTANAFITNpewaslfhlngsy 597
Cdd:pfam00501  321 plplDEDLRSLGSVGRPLPGTEVKIVDDETGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDED------------- 387

                          410       420
                   ....*....|....*....|....*....
gi 992230864   598 RFYKTGDLVRYNADGTIAYIGRKDTQVKL 626
Cdd:pfam00501  388 GWYRTGDLGRRDEDGYLEIVGRKKDQIKL 416
A_NRPS_ACVS-like cd17648
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ...
 246-733 8.97e-70

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: 242.69  E-value: 8.97e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  246 PDAQAICAWDGTITYRQLD-RLSSTVQGLLQQYDLGPGSVVPIIFKKSKWAIVAMLGVLKAGAAFCMLDQSYPTKRLVNI 324
Cdd:cd17648     1 PDRVAVVYGDKRLTYRELNeRANRLAHYLLSVAEIRPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  325 CKDVDAKVIVcsqelsigvsgstlsigdhntetatysaiqavnTASHDAAYVVYTSGSTGAPKGIVIEHGS---FCTNAI 401
Cdd:cd17648    81 LEDTGARVVI---------------------------------TNSTDLAYAIYTSGTTGKPKGVLVEHGSvvnLRTSLS 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  402 ASSQAQNlDRSSRVLQFASYAFDVSVHESLTPLLLGGCVCIPSEAQRVN--SLKEAVSTLRVNWVELTPTVARLWCPADI 479
Cdd:cd17648   128 ERYFGRD-NGDEAVLFFSNYVFDFFVEQMTLALLNGQKLVVPPDEMRFDpdRFYAYINREKVTYLSGTPSVLQQYDLARL 206

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  480 PTVKTLVMGGEPMLPNDIslwkDKLR------LVCAYGPAECTVVSTVQ--SCVQELGN-IGRSPCGTCWIVSKDNHHRL 550
Cdd:cd17648   207 PHLKRVDAAGEEFTAPVF----EKLRsrfaglIINAYGPTETTVTNHKRffPGDQRFDKsLGRPVRNTKCYVLNDAMKRV 282

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  551 mPVGCIGELIIGGPIVGRGYLKQPCLTANAFITNPEWASLFHLNGSY-RFYKTGDLVRYNADGTIAYIGRKDTQVKLNGQ 629
Cdd:cd17648   283 -PVGAVGELYLGGDGVARGYLNRPELTAERFLPNPFQTEQERARGRNaRLYKTGDLVRWLPSGELEYLGRNDFQVKIRGQ 361

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  630 RVELGEIEHQAQPY---FRDAVIAAEVAAPAGrkpililfiARKYEYSVnmdCTMLLRPPSIlfqeKAQGTNTLLQEVLP 706
Cdd:cd17648   362 RIEPGEVEAALASYpgvRECAVVAKEDASQAQ---------SRIQKYLV---GYYLPEPGHV----PESDLLSFLRAKLP 425

                         490       500
                  ....*....|....*....|....*..
gi 992230864  707 RHMIPAAYIELLAMPISRTGKVNRKLL 733
Cdd:cd17648   426 RYMVPARLVRLEGIPVTINGKLDVRAL 452
A_NRPS_LgrA-like cd17645
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ...
 235-733 1.18e-65

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: 230.13  E-value: 1.18e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  235 HTLFRLQCILQPDAQAICAWDGTITYRQLDRLSSTVQGLLQQYDLGPGSVVPIIFKKSKWAIVAMLGVLKAGAAFCMLDQ 314
Cdd:cd17645     1 HQLFEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  315 SYPTKRLVNICKDVDAKVIVcsqelsigvsgstlsigdhntetatysaiqavnTASHDAAYVVYTSGSTGAPKGIVIEHG 394
Cdd:cd17645    81 DYPGERIAYMLADSSAKILL---------------------------------TNPDDLAYVIYTSGSTGLPKGVMIEHH 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  395 SFCTNAIASSQAQNLDRSSRVLQFASYAFDVSVHESLTPLLLGGCVCIPSEAQR--VNSLKEAVSTLRVNWVELTPTVAR 472
Cdd:cd17645   128 NLVNLCEWHRPYFGVTPADKSLVYASFSFDASAWEIFPHLTAGAALHVVPSERRldLDALNDYFNQEGITISFLPTGAAE 207

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  473 LWCPADIPTVKTLVMGGEPMlpNDISlwKDKLRLVCAYGPAECTVVSTVQSCVQELGN--IGRSPCGT-CWIVSKDNhhR 549
Cdd:cd17645   208 QFMQLDNQSLRVLLTGGDKL--KKIE--RKGYKLVNNYGPTENTVVATSFEIDKPYANipIGKPIDNTrVYILDEAL--Q 281

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  550 LMPVGCIGELIIGGPIVGRGYLKQPCLTANAFITNPEWASlfhlngsYRFYKTGDLVRYNADGTIAYIGRKDTQVKLNGQ 629
Cdd:cd17645   282 LQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPFVPG-------ERMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGY 354

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  630 RVELGEIEHQAQPYFR---DAVIAAEvaaPAGRKPILILFIArkyeysvnmdctmllrPPSILFQEKAQGTntlLQEVLP 706
Cdd:cd17645   355 RIEPGEIEPFLMNHPLielAAVLAKE---DADGRKYLVAYVT----------------APEEIPHEELREW---LKNDLP 412

                         490       500
                  ....*....|....*....|....*..
gi 992230864  707 RHMIPAAYIELLAMPISRTGKVNRKLL 733
Cdd:cd17645   413 DYMIPTYFVHLKALPLTANGKVDRKAL 439
PRK05691 PRK05691
peptide synthase; Validated
 182-807 6.12e-61

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 233.14  E-value: 6.12e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  182 ANNIISTLEQiihcVIHSPGRPFADSCLLSKHHQDQIAEWNRnAPIHPFDSCIHTLFRLQCILQPDAQAIcAWDG-TITY 260
Cdd:PRK05691 1086 AEHFLALLEQ----VCEDPQRALGDVQLLDAAERAQLAQWGQ-APCAPAQAWLPELLNEQARQTPERIAL-VWDGgSLDY 1159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  261 RQLDRLSSTVQGLLQQYDLGPGSVVPIIFKKSKWAIVAMLGVLKAGAAFCMLDQSYPTKRLVNICKDVDAKVIVCSQELS 340
Cdd:PRK05691 1160 AELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSGVELLLTQSHLL 1239

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  341 IGVSGS--TLSIGDHNTETATY-SAIQAVNTASHDAAYVVYTSGSTGAPKGIVIEHGSFCTNAIASSQAQNLDRSSRVLQ 417
Cdd:PRK05691 1240 ERLPQAegVSAIALDSLHLDSWpSQAPGLHLHGDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYALDDSDVLMQ 1319

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  418 FASYAFDVSVHESLTPLLLGGCVCIPS-----EAQRVNSL--KEAVSTLrvnwvELTPTVARLWC----PADIPTVKTLV 486
Cdd:PRK05691 1320 KAPISFDVSVWECFWPLITGCRLVLAGpgehrDPQRIAELvqQYGVTTL-----HFVPPLLQLFIdeplAAACTSLRRLF 1394

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  487 MGGE---PMLPNDISLWKDKLRLVCAYGPAECTVVSTVQSCVQELGN---IGRsPCGTCWIVSKDNHHRLMPVGCIGELI 560
Cdd:PRK05691 1395 SGGEalpAELRNRVLQRLPQVQLHNRYGPTETAINVTHWQCQAEDGErspIGR-PLGNVLCRVLDAELNLLPPGVAGELC 1473

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  561 IGGPIVGRGYLKQPCLTANAFITNPEWaslfhlNGSYRFYKTGDLVRYNADGTIAYIGRKDTQVKLNGQRVELGEIEHQ- 639
Cdd:PRK05691 1474 IGGAGLARGYLGRPALTAERFVPDPLG------EDGARLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARl 1547

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  640 -AQPYFRDAVIAAEVAApAGrkPILILFiarkYEYSVNMDctmllrppsilfqEKAQGTNTLLQEVLPRHMIPAAYIELL 718
Cdd:PRK05691 1548 lAQPGVAQAAVLVREGA-AG--AQLVGY----YTGEAGQE-------------AEAERLKAALAAELPEYMVPAQLIRLD 1607

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  719 AMPISRTGKVNRKLLREAVEQASEkdfrayypitHNDmiqlPSTPVLDQLRLLFSAALRIPeeKIKPNDSFFHLGGDSVS 798
Cdd:PRK05691 1608 QMPLGPSGKLDRRALPEPVWQQRE----------HVE----PRTELQQQIAAIWREVLGLP--RVGLRDDFFALGGHSLL 1671


                  ....*....
gi 992230864  799 AIRLVGDAR 807
Cdd:PRK05691 1672 ATQIVSRTR 1680
CT_NRPS-like cd19542
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ...
 874-1265 1.13e-55

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: 199.84  E-value: 1.13e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  874 IYPCTPLQEALMAYTSKRPGAFQAQFRFQLPHQLDMLRLKEAWRIVIAANPILRTriVFCHTGA----LQVVLRpgeQLQ 949
Cdd:cd19542     1 IYPCTPMQEGMLLSQLRSPGLYFNHFVFDLDSSVDVERLRNAWRQLVQRHDILRT--VFVESSAegtfLQVVLK---SLD 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  950 WDLInGVHTSPGSLMSY-----------GVPLVDMAITNDTAGKlsRTFCLTMHHAIFDGWSYGLILGAVEDAYKHTNAV 1018
Cdd:cd19542    76 PPIE-EVETDEDSLDALtrdllddptlfGQPPHRLTLLETSSGE--VYLVLRISHALYDGVSLPIILRDLAAAYNGQLLP 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1019 QRP-FAPFIKYILHCNYESAKHFWCSEFKDMQALPFPVpplsrghmANSSTTTHRQIHVSEW----LSSYC-----TPST 1088
Cdd:cd19542   153 PAPpFSDYISYLQSQSQEESLQYWRKYLQGASPCAFPS--------LSPKRPAERSLSSTRRslakLEAFCaslgvTLAS 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1089 IIQLAFTLLIAWRTESMDVLFGLTVTGRNAPVAGIHRTTGPTIATFPLRTILYGTMNITDALLCMQNHIATLIPFEHTGL 1168
Cdd:cd19542   225 LFQAAWALVLARYTGSRDVVFGYVVSGRDLPVPGIDDIVGPCINTLPVRVKLDPDWTVLDLLRQLQQQYLRSLPHQHLSL 304

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1169 RRIKSFGTETARACQFQSLLIIQPVTYRESSEIFFELESNEHEQSKFSTCPLTLVCELRTHSVSVKAISDNAVVISGDME 1248
Cdd:cd19542   305 REIQRALGLWPSGTLFNTLVSYQNFEASPESELSGSSVFELSAAEDPTEYPVAVEVEPSGDSLKVSLAYSTSVLSEEQAE 384

                         410
                  ....*....|....*..
gi 992230864 1249 RLLDQLEYLIDMITKSP 1265
Cdd:cd19542   385 ELLEQFDDILEALLANP 401
PRK04813 PRK04813
D-alanine--poly(phosphoribitol) ligase subunit DltA;
245-737 1.22e-55

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


Pssm-ID: 235313 [Multi-domain]  Cd Length: 503  Bit Score: 202.82  E-value: 1.22e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  245 QPDAQAICAWDGTITYRQLDRLSSTVQGLLQQYDLGPGSVVpIIF-KKSKWAIVAMLGVLKAGAAFCMLDQSYPTKRLVN 323
Cdd:PRK04813   15 QPDFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPI-IVFgHMSPEMLATFLGAVKAGHAYIPVDVSSPAERIEM 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  324 ICKDVDAKVIVCSQELSIGVSG-STLSIGDHNTETA---TYSAIQAVNtaSHDAAYVVYTSGSTGAPKGIVIEHG---SF 396
Cdd:PRK04813   94 IIEVAKPSLIIATEELPLEILGiPVITLDELKDIFAtgnPYDFDHAVK--GDDNYYIIFTSGTTGKPKGVQISHDnlvSF 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  397 cTNAIASsqAQNLDRSSRVLQFASYAFDVSVHeSLTP-LLLGGC-VCIPSEA-QRVNSLKEAVSTLRVN-WVElTPTVAR 472
Cdd:PRK04813  172 -TNWMLE--DFALPEGPQFLNQAPYSFDLSVM-DLYPtLASGGTlVALPKDMtANFKQLFETLPQLPINvWVS-TPSFAD 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  473 L------WCPADIPTVKTLVMGGEpMLPNDISlwkDKL-------RLVCAYGPAECTV-VSTVQSCVQELGNIGRSPCG- 537
Cdd:PRK04813  247 MclldpsFNEEHLPNLTHFLFCGE-ELPHKTA---KKLlerfpsaTIYNTYGPTEATVaVTSIEITDEMLDQYKRLPIGy 322

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  538 ---TCWIVSKDNHHRLMPVGCIGELIIGGPIVGRGYLKQPCLTANAFitnpewaslFHLNGsYRFYKTGDLVrYNADGTI 614
Cdd:PRK04813  323 akpDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAF---------FTFDG-QPAYHTGDAG-YLEDGLL 391

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  615 AYIGRKDTQVKLNGQRVELGEIEHQ--AQPYFRDAviaaeVAAPagrkpililfiarkyeYSVNMDCTMLLR---PPSIL 689
Cdd:PRK04813  392 FYQGRIDFQIKLNGYRIELEEIEQNlrQSSYVESA-----VVVP----------------YNKDHKVQYLIAyvvPKEED 450

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|.
gi 992230864  690 FQEKAQGTNTL---LQEVLPRHMIPAAYIELLAMPISRTGKVNRKLLREAV 737
Cdd:PRK04813  451 FEREFELTKAIkkeLKERLMEYMIPRKFIYRDSLPLTPNGKIDRKALIEEV 501
PRK05691 PRK05691
peptide synthase; Validated
 205-829 3.03e-55

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 214.26  E-value: 3.03e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  205 ADSCLLSKHHQD-QIAEWNRNAPIHPFDSCIHTLFRLQCILQPDAQAICAWDGTITYRQLDRLSSTVQGLLQQYDLGPGS 283
Cdd:PRK05691 3692 SELPLLGEQERDfLLDGCNRSERDYPLEQSYVRLFEAQVAAHPQRIAASCLDQQWSYAELNRAANRLGHALRAAGVGVDQ 3771

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  284 VVPIIFKKSKWAIVAMLGVLKAGAAFCMLDQSYPTKRLVNICKDVDAKVIVCSQE-LSIGVSGSTLSIGDHNTETATYSA 362
Cdd:PRK05691 3772 PVALLAERGLDLLGMIVGSFKAGAGYLPLDPGLPAQRLQRIIELSRTPVLVCSAAcREQARALLDELGCANRPRLLVWEE 3851

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  363 IQAVNTASHDA---------AYVVYTSGSTGAPKGIVIEHGSFCTNAIASSQAQNLDRSSRVLQFASYAFDVSVHESLTP 433
Cdd:PRK05691 3852 VQAGEVASHNPgiysgpdnlAYVIYTSGSTGLPKGVMVEQRGMLNNQLSKVPYLALSEADVIAQTASQSFDISVWQFLAA 3931

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  434 LLLGGCVCI-PSE-AQRVNSLKEAVSTLRVNWVELTPTVARLWCPAD---IPTVKTLVMGGEPMLPNDISLWKDK---LR 505
Cdd:PRK05691 3932 PLFGARVEIvPNAiAHDPQGLLAHVQAQGITVLESVPSLIQGMLAEDrqaLDGLRWMLPTGEAMPPELARQWLQRypqIG 4011

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  506 LVCAYGPAECT---------VVSTVQSCVQelgnIGrSPCGTCWIVSKDNHHRLMPVGCIGELIIGGPIVGRGYLKQPCL 576
Cdd:PRK05691 4012 LVNAYGPAECSddvaffrvdLASTRGSYLP----IG-SPTDNNRLYLLDEALELVPLGAVGELCVAGTGVGRGYVGDPLR 4086

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  577 TANAFITNPewaslFHLNGSyRFYKTGDLVRYNADGTIAYIGRKDTQVKLNGQRVELGEIE---HQaQPYFRDAVIAAeV 653
Cdd:PRK05691 4087 TALAFVPHP-----FGAPGE-RLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEarlHE-QAEVREAAVAV-Q 4158

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  654 AAPAGRKPIlilfiarkyEYSVNMDCTMLlrpPSILFQEKAQgtntLLQEVLPRHMIPAAYIELLAMPISRTGKVNRKLL 733
Cdd:PRK05691 4159 EGVNGKHLV---------GYLVPHQTVLA---QGALLERIKQ----RLRAELPDYMVPLHWLWLDRLPLNANGKLDRKAL 4222

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  734 REA-VEQASEKDFRAyypithndmiqlPSTPVLDQLRLLFSAALRIpeEKIKPNDSFFHLGGDSVSAIRLVGDARDQ-GL 811
Cdd:PRK05691 4223 PALdIGQLQSQAYLA------------PRNELEQTLATIWADVLKV--ERVGVHDNFFELGGHSLLATQIASRVQKAlQR 4288

                         650
                  ....*....|....*...
gi 992230864  812 HITVESLFKRQTISKLAE 829
Cdd:PRK05691 4289 NVPLRAMFECSTVEELAE 4306
AFD_class_I cd04433
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ...
 372-728 2.22e-40

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: 153.60  E-value: 2.22e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  372 DAAYVVYTSGSTGAPKGIVIEHGSFCTNAIASSQAQNLDRSSRVLQFASYaFDVSVHESL-TPLLLGGCVCI--PSEAQR 448
Cdd:cd04433     1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPL-FHIGGLFGLlGALLAGGTVVLlpKFDPEA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  449 VNslkEAVSTLRVNWVELTPTVARLWC------PADIPTVKTLVMGGEPMLPNDISLWKD--KLRLVCAYGPAECTVVST 520
Cdd:cd04433    80 AL---ELIEREKVTILLGVPTLLARLLkapesaGYDLSSLRALVSGGAPLPPELLERFEEapGIKLVNGYGLTETGGTVA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  521 vqSCVQELGNIGRSPCGTCWIVSK----DNHHRLMPVGCIGELIIGGPIVGRGYLKQPCLTanAFITNPEWaslfhlngs 596
Cdd:cd04433   157 --TGPPDDDARKPGSVGRPVPGVEvrivDPDGGELPPGEIGELVVRGPSVMKGYWNNPEAT--AAVDEDGW--------- 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  597 yrfYKTGDLVRYNADGTIAYIGRKDTQVKLNGQRVELGEIEH--QAQPYFRDAVIaaeVAAP-AGRKPILILFIArkyey 673
Cdd:cd04433   224 ---YRTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAvlLGHPGVAEAAV---VGVPdPEWGERVVAVVV----- 292

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 992230864  674 svnmdctmlLRPPSILFQEKAQgtnTLLQEVLPRHMIPAAYIELLAMPISRTGKV 728
Cdd:cd04433   293 ---------LRPGADLDAEELR---AHVRERLAPYKVPRRVVFVDALPRTASGKI 335
FUM14_C_NRPS-like cd19545
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ...
 1545-1952 4.26e-39

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: 151.30  E-value: 4.26e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1545 AYPCSESHQGLLQTQMLRPFYYQSYTIWEVttrskSSPVSPVRLCNAWFTLARRHPALRTHLIDIPLCDGMsskiHVVHK 1624
Cdd:cd19545     1 IYPCTPLQEGLMALTARQPGAYVGQRVFEL-----PPDIDLARLQAAWEQVVQANPILRTRIVQSDSGGLL----QVVVK 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1625 DYmadaaILSCEDEHVITEL--RKPFLPSDTGLYyPHAFRICQTVSGRVFCKLEGGHAFLDATSVLIILRELAQAYDGQL 1702
Cdd:cd19545    72 ES-----PISWTESTSLDEYleEDRAAPMGLGGP-LVRLALVEDPDTERYFVWTIHHALYDGWSLPLILRQVLAAYQGEP 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1703 SSVPgPSYSSAVAWLQSLPNGDNRmDYWRRQLKDASPCIFPRL---RDQDSPSDTLVVTEQLastatltPVCTRHGLTVS 1779
Cdd:cd19545   146 VPQP-PPFSRFVKYLRQLDDEAAA-EFWRSYLAGLDPAVFPPLpssRYQPRPDATLEHSISL-------PSSASSGVTLA 216

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1780 NVLQVAWGLMLRRYTESDDVCFGALISGRDSRIPDVDKMVGPFFNVLVCQLRFGREDSLWDVLRRNQTEIGNRLLNQHCS 1859
Cdd:cd19545   217 TVLRAAWALVLSRYTGSDDVVFGVTLSGRNAPVPGIEQIVGPTIATVPLRVRIDPEQSVEDFLQTVQKDLLDMIPFEHTG 296

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1860 LIEVLRFSTYFGQ-PLFNTCISVeQPLSMDTPDASLCFKELETLEP----TEYGIIATITIGTTDVGLGLTYKSDLLTED 1934
Cdd:cd19545   297 LQNIRRLGPDARAaCNFQTLLVV-QPALPSSTSESLELGIEEESEDledfSSYGLTLECQLSGSGLRVRARYDSSVISEE 375

                         410
                  ....*....|....*...
gi 992230864 1935 QALAVADRFKMSITEIMG 1952
Cdd:cd19545   376 QVERLLDQFEHVLQQLAS 393
DCL_NRPS cd19543
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ...
 874-1265 3.25e-37

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: 146.58  E-value: 3.25e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  874 IYPCTPLQE-----ALMAYTSkrpGAFQAQFRFQLPHQLDMLRLKEAWRIVIAANPILRTRIVFCHTG-ALQVVLRPGEq 947
Cdd:cd19543     1 IYPLSPMQEgmlfhSLLDPGS---GAYVEQMVITLEGPLDPDRFRAAWQAVVDRHPILRTSFVWEGLGePLQVVLKDRK- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  948 LQWDLINGVHTSP-----------------------GSLMSygVPLVDMAitnDTAGKLSRTFcltmHHAIFDGWSYGLI 1004
Cdd:cd19543    77 LPWRELDLSHLSEaeqeaelealaeedrergfdlarAPLMR--LTLIRLG---DDRYRLVWSF----HHILLDGWSLPIL 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1005 LGAVEDAYKHTNAVQ-------RPFAPFIKYILHCNYESAKHFWCSEFKDMQALPfPVPPLSRGHMANSSTTTHRQIHVS 1077
Cdd:cd19543   148 LKELFAIYAALGEGQppslppvRPYRDYIAWLQRQDKEAAEAYWREYLAGFEEPT-PLPKELPADADGSYEPGEVSFELS 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1078 EWLSSYC---------TPSTIIQLAFTLLIAWRTESMDVLFGLTVTGRNAPVAGIHRTTGPTIATFPLRTILYGTMNITD 1148
Cdd:cd19543   227 AELTARLqelarqhgvTLNTVVQGAWALLLSRYSGRDDVVFGTTVSGRPAELPGIETMVGLFINTLPVRVRLDPDQTVLE 306

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1149 ALLCMQNHIATLIPFEHTGLRRIKSfGTETARACqFQSLLIIQ--PV-----TYRESSEIFFELESNEhEQSKFstcPLT 1221
Cdd:cd19543   307 LLKDLQAQQLELREHEYVPLYEIQA-WSEGKQAL-FDHLLVFEnyPVdesleEEQDEDGLRITDVSAE-EQTNY---PLT 380

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....
gi 992230864 1222 LVCeLRTHSVSVKAISDNAVVISGDMERLLDQLEYLIDMITKSP 1265
Cdd:cd19543   381 VVA-IPGEELTIKLSYDAEVFDEATIERLLGHLRRVLEQVAANP 423
DCL_NRPS cd19543
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ...
 1582-1944 8.23e-37

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: 145.42  E-value: 8.23e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1582 PVSPVRLCNAWFTLARRHPALRTHLIDiplcDGMSSKIHVVHKDYMADAAIL------SCEDEHVITEL-----RKPFLP 1650
Cdd:cd19543    35 PLDPDRFRAAWQAVVDRHPILRTSFVW----EGLGEPLQVVLKDRKLPWRELdlshlsEAEQEAELEALaeedrERGFDL 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1651 SDTGLyyphaFRIC--QTVSGRVFCKLEGGHAFLDATSVLIILRELAQAY----DGQLSSVPGP-SYSSAVAWLQSLPNG 1723
Cdd:cd19543   111 ARAPL-----MRLTliRLGDDRYRLVWSFHHILLDGWSLPILLKELFAIYaalgEGQPPSLPPVrPYRDYIAWLQRQDKE 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1724 DNRmDYWRRQLK---DASPCIFPRLRDQDSPSDTLVVTEQLASTAT--LTPVCTRHGLTVSNVLQVAWGLMLRRYTESDD 1798
Cdd:cd19543   186 AAE-AYWREYLAgfeEPTPLPKELPADADGSYEPGEVSFELSAELTarLQELARQHGVTLNTVVQGAWALLLSRYSGRDD 264

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1799 VCFGALISGRDSRIPDVDKMVGPFFNVLVCQLRFGREDSLWDVLRRNQTEIGNRLLNQHCSLIEVLRFSTyFGQPLFNTC 1878
Cdd:cd19543   265 VVFGTTVSGRPAELPGIETMVGLFINTLPVRVRLDPDQTVLELLKDLQAQQLELREHEYVPLYEIQAWSE-GKQALFDHL 343

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 992230864 1879 ISVE-----QPLSMDTPDASLCFKELETLEPTEYGIIATitigttdVGLG------LTYKSDLLTEDQALAVADRFK 1944
Cdd:cd19543   344 LVFEnypvdESLEEEQDEDGLRITDVSAEEQTNYPLTVV-------AIPGeeltikLSYDAEVFDEATIERLLGHLR 413
A_NRPS_acs4 cd17654
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ...
 255-733 7.28e-36

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: 143.38  E-value: 7.28e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  255 DGTITYRQLDRLSSTVQGLLQQYDLGPGSVVPIIFKKSKWAIVAMLGVLKAGAAFCMLDQSYPTKRLVNICKDVDAKVIV 334
Cdd:cd17654    14 DTTVSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVMKKCHVSYLL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  335 csqelsigvsgstlsIGDHNTETATYSAIQAVNTA-SHDA--AYVVYTSGSTGAPKGIVIEHGSFCTNAIASSQAQNLdR 411
Cdd:cd17654    94 ---------------QNKELDNAPLSFTPEHRHFNiRTDEclAYVIHTSGTTGTPKIVAVPHKCILPNIQHFRSLFNI-T 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  412 SSRVLQFASYA-FDVSVHESLTPLLLGGCVCIPSEAQRVNSLKEAVSTL---RVNWVELTPTVARLWCPADIP------- 480
Cdd:cd17654   158 SEDILFLTSPLtFDPSVVEIFLSLSSGATLLIVPTSVKVLPSKLADILFkrhRITVLQATPTLFRRFGSQSIKstvlsat 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  481 -TVKTLVMGGEPmLPND--ISLWK---DKLRLVCAYGPAECTVVSTVQSCVQELG--NIGrSPCGTCWIVSKDNHHRLMP 552
Cdd:cd17654   238 sSLRVLALGGEP-FPSLviLSSWRgkgNRTRIFNIYGITEVSCWALAYKVPEEDSpvQLG-SPLLGTVIEVRDQNGSEGT 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  553 vgciGELIIGGpIVGRGYLKQPCLTANAfitnpewaslfhlngsyRFYKTGDLVRYNaDGTIAYIGRKDTQVKLNGQRVE 632
Cdd:cd17654   316 ----GQVFLGG-LNRVCILDDEVTVPKG-----------------TMRATGDFVTVK-DGELFFLGRKDSQIKRRGKRIN 372

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  633 LGEIEHQAQPyfRDAVIAAEVAAPAGRKpiLILFIARKyeysvnmdctmllrppsilfQEKAQGTNTLLQEVLPRHMIPA 712
Cdd:cd17654   373 LDLIQQVIES--CLGVESCAVTLSDQQR--LIAFIVGE--------------------SSSSRIHKELQLTLLSSHAIPD 428

                         490       500
                  ....*....|....*....|.
gi 992230864  713 AYIELLAMPISRTGKVNRKLL 733
Cdd:cd17654   429 TFVQIDKLPLTSHGKVDKSEL 449
alpha_am_amid TIGR03443
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ...
 230-837 1.11e-35

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: 149.06  E-value: 1.11e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864   230 FDSCIHTLF---------RLQCILQPDAQAICAWDGTITYRQLDRLSSTVQGLLQQYDLGPGSVVPIIFKKSKWAIVAML 300
Cdd:TIGR03443  234 FRGAIHDIFadnaekhpdRTCVVETPSFLDPSSKTRSFTYKQINEASNILAHYLLKTGIKRGDVVMIYAYRGVDLVVAVM 313

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864   301 GVLKAGAAFCMLDQSYPTKR------------LVNICK--DVDAKVI-VCSQELSIGVSGSTLSIGDHNTETATYSAIQA 365
Cdd:TIGR03443  314 GVLKAGATFSVIDPAYPPARqtiylsvakpraLIVIEKagTLDQLVRdYIDKELELRTEIPALALQDDGSLVGGSLEGGE 393

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864   366 VNTASHDAAY------VV----------YTSGSTGAPKGIVIEHGSFCTNAIASSQAQNLDRSSRVLQFASYAFDVSVHE 429
Cdd:TIGR03443  394 TDVLAPYQALkdtptgVVvgpdsnptlsFTSGSEGIPKGVLGRHFSLAYYFPWMAKRFGLSENDKFTMLSGIAHDPIQRD 473

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864   430 SLTPLLLGGCVCIPS--EAQRVNSLKEAVSTLRVNWVELTPTVARLW---CPADIPTVKTLVMGGepmlpnDISLWKDKL 504
Cdd:TIGR03443  474 MFTPLFLGAQLLVPTadDIGTPGRLAEWMAKYGATVTHLTPAMGQLLsaqATTPIPSLHHAFFVG------DILTKRDCL 547

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864   505 RL------VC---AYGPAEC---------TVVSTVQSCVQELGNIgrSPCGTCWI------VSKDNHHRLMPVGCIGELI 560
Cdd:TIGR03443  548 RLqtlaenVCivnMYGTTETqravsyfeiPSRSSDSTFLKNLKDV--MPAGKGMKnvqllvVNRNDRTQTCGVGEVGEIY 625

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864   561 I--GGpiVGRGYLKQPCLTANAFITN---------------PEWASLFHLNGSYRFYKTGDLVRYNADGTIAYIGRKDTQ 623
Cdd:TIGR03443  626 VraGG--LAEGYLGLPELNAEKFVNNwfvdpshwidldkenNKPEREFWLGPRDRLYRTGDLGRYLPDGNVECCGRADDQ 703

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864   624 VKLNGQRVELGEIE-HQAQ-PYFRDAVIAaeVAAPAGRKPILILFIARKYEySVNMDCTMLLRPPS----------ILFQ 691
Cdd:TIGR03443  704 VKIRGFRIELGEIDtHLSQhPLVRENVTL--VRRDKDEEPTLVSYIVPQDK-SDELEEFKSEVDDEessdpvvkglIKYR 780

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864   692 EKAQGTNTLLQEVLPRHMIPAAYIELLAMPISRTGKVNRKLLR----EAVEQASEKDFRAYYPITHndmiqlpsTPVLDQ 767
Cdd:TIGR03443  781 KLIKDIREYLKKKLPSYAIPTVIVPLKKLPLNPNGKVDKPALPfpdtAQLAAVAKNRSASAADEEF--------TETERE 852

                          650       660       670       680       690       700       710
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 992230864   768 LRLLFSAALRIPEEKIKPNDSFFHLGGDSVSAIRLVGDARDQ-GLHITVESLFKRQTISKLAECTHQMSNG 837
Cdd:TIGR03443  853 IRDLWLELLPNRPATISPDDSFFDLGGHSILATRMIFELRKKlNVELPLGLIFKSPTIKGFAKEVDRLKKG 923
ligase_PEP_1 TIGR03098
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ...
 234-733 2.91e-35

acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an AMP-binding domain (pfam00501) associated with acyl CoA-ligases. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present next to a decarboxylase enzyme. A number of sequences from Burkholderia species also hit this model, but the genomic context is obviously different. The hypothesis of a constant substrate for this family is only strong where the exosortase context is present.


Pssm-ID: 211788 [Multi-domain]  Cd Length: 517  Bit Score: 143.00  E-value: 2.91e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864   234 IHTLFRLQCILQPDAQAICAWDGTITYRQLDRLSSTVQGLLQQYDLGPGSVVPIIFKKSKWAIVAMLGVLKAGAAFCMLD 313
Cdd:TIGR03098    2 LHHLLEDAAARLPDATALVHHDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPIN 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864   314 QSYPTKRLVNICKDVDAKVIVCSQE----LSIGVSG----STLSIGDHNTET----------------ATYSAIQAVNTA 369
Cdd:TIGR03098   82 PLLKAEQVAHILADCNVRLLVTSSErldlLHPALPGchdlRTLIIVGDPAHAseghpgeepaswpkllALGDADPPHPVI 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864   370 SHDAAYVVYTSGSTGAPKGIVIEHGSFCTNAIASSQAQNLDRSSRVLQFASYAFDVSVHESLTPLLLGGCVcIPSEAQRV 449
Cdd:TIGR03098  162 DSDMAAILYTSGSTGRPKGVVLSHRNLVAGAQSVATYLENRPDDRLLAVLPLSFDYGFNQLTTAFYVGATV-VLHDYLLP 240

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864   450 NSLKEAVSTLRVN--------WVELtptvARL-WCPADIPTVKTLVMGGEPMLPNDISLWKDKL---RLVCAYGPAECTV 517
Cdd:TIGR03098  241 RDVLKALEKHGITglaavpplWAQL----AQLdWPESAAPSLRYLTNSGGAMPRATLSRLRSFLpnaRLFLMYGLTEAFR 316

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864   518 VSTVQScvQEL----GNIGRS-PCGTCWIVSKDNHHRLmpVGCIGELIIGGPIVGRGYLKQPCLTANAFITNPEWASLFH 592
Cdd:TIGR03098  317 STYLPP--EEVdrrpDSIGKAiPNAEVLVLREDGSECA--PGEEGELVHRGALVAMGYWNDPEKTAERFRPLPPFPGELH 392

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864   593 LNGSYRFykTGDLVRYNADGTIAYIGRKDTQVKLNGQRVELGEIEhqaqpyfrDAVIA----AEVAAPAGRKPIL---IL 665
Cdd:TIGR03098  393 LPELAVW--SGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVE--------EVAYAtglvAEAVAFGVPDPTLgqaIV 462

                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 992230864   666 FIARkyeysvnmdctmllrpPSILFQEKAQGTNTLLQEVLPRHMIPAAYIELLAMPISRTGKVNRKLL 733
Cdd:TIGR03098  463 LVVT----------------PPGGEELDRAALLAECRARLPNYMVPALIHVRQALPRNANGKIDRKAL 514
FC-FACS_FadD_like cd05936
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ...
 237-734 2.48e-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: 2.48e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  237 LFRLQCILQPDAQAiCAWDG-TITYRQLDRLSSTVQGLLQQYDLGPGSVVPIIFKKSKWAIVAMLGVLKAGAAFCMLDQS 315
Cdd:cd05936     4 LLEEAARRFPDKTA-LIFMGrKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  316 YPTKRLVNICKDVDAKVIVCSQELSigvsgstlsigdHNTETATYSAIQAVNTAsHDAAYVVYTSGSTGAPKGIVIEHGS 395
Cdd:cd05936    83 YTPRELEHILNDSGAKALIVAVSFT------------DLLAAGAPLGERVALTP-EDVAVLQYTSGTTGVPKGAMLTHRN 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  396 FCTNA--IASSQAQNLDRSSRVLQ----FASYAFDVSVhesLTPLLLGGC-VCIPS----------EAQRVNSLKeAVST 458
Cdd:cd05936   150 LVANAlqIKAWLEDLLEGDDVVLAalplFHVFGLTVAL---LLPLALGATiVLIPRfrpigvlkeiRKHRVTIFP-GVPT 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  459 LrvnWVELTPTVARLwcPADIPTVKTLVMGGEPMLPNDISLWKDKL--RLVCAYGPAECTVVSTVQSC--VQELGNIGRS 534
Cdd:cd05936   226 M---YIALLNAPEFK--KRDFSSLRLCISGGAPLPVEVAERFEELTgvPIVEGYGLTETSPVVAVNPLdgPRKPGSIGIP 300

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  535 PCGTCW-IVSKDNHhrLMPVGCIGELIIGGPIVGRGYLKQPCLTANAFItnpewaslfhlNGsyrFYKTGDLVRYNADGT 613
Cdd:cd05936   301 LPGTEVkIVDDDGE--ELPPGEVGELWVRGPQVMKGYWNRPEETAEAFV-----------DG---WLRTGDIGYMDEDGY 364

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  614 IAYIGRKDTQVKLNGQRVELGEIE-----HqaqPYFRDAVIAAEVAAPAGRkpILILFIARKYEYSVNmdctmllrppsi 688
Cdd:cd05936   365 FFIVDRKKDMIIVGGFNVYPREVEevlyeH---PAVAEAAVVGVPDPYSGE--AVKAFVVLKEGASLT------------ 427

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*.
gi 992230864  689 lfqekAQGTNTLLQEVLPRHMIPAAYIELLAMPISRTGKVNRKLLR 734
Cdd:cd05936   428 -----EEEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILRRELR 468
DCL_NRPS-like cd19536
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ...
 1545-1952 5.55e-30

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: 125.25  E-value: 5.55e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1545 AYPCSESHQGLL---QTQMLRPFYYQSYTiWEVTTRSKSSpvspvRLCNAWFTLARRHPALRTHLIDiplcDGMSSKIHV 1621
Cdd:cd19536     1 MYPLSSLQEGMLfhsLLNPGGSVYLHNYT-YTVGRRLNLD-----LLLEALQVLIDRHDILRTSFIE----DGLGQPVQV 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1622 VHK-------------DYMADAAILSCEDEhvitELRKPFlpsDTGLYYPHAFRIC-QTVSGRVFCKLEGGHAFLDATSV 1687
Cdd:cd19536    71 VHRqaqvpvteldltpLEEQLDPLRAYKEE----TKIRRF---DLGRAPLVRAALVrKDERERFLLVISDHHSILDGWSL 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1688 LIILRELAQAYDGQLSSV-----PGPSYSSAVAWLQSLPNGDNRMDYWRRQLKDA--SPCIFPRLRDQDSPSDTLVVTEQ 1760
Cdd:cd19536   144 YLLVKEILAVYNQLLEYKplslpPAQPYRDFVAHERASIQQAASERYWREYLAGAtlATLPALSEAVGGGPEQDSELLVS 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1761 LASTATLTPVCTRHGLTVSNVLQVAWGLMLRRYTESDDVCFGALISGRDSRIPDVDKMVGPFFNVLVCQLRFgREDSLWD 1840
Cdd:cd19536   224 VPLPVRSRSLAKRSGIPLSTLLLAAWALVLSRHSGSDDVVFGTVVHGRSEETTGAERLLGLFLNTLPLRVTL-SEETVED 302

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1841 VLRRNQTEIGNRLLNQHCSLIEVLRFSTyfGQPLFNTCIS-VEQPLSMDTPDASLCFKELETL----EPTEYGIIATITI 1915
Cdd:cd19536   303 LLKRAQEQELESLSHEQVPLADIQRCSE--GEPLFDSIVNfRHFDLDFGLPEWGSDEGMRRGLlfseFKSNYDVNLSVLP 380

                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 992230864 1916 GTTDVGLGLTYKSDLLTEDQALAVADRFKMSITEIMG 1952
Cdd:cd19536   381 KQDRLELKLAYNSQVLDEEQAQRLAAYYKSAIAELAT 417
MACS_like cd05972
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ...
 259-734 9.21e-29

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: 121.68  E-value: 9.21e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  259 TYRQLDRLSSTVQGLLQQYDLGPGSVVPIIFKKSKWAIVAMLGVLKAGAAFCMLDQSYPTKRLVNICKDVDAKVIVCSQE 338
Cdd:cd05972     2 SFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTDAE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  339 lsigvsgstlsigdhntetatysaiqavntashDAAYVVYTSGSTGAPKGIVIEHGSFCTNAIASSQAQNLDRSSRVLQF 418
Cdd:cd05972    82 ---------------------------------DPALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLGLRPDDIHWNI 128

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  419 ASYAFDVSVHESLT-PLLLGGCVcIPSEAQRVNSLK--EAVSTLRVNWVELTPTVARLWCPADI-----PTVKTLVMGGE 490
Cdd:cd05972   129 ADPGWAKGAWSSFFgPWLLGATV-FVYEGPRFDAERilELLERYGVTSFCGPPTAYRMLIKQDLssykfSHLRLVVSAGE 207

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  491 PMLPNDISLWKDKLRLVC--AYGPAECTVVSTVQSCvQEL--GNIGRS-PCGTCWIVSKDNhhRLMPVGCIGELIIGGPI 565
Cdd:cd05972   208 PLNPEVIEWWRAATGLPIrdGYGQTETGLTVGNFPD-MPVkpGSMGRPtPGYDVAIIDDDG--RELPPGEEGDIAIKLPP 284

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  566 VG--RGYLKQPcltanafitnPEWASLFHlnGSYrfYKTGDLVRYNADGTIAYIGRKDTQVKLNGQR-----VELGEIEH 638
Cdd:cd05972   285 PGlfLGYVGDP----------EKTEASIR--GDY--YLTGDRAYRDEDGYFWFVGRADDIIKSSGYRigpfeVESALLEH 350

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  639 QAqpyfrdAVIAAEVAAP-AGRKPILILFIARKYEYSvnmdctmllrPPSILFQEkaqgtntlLQEVLPRHMIPAAY--- 714
Cdd:cd05972   351 PA------VAEAAVVGSPdPVRGEVVKAFVVLTSGYE----------PSEELAEE--------LQGHVKKVLAPYKYpre 406

                         490       500
                  ....*....|....*....|.
gi 992230864  715 IELLA-MPISRTGKVNRKLLR 734
Cdd:cd05972   407 IEFVEeLPKTISGKIRRVELR 427
A_NRPS_alphaAR cd17647
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ...
 257-733 9.44e-29

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: 123.01  E-value: 9.44e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  257 TITYRQLDRLSSTVQGLLQQYDLGPGSVVPIIFKKSKWAIVAMLGVLKAGAAFCMLDQSYPTKRLvNICKDVdAKvivcs 336
Cdd:cd17647    20 SFTYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPARQ-NIYLGV-AK----- 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  337 QELSIGVSGSTLSIGDHNTETATYsaiqavntashdaayvvyTSGSTGAPKGIVIEHGSFCTNAIASSQAQNLDRSSRVL 416
Cdd:cd17647    93 PRGLIVIRAAGVVVGPDSNPTLSF------------------TSGSEGIPKGVLGRHFSLAYYFPWMAKRFNLSENDKFT 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  417 QFASYAFDVSVHESLTPLLLGGCVCIPSEAQRVN--SLKEAVSTLRVNWVELTPTVARLWCP-ADIPTVKTLvmggEPML 493
Cdd:cd17647   155 MLSGIAHDPIQRDMFTPLFLGAQLLVPTQDDIGTpgRLAEWMAKYGATVTHLTPAMGQLLTAqATTPFPKLH----HAFF 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  494 PNDISLWKDKLRL---------VCAYGPAECT-VVS--TVQSCVQELGNIGRS----PCGT------CWIVSKDNHHRLM 551
Cdd:cd17647   231 VGDILTKRDCLRLqtlaenvriVNMYGTTETQrAVSyfEVPSRSSDPTFLKNLkdvmPAGRgmlnvqLLVVNRNDRTQIC 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  552 PVGCIGELIIGGPIVGRGYLKQPCLTANAFITN----PE-WASL----------FHLNGSYRFYKTGDLVRYNADGTIAY 616
Cdd:cd17647   311 GIGEVGEIYVRAGGLAEGYRGLPELNKEKFVNNwfvePDhWNYLdkdnnepwrqFWLGPRDRLYRTGDLGRYLPNGDCEC 390

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  617 IGRKDTQVKLNGQRVELGEIE-HQAQ-PYFRDAVIAaeVAAPAGRKPILILFIARKYEYSVNMDCTMLLRPPS------- 687
Cdd:cd17647   391 CGRADDQVKIRGFRIELGEIDtHISQhPLVRENITL--VRRDKDEEPTLVSYIVPRFDKPDDESFAQEDVPKEvstdpiv 468

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*....
gi 992230864  688 ---ILFQEKAQGTNTLLQEVLPRHMIPAAYIELLAMPISRTGKVNRKLL 733
Cdd:cd17647   469 kglIGYRKLIKDIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKL 517
FACL_like_6 cd05922
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 265-734 2.74e-28

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: 120.62  E-value: 2.74e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  265 RLSSTVQGLLQQYDLGPGSVVPIIFKKSKWAIVAMLGVLKAGAAFCM----LDQSYPTKRLVNICKDVDAKVIVCSQ--- 337
Cdd:cd05922     1 LGVSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRLGLvfvpLNPTLKESVLRYLVADAGGRIVLADAgaa 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  338 -ELSIG--VSGSTLSIGDHNTETATYSAIQAVNTASHDAAYVVYTSGSTGAPKGIVIEHGSFCTNAIASSQAQNLDRSSR 414
Cdd:cd05922    81 dRLRDAlpASPDPGTVLDADGIRAARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADDR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  415 VLQFASYAFDVSVHESLTPLLLGGCVCIPSEAQRVNSLKEAVSTLRVNWVELTPTVARL-----WCPADIPTVKTLVMGG 489
Cdd:cd05922   161 ALTVLPLSYDYGLSVLNTHLLRGATLVLTNDGVLDDAFWEDLREHGATGLAGVPSTYAMltrlgFDPAKLPSLRYLTQAG 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  490 EPMLPNDISLWKDKL---RLVCAYGPAECTVVSTVQSCVQE---LGNIGRSPCGTCWIVSKDNHHRLmPVGCIGELIIGG 563
Cdd:cd05922   241 GRLPQETIARLRELLpgaQVYVMYGQTEATRRMTYLPPERIlekPGSIGLAIPGGEFEILDDDGTPT-PPGEPGEIVHRG 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  564 PIVGRGYLKQPcltanAFITNP-EWASLFHlngsyrfykTGDLVRYNADGTIAYIGRKDTQVKLNGQRVELGEIEHQA-- 640
Cdd:cd05922   320 PNVMKGYWNDP-----PYRRKEgRGGGVLH---------TGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAArs 385

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  641 QPYFRDAVIAAeVAAPAGRKpiLILFIARKYEysvnMDCTMLLRppsilfqekaqgtntLLQEVLPRHMIPAAYIELLAM 720
Cdd:cd05922   386 IGLIIEAAAVG-LPDPLGEK--LALFVTAPDK----IDPKDVLR---------------SLAERLPPYKVPATVRVVDEL 443

                         490
                  ....*....|....
gi 992230864  721 PISRTGKVNRKLLR 734
Cdd:cd05922   444 PLTASGKVDYAALR 457
FACL_FadD13-like cd17631
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ...
 244-637 4.46e-28

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: 119.64  E-value: 4.46e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  244 LQPDAQAICAWDGTITYRQLDRLSSTVQGLLQQYDLGPGSVVPIIFKKSKWAIVAMLGVLKAGAAFCMLDQSYPTKRLVN 323
Cdd:cd17631     7 RHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEVAY 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  324 ICKDVDAKVIVcsqelsigvsgstlsigdhntetatysaiqavntasHDAAYVVYTSGSTGAPKGIVIEHGSFCTNAIAS 403
Cdd:cd17631    87 ILADSGAKVLF------------------------------------DDLALLMYTSGTTGRPKGAMLTHRNLLWNAVNA 130

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  404 SQAQNLDRSSRVLQ----FASYAFDVSVhesLTPLLLGGCVCIPS--EAQRVNSLKEAVstlRVNWVELTPTV--ARLWC 475
Cdd:cd17631   131 LAALDLGPDDVLLVvaplFHIGGLGVFT---LPTLLRGGTVVILRkfDPETVLDLIERH---RVTSFFLVPTMiqALLQH 204

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  476 PA----DIPTVKTLVMGGEPMLPNDISLWKDK-LRLVCAYGPAECTVVSTVQS---CVQELGNIGRsPCGTCWIVSKDNH 547
Cdd:cd17631   205 PRfattDLSSLRAVIYGGAPMPERLLRALQARgVKFVQGYGMTETSPGVTFLSpedHRRKLGSAGR-PVFFVEVRIVDPD 283

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  548 HRLMPVGCIGELIIGGPIVGRGYLKQPCLTANAFItnpewaslfhlNGSYRfykTGDLVRYNADGTIAYIGRKDTQVKLN 627
Cdd:cd17631   284 GREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAFR-----------DGWFH---TGDLGRLDEDGYLYIVDRKKDMIISG 349

                         410
                  ....*....|
gi 992230864  628 GQRVELGEIE 637
Cdd:cd17631   350 GENVYPAEVE 359
AAS_C cd05909
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ...
 256-734 5.08e-28

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: 120.51  E-value: 5.08e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  256 GTITYRQLDRLSSTVQGLLQQYDLgPGSVVPIIFKKSKWAIVAMLGVLKAGAAFCMLDQSYPTKRLVNICKDVDAKVIVC 335
Cdd:cd05909     6 TSLTYRKLLTGAIALARKLAKMTK-EGENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTVLT 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  336 SQ------------------------ELSIGVSGS-TLSIGDHNTETATYSAIQA--VNTASHDAAYVVYTSGSTGAPKG 388
Cdd:cd05909    85 SKqfieklklhhlfdveydarivyleDLRAKISKAdKCKAFLAGKFPPKWLLRIFgvAPVQPDDPAVILFTSGSEGLPKG 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  389 IVIEHGSFCTNAIASSQAQNLDRSSRVLQ----FASYAFDVSVhesLTPLLLGGCVCIPSEAQRVNSLKEAVSTLRVNWV 464
Cdd:cd05909   165 VVLSHKNLLANVEQITAIFDPNPEDVVFGalpfFHSFGLTGCL---WLPLLSGIKVVFHPNPLDYKKIPELIYDKKATIL 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  465 ELTPT----VARLWCPADIPTVKTLVMGGEPMLPNDISLWKDK--LRLVCAYGPAECTVV---STVQSCVQElGNIGR-S 534
Cdd:cd05909   242 LGTPTflrgYARAAHPEDFSSLRLVVAGAEKLKDTLRQEFQEKfgIRILEGYGTTECSPVisvNTPQSPNKE-GTVGRpL 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  535 PCGTCWIVSKDNHHRLmPVGCIGELIIGGPIVGRGYLKQPCLTANAFitNPEWaslfhlngsyrfYKTGDLVRYNADGTI 614
Cdd:cd05909   321 PGMEVKIVSVETHEEV-PIGEGGLLLVRGPNVMLGYLNEPELTSFAF--GDGW------------YDTGDIGKIDGEGFL 385

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  615 AYIGRKDTQVKLNGQRVELGEIEHQAQPYFRDAVIAAEVAAPAGRK-PILILFIARKyeysvnmdctmLLRPPSILFQEK 693
Cdd:cd05909   386 TITGRLSRFAKIAGEMVSLEAIEDILSEILPEDNEVAVVSVPDGRKgEKIVLLTTTT-----------DTDPSSLNDILK 454

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|.
gi 992230864  694 AQGTNTLLQevlprhmiPAAYIELLAMPISRTGKVNRKLLR 734
Cdd:cd05909   455 NAGISNLAK--------PSYIHQVEEIPLLGTGKPDYVTLK 487
Acs COG0365
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
257-744 1.99e-27

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


Pssm-ID: 440134 [Multi-domain]  Cd Length: 565  Bit Score: 119.83  E-value: 1.99e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  257 TITYRQLDRLSSTVQGLLQQYDLGPGSVVPIIFKKSKWAIVAMLGVLKAGAAFCMLDQSYPTKRLVNICKDVDAKVIVCS 336
Cdd:COG0365    39 TLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLITA 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  337 QELS-------------------------IGVSGSTLSI---GDHNTETATYSA---IQAVNTASHDAAYVVYTSGSTGA 385
Cdd:COG0365   119 DGGLrggkvidlkekvdealeelpslehvIVVGRTGADVpmeGDLDWDELLAAAsaeFEPEPTDADDPLFILYTSGTTGK 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  386 PKGIVIEHGSFCTNAIASSQA-QNLDRSSRVLQFA--------SYAFdvsvhesLTPLLLGGCVCI------PSEAQRvn 450
Cdd:COG0365   199 PKGVVHTHGGYLVHAATTAKYvLDLKPGDVFWCTAdigwatghSYIV-------YGPLLNGATVVLyegrpdFPDPGR-- 269

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  451 sLKEAVSTLRVNWVELTPTVARL---WCPA-----DIPTVKTLVMGGEPMLPNDISLWKD--KLRLVCAYGPAECTvvst 520
Cdd:COG0365   270 -LWELIEKYGVTVFFTAPTAIRAlmkAGDEplkkyDLSSLRLLGSAGEPLNPEVWEWWYEavGVPIVDGWGQTETG---- 344

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  521 vqSCVqeLGNIGRSPC--GTCW---------IVSKDNHHrlMPVGCIGELIIGGPIVG--RGYLKQPCLTANAFI-TNPE 586
Cdd:COG0365   345 --GIF--ISNLPGLPVkpGSMGkpvpgydvaVVDEDGNP--VPPGEEGELVIKGPWPGmfRGYWNDPERYRETYFgRFPG 418

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  587 WaslfhlngsyrfYKTGDLVRYNADGTIAYIGRKDTQVKLNGQRVELGEIE-----HqaqpyfrDAVI-AAEVAAP-AGR 659
Cdd:COG0365   419 W------------YRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIEsalvsH-------PAVAeAAVVGVPdEIR 479

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  660 KPILILFIArkyeysvnmdctmlLRPPsilFQEKAQGTNTLLQEV---LPRHMIPAAYIELLAMPISRTGKVNRKLLREA 736
Cdd:COG0365   480 GQVVKAFVV--------------LKPG---VEPSDELAKELQAHVreeLGPYAYPREIEFVDELPKTRSGKIMRRLLRKI 542


                  ....*...
gi 992230864  737 VEQASEKD 744
Cdd:COG0365   543 AEGRPLGD 550
Condensation pfam00668
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ...
 1542-1849 7.97e-27

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: 116.28  E-value: 7.97e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  1542 IEDAYPCSESHQGLLQTQMLrpfyYQSYTIWEVTTRSKSSP-VSPVRLCNAWFTLARRHPALRTHLI-----DIPLC--D 1613
Cdd:pfam00668    1 VQDEYPLSPAQKRMWFLEKL----EPHSSAYNMPAVLKLTGeLDPERLEKALQELINRHDALRTVFIrqengEPVQVilE 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  1614 GMSSKIHVVHKDYMADAAILSCEDEHVITELRKPFLPSDTGLYYPHAFRIcqtVSGRVFCKLEGGHAFLDATSVLIILRE 1693
Cdd:pfam00668   77 ERPFELEIIDISDLSESEEEEAIEAFIQRDLQSPFDLEKGPLFRAGLFRI---AENRHHLLLSMHHIIVDGVSLGILLRD 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  1694 LAQAYDG-----QLSSVPGPSYSSAVAWLQSLPNGDNRMD---YWRRQLKDASPCI-----FPRLRDQDSPSDTLVVTEQ 1760
Cdd:pfam00668  154 LADLYQQllkgePLPLPPKTPYKDYAEWLQQYLQSEDYQKdaaYWLEQLEGELPVLqlpkdYARPADRSFKGDRLSFTLD 233

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  1761 LASTATLTPVCTRHGLTVSNVLQVAWGLMLRRYTESDDVCFGALISGRDSriPDVDKMVGPFFNVLVCQLRFGREDSLWD 1840
Cdd:pfam00668  234 EDTEELLRKLAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPS--PDIERMVGMFVNTLPLRIDPKGGKTFSE 311


                   ....*....
gi 992230864  1841 VLRRNQTEI 1849
Cdd:pfam00668  312 LIKRVQEDL 320
FAAL cd05931
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ...
 245-670 9.14e-25

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: 111.18  E-value: 9.14e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  245 QPDAQAICAWDG------TITYRQLDRLSSTVQGLLQQYDlGPGSVVPIIFKKSKWAIVAMLGVLKAGAAFCMLdqSYPT 318
Cdd:cd05931     6 RPDRPAYTFLDDeggreeTLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPL--PPPT 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  319 -----KRLVNICKDVDAKVIVCSQELSIGVSGSTLSIGDHNT---------ETATYSAIQAVNTASHDAAYVVYTSGSTG 384
Cdd:cd05931    83 pgrhaERLAAILADAGPRVVLTTAAALAAVRAFAASRPAAGTprllvvdllPDTSAADWPPPSPDPDDIAYLQYTSGSTG 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  385 APKGIVIEHGSFCTNAIASSQAQNLDRSSRVLQFASYAFDVSVHES-LTPLLLGG-CVCIPSEA--QRvnslkeavsTLR 460
Cdd:cd05931   163 TPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGlLTPLYSGGpSVLMSPAAflRR---------PLR 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  461 vnWVEL----------TPTVARLWC-----PADIP-----TVKTLVMGGEPMLPNDISLWKDK-----LR---LVCAYGP 512
Cdd:cd05931   234 --WLRLisryratisaAPNFAYDLCvrrvrDEDLEgldlsSWRVALNGAEPVRPATLRRFAEAfapfgFRpeaFRPSYGL 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  513 AECTVVSTVQSC----------VQELGNIGRSP------------CGTCW------IVSkDNHHRLMPVGCIGELIIGGP 564
Cdd:cd05931   312 AEATLFVSGGPPgtgpvvlrvdRDALAGRAVAVaaddpaarelvsCGRPLpdqevrIVD-PETGRELPDGEVGEIWVRGP 390

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  565 IVGRGYLKQPCLTANAFITNPEwaslfhlNGSYRFYKTGDLVRYnADGTIaYI-GR-KDTQVkLNGQRVELGEIEH---Q 639
Cdd:cd05931   391 SVASGYWGRPEATAETFGALAA-------TDEGGWLRTGDLGFL-HDGEL-YItGRlKDLII-VRGRNHYPQDIEAtaeE 460

                         490       500       510
                  ....*....|....*....|....*....|.
gi 992230864  640 AQPYFRDAVIAAeVAAPAGRKPILILFIARK 670
Cdd:cd05931   461 AHPALRPGCVAA-FSVPDDGEERLVVVAEVE 490
MCS cd05941
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ...
 247-735 5.09e-24

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: 107.38  E-value: 5.09e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  247 DAQAICAWDGTITYRQLDRLS-STVQGLLQQYDLGPGSVVPIIFKKSKWAIVAMLGVLKAGAAFCMLDQSYPTKRLVNIC 325
Cdd:cd05941     1 DRIAIVDDGDSITYADLVARAaRLANRLLALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  326 KDVDAKVIVcsqelsigvsgstlsigdhntetatysaiqavntashDAAYVVYTSGSTGAPKGIVIEHGSFCTNAIASSQ 405
Cdd:cd05941    81 TDSEPSLVL-------------------------------------DPALILYTSGTTGRPKGVVLTHANLAANVRALVD 123

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  406 AQNLDRSSRVLQfASYAFDVS--VHESLTPLLLGG-CVCIPS-EAQRVNSLKE--------AVSTLR---VNWVELTPTV 470
Cdd:cd05941   124 AWRWTEDDVLLH-VLPLHHVHglVNALLCPLFAGAsVEFLPKfDPKEVAISRLmpsitvfmGVPTIYtrlLQYYEAHFTD 202

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  471 ARLWCPADIPTVKTLVMGGEPMLPNDISLWKDK--LRLVCAYGPAEcTVVSTvqSC----VQELGNIGRS-PCGTCWIVS 543
Cdd:cd05941   203 PQFARAAAAERLRLMVSGSAALPVPTLEEWEAItgHTLLERYGMTE-IGMAL--SNpldgERRPGTVGMPlPGVQARIVD 279

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  544 KDNHHRLmPVGCIGELIIGGPIVGRGYLKQPCLTANAFITNpewaslfhlngsyRFYKTGDLVRYNADGTIAYIGR-KDT 622
Cdd:cd05941   280 EETGEPL-PRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDD-------------GWFKTGDLGVVDEDGYYWILGRsSVD 345

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  623 QVKLNGQRVELGEIEHQ--AQPYFRD-AVIAaeVAAPA-GRKPILILFIArkyeysvNMDCTMLLRPpsilFQEKAqgtn 698
Cdd:cd05941   346 IIKSGGYKVSALEIERVllAHPGVSEcAVIG--VPDPDwGERVVAVVVLR-------AGAAALSLEE----LKEWA---- 408

                         490       500       510
                  ....*....|....*....|....*....|....*..
gi 992230864  699 tllQEVLPRHMIPAAYIELLAMPISRTGKVNRKLLRE 735
Cdd:cd05941   409 ---KQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
VL_LC_FACS_like cd05907
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ...
 257-672 5.52e-24

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: 107.68  E-value: 5.52e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  257 TITYRQL-DRLSSTVQGLLQQyDLGPGSVVPIIFKKSKWAIVAMLGVLKAGAAFCMLDQSYPTKRLVNICKDVDAKVIVC 335
Cdd:cd05907     5 PITWAEFaEEVRALAKGLIAL-GVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  336 sqelsigvsgstlsigDHNTETATysaiqavntashdaayVVYTSGSTGAPKGIVIEHGSFCTNAIASSQAQNLDRSSRV 415
Cdd:cd05907    84 ----------------EDPDDLAT----------------IIYTSGTTGRPKGVMLSHRNILSNALALAERLPATEGDRH 131

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  416 LQF--ASYAF-DVSVHesLTPLLLGGCVCIPSEAQRVNS-LKEA-----VSTLRVnW--------VELTPTVAR---LWC 475
Cdd:cd05907   132 LSFlpLAHVFeRRAGL--YVPLLAGARIYFASSAETLLDdLSEVrptvfLAVPRV-WekvyaaikVKAVPGLKRklfDLA 208

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  476 PADIptVKTLVMGGEPmLPNDISLWKDKLRL--VCAYGPAECTVVSTVQScvqelgnIGRSPCGTCWIVSKDNHHRLMPV 553
Cdd:cd05907   209 VGGR--LRFAASGGAP-LPAELLHFFRALGIpvYEGYGLTETSAVVTLNP-------PGDNRIGTVGKPLPGVEVRIADD 278

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  554 gciGELIIGGPIVGRGYLKQPCLTANAFITNPeWaslfhlngsyrfYKTGDLVRYNADGTIAYIGR-KDTQVKLNGQRVE 632
Cdd:cd05907   279 ---GEILVRGPNVMLGYYKNPEATAEALDADG-W------------LHTGDLGEIDEDGFLHITGRkKDLIITSGGKNIS 342

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 992230864  633 LGEIEHQAQ--PYFRDAVIAAEvaapagRKPILILFIARKYE 672
Cdd:cd05907   343 PEPIENALKasPLISQAVVIGD------GRPFLVALIVPDPE 378
23DHB-AMP_lg cd05920
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ...
 246-733 1.16e-23

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: 107.03  E-value: 1.16e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  246 PDAQAICAWDGTITYRQLDRLSSTVQGLLQQYDLGPGSVVPIIFKKSKWAIVAMLGVLKAGAA--FCMldqsyPTKRLVN 323
Cdd:cd05920    29 PDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAVpvLAL-----PSHRRSE 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  324 I---CKDVDAKVIVCSQELSIGvsgstlsigDHNtETATYSAiqavntASH-DAAYVVYTSGSTGAPKGIVIEHGSFCTN 399
Cdd:cd05920   104 LsafCAHAEAVAYIVPDRHAGF---------DHR-ALARELA------ESIpEVALFLLSGGTTGTPKLIPRTHNDYAYN 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  400 AIASSQAQNLDRSSRVLQF--ASYAFDVSVHESLTPLLLGGCVCIPSEAQRVNSLKeAVSTLRVNWVELTPTVARLWC-- 475
Cdd:cd05920   168 VRASAEVCGLDQDTVYLAVlpAAHNFPLACPGVLGTLLAGGRVVLAPDPSPDAAFP-LIEREGVTVTALVPALVSLWLda 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  476 ----PADIPTVKTLVMGGEPMLPNDISLWKDKL--RLVCAYGPAECTVVSTV--QSCVQELGNIGR--SPCGTCWIVskD 545
Cdd:cd05920   247 aasrRADLSSLRLLQVGGARLSPALARRVPPVLgcTLQQVFGMAEGLLNYTRldDPDEVIIHTQGRpmSPDDEIRVV--D 324

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  546 NHHRLMPVGCIGELIIGGPIVGRGYLKQPCLTANAFitNPewaslfhlNGsyrFYKTGDLVRYNADGTIAYIGRKDTQVK 625
Cdd:cd05920   325 EEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAF--TP--------DG---FYRTGDLVRRTPDGYLVVEGRIKDQIN 391

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  626 LNGQRVELGEIEHQ--AQPYFRDaviAAEVAAPAGrkpiliLFIARKYEYSVnmdctmlLRPPSI-LFQEKAQgtntLLQ 702
Cdd:cd05920   392 RGGEKIAAEEVENLllRHPAVHD---AAVVAMPDE------LLGERSCAFVV-------LRDPPPsAAQLRRF----LRE 451

                         490       500       510
                  ....*....|....*....|....*....|.
gi 992230864  703 EVLPRHMIPAAYIELLAMPISRTGKVNRKLL 733
Cdd:cd05920   452 RGLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
PRK06187 PRK06187
long-chain-fatty-acid--CoA ligase; Validated
 234-735 1.31e-23

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


Pssm-ID: 235730 [Multi-domain]  Cd Length: 521  Bit Score: 107.19  E-value: 1.31e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  234 IHTLFRLQCILQPDAQAICAWDGTITYRQLDRLSSTVQGLLQQYDLGPGSVVPIIFKKSKWAIVAMLGVLKAGAAFCMLD 313
Cdd:PRK06187    8 IGRILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPIN 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  314 QSYPTKRLVNICKDVDAKVIVCSQELS----------------IGVSGSTLSigDHNTETATYSAIQA--------VNTA 369
Cdd:PRK06187   88 IRLKPEEIAYILNDAEDRVVLVDSEFVpllaailpqlptvrtvIVEGDGPAA--PLAPEVGEYEELLAaasdtfdfPDID 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  370 SHDAAYVVYTSGSTGAPKGIVIEHGSFCTNAIASSQAQNLDRSSRVL----QFASYAFDVSVHesltPLLLGGCVCIPSE 445
Cdd:PRK06187  166 ENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLvivpMFHVHAWGLPYL----ALMAGAKQVIPRR 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  446 AQrVNSLKEAVSTLRVNWVELTPTV------ARLWCPADIPTVKTLVMGGEPMLPNDISLWKDKL--RLVCAYGPAECTV 517
Cdd:PRK06187  242 FD-PENLLDLIETERVTFFFAVPTIwqmllkAPRAYFVDFSSLRLVIYGGAALPPALLREFKEKFgiDLVQGYGMTETSP 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  518 VSTV-------QSCVQELGNIGRSPCGTCWIVSKDNHHRLMPV-GCIGELIIGGPIVGRGYLKQPCLTANAFItnpewas 589
Cdd:PRK06187  321 VVSVlppedqlPGQWTKRRSAGRPLPGVEARIVDDDGDELPPDgGEVGEIIVRGPWLMQGYWNRPEATAETID------- 393

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  590 lfhlNGsyrFYKTGDLVRYNADGTIaYI-GRKDTQVKLNGQRVELGEIEhqaqpyfrDAVIA----AEVA---AP---AG 658
Cdd:PRK06187  394 ----GG---WLHTGDVGYIDEDGYL-YItDRIKDVIISGGENIYPRELE--------DALYGhpavAEVAvigVPdekWG 457

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 992230864  659 RKPiLILFIARKyeysvNMDCTmllrPPSILfqekaqgtnTLLQEVLPRHMIPAAYIELLAMPISRTGKVNRKLLRE 735
Cdd:PRK06187  458 ERP-VAVVVLKP-----GATLD----AKELR---------AFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVLRE 515
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
 1553-1943 1.44e-23

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: 109.56  E-value: 1.44e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1553 QGLLQTQMLRPFYYQSYTIWEVTTRSKSSPVSPVRLCNAWFTLARRHPALRTHLIDIPLCDGMSSKIHVVHKDYMADAAI 1632
Cdd:COG1020    28 WLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAGRPVQVIQPVVAAPLPVVVLLVDLEALA 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1633 LSCEDEHVITELRKPFLPSDTGLYYPHAFRICQTVSGRVfckLEGGHAFLDATSVLIILRELAQAYD----GQLSSVPGP 1708
Cdd:COG1020   108 EAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLL---LALHHIISDGLSDGLLLAELLRLYLaayaGAPLPLPPL 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1709 SYSSA------VAWLQSLPNGDNRmDYWRRQLKDA-----SPCIFPRLRDQDSPSDTLVVTEQLASTATLTPVCTRHGLT 1777
Cdd:COG1020   185 PIQYAdyalwqREWLQGEELARQL-AYWRQQLAGLpplleLPTDRPRPAVQSYRGARVSFRLPAELTAALRALARRHGVT 263

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1778 VSNVLQVAWGLMLRRYTESDDVCFGALISGRDSriPDVDKMVGPFFNVLVCQLRFGREDSLWDVLRRNQTEIGNRLLNQH 1857
Cdd:COG1020   264 LFMVLLAAFALLLARYSGQDDVVVGTPVAGRPR--PELEGLVGFFVNTLPLRVDLSGDPSFAELLARVRETLLAAYAHQD 341

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1858 CS---LIEVLRFSTYFG-QPLFNTCISVEQ--PLSMDTPDASLCFKELETlEPTEYGIIATITIGTTDVGLGLTYKSDLL 1931
Cdd:COG1020   342 LPferLVEELQPERDLSrNPLFQVMFVLQNapADELELPGLTLEPLELDS-GTAKFDLTLTVVETGDGLRLTLEYNTDLF 420

                         410
                  ....*....|..
gi 992230864 1932 TEDQALAVADRF 1943
Cdd:COG1020   421 DAATIERMAGHL 432
PRK12316 PRK12316
peptide synthase; Provisional
 1540-1907 2.17e-23

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 109.28  E-value: 2.17e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1540 DSIEDAYPCSESHQGLLqtqmLRPFYYQSYTIWEVTTRSKSSPVSPVRLCNAWFTLARRHPALRTHLIDIplcDGMSSKI 1619
Cdd:PRK12316 1551 GEIADIYPLSPMQQGML----FHSLYEQEAGDYINQLRVDVQGLDPDRFRAAWQATVDRHEILRSGFLWQ---DGLEQPL 1623

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1620 HVVHK---------DYMADAAILSCEDEHVITELRKPFLPSDTGLyyphaFRIC--QTVSGRVFCKLEGGHAFLDATSVL 1688
Cdd:PRK12316 1624 QVIHKqvelpfaelDWRGREDLGQALDALAQAERQKGFDLTRAPL-----LRLVlvRTGEGRHHLIYTNHHILMDGWSNA 1698

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1689 IILRELAQAYDGQLSSVPGPSYSSAVAWLQSlPNGDNRMDYWRRQLKD-ASPCIFPR-LRDQDSPSD--TLVVTEQLAST 1764
Cdd:PRK12316 1699 QLLGEVLQRYAGQPVAAPGGRYRDYIAWLQR-QDAAASEAFWKEQLAAlEEPTRLAQaARTEDGQVGygDHQQLLDPAQT 1777

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1765 ATLTPVCTRHGLTVSNVLQVAWGLMLRRYTESDDVCFGALISGRDSRIPDVDKMVGPFFNVLVCQLRFGREDSLWDVLRR 1844
Cdd:PRK12316 1778 RALAEFARAQKVTLNTLVQAAWLLLLQRYTGQETVAFGATVAGRPAELPGIEQQIGLFINTLPVIAAPRPDQSVADWLQE 1857

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1845 NQTEigNRLL--NQHCSLIEVLRFSTYFGQPLFNTCISVE-----QPLSMDTPdASLCFKELETLEPTEY 1907
Cdd:PRK12316 1858 VQAL--NLALreHEHTPLYDIQRWAGQGGEALFDSLLVFEnypvaEALKQGAP-AGLVFGRVSNHEQTNY 1924
DCL_NRPS-like cd19536
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ...
 874-1137 2.36e-23

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: 105.22  E-value: 2.36e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  874 IYPCTPLQEALM---AYTSKRPGAFQaQFRFQLPHQLDMLRLKEAWRIVIAANPILRTRIVFCHTG-ALQVVLRpGEQLQ 949
Cdd:cd19536     1 MYPLSSLQEGMLfhsLLNPGGSVYLH-NYTYTVGRRLNLDLLLEALQVLIDRHDILRTSFIEDGLGqPVQVVHR-QAQVP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  950 WDLINGVHTSPGSLM--------------SYGVPLVDMAITNDTaGKLSRTFCLTMHHAIFDGWSYGLILGAVEDAYKHT 1015
Cdd:cd19536    79 VTELDLTPLEEQLDPlraykeetkirrfdLGRAPLVRAALVRKD-ERERFLLVISDHHSILDGWSLYLLVKEILAVYNQL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1016 NAVQR----PFAPFIKYILH--CNYESAKH--FWCSEFKD--MQALPFPV-----PPLSRGHMANSSTTTHRQihVSEWL 1080
Cdd:cd19536   158 LEYKPlslpPAQPYRDFVAHerASIQQAASerYWREYLAGatLATLPALSeavggGPEQDSELLVSVPLPVRS--RSLAK 235

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 992230864 1081 SSYCTPSTIIQLAFTLLIAWRTESMDVLFGLTVTGRNAPVAGIHRTTGPTIATFPLR 1137
Cdd:cd19536   236 RSGIPLSTLLLAAWALVLSRHSGSDDVVFGTVVHGRSEETTGAERLLGLFLNTLPLR 292
PRK12316 PRK12316
peptide synthase; Provisional
 1346-1933 1.76e-22

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 106.58  E-value: 1.76e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1346 PTDNIRWQLQQLISSLGQSLPRSAVPSLCLPVSFIPVDPLGQPDRIYLCEAASSMTLdflHSLTDPVNkyidyhilPEEA 1425
Cdd:PRK12316 2451 PDDAAEDLLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALPKPDVSQLR---QAYVAPQE--------GLEQ 2519

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1426 RLRGIVAHVLSIdpQNISPKDDFFTLGGDSISAMQVVSLCRKH-QLSLTALDIFNGRTIELIATRLMPLTPYTPPSTPAS 1504
Cdd:PRK12316 2520 RLAAIWQAVLKV--EQVGLDDHFFELGGHSLLATQVVSRVRQDlGLEVPLRILFERPTLAAFAASLESGQTSRAPVLQKV 2597

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1505 DRSLDrrfsllflnsdrdmerleslLMATYDIGSMDSIEDAYPCSESHQgllQTQMLRPfyyqsytiwevttrskSSPVS 1584
Cdd:PRK12316 2598 TRVQP--------------------LPLSHAQQRQWFLWQLEPESAAYH---LPSALHL----------------RGVLD 2638

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1585 PVRLCNAWFTLARRHPALRTHLIDIPlcDGMSSKIHVV--HKDYMADAAILSCE--DEHVITELRKPFLPSDTGLYYPHA 1660
Cdd:PRK12316 2639 QAALEQAFDALVLRHETLRTRFVEVG--EQTRQVILPNmsLRIVLEDCAGVADAaiRQRVAEEIQRPFDLARGPLLRVRL 2716

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1661 FRICQTVSGRVfckLEGGHAFLDATSVLIILRELAQAYDG--QLSSVPGPS----YSSAVAWLQSL---PNGDNRMDYWR 1731
Cdd:PRK12316 2717 LALDGQEHVLV---ITQHHIVSDGWSMQVMVDELVQAYAGarRGEQPTLPPlplqYADYAAWQRAWmdsGEGARQLDYWR 2793

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1732 RQLKDASPCI-----FPRLRDQDSPSDTLVVTEQLASTATLTPVCTRHGLTVSNVLQVAWGLMLRRYTESDDVCFGALIS 1806
Cdd:PRK12316 2794 ERLGGEQPVLelpldRPRPALQSHRGARLDVALDVALSRELLALARREGVTLFMLLLASFQVLLHRYSGQSDIRVGVPIA 2873

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1807 GRDSriPDVDKMVGPFFNVLVCQLRFGREDSLWDVLRRNQTEIGNRLLNQHC---SLIEVL-RFSTYFGQPLFNTCISVE 1882
Cdd:PRK12316 2874 NRNR--AETERLIGFFVNTQVLRAQVDAQLAFRDLLGQVKEQALGAQAHQDLpfeQLVEALqPERSLSHSPLFQVMYNHQ 2951

                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 992230864 1883 QPLSmdtPDASLCFKELETLEP----TEYGIIATITIGTTDVGLGLTYKSDLLTE 1933
Cdd:PRK12316 2952 SGER---AAAQLPGLHIESFAWdgaaTQFDLALDTWESAEGLGASLTYATDLFDA 3003
PRK09088 PRK09088
acyl-CoA synthetase; Validated
 240-736 3.33e-22

acyl-CoA synthetase; Validated


Pssm-ID: 181644 [Multi-domain]  Cd Length: 488  Bit Score: 102.58  E-value: 3.33e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  240 LQCILQPDAQAIC------AWdgtiTYRQLDRLSSTVQGLLQQYDLGPGSVVPIIFKKSKWAIVAMLGVLKAGAAFCMLD 313
Cdd:PRK09088    3 FHARLQPQRLAAVdlalgrRW----TYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLN 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  314 QSYPTKRLVNICKDVDAKVIVCSQELSIGvsgsTLSIGDHNTETATYSAIQAVNTASHDA---AYVVYTSGSTGAPKGIV 390
Cdd:PRK09088   79 WRLSASELDALLQDAEPRLLLGDDAVAAG----RTDVEDLAAFIASADALEPADTPSIPPervSLILFTSGTSGQPKGVM 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  391 IEHGSFCTNAIASSQAQNLDRSSRVLQFASYAFDVSVHESLTPLLL-GGCVCIPS--EAQRVNSlKEAVSTLRVNWVELT 467
Cdd:PRK09088  155 LSERNLQQTAHNFGVLGRVDAHSSFLCDAPMFHIIGLITSVRPVLAvGGSILVSNgfEPKRTLG-RLGDPALGITHYFCV 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  468 PTVARL------WCPADIPTVKTLVMGGEPMLPNDISLWKDK-LRLVCAYG----------PAECTVVSTvqscvqELGN 530
Cdd:PRK09088  234 PQMAQAfraqpgFDAAALRHLTALFTGGAPHAAEDILGWLDDgIPMVDGFGmseagtvfgmSVDCDVIRA------KAGA 307

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  531 IG-RSPCGTCWIVskDNHHRLMPVGCIGELIIGGPIVGRGYLKQPCLTANAFiTNPEWaslfhlngsyrfYKTGDLVRYN 609
Cdd:PRK09088  308 AGiPTPTVQTRVV--DDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAF-TGDGW------------FRTGDIARRD 372

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  610 ADGTIAYIGRKDTQVKLNGQRVELGEIEhqaqpyfrdAVIAAEvaaPAGRKPILI-LFIARKYEYSVnmdCTMLLRPPSI 688
Cdd:PRK09088  373 ADGFFWVVDRKKDMFISGGENVYPAEIE---------AVLADH---PGIRECAVVgMADAQWGEVGY---LAIVPADGAP 437

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*...
gi 992230864  689 LfqeKAQGTNTLLQEVLPRHMIPAAYIELLAMPISRTGKVNRKLLREA 736
Cdd:PRK09088  438 L---DLERIRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARLRDA 482
BCL_like cd05919
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ...
 250-734 4.03e-22

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: 101.77  E-value: 4.03e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  250 AICAWDGTITYRQLDRLSSTVQGLLQQYDLGPGSVVPIIFKKSKWAIVAMLGVLKAGAAFCMLDQSYPTKRLVNICKDVD 329
Cdd:cd05919     3 AFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  330 AKVIVCSQElsigvsgstlsigdhntetatysaiqavntashDAAYVVYTSGSTGAPKGIVIEHGS-------FCTNAIA 402
Cdd:cd05919    83 ARLVVTSAD---------------------------------DIAYLLYSSGTTGPPKGVMHAHRDpllfadaMAREALG 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  403 ssqaqnLDRSSRVLQFASYAFDVSVHESLT-PLLLGGCVCIPSEAQRVNSLKEAVSTLRVNWVELTPTV-ARL-----WC 475
Cdd:cd05919   130 ------LTPGDRVFSSAKMFFGYGLGNSLWfPLAVGASAVLNPGWPTAERVLATLARFRPTVLYGVPTFyANLldscaGS 203

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  476 PADIPTVKTLVMGGEPMLPNDISLWKDKLRLVCAYGPAeCTVVSTVQSCVQ----ELGNIGRS-PCGTCWIVSKDNHHrl 550
Cdd:cd05919   204 PDALRSLRLCVSAGEALPRGLGERWMEHFGGPILDGIG-ATEVGHIFLSNRpgawRLGSTGRPvPGYEIRLVDEEGHT-- 280

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  551 MPVGCIGELIIGGPIVGRGYLKQPCLTANAFitNPEWaslfhlngsyrfYKTGDLVRYNADGTIAYIGRKDTQVKLNGQR 630
Cdd:cd05919   281 IPPGEEGDLLVRGPSAAVGYWNNPEKSRATF--NGGW------------YRTGDKFCRDADGWYTHAGRADDMLKVGGQW 346

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  631 VELGEIEHQAQPYfrDAVI-AAEVAAPAGRKPI-LILFIarkyeysvnmdctmLLRPPSILFQEKAQGTNTLLQEVLPRH 708
Cdd:cd05919   347 VSPVEVESLIIQH--PAVAeAAVVAVPESTGLSrLTAFV--------------VLKSPAAPQESLARDIHRHLLERLSAH 410

                         490       500
                  ....*....|....*....|....*.
gi 992230864  709 MIPAAYIELLAMPISRTGKVNRKLLR 734
Cdd:cd05919   411 KVPRRIAFVDELPRTATGKLQRFKLR 436
PRK12316 PRK12316
peptide synthase; Provisional
 865-1295 5.69e-22

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 104.65  E-value: 5.69e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  865 SVFPEQIEDIYPCTPLQEALMAYTSKRP--GAFQAQFRFQLpHQLDMLRLKEAWRIVIAANPILRTRIVFcHTG---ALQ 939
Cdd:PRK12316 1547 PLPAGEIADIYPLSPMQQGMLFHSLYEQeaGDYINQLRVDV-QGLDPDRFRAAWQATVDRHEILRSGFLW-QDGleqPLQ 1624

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  940 VVLR----PGEQLQWDLINGVHTSPGSLMS---------YGVPLVDMAITNDTAGKLSRTFclTMHHAIFDGWSYGLILG 1006
Cdd:PRK12316 1625 VIHKqvelPFAELDWRGREDLGQALDALAQaerqkgfdlTRAPLLRLVLVRTGEGRHHLIY--TNHHILMDGWSNAQLLG 1702

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1007 AVEDAYkhtnAVQRPFAP------FIKYILHCNYESAKHFWCSEFKD-------MQALPFPVPPlsRGHMANSSTTTHRQ 1073
Cdd:PRK12316 1703 EVLQRY----AGQPVAAPggryrdYIAWLQRQDAAASEAFWKEQLAAleeptrlAQAARTEDGQ--VGYGDHQQLLDPAQ 1776

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1074 IHVsewLSSYC-----TPSTIIQLAFTLLIAWRTESMDVLFGLTVTGRNAPVAGIHRTTGPTIATFPLRTILYGTMNITD 1148
Cdd:PRK12316 1777 TRA---LAEFAraqkvTLNTLVQAAWLLLLQRYTGQETVAFGATVAGRPAELPGIEQQIGLFINTLPVIAAPRPDQSVAD 1853

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1149 ALLCMQNHIATLIPFEHTGLRRIKSFGTETARACqFQSLLIIQ--PVTyrESSE------IFFELESNeHEQSKFstcPL 1220
Cdd:PRK12316 1854 WLQEVQALNLALREHEHTPLYDIQRWAGQGGEAL-FDSLLVFEnyPVA--EALKqgapagLVFGRVSN-HEQTNY---PL 1926

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 992230864 1221 TLVCELrTHSVSVKAISDNAVVISGDMERLLDQLEYLIDMITKSPTLEIQNIipSPQDTYSYALQQSQyWSSHIE 1295
Cdd:PRK12316 1927 TLAVTL-GETLSLQYSYDRGHFDAAAIERLDRHLLHLLEQMAEDAQAALGEL--ALLDAGERQRILAD-WDRTPE 1997
Condensation pfam00668
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ...
 871-1269 1.41e-21

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: 100.10  E-value: 1.41e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864   871 IEDIYPCTPLQEAlMAYTSK---RPGAFQAQFRFQLPHQLDMLRLKEAWRIVIAANPILRTRIVFCHTGALQVVLRPGEQ 947
Cdd:pfam00668    1 VQDEYPLSPAQKR-MWFLEKlepHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIRQENGEPVQVILEERP 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864   948 LQWDLINGVHTSpgslMSYGVPLVDMAITNDTAGKL-----------------SRTFCL-TMHHAIFDGWSYGLILGAVE 1009
Cdd:pfam00668   80 FELEIIDISDLS----ESEEEEAIEAFIQRDLQSPFdlekgplfraglfriaeNRHHLLlSMHHIIVDGVSLGILLRDLA 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  1010 DAYKHT----NAVQRPFAPFIKYILHCN-------YESAKHFW---CSEFKDMQALPFPVPPLS-------------RGH 1062
Cdd:pfam00668  156 DLYQQLlkgePLPLPPKTPYKDYAEWLQqylqsedYQKDAAYWleqLEGELPVLQLPKDYARPAdrsfkgdrlsftlDED 235

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  1063 MANSSTTTHRQIHVsewlssycTPSTIIQLAFTLLIAWRTESMDVLFGLTVTGRNAPvaGIHRTTGPTIATFPLRTILYG 1142
Cdd:pfam00668  236 TEELLRKLAKAHGT--------TLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPSP--DIERMVGMFVNTLPLRIDPKG 305

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  1143 TMNITDALLCMQNHIATLIPFEHTGLRRIKSFGT---ETARACQFQSLLIIQPVTYRES-------SEIFFELESNEHEQ 1212
Cdd:pfam00668  306 GKTFSELIKRVQEDLLSAEPHQGYPFGDLVNDLRlprDLSRHPLFDPMFSFQNYLGQDSqeeefqlSELDLSVSSVIEEE 385

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 992230864  1213 SKFstcPLTLVCELRTHSVSVKAISDNAVVISGDMERLLDQLEYLIDMITKSPTLEI 1269
Cdd:pfam00668  386 AKY---DLSLTASERGGGLTIKIDYNTSLFDEETIERFAEHFKELLEQAIAHPSQPL 439
CHC_CoA_lg cd05903
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ...
 257-637 1.68e-21

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: 99.76  E-value: 1.68e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  257 TITYRQLDRLSSTVQGLLQQYDLGPGSVVpiIFKKSKW--AIVAMLGVLKAGAAFCMLDQSYPTKRLVNICKDVDAKVIV 334
Cdd:cd05903     1 RLTYSELDTRADRLAAGLAALGVGPGDVV--AFQLPNWweFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  335 CSQELsigvsGSTlsigDHNTETAtysaiqavntashDAAYVVYTSGSTGAPKGIVIEHGSFCTNAIASSQAQNLDRSSR 414
Cdd:cd05903    79 VPERF-----RQF----DPAAMPD-------------AVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPGDV 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  415 VLQFASYA-FDVSVHESLTPLLLGgcvcIPSEAQRVNSLKEAVSTLRVNWVEL----TPTVARL-----WCPADIPTVKT 484
Cdd:cd05903   137 FLVASPMAhQTGFVYGFTLPLLLG----APVVLQDIWDPDKALALMREHGVTFmmgaTPFLTDLlnaveEAGEPLSRLRT 212

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  485 LVMGGEPMLPNDIS-LWKDKLRLVC-AYGPAECTvvSTVQSC-----VQELGNIGRSPCGTCWIVSKDNHHRLMPvGCIG 557
Cdd:cd05903   213 FVCGGATVPRSLARrAAELLGAKVCsAYGSTECP--GAVTSItpapeDRRLYTDGRPLPGVEIKVVDDTGATLAP-GVEG 289

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  558 ELIIGGPIVGRGYLKQPCLTANAFitnPEwaslfhlngsyRFYKTGDLVRYNADGTIAYIGRKDTQVKLNGQRVELGEIE 637
Cdd:cd05903   290 ELLSRGPSVFLGYLDRPDLTADAA---PE-----------GWFRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVE 355
PRK06087 PRK06087
medium-chain fatty-acid--CoA ligase;
259-735 1.36e-20

medium-chain fatty-acid--CoA ligase;


Pssm-ID: 180393 [Multi-domain]  Cd Length: 547  Bit Score: 98.28  E-value: 1.36e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  259 TYRQLDRLSSTVQGLLQQYDLGPGSVVPiiFKKSKWA--IVAMLGVLKAGAAFCMLDQSYPTKRLVNICKDVDAKVIVC- 335
Cdd:PRK06087   51 TYSALDHAASRLANWLLAKGIEPGDRVA--FQLPGWCefTIIYLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFAp 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  336 ---------SQELSIGVSGSTLsigDH---------NTETATYSAI--------QAVNTASHDAAYVVYTSGSTGAPKGI 389
Cdd:PRK06087  129 tlfkqtrpvDLILPLQNQLPQL---QQivgvdklapATSSLSLSQIiadyepltTAITTHGDELAAVLFTSGTEGLPKGV 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  390 VIEHgsfcTNAIASSQA----QNLDRSSRVLQFASYAFDVSVHESLT-PLLLGGCVCIpseAQRVNSLK--EAVSTLRVN 462
Cdd:PRK06087  206 MLTH----NNILASERAycarLNLTWQDVFMMPAPLGHATGFLHGVTaPFLIGARSVL---LDIFTPDAclALLEQQRCT 278

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  463 WVE-LTPTVARLWC-----PADIPTVKTLVMGGEPmLPNDIS--LWKDKLRLVCAYGPAECT--VVSTVQSCVQELGNIG 532
Cdd:PRK06087  279 CMLgATPFIYDLLNllekqPADLSALRFFLCGGTT-IPKKVAreCQQRGIKLLSVYGSTESSphAVVNLDDPLSRFMHTD 357

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  533 RSPCGTCWIVSKDNHHRLMPVGCIGELIIGGPIVGRGYLKQPCLTANAfITNPEWaslfhlngsyrFYkTGDLVRYNADG 612
Cdd:PRK06087  358 GYAAAGVEIKVVDEARKTLPPGCEGEEASRGPNVFMGYLDEPELTARA-LDEEGW-----------YY-SGDLCRMDEAG 424

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  613 TIAYIGRKDTQVKLNGQRVELGEIE-HQAQ-PYFRDaviAAEVAAPAGRKPILIlfiarkyeysvnmdCTMLLRPPSILF 690
Cdd:PRK06087  425 YIKITGRKKDIIVRGGENISSREVEdILLQhPKIHD---ACVVAMPDERLGERS--------------CAYVVLKAPHHS 487

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*
gi 992230864  691 QEKAQGTNTLLQEVLPRHMIPAAYIELLAMPISRTGKVNRKLLRE 735
Cdd:PRK06087  488 LTLEEVVAFFSRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLLRK 532
PRK06188 PRK06188
acyl-CoA synthetase; Validated
 246-620 1.76e-20

acyl-CoA synthetase; Validated


Pssm-ID: 235731 [Multi-domain]  Cd Length: 524  Bit Score: 97.75  E-value: 1.76e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  246 PDAQAICAWDGTITYRQLDRLSSTVQGLLQQYDLGPGSVVPIIFKKSKWAIVAMLGVLKAGAAFCML-------DQSYpt 318
Cdd:PRK06188   26 PDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALhplgsldDHAY-- 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  319 krlvnICKDVDAKVIVC--------SQELSIGVSGST--LSIG------DHNTETATYSAIQAVNTASH-DAAYVVYTSG 381
Cdd:PRK06188  104 -----VLEDAGISTLIVdpapfverALALLARVPSLKhvLTLGpvpdgvDLLAAAAKFGPAPLVAAALPpDIAGLAYTGG 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  382 STGAPKGIVIEHGSFCTNAIASSQAQNLDRSSRVL-----QFASYAFDVSVhesltpLLLGGCVCI-----PSEAQRvns 451
Cdd:PRK06188  179 TTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFLmctplSHAGGAFFLPT------LLRGGTVIVlakfdPAEVLR--- 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  452 lkeAVSTLRVNWVELTPTV--ARLWCP----ADIPTVKTLVMGGEPMLPndislwkDKLR---------LVCAYGPAECT 516
Cdd:PRK06188  250 ---AIEEQRITATFLVPTMiyALLDHPdlrtRDLSSLETVYYGASPMSP-------VRLAeaierfgpiFAQYYGQTEAP 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  517 VVSTV-------QSCVQELGNIGRsPCGTCWIVSKDNHHRLMPVGCIGELIIGGPIVGRGYLKQPCLTANAFitnpewas 589
Cdd:PRK06188  320 MVITYlrkrdhdPDDPKRLTSCGR-PTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAF-------- 390

                         410       420       430
                  ....*....|....*....|....*....|.
gi 992230864  590 lfhLNGsyrFYKTGDLVRYNADGTIAYIGRK 620
Cdd:PRK06188  391 ---RDG---WLHTGDVAREDEDGFYYIVDRK 415
LC_FACS_like cd05935
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ...
 258-733 2.02e-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: 96.39  E-value: 2.02e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  258 ITYRQLDRLSSTVQGLLQQYDLGPGSVVPIIFKKSKWAIVAMLGVLKAGAAFCMLDQSYPTKRLVNICKDVDAKVIVCSQ 337
Cdd:cd05935     2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVGS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  338 ELSigvsgstlsigdhntetatysaiqavntashDAAYVVYTSGSTGAPKGIVIEHGSFCTNAIASSQAQNLDRSSRVLQ 417
Cdd:cd05935    82 ELD-------------------------------DLALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTPSDVILA 130

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  418 FASYaFDVS--VHESLTPLLLGGCVCIPSEAQRvNSLKEAVSTLRVN-WVELTPTVARLWCP-----ADIPTVKTLVMGG 489
Cdd:cd05935   131 CLPL-FHVTgfVGSLNTAVYVGGTYVLMARWDR-ETALELIEKYKVTfWTNIPTMLVDLLATpefktRDLSSLKVLTGGG 208

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  490 EPMLPNDISLWKDK--LRLVCAYGPAE-CTVVSTVQSCVQELGNIGRSPCGTCWIVSKDNHHRLMPVGCIGELIIGGPIV 566
Cdd:cd05935   209 APMPPAVAEKLLKLtgLRFVEGYGLTEtMSQTHTNPPLRPKLQCLGIP*FGVDARVIDIETGRELPPNEVGEIVVRGPQI 288

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  567 GRGYLKQPCLTANAFITnpewaslfhLNGSyRFYKTGDLVRYNADGTIAYIGRKDTQVKLNGQRVELGEIEhqAQPYFRD 646
Cdd:cd05935   289 FKGYWNRPEETEESFIE---------IKGR-RFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVE--AKLYKHP 356

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  647 AVI-AAEVAAP---AGRKPilILFIARKYEYSVNMDctmllrppsilfqekAQGTNTLLQEVLPRHMIPAAYIELLAMPI 722
Cdd:cd05935   357 AI*eVCVISVPderVGEEV--KAFIVLRPEYRGKVT---------------EEDIIEWAREQMAAYKYPREVEFVDELPR 419

                         490
                  ....*....|.
gi 992230864  723 SRTGKVNRKLL 733
Cdd:cd05935   420 SASGKILWRLL 430
MACS_like_3 cd05971
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
 259-734 2.03e-20

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: 96.35  E-value: 2.03e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  259 TYRQLDRLSSTVQGLLQQYDLGPGSVVPIIFKKSKWAIVAMLGVLKAGAafcmldqsyptkrlvnickdvdakvivcsqe 338
Cdd:cd05971     8 TFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGA------------------------------- 56

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  339 lsIGVSGSTLsIGDHNTE--TATYSAIQAVNTASHDAAYVVYTSGSTGAPKGIVIEHGSFCTNAIASSQAQNLDRSSRVL 416
Cdd:cd05971    57 --IAVPLFAL-FGPEALEyrLSNSGASALVTDGSDDPALIIYTSGTTGPPKGALHAHRVLLGHLPGVQFPFNLFPRDGDL 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  417 QF--ASYAFDVSVHESLTPLLLGGCVCIPSEAQRVNSLK--EAVSTLRVNWVELTPTVARLWCPADIP------TVKTLV 486
Cdd:cd05971   134 YWtpADWAWIGGLLDVLLPSLYFGVPVLAHRMTKFDPKAalDLMSRYGVTTAFLPPTALKMMRQQGEQlkhaqvKLRAIA 213

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  487 MGGEPmLPNDISLW-KDKLRLVCA--YGPAECTVVSTVQSCVQEL--GNIGRSPCGTCWIVSKDNHHRLmPVGCIGELII 561
Cdd:cd05971   214 TGGES-LGEELLGWaREQFGVEVNefYGQTECNLVIGNCSALFPIkpGSMGKPIPGHRVAIVDDNGTPL-PPGEVGEIAV 291

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  562 ggpivgrgylKQPCltANAFIT---NPEwASLFHLNGSYrfYKTGDLVRYNADGTIAYIGRKDTQVKLNGQRVELGEIEH 638
Cdd:cd05971   292 ----------ELPD--PVAFLGywnNPS-ATEKKMAGDW--LLTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEE 356

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  639 --QAQPYFRDaviAAEVAAP-AGRKPILILFIarkyeysvnmdctmLLRPPSILFQEKAQGTNTLLQEVLPRHMIPAAYI 715
Cdd:cd05971   357 clLKHPAVLM---AAVVGIPdPIRGEIVKAFV--------------VLNPGETPSDALAREIQELVKTRLAAHEYPREIE 419

                         490
                  ....*....|....*....
gi 992230864  716 ELLAMPISRTGKVNRKLLR 734
Cdd:cd05971   420 FVNELPRTATGKIRRRELR 438
PRK08633 PRK08633
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
 372-742 2.51e-20

2-acyl-glycerophospho-ethanolamine acyltransferase; Validated


Pssm-ID: 236315 [Multi-domain]  Cd Length: 1146  Bit Score: 98.84  E-value: 2.51e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  372 DAAYVVYTSGSTGAPKGIVIEHGSFCTNAIASSQAQNLDRSSRVLQ----FASYAFDVSVhesLTPLLLG-GCVCIPS-- 444
Cdd:PRK08633  783 DTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILSslpfFHSFGLTVTL---WLPLLEGiKVVYHPDpt 859

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  445 EAQRVNslkEAVSTLRVNWVELTPTVARLWC------PADIPTVKtLVMGGEPMLPNDISL-WKDK--LRLVCAYGPAEC 515
Cdd:PRK08633  860 DALGIA---KLVAKHRATILLGTPTFLRLYLrnkklhPLMFASLR-LVVAGAEKLKPEVADaFEEKfgIRILEGYGATET 935

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  516 TVVSTV--------QSCVQ---ELGNIGRSPCGTCW-IVSKDNHHRLmPVGCIGELIIGGPIVGRGYLKQPCLTANAfit 583
Cdd:PRK08633  936 SPVASVnlpdvlaaDFKRQtgsKEGSVGMPLPGVAVrIVDPETFEEL-PPGEDGLILIGGPQVMKGYLGDPEKTAEV--- 1011

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  584 npewasLFHLNGSyRFYKTGDLVRYNADGTIAYIGRKDTQVKLNGQRVELGEIEHQAQPYFRD-AVIAAEVAAPAgrkpi 662
Cdd:PRK08633 1012 ------IKDIDGI-GWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAKALGGeEVVFAVTAVPD----- 1079

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  663 lilfiARKYEYSVnmdctMLLRPPSILFQEKAQGtntLLQEVLPRHMIPAAYIELLAMPISRTGKVNRKLLREAVEQASE 742
Cdd:PRK08633 1080 -----EKKGEKLV-----VLHTCGAEDVEELKRA---IKESGLPNLWKPSRYFKVEALPLLGSGKLDLKGLKELALALLG 1146
beta-lac_NRPS cd19547
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ...
 874-1188 3.12e-20

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: 95.84  E-value: 3.12e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  874 IYPCTPLQEALMAYTSKRPG--AFQAQFRFQLPHQLDMLRLKEAWRIVIAANPILRTRIVFCHTGALQVVLRPGEQLQWD 951
Cdd:cd19547     1 VYPLAPMQEGMLFRGLFWPDsdAYFNQNVLELVGGTDEDVLREAWRRVADRYEILRTGFTWRDRAEPLQYVRDDLAPPWA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  952 LINGVHTSPgslmSYGVPLVDMAITNDTAGKLSRTFC----LTM--------------HHAIFDGWSYGLILGAVEDAYK 1013
Cdd:cd19547    81 LLDWSGEDP----DRRAELLERLLADDRAAGLSLADCplyrLTLvrlgggrhyllwshHHILLDGWCLSLIWGDVFRVYE 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1014 ---HTNAVQ----RPFAPFIKYILH--CNYESAKHFWCSEFKDMQALPFPVPPLSRG---HMANSSTTTHRQIHVSEWLS 1081
Cdd:cd19547   157 elaHGREPQlspcRPYRDYVRWIRArtAQSEESERFWREYLRDLTPSPFSTAPADREgefDTVVHEFPEQLTRLVNEAAR 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1082 SY-CTPSTIIQLAFTLLIAWRTESMDVLFGLTVTGRNAPVAGIHRTTGPTIATFPLRTILYGTMNITDALLCMQNHIATL 1160
Cdd:cd19547   237 GYgVTTNAISQAAWSMLLALQTGARDVVHGLTIAGRPPELEGSEHMVGIFINTIPLRIRLDPDQTVTGLLETIHRDLATT 316

                         330       340       350
                  ....*....|....*....|....*....|
gi 992230864 1161 IPFEHTGLRRIKSF--GTETARACQFQSLL 1188
Cdd:cd19547   317 AAHGHVPLAQIKSWasGERLSGGRVFDNLV 346
PRK12467 PRK12467
peptide synthase; Provisional
 866-1265 6.30e-20

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 97.92  E-value: 6.30e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  866 VFPEQIEDIYPCTPLQEALMAYT--SKRPGAFQAQFRFQLpHQLDMLRLKEAWRIVIAANPILRTRivFCHTGA----LQ 939
Cdd:PRK12467 2638 VAVGDIEDIYPLSPMQQGMLFHTlyEGGAGDYINQMRVDV-EGLDVERFRTAWQAVIDRHEILRSG--FLWDGEleepLQ 2714

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  940 VVLR----PGEQLQWdliNGVHTSPGSLMSYGV------------PLVDMAITNdTAGKLSRtFCLTMHHAIFDGWSYGL 1003
Cdd:PRK12467 2715 VVYKqarlPFSRLDW---RDRADLEQALDALAAadrqqgfdllsaPLLRLTLVR-TGEDRHH-LIYTNHHILMDGWSGSQ 2789

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1004 ILGAVEDAYkhtnAVQRPFAP------FIKYILHCNYESAKHFWCSEFKDMQ-------ALPF-PVPPLSrGHMAN---- 1065
Cdd:PRK12467 2790 LLGEVLQRY----FGQPPPARegryrdYIAWLQAQDAEASEAFWKEQLAALEeptrlarALYPaPAEAVA-GHGAHylhl 2864

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1066 SSTTTHRqihVSEWLSSY-CTPSTIIQLAFTLLIAWRTESMDVLFGLTVTGRNAPVAGIHRTTGPTIATFPLRTILYGTM 1144
Cdd:PRK12467 2865 DATQTRQ---LIEFARRHrVTLNTLVQGAWLLLLQRFTGQDTVCFGATVAGRPAQLRGAEQQLGLFINTLPVIASPRAEQ 2941

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1145 NITDALLCMQNHIATLIPFEHTGLRRIKSFGTETARACqFQSLLIIQ--PVTYR----ESSEIFFELESNeHEQSKFstc 1218
Cdd:PRK12467 2942 TVSDWLQQVQAQNLALREFEHTPLADIQRWAGQGGEAL-FDSILVFEnyPISEAlkqgAPSGLRFGAVSS-REQTNY--- 3016

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*..
gi 992230864 1219 PLTLVCELrTHSVSVKAISDNAVVISGDMERLLDQLEYLIDMITKSP 1265
Cdd:PRK12467 3017 PLTLAVGL-GDTLELEFSYDRQHFDAAAIERLAESFDRLLQAMLNNP 3062
PRK12467 PRK12467
peptide synthase; Provisional
 1522-1907 2.16e-19

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 96.00  E-value: 2.16e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1522 DMERLESLLMATYDIgsmdsiEDAYPCSESHQGLLqtqmLRPFYYQSYTIWEVTTRSKSSPVSPVRLCNAWFTLARRHPA 1601
Cdd:PRK12467 2629 SQEQLDRLPVAVGDI------EDIYPLSPMQQGML----FHTLYEGGAGDYINQMRVDVEGLDVERFRTAWQAVIDRHEI 2698

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1602 LRTHLIDIplcDGMSSKIHVVHKDYMADAAILSCEDEHVITELRKPFLPSDTG----LYYPHAFRICQTVSGRVFCKL-- 1675
Cdd:PRK12467 2699 LRSGFLWD---GELEEPLQVVYKQARLPFSRLDWRDRADLEQALDALAAADRQqgfdLLSAPLLRLTLVRTGEDRHHLiy 2775

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1676 EGGHAFLDATSVLIILRELAQAYDGQLSSVPGPSYSSAVAWLQSLPNGDNRMdYWRRQLKD-ASPCIFPRLRdQDSPSDT 1754
Cdd:PRK12467 2776 TNHHILMDGWSGSQLLGEVLQRYFGQPPPAREGRYRDYIAWLQAQDAEASEA-FWKEQLAAlEEPTRLARAL-YPAPAEA 2853

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1755 LVVTEQL------ASTATLTPVCTRHGLTVSNVLQVAWGLMLRRYTESDDVCFGALISGRDSRIPDVDKMVGPFFNVL-- 1826
Cdd:PRK12467 2854 VAGHGAHylhldaTQTRQLIEFARRHRVTLNTLVQGAWLLLLQRFTGQDTVCFGATVAGRPAQLRGAEQQLGLFINTLpv 2933

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1827 VCQLRfgREDSLWDVLRRNQTEigNRLLN--QHCSLIEVLRFSTYFGQPLFNTCISVEQ-PLS---MDTPDASLCFKELE 1900
Cdd:PRK12467 2934 IASPR--AEQTVSDWLQQVQAQ--NLALRefEHTPLADIQRWAGQGGEALFDSILVFENyPISealKQGAPSGLRFGAVS 3009


                  ....*..
gi 992230864 1901 TLEPTEY 1907
Cdd:PRK12467 3010 SREQTNY 3016
MACS_like_4 cd05969
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ...
 259-734 2.41e-19

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: 93.34  E-value: 2.41e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  259 TYRQLDRLSSTVQGLLQQYDLGPGSVVPIIFKKSKWAIVAMLGVLKAGAAFCMLDQSYPTKRLVNICKDVDAKVIVCSQE 338
Cdd:cd05969     2 TFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTEE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  339 LsigvsgstlsigdhntetatysaiqAVNTASHDAAYVVYTSGSTGAPKGIVIEHGSFCTNAIASSQAQNLDRSSRVLQF 418
Cdd:cd05969    82 L-------------------------YERTDPEDPTLLHYTSGTTGTPKGVLHVHDAMIFYYFTGKYVLDLHPDDIYWCT 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  419 ASYAFDVSVHESLTPLLLGGCVCIPSEAQ-RVNSLKEAVSTLRVNWVELTPTVARLWCPA--------DIPTVKTLVMGG 489
Cdd:cd05969   137 ADPGWVTGTVYGIWAPWLNGVTNVVYEGRfDAESWYGIIERVKVTVWYTAPTAIRMLMKEgdelarkyDLSSLRFIHSVG 216

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  490 EPMLPnDISLWKDK---LRLVCAYGPAEcTVVSTVQSCVQ---ELGNIGRSPCGTCWIVSKDNHHRLmPVGCIGELII-- 561
Cdd:cd05969   217 EPLNP-EAIRWGMEvfgVPIHDTWWQTE-TGSIMIANYPCmpiKPGSMGKPLPGVKAAVVDENGNEL-PPGTKGILALkp 293

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  562 GGPIVGRGYLKQPCLTANAFITNpewaslfhlngsyrFYKTGDLVRYNADGTIAYIGRKDTQVKLNGQR-----VELGEI 636
Cdd:cd05969   294 GWPSMFRGIWNDEERYKNSFIDG--------------WYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRvgpfeVESALM 359

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  637 EHQAqpyfrdaviAAEVAAPAGRKPIL----ILFIARKYEYSVnmdcTMLLRPPSILFQEKAQGTNtllqeVLPRHmipa 712
Cdd:cd05969   360 EHPA---------VAEAGVIGKPDPLRgeiiKAFISLKEGFEP----SDELKEEIINFVRQKLGAH-----VAPRE---- 417

                         490       500
                  ....*....|....*....|...
gi 992230864  713 ayIELL-AMPISRTGKVNRKLLR 734
Cdd:cd05969   418 --IEFVdNLPKTRSGKIMRRVLK 438
PRK07786 PRK07786
long-chain-fatty-acid--CoA ligase; Validated
 244-744 3.85e-19

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


Pssm-ID: 169098 [Multi-domain]  Cd Length: 542  Bit Score: 93.69  E-value: 3.85e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  244 LQPDAQAICAWDGTITYRQLDRLSSTVQGLLQQYDLGPGSVVPIIFKKSKWAIVAMLGVLKAGAAFCMLDQSYPTKRLVN 323
Cdd:PRK07786   29 MQPDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAF 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  324 ICKDVDAKVIVCSQELS------------------IGVSGSTLSIGDHNTETATYSAIQAVNTASHDAAYVVYTSGSTGA 385
Cdd:PRK07786  109 LVSDCGAHVVVTEAALApvatavrdivpllstvvvAGGSSDDSVLGYEDLLAEAGPAHAPVDIPNDSPALIMYTSGTTGR 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  386 PKGIVIEHGSFCTNAIASSQAQNLDRSSRVLQFASYAFDVSVHESLTP-LLLGGCVCI-PSEAQRVNSLKEAVSTLRVNW 463
Cdd:PRK07786  189 PKGAVLTHANLTGQAMTCLRTNGADINSDVGFVGVPLFHIAGIGSMLPgLLLGAPTVIyPLGAFDPGQLLDVLEAEKVTG 268

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  464 VELTPTVARLWC------PADIpTVKTLVMGGEP---MLPNDISLWKDKLRLVCAYGPAECTVVSTV---QSCVQELGNI 531
Cdd:PRK07786  269 IFLVPAQWQAVCaeqqarPRDL-ALRVLSWGAAPasdTLLRQMAATFPEAQILAAFGQTEMSPVTCMllgEDAIRKLGSV 347

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  532 GRsPCGTCWIVSKDNHHRLMPVGCIGELIIGGPIVGRGYLKQPCLTANAFITNpeWaslFHlngsyrfykTGDLVRYNAD 611
Cdd:PRK07786  348 GK-VIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFAGG--W---FH---------SGDLVRQDEE 412

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  612 GTIAYIGRKDTQVKLNGQRVELGEIEH--QAQPYFRDAVIAAEVAAPAGRKPILIlfiarkyeysvnmdctMLLRPPS-- 687
Cdd:PRK07786  413 GYVWVVDRKKDMIISGGENIYCAEVENvlASHPDIVEVAVIGRADEKWGEVPVAV----------------AAVRNDDaa 476

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 992230864  688 ILFQEKAQgtntLLQEVLPRHMIPAAYIELLAMPISRTGKVNRKLLREAVEQASEKD 744
Cdd:PRK07786  477 LTLEDLAE----FLTDRLARYKHPKALEIVDALPRNPAGKVLKTELRERYGACVNVE 529
menE TIGR01923
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ...
 259-733 4.45e-19

O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, which is involved in the fourth step of the menaquinone biosynthesis pathway. O-succinylbenzoate-CoA ligase, together with menB - naphtoate synthase, take 2-succinylbenzoate and convert it into 1,4-di-hydroxy-2- naphtoate. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 162605 [Multi-domain]  Cd Length: 436  Bit Score: 92.51  E-value: 4.45e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864   259 TYRQLDRLSSTVQGLLQQYDLGPGSVVPIIFKKSKWAIVAMLGVLKAGAAFCMLDQSYPTKRLVNICKDVDAKVIVCSQE 338
Cdd:TIGR01923    1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTDSL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864   339 LSIGVsgsTLSIGDHNTETATYSAIQAVNTASHDA-AYVVYTSGSTGAPKGIVIEHGSFCTNAIASSQAQNLDRSSRVLq 417
Cdd:TIGR01923   81 LEEKD---FQADSLDRIEAAGRYETSLSASFNMDQiATLMFTSGTTGKPKAVPHTFRNHYASAVGSKENLGFTEDDNWL- 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864   418 FASYAFDVSVHESL-TPLLLGGCVCIPseaQRVNSLKEAVSTLRVNWVELTPTVARLWCPADIP--TVKTLVMGGEPM-- 492
Cdd:TIGR01923  157 LSLPLYHISGLSILfRWLIEGATLRIV---DKFNQLLEMIANERVTHISLVPTQLNRLLDEGGHneNLRKILLGGSAIpa 233

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864   493 ------LPNDISLWKdklrlvcAYGPAE-CTVVSTVQSCV-QELGNIGRsPCGTCWI-VSKDNHHRlmpvgcIGELIIGG 563
Cdd:TIGR01923  234 plieeaQQYGLPIYL-------SYGMTEtCSQVTTATPEMlHARPDVGR-PLAGREIkIKVDNKEG------HGEIMVKG 299

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864   564 PIVGRGYLKQPCLTanafitnpewaSLFHLNGsyrFYKTGDLVRYNADGTIAYIGRKDTQVKLNGQRVELGEIEHQAQ-- 641
Cdd:TIGR01923  300 ANLMKGYLYQGELT-----------PAFEQQG---WFNTGDIGELDGEGFLYVLGRRDDLIISGGENIYPEEIETVLYqh 365

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864   642 PYFRDAVIAAEVAAPAGRKPILIlFIARKyeysvnmdctmllrPPSilfqeKAQGTNtLLQEVLPRHMIPAAYIELLAMP 721
Cdd:TIGR01923  366 PGIQEAVVVPKPDAEWGQVPVAY-IVSES--------------DIS-----QAKLIA-YLTEKLAKYKVPIAFEKLDELP 424

                          490
                   ....*....|..
gi 992230864   722 ISRTGKVNRKLL 733
Cdd:TIGR01923  425 YNASGKILRNQL 436
C_NRPS-like cd19066
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ...
 1679-1950 8.65e-19

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: 91.32  E-value: 8.65e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1679 HAFLDATSVLIILRELAQAYDGQL-----SSVPGPSYSSAVAWLQSLPNG---DNRMDYWRRQLKDASP-CIFPRL-RDQ 1748
Cdd:cd19066   134 HIIVDGGSFQILFEDISSVYDAAErqkptLPPPVGSYADYAAWLEKQLESeaaQADLAYWTSYLHGLPPpLPLPKAkRPS 213

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1749 DSPSDTLVVTEQ---LASTATLTPVCTRHGLTVSNVLQVAWGLMLRRYTESDDVCFGALISGRDSriPDVDKMVGPFFNV 1825
Cdd:cd19066   214 QVASYEVLTLEFflrSEETKRLREVARESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRPD--EAVEDTIGLFLNL 291

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1826 LVCQLRFGREDSLWDVLRRNQTEIGNRLLNQHCSLIEVLRFSTYFGQ----PLFNTCISVEQPLSMD--TPDASLCFKEL 1899
Cdd:cd19066   292 LPLRIDTSPDATFPELLKRTKEQSREAIEHQRVPFIELVRHLGVVPEapkhPLFEPVFTFKNNQQQLgkTGGFIFTTPVY 371

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 992230864 1900 ETLEPTEYGIIATITIGTT-DVGLGLTYKSDLLTEDQALAVADRFKMSITEI 1950
Cdd:cd19066   372 TSSEGTVFDLDLEASEDPDgDLLLRLEYSRGVYDERTIDRFAERYMTALRQL 423
PRK05691 PRK05691
peptide synthase; Validated
 1542-1877 9.15e-19

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 94.08  E-value: 9.15e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1542 IEDAYPCSESHQGLLQTQMLRP----FYYQS-YTIwevttrskSSPVSPVRLCNAWFTLARRHPALRTHLIdiplCDGMS 1616
Cdd:PRK05691 3254 IEDVYPLTPMQEGLLLHTLLEPgtglYYMQDrYRI--------NSALDPERFAQAWQAVVARHEALRASFS----WNAGE 3321

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1617 SKIHVVHK------DY-----MADA-------AILSCEDEHVITELRKPflpsdtglyyPHAFRICQTVSGRVFCKLEGG 1678
Cdd:PRK05691 3322 TMLQVIHKpgrtpiDYldwrgLPEDgqeqrlqALHKQEREAGFDLLNQP----------PFHLRLIRVDEARYWFMMSNH 3391

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1679 HAFLDA--TSVLI-----ILRELAQAYDGQLSsvPGPSYSSAVAWLQSLPNGDNRmDYWRRQLK-----DASPCIFPRLR 1746
Cdd:PRK05691 3392 HILIDAwcRSLLMndffeIYTALGEGREAQLP--VPPRYRDYIGWLQRQDLAQAR-QWWQDNLRgferpTPIPSDRPFLR 3468

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1747 DQDSPSDTLVVTE-----QLASTATLTPVCTRHGLTVSNVLQVAWGLMLRRYTESDDVCFGALISGRDSRIPDVDKMVGP 1821
Cdd:PRK05691 3469 EHAGDSGGMVVGDcytrlDAADGARLRELAQAHQLTVNTFAQAAWALVLRRYSGDRDVLFGVTVAGRPVSMPQMQRTVGL 3548

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 992230864 1822 FFNVLVCQLRFGREDSlwdvlRRNQTEIGNRLLN--------QHCSLIEVLRFSTY-FGQPLFNT 1877
Cdd:PRK05691 3549 FINSIALRVQLPAAGQ-----RCSVRQWLQGLLDsnmelreyEYLPLVAIQECSELpKGQPLFDS 3608
EntE COG1021
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ...
 234-739 1.43e-18

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: 91.75  E-value: 1.43e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  234 IHTLFRLQCILQPDAQAICAWDGTITYRQLDRLSSTVQGLLQQYDLGPGSVV----PII--FkkskwaIVAMLGVLKAGA 307
Cdd:COG1021    27 LGDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVvvqlPNVaeF------VIVFFALFRAGA 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  308 A--FCMldqsyPTKR---LVNICKDVDAKVIVCS------------QELSIGVSG--STLSIGDHNTETATYSAIQA--- 365
Cdd:COG1021   101 IpvFAL-----PAHRraeISHFAEQSEAVAYIIPdrhrgfdyralaRELQAEVPSlrHVLVVGDAGEFTSLDALLAApad 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  366 ---VNTASHDAAYVVYTSGSTGAPKGIVIEHGSFCTNAIASSQAQNLDRSSRVLQF--ASYAFDVSVHESLTPLLLGGC- 439
Cdd:COG1021   176 lsePRPDPDDVAFFQLSGGTTGLPKLIPRTHDDYLYSVRASAEICGLDADTVYLAAlpAAHNFPLSSPGVLGVLYAGGTv 255

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  440 VCIPS-EAQRVNSLKEAVstlRVNWVELTPTVARLWC------PADIPTVKTLVMGGEPMLPNDISLWKDKL--RLVCAY 510
Cdd:COG1021   256 VLAPDpSPDTAFPLIERE---RVTVTALVPPLALLWLdaaersRYDLSSLRVLQVGGAKLSPELARRVRPALgcTLQQVF 332

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  511 GPAE----CT--------VVSTVqscvqelgniGR--SPCGTCWIVskDNHHRLMPVGCIGELIIGGPIVGRGYLKQPCL 576
Cdd:COG1021   333 GMAEglvnYTrlddpeevILTTQ----------GRpiSPDDEVRIV--DEDGNPVPPGEVGELLTRGPYTIRGYYRAPEH 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  577 TANAFiTNpewaslfhlNGsyrFYKTGDLVRYNADGTIAYIGRKDTQVKLNGQRVELGEIEHQ--AQPyfrdAVI-AAEV 653
Cdd:COG1021   401 NARAF-TP---------DG---FYRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLllAHP----AVHdAAVV 463

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  654 AAPagrkpililfiarkyeysvnmDCTM--------LLRPPSIlfqeKAQGTNTLLQEV-LPRHMIPAAyIELL-AMPIS 723
Cdd:COG1021   464 AMP---------------------DEYLgerscafvVPRGEPL----TLAELRRFLRERgLAAFKLPDR-LEFVdALPLT 517

                         570
                  ....*....|....*.
gi 992230864  724 RTGKVNRKLLREAVEQ 739
Cdd:COG1021   518 AVGKIDKKALRAALAA 533
C_NRPS-like cd19066
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ...
 875-1265 2.44e-18

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: 89.78  E-value: 2.44e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  875 YPCTPLQEAL--MAYTSKRPGAFQAQFRFQLPHQLDMLRLKEAWRIVIAANPILRTRIVFCHTGALQVVLRPGEQLQWDL 952
Cdd:cd19066     2 IPLSPMQRGMwfLKKLATDPSAFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRFCEEAGRYEQVVLDKTVRFRIEI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  953 IN--GVHTSPGSLMSYGVPLVdMAITNDTAGKLSR-----------TFCLTMHHAIFDGWSYGLILGAVEDAY----KHT 1015
Cdd:cd19066    82 IDlrNLADPEARLLELIDQIQ-QTIYDLERGPLVRvalfrladerdVLVVAIHHIIVDGGSFQILFEDISSVYdaaeRQK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1016 NAVQRPFAPFIKYILHcnYESAKH---------FWcsefKDMQALPFPVPPLSRGHM--ANSSTTTHrqiHVSEWL---- 1080
Cdd:cd19066   161 PTLPPPVGSYADYAAW--LEKQLEseaaqadlaYW----TSYLHGLPPPLPLPKAKRpsQVASYEVL---TLEFFLrsee 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1081 ---------SSYCTPSTIIQLAFTLLIAWRTESMDVLFGLTVTGRNAPvaGIHRTTGPTIATFPLRtiLYGTMNIT-DAL 1150
Cdd:cd19066   232 tkrlrevarESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRPDE--AVEDTIGLFLNLLPLR--IDTSPDATfPEL 307

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1151 L---------CMQNHIatlIPFEHtgLRRIKSFGTETARACQFQSLLIIQPVTYRESSEIFFELESNEHeqSKFSTCPLT 1221
Cdd:cd19066   308 LkrtkeqsreAIEHQR---VPFIE--LVRHLGVVPEAPKHPLFEPVFTFKNNQQQLGKTGGFIFTTPVY--TSSEGTVFD 380

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*....
gi 992230864 1222 LVCELRTHS-----VSVKAISDnaVVISGDMERLLDQLEYLIDMITKSP 1265
Cdd:cd19066   381 LDLEASEDPdgdllLRLEYSRG--VYDERTIDRFAERYMTALRQLIENP 427
FACL_DitJ_like cd05934
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 258-734 2.97e-18

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: 89.66  E-value: 2.97e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  258 ITYRQLDRLSSTVQGLLQQYDLGPGSVVPIIFKKSKWAIVAMLGVLKAGAAFCMLDQSYPTKRLVNICKDVDAKVIVCsq 337
Cdd:cd05934     4 WTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV-- 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  338 elsigvsgstlsigdhntetatysaiqavntashDAAYVVYTSGSTGAPKGIVIEHGSFCTNAIASSQAQNLDRSSRVLQ 417
Cdd:cd05934    82 ----------------------------------DPASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLGEDDVYLT 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  418 ----FASYAFDVSVheslTPLLLGGCVCIPSEAQRVNSLKEAVSTLRVNWVELTPTVARLWC---PADIPTVKTL-VMGG 489
Cdd:cd05934   128 vlplFHINAQAVSV----LAALSVGATLVLLPRFSASRFWSDVRRYGATVTNYLGAMLSYLLaqpPSPDDRAHRLrAAYG 203

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  490 EPMLPNDISLWKDK--LRLVCAYGPAE--CTVVSTVQSCVQElGNIGR-SPCGTCWIVskDNHHRLMPVGCIGELII--- 561
Cdd:cd05934   204 APNPPELHEEFEERfgVRLLEGYGMTEtiVGVIGPRDEPRRP-GSIGRpAPGYEVRIV--DDDGQELPAGEPGELVIrgl 280

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  562 GGPIVGRGYLKQPCLTANAfitnpeWAslfhlNGsyrFYKTGDLVRYNADGTIAYIGRKDTQVKLNGQRVELGEIEHQAQ 641
Cdd:cd05934   281 RGWGFFKGYYNMPEATAEA------MR-----NG---WFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAIL 346

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  642 --PYFRDAVIAA--------EVAApagrkpililfiarkyeysvnmdcTMLLRPPSILFQEKAQgtnTLLQEVLPRHMIP 711
Cdd:cd05934   347 rhPAVREAAVVAvpdevgedEVKA------------------------VVVLRPGETLDPEELF---AFCEGQLAYFKVP 399

                         490       500
                  ....*....|....*....|....
gi 992230864  712 aAYIELL-AMPISRTGKVNRKLLR 734
Cdd:cd05934   400 -RYIRFVdDLPKTPTEKVAKAQLR 422
PRK08314 PRK08314
long-chain-fatty-acid--CoA ligase; Validated
 246-612 3.35e-18

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


Pssm-ID: 236235 [Multi-domain]  Cd Length: 546  Bit Score: 90.40  E-value: 3.35e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  246 PDAQAICAWDGTITYRQL----DRLSSTVQgllQQYDLGPGSVVPIIFKKSKWAIVAMLGVLKAGAAFCMLDQSYPTKRL 321
Cdd:PRK08314   24 PDKTAIVFYGRAISYRELleeaERLAGYLQ---QECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEEL 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  322 VNICKDVDAKVIVCSQELSIGVSGSTLSIGDHNTETATYS----------------------------------AIQA-- 365
Cdd:PRK08314  101 AHYVTDSGARVAIVGSELAPKVAPAVGNLRLRHVIVAQYSdylpaepeiavpawlraepplqalapggvvawkeALAAgl 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  366 ----VNTASHDAAYVVYTSGSTGAPKGIVIEHGSFCTNAIASSQAQNLDRSSRVLQFASYaFDVS--VHESLTPLLLGGC 439
Cdd:PRK08314  181 apppHTAGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVLAVLPL-FHVTgmVHSMNAPIYAGAT 259

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  440 VCIPSEAQRvNSLKEAVSTLRV-NW-------VEL--TPTVARlwcpADIPTVKTLVMGGEPMlPNDIS--LWKD-KLRL 506
Cdd:PRK08314  260 VVLMPRWDR-EAAARLIERYRVtHWtniptmvVDFlaSPGLAE----RDLSSLRYIGGGGAAM-PEAVAerLKELtGLDY 333

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  507 VCAYGPAEcTVVSTV--------QSCvqeLGnigrspcgtcwIVSKDNHHRL--------MPVGCIGELIIGGPIVGRGY 570
Cdd:PRK08314  334 VEGYGLTE-TMAQTHsnppdrpkLQC---LG-----------IPTFGVDARVidpetleeLPPGEVGEIVVHGPQVFKGY 398

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 992230864  571 LKQPCLTANAFITnpewaslfhLNGSyRFYKTGDLVRYNADG 612
Cdd:PRK08314  399 WNRPEATAEAFIE---------IDGK-RFFRTGDLGRMDEEG 430
PRK12316 PRK12316
peptide synthase; Provisional
 862-1286 3.55e-18

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 92.33  E-value: 3.55e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  862 EQCSVFPEQIEDIYPCTPLQEALMAYT--SKRPGAFQAQFRFQLpHQLDMLRLKEAWRIVIAANPILRTRIVF--CHTGA 937
Cdd:PRK12316 4090 DALPLPLGEIEDIYPLSPMQQGMLFHSlyEQEAGDYINQMRVDV-QGLDVERFRAAWQAALDRHDVLRSGFVWqgELGRP 4168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  938 LQVVLR----PGEQLQWDlingvhtspgslmsyGVPLVDMAITNDTAGKLSRTFCL----------------------TM 991
Cdd:PRK12316 4169 LQVVHKqvslPFAELDWR---------------GRADLQAALDALAAAERERGFDLqrapllrlvlvrtaegrhhliyTN 4233

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  992 HHAIFDGWSYGLILGAVEDAYKHTNAVQRP--FAPFIKYILHCNYESAKHFWCSEFKDMQALPFPVPPLSRGHMANSSTT 1069
Cdd:PRK12316 4234 HHILMDGWSNSQLLGEVLERYSGRPPAQPGgrYRDYIAWLQRQDAAASEAFWREQLAALDEPTRLAQAIARADLRSANGY 4313

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1070 THrqiHVSEW-------LSSYC-----TPSTIIQLAFTLLIAWRTESMDVLFGLTVTGRNAPVAGIHRTTGPTIATFPLR 1137
Cdd:PRK12316 4314 GE---HVRELdatatarLREFArtqrvTLNTLVQAAWLLLLQRYTGQDTVAFGATVAGRPAELPGIEGQIGLFINTLPVI 4390

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1138 TILYGTMNITDALLCMQNHIATLIPFEHTGLRRIKSFGTETARACqFQSLLIIQ--PVT---YRESSE--IFFELESneH 1210
Cdd:PRK12316 4391 ATPRAQQSVVEWLQQVQRQNLALREHEHTPLYEIQRWAGQGGEAL-FDSLLVFEnyPVSealQQGAPGglRFGEVTN--H 4467

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 992230864 1211 EQSKFstcPLTLVCELrTHSVSVKAISDNAVVISGDMERLLDQLEYLIDMITKSPTLEIQNIIPSPQDTYSYALQQ 1286
Cdd:PRK12316 4468 EQTNY---PLTLAVGL-GETLSLQFSYDRGHFDAATIERLARHLTNLLEAMAEDPQRRLGELQLLEKAEQQRIVAL 4539
PRK06178 PRK06178
acyl-CoA synthetase; Validated
 244-740 4.00e-18

acyl-CoA synthetase; Validated


Pssm-ID: 235724 [Multi-domain]  Cd Length: 567  Bit Score: 90.49  E-value: 4.00e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  244 LQPDAQAICAWDGTITYRQLDRLSSTVQGLLQQYDLGPGSVVPIIFKKSKWAIVAMLGVLKAGAAFCMLDQSYPTKRLVN 323
Cdd:PRK06178   45 ERPQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSY 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  324 ICKDVDAKVIVC-----------SQELSI----------------------GVSGSTLSIGDH----NTETATYSAIQAV 366
Cdd:PRK06178  125 ELNDAGAEVLLAldqlapvveqvRAETSLrhvivtsladvlpaeptlplpdSLRAPRLAAAGAidllPALRACTAPVPLP 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  367 NTASHDAAYVVYTSGSTGAPKGIVIEHGSFC-TNAIASSQAQNLDRSSRVLQF------ASYAFDVsvhesLTPLLLGGC 439
Cdd:PRK06178  205 PPALDALAALNYTGGTTGMPKGCEHTQRDMVyTAAAAYAVAVVGGEDSVFLSFlpefwiAGENFGL-----LFPLFSGAT 279

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  440 VCIPSEAQRVNSLkEAVSTLRV--------NWVEL--TPTVARLwcpaDIPTVK-TLVMGGEPMLPNDI-SLWKDKLRLV 507
Cdd:PRK06178  280 LVLLARWDAVAFM-AAVERYRVtrtvmlvdNAVELmdHPRFAEY----DLSSLRqVRVVSFVKKLNPDYrQRWRALTGSV 354

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  508 ---CAYGPAECTVVSTVQSCVQ----ELGN----IGRSPCGTCWIVSKDNHHRLMPVGCIGELIIGGPIVGRGYLKQPCL 576
Cdd:PRK06178  355 laeAAWGMTETHTCDTFTAGFQdddfDLLSqpvfVGLPVPGTEFKICDFETGELLPLGAEGEIVVRTPSLLKGYWNKPEA 434

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  577 TANAFITNpeWaslfhlngsyrfYKTGDLVRYNADGTIAYIGRKDTQVKLNGQRVELGEIE-----HqaqPyfrdAVIAA 651
Cdd:PRK06178  435 TAEALRDG--W------------LHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEallgqH---P----AVLGS 493

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  652 EVAAPA--GRKPILILFIarkyeysvnmdctmLLRPPSILFQEKaqgtntlLQEVLPRHMipAAY----IELL-AMPISR 724
Cdd:PRK06178  494 AVVGRPdpDKGQVPVAFV--------------QLKPGADLTAAA-------LQAWCRENM--AVYkvpeIRIVdALPMTA 550

                         570
                  ....*....|....*.
gi 992230864  725 TGKVNRKLLREAVEQA 740
Cdd:PRK06178  551 TGKVRKQDLQALAEEL 566
PRK08043 PRK08043
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
372-666 4.50e-18

bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;


Pssm-ID: 181207 [Multi-domain]  Cd Length: 718  Bit Score: 90.92  E-value: 4.50e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  372 DAAYVVYTSGSTGAPKGIVIEHGSFCTN-----AIASSQAQNLDRSSRVLqFASYAFDVSVhesLTPLLLGGCVCI-PSE 445
Cdd:PRK08043  366 DAALILFTSGSEGHPKGVVHSHKSLLANveqikTIADFTPNDRFMSALPL-FHSFGLTVGL---FTPLLTGAEVFLyPSP 441

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  446 AQ-RVnsLKEAV-----------STLRVNWveltptvARLWCPADIPTVKTLVMGGEPMLPNDISLWKDK--LRLVCAYG 511
Cdd:PRK08043  442 LHyRI--VPELVydrnctvlfgtSTFLGNY-------ARFANPYDFARLRYVVAGAEKLQESTKQLWQDKfgLRILEGYG 512

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  512 PAECT-VVSTVQSCVQELGNIGRSPCGTcwivskdnHHRLMPVGCI---GELIIGGPIVGRGYLKqpclTANAFITNPEW 587
Cdd:PRK08043  513 VTECApVVSINVPMAAKPGTVGRILPGM--------DARLLSVPGIeqgGRLQLKGPNIMNGYLR----VEKPGVLEVPT 580

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 992230864  588 ASLFHLNGSYRFYKTGDLVRYNADGTIAYIGRKDTQVKLNGQRVELGEIEHQAQPYFRDAVIAAEVAAPAGRKPILILF 666
Cdd:PRK08043  581 AENARGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKQHATAIKSDASKGEALVLF 659
Firefly_Luc_like cd05911
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ...
 251-637 5.95e-18

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: 89.19  E-value: 5.95e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  251 ICAWDG-TITYRQLDRLSSTVQGLLQQYDLGPGSVVPIIFKKSKWAIVAMLGVLKAGAAFCMLDQSYPTKRLVNICKDVD 329
Cdd:cd05911     3 IDADTGkELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  330 AKVIVCSQEL---------SIGVSGSTLSIGDHN-------------TETATYSAIQAVNTASHDAAYVVYTSGSTGAPK 387
Cdd:cd05911    83 PKVIFTDPDGlekvkeaakELGPKDKIIVLDDKPdgvlsiedllsptLGEEDEDLPPPLKDGKDDTAAILYSSGTTGLPK 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  388 GIVIEHGSFCTNaiaSSQAQ-----NLDRSSRVLQFAS----YAFDVSVHesltpLLLGGCVCIPSEAQRVNSLKEAVST 458
Cdd:cd05911   163 GVCLSHRNLIAN---LSQVQtflygNDGSNDVILGFLPlyhiYGLFTTLA-----SLLNGATVIIMPKFDSELFLDLIEK 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  459 LRVNWVELTPTVArLW---CP----ADIPTVKTLVMGGEPM-------LPNDISLWkdklRLVCAYGPAECTVVSTV-QS 523
Cdd:cd05911   235 YKITFLYLVPPIA-AAlakSPlldkYDLSSLRVILSGGAPLskelqelLAKRFPNA----TIKQGYGMTETGGILTVnPD 309

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  524 CVQELGNIGR-SPCGTCWIVSKDNHHRLmPVGCIGELIIGGPIVGRGYLKQPclTANafitnpewASLFHLNGsyrFYKT 602
Cdd:cd05911   310 GDDKPGSVGRlLPNVEAKIVDDDGKDSL-GPNEPGEICVRGPQVMKGYYNNP--EAT--------KETFDEDG---WLHT 375

                         410       420       430
                  ....*....|....*....|....*....|....*
gi 992230864  603 GDLVRYNADGTIAYIGRKDTQVKLNGQRVELGEIE 637
Cdd:cd05911   376 GDIGYFDEDGYLYIVDRKKELIKYKGFQVAPAELE 410
PRK05691 PRK05691
peptide synthase; Validated
 819-1137 2.01e-17

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 89.84  E-value: 2.01e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  819 FKRQTISKLAE---------CTHQMSNGIGSPIPP-FslldPLGKgtyIAQAT-EQCSVFPEQIEDIYPCTPLQEALMAY 887
Cdd:PRK05691 3198 YDEQTIAELAEaylaelqalIAHCLADGAGGLTPSdF----PLAQ---LTQAQlDALPVPAAEIEDVYPLTPMQEGLLLH 3270

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  888 TSKRPGA--FQAQFRFQLPHQLDMLRLKEAWRIVIAANPILRTRivFCHTGA---LQVVLRPG----EQLQWDLINGVHT 958
Cdd:PRK05691 3271 TLLEPGTglYYMQDRYRINSALDPERFAQAWQAVVARHEALRAS--FSWNAGetmLQVIHKPGrtpiDYLDWRGLPEDGQ 3348

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  959 SP------GSLMSYGVPLVDMA------ITNDTAgklSRTFCLTMHHAIFDGWSYGLILGAVEDAYK---HTNAVQRPFA 1023
Cdd:PRK05691 3349 EQrlqalhKQEREAGFDLLNQPpfhlrlIRVDEA---RYWFMMSNHHILIDAWCRSLLMNDFFEIYTalgEGREAQLPVP 3425

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1024 P----FIKYILHCNYESAKHFWCSEFKDMQAlPFPVP---PLSRGHMANSSTT------THRQIHVSEWLSSYC-----T 1085
Cdd:PRK05691 3426 PryrdYIGWLQRQDLAQARQWWQDNLRGFER-PTPIPsdrPFLREHAGDSGGMvvgdcyTRLDAADGARLRELAqahqlT 3504

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 992230864 1086 PSTIIQLAFTLLIAWRTESMDVLFGLTVTGRNAPVAGIHRTTGPTIATFPLR 1137
Cdd:PRK05691 3505 VNTFAQAAWALVLRRYSGDRDVLFGVTVAGRPVSMPQMQRTVGLFINSIALR 3556
PRK06145 PRK06145
acyl-CoA synthetase; Validated
 246-637 4.96e-17

acyl-CoA synthetase; Validated


Pssm-ID: 102207 [Multi-domain]  Cd Length: 497  Bit Score: 86.48  E-value: 4.96e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  246 PDAQAICAWDGTITYRQLDRLSSTVQGLLQQYDLGPGSVVPIIFKKSKWAIVAMLGVLKAGAAFCMLDQSYPTKRLVNIC 325
Cdd:PRK06145   16 PDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYIL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  326 KDVDAKVIVCSQELSI--GVSGSTLSIGDHNTETATY------SAIQAVNTASHDAAYVVYTSGSTGAPKGIVIEHGSFC 397
Cdd:PRK06145   96 GDAGAKLLLVDEEFDAivALETPKIVIDAAAQADSRRlaqgglEIPPQAAVAPTDLVRLMYTSGTTDRPKGVMHSYGNLH 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  398 TNAIASSQAQNLDRSSRVLQFASY----AFDVSvheSLTPLLLGGCVCIPSEAQRVNSLkEAVSTLRVN--WVELTPTVA 471
Cdd:PRK06145  176 WKSIDHVIALGLTASERLLVVGPLyhvgAFDLP---GIAVLWVGGTLRIHREFDPEAVL-AAIERHRLTcaWMAPVMLSR 251

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  472 RLWCPA----DIPTVKTLVMGGE--PMLP-NDISLWKDKLRLVCAYGPAECTVVSTVQSCVQELGNIGRS--PCGTCWIV 542
Cdd:PRK06145  252 VLTVPDrdrfDLDSLAWCIGGGEktPESRiRDFTRVFTRARYIDAYGLTETCSGDTLMEAGREIEKIGSTgrALAHVEIR 331

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  543 SKDNHHRLMPVGCIGELIIGGPIVGRGYLKQPCLTANAFITNpeWaslfhlngsyrfYKTGDLVRYNADGTIAYIGRKDT 622
Cdd:PRK06145  332 IADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYGD--W------------FRSGDVGYLDEEGFLYLTDRKKD 397

                         410
                  ....*....|....*
gi 992230864  623 QVKLNGQRVELGEIE 637
Cdd:PRK06145  398 MIISGGENIASSEVE 412
PRK09274 PRK09274
peptide synthase; Provisional
 245-644 5.93e-17

peptide synthase; Provisional


Pssm-ID: 236443 [Multi-domain]  Cd Length: 552  Bit Score: 86.49  E-value: 5.93e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  245 QPDAQAICAWDG----------TITYRQLDRLSSTVQGLLQQYDLGPGSVVPIIFKKSKWAIVAMLGVLKAGAAFCMLDQ 314
Cdd:PRK09274   19 RPDQLAVAVPGGrgadgklaydELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKAGAVPVLVDP 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  315 SYPTKRLVNICKDVDA------------------------KVIVCSQELSIGvsGSTLSIGDHNTETATYsaiQAVNTAS 370
Cdd:PRK09274   99 GMGIKNLKQCLAEAQPdafigipkahlarrlfgwgkpsvrRLVTVGGRLLWG--GTTLATLLRDGAAAPF---PMADLAP 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  371 HDAAYVVYTSGSTGAPKGIVIEHGSFCtnaiasSQAQNLDrssrvlqfASYAF---DVSVHE----SLTPLLLGGCVCIP 443
Cdd:PRK09274  174 DDMAAILFTSGSTGTPKGVVYTHGMFE------AQIEALR--------EDYGIepgEIDLPTfplfALFGPALGMTSVIP 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  444 ----SEAQRVNSLK-------EAVSTLRVNwveltPT----VARlWCPAD---IPTVKTLVMGGEP-----------MLP 494
Cdd:PRK09274  240 dmdpTRPATVDPAKlfaaierYGVTNLFGS-----PAllerLGR-YGEANgikLPSLRRVISAGAPvpiavierfraMLP 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  495 NDISLWKdklrlvcAYGPAECTVVSTVQS--CVQELGNIGRSPCGTCW------------------IVSKDNHHRLmPVG 554
Cdd:PRK09274  314 PDAEILT-------PYGATEALPISSIESreILFATRAATDNGAGICVgrpvdgvevriiaisdapIPEWDDALRL-ATG 385

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  555 CIGELIIGGPIVGRGYLKQPCLTANAFITNPEwASLFHlngsyrfyKTGDLVRYNADGTIAYIGRKdtqvklnGQRVELg 634
Cdd:PRK09274  386 EIGEIVVAGPMVTRSYYNRPEATRLAKIPDGQ-GDVWH--------RMGDLGYLDAQGRLWFCGRK-------AHRVET- 448

                         490
                  ....*....|
gi 992230864  635 eiehQAQPYF 644
Cdd:PRK09274  449 ----AGGTLY 454
PRK05605 PRK05605
long-chain-fatty-acid--CoA ligase; Validated
 368-743 6.83e-17

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


Pssm-ID: 235531 [Multi-domain]  Cd Length: 573  Bit Score: 86.59  E-value: 6.83e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  368 TASHDAAYVVYTSGSTGAPKGIVIEHGSFCTNAiASSQA--QNL-DRSSRVLQ----FasYAFDVSVHESLTPLLLGGCV 440
Cdd:PRK05605  216 PTPDDVALILYTSGTTGKPKGAQLTHRNLFANA-AQGKAwvPGLgDGPERVLAalpmF--HAYGLTLCLTLAVSIGGELV 292

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  441 CIPseAQRVNSLKEAVSTLRVNWVELTPTV-ARLWCPA-----DIPTVKTLVMGGEPMLPNDISLWKDKL--RLVCAYGP 512
Cdd:PRK05605  293 LLP--APDIDLILDAMKKHPPTWLPGVPPLyEKIAEAAeergvDLSGVRNAFSGAMALPVSTVELWEKLTggLLVEGYGL 370

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  513 AECT--VVSTVQSCVQELGNIGRS-PCGTCWIVSKDNHHRLMPVGCIGELIIGGPIVGRGYLKQPCLTANAFItnPEWas 589
Cdd:PRK05605  371 TETSpiIVGNPMSDDRRPGYVGVPfPDTEVRIVDPEDPDETMPDGEEGELLVRGPQVFKGYWNRPEETAKSFL--DGW-- 446

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  590 lfhlngsyrfYKTGDLVRYNADGTIAYIGRKDTQVKLNGQRVELGEIEH--QAQPYFRDA-------------VIAAEVA 654
Cdd:PRK05605  447 ----------FRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEvlREHPGVEDAavvglpredgseeVVAAVVL 516

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  655 APAgrkpililfiarkyeysVNMDctmllrppsilfqekAQGTNTLLQEVLPRHMIPAAYIELLAMPISRTGKVNRKLLR 734
Cdd:PRK05605  517 EPG-----------------AALD---------------PEGLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRRREVR 564


                  ....*....
gi 992230864  735 EAVEQASEK 743
Cdd:PRK05605  565 EELLEKLGA 573
PRK06839 PRK06839
o-succinylbenzoate--CoA ligase;
241-735 1.26e-16

o-succinylbenzoate--CoA ligase;


Pssm-ID: 168698 [Multi-domain]  Cd Length: 496  Bit Score: 85.30  E-value: 1.26e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  241 QCILQPDAQAICAWDGTITYRQL-DRLSSTVQGLLQQYDLGPGSVVPIIFKKSKWAIVAMLGVLKAGAAFCMLDQSYPTK 319
Cdd:PRK06839   11 RAYLHPDRIAIITEEEEMTYKQLhEYVSKVAAYLIYELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTEN 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  320 RLVNICKDVDAKVIVCSQELSIGVSGSTLSIGDHN-------TETATYSAIQAVNTASHDAAYVVYTSGSTGAPKGIVIE 392
Cdd:PRK06839   91 ELIFQLKDSGTTVLFVEKTFQNMALSMQKVSYVQRvisitslKEIEDRKIDNFVEKNESASFIICYTSGTTGKPKGAVLT 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  393 HGSFCTNAIASSQAQNL---DRSSRVLQF------ASYAFDVsvhesltpLLLGGCVCIPSEAQRVNSLKeAVSTLRVNW 463
Cdd:PRK06839  171 QENMFWNALNNTFAIDLtmhDRSIVLLPLfhiggiGLFAFPT--------LFAGGVIIVPRKFEPTKALS-MIEKHKVTV 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  464 VELTPTV--ARLWCP----ADIPTVKTLVMGGEPMLPNDISLWKDK-LRLVCAYGPAECTvvSTVQSCVQE-----LGNI 531
Cdd:PRK06839  242 VMGVPTIhqALINCSkfetTNLQSVRWFYNGGAPCPEELMREFIDRgFLFGQGFGMTETS--PTVFMLSEEdarrkVGSI 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  532 GRsPCGTCWIVSKDNHHRLMPVGCIGELIIGGPIVGRGYLKQPCLTANAfITNpEWaslFHlngsyrfykTGDLVRYNAD 611
Cdd:PRK06839  320 GK-PVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEET-IQD-GW---LC---------TGDLARVDED 384

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  612 GTIAYIGRKDTQVKLNGQRVELGEIEhQAQPYFRDAVIAAEVAAPAGR-KPILILFIARKyeysvnmdctmllrpPSILF 690
Cdd:PRK06839  385 GFVYIVGRKKEMIISGGENIYPLEVE-QVINKLSDVYEVAVVGRQHVKwGEIPIAFIVKK---------------SSSVL 448

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*
gi 992230864  691 QEKAQGTNTLLQevLPRHMIPAAYIELLAMPISRTGKVNRKLLRE 735
Cdd:PRK06839  449 IEKDVIEHCRLF--LAKYKIPKEIVFLKELPKNATGKIQKAQLVN 491
PRK07656 PRK07656
long-chain-fatty-acid--CoA ligase; Validated
 246-620 2.00e-16

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


Pssm-ID: 236072 [Multi-domain]  Cd Length: 513  Bit Score: 84.57  E-value: 2.00e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  246 PDAQAICAWDGTITYRQLDRLSSTVQGLLQQYDLGPGSVVPIIFKKSKWAIVAMLGVLKAGAAFCMLDQSYPTKRLVNIC 325
Cdd:PRK07656   19 GDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTADEAAYIL 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  326 KDVDAKVIVCSQEL---SIGVSGSTLSIG-----------DHNTETATYSAI--------QAVNTASHDAAYVVYTSGST 383
Cdd:PRK07656   99 ARGDAKALFVLGLFlgvDYSATTRLPALEhvviceteeddPHTEKMKTFTDFlaagdpaeRAPEVDPDDVADILFTSGTT 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  384 GAPKGIVIEHGSFCTNAIASSQAQNLDRSSRVLQ----FASYAFDVSVhesLTPLLLGGCVCI-----PSE------AQR 448
Cdd:PRK07656  179 GRPKGAMLTHRQLLSNAADWAEYLGLTEGDRYLAanpfFHVFGYKAGV---NAPLMRGATILPlpvfdPDEvfrlieTER 255

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  449 V----------NSL-------KEAVSTLRvnwveLTPTVArlwcpADIPTVktLVMGGEPMLPNDISLwkdklrlvCAYG 511
Cdd:PRK07656  256 ItvlpgpptmyNSLlqhpdrsAEDLSSLR-----LAVTGA-----ASMPVA--LLERFESELGVDIVL--------TGYG 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  512 PAECTVVSTV----QSCVQELGNIGRSpcgtCW-----IVskDNHHRLMPVGCIGELIIGGPIVGRGYLKQPCLTANAfI 582
Cdd:PRK07656  316 LSEASGVTTFnrldDDRKTVAGTIGTA----IAgvenkIV--NELGEEVPVGEVGELLVRGPNVMKGYYDDPEATAAA-I 388

                         410       420       430
                  ....*....|....*....|....*....|....*...
gi 992230864  583 TNPEWaslFHlngsyrfykTGDLVRYNADGTIAYIGRK 620
Cdd:PRK07656  389 DADGW---LH---------TGDLGRLDEEGYLYIVDRK 414
PRK05691 PRK05691
peptide synthase; Validated
 258-1005 2.02e-16

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 86.38  E-value: 2.02e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  258 ITYRQLDRLSSTVQGLLQQyDLGPGSVVPIIFKKSKWAIVAMLGVLKAGAafcMLDQSYP--------TKRLVNICKDVD 329
Cdd:PRK05691   41 LSYRDLDLRARTIAAALQA-RASFGDRAVLLFPSGPDYVAAFFGCLYAGV---IAVPAYPpesarrhhQERLLSIIADAE 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  330 AKVIVCSQELSIGVSGSTLSIGDHNTETATYSAI--------QAVNTASHDAAYVVYTSGSTGAPKGIVIEHGSFCTNAI 401
Cdd:PRK05691  117 PRLLLTVADLRDSLLQMEELAAANAPELLCVDTLdpalaeawQEPALQPDDIAFLQYTSGSTALPKGVQVSHGNLVANEQ 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  402 ASSQAQNLDRSSRvlqfasyafDVSVheSLTPL-----LLGG----------CVCIPSE---AQRVNSLkEAVSTLRvNW 463
Cdd:PRK05691  197 LIRHGFGIDLNPD---------DVIV--SWLPLyhdmgLIGGllqpifsgvpCVLMSPAyflERPLRWL-EAISEYG-GT 263

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  464 VELTPTVARLWCPA----------DIPTVKTLVMGGEPMLPNDISLWKDKL--------RLVCAYGPAECTVV------- 518
Cdd:PRK05691  264 ISGGPDFAYRLCSErvsesalerlDLSRWRVAYSGSEPIRQDSLERFAEKFaacgfdpdSFFASYGLAEATLFvsggrrg 343

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  519 -----------------------STVQSCvqelgniGRSPCGTCWIVSKDNHHRLMPVGCIGELIIGGPIVGRGYLKQPC 575
Cdd:PRK05691  344 qgipaleldaealarnraepgtgSVLMSC-------GRSQPGHAVLIVDPQSLEVLGDNRVGEIWASGPSIAHGYWRNPE 416

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  576 LTANAFItnpewaslfHLNGSyRFYKTGDLvRYNADGTIAYIGRKDTQVKLNGQRVELGEIEHQAQ---PYFRDAVIAAE 652
Cdd:PRK05691  417 ASAKTFV---------EHDGR-TWLRTGDL-GFLRDGELFVTGRLKDMLIVRGHNLYPQDIEKTVErevEVVRKGRVAAF 485

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  653 VAAPAGRKPILILF-IARKYEYSVnmdctmllrPPSILFqekaqgtNTLLQEVLPRHMIPAAYIELL---AMPISRTGKV 728
Cdd:PRK05691  486 AVNHQGEEGIGIAAeISRSVQKIL---------PPQALI-------KSIRQAVAEACQEAPSVVLLLnpgALPKTSSGKL 549

                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  729 NRKLLREAVEQASEKDFRAYYPITHNDMIQLPSTP--VLDQLRLLFSAALRIpeEKIKPNDSFFHLGGDSVSAIRLVGDA 806
Cdd:PRK05691  550 QRSACRLRLADGSLDSYALFPALQAVEAAQTAASGdeLQARIAAIWCEQLKV--EQVAADDHFFLLGGNSIAATQVVARL 627

                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  807 RDQ-GLHITVESLFKRQTISKLAECTHQMSNGIGSPIPPfslLDPLGKGTYIAQATEQCSV-FPEQIEDiypctplQEAl 884
Cdd:PRK05691  628 RDElGIDLNLRQLFEAPTLAAFSAAVARQLAGGGAAQAA---IARLPRGQALPQSLAQNRLwLLWQLDP-------QSA- 696

                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  885 mAYTSkrPGAfqaqfrFQLPHQLDMLRLKEAWRIVIAANPILRTRIVFCHTGALQVVLRPGE------------------ 946
Cdd:PRK05691  697 -AYNI--PGG------LHLRGELDEAALRASFQRLVERHESLRTRFYERDGVALQRIDAQGEfalqridlsdlpeaerea 767

                         810       820       830       840       850       860       870
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 992230864  947 ----------QLQWDLINGvhtspgslmsygvPL--VDMAITNDTAGKLsrtfCLTMHHAIFDGWSYGLIL 1005
Cdd:PRK05691  768 raaqireeeaRQPFDLEKG-------------PLlrVTLVRLDDEEHQL----LVTLHHIVADGWSLNILL 821
FAA1 COG1022
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
237-649 2.70e-16

Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];


Pssm-ID: 440645 [Multi-domain]  Cd Length: 603  Bit Score: 84.77  E-value: 2.70e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  237 LFRLQCILQPDAQAICAWDG----TITYRQLDRLSSTVQGLLQQYDLGPGSVVPIIfkkSK----WAIvAMLGVLKAGAA 308
Cdd:COG1022    16 LLRRRAARFPDRVALREKEDgiwqSLTWAEFAERVRALAAGLLALGVKPGDRVAIL---SDnrpeWVI-ADLAILAAGAV 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  309 FCMLDQSYPTKRLVNICKDVDAKVIVCSQE------LSIGVSGSTL--------SIGDHNTETATYSAIQAVNTASHDAA 374
Cdd:COG1022    92 TVPIYPTSSAEEVAYILNDSGAKVLFVEDQeqldklLEVRDELPSLrhivvldpRGLRDDPRLLSLDELLALGREVADPA 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  375 YV---------------VYTSGSTGAPKGIVIEHGSFCTNAIASSQAQNLDRSSRVL----------QFASYAFdvsvhe 429
Cdd:COG1022   172 ELearraavkpddlatiIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLsflplahvfeRTVSYYA------ 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  430 sltpLLLGGCVCIPseaqrvNSLKEAVSTLRvnwvELTPT----VARLW------------------------------- 474
Cdd:COG1022   246 ----LAAGATVAFA------ESPDTLAEDLR----EVKPTfmlaVPRVWekvyagiqakaeeagglkrklfrwalavgrr 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  475 -----------CPADIPT-------------------VKTLVMGGEPMLPnDISLWKD--KLRLVCAYGPAECTVVSTVQ 522
Cdd:COG1022   312 yararlagkspSLLLRLKhaladklvfsklrealggrLRFAVSGGAALGP-ELARFFRalGIPVLEGYGLTETSPVITVN 390

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  523 --SCVQeLGNIGRSPCGTCWIVSKDnhhrlmpvgciGELIIGGPIVGRGYLKQPCLTANAFITNpEWaslFHlngsyrfy 600
Cdd:COG1022   391 rpGDNR-IGTVGPPLPGVEVKIAED-----------GEILVRGPNVMKGYYKNPEATAEAFDAD-GW---LH-------- 446

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|..
gi 992230864  601 kTGDLVRYNADGTIAYIGR-KDTQVKLNGQRVELGEIEHQ--AQPYFRDAVI 649
Cdd:COG1022   447 -TGDIGELDEDGFLRITGRkKDLIVTSGGKNVAPQPIENAlkASPLIEQAVV 497
A_NRPS_TubE_like cd05906
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ...
 255-739 2.72e-16

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: 84.64  E-value: 2.72e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  255 DGT---ITYRQLDRLSSTVQGLLQQYDLGPGSVVPIIFKKSKWAIVAMLGVLKAGAAFCML-------DQSYPTKRLVNI 324
Cdd:cd05906    34 DGSeefQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPLtvpptydEPNARLRKLRHI 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  325 CKDVDAKVIVCSQELSIGVSG----------STLSIGDhntETATYSAIQAVNTASHDAAYVVYTSGSTGAPKGIVIEHG 394
Cdd:cd05906   114 WQLLGSPVVLTDAELVAEFAGletlsglpgiRVLSIEE---LLDTAADHDLPQSRPDDLALLMLTSGSTGFPKAVPLTHR 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  395 SFCTNAIASSQAQNLDRSSRVLQFAsyAFD---VSVHESLTPLLLGgcvcipseAQRVNSLKEAVSTLRVNWVELTPT-- 469
Cdd:cd05906   191 NILARSAGKIQHNGLTPQDVFLNWV--PLDhvgGLVELHLRAVYLG--------CQQVHVPTEEILADPLRWLDLIDRyr 260

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  470 VARLWCP------------------ADIPTVKTLVMGGEPMLPNDIS-----LWKDKLR---LVCAYGPAE-CTVVSTVQ 522
Cdd:cd05906   261 VTITWAPnfafallndlleeiedgtWDLSSLRYLVNAGEAVVAKTIRrllrlLEPYGLPpdaIRPAFGMTEtCSGVIYSR 340

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  523 SCVQElgNIGRSP----CGTCW------IVSKDNhhRLMPVGCIGELIIGGPIVGRGYLKQPCLTANAFiTNPEWaslfh 592
Cdd:cd05906   341 SFPTY--DHSQALefvsLGRPIpgvsmrIVDDEG--QLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAF-TEDGW----- 410

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  593 lngsyrfYKTGDLVrYNADGTIAYIGRKDTQVKLNGQRVELGEIEH---QAQpyfrdAVIAAEVAAPAGRKP-----ILI 664
Cdd:cd05906   411 -------FRTGDLG-FLDNGNLTITGRTKDTIIVNGVNYYSHEIEAaveEVP-----GVEPSFTAAFAVRDPgaeteELA 477

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 992230864  665 LFIARKYEYSVNMDCTMllrppsilfqEKAQGTNTLLQEVLPRHMIPaayIELLAMPISRTGKVNRKLLREAVEQ 739
Cdd:cd05906   478 IFFVPEYDLQDALSETL----------RAIRSVVSREVGVSPAYLIP---LPKEEIPKTSLGKIQRSKLKAAFEA 539
LC_FACS_like cd17640
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ...
 257-637 5.32e-16

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: 83.18  E-value: 5.32e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  257 TITYRQL-DRLSSTVQGLLqqyDLG--PGSVVPIIFKKSKWAIVAMLGVLKAGAafcmldqsyptkrlVNICKDVDAKVi 333
Cdd:cd17640     5 RITYKDLyQEILDFAAGLR---SLGvkAGEKVALFADNSPRWLIADQGIMALGA--------------VDVVRGSDSSV- 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  334 vcsQELSIgvsgstlsIGDHNTETATYsaiqaVNTASHDAAYVVYTSGSTGAPKGIVIEHGSFCTNAIASSQAQNLDRSS 413
Cdd:cd17640    67 ---EELLY--------ILNHSESVALV-----VENDSDDLATIIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVPPQPGD 130

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  414 RVLQFAS--YAFDVSVHeslTPLLLGGCVCIPSEaqrVNSLKEAVSTLRVNwveLTPTVARLW--------------CPA 477
Cdd:cd17640   131 RFLSILPiwHSYERSAE---YFIFACGCSQAYTS---IRTLKDDLKRVKPH---YIVSVPRLWeslysgiqkqvsksSPI 201

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  478 DIPTVKTLVMGGEPMLP----NDISLWKDK------LRLVCAYGPAECTVVSTVQ--SCVQeLGNIGRSPCGTCWIVSKD 545
Cdd:cd17640   202 KQFLFLFFLSGGIFKFGisggGALPPHVDTffeaigIEVLNGYGLTETSPVVSARrlKCNV-RGSVGRPLPGTEIKIVDP 280

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  546 NHHRLMPVGCIGELIIGGPIVGRGYLKQPCLTANAfITNPEWaslfhlngsyrfYKTGDLVRYNADGTIAYIGR-KDTQV 624
Cdd:cd17640   281 EGNVVLPPGEKGIVWVRGPQVMKGYYKNPEATSKV-LDSDGW------------FNTGDLGWLTCGGELVLTGRaKDTIV 347

                         410
                  ....*....|...
gi 992230864  625 KLNGQRVELGEIE 637
Cdd:cd17640   348 LSNGENVEPQPIE 360
ACS-like cd17634
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ...
 246-728 6.72e-16

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: 83.40  E-value: 6.72e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  246 PDAQAICaWDG-------TITYRQLDRLSSTVQGLLQQYDLGPGSVVPIIFKKSKWAIVAMLGVLKAGAAFCML------ 312
Cdd:cd17634    67 GDRTAII-YEGddtsqsrTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIfggfap 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  313 ------------------DQSYPTKRLVNICKDVD--AKVIVCSQELSIGVSGSTLSIGD--------HNTETATYSAIQ 364
Cdd:cd17634   146 eavagriidsssrllitaDGGVRAGRSVPLKKNVDdaLNPNVTSVEHVIVLKRTGSDIDWqegrdlwwRDLIAKASPEHQ 225

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  365 AVNTASHDAAYVVYTSGSTGAPKGIVIEHGSFCTNAiASSQAQNLD-RSSRVLQFASYAFDVSVHESLT--PLLLGGCVC 441
Cdd:cd17634   226 PEAMNAEDPLFILYTSGTTGKPKGVLHTTGGYLVYA-ATTMKYVFDyGPGDIYWCTADVGWVTGHSYLLygPLACGATTL 304

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  442 I-------PSEAQrvnsLKEAVSTLRVNWVELTPTVARLWCPA--------DIPTVKTLVMGGEPMLPNDISLWKDKLrl 506
Cdd:cd17634   305 LyegvpnwPTPAR----MWQVVDKHGVNILYTAPTAIRALMAAgddaiegtDRSSLRILGSVGEPINPEAYEWYWKKI-- 378

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  507 vcayGPAECTVVS------TVQSCVQEL-GNIG-RSPCGTCWIVSK-----DNHHRLMPVGCIGELIIGGPIVGRgylkq 573
Cdd:cd17634   379 ----GKEKCPVVDtwwqteTGGFMITPLpGAIElKAGSATRPVFGVqpavvDNEGHPQPGGTEGNLVITDPWPGQ----- 449

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  574 pcltANAFITNPEWASLFHLNGSYRFYKTGDLVRYNADGTIAYIGRKDTQVKLNGQRVELGEIEH--QAQPYFRDAVIAA 651
Cdd:cd17634   450 ----TRTLFGDHERFEQTYFSTFKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESvlVAHPKVAEAAVVG 525

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  652 EVAAPAGRKPIlilfiarkyeysvnmdCTMLLR----PPSILFQEkaqgtntlLQEVLPRHMIPAAYIELL----AMPIS 723
Cdd:cd17634   526 IPHAIKGQAPY----------------AYVVLNhgvePSPELYAE--------LRNWVRKEIGPLATPDVVhwvdSLPKT 581


                  ....*
gi 992230864  724 RTGKV 728
Cdd:cd17634   582 RSGKI 586
SgcC5_NRPS-like cd19539
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ...
 1591-1864 7.48e-16

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: 82.43  E-value: 7.48e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1591 AWFTLARRHPALRTHLI----DIP----LCDGMSSKIHVVHKDYMADaaiLSCEDEHVITEL-RKPFLPSDTGLYYPHAF 1661
Cdd:cd19539    44 ALRDVVARHEALRTLLVrddgGVPrqeiLPPGPAPLEVRDLSDPDSD---RERRLEELLREReSRGFDLDEEPPIRAVLG 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1662 RIcqtVSGRVFCKLEGGHAFLDATSVLIILRELAQAYD----GQLSSVPGP--SYSSAVAWlQSLPNGDNRM----DYWR 1731
Cdd:cd19539   121 RF---DPDDHVLVLVAHHTAFDAWSLDVFARDLAALYAarrkGPAAPLPELrqQYKEYAAW-QREALAAPRAaellDFWR 196

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1732 RQLKDASPC--IFPRLRDQDSPSDT----LVVTEQLasTATLTPVCTRHGLTVSNVLQVAWGLMLRRYTESDDVCFGALI 1805
Cdd:cd19539   197 RRLRGAEPTalPTDRPRPAGFPYPGadlrFELDAEL--VAALRELAKRARSSLFMVLLAAYCVLLRRYTGQTDIVVGTPV 274

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 992230864 1806 SGRDSriPDVDKMVGPFFNVLVCQLRFGREDSLWDVLRRNQTEIGNRLLNQHCSLIEVL 1864
Cdd:cd19539   275 AGRNH--PRFESTVGFFVNLLPLRVDVSDCATFRDLIARVRKALVDAQRHQELPFQQLV 331
FACL_fum10p_like cd05926
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ...
 246-735 8.98e-16

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: 82.36  E-value: 8.98e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  246 PDAQAICAWDGT--ITYRQLDRLSSTVQGLLQQYDLGPGSVVPIIFKKSKWAIVAMLGVLKAGAAFCMLDQSYPTKRLVN 323
Cdd:cd05926     1 PDAPALVVPGSTpaLTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  324 ICKDVDAKVIV-------------------------CSQELSIGVSGSTLSIGDhntETATYSAIQAVNTAShDAAYVVY 378
Cdd:cd05926    81 YLADLGSKLVLtpkgelgpasraasklglailelalDVGVLIRAPSAESLSNLL---ADKKNAKSEGVPLPD-DLALILH 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  379 TSGSTGAPKGIVIEHGSFCTNAIASSQAQNLDRSSRVLQ----FASYAFDVSVhesLTPLLLGGCVCIP--SEAQRVNSL 452
Cdd:cd05926   157 TSGTTGRPKGVPLTHRNLAASATNITNTYKLTPDDRTLVvmplFHVHGLVASL---LSTLAAGGSVVLPprFSASTFWPD 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  453 KEAVstlRVNWVELTPTVARLWC---PADIPTVKTLVM----GGEPMLPNDISLWKDKLR--LVCAYGPAECTVVST--- 520
Cdd:cd05926   234 VRDY---NATWYTAVPTIHQILLnrpEPNPESPPPKLRfirsCSASLPPAVLEALEATFGapVLEAYGMTEAAHQMTsnp 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  521 VQSCVQELGNIGRsPCGTcWIVSKDNHHRLMPVGCIGELIIGGPIVGRGYLKQPCLTANAFITNPewaslfhlngsyrFY 600
Cdd:cd05926   311 LPPGPRKPGSVGK-PVGV-EVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDG-------------WF 375

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  601 KTGDLVRYNADGTIAYIGRKDTQVKLNGQRVELGEIEHQAqpYFRDAViaAEVAAPAGRKPililfiarKYEYSVNMdct 680
Cdd:cd05926   376 RTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVL--LSHPAV--LEAVAFGVPDE--------KYGEEVAA--- 440

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 992230864  681 mllrppSILFQEKAQGTNTLLQEVLPRHM----IPAAYIELLAMPISRTGKVNRKLLRE 735
Cdd:cd05926   441 ------AVVLREGASVTEEELRAFCRKHLaafkVPKKVYFVDELPKTATGKIQRRKVAE 493
4CL cd05904
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ...
 257-670 1.30e-15

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: 82.28  E-value: 1.30e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  257 TITYRQLDRLSSTVQG-----LLQQYD----LGPGSV-VPIIFkkskwaivamLGVLKAGAAFCMLDQSYPTKRLVNICK 326
Cdd:cd05904    32 ALTYAELERRVRRLAAglakrGGRKGDvvllLSPNSIeFPVAF----------LAVLSLGAVVTTANPLSTPAEIAKQVK 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  327 DVDAKVIVCSQEL---------SIGVSGSTLSIGDHNTE---TATYSAIQAVNTASHDAAYVVYTSGSTGAPKGIVIEHG 394
Cdd:cd05904   102 DSGAKLAFTTAELaeklaslalPVVLLDSAEFDSLSFSDllfEADEAEPPVVVIKQDDVAALLYSSGTTGRSKGVMLTHR 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  395 SFCTNA--IASSQAQNLDRSSRVL----QFASYAFDVSVhesLTPLLLGGCVCIPSEAQrVNSLKEAVSTLRVNWVELTP 468
Cdd:cd05904   182 NLIAMVaqFVAGEGSNSDSEDVFLcvlpMFHIYGLSSFA---LGLLRLGATVVVMPRFD-LEELLAAIERYKVTHLPVVP 257

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  469 TV------ARLWCPADIPTVKTLVMGGEPMLPNDISLWKDKL---RLVCAYGPAECTVVSTvqSCVQELGNIGRSpcGTC 539
Cdd:cd05904   258 PIvlalvkSPIVDKYDLSSLRQIMSGAAPLGKELIEAFRAKFpnvDLGQGYGMTESTGVVA--MCFAPEKDRAKY--GSV 333

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  540 -WIVSK------D-NHHRLMPVGCIGELIIGGPIVGRGYLKQPCLTANAFitNPEwaslfhlngsyRFYKTGDLVRYNAD 611
Cdd:cd05904   334 gRLVPNveakivDpETGESLPPNQTGELWIRGPSIMKGYLNNPEATAATI--DKE-----------GWLHTGDLCYIDED 400

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 992230864  612 GTIAYIGR-KDTqVKLNGQRVELGEIEH--QAQPYFRDaviAAEVAAP---AGRKPilILFIARK 670
Cdd:cd05904   401 GYLFIVDRlKEL-IKYKGFQVAPAELEAllLSHPEILD---AAVIPYPdeeAGEVP--MAFVVRK 459
BCL_4HBCL cd05959
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ...
 256-734 1.53e-15

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: 82.03  E-value: 1.53e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  256 GTITYRQLDRLSSTVQGLLQQYDLGPGSVVPIIFKKSKWAIVAMLGVLKAGAAFCMLDQSYPTKRLVNICKDVDAKVIVC 335
Cdd:cd05959    28 GSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARVVVV 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  336 SQEL---------SIGVSGSTL-SIGDHNTETATYS----------AIQAVNTASHDAAYVVYTSGSTGAPKGIVIEHGS 395
Cdd:cd05959   108 SGELapvlaaaltKSEHTLVVLiVSGGAGPEAGALLlaelvaaeaeQLKPAATHADDPAFWLYSSGSTGRPKGVVHLHAD 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  396 FctNAIASSQAQN---LDRSSRVLQFASYAFDVSVHESLT-PLLLGG-CVCIPSE---------AQRVN-SLKEAVSTLR 460
Cdd:cd05959   188 I--YWTAELYARNvlgIREDDVCFSAAKLFFAYGLGNSLTfPLSVGAtTVLMPERptpaavfkrIRRYRpTVFFGVPTLY 265

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  461 VNWveltpTVARLWCPADIPTVKTLVMGGEPmLPNDISL-WKDKlrlvcaYGpaeCTVVSTVQScvQELGNI------GR 533
Cdd:cd05959   266 AAM-----LAAPNLPSRDLSSLRLCVSAGEA-LPAEVGErWKAR------FG---LDILDGIGS--TEMLHIflsnrpGR 328

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  534 SPCGTCW---------IVSKDNHHrlMPVGCIGELIIGGPIVGRGYLKQPCLTANAFITnpEWaslfhlngsyrfYKTGD 604
Cdd:cd05959   329 VRYGTTGkpvpgyeveLRDEDGGD--VADGEPGELYVRGPSSATMYWNNRDKTRDTFQG--EW------------TRTGD 392

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  605 LVRYNADGTIAYIGRKDTQVKLNGQRVELGEIEH--QAQPYFRD-AVIAAEvaAPAGR-KPILILFIARKYEysvnmdct 680
Cdd:cd05959   393 KYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESalVQHPAVLEaAVVGVE--DEDGLtKPKAFVVLRPGYE-------- 462

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....
gi 992230864  681 mllrPPSILFQEkaqgTNTLLQEVLPRHMIPAAYIELLAMPISRTGKVNRKLLR 734
Cdd:cd05959   463 ----DSEALEEE----LKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKLR 508
MACS_like_2 cd05973
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
 258-734 6.31e-15

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: 79.48  E-value: 6.31e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  258 ITYRQLDRLSSTVQGLLQQYDLGPGSVVPIIFKKSKWAIVAMLGVLKAGAAFCMLDQSYPTKRLVNICKDVDAKVIVCSq 337
Cdd:cd05973     1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTD- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  338 elsigvsgstlsigdhntetatysaiqAVNTASHDAAYVV--YTSGSTGAPKGIVIEhgsfcTNAIASSQAQ-----NLD 410
Cdd:cd05973    80 ---------------------------AANRHKLDSDPFVmmFTSGTTGLPKGVPVP-----LRALAAFGAYlrdavDLR 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  411 RSSRVLQFASYAFDVSVHESLT-PLLLGGCVCIPSEAQRVNSLKEAVSTLRVNWVELTPTVARLW--CPADIPTVKTLVM 487
Cdd:cd05973   128 PEDSFWNAADPGWAYGLYYAITgPLALGHPTILLEGGFSVESTWRVIERLGVTNLAGSPTAYRLLmaAGAEVPARPKGRL 207

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  488 -----GGEPMLPNDISLWKDKLRLVCA--YGPAEC-TVVSTVQSCVQEL--GNIGRSPCGTCWIVSKDNHHRLMPvGCIG 557
Cdd:cd05973   208 rrvssAGEPLTPEVIRWFDAALGVPIHdhYGQTELgMVLANHHALEHPVhaGSAGRAMPGWRVAVLDDDGDELGP-GEPG 286

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  558 ELII---GGPIVG-RGYLKQPCLTANAfitnpewaslfhlngsyRFYKTGDLVRYNADGTIAYIGRKDTQVKLNGQR--- 630
Cdd:cd05973   287 RLAIdiaNSPLMWfRGYQLPDTPAIDG-----------------GYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRigp 349

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  631 --VELGEIEHQaqpyfrdAVI-AAEVAAPAG-RKPILILFIarkyeysvnmdctmLLRPPSILFQEKAQGTNTLLQEVLP 706
Cdd:cd05973   350 fdVESALIEHP-------AVAeAAVIGVPDPeRTEVVKAFV--------------VLRGGHEGTPALADELQLHVKKRLS 408

                         490       500
                  ....*....|....*....|....*...
gi 992230864  707 RHMIPAAYIELLAMPISRTGKVNRKLLR 734
Cdd:cd05973   409 AHAYPRTIHFVDELPKTPSGKIQRFLLR 436
PRK12467 PRK12467
peptide synthase; Provisional
 1356-1844 1.52e-14

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 80.21  E-value: 1.52e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1356 QLISSLGQSLPRSAVPSLCLPVSFIPVDPLGQPDRIYLCEAASSmtldflhsltdPVNKYIDYHILPEEARLRGIVAHVL 1435
Cdd:PRK12467  975 ELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKALPKPDAS-----------AVQATFVAPQTELEKRLAAIWADVL 1043

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1436 SIDPqnISPKDDFFTLGGDSISAMQVVSLCRKH---QLSLTALdiFNGRTIELIATRLMPLTPYTPPSTPASDRslDRRF 1512
Cdd:PRK12467 1044 KVER--VGLTDNFFELGGHSLLATQVISRVRQRlgiQVPLRTL--FEHQTLAGFAQAVAAQQQGAQPALPDVDR--DQPL 1117

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1513 SLLFLNsdrdmERLesllmatYDIGSMDSIEDAY--PCSESHQGLLQTQMLRpfyyqsytiwevttrsksspvspvrlcN 1590
Cdd:PRK12467 1118 PLSYAQ-----ERQ-------WFLWQLEPGSAAYhiPQALRLKGPLDIEALE---------------------------R 1158

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1591 AWFTLARRHPALRTHLIDIplcDGMSSK-IHVV------HKDYMADAAILSCEDEHVITELRKPFLPSDTGLYYPHAFRI 1663
Cdd:PRK12467 1159 SFDALVARHESLRTTFVQE---DGRTRQvIHPVgsltleEPLLLAADKDEAQLKVYVEAEARQPFDLEQGPLLRVGLLRL 1235

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1664 CQTVSGRVfckLEGGHAFLDATSVLIILRELAQAYDG-------QLSSVPgPSYSSAVAWL-QSLPNG--DNRMDYWRRQ 1733
Cdd:PRK12467 1236 AADEHVLV---LTLHHIVSDGWSMQVLVDELVALYAAysqgqslQLPALP-IQYADYAVWQrQWMDAGerARQLAYWKAQ 1311

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1734 LKDASPCI-----FPRLRDQDSPSDTLVVTEQLASTATLTPVCTRHGLTVSNVLQVAWGLMLRRYTESDDVCFGALISGR 1808
Cdd:PRK12467 1312 LGGEQPVLelptdRPRPAVQSHRGARLAFELPPALAEGLRALARREGVTLFMLLLASFQTLLHRYSGQDDIRVGVPIANR 1391

                         490       500       510
                  ....*....|....*....|....*....|....*.
gi 992230864 1809 DSRipDVDKMVGPFFNVLVCQLRFGREDSLWDVLRR 1844
Cdd:PRK12467 1392 NRA--ETEGLIGFFVNTQVLRAEVDGQASFQQLLQQ 1425
PRK05852 PRK05852
fatty acid--CoA ligase family protein;
246-637 1.62e-14

fatty acid--CoA ligase family protein;


Pssm-ID: 235625 [Multi-domain]  Cd Length: 534  Bit Score: 78.78  E-value: 1.62e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  246 PDAQAICAWDG--TITYRQLDRLSSTVQGLLQQYDLGPGSVVPIIFKKSKWAIVAMLGVLKAGAAFCMLDQSYPTKRLVN 323
Cdd:PRK05852   30 PEAPALVVTADriAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEQRV 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  324 ICKDVDAKVI------VCSQEL--------------SIGVSGSTLSIgdHNTETATYSAIQAVNTA-SHDAAYVVYTSGS 382
Cdd:PRK05852  110 RSQAAGARVVlidadgPHDRAEpttrwwpltvnvggDSGPSGGTLSV--HLDAATEPTPATSTPEGlRPDDAMIMFTGGT 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  383 TGAPKGIVIEHGSFCTNAIASSQAQNL-DRSSRVLQFASYAFDVSVHESLTPLLLGGCVCIPSEAQ-RVNSLKEAVSTLR 460
Cdd:PRK05852  188 TGLPKMVPWTHANIASSVRAIITGYRLsPRDATVAVMPLYHGHGLIAALLATLASGGAVLLPARGRfSAHTFWDDIKAVG 267

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  461 VNWVELTPTVARL--------WCPADIPTVKTLVMGGEPMLPNDISLWKDKLR--LVCAYGPAECT--VVST-------V 521
Cdd:PRK05852  268 ATWYTAVPTIHQIlleraatePSGRKPAALRFIRSCSAPLTAETAQALQTEFAapVVCAFGMTEAThqVTTTqiegigqT 347

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  522 QSCVQELGNIGRSPCGTCWIVSKDNHHrlMPVGCIGELIIGGPIVGRGYLKQPCLTANAFITNpeWaslfhlngsyrfYK 601
Cdd:PRK05852  348 ENPVVSTGLVGRSTGAQIRIVGSDGLP--LPAGAVGEVWLRGTTVVRGYLGDPTITAANFTDG--W------------LR 411

                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 992230864  602 TGDLVRYNADGTIAYIGRKDTQVKLNGQRVELGEIE 637
Cdd:PRK05852  412 TGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVE 447
CBAL cd05923
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ...
 245-649 3.55e-14

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: 77.55  E-value: 3.55e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  245 QPDAQAICAWDGT--ITYRQL-DRLSSTVQGLLQQyDLGPGSVVPIIFKKSKWAIVAMLGVLKAGAAFCMLDQSYPTKRL 321
Cdd:cd05923    14 APDACAIADPARGlrLTYSELrARIEAVAARLHAR-GLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAEL 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  322 VN-ICKDVDAKVIVCSQEL----SIGVSGSTLSIGDHNTETATYSA---IQAVNTASHDAAYVVYTSGSTGAPKGIVIEH 393
Cdd:cd05923    93 AElIERGEMTAAVIAVDAQvmdaIFQSGVRVLALSDLVGLGEPESAgplIEDPPREPEQPAFVFYTSGTTGLPKGAVIPQ 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  394 GSFCTNAIA-SSQAQNL-DRSSRVLQFASYAFDVSVHESLT-PLLLGGCVCIPSEAQRVNSLKeAVSTLRVNWVELTPT- 469
Cdd:cd05923   173 RAAESRVLFmSTQAGLRhGRHNVVLGLMPLYHVIGFFAVLVaALALDGTYVVVEEFDPADALK-LIEQERVTSLFATPTh 251

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  470 -----VARLWCPADIPTVKTLVMGGEPMlpNDISLwkDKL------RLVCAYGPAEcTVVSTVQSCVQElGNIGR----S 534
Cdd:cd05923   252 ldalaAAAEFAGLKLSSLRHVTFAGATM--PDAVL--ERVnqhlpgEKVNIYGTTE-AMNSLYMRDART-GTEMRpgffS 325

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  535 PCGTCWIVSKDNHhrLMPVGCIGELII--GGPIVGRGYLKQPCLTANafitnpewaslfhlNGSYRFYKTGDLVRYNADG 612
Cdd:cd05923   326 EVRIVRIGGSPDE--ALANGEEGELIVaaAADAAFTGYLNQPEATAK--------------KLQDGWYRTGDVGYVDPSG 389

                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 992230864  613 TIAYIGRKDTQVKLNGQRVELGEIEH--QAQPYFRDAVI 649
Cdd:cd05923   390 DVRILGRVDDMIISGGENIHPSEIERvlSRHPGVTEVVV 428
LCL_NRPS-like cd19531
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ...
 1683-1844 4.88e-14

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: 76.62  E-value: 4.88e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1683 DATSVLIILRELAQAYD----GQLSSVPGPS-----YssAV---AWLQSlPNGDNRMDYWRRQLKDASPCI-----FPRL 1745
Cdd:cd19531   139 DGWSMGVLLRELAALYAaflaGRPSPLPPLPiqyadY--AVwqrEWLQG-EVLERQLAYWREQLAGAPPVLelptdRPRP 215

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1746 RDQDSPSDTLVVT--EQLasTATLTPVCTRHGLTVSNVLQVAWGLMLRRYTESDDVCFGALISGRDSriPDVDKMVGPFF 1823
Cdd:cd19531   216 AVQSFRGARVRFTlpAEL--TAALRALARREGATLFMTLLAAFQVLLHRYSGQDDIVVGTPVAGRNR--AELEGLIGFFV 291

                         170       180
                  ....*....|....*....|.
gi 992230864 1824 NVLVCQLRFGREDSLWDVLRR 1844
Cdd:cd19531   292 NTLVLRTDLSGDPTFRELLAR 312
C_PKS-NRPS cd19532
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
 1582-1844 5.42e-14

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: 76.34  E-value: 5.42e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1582 PVSPVRLCNAWFTLARRHPALRThlidiplC------DGM-------SSKIHVVHKDYMADAAIlscedEHVITELRKpf 1648
Cdd:cd19532    35 PLDVARLERAVRAVGQRHEALRT-------CfftdpeDGEpmqgvlaSSPLRLEHVQISDEAEV-----EEEFERLKN-- 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1649 lpsdtglyypHAFRIcqtVSGRVF----CKLEGGHAFL---------DATSVLIILRELAQAYDGQLSSVPGPSYSS-AV 1714
Cdd:cd19532   101 ----------HVYDL---ESGETMrivlLSLSPTEHYLifgyhhiamDGVSFQIFLRDLERAYNGQPLLPPPLQYLDfAA 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1715 AWLQSLPNG--DNRMDYWRRQLKDASPCI--FPRLRDQDSPSdtLVVTEQLASTATLTP--------VCTRHGLTVSN-- 1780
Cdd:cd19532   168 RQRQDYESGalDEDLAYWKSEFSTLPEPLplLPFAKVKSRPP--LTRYDTHTAERRLDAalaarikeASRKLRVTPFHfy 245

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 992230864 1781 --VLQVawglMLRRYTESDDVCFGALISGRDSriPDVDKMVGPFFNVLVCQLRFGREDSLWDVLRR 1844
Cdd:cd19532   246 laALQV----LLARLLDVDDICIGIADANRTD--EDFMETIGFFLNLLPLRFRRDPSQTFADVLKE 305
entE PRK10946
(2,3-dihydroxybenzoyl)adenylate synthase;
245-742 5.72e-14

(2,3-dihydroxybenzoyl)adenylate synthase;


Pssm-ID: 236803 [Multi-domain]  Cd Length: 536  Bit Score: 76.95  E-value: 5.72e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  245 QPDAQAICAWDGTITYRQLDRLSSTVQGLLQQYDLGPGSVvpiifkkskwAIV----------AMLGVLKAGAAFCMLDQ 314
Cdd:PRK10946   36 ASDAIAVICGERQFSYRELNQASDNLACSLRRQGIKPGDT----------ALVqlgnvaefyiTFFALLKLGVAPVNALF 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  315 SYPTKRLVNICKDVDAKVIVCS------------QELSIGVSG-STLSIGDHNTETATYSAIQ-------AVNTASHDAA 374
Cdd:PRK10946  106 SHQRSELNAYASQIEPALLIADrqhalfsdddflNTLVAEHSSlRVVLLLNDDGEHSLDDAINhpaedftATPSPADEVA 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  375 YVVYTSGSTGAPKGIVIEHGSFCTNAIASSQAQNLDRSSRVLQF--ASYAFDVSVHESLTPLLLGGCVCIPSEAQRVNSL 452
Cdd:PRK10946  186 FFQLSGGSTGTPKLIPRTHNDYYYSVRRSVEICGFTPQTRYLCAlpAAHNYPMSSPGALGVFLAGGTVVLAPDPSATLCF 265

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  453 kEAVSTLRVNWVELTPTVARLWCPA--------DIPTVKTLVMGGEPM-------LPNDISLwkdKLRLVcaYGPAECTV 517
Cdd:PRK10946  266 -PLIEKHQVNVTALVPPAVSLWLQAiaeggsraQLASLKLLQVGGARLsetlarrIPAELGC---QLQQV--FGMAEGLV 339

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  518 VSTV--QSCVQELGNIGR--SPCGTCWIVskDNHHRLMPVGCIGELIIGGPIVGRGYLKQPCLTANAFITNPewaslfhl 593
Cdd:PRK10946  340 NYTRldDSDERIFTTQGRpmSPDDEVWVA--DADGNPLPQGEVGRLMTRGPYTFRGYYKSPQHNASAFDANG-------- 409

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  594 ngsyrFYKTGDLVRYNADGTIAYIGRKDTQVKLNGQRVELGEIEHQ--AQPyfrdAVI-AAEVAAP---AGRKpililfi 667
Cdd:PRK10946  410 -----FYCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLllRHP----AVIhAALVSMEdelMGEK------- 473

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  668 arkyeysvnmDCTML-----LRPPSILFQEKAQGtntLLQEVLPRHmipaayIELL-AMPISRTGKVNRKLLREAVEQAS 741
Cdd:PRK10946  474 ----------SCAFLvvkepLKAVQLRRFLREQG---IAEFKLPDR------VECVdSLPLTAVGKVDKKQLRQWLASRA 534


                  .
gi 992230864  742 E 742
Cdd:PRK10946  535 S 535
beta-lac_NRPS cd19547
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ...
 1588-1907 6.02e-14

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: 76.20  E-value: 6.02e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1588 LCNAWFTLARRHPALRTHLIdiplCDGMSSKIHVVHKDYMADAAIL--SCEDEHVITELRKPFLPSD--TGLYYP----H 1659
Cdd:cd19547    41 LREAWRRVADRYEILRTGFT----WRDRAEPLQYVRDDLAPPWALLdwSGEDPDRRAELLERLLADDraAGLSLAdcplY 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1660 AFRICQTVSGRVFCKLEGGHAFLDA-------TSVLIILRELAQAYDGQLSsvPGPSYSSAVAWLQS-LPNGDNRMDYWR 1731
Cdd:cd19547   117 RLTLVRLGGGRHYLLWSHHHILLDGwclsliwGDVFRVYEELAHGREPQLS--PCRPYRDYVRWIRArTAQSEESERFWR 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1732 RQLKDASPCIFPRL-RDQDSPSDTLV--VTEQLasTATLTPVCTRHGLTVSNVLQVAWGLMLRRYTESDDVCFGALISGR 1808
Cdd:cd19547   195 EYLRDLTPSPFSTApADREGEFDTVVheFPEQL--TRLVNEAARGYGVTTNAISQAAWSMLLALQTGARDVVHGLTIAGR 272

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1809 DSRIPDVDKMVGPFFNVLVCQLRFGREDSLWDVLRRNQTEIGNRLLNQHCSLIEVLRFST---YFGQPLFNTCISVEQPL 1885
Cdd:cd19547   273 PPELEGSEHMVGIFINTIPLRIRLDPDQTVTGLLETIHRDLATTAAHGHVPLAQIKSWASgerLSGGRVFDNLVAFENYP 352

                         330       340
                  ....*....|....*....|....
gi 992230864 1886 SMDTPDASLCFK--ELETLEPTEY 1907
Cdd:cd19547   353 EDNLPGDDLSIQiiDLHAQEKTEY 376
AACS_like cd05968
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ...
 210-736 1.81e-13

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: 75.60  E-value: 1.81e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  210 LSKHHQdqIAEWNRNAPIHPFDSCIHTLFRlqcilQPDAQAICAWDG------TITYRQLDRLSSTVQGLLQQYDLGPGS 283
Cdd:cd05968    45 LSGGKP--WAAWFVGGRMNIVEQLLDKWLA-----DTRTRPALRWEGedgtsrTLTYGELLYEVKRLANGLRALGVGKGD 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  284 VVPIIFKKSKWAIVAMLGVLKAGAAFCML------------------------DQSYPTKRLVNICKDVDAKVIVCSQ-E 338
Cdd:cd05968   118 RVGIYLPMIPEIVPAFLAVARIGGIVVPIfsgfgkeaaatrlqdaeakalitaDGFTRRGREVNLKEEADKACAQCPTvE 197

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  339 LSIGVSGSTLSIGDHN------TETATYSAIQAVNTASHDAAYVVYTSGSTGAPKGIVIEHGSFCTNAIASSQAQ-NLDR 411
Cdd:cd05968   198 KVVVVRHLGNDFTPAKgrdlsyDEEKETAGDGAERTESEDPLMIIYTSGTTGKPKGTVHVHAGFPLKAAQDMYFQfDLKP 277

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  412 SSRVLQFASYAFDVSVHESLTPLLLGGCVCIPSEA---QRVNSLKEAVSTLRVNWVELTPTVARLWCPA--------DIP 480
Cdd:cd05968   278 GDLLTWFTDLGWMMGPWLIFGGLILGATMVLYDGApdhPKADRLWRMVEDHEITHLGLSPTLIRALKPRgdapvnahDLS 357

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  481 TVKTLVMGGEPMLPnDISLW------KDKLRLVCAYGPAE-------CTVVSTVQSCvqelGNIGRSPcGTCWIVSKDNH 547
Cdd:cd05968   358 SLRVLGSTGEPWNP-EPWNWlfetvgKGRNPIINYSGGTEisggilgNVLIKPIKPS----SFNGPVP-GMKADVLDESG 431

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  548 HRLMPVgcIGELIIGGPIVG--RGYLKQPCLTANAFitnpeWASLfhlngsYRFYKTGDLVRYNADGTIAYIGRKDTQVK 625
Cdd:cd05968   432 KPARPE--VGELVLLAPWPGmtRGFWRDEDRYLETY-----WSRF------DNVWVHGDFAYYDEEGYFYILGRSDDTIN 498

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  626 LNGQRVELGEIEH--QAQPYFRDaviAAEVAAP---AGRKPIlilfiarkyeysvnmdCTMLLRPPSILFQEKAQGTNTL 700
Cdd:cd05968   499 VAGKRVGPAEIESvlNAHPAVLE---SAAIGVPhpvKGEAIV----------------CFVVLKPGVTPTEALAEELMER 559

                         570       580       590
                  ....*....|....*....|....*....|....*.
gi 992230864  701 LQEVLPRHMIPAAYIELLAMPISRTGKVNRKLLREA 736
Cdd:cd05968   560 VADELGKPLSPERILFVKDLPKTRNAKVMRRVIRAA 595
COG4908 COG4908
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ...
 1580-1778 2.63e-13

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


Pssm-ID: 443936 [Multi-domain]  Cd Length: 243  Bit Score: 71.61  E-value: 2.63e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1580 SSPVSPVRLCNAWFTLARRHPALRTHLIDIP------LCDGMSSKIHVVHKDYMADAAILSCEDEHVITELRKPFLPSDT 1653
Cdd:COG4908    27 EGPLDVEALERALRELVRRHPALRTRFVEEDgepvqrIDPDADLPLEVVDLSALPEPEREAELEELVAEEASRPFDLARG 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1654 GLyyphaFRIcqtvsgRVFCKLEGGHAFL--------DATSVLIILRELAQAY----DGQLSSVPGP--SYSSAVAWLQS 1719
Cdd:COG4908   107 PL-----LRA------ALIRLGEDEHVLLltihhiisDGWSLGILLRELAALYaallEGEPPPLPELpiQYADYAAWQRA 175

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 992230864 1720 LPNGDNR---MDYWRRQLKDAS-----PCIFPRLRDQDSPSDTLVVT--EQLasTATLTPVCTRHGLTV 1778
Cdd:COG4908   176 WLQSEALekqLEYWRQQLAGAPpvlelPTDRPRPAVQTFRGATLSFTlpAEL--TEALKALAKAHGATV 242
PRK06814 PRK06814
acyl-[ACP]--phospholipid O-acyltransferase;
256-742 2.68e-13

acyl-[ACP]--phospholipid O-acyltransferase;


Pssm-ID: 235865 [Multi-domain]  Cd Length: 1140  Bit Score: 75.77  E-value: 2.68e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  256 GTITYRQLdRLSSTVQGLLQQYDLGPGSVVPIIFKKSKWAIVAMLGVLKAGAAFCMLDQSYPTKRLVNICKDVDAKVIVC 335
Cdd:PRK06814  657 GPLTYRKL-LTGAFVLGRKLKKNTPPGENVGVMLPNANGAAVTFFALQSAGRVPAMINFSAGIANILSACKAAQVKTVLT 735

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  336 S---------QELSIGVSGS-----------TLSIGDHNTETATYSAIQAVNTASH--DAAYVVYTSGSTGAPKGIVIEH 393
Cdd:PRK06814  736 SrafiekarlGPLIEALEFGiriiyledvraQIGLADKIKGLLAGRFPLVYFCNRDpdDPAVILFTSGSEGTPKGVVLSH 815

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  394 GSFCTNAIASSQAQNLDRSSRVLQ----FASYAFDVSVhesLTPLLLGGCV----------CIPSEAQRVNS-LKEAVST 458
Cdd:PRK06814  816 RNLLANRAQVAARIDFSPEDKVFNalpvFHSFGLTGGL---VLPLLSGVKVflypsplhyrIIPELIYDTNAtILFGTDT 892

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  459 LRVNWveltptvARLWCPADIPTVKTLVMGGEPMLPNDISLWKDK--LRLVCAYGPAECTVVSTVQSCVQ-ELGNIGRSP 535
Cdd:PRK06814  893 FLNGY-------ARYAHPYDFRSLRYVFAGAEKVKEETRQTWMEKfgIRILEGYGVTETAPVIALNTPMHnKAGTVGRLL 965

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  536 CGTcwivskdnHHRLMPVGCI---GELIIGGPIVGRGYLKqpcLTANAFITNPE--WaslfhlngsyrfYKTGDLVRYNA 610
Cdd:PRK06814  966 PGI--------EYRLEPVPGIdegGRLFVRGPNVMLGYLR---AENPGVLEPPAdgW------------YDTGDIVTIDE 1022

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  611 DGTIAYIGRKDTQVKLNGQRVELGEIEHQAQPYFRDAVIAAeVAAPAGRK-PILILFIARKyeysvnmDCTMllrpPSIL 689
Cdd:PRK06814 1023 EGFITIKGRAKRFAKIAGEMISLAAVEELAAELWPDALHAA-VSIPDARKgERIILLTTAS-------DATR----AAFL 1090

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 992230864  690 FQEKAQGtntllqevLPRHMIPAAYIELLAMPISRTGKVN----RKLLREAVEQASE 742
Cdd:PRK06814 1091 AHAKAAG--------ASELMVPAEIITIDEIPLLGTGKIDyvavTKLAEEAAAKPEA 1139
FADD10 cd17635
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ...
 372-730 3.67e-13

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: 73.06  E-value: 3.67e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  372 DAAYVVYTSGSTGAPKGIVIEHGSFCTNAIASSQAQNLDRSSRVLQFASY-AFDVSVHESLTPLLLGGCVCIPSEAQRVN 450
Cdd:cd17635     2 DPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGLNWVVGDVTYLPLPaTHIGGLWWILTCLIHGGLCVTGGENTTYK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  451 SLKEAVSTLRVNWVELTPTvarLWCP---------ADIPTVKTLVMGGEPMLPNDIS--LWKDKLRLVCAYGPAECTVVS 519
Cdd:cd17635    82 SLFKILTTNAVTTTCLVPT---LLSKlvselksanATVPSLRLIGYGGSRAIAADVRfiEATGLTNTAQVYGLSETGTAL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  520 TVQ--SCVQELGNIGRSPCGTCWIVsKDNHHRLMPVGCIGELIIGGPIVGRGYLKQPCLTANAFITnpEWaslfhlngsy 597
Cdd:cd17635   159 CLPtdDDSIEINAVGRPYPGVDVYL-AATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLID--GW---------- 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  598 rfYKTGDLVRYNADGTIAYIGRKDTQVKLNGQRVELGEIEHQAQ--PYFRDAVIAAEVAAPAGRKPILILFIArkyeysv 675
Cdd:cd17635   226 --VNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEgvSGVQECACYEISDEEFGELVGLAVVAS------- 296

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 992230864  676 nmdctmllrppSILFQEKAQGTNTLLQEVLPRHMIPAAYIELLAMPISRTGKVNR 730
Cdd:cd17635   297 -----------AELDENAIRALKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
MACS_AAE_MA_like cd05970
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ...
 245-637 4.95e-13

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: 74.07  E-value: 4.95e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  245 QPDAQAIcAW--DGT----ITYRQLDRLSSTVQGLLQQYDLGPGSVVPIIFKKSKWAIVAMLGVLKAGAAFCMLDQSYPT 318
Cdd:cd05970    30 YPDKLAL-VWcdDAGeeriFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPATHQLTA 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  319 KRLVNICKDVDAKVIVCSQELSI-----------GVSGSTLSIGDHNTE------------TATYSAIQA-VNTASHDAA 374
Cdd:cd05970   109 KDIVYRIESADIKMIVAIAEDNIpeeiekaapecPSKPKLVWVGDPVPEgwidfrkliknaSPDFERPTAnSYPCGEDIL 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  375 YVVYTSGSTGAPKGIVIEHGSFCTNAIASSQAQNLDRSSRVLQFASYAFDVSVHESLTPLLLGGCVCIPSEAQRVN--SL 452
Cdd:cd05970   189 LVYFSSGTTGMPKMVEHDFTYPLGHIVTAKYWQNVREGGLHLTVADTGWGKAVWGKIYGQWIAGAAVFVYDYDKFDpkAL 268

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  453 KEAVSTLRVNWVELTPTVARLWCPADI-----PTVKTLVMGGEPMLPNDISLWKDK--LRLVCAYGPAECTVVSTVQSCV 525
Cdd:cd05970   269 LEKLSKYGVTTFCAPPTIYRFLIREDLsrydlSSLRYCTTAGEALNPEVFNTFKEKtgIKLMEGFGQTETTLTIATFPWM 348

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  526 Q-ELGNIGRsPCGTCWIVSKDNHHRLMPVGCIGELII----GGPI-VGRGYLKQPCLTANAFITNpewaslfhlngsyrF 599
Cdd:cd05970   349 EpKPGSMGK-PAPGYEIDLIDREGRSCEAGEEGEIVIrtskGKPVgLFGGYYKDAEKTAEVWHDG--------------Y 413

                         410       420       430
                  ....*....|....*....|....*....|....*...
gi 992230864  600 YKTGDLVRYNADGTIAYIGRKDTQVKLNGQRVELGEIE 637
Cdd:cd05970   414 YHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVE 451
PRK08751 PRK08751
long-chain fatty acid--CoA ligase;
247-655 5.42e-13

long-chain fatty acid--CoA ligase;


Pssm-ID: 181546 [Multi-domain]  Cd Length: 560  Bit Score: 74.14  E-value: 5.42e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  247 DAQAICAWDGTITYRQLDRLSSTVQG-LLQQYDLGPGSVVPIIFKKSKWAIVAMLGVLKAGAAFCMLDQSYPTKRLVNIC 325
Cdd:PRK08751   40 DRPAYHSFGKTITYREADQLVEQFAAyLLGELQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHQL 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  326 KDVDAKVIVCSQELSIGVSGS----------TLSIGD---------------------------------HNTETATYSA 362
Cdd:PRK08751  120 IDSGASVLVVIDNFGTTVQQViadtpvkqviTTGLGDmlgfpkaalvnfvvkyvkklvpeyringairfrEALALGRKHS 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  363 IQAVNTASHDAAYVVYTSGSTGAPKGIVIEHGSFCTNAIASSQ----AQNLDRSSRVLQFA--SYAFDVSVHESLTPLLL 436
Cdd:PRK08751  200 MPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQwlagTGKLEEGCEVVITAlpLYHIFALTANGLVFMKI 279

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  437 GGCVCIPSEAQR----VNSLKE-------AVSTLrVNWVELTPTVARLwcpaDIPTVKTLVMGGEPMLPNDISLWKD--K 503
Cdd:PRK08751  280 GGCNHLISNPRDmpgfVKELKKtrftaftGVNTL-FNGLLNTPGFDQI----DFSSLKMTLGGGMAVQRSVAERWKQvtG 354

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  504 LRLVCAYGPAEctvvSTVQSCVQEL------GNIGRsPCGTCWIVSKDNHHRLMPVGCIGELIIGGPIVGRGYLKQPCLT 577
Cdd:PRK08751  355 LTLVEAYGLTE----TSPAACINPLtlkeynGSIGL-PIPSTDACIKDDAGTVLAIGEIGELCIKGPQVMKGYWKRPEET 429

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  578 ANAfITNPEWaslFHlngsyrfykTGDLVRYNADGTIAYIGRKDTQVKLNGQRVELGEIEHqaqpyfrdaVIA-----AE 652
Cdd:PRK08751  430 AKV-MDADGW---LH---------TGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIED---------VIAmmpgvLE 487


                  ...
gi 992230864  653 VAA 655
Cdd:PRK08751  488 VAA 490
PRK07514 PRK07514
malonyl-CoA synthase; Validated
 246-402 7.57e-13

malonyl-CoA synthase; Validated


Pssm-ID: 181011 [Multi-domain]  Cd Length: 504  Bit Score: 73.37  E-value: 7.57e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  246 PDAQAICAWDG-TITYRQLDRLSSTVQGLLQQYDLGPGSVVPIIFKKSKWAIVAMLGVLKAGAAFCMLDQSYPTKRLVNI 324
Cdd:PRK07514   16 RDAPFIETPDGlRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDYF 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  325 CKDVDAKVIVCSQELSIGVS--------GSTLSIGDHNTETATYSAIQA------VNTASHDAAYVVYTSGSTGAPKGIV 390
Cdd:PRK07514   96 IGDAEPALVVCDPANFAWLSkiaaaagaPHVETLDADGTGSLLEAAAAApddfetVPRGADDLAAILYTSGTTGRSKGAM 175

                         170
                  ....*....|..
gi 992230864  391 IEHGSFCTNAIA 402
Cdd:PRK07514  176 LSHGNLLSNALT 187
OSB_MenE-like cd17630
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ...
 374-735 2.22e-12

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: 70.44  E-value: 2.22e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  374 AYVVYTSGSTGAPKGIVIEHGSFCTNAIASSQAQNLDRSSRVLqFASYAFDVS----VHESltpLLLGGCVCIPSEAQrv 449
Cdd:cd17630     3 ATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWL-LSLPLYHVGglaiLVRS---LLAGAELVLLERNQ-- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  450 nSLKEAVSTLRVNWVELTPT-----VARLWCPADIPTVKTLVMGGEPMLPND-ISLWKDKLRLVCAYGPAEctVVSTVqs 523
Cdd:cd17630    77 -ALAEDLAPPGVTHVSLVPTqlqrlLDSGQGPAALKSLRAVLLGGAPIPPELlERAADRGIPLYTTYGMTE--TASQV-- 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  524 CVQELGNIGRSPCGtcwivsKDNHHRLMPVGCIGELIIGGPIVGRGYLKQPCLTANAfitNPEWaslFHlngsyrfykTG 603
Cdd:cd17630   152 ATKRPDGFGRGGVG------VLLPGRELRIVEDGEIWVGGASLAMGYLRGQLVPEFN---EDGW---FT---------TK 210

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  604 DLVRYNADGTIAYIGRKDTQVKLNGQRVELGEIEH--QAQPYFRDAVIAAEVAAPAGRKPILIlfiarkyeYSVNMDctm 681
Cdd:cd17630   211 DLGELHADGRLTVLGRADNMIISGGENIQPEEIEAalAAHPAVRDAFVVGVPDEELGQRPVAV--------IVGRGP--- 279

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 992230864  682 llRPPSILfqekaqgtNTLLQEVLPRHMIPAAYIELLAMPISRTGKVNRKLLRE 735
Cdd:cd17630   280 --ADPAEL--------RAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRA 323
Cyc_NRPS cd19535
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
 1583-1865 2.34e-12

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: 71.37  E-value: 2.34e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1583 VSPVRLCNAWFTLARRHPALRTHLIDiplcDGMSSKIHVVHKDYMA--DAAILSCED-EHVITELRKpflpsdtglYYPH 1659
Cdd:cd19535    37 LDPDRLERAWNKLIARHPMLRAVFLD----DGTQQILPEVPWYGITvhDLRGLSEEEaEAALEELRE---------RLSH 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1660 afRICQTVSGRVF----CKLEGGHAFL---------DATSVLIILRELAQAY---DGQLSSVPgPSYSSAVAWLQSLPNG 1723
Cdd:cd19535   104 --RVLDVERGPLFdirlSLLPEGRTRLhlsidllvaDALSLQILLRELAALYedpGEPLPPLE-LSFRDYLLAEQALRET 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1724 DNR--MDYWRRQLKDaspciFPrlrdqDSPSDTLVV-TEQLAST------ATLTP--------VCTRHGLTVSNVLQVAW 1786
Cdd:cd19535   181 AYEraRAYWQERLPT-----LP-----PAPQLPLAKdPEEIKEPrftrreHRLSAeqwqrlkeRARQHGVTPSMVLLTAY 250

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1787 GLMLRRYTESDDVCFGALISGRDSRIPDVDKMVGPFFNVLVCQLRFGREDSLWDVLRRNQTEIGNRLlnQHCSL--IEVL 1864
Cdd:cd19535   251 AEVLARWSGQPRFLLNLTLFNRLPLHPDVNDVVGDFTSLLLLEVDGSEGQSFLERARRLQQQLWEDL--DHSSYsgVVVV 328


                  .
gi 992230864 1865 R 1865
Cdd:cd19535   329 R 329
PRK12316 PRK12316
peptide synthase; Provisional
 1357-1822 3.03e-12

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 72.68  E-value: 3.03e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1357 LISSLGQSLPRSAVPSLCLPVSFIPVDPLGQPDRIYLCEAASSmtlDFLHSLTDPVNKYidyhilpeEARLRGIVAHVLS 1436
Cdd:PRK12316  964 LKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKALPAPEAS---VAQQGYVAPRNAL--------ERTLAAIWQDVLG 1032

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1437 IDPqnISPKDDFFTLGGDSISAMQVVSLCRKHQLSLTALDIFNGRTIE---LIATR-------------LMPLTPytpps 1500
Cdd:PRK12316 1033 VER--VGLDDNFFELGGDSIVSIQVVSRARQAGIQLSPRDLFQHQTIRslaLVAKAgqataadqgpasgEVALAP----- 1105

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1501 tpasdrsLDRRFsllflnsdrdmerlesllmatydigsmdsIEDAYPcseSHQGLLQTQMLRPfyyqsytiwevttrskS 1580
Cdd:PRK12316 1106 -------VQRWF-----------------------------FEQAIP---QRQHWNQSLLLQA----------------R 1130

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1581 SPVSPVRLCNAWFTLARRHPALRTHLIDIplcDGMSSKIH-------VVHKDYMADAAILS--CEDEHVITELRK-PFLP 1650
Cdd:PRK12316 1131 QPLDPDRLGRALERLVAHHDALRLRFREE---DGGWQQAYaapqageVLWQRQAASEEELLalCEEAQRSLDLEQgPLLR 1207

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1651 SdtglyyphafRICQTVSGRVFCKLEGGHAFLDATSVLIILRELAQAYDGQLSSVPGPSySSAVAWLQSL----PNGDNR 1726
Cdd:PRK12316 1208 A----------LLVDMADGSQRLLLVIHHLVVDGVSWRILLEDLQRAYADLDADLPART-SSYQAWARRLhehaGARAEE 1276

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1727 MDYWRRQLKDAS---PCIFPRLRDQDSPSDTLVVT---EQLASTATLTPVCTRhgLTVSNVLQVAWGLMLRRYTESDDVC 1800
Cdd:PRK12316 1277 LDYWQAQLEDAPhelPCENPDGALENRHERKLELRldaERTRQLLQEAPAAYR--TQVNDLLLTALARVTCRWSGQASVL 1354

                         490       500
                  ....*....|....*....|....
gi 992230864 1801 FGALISGRDSRIPDVD--KMVGPF 1822
Cdd:PRK12316 1355 VQLEGHGREDLFEDIDlsRTVGWF 1378
PRK07768 PRK07768
long-chain-fatty-acid--CoA ligase; Validated
 258-641 3.10e-12

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


Pssm-ID: 236091 [Multi-domain]  Cd Length: 545  Bit Score: 71.57  E-value: 3.10e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  258 ITYRQLDRLSSTVQGLLQQYDLGPGSVVPIIFKKSKWAIVAMLGVLKAGAAFCMLDQsyPTKRL---------VNICKDV 328
Cdd:PRK07768   30 HTWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGASLTMLHQ--PTPRTdlavwaedtLRVIGMI 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  329 DAKVIVCSQ------ELSIGVSGSTLSIGDHNTETAtysaIQAVNTASHDAAYVVYTSGSTGAPKGIVIEHGSFCTNAIA 402
Cdd:PRK07768  108 GAKAVVVGEpflaaaPVLEEKGIRVLTVADLLAADP----IDPVETGEDDLALMQLTSGSTGSPKAVQITHGNLYANAEA 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  403 SSQAqnldrssrvlqfASYAFDVSVHESLTPLL----LGGCVCIP----SEAQRVNSLKEAVSTLRvnWVEL------TP 468
Cdd:PRK07768  184 MFVA------------AEFDVETDVMVSWLPLFhdmgMVGFLTVPmyfgAELVKVTPMDFLRDPLL--WAELiskyrgTM 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  469 TVA----------RLWCPA-----DIPTVKTLVMGGEPMLPNDISLWKD-----KLR---LVCAYGPAECT--------- 516
Cdd:PRK07768  250 TAApnfayallarRLRRQAkpgafDLSSLRFALNGAEPIDPADVEDLLDagarfGLRpeaILPAYGMAEATlavsfspcg 329

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  517 ---VVSTVqsCVQELGNIGRS-PcgtcwiVSKDNHHRLMPVG---------------------CIGELIIGGPIVGRGYl 571
Cdd:PRK07768  330 aglVVDEV--DADLLAALRRAvP------ATKGNTRRLATLGpplpglevrvvdedgqvlpprGVGVIELRGESVTPGY- 400

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  572 kqpcLTANAFITnpewaslfhLNGSYRFYKTGDLVRYNADGTIAYIGRKDTQVKLNGQRVELGEIEHQAQ 641
Cdd:PRK07768  401 ----LTMDGFIP---------AQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERAAA 457
LC_FACL_like cd05914
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ...
 257-637 4.43e-12

Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341240 [Multi-domain]  Cd Length: 463  Bit Score: 70.55  E-value: 4.43e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  257 TITYRQLDRLSSTVQGLLQQYDLGPGSVVPIIFKKSKWAIVAMLGVLKAGAAFCMLDQSYPTKRLVNICKDVDAKVIVCS 336
Cdd:cd05914     7 PLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFVS 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  337 QElsigvsgstlsigdhntetatysaiqavntasHDAAYVVYTSGSTGAPKGIVIEHGSFCTNAIASSQAQNLDRSSRVL 416
Cdd:cd05914    87 DE--------------------------------DDVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVLLGKGDKIL 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  417 QFASYA------FDVsvhesLTPLLLGGCVC----IPSEaqRVNSLKEAVSTLR----VNWV-------ELTPTVAR--- 472
Cdd:cd05914   135 SILPLHhiypltFTL-----LLPLLNGAHVVfldkIPSA--KIIALAFAQVTPTlgvpVPLViekifkmDIIPKLTLkkf 207

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  473 LWCPADIPTV-------------------KTLVMGGEPMLPN-DISLWKDKLRLVCAYGPAECT-VVSTVQSCVQELGNI 531
Cdd:cd05914   208 KFKLAKKINNrkirklafkkvheafggniKEFVIGGAKINPDvEEFLRTIGFPYTIGYGMTETApIISYSPPNRIRLGSA 287

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  532 GRSPCGTCWIVSKDNhhrlmPVGCIGELIIGGPIVGRGYLKQPCLTANAFITNpEWaslFHlngsyrfykTGDLVRYNAD 611
Cdd:cd05914   288 GKVIDGVEVRIDSPD-----PATGEGEIIVRGPNVMKGYYKNPEATAEAFDKD-GW---FH---------TGDLGKIDAE 349

                         410       420
                  ....*....|....*....|....*..
gi 992230864  612 GTIAYIGRKDTQVKL-NGQRVELGEIE 637
Cdd:cd05914   350 GYLYIRGRKKEMIVLsSGKNIYPEEIE 376
COG4908 COG4908
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ...
 878-1055 1.04e-11

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


Pssm-ID: 443936 [Multi-domain]  Cd Length: 243  Bit Score: 66.99  E-value: 1.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  878 TPLQEALMAYtSKRPGAFQAQFRFQLPHQLDMLRLKEAWRIVIAANPILRTRIVFCHTGALQVVLrPGEQLQWDLINGVH 957
Cdd:COG4908     2 SPAQKRFLFL-EPGSNAYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFVEEDGEPVQRID-PDADLPLEVVDLSA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  958 TSPGSLMSYGVPLVDMAITND---TAGKLSR-----------TFCLTMHHAIFDGWSYGLILGAVEDAYkhTNAVQ---- 1019
Cdd:COG4908    80 LPEPEREAELEELVAEEASRPfdlARGPLLRaalirlgedehVLLLTIHHIISDGWSLGILLRELAALY--AALLEgepp 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 992230864 1020 ------RPFAPFI----KYILHCNYESAKHFWCSEFKDM-QALPFPV 1055
Cdd:COG4908   158 plpelpIQYADYAawqrAWLQSEALEKQLEYWRQQLAGApPVLELPT 204
FACL_like_1 cd05910
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 257-624 1.27e-11

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


Pssm-ID: 341236 [Multi-domain]  Cd Length: 457  Bit Score: 69.03  E-value: 1.27e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  257 TITYRQLDRLSSTVQGLLQQYDLGPGSVVPIIFKKSKWAIVAMLGVLKAGAAFCMLDQSYPTKRLVNICKDVDAKVIvcs 336
Cdd:cd05910     2 RLSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQEAEPDAF--- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  337 qelsIGVsgstlsigdhntetatysaiqavnTASHDAAYVVYTSGSTGAPKGIVIEHGSFCTNAIASSQAQNLDRSSRVL 416
Cdd:cd05910    79 ----IGI------------------------PKADEPAAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPGEVDL 130

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  417 Q-FASYA-FDVsvhesltplLLGGCVCIP----SEAQRVN--SLKEAVSTLRVNWVELTP----TVARlWCPAD---IPT 481
Cdd:cd05910   131 AtFPLFAlFGP---------ALGLTSVIPdmdpTRPARADpqKLVGAIRQYGVSIVFGSPalleRVAR-YCAQHgitLPS 200

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  482 VKTLVMGGEPMLPNDIS----LWKDKLRLVCAYGPAECTVVSTVQScvQELGNIGRSPC----GTC-------------- 539
Cdd:cd05910   201 LRRVLSAGAPVPIALAArlrkMLSDEAEILTPYGATEALPVSSIGS--RELLATTTAATsggaGTCvgrpipgvrvriie 278

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  540 ----WIVSKDNHHRLmPVGCIGELIIGGPIVGRGYLKQPCLTANAFITNPewaslfhlngSYRF-YKTGDLVRYNADGTI 614
Cdd:cd05910   279 iddePIAEWDDTLEL-PRGEIGEITVTGPTVTPTYVNRPVATALAKIDDN----------SEGFwHRMGDLGYLDDEGRL 347

                         410
                  ....*....|
gi 992230864  615 AYIGRKDTQV 624
Cdd:cd05910   348 WFCGRKAHRV 357
OSB_CoA_lg cd05912
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ...
 257-735 1.37e-11

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: 68.91  E-value: 1.37e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  257 TITYRQLDRLSSTVQGLLQQYDLGPGSVVPIIFKKSKWAIVAMLGVLKAGAAFCMLDQSYPTKRLVNICKDVDAKVivcs 336
Cdd:cd05912     1 SYTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVKL---- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  337 qelsigvsgstlsigdhntetatysaiqavntasHDAAYVVYTSGSTGAPKGIVIEHGSFCTNAIASSQAQNLDRSSRVL 416
Cdd:cd05912    77 ----------------------------------DDIATIMYTSGTTGKPKGVQQTFGNHWWSAIGSALNLGLTEDDNWL 122

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  417 qFASYAFDVSVHESLTPLLLGGCVCIPSEAQRVNSLKEAVSTLRVNWVELTPT-VARL------WCPadiPTVKTLVMGG 489
Cdd:cd05912   123 -CALPLFHISGLSILMRSVIYGMTVYLVDKFDAEQVLHLINSGKVTIISVVPTmLQRLleilgeGYP---NNLRCILLGG 198

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  490 EPMLPNDISLWKDK-LRLVCAYGPAE-CTVVSTV--QSCVQELGNIGRsPCGTCWIVSKDNhhrLMPVGCIGELIIGGPI 565
Cdd:cd05912   199 GPAPKPLLEQCKEKgIPVYQSYGMTEtCSQIVTLspEDALNKIGSAGK-PLFPVELKIEDD---GQPPYEVGEILLKGPN 274

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  566 VGRGYLKQPCLTANAFITNpeWaslfhlngsyrfYKTGDLVRYNADGTIAYIGRKDTQVKLNGQRVELGEIEH--QAQPY 643
Cdd:cd05912   275 VTKGYLNRPDATEESFENG--W------------FKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEvlLSHPA 340

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  644 FRDAVIAAEVAAPAGRKPilILFIARKYEYSvnmdctmllrppsilfQEKAQgtnTLLQEVLPRHMIPAAYIELLAMPIS 723
Cdd:cd05912   341 IKEAGVVGIPDDKWGQVP--VAFVVSERPIS----------------EEELI---AYCSEKLAKYKVPKKIYFVDELPRT 399

                         490
                  ....*....|..
gi 992230864  724 RTGKVNRKLLRE 735
Cdd:cd05912   400 ASGKLLRHELKQ 411
PRK07788 PRK07788
acyl-CoA synthetase; Validated
 246-411 1.46e-11

acyl-CoA synthetase; Validated


Pssm-ID: 236097 [Multi-domain]  Cd Length: 549  Bit Score: 69.19  E-value: 1.46e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  246 PDAQAICAWDGTITYRQLDRLSSTVQGLLQQYDLGPGSVVPIIFKKSKWAIVAMLGVLKAGAAFCMLDQSYPTKRLVNIC 325
Cdd:PRK07788   63 PDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGPQLAEVA 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  326 KDVDAKVIVCSQE---------------LSIGVSGSTLSIGDHNTET-----ATYSAIQAVNTASHdAAYVVYTSGSTGA 385
Cdd:PRK07788  143 AREGVKALVYDDEftdllsalppdlgrlRAWGGNPDDDEPSGSTDETlddliAGSSTAPLPKPPKP-GGIVILTSGTTGT 221

                         170       180
                  ....*....|....*....|....*.
gi 992230864  386 PKGIVIEHGSfctnaIASSQAQNLDR 411
Cdd:PRK07788  222 PKGAPRPEPS-----PLAPLAGLLSR 242
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
 987-1272 3.22e-11

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: 69.12  E-value: 3.22e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  987 FCLTMHHAIFDGWSYGLIL--GAVEDAYKHTNAVQRPFAPFIKYILHCNY----------ESAKHFWCSEFKDMQALPFP 1054
Cdd:COG1020   145 LLLALHHIISDGLSDGLLLaeLLRLYLAAYAGAPLPLPPLPIQYADYALWqrewlqgeelARQLAYWRQQLAGLPPLLEL 224

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1055 VPPLSRGHMANSSTTTHRQI---HVSEWLSSYC-----TPSTIIQLAFTLLIAWRTESMDVLFGLTVTGRNAPvaGIHRT 1126
Cdd:COG1020   225 PTDRPRPAVQSYRGARVSFRlpaELTAALRALArrhgvTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPRP--ELEGL 302

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1127 TGPTIATFPLRTILYGTMNITDALLCMQNHIATL-----IPFEHtgLRRIKSFGTETARACQFQSLLIIQ--PVTYRESS 1199
Cdd:COG1020   303 VGFFVNTLPLRVDLSGDPSFAELLARVRETLLAAyahqdLPFER--LVEELQPERDLSRNPLFQVMFVLQnaPADELELP 380

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 992230864 1200 EIFFELESNEHEQSKFstcPLTLVCELRTHSVSVKAISDNAVVISGDMERLLDQLEYLIDMITKSPTLEIQNI 1272
Cdd:COG1020   381 GLTLEPLELDSGTAKF---DLTLTVVETGDGLRLTLEYNTDLFDAATIERMAGHLVTLLEALAADPDQPLGDL 450
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
 1425-1484 3.39e-11

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: 60.27  E-value: 3.39e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 992230864  1425 ARLRGIVAHVLSIDPQNISPKDDFFTLGGDSISAMQVVS-LCRKHQLSLTALDIFNGRTIE 1484
Cdd:pfam00550    1 ERLRELLAEVLGVPAEEIDPDTDLFDLGLDSLLAVELIArLEEEFGVEIPPSDLFEHPTLA 61
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
 760-829 3.56e-11

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: 60.64  E-value: 3.56e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 992230864  760 PSTPVLDQLRLLFSAALRIPEEKIKPNDSFFH-LGGDSVSAIRLVGDARDQ-GLHITVESLFKRQTISKLAE 829
Cdd:COG0236     2 PREELEERLAEIIAEVLGVDPEEITPDDSFFEdLGLDSLDAVELIAALEEEfGIELPDTELFEYPTVADLAD 73
AcpA COG3433
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ...
 1424-1490 4.23e-11

Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442659 [Multi-domain]  Cd Length: 295  Bit Score: 65.93  E-value: 4.23e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 992230864 1424 EARLRGIVAHVLSIDPQNISPKDDFFTLGGDSISAMQVVSLCRKHQLSLTALDIFNGRTIELIATRL 1490
Cdd:COG3433   221 EEELRADVAELLGVDPEEIDPDDNLFDLGLDSIRLMQLVERWRKAGLDVSFADLAEHPTLAAWWALL 287
PRK07529 PRK07529
AMP-binding domain protein; Validated
 350-621 4.28e-11

AMP-binding domain protein; Validated


Pssm-ID: 236043 [Multi-domain]  Cd Length: 632  Bit Score: 68.06  E-value: 4.28e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  350 IGDHNTETATYSAIQAV---NTASHDAAYVVYTSGSTGAPKGIVIEHGSFCTNAIASSQAQNLDrSSRVLQFASYAFDV- 425
Cdd:PRK07529  189 ILDFDAELARQPGDRLFsgrPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVANAWLGALLLGLG-PGDTVFCGLPLFHVn 267

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  426 -SVHESLTPLLLGGCVCIPSEA-----QRVNSLKEAVSTLRVNWVELTPTV--ARLWCP---ADIPTVKTLVMGGEPMLP 494
Cdd:PRK07529  268 aLLVTGLAPLARGAHVVLATPQgyrgpGVIANFWKIVERYRINFLSGVPTVyaALLQVPvdgHDISSLRYALCGAAPLPV 347

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  495 NDISLWKDK--LRLVCAYGPAECTVVSTVQSCVQE--LGNIG-RSPCGTCWIVSKDNHHRLM---PVGCIGELIIGGPIV 566
Cdd:PRK07529  348 EVFRRFEAAtgVRIVEGYGLTEATCVSSVNPPDGErrIGSVGlRLPYQRVRVVILDDAGRYLrdcAVDEVGVLCIAGPNV 427

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 992230864  567 GRGYLKQpclTANAFItnpeWASLFHLNgsyrfykTGDLVRYNADGTIAYIGR-KD 621
Cdd:PRK07529  428 FSGYLEA---AHNKGL----WLEDGWLN-------TGDLGRIDADGYFWLTGRaKD 469
MACS_euk cd05928
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ...
 366-735 4.98e-11

Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.


Pssm-ID: 341251 [Multi-domain]  Cd Length: 530  Bit Score: 67.49  E-value: 4.98e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  366 VNTASHDAAYVVYTSGSTGAPKGIVIEHGSFCTNAIASSQA-QNLDRSSRVLQFASYAFDVSVHESL-TPLLLGGCVCIP 443
Cdd:cd05928   169 VETGSQEPMAIYFTSGTTGSPKMAEHSHSSLGLGLKVNGRYwLDLTASDIMWNTSDTGWIKSAWSSLfEPWIQGACVFVH 248

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  444 SEAQ-RVNSLKEAVSTLRVNWVELTPTVARLWCPADI-----PTVKTLVMGGEPMLPNDISLWKDK--LRLVCAYGPAEC 515
Cdd:cd05928   249 HLPRfDPLVILKTLSSYPITTFCGAPTVYRMLVQQDLssykfPSLQHCVTGGEPLNPEVLEKWKAQtgLDIYEGYGQTET 328

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  516 TVVSTVQSCVQ-ELGNIGR-SPCGTCWIVskDNHHRLMPVGCIGELIIggpivgRGYLKQPCLTANAFITNPE-WASLFH 592
Cdd:cd05928   329 GLICANFKGMKiKPGSMGKaSPPYDVQII--DDNGNVLPPGTEGDIGI------RVKPIRPFGLFSGYVDNPEkTAATIR 400

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  593 LNgsyrFYKTGDLVRYNADGTIAYIGRKDTQVKLNGQR-----VELGEIEHQAqpyfrdAVIAAEVAAPAG-RKPILILF 666
Cdd:cd05928   401 GD----FYLTGDRGIMDEDGYFWFMGRADDVINSSGYRigpfeVESALIEHPA------VVESAVVSSPDPiRGEVVKAF 470

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 992230864  667 IARKYEYsvnmdctmLLRPPSILFQEkaqgtntlLQEVLPRHMIPAAY---IELLA-MPISRTGKVNRKLLRE 735
Cdd:cd05928   471 VVLAPQF--------LSHDPEQLTKE--------LQQHVKSVTAPYKYprkVEFVQeLPKTVTGKIQRNELRD 527
PRK12583 PRK12583
acyl-CoA synthetase; Provisional
 356-637 5.41e-11

acyl-CoA synthetase; Provisional


Pssm-ID: 237145 [Multi-domain]  Cd Length: 558  Bit Score: 67.49  E-value: 5.41e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  356 ETATYSAIQAVNTA--SHDAAYVVYTSGSTGAPKGIVIEHGSFCTNAIASSQAQNLDRSSR-VLQFASYAFDVSVHESLT 432
Cdd:PRK12583  184 ETVSREALAERQASldRDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRlCVPVPLYHCFGMVLANLG 263

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  433 PLLLGGCVCIPSEAQRVNSLKEAVSTLRVNWVELTPT--VARLWCPA----DIPTVKTLVMGGEPMLPNDISLWKDKLRL 506
Cdd:PRK12583  264 CMTVGACLVYPNEAFDPLATLQAVEEERCTALYGVPTmfIAELDHPQrgnfDLSSLRTGIMAGAPCPIEVMRRVMDEMHM 343

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  507 ---VCAYGPAECTVVSTvQSCVQE-----LGNIGRS-PCGTCWIVskDNHHRLMPVGCIGELIIGGPIVGRGYLKQPCLT 577
Cdd:PRK12583  344 aevQIAYGMTETSPVSL-QTTAADdlerrVETVGRTqPHLEVKVV--DPDGATVPRGEIGELCTRGYSVMKGYWNNPEAT 420

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  578 ANAfITNPEWaslFHlngsyrfykTGDLVRYNADGTIAYIGRKDTQVKLNGQRVELGEIE 637
Cdd:PRK12583  421 AES-IDEDGW---MH---------TGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIE 467
FACL_like_4 cd05944
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 372-734 7.30e-11

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


Pssm-ID: 341266 [Multi-domain]  Cd Length: 359  Bit Score: 65.96  E-value: 7.30e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  372 DAAYVVYTSGSTGAPKgiVIEHGSFCTNAIASSQAQNLDRSSR-VLQFASYAFDV--SVHESLTPLLLGGCVCIPSEA-- 446
Cdd:cd05944     3 DVAAYFHTGGTTGTPK--LAQHTHSNEVYNAWMLALNSLFDPDdVLLCGLPLFHVngSVVTLLTPLASGAHVVLAGPAgy 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  447 ---QRVNSLKEAVSTLRVNWVELTPTV--ARLWCP--ADIPTVKTLVMGGEPMLPNDISLWKDK--LRLVCAYGPAECTV 517
Cdd:cd05944    81 rnpGLFDNFWKLVERYRITSLSTVPTVyaALLQVPvnADISSLRFAMSGAAPLPVELRARFEDAtgLPVVEGYGLTEATC 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  518 VSTVQ--SCVQELGNIG-RSPCGTCWIVSKD---NHHRLMPVGCIGELIIGGPIVGRGYLKQPcLTANAFITNpewaslf 591
Cdd:cd05944   161 LVAVNppDGPKRPGSVGlRLPYARVRIKVLDgvgRLLRDCAPDEVGEICVAGPGVFGGYLYTE-GNKNAFVAD------- 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  592 hlngsyRFYKTGDLVRYNADGTIAYIGRKDTQVKLNGQRVELGEIEH--QAQPyfrdAV-IAAEVAAP---AGRKPILIL 665
Cdd:cd05944   233 ------GWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEalLRHP----AVaFAGAVGQPdahAGELPVAYV 302

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 992230864  666 FIARKYEYSVnmdcTMLLRPPSILFQEKAqgtntllqeVLPRHMIPaayieLLAMPISRTGKVNRKLLR 734
Cdd:cd05944   303 QLKPGAVVEE----EELLAWARDHVPERA---------AVPKHIEV-----LEELPVTAVGKVFKPALR 353
PRK12492 PRK12492
long-chain-fatty-acid--CoA ligase; Provisional
 221-735 7.42e-11

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


Pssm-ID: 171539 [Multi-domain]  Cd Length: 562  Bit Score: 67.15  E-value: 7.42e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  221 WNRNAP--------IHPFDSCIHtLFRLQCILQPDAQAICAWDGTITYRQLDRLSSTVQGLLQQY-DLGPGSVVPIIFKK 291
Cdd:PRK12492    6 WNDKRPagvpstidLAAYKSVVE-VFERSCKKFADRPAFSNLGVTLSYAELERHSAAFAAYLQQHtDLVPGDRIAVQMPN 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  292 SKWAIVAMLGVLKAGAAFCMLDQSYPTKRLVNICKDVDAKVIV-------CSQELSIGVSGSTL---SIGD--------- 352
Cdd:PRK12492   85 VLQYPIAVFGALRAGLIVVNTNPLYTAREMRHQFKDSGARALVylnmfgkLVQEVLPDTGIEYLieaKMGDllpaakgwl 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  353 ---------------HNTETATY---------SAIQAVNTASHDAAYVVYTSGSTGAPKGIVIEHGSFCTNAIA------ 402
Cdd:PRK12492  165 vntvvdkvkkmvpayHLPQAVPFkqalrqgrgLSLKPVPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVANMLQvracls 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  403 --SSQAQNLDRSSRVLQFAS------YAFDVSV--------HESL--TPLLLGGCVcipSEAQRVN-SLKEAVSTLRVNW 463
Cdd:PRK12492  245 qlGPDGQPLMKEGQEVMIAPlplyhiYAFTANCmcmmvsgnHNVLitNPRDIPGFI---KELGKWRfSALLGLNTLFVAL 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  464 VElTPTVARLwcpaDIPTVKTLVMGGEPMLPNDISLWKD--KLRLVCAYGPAECTVVSTVQSCVQ--ELGNIGRSPCGTC 539
Cdd:PRK12492  322 MD-HPGFKDL----DFSALKLTNSGGTALVKATAERWEQltGCTIVEGYGLTETSPVASTNPYGElaRLGTVGIPVPGTA 396

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  540 WIVSKDNHHRLmPVGCIGELIIGGPIVGRGYLKQPCLTANAfITNPEWaslfhlngsyrfYKTGDLVRYNADGTIAYIGR 619
Cdd:PRK12492  397 LKVIDDDGNEL-PLGERGELCIKGPQVMKGYWQQPEATAEA-LDAEGW------------FKTGDIAVIDPDGFVRIVDR 462

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  620 KDTQVKLNGQRVELGEIEHQAQPYFRDAVIAAeVAAPAGRK-PILILFIarkyeysvnmdctmLLRPPSILFQE-KAQGT 697
Cdd:PRK12492  463 KKDLIIVSGFNVYPNEIEDVVMAHPKVANCAA-IGVPDERSgEAVKLFV--------------VARDPGLSVEElKAYCK 527

                         570       580       590
                  ....*....|....*....|....*....|....*...
gi 992230864  698 NTLLQEVLPRHMIPAAyiellAMPISRTGKVNRKLLRE 735
Cdd:PRK12492  528 ENFTGYKVPKHIVLRD-----SLPMTPVGKILRRELRD 560
PRK07769 PRK07769
long-chain-fatty-acid--CoA ligase; Validated
 258-661 9.56e-11

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


Pssm-ID: 181109 [Multi-domain]  Cd Length: 631  Bit Score: 67.06  E-value: 9.56e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  258 ITYRQLDRLSSTVQGLLQQYDlGPGSVVPIIFKKSKWAIVAMLGVLKAGA-AFCMLDQSYP--TKRLVNICKDVDAKVIV 334
Cdd:PRK07769   56 LTWSQFGARNRAVGARLQQVT-KPGDRVAILAPQNLDYLIAFFGALYAGRiAVPLFDPAEPghVGRLHAVLDDCTPSAIL 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  335 CSQELSIGVSG--STLSIGDH----------NTETATYsaiQAVNTASHDAAYVVYTSGSTGAPKGIVIEHGSFCTNAIA 402
Cdd:PRK07769  135 TTTDSAEGVRKffRARPAKERprviavdavpDEVGATW---VPPEANEDTIAYLQYTSGSTRIPAGVQITHLNLPTNVLQ 211

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  403 SSQAQNLDRSSRVLQFASYAFDVSVHESLTPLLLGGCVCIPSEAQRVNS----LKE--AVSTLRVNWVELTPTVARLWC- 475
Cdd:PRK07769  212 VIDALEGQEGDRGVSWLPFFHDMGLITVLLPALLGHYITFMSPAAFVRRpgrwIRElaRKPGGTGGTFSAAPNFAFEHAa 291

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  476 ----------PADIPTVKTLVMGGEPMLPNDISLWKD--------KLRLVCAYGPAECTV-VSTVQSCVQ---------E 527
Cdd:PRK07769  292 arglpkdgepPLDLSNVKGLLNGSEPVSPASMRKFNEafapyglpPTAIKPSYGMAEATLfVSTTPMDEEptviyvdrdE 371

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  528 LGNiGR-------SP-------CGTC----W--IVSKDNHHRLmPVGCIGELIIGGPIVGRGYLKQPCLTANAF---ITN 584
Cdd:PRK07769  372 LNA-GRfvevpadAPnavaqvsAGKVgvseWavIVDPETASEL-PDGQIGEIWLHGNNIGTGYWGKPEETAATFqniLKS 449

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  585 PEWASlfHLNGS---YRFYKTGDLVRYnADGTIAYIGRKDTQVKLNGQRVELGEIEHQAQ---PYFRDAVIAAeVAAPAG 658
Cdd:PRK07769  450 RLSES--HAEGApddALWVRTGDYGVY-FDGELYITGRVKDLVIIDGRNHYPQDLEYTAQeatKALRTGYVAA-FSVPAN 525


                  ...
gi 992230864  659 RKP 661
Cdd:PRK07769  526 QLP 528
AcpA COG3433
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ...
 552-829 1.05e-10

Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 442659 [Multi-domain]  Cd Length: 295  Bit Score: 64.77  E-value: 1.05e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  552 PVGCIGELIIGGPIVGRGYLKQPCLTANAFITNPEWaslfhlngSYRFYKTGDLVRYNADGTIAYIGRKDTQVKlnGQRV 631
Cdd:COG3433    42 GFGGEGGLLGAGLLLRIRLLAAAARAPFIPVPYPAQ--------PGRQADDLRLLLRRGLGPGGGLERLVQQVV--IRAE 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  632 ELGEIEHQAQPYFRDAVIAAEVAAPAGRKPILILFIArkyeYSVNMDCTMllrppsilfqekaqgTNTLLQEVLPRHMIP 711
Cdd:COG3433   112 RGEEEELLLVLRAAAVVRVAVLAALRGAGVGLLLIVG----AVAALDGLA---------------AAAALAALDKVPPDV 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  712 AAYIELLAMPISRTGKVNRKLLREAVEQAsEKDFRAYYPITHNDmiqlPSTPVLDQLRLLFSAALRIPEEKIKPNDSFFH 791
Cdd:COG3433   173 VAASAVVALDALLLLALKVVARAAPALAA-AEALLAAASPAPAL----ETALTEEELRADVAELLGVDPEEIDPDDNLFD 247

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 992230864  792 LGGDSVSAIRLVGDARDQGLHITVESLFKRQTISKLAE 829
Cdd:COG3433   248 LGLDSIRLMQLVERWRKAGLDVSFADLAEHPTLAAWWA 285
E-C_NRPS cd19544
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); ...
 874-1168 1.20e-10

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: 65.92  E-value: 1.20e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  874 IYPCTPLQEA-----LMA-----YTSkrpgafQAQFRFQLPHQLDmlRLKEAWRIVIAANPILRTRIVfcHTG---ALQV 940
Cdd:cd19544     1 IYPLAPLQEGilfhhLLAeegdpYLL------RSLLAFDSRARLD--AFLAALQQVIDRHDILRTAIL--WEGlsePVQV 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  941 VLR----PGEQLQWDLINGV------HTSPGSL-MSYGV-PLVDMAITNDTAGklSRTF-CLTMHHAIFDGWSYGLILGA 1007
Cdd:cd19544    71 VWRqaelPVEELTLDPGDDAlaqlraRFDPRRYrLDLRQaPLLRAHVAEDPAN--GRWLlLLLFHHLISDHTSLELLLEE 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1008 VEdAYKHTNAVQ----RPFAPFIKYILHCNYES-AKHFwcseFKDMQA------LPF-----------------PVPP-L 1058
Cdd:cd19544   149 IQ-AILAGRAAAlpppVPYRNFVAQARLGASQAeHEAF----FREMLGdvdeptAPFglldvqgdgsditearlALDAeL 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1059 S---RGHManssttthRQIHVSewlssyctPSTIIQLAFTLLIAWRTESMDVLFGlTV-TGRNAPVAGIHRTTGPTIATF 1134
Cdd:cd19544   224 AqrlRAQA--------RRLGVS--------PASLFHLAWALVLARCSGRDDVVFG-TVlSGRMQGGAGADRALGMFINTL 286

                         330       340       350
                  ....*....|....*....|....*....|....
gi 992230864 1135 PLRTILyGTMNITDALLCMQNHIATLIPFEHTGL 1168
Cdd:cd19544   287 PLRVRL-GGRSVREAVRQTHARLAELLRHEHASL 319
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
 1424-1490 1.37e-10

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: 59.10  E-value: 1.37e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 992230864 1424 EARLRGIVAHVLSIDPQNISPKDDFFT-LGGDSISAMQVVSLCRKH-QLSLTALDIFNGRTIELIATRL 1490
Cdd:COG0236     7 EERLAEIIAEVLGVDPEEITPDDSFFEdLGLDSLDAVELIAALEEEfGIELPDTELFEYPTVADLADYL 75
PRK08316 PRK08316
acyl-CoA synthetase; Validated
 245-654 1.51e-10

acyl-CoA synthetase; Validated


Pssm-ID: 181381 [Multi-domain]  Cd Length: 523  Bit Score: 66.11  E-value: 1.51e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  245 QPDAQAICAWDGTITYRQLDRLSSTVQGLLQQYDLGPGSVVPIIFKKSkWAIVAM-LGVLKAGA--------------AF 309
Cdd:PRK08316   24 YPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNS-DAYALLwLACARAGAvhvpvnfmltgeelAY 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  310 CmLDQSYPT-----KRLVNICKDVDAKVIVCSQELSIGVSGSTLSIGDHNTE---TATYSAIQAVNTASHDAAYVVYTSG 381
Cdd:PRK08316  103 I-LDHSGARaflvdPALAPTAEAALALLPVDTLILSLVLGGREAPGGWLDFAdwaEAGSVAEPDVELADDDLAQILYTSG 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  382 STGAPKGIVIEHGSFCTNAIASSQAQNLDRSSRVLQ----FASYAFDVsvheSLTPLLLGGCVCIPSEAQRVNSLKEAVS 457
Cdd:PRK08316  182 TESLPKGAMLTHRALIAEYVSCIVAGDMSADDIPLHalplYHCAQLDV----FLGPYLYVGATNVILDAPDPELILRTIE 257

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  458 TLRVNWVELTPTV--ARLWCP----ADIPTVKTLVMGGEPM-----------LPNdislwkdkLRLVCAYGPAECTVVST 520
Cdd:PRK08316  258 AERITSFFAPPTVwiSLLRHPdfdtRDLSSLRKGYYGASIMpvevlkelrerLPG--------LRFYNCYGQTEIAPLAT 329

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  521 VQSCVQELGNIGrsPCG------TCWIVskDNHHRLMPVGCIGELIIGGPIVGRGYLKQPCLTANAFITNpeWaslFHln 594
Cdd:PRK08316  330 VLGPEEHLRRPG--SAGrpvlnvETRVV--DDDGNDVAPGEVGEIVHRSPQLMLGYWDDPEKTAEAFRGG--W---FH-- 398

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  595 gsyrfykTGDLVRYNADGTIAYIGRKDTQVKLNGQRVELGEIEHQAqpYFRDAViaAEVA 654
Cdd:PRK08316  399 -------SGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEAL--YTHPAV--AEVA 447
SgcC5_NRPS-like cd19539
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ...
 876-1165 1.78e-10

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: 65.48  E-value: 1.78e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  876 PCTPLQEALMAYTSKRPG--AFQAQFRFQLPHQLDMLRLKEAWRIVIAANPILRTRIVFCHTG-ALQVVLRPG------- 945
Cdd:cd19539     3 PLSFAQERLWFIDQGEDGgpAYNIPGAWRLTGPLDVEALREALRDVVARHEALRTLLVRDDGGvPRQEILPPGpaplevr 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  946 ---------EQLQWDLINGVHTSPGSLmsYGVPLVDMAItndtaGKLSRT---FCLTMHHAIFDGWSYGLILGAVEDAYK 1013
Cdd:cd19539    83 dlsdpdsdrERRLEELLRERESRGFDL--DEEPPIRAVL-----GRFDPDdhvLVLVAHHTAFDAWSLDVFARDLAALYA 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1014 --HTNAVQRPFAPFIKYILHCNYES----------AKHFWCSEFKDMQALPFPvPPLSRGHMANSSTTTHRQIHVSEWLS 1081
Cdd:cd19539   156 arRKGPAAPLPELRQQYKEYAAWQRealaapraaeLLDFWRRRLRGAEPTALP-TDRPRPAGFPYPGADLRFELDAELVA 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1082 SY--------CTPSTIIQLAFTLLIAWRTESMDVLFGLTVTGRNAPvaGIHRTTGPTIATFPLRTILYGTMNITD----- 1148
Cdd:cd19539   235 ALrelakrarSSLFMVLLAAYCVLLRRYTGQTDIVVGTPVAGRNHP--RFESTVGFFVNLLPLRVDVSDCATFRDliarv 312

                         330
                  ....*....|....*....
gi 992230864 1149 --ALLCMQNHIAtlIPFEH 1165
Cdd:cd19539   313 rkALVDAQRHQE--LPFQQ 329
PLN02860 PLN02860
o-succinylbenzoate-CoA ligase
 241-637 2.33e-10

o-succinylbenzoate-CoA ligase


Pssm-ID: 215464 [Multi-domain]  Cd Length: 563  Bit Score: 65.59  E-value: 2.33e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  241 QCI-----LQPDAQAICAWDGTITYRQ-LDRLSSTVQGLLQqYDLGPGSVVPIIFKKSKWAIVAMLGVLKAG-------- 306
Cdd:PLN02860   11 QCLtrlatLRGNAVVTISGNRRRTGHEfVDGVLSLAAGLLR-LGLRNGDVVAIAALNSDLYLEWLLAVACAGgivaplny 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  307 ------AAFCML---------DQS---YPTKRLVNICKDVDAKVIVCSQELSIGVSGSTLSIGDHNTETATYSAIQAVNT 368
Cdd:PLN02860   90 rwsfeeAKSAMLlvrpvmlvtDETcssWYEELQNDRLPSLMWQVFLESPSSSVFIFLNSFLTTEMLKQRALGTTELDYAW 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  369 ASHDAAYVVYTSGSTGAPKGIVIEHGSFCTNAIASsqaqnldrssrvLQFASYA-FDVSVHES-----------LTPLLL 436
Cdd:PLN02860  170 APDDAVLICFTSGTTGRPKGVTISHSALIVQSLAK------------IAIVGYGeDDVYLHTAplchigglssaLAMLMV 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  437 GGC-VCIPS----------EAQRVNSLKeAVSTLRVNWVELTPTvARLWcpADIPTVKTLVMGGEPM---LPNDISLWKD 502
Cdd:PLN02860  238 GAChVLLPKfdakaalqaiKQHNVTSMI-TVPAMMADLISLTRK-SMTW--KVFPSVRKILNGGGSLssrLLPDAKKLFP 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  503 KLRLVCAYGPAE-CTVVS-------TVQSCVQELGNIGRS-------PCGTCwiVSKDNHHRLMPVGC-----IGELIIG 562
Cdd:PLN02860  314 NAKLFSAYGMTEaCSSLTfmtlhdpTLESPKQTLQTVNQTksssvhqPQGVC--VGKPAPHVELKIGLdessrVGRILTR 391

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 992230864  563 GPIVGRGYLKQPCLTANAfITNPEWASlfhlngsyrfykTGDLVRYNADGTIAYIGRKDTQVKLNGQRVELGEIE 637
Cdd:PLN02860  392 GPHVMLGYWGQNSETASV-LSNDGWLD------------TGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVE 453
PtmA cd17636
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ...
 372-649 2.84e-10

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: 63.86  E-value: 2.84e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  372 DAAYVVYTSGSTGAPKGIVIEHGSFCTNAIASSQAQNLDRSSRVLQfASYAFDVSV-HESLTPLLLGG-CVCIP-SEAQR 448
Cdd:cd17636     1 DPVLAIYTAAFSGRPNGALLSHQALLAQALVLAVLQAIDEGTVFLN-SGPLFHIGTlMFTLATFHAGGtNVFVRrVDAEE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  449 VNSLKEAVstlRVNWVELT-PTVA--------------RLWCPADIPtvktlvmGGEPMLPNDISLWKDKLRlvcAYGPA 513
Cdd:cd17636    80 VLELIEAE---RCTHAFLLpPTIDqivelnadglydlsSLRSSPAAP-------EWNDMATVDTSPWGRKPG---GYGQT 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  514 ECT-VVSTVQSCVQELGNIGR-SPCGTCWIVSKDNhhRLMPVGCIGELIIGGPIVGRGYLKQPCLtaNAFITNPEWaslf 591
Cdd:cd17636   147 EVMgLATFAALGGGAIGGAGRpSPLVQVRILDEDG--REVPDGEVGEIVARGPTVMAGYWNRPEV--NARRTRGGW---- 218

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 992230864  592 hlngsyrfYKTGDLVRYNADGTIAYIGRKDTQVKLNGQRVELGEIEH--QAQPYFRD-AVI 649
Cdd:cd17636   219 --------HHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERclRQHPAVADaAVI 271
PRK13390 PRK13390
acyl-CoA synthetase; Provisional
 246-638 5.14e-10

acyl-CoA synthetase; Provisional


Pssm-ID: 139538 [Multi-domain]  Cd Length: 501  Bit Score: 64.26  E-value: 5.14e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  246 PDAQA-ICAWDG-TITYRQLDRLSSTVQGLLQQYDLGPGSVVPIIFKKSKWAIVAMLGVLKAGAAFCMLDQSYPTKRLVN 323
Cdd:PRK13390   11 PDRPAvIVAETGeQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADY 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  324 ICKDVDAKVIVCSQELSiGVSGST-------LSIGDHNTETATYSAIQAVN----TASHDAAYVVYTSGSTGAPKGIVie 392
Cdd:PRK13390   91 IVGDSGARVLVASAALD-GLAAKVgadlplrLSFGGEIDGFGSFEAALAGAgprlTEQPCGAVMLYSSGTTGFPKGIQ-- 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  393 hgsfctnaiASSQAQNLDR-SSRVLQFASYAFDVS---VHESLTPLL-------------LGGCVCIPSEAQRVNSLKEa 455
Cdd:PRK13390  168 ---------PDLPGRDVDApGDPIVAIARAFYDISesdIYYSSAPIYhaaplrwcsmvhaLGGTVVLAKRFDAQATLGH- 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  456 VSTLRVNWVELTPTV--------ARLWCPADIPTVKTLVMGGEPmLPNDIslwkdKLRLVCAYGPA-----------ECT 516
Cdd:PRK13390  238 VERYRITVTQMVPTMfvrllkldADVRTRYDVSSLRAVIHAAAP-CPVDV-----KHAMIDWLGPIvyeyyssteahGMT 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  517 VVSTVQSCVQElGNIGRSPCGTCWIVSKDNHHrlMPVGCIGELIIGGPIVGRGYLKQPCLTANA-FITNPEWASLfhlng 595
Cdd:PRK13390  312 FIDSPDWLAHP-GSVGRSVLGDLHICDDDGNE--LPAGRIGTVYFERDRLPFRYLNDPEKTAAAqHPAHPFWTTV----- 383

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 992230864  596 syrfyktGDLVRYNADGTIAYIGRKDTQVKLNGQRVELGEIEH 638
Cdd:PRK13390  384 -------GDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETEN 419
PLN02574 PLN02574
4-coumarate--CoA ligase-like
 257-734 6.08e-10

4-coumarate--CoA ligase-like


Pssm-ID: 215312 [Multi-domain]  Cd Length: 560  Bit Score: 64.09  E-value: 6.08e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  257 TITYRQLDRL-SSTVQGLLQQYDLGPGSVVPIIFKKSKWAIVAMLGVLKAGA-AFCMLDQSYPTkrlvnickDVDAKVIV 334
Cdd:PLN02574   66 SISYSELQPLvKSMAAGLYHVMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGiVTTMNPSSSLG--------EIKKRVVD 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  335 CSQELS-----------------IGVSGStlsiGDHNTETATYSAIQAVNTAS-----------HDAAYVVYTSGSTGAP 386
Cdd:PLN02574  138 CSVGLAftspenveklsplgvpvIGVPEN----YDFDSKRIEFPKFYELIKEDfdfvpkpvikqDDVAAIMYSSGTTGAS 213

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  387 KGIVIEHGSFCTNA-----IASSQAQNLDRSSRVL----QFASYAFDVSVheslTPLLLGGCVCIPSEAQRVNSLKEAVS 457
Cdd:PLN02574  214 KGVVLTHRNLIAMVelfvrFEASQYEYPGSDNVYLaalpMFHIYGLSLFV----VGLLSLGSTIVVMRRFDASDMVKVID 289

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  458 TLRVNWVELTPTV-------ARLWCPADIPTVKTLVMGGEPMLPNDISLWKDKL---RLVCAYGPAECTVVSTVQSCVQE 527
Cdd:PLN02574  290 RFKVTHFPVVPPIlmaltkkAKGVCGEVLKSLKQVSCGAAPLSGKFIQDFVQTLphvDFIQGYGMTESTAVGTRGFNTEK 369

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  528 LGN---IGR-SPCGTCWIVSKDNHHRLMPVGCiGELIIGGPIVGRGYLKQPCLTANAfITNPEWaslfhlngsyrfYKTG 603
Cdd:PLN02574  370 LSKyssVGLlAPNMQAKVVDWSTGCLLPPGNC-GELWIQGPGVMKGYLNNPKATQST-IDKDGW------------LRTG 435

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  604 DLVRYNADGTIAYIGRKDTQVKLNGQRVELGEIEHQ--AQPYFRDAVIAAEVAAPAGRKPilILFIARkyeysvnmdctm 681
Cdd:PLN02574  436 DIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVliSHPEIIDAAVTAVPDKECGEIP--VAFVVR------------ 501

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|...
gi 992230864  682 llRPPSILFQEkaQGTNTLLQEVLPRHMIPAAyIELLAMPISRTGKVNRKLLR 734
Cdd:PLN02574  502 --RQGSTLSQE--AVINYVAKQVAPYKKVRKV-VFVQSIPKSPAGKILRRELK 549
PRK07798 PRK07798
acyl-CoA synthetase; Validated
 246-661 6.80e-10

acyl-CoA synthetase; Validated


Pssm-ID: 236100 [Multi-domain]  Cd Length: 533  Bit Score: 63.75  E-value: 6.80e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  246 PDAQAICAWDGTITYRQLDRLSSTVQGLLQQYDLGPGSVVPIIFKKSKWAIVAMLGVLKAGAAFCMLDQSYPTKRLVNIC 325
Cdd:PRK07798   17 PDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELRYLL 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  326 KDVDAKVIVCSQELSIGV-------------------SGSTLSIGDHNTETA--TYSAIQAVNTASHDAAYVVYTSGSTG 384
Cdd:PRK07798   97 DDSDAVALVYEREFAPRVaevlprlpklrtlvvvedgSGNDLLPGAVDYEDAlaAGSPERDFGERSPDDLYLLYTGGTTG 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  385 APKGIVIEHGSF-----------CTNAIASSQAQnldrSSRVLQ-FASYAFDVS--VH-----ESLTPLLLGGCVCIPSE 445
Cdd:PRK07798  177 MPKGVMWRQEDIfrvllggrdfaTGEPIEDEEEL----AKRAAAgPGMRRFPAPplMHgagqwAAFAALFSGQTVVLLPD 252

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  446 AQ-RVNSLKEAVSTLRVNWVELT------PTVARLWC--PADIPTVKTLVMGGEPMLPNdislWKDKLR-------LVCA 509
Cdd:PRK07798  253 VRfDADEVWRTIEREKVNVITIVgdamarPLLDALEArgPYDLSSLFAIASGGALFSPS----VKEALLellpnvvLTDS 328

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  510 YGPAEC------TVVSTVQSCVQELGNIGRSPCgtcwiVSKDNHHRLMP-VGCIGELIIGGPIvGRGYLKQPCLTANAFI 582
Cdd:PRK07798  329 IGSSETgfggsgTVAKGAVHTGGPRFTIGPRTV-----VLDEDGNPVEPgSGEIGWIARRGHI-PLGYYKDPEKTAETFP 402

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  583 TnpewaslfhLNGSyRFYKTGDLVRYNADGTIAYIGRKDTQVKLNGQRVELGEIEH--QAQPYFRDAV------------ 648
Cdd:PRK07798  403 T---------IDGV-RYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEalKAHPDVADALvvgvpderwgqe 472

                         490
                  ....*....|...
gi 992230864  649 IAAEVAAPAGRKP 661
Cdd:PRK07798  473 VVAVVQLREGARP 485
PRK13295 PRK13295
cyclohexanecarboxylate-CoA ligase; Reviewed
 246-741 6.94e-10

cyclohexanecarboxylate-CoA ligase; Reviewed


Pssm-ID: 171961 [Multi-domain]  Cd Length: 547  Bit Score: 63.92  E-value: 6.94e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  246 PDAQAICAWDG------TITYRQLDRLSSTVQGLLQQYDLGPGSVVPIIFKKSkWAIVAM-LGVLKAGAAFCMLDQSYPT 318
Cdd:PRK13295   38 PDKTAVTAVRLgtgaprRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNW-WEFTVLyLACSRIGAVLNPLMPIFRE 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  319 KRLVNICKDVDAKVIVCSQE-----------------------LSIGVSGSTlSIGDHNTETA--TYSAIQAVNTASH-- 371
Cdd:PRK13295  117 RELSFMLKHAESKVLVVPKTfrgfdhaamarrlrpelpalrhvVVVGGDGAD-SFEALLITPAweQEPDAPAILARLRpg 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  372 --DAAYVVYTSGSTGAPKGIVIEHGSFCTNAIASSQAQNLDRSSRVLQFASYAFDVS-VHESLTPLLLGGCVCI-----P 443
Cdd:PRK13295  196 pdDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVILMASPMAHQTGfMYGLMMPVMLGATAVLqdiwdP 275

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  444 SEAQRVnslkeaVSTLRVNWV--------ELTPTVARLwcPADIPTVKTLVMGGEPMLPNDISLWKDKL--RLVCAYGPA 513
Cdd:PRK13295  276 ARAAEL------IRTEGVTFTmastpfltDLTRAVKES--GRPVSSLRTFLCAGAPIPGALVERARAALgaKIVSAWGMT 347

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  514 ECTVVSTVqscvqELGN-----IGRSPCGTCWIVSK--DNHHRLMPVGCIGELIIGGPIVGRGYLKQPCLTANAFitnpe 586
Cdd:PRK13295  348 ENGAVTLT-----KLDDpderaSTTDGCPLPGVEVRvvDADGAPLPAGQIGRLQVRGCSNFGGYLKRPQLNGTDA----- 417

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  587 waslfhlNGsyrFYKTGDLVRYNADGTIAYIGR-KDTQVKlNGQRVELGEIEhqaQPYFRDAVIA--AEVAAPAgrkpil 663
Cdd:PRK13295  418 -------DG---WFDTGDLARIDADGYIRISGRsKDVIIR-GGENIPVVEIE---ALLYRHPAIAqvAIVAYPD------ 477

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  664 ilfiARKYEYSvnmdCTML-LRP-PSILFQE-----KAQGtntllqevLPRHMIPAAYIELLAMPISRTGKVNRKLLREA 736
Cdd:PRK13295  478 ----ERLGERA----CAFVvPRPgQSLDFEEmveflKAQK--------VAKQYIPERLVVRDALPRTPSGKIQKFRLREM 541


                  ....*
gi 992230864  737 VEQAS 741
Cdd:PRK13295  542 LRGED 546
PRK06164 PRK06164
acyl-CoA synthetase; Validated
 245-745 1.13e-09

acyl-CoA synthetase; Validated


Pssm-ID: 235722 [Multi-domain]  Cd Length: 540  Bit Score: 63.22  E-value: 1.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  245 QPDAQAICAWDGTITYRQLDRLSSTVQGLLQQYDLGPGSVVPIIFKKSKWAIVAMLGVLKAGAAFCMLDQSYPT------ 318
Cdd:PRK06164   23 RPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRShevahi 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  319 ---------------------KRLVNICKDVDAKV----IVC--SQELSIGVSGSTLSIGD-HNTETATYSAIQAvntAS 370
Cdd:PRK06164  103 lgrgrarwlvvwpgfkgidfaAILAAVPPDALPPLraiaVVDdaADATPAPAPGARVQLFAlPDPAPPAAAGERA---AD 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  371 HDAAYVVYT-SGSTGAPKGIVIEHGSFCTNAIASSQAQNLDRSSRVLQFASY--AFDVSvheSLTPLLLGGC--VCIP-- 443
Cdd:PRK06164  180 PDAGALLFTtSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFcgVFGFS---TLLGALAGGAplVCEPvf 256

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  444 SEAQRVNSLKEAVSTLRVNWVELTPTVARLW-CPADIPTVKtlVMGGEPMLPNdislWKDKLRLVCA--------YGPAE 514
Cdd:PRK06164  257 DAARTARALRRHRVTHTFGNDEMLRRILDTAgERADFPSAR--LFGFASFAPA----LGELAALARArgvpltglYGSSE 330

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  515 ------CTVVSTVQSCVQELGNIGRSPCGTCWIVSKDNHhRLMPVGCIGELIIGGPIVGRGYLKQPCLTANAFITNPewa 588
Cdd:PRK06164  331 vqalvaLQPATDPVSVRIEGGGRPASPEARVRARDPQDG-ALLPDGESGEIEIRAPSLMRGYLDNPDATARALTDDG--- 406

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  589 slfhlngsyrFYKTGDLVRYNADGTIAYIGRKDTQVKLNGQRVELGEIEH--QAQPYFRDAVIaaeVAAPAGRKPILILF 666
Cdd:PRK06164  407 ----------YFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHalEALPGVAAAQV---VGATRDGKTVPVAF 473

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  667 IArkYEYSVNMDCTMLLRPpsilfqekaqgtntlLQEVLPRHMIPAAYIELLAMPISRTG---KVNRKLLREAVEQ--AS 741
Cdd:PRK06164  474 VI--PTDGASPDEAGLMAA---------------CREALAGFKVPARVQVVEAFPVTESAngaKIQKHRLREMAQArlAA 536


                  ....
gi 992230864  742 EKDF 745
Cdd:PRK06164  537 ERAA 540
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
 766-825 1.27e-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: 55.65  E-value: 1.27e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 992230864   766 DQLRLLFSAALRIPEEKIKPNDSFFHLGGDSVSAIRLVGDARDQ-GLHITVESLFKRQTIS 825
Cdd:pfam00550    1 ERLRELLAEVLGVPAEEIDPDTDLFDLGLDSLLAVELIARLEEEfGVEIPPSDLFEHPTLA 61
FACL_like_2 cd05917
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 371-637 1.34e-09

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: 61.91  E-value: 1.34e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  371 HDAAYVVYTSGSTGAPKGIVIEHGSFCTNAIASSQAQNLDRSSRV-LQFASYAFDVSVHESLTPLLLGGCVCIPSEAQRV 449
Cdd:cd05917     2 DDVINIQFTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLcIPVPLFHCFGSVLGVLACLTHGATMVFPSPSFDP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  450 NSLKEAVSTLRVNWVELTPT--VARLWCPA----DIPTVKTLVMGGEPMLPNDISLWKDKLR---LVCAYGPAECTVVST 520
Cdd:cd05917    82 LAVLEAIEKEKCTALHGVPTmfIAELEHPDfdkfDLSSLRTGIMAGAPCPPELMKRVIEVMNmkdVTIAYGMTETSPVST 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  521 ----VQSCVQELGNIGR-SPCGTCWIVSKDNHhRLMPVGCIGELIIGGPIVGRGYLKQPCLTANAfITNPEWaslfhlng 595
Cdd:cd05917   162 qtrtDDSIEKRVNTVGRiMPHTEAKIVDPEGG-IVPPVGVPGELCIRGYSVMKGYWNDPEKTAEA-IDGDGW-------- 231

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 992230864  596 syrfYKTGDLVRYNADGTIAYIGR-KDTQVKlNGQRVELGEIE 637
Cdd:cd05917   232 ----LHTGDLAVMDEDGYCRIVGRiKDMIIR-GGENIYPREIE 269
E-C_NRPS cd19544
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); ...
 1679-1877 1.35e-09

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: 62.45  E-value: 1.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1679 HAFLDATSVLIILRELAQAYDGQLSSVPGP-SYSSAVAWLQSLPNGDNRMDYWRRQLKD-ASPCI-FpRLRD-QDSPSD- 1753
Cdd:cd19544   134 HLISDHTSLELLLEEIQAILAGRAAALPPPvPYRNFVAQARLGASQAEHEAFFREMLGDvDEPTApF-GLLDvQGDGSDi 212

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1754 ---TLVVTEQLAstATLTPVCTRHGLTVSNVLQVAWGLMLRRYTESDDVCFGALISGRDSRIPDVDKMVGPFFNVLVCQL 1830
Cdd:cd19544   213 teaRLALDAELA--QRLRAQARRLGVSPASLFHLAWALVLARCSGRDDVVFGTVLSGRMQGGAGADRALGMFINTLPLRV 290

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 992230864 1831 RFGrEDSLWDVLRRNQTEIGNRLLNQHCSLIEVLRFS-TYFGQPLFNT 1877
Cdd:cd19544   291 RLG-GRSVREAVRQTHARLAELLRHEHASLALAQRCSgVPAPTPLFSA 337
PRK05677 PRK05677
long-chain-fatty-acid--CoA ligase; Validated
 234-637 1.48e-09

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


Pssm-ID: 168170 [Multi-domain]  Cd Length: 562  Bit Score: 62.86  E-value: 1.48e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  234 IHTLFRLQCILQPDAQAICAWDGTITYRQLDRLSSTVQGLLQQY-DLGPGSVVPIIFKKSKWAIVAMLGVLKAGAAFCML 312
Cdd:PRK05677   26 IQAVLKQSCQRFADKPAFSNLGKTLTYGELYKLSGAFAAWLQQHtDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVNT 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  313 DQSYPTKRLVNICKDVDAKVIVCSQELSIGVSGSTLSIGDHN---TETA-----------------------TYSAIQAV 366
Cdd:PRK05677  106 NPLYTAREMEHQFNDSGAKALVCLANMAHLAEKVLPKTGVKHvivTEVAdmlpplkrllinavvkhvkkmvpAYHLPQAV 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  367 -----------------NTASHDAAYVVYTSGSTGAPKGIVIEHGSFCTNAIASSQ--AQNLDRSSRVL-----QFASYA 422
Cdd:PRK05677  186 kfndalakgagqpvteaNPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCRAlmGSNLNEGCEILiaplpLYHIYA 265

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  423 FdvSVHESLTPLLLGGCVCIPSEAQRVNSLKEAVSTLRVNWVELTPTVARLwCPA------DIPTVKTLVMGGEPMLPND 496
Cdd:PRK05677  266 F--TFHCMAMMLIGNHNILISNPRDLPAMVKELGKWKFSGFVGLNTLFVAL-CNNeafrklDFSALKLTLSGGMALQLAT 342

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  497 ISLWKDKLRL-VC-AYGPAECTVVSTVQ--SCVQeLGNIGRS-PCGTCWIVSKDNHHrlMPVGCIGELIIGGPIVGRGYL 571
Cdd:PRK05677  343 AERWKEVTGCaICeGYGMTETSPVVSVNpsQAIQ-VGTIGIPvPSTLCKVIDDDGNE--LPLGEVGELCVKGPQVMKGYW 419

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 992230864  572 KQPCLTANAFiTNPEWaslfhlngsyrfYKTGDLVRYNADGTIAYIGRKDTQVKLNGQRVELGEIE 637
Cdd:PRK05677  420 QRPEATDEIL-DSDGW------------LKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELE 472
LC_FACS_euk1 cd17639
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ...
 372-637 1.85e-09

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: 62.62  E-value: 1.85e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  372 DAAYVVYTSGSTGAPKGIVIEHGSFC--TNAIASSQAQNLDRSSRVLQFASYA--FDVSVhESLTpLLLGGCVCIPSeaq 447
Cdd:cd17639    89 DLACIMYTSGSTGNPKGVMLTHGNLVagIAGLGDRVPELLGPDDRYLAYLPLAhiFELAA-ENVC-LYRGGTIGYGS--- 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  448 rVNSLKEAvSTLRVN--WVELTPT----VARLW------CPADIPTV----------------KTLVMGGEPMLPNDISL 499
Cdd:cd17639   164 -PRTLTDK-SKRGCKgdLTEFKPTlmvgVPAIWdtirkgVLAKLNPMgglkrtlfwtayqsklKALKEGPGTPLLDELVF 241

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  500 WK------DKLR------------------LVCA-----YGPAECTVVSTVQSCVQ-ELGNIGRsPCGTC------WIVS 543
Cdd:cd17639   242 KKvraalgGRLRymlsggaplsadtqeflnIVLCpviqgYGLTETCAGGTVQDPGDlETGRVGP-PLPCCeiklvdWEEG 320

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  544 KDNHHRLMPVGcigELIIGGPIVGRGYLKQPCLTANAFitNPEwaslfhlngsyRFYKTGDLVRYNADGTIAYIGRKDTQ 623
Cdd:cd17639   321 GYSTDKPPPRG---EILIRGPNVFKGYYKNPEKTKEAF--DGD-----------GWFHTGDIGEFHPDGTLKIIDRKKDL 384

                         330
                  ....*....|....*
gi 992230864  624 VKL-NGQRVELGEIE 637
Cdd:cd17639   385 VKLqNGEYIALEKLE 399
PRK12582 PRK12582
acyl-CoA synthetase; Provisional
 216-652 1.93e-09

acyl-CoA synthetase; Provisional


Pssm-ID: 237144 [Multi-domain]  Cd Length: 624  Bit Score: 62.76  E-value: 1.93e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  216 DQIAEWNRNAPIHPFdscihtlfrlqcILQPDAQAiCAWDGtITYRQLDRLSSTV-QGLLQQyDLGPGSVVPIIFKKSKW 294
Cdd:PRK12582   53 HLLAKWAAEAPDRPW------------LAQREPGH-GQWRK-VTYGEAKRAVDALaQALLDL-GLDPGRPVMILSGNSIE 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  295 AIVAMLGVLKAGA----------------------------AFCMLDQSYPTKRLVNICKDVDAKVIVCSQElsiGVSGS 346
Cdd:PRK12582  118 HALMTLAAMQAGVpaapvspayslmshdhaklkhlfdlvkpRVVFAQSGAPFARALAALDLLDVTVVHVTGP---GEGIA 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  347 TLSIGDHNTETATYSAIQAVNTASHDA-AYVVYTSGSTGAPKGIVIEHGSFCTNAIASSQAQNLDRS---SRVLQFASYA 422
Cdd:PRK12582  195 SIAFADLAATPPTAAVAAAIAAITPDTvAKYLFTSGSTGMPKAVINTQRMMCANIAMQEQLRPREPDpppPVSLDWMPWN 274

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  423 FDVSVHESLTPLLLGGCVCIPSEAQRVNSLKEavSTLRvNWVELTPTVArlwcpADIPTVKTLVMggePMLPNDISLWKD 502
Cdd:PRK12582  275 HTMGGNANFNGLLWGGGTLYIDDGKPLPGMFE--ETIR-NLREISPTVY-----GNVPAGYAMLA---EAMEKDDALRRS 343

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  503 ---KLRLVcAYGPAecTVVSTVQSCVQELG--NIGR---------------SPCGTCWIVSKDN---------HHRLMPV 553
Cdd:PRK12582  344 ffkNLRLM-AYGGA--TLSDDLYERMQALAvrTTGHripfytgygatetapTTTGTHWDTERVGliglplpgvELKLAPV 420

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  554 GCIGELIIGGPIVGRGYLKQPCLTANAFitNPEwaslfhlnGsyrFYKTGDLVRY----NADGTIAYIGRKDTQVKL-NG 628
Cdd:PRK12582  421 GDKYEVRVKGPNVTPGYHKDPELTAAAF--DEE--------G---FYRLGDAARFvdpdDPEKGLIFDGRVAEDFKLsTG 487

                         490       500
                  ....*....|....*....|....*...
gi 992230864  629 QRVELGEIEHQA----QPYFRDAVIAAE 652
Cdd:PRK12582  488 TWVSVGTLRPDAvaacSPVIHDAVVAGQ 515
PRK04319 PRK04319
acetyl-CoA synthetase; Provisional
 257-394 2.71e-09

acetyl-CoA synthetase; Provisional


Pssm-ID: 235279 [Multi-domain]  Cd Length: 570  Bit Score: 62.22  E-value: 2.71e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  257 TITYRQLDRLSSTVQGLLQQYDLGPGSVVPIIFKKSKWAIVAMLGVLKAGAAFCMLDQSY---PTKRLVNICkdvDAKVI 333
Cdd:PRK04319   73 KYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFmeeAVRDRLEDS---EAKVL 149

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 992230864  334 VCSQELSIGVSGSTLS-------IGDHNTETA-TYSAIQAVNTASH----------DAAYVVYTSGSTGAPKGIVIEHG 394
Cdd:PRK04319  150 ITTPALLERKPADDLPslkhvllVGEDVEEGPgTLDFNALMEQASDefdiewtdreDGAILHYTSGSTGKPKGVLHVHN 228
ACLS-CaiC cd17637
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ...
 372-620 3.40e-09

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: 60.75  E-value: 3.40e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  372 DAAYVVYTSGSTGAPKGIVIEHGSFCTNAIASSQAQNL---DRSSRVLQFasyaFDVS-VHESLTPLLLGGCVCI----- 442
Cdd:cd17637     1 DPFVIIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLteaDVYLNMLPL----FHIAgLNLALATFHAGGANVVmekfd 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  443 PSEAQRVnSLKEAVSTlrvnWVELTPTVARLW-----CPADIPTVKtLVMGGEpmLPNDISLWKDKL--RLVCAYGPAEC 515
Cdd:cd17637    77 PAEALEL-IEEEKVTL----MGSFPPILSNLLdaaekSGVDLSSLR-HVLGLD--APETIQRFEETTgaTFWSLYGQTET 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  516 TVVSTVQSCVQELGNIGR-SPCGTCWIVskDNHHRLMPVGCIGELIIGGPIVGRGYLKQPCLTANAFitnpewaslfhLN 594
Cdd:cd17637   149 SGLVTLSPYRERPGSAGRpGPLVRVRIV--DDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTF-----------RN 215

                         250       260
                  ....*....|....*....|....*.
gi 992230864  595 GsyrFYKTGDLVRYNADGTIAYIGRK 620
Cdd:cd17637   216 G---WHHTGDLGRFDEDGYLWYAGRK 238
PRK05691 PRK05691
peptide synthase; Validated
 1353-1831 3.58e-09

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 62.49  E-value: 3.58e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1353 QLQQLISSLGQSLPRSAVPSLCLPVSFIPVDPLGQPDRiylceaassmtldflHSLTDPVNKYIDyHILPEEARLRGIVA 1432
Cdd:PRK05691 1582 EAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDR---------------RALPEPVWQQRE-HVEPRTELQQQIAA 1645

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1433 ---HVLSIdPQnISPKDDFFTLGGDSISAMQVVSLCRKH---QLSLTALdiFNGRTIELIATRLmpltpytppstpASDR 1506
Cdd:PRK05691 1646 iwrEVLGL-PR-VGLRDDFFALGGHSLLATQIVSRTRQAcdvELPLRAL--FEASELGAFAEQV------------ARIQ 1709

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1507 SLDRRfsllflNSDRDMERLESllmatydigsmdsiEDAYPCSESHQG---LLQTQMLRPFYyqsytiwEVTTRSKSSPV 1583
Cdd:PRK05691 1710 AAGER------NSQGAIARVDR--------------SQPVPLSYSQQRmwfLWQMEPDSPAY-------NVGGMARLSGV 1762

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1584 SPV-RLCNAWFTLARRHPALRThliDIPLCDGMS-------SKIHVVHKDYMADAA--------ILSCEDEHVITEL-RK 1646
Cdd:PRK05691 1763 LDVdRFEAALQALILRHETLRT---TFPSVDGVPvqqvaedSGLRMDWQDFSALPAdarqqrlqQLADSEAHQPFDLeRG 1839

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1647 PFLpsdtglyyphafRICQTVSGRV--FCKLEGGHAFLDATSVLIILRELAQAYDGQLSSVPGPSYSSAVAWL------- 1717
Cdd:PRK05691 1840 PLL------------RACLVKAAERehYFVLTLHHIVTEGWAMDIFARELGALYEAFLDDRESPLEPLPVQYLdysvwqr 1907

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1718 QSLPNGD--NRMDYWRRQLKDASPCI-----FPRLRDQDSPSDTLVVTEQLASTATLTPVCTRHGLTVSNVLQVAWGLML 1790
Cdd:PRK05691 1908 QWLESGErqRQLDYWKAQLGNEHPLLelpadRPRPPVQSHRGELYRFDLSPELAARVRAFNAQRGLTLFMTMTATLAALL 1987

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|...
gi 992230864 1791 RRYTESDDVCFGALISGRDSriPDVDKMVGPFFN--VLVCQLR 1831
Cdd:PRK05691 1988 YRYSGQRDLRIGAPVANRIR--PESEGLIGAFLNtqVLRCQLD 2028
C_NRPS-like cd19537
Condensation family domain with an atypical active site motif; Condensation (C) domains of ...
 1580-1822 4.94e-09

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: 60.66  E-value: 4.94e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1580 SSPVSPVRLCNAWFTLARRHPALRTHLIDIPlcdgmsskiHVVHKDYmADAAILSCEDEH--VITELRKPFLPSDTglyy 1657
Cdd:cd19537    33 SGDVDRDRLASAWNTVLARHRILRSRYVPRD---------GGLRRSY-SSSPPRVQRVDTldVWKEINRPFDLERE---- 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1658 pHAFRICQT-------VSgrvfckleggHAFLDATSVLIILRELAQAYDGQLSSVPGPSYSSAVAWLQSLPNGDnrMDYW 1730
Cdd:cd19537    99 -DPIRVFISpdtllvvMS----------HIICDLTTLQLLLREVSAAYNGKLLPPVRREYLDSTAWSRPASPED--LDFW 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1731 RRQLKDASPCIFPRLRDQDSPSDTLVVTEQLASTAT-LTPVCTRHGLTVSNVLQVAWGLMLRRYTESDDVCFGALISGRD 1809
Cdd:cd19537   166 SEYLSGLPLLNLPRRTSSKSYRGTSRVFQLPGSLYRsLLQFSTSSGITLHQLALAAVALALQDLSDRTDIVLGAPYLNRT 245

                         250
                  ....*....|...
gi 992230864 1810 SriPDVDKMVGPF 1822
Cdd:cd19537   246 S--EEDMETVGLF 256
AFD_YhfT-like cd17633
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ...
 375-730 5.28e-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: 60.11  E-value: 5.28e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  375 YVVYTSGSTGAPKGIVIEHGSFCTNAIASSQAQNLDRSSRVLQFASYAFDVSVHESLTPLLLGGCVCIPSEAQrVNSLKE 454
Cdd:cd17633     4 YIGFTSGTTGLPKAYYRSERSWIESFVCNEDLFNISGEDAILAPGPLSHSLFLYGAISALYLGGTFIGQRKFN-PKSWIR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  455 AVSTLRVNWVELTPTVARLWCPADIP--TVKTLVMGG---EPMLPNDISLWKDKLRLVCAYGPAECTVVSTvqSCVQEL- 528
Cdd:cd17633    83 KINQYNATVIYLVPTMLQALARTLEPesKIKSIFSSGqklFESTKKKLKNIFPKANLIEFYGTSELSFITY--NFNQESr 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  529 --GNIGRsPCGTCWIVSKDNHHrlmpvGCIGELIIGGPIVGRGYLKQPCLTANafitnpEWaslfhlngsyrfYKTGDLV 606
Cdd:cd17633   161 ppNSVGR-PFPNVEIEIRNADG-----GEIGKIFVKSEMVFSGYVRGGFSNPD------GW------------MSVGDIG 216

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  607 RYNADGTIAYIGRKDTQVKLNGQRVELGEIEHQ--AQPYFRDAVIAAEVAAPAGRKPILILFIArkyeysvNMDCTMLLR 684
Cdd:cd17633   217 YVDEEGYLYLVGRESDMIIIGGINIFPTEIESVlkAIPGIEEAIVVGIPDARFGEIAVALYSGD-------KLTYKQLKR 289

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 992230864  685 ppsilfqekaqgtntLLQEVLPRHMIPAAYIELLAMPISRTGKVNR 730
Cdd:cd17633   290 ---------------FLKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
PRK05857 PRK05857
fatty acid--CoA ligase;
245-641 5.64e-09

fatty acid--CoA ligase;


Pssm-ID: 180293 [Multi-domain]  Cd Length: 540  Bit Score: 61.18  E-value: 5.64e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  245 QPDAQAICAWDGT--ITYRQLDRLSSTVQGLLQQYDLGPGSVVPIIFKKSKWAIVAMLGVLKAGAAFCMLDQSYPTKRLV 322
Cdd:PRK05857   27 QPEAIALRRCDGTsaLRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLPIAAIE 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  323 NICKDVDAKVIVCSQELSIGVSG------STLSIGDHNTETATYSAIQA--------VNTASHDAAYVVYTSGSTGAPKG 388
Cdd:PRK05857  107 RFCQITDPAAALVAPGSKMASSAvpealhSIPVIAVDIAAVTRESEHSLdaaslagnADQGSEDPLAMIFTSGTTGEPKA 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  389 IVIEHGSFCtnAIASS-QAQNLDRSSRVLQFASYAFDVSVHES-----LTPLLLGGcVCIpSEAQRVNSLKEAVSTLRVN 462
Cdd:PRK05857  187 VLLANRTFF--AVPDIlQKEGLNWVTWVVGETTYSPLPATHIGglwwiLTCLMHGG-LCV-TGGENTTSLLEILTTNAVA 262

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  463 WVELTPT-VARL-----WCPADIPTVKTLVMGGEPMLPNDISLWKDK-LRLVCAYGPAE--CTV--VSTVQSCVQ--ELG 529
Cdd:PRK05857  263 TTCLVPTlLSKLvselkSANATVPSLRLVGYGGSRAIAADVRFIEATgVRTAQVYGLSEtgCTAlcLPTDDGSIVkiEAG 342

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  530 NIGRS-PCGTCWIVSKD----NHHRLMPVGCIGELIIGGPIVGRGYLKQPCLTANAFITNpeWASlfhlngsyrfykTGD 604
Cdd:PRK05857  343 AVGRPyPGVDVYLAATDgigpTAPGAGPSASFGTLWIKSPANMLGYWNNPERTAEVLIDG--WVN------------TGD 408

                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 992230864  605 LVRYNADGTIAYIGRKDTQVKLNGQRVELGEIEHQAQ 641
Cdd:PRK05857  409 LLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAE 445
PRK13383 PRK13383
acyl-CoA synthetase; Provisional
 235-389 7.44e-09

acyl-CoA synthetase; Provisional


Pssm-ID: 139531 [Multi-domain]  Cd Length: 516  Bit Score: 60.40  E-value: 7.44e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  235 HTLFRLQCILQPDAQAICAWDGTITYRQLDRLSSTVQGLLQQYDLGPGSVVPIIFKKSKWAIVAMLGVLKAGAAFCMLDQ 314
Cdd:PRK13383   38 YTLLAVTAARWPGRTAIIDDDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPIST 117

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 992230864  315 SYPTKRLVNICKDVDAKVIVCSQELSIGVSGSTLSIGDHNTETATYSAIQAVNTASHDAAYVVYTSGSTGAPKGI 389
Cdd:PRK13383  118 EFRSDALAAALRAHHISTVVADNEFAERIAGADDAVAVIDPATAGAEESGGRPAVAAPGRIVLLTSGTTGKPKGV 192
PTZ00237 PTZ00237
acetyl-CoA synthetase; Provisional
 295-637 7.70e-09

acetyl-CoA synthetase; Provisional


Pssm-ID: 240325 [Multi-domain]  Cd Length: 647  Bit Score: 60.91  E-value: 7.70e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  295 AIVAMLGVLKAGAAFCMLDQSYPTKRLVNICKDVDAKVIVCSQ-------------------ELS--------------- 340
Cdd:PTZ00237  130 PLIAMLSCARIGATHCVLFDGYSVKSLIDRIETITPKLIITTNygilndeiitftpnlkeaiELStfkpsnvitlfrndi 209

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  341 -----------IGVSGSTLSIGDH------NTETATYsaiQAVNTASHDAAYVVYTSGSTGAPKGIVIEHGS--FCTNAI 401
Cdd:PTZ00237  210 tsesdlkkietIPTIPNTLSWYDEikkikeNNQSPFY---EYVPVESSHPLYILYTSGTTGNSKAVVRSNGPhlVGLKYY 286

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  402 ASSQAQNlDRSSRVLQFASYAFdVSVHESLTPLLLGGCVCIPSEA------------------QRVNSLKEAVSTLRvNW 463
Cdd:PTZ00237  287 WRSIIEK-DIPTVVFSHSSIGW-VSFHGFLYGSLSLGNTFVMFEGgiiknkhieddlwntiekHKVTHTLTLPKTIR-YL 363

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  464 VELTPTVARLWCPADIPTVKTLVMGGEPM---LPNDIslwKDKLRLVCA--YGPAECTVVSTVqsCVQELgNIGRSPCGT 538
Cdd:PTZ00237  364 IKTDPEATIIRSKYDLSNLKEIWCGGEVIeesIPEYI---ENKLKIKSSrgYGQTEIGITYLY--CYGHI-NIPYNATGV 437

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  539 CW------IVSKDNhhRLMPVGCIGELIIGGPIvgrgylkqPCLTANAFITNPE-WASLFHLNGSYrfYKTGDLVRYNAD 611
Cdd:PTZ00237  438 PSifikpsILSEDG--KELNVNEIGEVAFKLPM--------PPSFATTFYKNDEkFKQLFSKFPGY--YNSGDLGFKDEN 505

                         410       420
                  ....*....|....*....|....*.
gi 992230864  612 GTIAYIGRKDTQVKLNGQRVELGEIE 637
Cdd:PTZ00237  506 GYYTIVSRSDDQIKISGNKVQLNTIE 531
C_PKS-NRPS cd20483
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
 1588-1843 9.07e-09

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: 59.97  E-value: 9.07e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1588 LCNAWFTLARRHPALRTHLID--------IPlcdgMSSKIHVVHKDYMADAAILSCEDEHViTELRKpflpsdtglyypH 1659
Cdd:cd20483    41 LQKALSELVRRHEVLRTAYFEgddfgeqqVL----DDPSFHLIVIDLSEAADPEAALDQLV-RNLRR------------Q 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1660 AFRICQTVSGRV-FCKL-EGGHAFL--------DATSVLIILRELAQAYD-----GQLSSVPGPSYSSA------VAWLQ 1718
Cdd:cd20483   104 ELDIEEGEVIRGwLVKLpDEEFALVlashhiawDRGSSKSIFEQFTALYDalragRDLATVPPPPVQYIdftlwhNALLQ 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1719 SlPNGDNRMDYWRRQLKDASPCI--FP-RLRDQDSPSDTLVVTEQLASTATLTP----VCTRHGLTVSNVLQVAWGLMLR 1791
Cdd:cd20483   184 S-PLVQPLLDFWKEKLEGIPDASklLPfAKAERPPVKDYERSTVEATLDKELLArmkrICAQHAVTPFMFLLAAFRAFLY 262

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 992230864 1792 RYTESDDVCFGaLISGRDSRiPDVDKMVGPFFNVLVCQLRFGREDSLWDVLR 1843
Cdd:cd20483   263 RYTEDEDLTIG-MVDGDRPH-PDFDDLVGFFVNMLPIRCRMDCDMSFDDLLE 312
FCS cd05921
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ...
 257-652 1.05e-08

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: 60.14  E-value: 1.05e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  257 TITYRQLDRLSSTVQGLLQQYDLGPGSVVPIIFKKS-KWAIVAmLGVLKAGAAFCMLDQSYPTK-----RLVNICKDV-- 328
Cdd:cd05921    25 RVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSiEHALMA-LAAMYAGVPAAPVSPAYSLMsqdlaKLKHLFELLkp 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  329 ------------DAKVIVCSQELSIGVSGSTLSIGD--HNTETATYSAIQAVNtASHDA------AYVVYTSGSTGAPKG 388
Cdd:cd05921   104 glvfaqdaapfaRALAAIFPLGTPLVVSRNAVAGRGaiSFAELAATPPTAAVD-AAFAAvgpdtvAKFLFTSGSTGLPKA 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  389 IVIEHGSFCTNA--IASSQAQNLDRSSRVLQFASYAFDVSVHESLTPLLL-GGCVCI----PSE---AQRVNSLKEAVST 458
Cdd:cd05921   183 VINTQRMLCANQamLEQTYPFFGEEPPVLVDWLPWNHTFGGNHNFNLVLYnGGTLYIddgkPMPggfEETLRNLREISPT 262

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  459 LRVN----WVELTPTVAR--LWCPADIPTVKTLVMGGEPMLPNdisLWK-----------DKLRLVCAYGPAECTVVSTV 521
Cdd:cd05921   263 VYFNvpagWEMLVAALEKdeALRRRFFKRLKLMFYAGAGLSQD---VWDrlqalavatvgERIPMMAGLGATETAPTATF 339

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  522 QSCVQEL-GNIGRSPCGTcwivskdnHHRLMPVGCIGELIIGGPIVGRGYLKQPCLTANAFitNPEwaslfhlngsyRFY 600
Cdd:cd05921   340 THWPTERsGLIGLPAPGT--------ELKLVPSGGKYEVRVKGPNVTPGYWRQPELTAQAF--DEE-----------GFY 398

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 992230864  601 KTGDLVRYnADGT-----IAYIGRKDTQVKLN-GQRVELGEIEHQA----QPYFRDAVIAAE 652
Cdd:cd05921   399 CLGDAAKL-ADPDdpakgLVFDGRVAEDFKLAsGTWVSVGPLRARAvaacAPLVHDAVVAGE 459
A_NRPS_SidN3_like cd05918
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ...
 1294-1401 1.09e-08

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: 59.86  E-value: 1.09e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1294 IEKKVYDYFGGDVFVLVDAIVPNGSSNRST-AMFVCETKRRREPTETSGLFTRPTDNIRWQLQQLISSLGQSLPRSAVPS 1372
Cdd:cd05918   373 IEHHLRQSLPGAKEVVVEVVKPKDGSSSPQlVAFVVLDGSSSGSGDGDSLFLEPSDEFRALVAELRSKLRQRLPSYMVPS 452

                          90       100
                  ....*....|....*....|....*....
gi 992230864 1373 LCLPVSFIPVDPLGQPDRIYLCEAASSMT 1401
Cdd:cd05918   453 VFLPLSHLPLTASGKIDRRALRELAESLS 481
PRK08279 PRK08279
long-chain-acyl-CoA synthetase; Validated
 245-394 1.29e-08

long-chain-acyl-CoA synthetase; Validated


Pssm-ID: 236217 [Multi-domain]  Cd Length: 600  Bit Score: 59.89  E-value: 1.29e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  245 QPDAQAICAWDGTITYRQLDRLSSTVQGLLQQYDLGPGSVVPIIFKKSKWAIVAMLGVLKAGAAFCMLDQSYPTKRLVNI 324
Cdd:PRK08279   50 HPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVALLNTQQRGAVLAHS 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  325 CKDVDAKVIVCSQELSIGVSgstlSIGDHNTETATY-----------SAIQAVNTASH----------------DAAYVV 377
Cdd:PRK08279  130 LNLVDAKHLIVGEELVEAFE----EARADLARPPRLwvaggdtlddpEGYEDLAAAAAgapttnpasrsgvtakDTAFYI 205

                         170
                  ....*....|....*..
gi 992230864  378 YTSGSTGAPKGIVIEHG 394
Cdd:PRK08279  206 YTSGTTGLPKAAVMSHM 222
LC-FACS_euk cd05927
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ...
 372-626 2.41e-08

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: 58.77  E-value: 2.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  372 DAAYVVYTSGSTGAPKGIVIEHGSFCTNaIASsqaqnLDRSSRVLQFASyAFDVsvHESLTPL-------LLGGCVCIPS 444
Cdd:cd05927   115 DLATICYTSGTTGNPKGVMLTHGNIVSN-VAG-----VFKILEILNKIN-PTDV--YISYLPLahifervVEALFLYHGA 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  445 eaqRVNSLKEAVSTLRVNWVELTPT----VARLW---------CPADIPT------------------------------ 481
Cdd:cd05927   186 ---KIGFYSGDIRLLLDDIKALKPTvfpgVPRVLnriydkifnKVQAKGPlkrklfnfalnyklaelrsgvvraspfwdk 262

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  482 -------------VKTLVMGGEPMLPNDIslwkDKLRLVCA------YGPAECTVVSTVQ-SCVQELGNIGrSPCGTCWI 541
Cdd:cd05927   263 lvfnkikqalggnVRLMLTGSAPLSPEVL----EFLRVALGcpvlegYGQTECTAGATLTlPGDTSVGHVG-GPLPCAEV 337

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  542 VSKD----NHHRLMPVGcIGELIIGGPIVGRGYLKQPCLTANAFITnpewaslfhlNGsyrFYKTGDLVRYNADGTIAYI 617
Cdd:cd05927   338 KLVDvpemNYDAKDPNP-RGEVCIRGPNVFSGYYKDPEKTAEALDE----------DG---WLHTGDIGEWLPNGTLKII 403


                  ....*....
gi 992230864  618 GRKDTQVKL 626
Cdd:cd05927   404 DRKKNIFKL 412
PRK03640 PRK03640
o-succinylbenzoate--CoA ligase;
244-740 5.65e-08

o-succinylbenzoate--CoA ligase;


Pssm-ID: 235146 [Multi-domain]  Cd Length: 483  Bit Score: 57.66  E-value: 5.65e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  244 LQPDAQAICAWDGTITYRQLDRLSSTVQGLLQQYDLGPGSVVPIIFKKSKWAIVAMLGVLKAGAAFCMLDQSYPTKRLVN 323
Cdd:PRK03640   14 LTPDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLW 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  324 ICKDVDAKVIVCSQEL-SIGVSGSTLSIGDhnTETATYSAIQAVNTASHD-AAYVVYTSGSTGAPKGIVIEHGSFCTNAI 401
Cdd:PRK03640   94 QLDDAEVKCLITDDDFeAKLIPGISVKFAE--LMNGPKEEAEIQEEFDLDeVATIMYTSGTTGKPKGVIQTYGNHWWSAV 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  402 ASsqAQNL-----DR----------SSRVLQFAS--YAFDVSVHESLtplllggcvcipsEAQRVNSLKE--AVSTLRVN 462
Cdd:PRK03640  172 GS--ALNLgltedDCwlaavpifhiSGLSILMRSviYGMRVVLVEKF-------------DAEKINKLLQtgGVTIISVV 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  463 WVELTPTVARL---WCPadiPTVKTLVMGGEPMLPNDISLWKDK-LRLVCAYGPAE-CTVVSTVQS--CVQELGNIGRS- 534
Cdd:PRK03640  237 STMLQRLLERLgegTYP---SSFRCMLLGGGPAPKPLLEQCKEKgIPVYQSYGMTEtASQIVTLSPedALTKLGSAGKPl 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  535 -PCGTCwiVSKDNhhRLMPVGCIGELIIGGPIVGRGYLKQPCLTANAFITNpeWaslfhlngsyrfYKTGDLVRYNADGT 613
Cdd:PRK03640  314 fPCELK--IEKDG--VVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQDG--W------------FKTGDIGYLDEEGF 375

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  614 IAYIGRKDTQVKLNGQRVELGEIEH--QAQPYFRDAVIAAEVAAPAGRKPilILFIARKYEYSVNmdctmllrppsilfQ 691
Cdd:PRK03640  376 LYVLDRRSDLIISGGENIYPAEIEEvlLSHPGVAEAGVVGVPDDKWGQVP--VAFVVKSGEVTEE--------------E 439

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*....
gi 992230864  692 EKAQGtntllQEVLPRHMIPAAYIELLAMPISRTGKVNRKLLREAVEQA 740
Cdd:PRK03640  440 LRHFC-----EEKLAKYKVPKRFYFVEELPRNASGKLLRHELKQLVEEM 483
PRK07470 PRK07470
acyl-CoA synthetase; Validated
 372-744 6.58e-08

acyl-CoA synthetase; Validated


Pssm-ID: 180988 [Multi-domain]  Cd Length: 528  Bit Score: 57.36  E-value: 6.58e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  372 DAAYVVYTSGSTGAPKGIVIEHGSFC---TNAIA-----SSQAqnlDRSsrvLQFASYAFDVSVHEsLTPLLLGG-CVCI 442
Cdd:PRK07470  164 DPCWFFFTSGTTGRPKAAVLTHGQMAfviTNHLAdlmpgTTEQ---DAS---LVVAPLSHGAGIHQ-LCQVARGAaTVLL 236

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  443 PSEAQRVNSLKEAVSTLRVNWVELTPTVARLWC--PA----DIPTVKTLVMGGEPMLPNDISLWKDKL--RLVCAYGPAE 514
Cdd:PRK07470  237 PSERFDPAEVWALVERHRVTNLFTVPTILKMLVehPAvdryDHSSLRYVIYAGAPMYRADQKRALAKLgkVLVQYFGLGE 316

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  515 CTVVSTV-QSCVQELG-----NIGrsPCG---TCWIVS-KDNHHRLMPVGCIGELIIGGPIVGRGYLKQPCLTANAFItn 584
Cdd:PRK07470  317 VTGNITVlPPALHDAEdgpdaRIG--TCGferTGMEVQiQDDEGRELPPGETGEICVIGPAVFAGYYNNPEANAKAFR-- 392

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  585 pewaslfhlNGSYRfykTGDLVRYNADGTIAYIGRKDTQVKLNGQRVELGEIEHQ--AQPyfrdAViaAEVAapagrkpi 662
Cdd:PRK07470  393 ---------DGWFR---TGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKllTHP----AV--SEVA-------- 446

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  663 lILFIARKY--EYSVnMDCtmLLRPPSILfqeKAQGTNTLLQEVLPRHMIPAAYIELLAMPISRTGKVNRKLLREAVEQA 740
Cdd:PRK07470  447 -VLGVPDPVwgEVGV-AVC--VARDGAPV---DEAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMVREELEER 519


                  ....
gi 992230864  741 SEKD 744
Cdd:PRK07470  520 GLLD 523
FATP_FACS cd05940
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ...
 255-394 8.98e-08

Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.


Pssm-ID: 341263 [Multi-domain]  Cd Length: 449  Bit Score: 56.98  E-value: 8.98e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  255 DGTITYRQLDRLSSTVQGLLQQYDLGPGSVVPIIFKKSKWAIVAMLGVLKAGAAFCMLDQSYPTKRLVNICKDVDAKVIV 334
Cdd:cd05940     1 DEALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLV 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  335 CsqelsigvsgstlsigdhntetatysaiqavntashDAAYVVYTSGSTGAPKGIVIEHG 394
Cdd:cd05940    81 V------------------------------------DAALYIYTSGTTGLPKAAIISHR 104
PRK07059 PRK07059
Long-chain-fatty-acid--CoA ligase; Validated
 237-637 1.02e-07

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


Pssm-ID: 235923 [Multi-domain]  Cd Length: 557  Bit Score: 56.95  E-value: 1.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  237 LFRLQCILQPDAQAICAWDGTITYRQLDRLSSTVQGLLQQYDLGPGSVVPIIFKKSKWAIVAMLGVLKAGAAFCMLDQSY 316
Cdd:PRK07059   28 LLEESFRQYADRPAFICMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVNVNPLY 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  317 PTKRLVNICKDVDAK-----------------------VIVCSQELSIGVSGSTL--------------SIGDHNTETAT 359
Cdd:PRK07059  108 TPRELEHQLKDSGAEaivvlenfattvqqvlaktavkhVVVASMGDLLGFKGHIVnfvvrrvkkmvpawSLPGHVRFNDA 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  360 YSA-----IQAVNTASHDAAYVVYTSGSTGAPKGIVIEHGSFCTNAIASSQAQN--LDRSSRVLQFAS-------YAFDV 425
Cdd:PRK07059  188 LAEgarqtFKPVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVLQMEAWLQpaFEKKPRPDQLNFvcalplyHIFAL 267

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  426 SVHeSLTPLLLGGC-VCIPSEAQRVNSLKE----------AVSTLrVNWVELTPTVARLwcpaDIPTVKTLVMGG----E 490
Cdd:PRK07059  268 TVC-GLLGMRTGGRnILIPNPRDIPGFIKElkkyqvhifpAVNTL-YNALLNNPDFDKL----DFSKLIVANGGGmavqR 341

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  491 PMLPNdislWKDKLR--LVCAYGPAECTVVSTVQSC-VQEL-GNIGRsPCGTCWIVSKDNHHRLMPVGCIGELIIGGPIV 566
Cdd:PRK07059  342 PVAER----WLEMTGcpITEGYGLSETSPVATCNPVdATEFsGTIGL-PLPSTEVSIRDDDGNDLPLGEPGEICIRGPQV 416

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 992230864  567 GRGYLKQPCLTANAFITNPewaslfhlngsyrFYKTGDLVRYNADGTIAYIGRKDTQVKLNGQRVELGEIE 637
Cdd:PRK07059  417 MAGYWNRPDETAKVMTADG-------------FFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIE 474
PRK07787 PRK07787
acyl-CoA synthetase; Validated
 373-637 1.54e-07

acyl-CoA synthetase; Validated


Pssm-ID: 236096 [Multi-domain]  Cd Length: 471  Bit Score: 56.15  E-value: 1.54e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  373 AAYVVYTSGSTGAPKGIVIEHgsfctNAIASsqaqNLDRSSRVLQFAsyAFDVSVHE------------SLTPLLLGGCV 440
Cdd:PRK07787  130 PALIVYTSGTTGPPKGVVLSR-----RAIAA----DLDALAEAWQWT--ADDVLVHGlplfhvhglvlgVLGPLRIGNRF 198

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  441 ---------CIPSEAQRVNSLKEAVSTLrvnWVELT--PTVARLWCPAdiptvKTLVMGGEPmLPNDISlwkDKL----- 504
Cdd:PRK07787  199 vhtgrptpeAYAQALSEGGTLYFGVPTV---WSRIAadPEAARALRGA-----RLLVSGSAA-LPVPVF---DRLaaltg 266

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  505 -RLVCAYGPAECTV-VSTVQSCVQELGNIGRSPCGTcwivskdnHHRLM-----PVGC----IGELIIGGPIVGRGYLKQ 573
Cdd:PRK07787  267 hRPVERYGMTETLItLSTRADGERRPGWVGLPLAGV--------ETRLVdedggPVPHdgetVGELQVRGPTLFDGYLNR 338

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 992230864  574 PCLTANAFiTNPEWaslfhlngsyrfYKTGDLVRYNADGTIAYIGRKDTQ-VKLNGQRVELGEIE 637
Cdd:PRK07787  339 PDATAAAF-TADGW------------FRTGDVAVVDPDGMHRIVGRESTDlIKSGGYRIGAGEIE 390
PRK12467 PRK12467
peptide synthase; Provisional
 1354-1516 1.83e-07

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 56.71  E-value: 1.83e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1354 LQQLISSLGQSLPRSAVPSLCLPVSFIPVDPLGQPDRiylceaassmtldflHSLTDPVNKYIDYHILPE---EARLRGI 1430
Cdd:PRK12467 3549 RETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDR---------------KALPDPDAKGSREYVAPRsevEQQLAAI 3613

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1431 VAHVLSIdpQNISPKDDFFTLGGDSISAMQVVSLCRKH---QLSLTalDIFNGRTIELIATRL----MPLTPYTPPStpa 1503
Cdd:PRK12467 3614 WADVLGV--EQVGVTDNFFELGGDSLLALQVLSRIRQSlglKLSLR--DLMSAPTIAELAGYSplgdVPVNLLLDLN--- 3686

                         170
                  ....*....|...
gi 992230864 1504 sdrSLDRRFSLLF 1516
Cdd:PRK12467 3687 ---RLETGFPALF 3696
PRK08276 PRK08276
long-chain-fatty-acid--CoA ligase; Validated
 250-434 3.87e-07

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


Pssm-ID: 236215 [Multi-domain]  Cd Length: 502  Bit Score: 54.91  E-value: 3.87e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  250 AICAWDG-TITYRQLDRLSSTVQGLLQQYDLGPGSVVPIIFKKSKWAIVAMLGVLKAGAAFCMLDQSYPTKRLVNICKDV 328
Cdd:PRK08276    3 VIMAPSGeVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDS 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  329 DAKVIVCS-----------QELSIGVSGSTLSIGDHNTeTATYSAIQAVNTASHDA-----AYVVYTSGSTGAPKGIVIE 392
Cdd:PRK08276   83 GAKVLIVSaaladtaaelaAELPAGVPLLLVVAGPVPG-FRSYEEALAAQPDTPIAdetagADMLYSSGTTGRPKGIKRP 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 992230864  393 hgsfctnAIASSQAQNLDRSSRVLQFASYAFDVSVHESLTPL 434
Cdd:PRK08276  162 -------LPGLDPDEAPGMMLALLGFGMYGGPDSVYLSPAPL 196
PRK12467 PRK12467
peptide synthase; Provisional
 1356-1488 4.07e-07

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 55.55  E-value: 4.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1356 QLISSLGQSLPRSAVPSLCLPVSFIPVDPLGQPDRIYLCEAASSMtldFLHSLTDPVNKYidyhilpeEARLRGIVAHVL 1435
Cdd:PRK12467 2042 ILKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKALPAPDASE---LQQAYVAPQSEL--------EQRLAAIWQDVL 2110

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 992230864 1436 SIdpQNISPKDDFFTLGGDSISAMQVVSLCRKHQLSLTALDIFNGRTIELIAT 1488
Cdd:PRK12467 2111 GL--EQVGLHDNFFELGGDSIISIQVVSRARQAGIRFTPKDLFQHQTVQSLAA 2161
MACS_like_1 cd05974
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
 258-637 4.09e-07

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: 54.88  E-value: 4.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  258 ITYRQLDRLSSTVQGLLQQYDLGPGSVVPIIFKKSKWAIVAMLGVLKAGAAfcmldqsyptkrlvnickdvdakVIVCSQ 337
Cdd:cd05974     1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAV-----------------------VIPATT 57

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  338 ELSIGVSGSTLSIGDHNTetatysAIQAVNTASHDAAYVVYTSGSTGAPKGIVIEHGSFCTNAIASSQAQNLDRSSRVLQ 417
Cdd:cd05974    58 LLTPDDLRDRVDRGGAVY------AAVDENTHADDPMLLYFTSGTTSKPKLVEHTHRSYPVGHLSTMYWIGLKPGDVHWN 131

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  418 FASYAFDVSVHESL-TPLLLGGCVCIPSEAQ-RVNSLKEAVSTLRVNWVELTPTVARLWCPADIPTVKT----LVMGGEP 491
Cdd:cd05974   132 ISSPGWAKHAWSCFfAPWNAGATVFLFNYARfDAKRVLAALVRYGVTTLCAPPTVWRMLIQQDLASFDVklreVVGAGEP 211

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  492 MLPNDI----SLWKDKLRlvCAYGPAECTV-VSTVQSCVQELGNIGRsPCGTCWIVSKDNHHRLMPVGCIGELIIGGPIV 566
Cdd:cd05974   212 LNPEVIeqvrRAWGLTIR--DGYGQTETTAlVGNSPGQPVKAGSMGR-PLPGYRVALLDPDGAPATEGEVALDLGDTRPV 288

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 992230864  567 G--RGYLKQPCLTANAfitnpewaslfhLNGSYrfYKTGDLVRYNADGTIAYIGRKDTQVKLNGQRVELGEIE 637
Cdd:cd05974   289 GlmKGYAGDPDKTAHA------------MRGGY--YRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELE 347
FACL_like_5 cd05924
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 369-655 5.06e-07

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: 53.93  E-value: 5.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  369 ASHDAAYVVYTSGSTGAPKGIVIEHGSF--------------CTNAIASSQAQNLDRSSRVLQFASYAFDVSVHESLTPL 434
Cdd:cd05924     1 RSADDLYILYTGGTTGMPKGVMWRQEDIfrmlmggadfgtgeFTPSEDAHKAAAAAAGTVMFPAPPLMHGTGSWTAFGGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  435 LLGGCVCIPSEAQRVNSLKEAVSTLRVNWVELT------PTVARL--WCPADIPTVKTLVMGGEPMLPNdislWKDKL-- 504
Cdd:cd05924    81 LGGQTVVLPDDRFDPEEVWRTIEKHKVTSMTIVgdamarPLIDALrdAGPYDLSSLFAISSGGALLSPE----VKQGLle 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  505 -----RLVCAYGPAEC--TVVSTVQSCVQELGNIGRSPCGTCWIvskDNHHRLMPVGcigeliigGPIVGR--------- 568
Cdd:cd05924   157 lvpniTLVDAFGSSETgfTGSGHSAGSGPETGPFTRANPDTVVL---DDDGRVVPPG--------SGGVGWiarrghipl 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  569 GYLKQPCLTANAFITnpewaslfhLNGSyRFYKTGDLVRYNADGTIAYIGRKDTQVKLNGQRVELGEIEH--QAQPYFRD 646
Cdd:cd05924   226 GYYGDEAKTAETFPE---------VDGV-RYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEalKSHPAVYD 295

                         330
                  ....*....|....*..
gi 992230864  647 AVIAA--------EVAA 655
Cdd:cd05924   296 VLVVGrpderwgqEVVA 312
C_NRPS-like cd19537
Condensation family domain with an atypical active site motif; Condensation (C) domains of ...
 894-1119 5.07e-07

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: 54.11  E-value: 5.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  894 AFQAQFRFQLPHQLDMLRLKEAWRIVIAANPILRTRIVFCHTGALQVVLRPGEQLQW----DLINGVHTsPGSLmsYGVP 969
Cdd:cd19537    23 SFNVSFACRLSGDVDRDRLASAWNTVLARHRILRSRYVPRDGGLRRSYSSSPPRVQRvdtlDVWKEINR-PFDL--ERED 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  970 LVDMAITNDtagklsrTFCLTMHHAIFDGWSYGLILGAVEDAYKHTNAVQrpfaPFIKYIlHCNY------ESAKHFWCS 1043
Cdd:cd19537   100 PIRVFISPD-------TLLVVMSHIICDLTTLQLLLREVSAAYNGKLLPP----VRREYL-DSTAwsrpasPEDLDFWSE 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1044 EFKDMQALPFPVPPLSRGHMANS-----STTTHRQihvsewLSSYCTPS--TIIQLAFT---LLIAWRTESMDVLFGLTV 1113
Cdd:cd19537   168 YLSGLPLLNLPRRTSSKSYRGTSrvfqlPGSLYRS------LLQFSTSSgiTLHQLALAavaLALQDLSDRTDIVLGAPY 241


                  ....*.
gi 992230864 1114 TGRNAP 1119
Cdd:cd19537   242 LNRTSE 247
hsFATP2a_ACSVL_like cd05938
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ...
 255-393 1.31e-06

Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.


Pssm-ID: 341261 [Multi-domain]  Cd Length: 537  Bit Score: 53.45  E-value: 1.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  255 DGTITYRQLDRLSSTV-QGLLQQYDLGPGSVVPIIFKKSKWAIVAMLGVLKAGAAFCMLDQSYPTKRLVNICKDVDAKVI 333
Cdd:cd05938     3 GETYTYRDVDRRSNQAaRALLAHAGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAKVL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  334 VCSQELSIGVS---------GSTLSIGDHNTETATYSAIQA-VNTASHDA--------------AYVVYTSGSTGAPKGI 389
Cdd:cd05938    83 VVAPELQEAVEevlpalradGVSVWYLSHTSNTEGVISLLDkVDAASDEPvpaslrahvtikspALYIYTSGTTGLPKAA 162


                  ....
gi 992230864  390 VIEH 393
Cdd:cd05938   163 RISH 166
PRK09029 PRK09029
O-succinylbenzoic acid--CoA ligase; Provisional
 244-390 1.91e-06

O-succinylbenzoic acid--CoA ligase; Provisional


Pssm-ID: 236363 [Multi-domain]  Cd Length: 458  Bit Score: 52.57  E-value: 1.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  244 LQPDAQAICAWDGTITYRQL-DRLSSTVQGLLQQydlG--PGSVVPIIFKKSKWAIVAMLGVLKAGAAFCMLDQSYPTKR 320
Cdd:PRK09029   15 VRPQAIALRLNDEVLTWQQLcARIDQLAAGFAQQ---GvvEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPL 91

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 992230864  321 LVNICKDVDAKVIVCSQelsigvsgstlsigDHNTETATYSAIQAVNTASHDAAY-------VVYTSGSTGAPKGIV 390
Cdd:PRK09029   92 LEELLPSLTLDFALVLE--------------GENTFSALTSLHLQLVEGAHAVAWqpqrlatMTLTSGSTGLPKAAV 154
PRK06334 PRK06334
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
 250-666 2.46e-06

long chain fatty acid--[acyl-carrier-protein] ligase; Validated


Pssm-ID: 180533 [Multi-domain]  Cd Length: 539  Bit Score: 52.51  E-value: 2.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  250 AICAWD---GTITYRQLDRLSSTVQGLLQQYdlgPGSVVPIIFKKSKWAIVAMLGVLKAGAAFCMLDQSYPTKRLVNICK 326
Cdd:PRK06334   35 ATVCWDeqlGKLSYNQVRKAVIALATKVSKY---PDQHIGIMMPASAGAYIAYFATLLSGKIPVMINWSQGLREVTACAN 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  327 DVDAKVIVCSQEL--------SIGVS-----------GSTLSIGDhNTETATYSAI---------QAVNTASHDAAYVVY 378
Cdd:PRK06334  112 LVGVTHVLTSKQLmqhlaqthGEDAEypfsliymeevRKELSFWE-KCRIGIYMSIpfewlmrwfGVSDKDPEDVAVILF 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  379 TSGSTGAPKGIVIEHGSFCTNAIAS----SQAQNLDRSSRVLQFASYAFDVSvheSLTPLLLGGCVCIPSEAQRVNSLKE 454
Cdd:PRK06334  191 TSGTEKLPKGVPLTHANLLANQRAClkffSPKEDDVMMSFLPPFHAYGFNSC---TLFPLLSGVPVVFAYNPLYPKKIVE 267

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  455 AVSTLRVNWVELTP-------TVARLwCPADIPTVKTLVMGGEpmlpndisLWKDKLR-----------LVCAYGPAECT 516
Cdd:PRK06334  268 MIDEAKVTFLGSTPvffdyilKTAKK-QESCLPSLRFVVIGGD--------AFKDSLYqealktfphiqLRQGYGTTECS 338

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  517 VVSTV--------QSCVqelgniGRSPCGT-CWIVSKDNHhrlMPV--GCIGELIIGGPIVGRGYLKqpcltanafitNP 585
Cdd:PRK06334  339 PVITIntvnspkhESCV------GMPIRGMdVLIVSEETK---VPVssGETGLVLTRGTSLFSGYLG-----------ED 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  586 EWASLFHLNGSyRFYKTGDLVRYNADGTIAYIGRKDTQVKLNGQRVELGE-----IEHQAQPYFRDAvIAAEVAAPAGRK 660
Cdd:PRK06334  399 FGQGFVELGGE-TWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEAlesilMEGFGQNAADHA-GPLVVCGLPGEK 476


                  ....*.
gi 992230864  661 PILILF 666
Cdd:PRK06334  477 VRLCLF 482
LCL_NRPS-like cd19540
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ...
 1728-1831 2.93e-06

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: 52.04  E-value: 2.93e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1728 DYWRRQLKDAS-----PCIFPRLRDQDSPSDTLVVTEQLASTATLTPVCTRHGLTVSNVLQVAWGLMLRRYTESDDVCFG 1802
Cdd:cd19540   193 AYWRETLAGLPeelelPTDRPRPAVASYRGGTVEFTIDAELHARLAALAREHGATLFMVLHAALAVLLSRLGAGDDIPIG 272

                          90       100
                  ....*....|....*....|....*....
gi 992230864 1803 ALISGRDSriPDVDKMVGPFFNVLVcqLR 1831
Cdd:cd19540   273 TPVAGRGD--EALDDLVGMFVNTLV--LR 297
PrpE cd05967
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ...
 257-637 2.96e-06

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: 52.32  E-value: 2.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  257 TITYRQLDRLSSTVQGLLQQYDLGPGSVVPIIFKKSKWAIVAMLGVLKAGAAFCMLDQSYPTKRLVNICKDVDAKVIVCS 336
Cdd:cd05967    82 TYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHSVVFGGFAAKELASRIDDAKPKLIVTA 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  337 qelSIGVSG-----------STLSIGDH--------------------------NTETATYSAIQAVNTASHDAAYVVYT 379
Cdd:cd05967   162 ---SCGIEPgkvvpykplldKALELSGHkphhvlvlnrpqvpadltkpgrdldwSELLAKAEPVDCVPVAATDPLYILYT 238

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  380 SGSTGAPKGIVIEHGSFCTNAIASSQAQNLDRSSRVLQFASyafDVS--VHESLT---PLLLGGC--------VCIPS-- 444
Cdd:cd05967   239 SGTTGKPKGVVRDNGGHAVALNWSMRNIYGIKPGDVWWAAS---DVGwvVGHSYIvygPLLHGATtvlyegkpVGTPDpg 315

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  445 ------EAQRVNSLKEAVSTLRVnwVELTPTVARLWCPADIPTVKTLVMGGEPMLPNDISLWKDKL-RLVCAY------G 511
Cdd:cd05967   316 afwrviEKYQVNALFTAPTAIRA--IRKEDPDGKYIKKYDLSSLRTLFLAGERLDPPTLEWAENTLgVPVIDHwwqtetG 393

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  512 PAECTVVSTVQSCVQELGNIGRSPCGTCWIVSKDNHHRLmPVGCIGELIIGGPIvgrgylkqPCLTANAFITNPEWASLF 591
Cdd:cd05967   394 WPITANPVGLEPLPIKAGSPGKPVPGYQVQVLDEDGEPV-GPNELGNIVIKLPL--------PPGCLLTLWKNDERFKKL 464

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 992230864  592 HLNGSYRFYKTGDLVRYNADGTIAYIGRKDTQVKLNGQRVELGEIE 637
Cdd:cd05967   465 YLSKFPGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEME 510
PRK05691 PRK05691
peptide synthase; Validated
 1357-1488 1.08e-05

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 50.94  E-value: 1.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1357 LISSLGQSLPRSAVPSLCLPVSFIPVDPLGQPDRIYLceaassmtldflhSLTDPVNKYIDYhILPE---EARLRGIVAH 1433
Cdd:PRK05691 2655 LKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRAL-------------PAPDPELNRQAY-QAPRselEQQLAQIWRE 2720

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 992230864 1434 VLSIdpQNISPKDDFFTLGGDSISAMQVVSLCRKHQLSLTALDIFNGRTIELIAT 1488
Cdd:PRK05691 2721 VLNV--ERVGLGDNFFELGGDSILSIQVVSRARQLGIHFSPRDLFQHQTVQTLAA 2773
PRK12467 PRK12467
peptide synthase; Provisional
 1679-1844 1.87e-05

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 50.16  E-value: 1.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1679 HAFLDATSVLIILRELAQAYD----GQLSSVPG-P-SYSSAVAWLQS-LPNGDN--RMDYWRRQLKDASPCI-----FPR 1744
Cdd:PRK12467  183 HIISDGWSMRVLVEELVQLYSaysqGREPSLPAlPiQYADYAIWQRSwLEAGERerQLAYWQEQLGGEHTVLelptdRPR 262

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1745 LRDQDSPSDTLVVTEQLASTATLTPVCTRHGLTVSNVLQVAWGLMLRRYTESDDVCFGALISGRDsRIpDVDKMVGPFFN 1824
Cdd:PRK12467  263 PAVPSYRGARLRVDLPQALSAGLKALAQREGVTLFMVLLASFQTLLHRYSGQSDIRIGVPNANRN-RV-ETERLIGFFVN 340

                         170       180
                  ....*....|....*....|
gi 992230864 1825 VLVCQLRFGREDSLWDVLRR 1844
Cdd:PRK12467  341 TQVLKAEVDPQASFLELLQQ 360
PLN02387 PLN02387
long-chain-fatty-acid-CoA ligase family protein
 557-637 2.27e-05

long-chain-fatty-acid-CoA ligase family protein


Pssm-ID: 215217 [Multi-domain]  Cd Length: 696  Bit Score: 49.34  E-value: 2.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  557 GELIIGGPIVGRGYLKQPCLTANAFITNPewaslfhlNGSYRFYkTGDLVRYNADGTIAYIGRKDTQVKL-NGQRVELGE 635
Cdd:PLN02387  503 GEIVIGGPSVTLGYFKNQEKTDEVYKVDE--------RGMRWFY-TGDIGQFHPDGCLEIIDRKKDIVKLqHGEYVSLGK 573


                  ..
gi 992230864  636 IE 637
Cdd:PLN02387  574 VE 575
PLN02736 PLN02736
long-chain acyl-CoA synthetase
 354-406 2.61e-05

long-chain acyl-CoA synthetase


Pssm-ID: 178337 [Multi-domain]  Cd Length: 651  Bit Score: 49.33  E-value: 2.61e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 992230864  354 NTETATYSAIQAVNTAS---------HDAAYVVYTSGSTGAPKGIVIEHGSFCTNAIASSQA 406
Cdd:PLN02736  195 GVEIVTYSKLLAQGRSSpqpfrppkpEDVATICYTSGTTGTPKGVVLTHGNLIANVAGSSLS 256
hsFATP4_like cd05939
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ...
 255-396 2.73e-05

Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. 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.


Pssm-ID: 341262 [Multi-domain]  Cd Length: 474  Bit Score: 48.96  E-value: 2.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  255 DGTITYRQLDRLSSTVQGLLQQYDLGPGSVVPIIFKKSKWAIVAMLGVLKAGAAFCMLDQSYPTKRLVNickdvdakviv 334
Cdd:cd05939     1 DRHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLH----------- 69

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 992230864  335 csqelSIGVSGSTLSIGDHNT---ETATYSAIQAVNTASHDAAYVVYTSGSTGAPKGIVIEHGSF 396
Cdd:cd05939    70 -----CITVSKAKALIFNLLDpllTQSSTEPPSQDDVNFRDKLFYIYTSGTTGLPKAAVIVHSRY 129
FadD3 cd17638
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ...
 372-638 3.70e-05

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: 47.88  E-value: 3.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  372 DAAYVVYTSGSTGAPKGIVIEHGSFCTNAIASSQAQNLDRSSRVLQFASYAFDVSVHESLTPLLLGGCVCIPSEAQRVNS 451
Cdd:cd17638     1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIINPFFHTFGYKAGIVACLLTGATVVPVAVFDVDA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  452 LKEAVSTLRVNWVELTPTV--ARLWCPA----DIPTVKTLVMGGEPMLPNDISLWKDKL---RLVCAYGPAECTVVS--- 519
Cdd:cd17638    81 ILEAIERERITVLPGPPTLfqSLLDHPGrkkfDLSSLRAAVTGAATVPVELVRRMRSELgfeTVLTAYGLTEAGVATmcr 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  520 TVQSCVQELGNIGRSPCGtcwivskdnhhrlMPVGCI--GELIIGGPIVGRGYLKQPCLTANAfITNPEWaslFHlngsy 597
Cdd:cd17638   161 PGDDAETVATTCGRACPG-------------FEVRIAddGEVLVRGYNVMQGYLDDPEATAEA-IDADGW---LH----- 218

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 992230864  598 rfykTGDLVRYNADGTIAYIGRKDTQVKLNGQRVELGEIEH 638
Cdd:cd17638   219 ----TGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEG 255
alpha_am_amid TIGR03443
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ...
 1361-1487 5.17e-05

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: 48.52  E-value: 5.17e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  1361 LGQSLPRSAVPSLCLPVSFIPVDPLGQPDRIYLCEAASSMtLDFLHSLTDPVNKYIDYHilPEEARLRGIVAHVLSIDPQ 1440
Cdd:TIGR03443  790 LKKKLPSYAIPTVIVPLKKLPLNPNGKVDKPALPFPDTAQ-LAAVAKNRSASAADEEFT--ETEREIRDLWLELLPNRPA 866

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 992230864  1441 NISPKDDFFTLGGDSISAMQVVSLCRKH---QLSLTAldIFNGRTIELIA 1487
Cdd:TIGR03443  867 TISPDDSFFDLGGHSILATRMIFELRKKlnvELPLGL--IFKSPTIKGFA 914
starter-C_NRPS cd19533
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ...
 989-1150 5.47e-05

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: 47.75  E-value: 5.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  989 LTMHHAIFDGWSYGLILGAVEDAY----KHTNAVQRPFAPFIKYIL-------HCNYESAKHFWCSEFKDmqaLPFPV-- 1055
Cdd:cd19533   129 QRVHHIVMDGFSFALFGQRVAEIYtallKGRPAPPAPFGSFLDLVEeeqayrqSERFERDRAFWTEQFED---LPEPVsl 205

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1056 ----PPLSRG---HMANSSTTTHRQIhvSEWLSSY-CTPSTIIQLAFTLLIAWRTESMDVLFGLTVTGRnAPVAGIHrTT 1127
Cdd:cd19533   206 arraPGRSLAflrRTAELPPELTRTL--LEAAEAHgASWPSFFIALVAAYLHRLTGANDVVLGVPVMGR-LGAAARQ-TP 281

                         170       180
                  ....*....|....*....|...
gi 992230864 1128 GPTIATFPLRTILYGTMNITDAL 1150
Cdd:cd19533   282 GMVANTLPLRLTVDPQQTFAELV 304
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
 764-829 5.81e-05

Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.


Pssm-ID: 214834 [Multi-domain]  Cd Length: 86  Bit Score: 43.39  E-value: 5.81e-05
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 992230864    764 VLDQLRLLFSAALRI-PEEKIKPNDSFFHLGGDSVSAIRLVGDARDQ-GLHITVESLFKRQTISKLAE 829
Cdd:smart00823   13 LLDLVREQVAAVLGHaAAEAIDPDRPFRDLGLDSLMAVELRNRLEAAtGLRLPATLVFDHPTPAALAE 80
C_PKS-NRPS_PksJ-like cd20484
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
 1679-1846 6.00e-05

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: 47.70  E-value: 6.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1679 HAFLDATSVLIILRELAQAY----DGQ--LSSVPGPSYSSAVAWLQSL---PNGDNRMDYWRRQLKDASPCI-----FPR 1744
Cdd:cd20484   131 HIIFDGSSSLTLIHSLLDAYqallQGKqpTLASSPASYYDFVAWEQDMlagAEGEEHRAYWKQQLSGTLPILelpadRPR 210

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1745 LRDQDSPSDTLVVT------EQLASTATLtpvctrHGLTVSNVLQVAWGLMLRRYTESDDVCFGALISGR-DSRIpdvDK 1817
Cdd:cd20484   211 SSAPSFEGQTYTRRlpselsNQIKSFARS------QSINLSTVFLGIFKLLLHRYTGQEDIIVGMPTMGRpEERF---DS 281

                         170       180
                  ....*....|....*....|....*....
gi 992230864 1818 MVGPFFNVLVCQLRFGREDSLWDVLRRNQ 1846
Cdd:cd20484   282 LIGYFINMLPIRSRILGEETFSDFIRKLQ 310
ACSBG_like cd05933
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ...
 377-474 6.86e-05

Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very long-chain fatty acid CoA synthetase is named bubblegum because Drosophila melanogaster mutant bubblegum (BGM) has elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene of this family. The human homolog (hsBG) has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. VL-FACS is involved in the first reaction step of very long chain fatty acid degradation. It catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341256 [Multi-domain]  Cd Length: 596  Bit Score: 47.74  E-value: 6.86e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  377 VYTSGSTGAPKGIVIEHGSFCTNAIASSQAQNLdRSSRVLQ--FASY---------AFDVsvhesLTPLLLGGCVCIPSE 445
Cdd:cd05933   156 IYTSGTTGMPKGVMLSHDNITWTAKAASQHMDL-RPATVGQesVVSYlplshiaaqILDI-----WLPIKVGGQVYFAQP 229

                          90       100       110
                  ....*....|....*....|....*....|....
gi 992230864  446 aqrvNSLKEA-VSTLRvnwvELTPT----VARLW 474
Cdd:cd05933   230 ----DALKGTlVKTLR----EVRPTafmgVPRVW 255
PRK12316 PRK12316
peptide synthase; Provisional
 1355-1490 7.88e-05

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 48.03  E-value: 7.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1355 QQLISSLGQSLPRSAVPSLCLPVSFIPVDPLGQPDRIYLCEA-ASSMTLDFLHSLTDPvnkyidyhilpeEARLRGIVAH 1433
Cdd:PRK12316 5016 DELKAALRERLPEYMVPAHLVFLARMPLTPNGKLDRKALPQPdASLLQQAYVAPRSEL------------EQQVAAIWAE 5083

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 992230864 1434 VLSIdpQNISPKDDFFTLGGDSISAMQVVSLCRKH-QLSLTALDIFNGRTIELIATRL 1490
Cdd:PRK12316 5084 VLQL--ERVGLDDNFFELGGHSLLAIQVTSRIQLElGLELPLRELFQTPTLAAFVELA 5139
LCL_NRPS cd19538
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ...
 1588-1831 1.13e-04

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: 46.87  E-value: 1.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1588 LCNAWFTLARRHPALRTHlidIPLCDGMSSKIHVVHKDYMADAAILSCEDEHVITELrkpflpsDTGLYYPhaFRICQTV 1667
Cdd:cd19538    41 LQQALYDVVERHESLRTV---FPEEDGVPYQLILEEDEATPKLEIKEVDEEELESEI-------NEAVRYP--FDLSEEP 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1668 SGRV--FCKLEGGHAFL--------DATSVLIILRELAQAY-------DGQLSSVPgPSYSSAVAWLQSLPNGDN----- 1725
Cdd:cd19538   109 PFRAtlFELGENEHVLLlllhhiaaDGWSLAPLTRDLSKAYrarckgeAPELAPLP-VQYADYALWQQELLGDESdpdsl 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1726 ---RMDYWRRQLKDAS-----PCIFPRlrdQDSPSD-----TLVVTEQLAStaTLTPVCTRHGLTVSNVLQVAWGLMLRR 1792
Cdd:cd19538   188 iarQLAYWKKQLAGLPdeielPTDYPR---PAESSYeggtlTFEIDSELHQ--QLLQLAKDNNVTLFMVLQAGFAALLTR 262

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 992230864 1793 YTESDDVCFGALISGRDSRipDVDKMVGPFFNVLVcqLR 1831
Cdd:cd19538   263 LGAGTDIPIGSPVAGRNDD--SLEDLVGFFVNTLV--LR 297
PRK12316 PRK12316
peptide synthase; Provisional
 1679-1843 1.23e-04

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 47.64  E-value: 1.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1679 HAFLDATSVLIILRELAQAYDG-------QLSSVPgPSYSSAVAWLQS-LPNGDN--RMDYWRRQLKDASPCI-FPRLRD 1747
Cdd:PRK12316  183 HIVSDGWSMNVLIEEFSRFYSAyatgaepGLPALP-IQYADYALWQRSwLEAGEQerQLEYWRAQLGEEHPVLeLPTDHP 261

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1748 Q---DSPSDTLV---VTEQLAstATLTPVCTRHGLTVSNVLQVAWGLMLRRYTESDDVCFGALISGRDSRipDVDKMVGP 1821
Cdd:PRK12316  262 RpavPSYRGSRYefsIDPALA--EALRGTARRQGLTLFMLLLGAFNVLLHRYSGQTDIRVGVPIANRNRA--EVEGLIGF 337

                         170       180
                  ....*....|....*....|..
gi 992230864 1822 FFNVLVCQLRFGREDSLWDVLR 1843
Cdd:PRK12316  338 FVNTQVLRSVFDGRTRVATLLA 359
PLN02387 PLN02387
long-chain-fatty-acid-CoA ligase family protein
 324-394 2.60e-04

long-chain-fatty-acid-CoA ligase family protein


Pssm-ID: 215217 [Multi-domain]  Cd Length: 696  Bit Score: 45.88  E-value: 2.60e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 992230864  324 ICKDVDAkviVCSQELSIGVSGSTLSIGDHNTETATYSAIQAVNTASHDAAYVVYTSGSTGAPKGIVIEHG 394
Cdd:PLN02387  206 IYMDDEG---VDSDSSLSGSSNWTVSSFSEVEKLGKENPVDPDLPSPNDIAVIMYTSGSTGLPKGVMMTHG 273
PRK07638 PRK07638
acyl-CoA synthetase; Validated
 244-442 2.61e-04

acyl-CoA synthetase; Validated


Pssm-ID: 236071 [Multi-domain]  Cd Length: 487  Bit Score: 45.93  E-value: 2.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  244 LQPDAQAICAWDGTITYRQLDRLSSTVQGLLQQYDLGPGSVVpIIFKKSKWAIVAMLGVLKAGAAFCMLDQSYPTKRLVN 323
Cdd:PRK07638   13 LQPNKIAIKENDRVLTYKDWFESVCKVANWLNEKESKNKTIA-ILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELKE 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  324 ICKDVDAKVIVCSQELS---IGVSGSTLSIGDHNTETATYSAIQA-VNTASHDAAYVVYTSGSTGAPKGIVIEHGSFCTN 399
Cdd:PRK07638   92 RLAISNADMIVTERYKLndlPDEEGRVIEIDEWKRMIEKYLPTYApIENVQNAPFYMGFTSGSTGKPKAFLRAQQSWLHS 171

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 992230864  400 AIASSQAQNLDRSSRVLQFASYAFDVSVHESLTPLLLGGCVCI 442
Cdd:PRK07638  172 FDCNVHDFHMKREDSVLIAGTLVHSLFLYGAISTLYVGQTVHL 214
X-Domain_NRPS cd19546
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ...
 1683-1822 2.80e-04

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: 45.55  E-value: 2.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1683 DATSVLIILRELAQAYDGQLSS-----VPGP-SYSSAVAWLQSLPNGDNRMD--------YWRRQLKDASPCI---FPRL 1745
Cdd:cd19546   137 DDESLDVLVRDLAAAYGARREGraperAPLPlQFADYALWERELLAGEDDRDsligdqiaYWRDALAGAPDELelpTDRP 216

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 992230864 1746 RDQDSPSDTLVVTEQL--ASTATLTPVCTRHGLTVSNVLQVAWGLMLRRYTESDDVCFGALISGRDSRIpDVDKMVGPF 1822
Cdd:cd19546   217 RPVLPSRRAGAVPLRLdaEVHARLMEAAESAGATMFTVVQAALAMLLTRLGAGTDVTVGTVLPRDDEEG-DLEGMVGPF 294
ttLC_FACS_AEE21_like cd12118
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ...
 259-416 3.55e-04

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: 45.37  E-value: 3.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  259 TYRQLDRLSSTVQGLLqqydLGPGSVVPIIFKKSKWAIVAMLGVLKAGAAFCMLDQSYPTKRLVNICKDVDAKVIVCSQE 338
Cdd:cd12118    35 TYDRCRRLASALAALG----ISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFILRHSEAKVLFVDRE 110

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 992230864  339 LSigvSGSTLSIGDHNtetatYSAIQAVNtaSHDAAYVVYTSGSTGAPKGIVIEHGSFCTNAIASSQAQNLDRSSRVL 416
Cdd:cd12118   111 FE---YEDLLAEGDPD-----FEWIPPAD--EWDPIALNYTSGTTGRPKGVVYHHRGAYLNALANILEWEMKQHPVYL 178
PLN02246 PLN02246
4-coumarate--CoA ligase
 252-669 7.46e-04

4-coumarate--CoA ligase


Pssm-ID: 215137 [Multi-domain]  Cd Length: 537  Bit Score: 44.20  E-value: 7.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  252 CAWDG----TITYRQLDRLSSTVQGLLQQYDLGPGSVVPIIFKKSKWAIVAMLGVLKAGAA------FCM---------- 311
Cdd:PLN02246   41 CLIDGatgrVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVtttanpFYTpaeiakqaka 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  312 ------LDQSYPTKRLVNICKDVDAKVIVCSQELSIGVSGSTLSIGDHNtetatysAIQAVNTASHDAAYVVYTSGSTGA 385
Cdd:PLN02246  121 sgakliITQSCYVDKLKGLAEDDGVTVVTIDDPPEGCLHFSELTQADEN-------ELPEVEISPDDVVALPYSSGTTGL 193

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  386 PKGIVIEHGSFCTnaiasSQAQNLDRSSRVLQFASYafDVSV------H-ESLTPLLL-----GGCVCIPSEAQrVNSLK 453
Cdd:PLN02246  194 PKGVMLTHKGLVT-----SVAQQVDGENPNLYFHSD--DVILcvlpmfHiYSLNSVLLcglrvGAAILIMPKFE-IGALL 265

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  454 EAVSTLRVNWVELTP--TVARLWCPA----DIPTVKTLVMGGEPM-----------LPNDIslwkdklrLVCAYGPAEC- 515
Cdd:PLN02246  266 ELIQRHKVTIAPFVPpiVLAIAKSPVvekyDLSSIRMVLSGAAPLgkeledafrakLPNAV--------LGQGYGMTEAg 337

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  516 TVVSTVQSCVQELGNIGRSPCGTCW------IVSKDNHHRLmPVGCIGELIIGGPIVGRGYLKQPCLTANAfITNPEWas 589
Cdd:PLN02246  338 PVLAMCLAFAKEPFPVKSGSCGTVVrnaelkIVDPETGASL-PRNQPGEICIRGPQIMKGYLNDPEATANT-IDKDGW-- 413

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  590 lFHlngsyrfykTGDLVRYNADGTIAYIGRKDTQVKLNGQRVELGEIEH--QAQPYFRDAVIAAEVAAPAGRKPilILFI 667
Cdd:PLN02246  414 -LH---------TGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEAllISHPSIADAAVVPMKDEVAGEVP--VAFV 481


                  ..
gi 992230864  668 AR 669
Cdd:PLN02246  482 VR 483
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
1357-1490 8.73e-04

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 44.65  E-value: 8.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864 1357 LISSLGQSLPRSAVPSLCLPVSFIPVDPLGQPDRiylcEAASSMTLDFLHSLTDPVNkyidyhilPEEARLRGIVAHVLS 1436
Cdd:PRK10252  925 LQAQLRERLPPHMVPVVLLQLDQLPLSANGKLDR----KALPLPELKAQVPGRAPKT--------GTETIIAAAFSSLLG 992

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 992230864 1437 IDPQNIspKDDFFTLGGDSISAMQV-VSLCRKHQLSLTALDIFNGRTIELIATRL 1490
Cdd:PRK10252  993 CDVVDA--DADFFALGGHSLLAMKLaAQLSRQFARQVTPGQVMVASTVAKLATLL 1045
ACS cd05966
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ...
 246-390 9.75e-04

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: 44.09  E-value: 9.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  246 PDAQAIcAWDG-------TITYRQLDRLSSTVQGLLQQYDLGPGSVVPIIFKKSKWAIVAMLGVLKAGA----------- 307
Cdd:cd05966    67 GDKVAI-IWEGdepdqsrTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAvhsvvfagfsa 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 992230864  308 ---------AFCML----DQSY------PTKRLVN----ICKDVDaKVIVCsQELSIGVS---GSTLsigDHNTETATYS 361
Cdd:cd05966   146 esladrindAQCKLvitaDGGYrggkviPLKEIVDealeKCPSVE-KVLVV-KRTGGEVPmteGRDL---WWHDLMAKQS 220

                         170       180       190
                  ....*....|....*....|....*....|
gi 992230864  362 A-IQAVNTASHDAAYVVYTSGSTGAPKGIV 390
Cdd:cd05966   221 PeCEPEWMDSEDPLFILYTSGSTGKPKGVV 250
PTZ00342 PTZ00342
acyl-CoA synthetase; Provisional
 557-632 1.08e-03

acyl-CoA synthetase; Provisional


Pssm-ID: 240370 [Multi-domain]  Cd Length: 746  Bit Score: 43.94  E-value: 1.08e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 992230864  557 GELIIGGPIVGRGYLKQPCLTANAFITNpewaslfhlngsyRFYKTGDLVRYNADGTIAYIGRKDTQVKLN-GQRVE 632
Cdd:PTZ00342  542 GELLIKSDSIFSGYFLEKEQTKNAFTED-------------GYFKTGDIVQINKNGSLTFLDRSKGLVKLSqGEYIE 605
PTZ00216 PTZ00216
acyl-CoA synthetase; Provisional
 557-619 7.87e-03

acyl-CoA synthetase; Provisional


Pssm-ID: 240316 [Multi-domain]  Cd Length: 700  Bit Score: 41.12  E-value: 7.87e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 992230864  557 GELIIGGPIVGRGYLKQPCLTANAfITNPEWaslFHlngsyrfykTGDLVRYNADGTIAYIGR 619
Cdd:PTZ00216  508 GEILLRGPFLFKGYYKQEELTREV-LDEDGW---FH---------TGDVGSIAANGTLRIIGR 557
 
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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