NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|517718121|ref|WP_018888329|]
View 

non-ribosomal peptide synthetase [Paenibacillus massiliensis]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
LCL_NRPS-like cd19531
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ...
 951-1363 1.00e-131

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: 412.90  E-value: 1.00e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  951 YYPLTAAQMRV-FMDeQLVNTGSGYHITTAFMIYGPIDVTRLERACGQLIERHEALRTSFDIVDGDPVQRIHEHCDFHLE 1029
Cdd:cd19531     1 PLPLSFAQQRLwFLD-QLEPGSAAYNIPGALRLRGPLDVAALERALNELVARHEALRTTFVEVDGEPVQVILPPLPLPLP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1030 IVHLQG-------QQLHTAVNG-CIRPFQLERAPLIRSILIPLAEEQHLLVLDMHHIVADGKSVFLLQRDLAALYEGR-- 1099
Cdd:cd19531    80 VVDLSGlpeaereAEAQRLAREeARRPFDLARGPLLRATLLRLGEDEHVLLLTMHHIVSDGWSMGVLLRELAALYAAFla 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1100 ----ELHDLPVQYVDFAQWQTSAPVVEDLRRQEQFWQSMFADYRPLPGIPTDHTPEAnERSFAGGHITWEPDPVLSRRLY 1175
Cdd:cd19531   160 grpsPLPPLPIQYADYAVWQREWLQGEVLERQLAYWREQLAGAPPVLELPTDRPRPA-VQSFRGARVRFTLPAELTAALR 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1176 AVAAEQQTTLFMVLLAAFHVLYAKYSAREEVTVGTPVEGRRRAEVRQVVGMFVNALAIRSYPEGDKPFSSFLQEIRGTML 1255
Cdd:cd19531   239 ALARREGATLFMTLLAAFQVLLHRYSGQDDIVVGTPVAGRNRAELEGLIGFFVNTLVLRTDLSGDPTFRELLARVRETAL 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1256 QAYEHQDYPLERLAKQLDLHHSRDH--LmFDTVFSMLNYEDFAVRSDDLQFEYAELPTLSEIYNLRVEIVESPERLRGTF 1333
Cdd:cd19531   319 EAYAHQDLPFEKLVEALQPERDLSRspL-FQVMFVLQNAPAAALELPGLTVEPLEVDSGTAKFDLTLSLTETDGGLRGSL 397

                         410       420       430
                  ....*....|....*....|....*....|
gi 517718121 1334 KYGQELYEARTVSQLAQDYERILAAVAESP 1363
Cdd:cd19531   398 EYNTDLFDAATIERMAGHFQTLLEAIVADP 427
A_NRPS cd05930
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ...
 17-449 1.17e-129

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: 408.07  E-value: 1.17e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   17 PERKAIECGQQTLSYKELDAESDRICELLHAHGAAQYDHIGILMQDRCASIAAVIGILKLGGVFVPLDPLHPDERLVTML 96
Cdd:cd05930     1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   97 DTAEVSCLLCDdaqferaetlqghegkyfvlrarqamsvqagskeayshsanATDPIYIYFTSGSTGKPKAVVGKNESLL 176
Cdd:cd05930    81 EDSGAKLVLTD-----------------------------------------PDDLAYVIYTSGSTGKPKGVMVEHRGLV 119

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  177 HFMNWEASWLDLTDPMRVSQLTSIGFDAVLRDIFVPICAGGTICIPEsREIILDPLRLVHWLEHSRVHVVHCTPSLFR-F 255
Cdd:cd05930   120 NLLLWMQEAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLP-EEVRKDPEALADLLAEEGITVLHLTPSLLRlL 198

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  256 INHLSLTAdsYPDLRYVLLAGETIRPESLKNWYDnLGNRVRLVNLYGPTETTMIKLFYPIKPEDVHRESIPIGRPLPDTS 335
Cdd:cd05930   199 LQELELAA--LPSLRLVLVGGEALPPDLVRRWRE-LLPGARLVNLYGPTEATVDATYYRVPPDDEEDGRVPIGRPIPNTR 275

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  336 VYLLDEQQQPVSGSEAGEICIATRYMTHGYFPSshPDQTA--FIPDPCRdqsGEIMMYRTGDMGRWLPEGELALLGRKDN 413
Cdd:cd05930   276 VYVLDENLRPVPPGVPGELYIGGAGLARGYLNR--PELTAerFVPNPFG---PGERMYRTGDLVRWLPDGNLEFLGRIDD 350

                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 517718121  414 QVKIRGNRVELGDIEHRLTNMAGIREAVVRMRAKAD 449
Cdd:cd05930   351 QVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGD 386
PRK12467 super family cl36129
peptide synthase; Provisional
 783-1115 2.29e-30

peptide synthase; Provisional


The actual alignment was detected with superfamily member PRK12467:

Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 131.44  E-value: 2.29e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  783 VQLQVEEAQEPLLIAYYLADKMIDD--EQLSVYLRRFLPDYMIPARFIRLDKMPLTPNGKLDYNALPSPFEQDttARIYK 860
Cdd:PRK12467 3523 VVLARDGAGGKQLVAYVVPADPQGDwrETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDRKALPDPDAKG--SREYV 3600

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  861 APNSSTELKLLDIWTHILGIKRISADDHFLQIGVHSLNIMTLIAQVYENFQVELPLEQVFEHDTLEEIAAYIDEQDsqyg 940
Cdd:PRK12467 3601 APRSEVEQQLAAIWADVLGVEQVGVTDNFFELGGDSLLALQVLSRIRQSLGLKLSLRDLMSAPTIAELAGYSPLGD---- 3676

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  941 VRIEPAakqayypltaaqmrvfmdeqlvntgsgyhittafmiygpIDVTRLERACGQLIERHEALRTSFdivDGDPVQRI 1020
Cdd:PRK12467 3677 VPVNLL---------------------------------------LDLNRLETGFPALFCRHEGLGTVF---DYEPLAVI 3714

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1021 hehcdfhleivhlqgqqlhtavngcirpfqleraplirsilipLAEEQHLLVLDMHHIVADGksvfllqrdlaalYEGRE 1100
Cdd:PRK12467 3715 -------------------------------------------LEGDRHVLGLTCRHLLDDG-------------WQDTS 3738

                         330
                  ....*....|....*
gi 517718121 1101 LHDLPVQYVDFAQWQ 1115
Cdd:PRK12467 3739 LQAMAVQYADYILWQ 3753
AANH_superfamily super family cl00292
Adenine nucleotide alpha hydrolase (AANH) superfamily; The adenine nucleotide alpha hydrolase ...
 513-626 1.01e-27

Adenine nucleotide alpha hydrolase (AANH) superfamily; The adenine nucleotide alpha hydrolase (AANH) superfamily includes N-type ATP PPases, ATP sulfurylases, universal stress response proteins (USPs), and electron transfer flavoproteins (ETFs). The domain forms an alpha/beta/alpha fold which binds to adenosine nucleotide.


The actual alignment was detected with superfamily member cd01996:

Pssm-ID: 469708 [Multi-domain]  Cd Length: 158  Bit Score: 110.54  E-value: 1.01e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  513 NQPSYDCLLLYSGGKDSTYALYRLVEM-GARVLAYTFDNGYISSAAFRNIDSVVKELGVDHIVGTFDG--MLDIFKEGLK 589
Cdd:cd01996     2 KGKPYDCIIGVSGGKDSTYAAHKAKEKyGLRPLLVTVDAGWNSPEAVKNIEKLVRALGVDLITFVPNWkeMRDLQRLAFK 81

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 517718121  590 QECSVCNGCFKAMRILSTRVAAERGIPYIVTGLSRGQ 626
Cdd:cd01996    82 SNGDQDWPQDHGIFTSLYKMAVKFGIPLIIWGENPAE 118
 
Name Accession Description Interval E-value
LCL_NRPS-like cd19531
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ...
 951-1363 1.00e-131

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: 412.90  E-value: 1.00e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  951 YYPLTAAQMRV-FMDeQLVNTGSGYHITTAFMIYGPIDVTRLERACGQLIERHEALRTSFDIVDGDPVQRIHEHCDFHLE 1029
Cdd:cd19531     1 PLPLSFAQQRLwFLD-QLEPGSAAYNIPGALRLRGPLDVAALERALNELVARHEALRTTFVEVDGEPVQVILPPLPLPLP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1030 IVHLQG-------QQLHTAVNG-CIRPFQLERAPLIRSILIPLAEEQHLLVLDMHHIVADGKSVFLLQRDLAALYEGR-- 1099
Cdd:cd19531    80 VVDLSGlpeaereAEAQRLAREeARRPFDLARGPLLRATLLRLGEDEHVLLLTMHHIVSDGWSMGVLLRELAALYAAFla 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1100 ----ELHDLPVQYVDFAQWQTSAPVVEDLRRQEQFWQSMFADYRPLPGIPTDHTPEAnERSFAGGHITWEPDPVLSRRLY 1175
Cdd:cd19531   160 grpsPLPPLPIQYADYAVWQREWLQGEVLERQLAYWREQLAGAPPVLELPTDRPRPA-VQSFRGARVRFTLPAELTAALR 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1176 AVAAEQQTTLFMVLLAAFHVLYAKYSAREEVTVGTPVEGRRRAEVRQVVGMFVNALAIRSYPEGDKPFSSFLQEIRGTML 1255
Cdd:cd19531   239 ALARREGATLFMTLLAAFQVLLHRYSGQDDIVVGTPVAGRNRAELEGLIGFFVNTLVLRTDLSGDPTFRELLARVRETAL 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1256 QAYEHQDYPLERLAKQLDLHHSRDH--LmFDTVFSMLNYEDFAVRSDDLQFEYAELPTLSEIYNLRVEIVESPERLRGTF 1333
Cdd:cd19531   319 EAYAHQDLPFEKLVEALQPERDLSRspL-FQVMFVLQNAPAAALELPGLTVEPLEVDSGTAKFDLTLSLTETDGGLRGSL 397

                         410       420       430
                  ....*....|....*....|....*....|
gi 517718121 1334 KYGQELYEARTVSQLAQDYERILAAVAESP 1363
Cdd:cd19531   398 EYNTDLFDAATIERMAGHFQTLLEAIVADP 427
A_NRPS cd05930
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ...
 17-449 1.17e-129

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: 408.07  E-value: 1.17e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   17 PERKAIECGQQTLSYKELDAESDRICELLHAHGAAQYDHIGILMQDRCASIAAVIGILKLGGVFVPLDPLHPDERLVTML 96
Cdd:cd05930     1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   97 DTAEVSCLLCDdaqferaetlqghegkyfvlrarqamsvqagskeayshsanATDPIYIYFTSGSTGKPKAVVGKNESLL 176
Cdd:cd05930    81 EDSGAKLVLTD-----------------------------------------PDDLAYVIYTSGSTGKPKGVMVEHRGLV 119

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  177 HFMNWEASWLDLTDPMRVSQLTSIGFDAVLRDIFVPICAGGTICIPEsREIILDPLRLVHWLEHSRVHVVHCTPSLFR-F 255
Cdd:cd05930   120 NLLLWMQEAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLP-EEVRKDPEALADLLAEEGITVLHLTPSLLRlL 198

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  256 INHLSLTAdsYPDLRYVLLAGETIRPESLKNWYDnLGNRVRLVNLYGPTETTMIKLFYPIKPEDVHRESIPIGRPLPDTS 335
Cdd:cd05930   199 LQELELAA--LPSLRLVLVGGEALPPDLVRRWRE-LLPGARLVNLYGPTEATVDATYYRVPPDDEEDGRVPIGRPIPNTR 275

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  336 VYLLDEQQQPVSGSEAGEICIATRYMTHGYFPSshPDQTA--FIPDPCRdqsGEIMMYRTGDMGRWLPEGELALLGRKDN 413
Cdd:cd05930   276 VYVLDENLRPVPPGVPGELYIGGAGLARGYLNR--PELTAerFVPNPFG---PGERMYRTGDLVRWLPDGNLEFLGRIDD 350

                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 517718121  414 QVKIRGNRVELGDIEHRLTNMAGIREAVVRMRAKAD 449
Cdd:cd05930   351 QVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGD 386
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
 14-442 3.39e-120

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: 407.71  E-value: 3.39e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   14 AAFPERKAIECGQQTLSYKELDAESDRICELLHAHGAAQYDHIGILMqDRCA-SIAAVIGILKLGGVFVPLDPLHPDERL 92
Cdd:COG1020   487 ARTPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCL-ERSLeMVVALLAVLKAGAAYVPLDPAYPAERL 565

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   93 VTMLDTAEVSCLLCDDAQferAETLQGHEGKYFVLrarQAMSVQAGSKEAYSHSANATDPIYIYFTSGSTGKPKAVVGKN 172
Cdd:COG1020   566 AYMLEDAGARLVLTQSAL---AARLPELGVPVLAL---DALALAAEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEH 639

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  173 ESLLHFMNWEASWLDLTDPMRVSQLTSIGFDAVLRDIFVPICAGGTICIPeSREIILDPLRLVHWLEHSRVHVVHCTPSL 252
Cdd:COG1020   640 RALVNLLAWMQRRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATLVLA-PPEARRDPAALAELLARHRVTVLNLTPSL 718

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  253 FR-FINHLsltADSYPDLRYVLLAGETIRPESLKNWYDNLGnRVRLVNLYGPTETTMIKLFYPIKPEDVHRESIPIGRPL 331
Cdd:COG1020   719 LRaLLDAA---PEALPSLRLVLVGGEALPPELVRRWRARLP-GARLVNLYGPTETTVDSTYYEVTPPDADGGSVPIGRPI 794

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  332 PDTSVYLLDEQQQPVSGSEAGEICIATRYMTHGYFpsSHPDQTA--FIPDPCrDQSGEIMmYRTGDMGRWLPEGELALLG 409
Cdd:COG1020   795 ANTRVYVLDAHLQPVPVGVPGELYIGGAGLARGYL--NRPELTAerFVADPF-GFPGARL-YRTGDLARWLPDGNLEFLG 870

                         410       420       430
                  ....*....|....*....|....*....|...
gi 517718121  410 RKDNQVKIRGNRVELGDIEHRLTNMAGIREAVV 442
Cdd:COG1020   871 RADDQVKIRGFRIELGEIEAALLQHPGVREAVV 903
PRK12467 PRK12467
peptide synthase; Provisional
 783-1375 3.45e-115

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 401.46  E-value: 3.45e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  783 VQLQVEEAQEPLLIAYYLADKMIDD-------EQLSVYLRRFLPDYMIPARFIRLDKMPLTPNGKLDYNALPSPfEQDTT 855
Cdd:PRK12467  942 VVLAQPGDAGLQLVAYLVPAAVADGaehqatrDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKALPKP-DASAV 1020

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  856 ARIYKAPNSSTELKLLDIWTHILGIKRISADDHFLQIGVHSLNIMTLIAQVYENFQVELPLEQVFEHDTLEEIAAYIDEQ 935
Cdd:PRK12467 1021 QATFVAPQTELEKRLAAIWADVLKVERVGLTDNFFELGGHSLLATQVISRVRQRLGIQVPLRTLFEHQTLAGFAQAVAAQ 1100

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  936 DSQYGVRIEPAAKQAYYPLTAAQMRVFMDEQLVNTGSGYHITTAFMIYGPIDVTRLERACGQLIERHEALRTSFDIVDGD 1015
Cdd:PRK12467 1101 QQGAQPALPDVDRDQPLPLSYAQERQWFLWQLEPGSAAYHIPQALRLKGPLDIEALERSFDALVARHESLRTTFVQEDGR 1180

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1016 PVQRIHEHCDFHLEIVHLQG-----QQLHTAVNGCIR-PFQLERAPLIRSILIPLAEEQHLLVLDMHHIVADGKSVFLLQ 1089
Cdd:PRK12467 1181 TRQVIHPVGSLTLEEPLLLAadkdeAQLKVYVEAEARqPFDLEQGPLLRVGLLRLAADEHVLVLTLHHIVSDGWSMQVLV 1260

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1090 RDLAALYEGR------ELHDLPVQYVDFAQWQTSAPVVEDLRRQEQFWQSMFADYRPLPGIPTDHtPEANERSFAGGHIT 1163
Cdd:PRK12467 1261 DELVALYAAYsqgqslQLPALPIQYADYAVWQRQWMDAGERARQLAYWKAQLGGEQPVLELPTDR-PRPAVQSHRGARLA 1339

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1164 WEPDPVLSRRLYAVAAEQQTTLFMVLLAAFHVLYAKYSAREEVTVGTPVEGRRRAEVRQVVGMFVNALAIRSYPEGDKPF 1243
Cdd:PRK12467 1340 FELPPALAEGLRALARREGVTLFMLLLASFQTLLHRYSGQDDIRVGVPIANRNRAETEGLIGFFVNTQVLRAEVDGQASF 1419

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1244 SSFLQEIRGTMLQAYEHQDYPLERLAKQLDLHHSRDH-----LMFD---TVFSM------LNYEDFAVRSDDLQFEyael 1309
Cdd:PRK12467 1420 QQLLQQVKQAALEAQAHQDLPFEQLVEALQPERSLSHsplfqVMFNhqrDDHQAqaqlpgLSVESLSWESQTAQFD---- 1495

                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517718121 1310 ptlseiynLRVEIVESPERLRGTFKYGQELYEARTVSQLAQDYERILAAVAESPNIKLKDIEIRTP 1375
Cdd:PRK12467 1496 --------LTLDTYESSEGLQASLTYATDLFEASTIERLAGHWLNLLQGLVADPERRLGELDLLDE 1553
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
 30-442 5.46e-111

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: 356.19  E-value: 5.46e-111
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121    30 SYKELDAESDRICELLHAHGAAQY-DHIGILMqDRCAS-IAAVIGILKLGGVFVPLDPLHPDERLVTMLDTAEVSCLLCD 107
Cdd:TIGR01733    1 TYRELDERANRLARHLRAAGGVGPgDRVAVLL-ERSAElVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTD 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   108 DAQFERAETLQGHEGkyfVLRARQAMSVQAGSKEAYSHS-ANATDPIYIYFTSGSTGKPKAVVGKNESLLHFMNWEASWL 186
Cdd:TIGR01733   80 SALASRLAGLVLPVI---LLDPLELAALDDAPAPPPPDApSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRY 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   187 DLTDPMRVSQLTSIGFDAVLRDIFVPICAGGTICIPESREIILDPLRLVHWLEHSRVHVVHCTPSLFRfinHLSLTADSY 266
Cdd:TIGR01733  157 GLDPDDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAALLAALIAEHPVTVLNLTPSLLA---LLAAALPPA 233

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   267 PD-LRYVLLAGETIRPESLKNWYDNLGNrVRLVNLYGPTETTMIKLFYPIKPEDVHRES-IPIGRPLPDTSVYLLDEQQQ 344
Cdd:TIGR01733  234 LAsLRLVILGGEALTPALVDRWRARGPG-ARLINLYGPTETTVWSTATLVDPDDAPRESpVPIGRPLANTRLYVLDDDLR 312

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   345 PVSGSEAGEICIATRYMTHGYFpsSHPDQTA--FIPDPCRDQSGEiMMYRTGDMGRWLPEGELALLGRKDNQVKIRGNRV 422
Cdd:TIGR01733  313 PVPVGVVGELYIGGPGVARGYL--NRPELTAerFVPDPFAGGDGA-RLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRI 389

                          410       420
                   ....*....|....*....|
gi 517718121   423 ELGDIEHRLTNMAGIREAVV 442
Cdd:TIGR01733  390 ELGEIEAALLRHPGVREAVV 409
Condensation pfam00668
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ...
 948-1372 1.54e-95

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: 315.43  E-value: 1.54e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   948 KQAYYPLTAAQMRVFMDEQLVNTGSGYHITTAFMIYGPIDVTRLERACGQLIERHEALRTSFDI-VDGDPVQRIHEHCDF 1026
Cdd:pfam00668    1 VQDEYPLSPAQKRMWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIRqENGEPVQVILEERPF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  1027 HL---EIVHLQGQQLHTAVNGCIR-----PFQLERAPLIRSILIPLAEEQHLLVLDMHHIVADGKSVFLLQRDLAALYE- 1097
Cdd:pfam00668   81 ELeiiDISDLSESEEEEAIEAFIQrdlqsPFDLEKGPLFRAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLYQq 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  1098 ---GRELHDLPVQ-YVDFAQWQTSAPVVEDLRRQEQFWQSMFADYRPLPGIPTDHTPEANeRSFAGGHITWEPDPVLSRR 1173
Cdd:pfam00668  161 llkGEPLPLPPKTpYKDYAEWLQQYLQSEDYQKDAAYWLEQLEGELPVLQLPKDYARPAD-RSFKGDRLSFTLDEDTEEL 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  1174 LYAVAAEQQTTLFMVLLAAFHVLYAKYSAREEVTVGTPVEGRRRAEVRQVVGMFVNALAIRSYPEGDKPFSSFLQEIRGT 1253
Cdd:pfam00668  240 LRKLAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPSPDIERMVGMFVNTLPLRIDPKGGKTFSELIKRVQED 319

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  1254 MLQAYEHQDYPLERLAKQLDLHHS-RDHLMFDTVFSMLNYedfavrsdDLQFEYAELPTLSEI-------------YNLR 1319
Cdd:pfam00668  320 LLSAEPHQGYPFGDLVNDLRLPRDlSRHPLFDPMFSFQNY--------LGQDSQEEEFQLSELdlsvssvieeeakYDLS 391

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|...
gi 517718121  1320 VEIVESPERLRGTFKYGQELYEARTVSQLAQDYERILAAVAESPNIKLKDIEI 1372
Cdd:pfam00668  392 LTASERGGGLTIKIDYNTSLFDEETIERFAEHFKELLEQAIAHPSQPLSELDL 444
AMP-binding pfam00501
AMP-binding enzyme;
9-418 1.03e-83

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 280.74  E-value: 1.03e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121     9 LARAFAAFPERKAIECG-QQTLSYKELDAESDRICELLHAHGAAQYDHIGILMQDRCASIAAVIGILKLGGVFVPLDPLH 87
Cdd:pfam00501    1 LERQAARTPDKTALEVGeGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121    88 PDERLVTMLDTAEVSCLLCDDAQ------------FERAETLQGHEGKYFVLRARQAMSVQAGSKEAYSHSANATDPIYI 155
Cdd:pfam00501   81 PAEELAYILEDSGAKVLITDDALkleellealgklEVVKLVLVLDRDPVLKEEPLPEEAKPADVPPPPPPPPDPDDLAYI 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   156 YFTSGSTGKPKAVVGKNESLLHFM----NWEASWLDLTDPMRVSQLTSIGFDA-VLRDIFVPICAGGTICIPEsREIILD 230
Cdd:pfam00501  161 IYTSGTTGKPKGVMLTHRNLVANVlsikRVRPRGFGLGPDDRVLSTLPLFHDFgLSLGLLGPLLAGATVVLPP-GFPALD 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   231 PLRLVHWLEHSRVHVVHCTPSLFRFI-NHLSLTADSYPDLRYVLLAGETIRPESLKNWYDNLGNRVrlVNLYGPTETTMI 309
Cdd:pfam00501  240 PAALLELIERYKVTVLYGVPTLLNMLlEAGAPKRALLSSLRLVLSGGAPLPPELARRFRELFGGAL--VNGYGLTETTGV 317

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   310 KLFYPikPEDVHRESIP-IGRPLPDTSVYLLDEQ-QQPVSGSEAGEICIATRYMTHGYFpsSHPDQTA--FIPDPcrdqs 385
Cdd:pfam00501  318 VTTPL--PLDEDLRSLGsVGRPLPGTEVKIVDDEtGEPVPPGEPGELCVRGPGVMKGYL--NDPELTAeaFDEDG----- 388

                          410       420       430
                   ....*....|....*....|....*....|...
gi 517718121   386 geimMYRTGDMGRWLPEGELALLGRKDNQVKIR 418
Cdd:pfam00501  389 ----WYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
 942-1376 1.02e-78

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: 285.98  E-value: 1.02e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  942 RIEPAAKQAYYPLTAAQMRVFMDEQLVNTGSGYHITTAFMIYGPIDVTRLERACGQLIERHEALRTSFDIVDGDPVQRIH 1021
Cdd:COG1020     8 ALPPAAAAAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAGRPVQVIQ 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1022 EHCDFHLEIVHLQ--------GQQLHTAVNGCIRPFQLERAPLIRSILIPLAEEQHLLVLDMHHIVADGKSVFLLQRDLA 1093
Cdd:COG1020    88 PVVAAPLPVVVLLvdlealaeAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDGLLLAELL 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1094 ALY------EGRELHDLPVQYVDFAQWQTSAPVVEDLRRQEQFWQSMFADYRPLPGIPTDHTPEAnERSFAGGHITWEPD 1167
Cdd:COG1020   168 RLYlaayagAPLPLPPLPIQYADYALWQREWLQGEELARQLAYWRQQLAGLPPLLELPTDRPRPA-VQSYRGARVSFRLP 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1168 PVLSRRLYAVAAEQQTTLFMVLLAAFHVLYAKYSAREEVTVGTPVEGRRRAEVRQVVGMFVNALAIRSYPEGDKPFSSFL 1247
Cdd:COG1020   247 AELTAALRALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPRPELEGLVGFFVNTLPLRVDLSGDPSFAELL 326

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1248 QEIRGTMLQAYEHQDYPLERLAKQLDLHHSRDHL-MFDTVFSMLNYEDFAVRSDDLQFEYAELPTLSEIYNLRVEIVESP 1326
Cdd:COG1020   327 ARVRETLLAAYAHQDLPFERLVEELQPERDLSRNpLFQVMFVLQNAPADELELPGLTLEPLELDSGTAKFDLTLTVVETG 406

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 517718121 1327 ERLRGTFKYGQELYEARTVSQLAQDYERILAAVAESPNIKLKDIEIRTPQ 1376
Cdd:COG1020   407 DGLRLTLEYNTDLFDAATIERMAGHLVTLLEALAADPDQPLGDLPLLTAA 456
PRK12316 PRK12316
peptide synthase; Provisional
 14-442 6.21e-74

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 273.37  E-value: 6.21e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   14 AAFPERKAIECGQQTLSYKELDAESDRICELLHAHGAAQYDHIGILMQDRCASIAAVIGILKLGGVFVPLDPLHPDERLV 93
Cdd:PRK12316 4562 RMTPDAVAVVFDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLA 4641

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   94 TMLDTAEVSCLLCDDAQFERAETLQGhegkyfvlraRQAMSV-QAGSKEAYSHS--ANATDP---IYIYFTSGSTGKPKA 167
Cdd:PRK12316 4642 YMMEDSGAALLLTQSHLLQRLPIPDG----------LASLALdRDEDWEGFPAHdpAVRLHPdnlAYVIYTSGSTGRPKG 4711

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  168 VVGKNESLLHFMNWEASWLDLTDPMRVSQLTSIGFDAVLRDIFVPICAGGTICIPESReiILDPLRLVHWLEHSRVHVVH 247
Cdd:PRK12316 4712 VAVSHGSLVNHLHATGERYELTPDDRVLQFMSFSFDGSHEGLYHPLINGASVVIRDDS--LWDPERLYAEIHEHRVTVLV 4789

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  248 CTPSLFR-FINHLSLTADsYPDLRYVLLAGETIRPESLKNWYDNLGNrVRLVNLYGPTETTMIKLFYPIKPEDVH-RESI 325
Cdd:PRK12316 4790 FPPVYLQqLAEHAERDGE-PPSLRVYCFGGEAVAQASYDLAWRALKP-VYLFNGYGPTETTVTVLLWKARDGDACgAAYM 4867

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  326 PIGRPLPDTSVYLLDEQQQPVSGSEAGEICIATRYMTHGYFpsSHPDQTA--FIPDPCRDQSGEimMYRTGDMGRWLPEG 403
Cdd:PRK12316 4868 PIGTPLGNRSGYVLDGQLNPLPVGVAGELYLGGEGVARGYL--ERPALTAerFVPDPFGAPGGR--LYRTGDLARYRADG 4943

                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 517718121  404 ELALLGRKDNQVKIRGNRVELGDIEHRLTNMAGIREAVV 442
Cdd:PRK12316 4944 VIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVV 4982
PRK12467 PRK12467
peptide synthase; Provisional
 783-1115 2.29e-30

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 131.44  E-value: 2.29e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  783 VQLQVEEAQEPLLIAYYLADKMIDD--EQLSVYLRRFLPDYMIPARFIRLDKMPLTPNGKLDYNALPSPFEQDttARIYK 860
Cdd:PRK12467 3523 VVLARDGAGGKQLVAYVVPADPQGDwrETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDRKALPDPDAKG--SREYV 3600

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  861 APNSSTELKLLDIWTHILGIKRISADDHFLQIGVHSLNIMTLIAQVYENFQVELPLEQVFEHDTLEEIAAYIDEQDsqyg 940
Cdd:PRK12467 3601 APRSEVEQQLAAIWADVLGVEQVGVTDNFFELGGDSLLALQVLSRIRQSLGLKLSLRDLMSAPTIAELAGYSPLGD---- 3676

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  941 VRIEPAakqayypltaaqmrvfmdeqlvntgsgyhittafmiygpIDVTRLERACGQLIERHEALRTSFdivDGDPVQRI 1020
Cdd:PRK12467 3677 VPVNLL---------------------------------------LDLNRLETGFPALFCRHEGLGTVF---DYEPLAVI 3714

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1021 hehcdfhleivhlqgqqlhtavngcirpfqleraplirsilipLAEEQHLLVLDMHHIVADGksvfllqrdlaalYEGRE 1100
Cdd:PRK12467 3715 -------------------------------------------LEGDRHVLGLTCRHLLDDG-------------WQDTS 3738

                         330
                  ....*....|....*
gi 517718121 1101 LHDLPVQYVDFAQWQ 1115
Cdd:PRK12467 3739 LQAMAVQYADYILWQ 3753
AANH_WbpG-like cd01996
Rhizobium leguminosarum WbpG protein and similar proteins; This subfamily includes Rhizobium ...
 513-626 1.01e-27

Rhizobium leguminosarum WbpG protein and similar proteins; This subfamily includes Rhizobium leguminosarum WbpG and Campylobacter jejuni PseA proteins. They belong to the of adenine nucleotide alpha hydrolase (AANH) superfamily that also includes N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to adenosine group. This subfamily of proteins is predicted to bind ATP. This domain has a strongly conserved motif SGGKD at the N-terminus.


Pssm-ID: 467500 [Multi-domain]  Cd Length: 158  Bit Score: 110.54  E-value: 1.01e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  513 NQPSYDCLLLYSGGKDSTYALYRLVEM-GARVLAYTFDNGYISSAAFRNIDSVVKELGVDHIVGTFDG--MLDIFKEGLK 589
Cdd:cd01996     2 KGKPYDCIIGVSGGKDSTYAAHKAKEKyGLRPLLVTVDAGWNSPEAVKNIEKLVRALGVDLITFVPNWkeMRDLQRLAFK 81

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 517718121  590 QECSVCNGCFKAMRILSTRVAAERGIPYIVTGLSRGQ 626
Cdd:cd01996    82 SNGDQDWPQDHGIFTSLYKMAVKFGIPLIIWGENPAE 118
WbuX TIGR03573
N-acetyl sugar amidotransferase; This enzyme has been implicated in the formation of the ...
 456-758 2.99e-24

N-acetyl sugar amidotransferase; This enzyme has been implicated in the formation of the acetamido moiety (sugar-NC(=NH)CH3) which is found on some exopolysaccharides and is positively charged at neutral pH. The reaction involves ligation of ammonia with a sugar N-acetyl group, displacing water. In E. coli (O145 strain) and Pseudomonas aeruginosa (O12 strain) this gene is known as wbuX and ifnA respectively and likely acts on sialic acid. In Campylobacter jejuni, the gene is known as pseA and acts on pseudaminic acid in the process of flagellin glycosylation. In other Pseudomonas strains and various organisms it is unclear what the identity of the sugar substrate is, and in fact, the phylogenetic tree of this family sports a considerably deep branching suggestive of possible major differences in substrate structure. Nevertheless, the family is characterized by a conserved tetracysteine motif (CxxC.....[GN]xCxxC) possibly indicative of a metal binding site, as well as an invariable contextual association with homologs of the HisH and HisF proteins known as WbuY and WbuZ, respectively. These two proteins are believed to supply the enzyme with ammonium by hydrolysis of glutamine and delivery through an ammonium conduit.


Pssm-ID: 274658  Cd Length: 343  Bit Score: 105.85  E-value: 2.99e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   456 QQHCAACGLPSTYPGISFDDMGKCSVCTGQEQyrsaAEQ--YFQGMEQLQSKLQPVEKENQPSYDCLLLYSGGKDSTYAL 533
Cdd:TIGR03573    1 MKFCKRCVMPTTRPGITFDEDGVCSACRNFEE----KSKidWDEREKELEELVDKIKKKGGGRYDCIIGVSGGKDSTYQA 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   534 YRLVE-MGARVLAYTFDNGYISSAAFRNIDSVVKELGVDHIVGTFDG--MLDIFKEGLKQECSVCNGCFKAMRILSTRVA 610
Cdd:TIGR03573   77 HVLKKkLGLNPLLVTVDPGWNTELGVKNLNNLIKKLGFDLHTITINPetFRKLQRAYFKKVGDPEWPQDHAIFASVYQVA 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   611 AERGIPYIVTGLS---------------RGQIYDVRLYDilqqgyrttAEIELKIQEQRVlyhGKKDYVAEAFERDELIN 675
Cdd:TIGR03573  157 LKFNIPLIIWGENiaeeyggdseeelnpDEWKYNKRGID---------AANIKDFSDKGL---SERDLYAYTYPDKEKLQ 224

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   676 RSMLDQVELVDFYRYcdvSKQDILSFlqSKSEC-WSNPEDTG----FCSSNCLINDAGIYVQRTQLGYDNYAFPNSWEVR 750
Cdd:TIGR03573  225 SKGVKVIYLGYYVKW---DKKKNYEF--IKKRGgWREGPHPGtyenYKHIDSIFTIFHDYLKYLKFGFGRATDHASIDIR 299


                   ....*...
gi 517718121   751 TGHITLEQ 758
Cdd:TIGR03573  300 SGRITREE 307
alpha_am_amid TIGR03443
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ...
 788-950 5.74e-20

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: 97.06  E-value: 5.74e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   788 EEAQEPL---LIAYYladKMIDDeqLSVYLRRFLPDYMIPARFIRLDKMPLTPNGKLDYNALPSPfeqDTTARIYKAPNS 864
Cdd:TIGR03443  766 EESSDPVvkgLIKYR---KLIKD--IREYLKKKLPSYAIPTVIVPLKKLPLNPNGKVDKPALPFP---DTAQLAAVAKNR 837

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   865 S----------TELKLLDIWTHILGIK--RISADDHFLQIGVHSLNIMTLIAQVYENFQVELPLEQVFEHDTLEEIAAYI 932
Cdd:TIGR03443  838 SasaadeefteTEREIRDLWLELLPNRpaTISPDDSFFDLGGHSILATRMIFELRKKLNVELPLGLIFKSPTIKGFAKEV 917

                          170       180
                   ....*....|....*....|...
gi 517718121   933 D-----EQDSQYGVRIEPAAKQA 950
Cdd:TIGR03443  918 DrlkkgEELADEGDSEIEEEETV 940
A_NRPS_Bac cd17655
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ...
 788-849 3.83e-17

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: 86.23  E-value: 3.83e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517718121  788 EEAQEPLLIAYYLADKMIDDEQLSVYLRRFLPDYMIPARFIRLDKMPLTPNGKLDYNALPSP 849
Cdd:cd17655   428 DEQGQNYLCAYIVSEKELPVAQLREFLARELPDYMIPSYFIKLDEIPLTPNGKVDRKALPEP 489
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
 861-935 7.27e-13

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: 65.26  E-value: 7.27e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517718121  861 APNSSTELKLLDIWTHILGIK--RISADDHFLQ-IGVHSLNIMTLIAQVYENFQVELPLEQVFEHDTLEEIAAYIDEQ 935
Cdd:COG0236     1 MPREELEERLAEIIAEVLGVDpeEITPDDSFFEdLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLEEK 78
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
 869-927 1.99e-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: 60.65  E-value: 1.99e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517718121   869 KLLDIWTHILGI--KRISADDHFLQIGVHSLNIMTLIAQVYENFQVELPLEQVFEHDTLEE 927
Cdd:pfam00550    2 RLRELLAEVLGVpaEEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLAE 62
COG1606 COG1606
ATP-utilizing enzyme, PP-loop superfamily [General function prediction only];
500-621 4.83e-07

ATP-utilizing enzyme, PP-loop superfamily [General function prediction only];


Pssm-ID: 441214 [Multi-domain]  Cd Length: 265  Bit Score: 52.81  E-value: 4.83e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  500 EQLQSKLQPVEKenqpsydCLLLYSGGKDSTYALYRLVE-MGARVLAYTFDNGYISSAAFRNIDSVVKELGVDHIVGTFD 578
Cdd:COG1606     6 ERLKAILKELGS-------VLVAFSGGVDSTLLAKVAHDvLGDRVLAVTADSPSLPERELEEAKELAKEIGIRHEVIETD 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 517718121  579 gMLDI--FKEGLKQECSVCngcfKAMRILS-TRVAAERGIPYIVTG 621
Cdd:COG1606    79 -ELEDpeFVANPPDRCYHC----KKELFSKlKELAKELGYAVVADG 119
PRK08349 PRK08349
hypothetical protein; Validated
 522-627 1.06e-04

hypothetical protein; Validated


Pssm-ID: 169396  Cd Length: 198  Bit Score: 44.73  E-value: 1.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  522 LYSGGKDSTYALYRLVEMGARVLAYTFDNGYISSAAFRNIDSVVKELGVD-----HIVGTFDGMLDIFkEGLKQECS--- 593
Cdd:PRK08349    6 LLSSGIDSPVAIYLMLRRGVEVYPVHFRQDEKKEEKVRELVERLQELHGGklkdpVVVDAFEEQGPVF-EKLRELKKekw 84

                          90       100       110
                  ....*....|....*....|....*....|....
gi 517718121  594 VCNGCFKAMRILSTRVAAERGIPYIVTGLSRGQI 627
Cdd:PRK08349   85 TCIFCKYTMYRKAERIAHEIGASAIITGDSLGQV 118
QueC pfam06508
Queuosine biosynthesis protein QueC; This family of proteins participate in the biosynthesis ...
 519-574 2.16e-04

Queuosine biosynthesis protein QueC; This family of proteins participate in the biosynthesis of 7-carboxy-7-deazaguanine. They catalyze the conversion of 7-deaza-7-carboxyguanine to preQ0.


Pssm-ID: 428982 [Multi-domain]  Cd Length: 210  Bit Score: 44.15  E-value: 2.16e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 517718121   519 CLLLYSGGKDSTYALYRLVEMGARVLAYTFDNGYISSAAFRNIDSVVKELGVDHIV 574
Cdd:pfam06508    2 AVVLLSGGLDSTTCLAWAKKEGYEVYALSFDYGQRHRKELECAKKIAKALGVEHKI 57
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
 870-935 2.16e-04

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: 41.47  E-value: 2.16e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517718121    870 LLDIWTHILGI---KRISADDHFLQIGVHSLNIMTLIAQVYENFQVELPLEQVFEHDTLEEIAAYIDEQ 935
Cdd:smart00823   17 VREQVAAVLGHaaaEAIDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAEHLAAE 85
 
Name Accession Description Interval E-value
LCL_NRPS-like cd19531
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ...
 951-1363 1.00e-131

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: 412.90  E-value: 1.00e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  951 YYPLTAAQMRV-FMDeQLVNTGSGYHITTAFMIYGPIDVTRLERACGQLIERHEALRTSFDIVDGDPVQRIHEHCDFHLE 1029
Cdd:cd19531     1 PLPLSFAQQRLwFLD-QLEPGSAAYNIPGALRLRGPLDVAALERALNELVARHEALRTTFVEVDGEPVQVILPPLPLPLP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1030 IVHLQG-------QQLHTAVNG-CIRPFQLERAPLIRSILIPLAEEQHLLVLDMHHIVADGKSVFLLQRDLAALYEGR-- 1099
Cdd:cd19531    80 VVDLSGlpeaereAEAQRLAREeARRPFDLARGPLLRATLLRLGEDEHVLLLTMHHIVSDGWSMGVLLRELAALYAAFla 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1100 ----ELHDLPVQYVDFAQWQTSAPVVEDLRRQEQFWQSMFADYRPLPGIPTDHTPEAnERSFAGGHITWEPDPVLSRRLY 1175
Cdd:cd19531   160 grpsPLPPLPIQYADYAVWQREWLQGEVLERQLAYWREQLAGAPPVLELPTDRPRPA-VQSFRGARVRFTLPAELTAALR 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1176 AVAAEQQTTLFMVLLAAFHVLYAKYSAREEVTVGTPVEGRRRAEVRQVVGMFVNALAIRSYPEGDKPFSSFLQEIRGTML 1255
Cdd:cd19531   239 ALARREGATLFMTLLAAFQVLLHRYSGQDDIVVGTPVAGRNRAELEGLIGFFVNTLVLRTDLSGDPTFRELLARVRETAL 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1256 QAYEHQDYPLERLAKQLDLHHSRDH--LmFDTVFSMLNYEDFAVRSDDLQFEYAELPTLSEIYNLRVEIVESPERLRGTF 1333
Cdd:cd19531   319 EAYAHQDLPFEKLVEALQPERDLSRspL-FQVMFVLQNAPAAALELPGLTVEPLEVDSGTAKFDLTLSLTETDGGLRGSL 397

                         410       420       430
                  ....*....|....*....|....*....|
gi 517718121 1334 KYGQELYEARTVSQLAQDYERILAAVAESP 1363
Cdd:cd19531   398 EYNTDLFDAATIERMAGHFQTLLEAIVADP 427
A_NRPS cd05930
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ...
 17-449 1.17e-129

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: 408.07  E-value: 1.17e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   17 PERKAIECGQQTLSYKELDAESDRICELLHAHGAAQYDHIGILMQDRCASIAAVIGILKLGGVFVPLDPLHPDERLVTML 96
Cdd:cd05930     1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   97 DTAEVSCLLCDdaqferaetlqghegkyfvlrarqamsvqagskeayshsanATDPIYIYFTSGSTGKPKAVVGKNESLL 176
Cdd:cd05930    81 EDSGAKLVLTD-----------------------------------------PDDLAYVIYTSGSTGKPKGVMVEHRGLV 119

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  177 HFMNWEASWLDLTDPMRVSQLTSIGFDAVLRDIFVPICAGGTICIPEsREIILDPLRLVHWLEHSRVHVVHCTPSLFR-F 255
Cdd:cd05930   120 NLLLWMQEAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLP-EEVRKDPEALADLLAEEGITVLHLTPSLLRlL 198

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  256 INHLSLTAdsYPDLRYVLLAGETIRPESLKNWYDnLGNRVRLVNLYGPTETTMIKLFYPIKPEDVHRESIPIGRPLPDTS 335
Cdd:cd05930   199 LQELELAA--LPSLRLVLVGGEALPPDLVRRWRE-LLPGARLVNLYGPTEATVDATYYRVPPDDEEDGRVPIGRPIPNTR 275

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  336 VYLLDEQQQPVSGSEAGEICIATRYMTHGYFPSshPDQTA--FIPDPCRdqsGEIMMYRTGDMGRWLPEGELALLGRKDN 413
Cdd:cd05930   276 VYVLDENLRPVPPGVPGELYIGGAGLARGYLNR--PELTAerFVPNPFG---PGERMYRTGDLVRWLPDGNLEFLGRIDD 350

                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 517718121  414 QVKIRGNRVELGDIEHRLTNMAGIREAVVRMRAKAD 449
Cdd:cd05930   351 QVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGD 386
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
 14-442 3.39e-120

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: 407.71  E-value: 3.39e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   14 AAFPERKAIECGQQTLSYKELDAESDRICELLHAHGAAQYDHIGILMqDRCA-SIAAVIGILKLGGVFVPLDPLHPDERL 92
Cdd:COG1020   487 ARTPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCL-ERSLeMVVALLAVLKAGAAYVPLDPAYPAERL 565

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   93 VTMLDTAEVSCLLCDDAQferAETLQGHEGKYFVLrarQAMSVQAGSKEAYSHSANATDPIYIYFTSGSTGKPKAVVGKN 172
Cdd:COG1020   566 AYMLEDAGARLVLTQSAL---AARLPELGVPVLAL---DALALAAEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEH 639

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  173 ESLLHFMNWEASWLDLTDPMRVSQLTSIGFDAVLRDIFVPICAGGTICIPeSREIILDPLRLVHWLEHSRVHVVHCTPSL 252
Cdd:COG1020   640 RALVNLLAWMQRRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATLVLA-PPEARRDPAALAELLARHRVTVLNLTPSL 718

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  253 FR-FINHLsltADSYPDLRYVLLAGETIRPESLKNWYDNLGnRVRLVNLYGPTETTMIKLFYPIKPEDVHRESIPIGRPL 331
Cdd:COG1020   719 LRaLLDAA---PEALPSLRLVLVGGEALPPELVRRWRARLP-GARLVNLYGPTETTVDSTYYEVTPPDADGGSVPIGRPI 794

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  332 PDTSVYLLDEQQQPVSGSEAGEICIATRYMTHGYFpsSHPDQTA--FIPDPCrDQSGEIMmYRTGDMGRWLPEGELALLG 409
Cdd:COG1020   795 ANTRVYVLDAHLQPVPVGVPGELYIGGAGLARGYL--NRPELTAerFVADPF-GFPGARL-YRTGDLARWLPDGNLEFLG 870

                         410       420       430
                  ....*....|....*....|....*....|...
gi 517718121  410 RKDNQVKIRGNRVELGDIEHRLTNMAGIREAVV 442
Cdd:COG1020   871 RADDQVKIRGFRIELGEIEAALLQHPGVREAVV 903
PRK12467 PRK12467
peptide synthase; Provisional
 783-1375 3.45e-115

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 401.46  E-value: 3.45e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  783 VQLQVEEAQEPLLIAYYLADKMIDD-------EQLSVYLRRFLPDYMIPARFIRLDKMPLTPNGKLDYNALPSPfEQDTT 855
Cdd:PRK12467  942 VVLAQPGDAGLQLVAYLVPAAVADGaehqatrDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKALPKP-DASAV 1020

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  856 ARIYKAPNSSTELKLLDIWTHILGIKRISADDHFLQIGVHSLNIMTLIAQVYENFQVELPLEQVFEHDTLEEIAAYIDEQ 935
Cdd:PRK12467 1021 QATFVAPQTELEKRLAAIWADVLKVERVGLTDNFFELGGHSLLATQVISRVRQRLGIQVPLRTLFEHQTLAGFAQAVAAQ 1100

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  936 DSQYGVRIEPAAKQAYYPLTAAQMRVFMDEQLVNTGSGYHITTAFMIYGPIDVTRLERACGQLIERHEALRTSFDIVDGD 1015
Cdd:PRK12467 1101 QQGAQPALPDVDRDQPLPLSYAQERQWFLWQLEPGSAAYHIPQALRLKGPLDIEALERSFDALVARHESLRTTFVQEDGR 1180

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1016 PVQRIHEHCDFHLEIVHLQG-----QQLHTAVNGCIR-PFQLERAPLIRSILIPLAEEQHLLVLDMHHIVADGKSVFLLQ 1089
Cdd:PRK12467 1181 TRQVIHPVGSLTLEEPLLLAadkdeAQLKVYVEAEARqPFDLEQGPLLRVGLLRLAADEHVLVLTLHHIVSDGWSMQVLV 1260

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1090 RDLAALYEGR------ELHDLPVQYVDFAQWQTSAPVVEDLRRQEQFWQSMFADYRPLPGIPTDHtPEANERSFAGGHIT 1163
Cdd:PRK12467 1261 DELVALYAAYsqgqslQLPALPIQYADYAVWQRQWMDAGERARQLAYWKAQLGGEQPVLELPTDR-PRPAVQSHRGARLA 1339

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1164 WEPDPVLSRRLYAVAAEQQTTLFMVLLAAFHVLYAKYSAREEVTVGTPVEGRRRAEVRQVVGMFVNALAIRSYPEGDKPF 1243
Cdd:PRK12467 1340 FELPPALAEGLRALARREGVTLFMLLLASFQTLLHRYSGQDDIRVGVPIANRNRAETEGLIGFFVNTQVLRAEVDGQASF 1419

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1244 SSFLQEIRGTMLQAYEHQDYPLERLAKQLDLHHSRDH-----LMFD---TVFSM------LNYEDFAVRSDDLQFEyael 1309
Cdd:PRK12467 1420 QQLLQQVKQAALEAQAHQDLPFEQLVEALQPERSLSHsplfqVMFNhqrDDHQAqaqlpgLSVESLSWESQTAQFD---- 1495

                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517718121 1310 ptlseiynLRVEIVESPERLRGTFKYGQELYEARTVSQLAQDYERILAAVAESPNIKLKDIEIRTP 1375
Cdd:PRK12467 1496 --------LTLDTYESSEGLQASLTYATDLFEASTIERLAGHWLNLLQGLVADPERRLGELDLLDE 1553
AA-adenyl-dom TIGR01733
amino acid adenylation domain; This model represents a domain responsible for the specific ...
 30-442 5.46e-111

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: 356.19  E-value: 5.46e-111
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121    30 SYKELDAESDRICELLHAHGAAQY-DHIGILMqDRCAS-IAAVIGILKLGGVFVPLDPLHPDERLVTMLDTAEVSCLLCD 107
Cdd:TIGR01733    1 TYRELDERANRLARHLRAAGGVGPgDRVAVLL-ERSAElVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTD 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   108 DAQFERAETLQGHEGkyfVLRARQAMSVQAGSKEAYSHS-ANATDPIYIYFTSGSTGKPKAVVGKNESLLHFMNWEASWL 186
Cdd:TIGR01733   80 SALASRLAGLVLPVI---LLDPLELAALDDAPAPPPPDApSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRY 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   187 DLTDPMRVSQLTSIGFDAVLRDIFVPICAGGTICIPESREIILDPLRLVHWLEHSRVHVVHCTPSLFRfinHLSLTADSY 266
Cdd:TIGR01733  157 GLDPDDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAALLAALIAEHPVTVLNLTPSLLA---LLAAALPPA 233

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   267 PD-LRYVLLAGETIRPESLKNWYDNLGNrVRLVNLYGPTETTMIKLFYPIKPEDVHRES-IPIGRPLPDTSVYLLDEQQQ 344
Cdd:TIGR01733  234 LAsLRLVILGGEALTPALVDRWRARGPG-ARLINLYGPTETTVWSTATLVDPDDAPRESpVPIGRPLANTRLYVLDDDLR 312

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   345 PVSGSEAGEICIATRYMTHGYFpsSHPDQTA--FIPDPCRDQSGEiMMYRTGDMGRWLPEGELALLGRKDNQVKIRGNRV 422
Cdd:TIGR01733  313 PVPVGVVGELYIGGPGVARGYL--NRPELTAerFVPDPFAGGDGA-RLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRI 389

                          410       420
                   ....*....|....*....|
gi 517718121   423 ELGDIEHRLTNMAGIREAVV 442
Cdd:TIGR01733  390 ELGEIEAALLRHPGVREAVV 409
A_NRPS_Srf_like cd12117
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ...
 10-452 2.02e-101

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: 332.63  E-value: 2.02e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   10 ARAFAAFPERKAIECGQQTLSYKELDAESDRICELLHAHGAAQYDHIGILMQDRCASIAAVIGILKLGGVFVPLDPLHPD 89
Cdd:cd12117     4 EEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELPA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   90 ERLVTMLDTAEVSCLLCDdaqfeRAETLQGHEGKYFVLRARQAMsvqAGSKEAYSHSANATDPIYIYFTSGSTGKPKAVV 169
Cdd:cd12117    84 ERLAFMLADAGAKVLLTD-----RSLAGRAGGLEVAVVIDEALD---AGPAGNPAVPVSPDDLAYVMYTSGSTGRPKGVA 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  170 GKNESLLHFMNwEASWLDLTDPMRVSQLTSIGFDAVLRDIFVPICAGGTiCIPESREIILDPLRLVHWLEHSRVHVVHCT 249
Cdd:cd12117   156 VTHRGVVRLVK-NTNYVTLGPDDRVLQTSPLAFDASTFEIWGALLNGAR-LVLAPKGTLLDPDALGALIAEEGVTVLWLT 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  250 PSLFRFInhlsltADSYPD----LRYVLLAGETIRPESLKNWYDNLGnRVRLVNLYGPTETTMIKLFYPIKPEDVHRESI 325
Cdd:cd12117   234 AALFNQL------ADEDPEcfagLRELLTGGEVVSPPHVRRVLAACP-GLRLVNGYGPTENTTFTTSHVVTELDEVAGSI 306

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  326 PIGRPLPDTSVYLLDEQQQPVSGSEAGEICIATRYMTHGYFpsSHPDQTA--FIPDPcrDQSGEiMMYRTGDMGRWLPEG 403
Cdd:cd12117   307 PIGRPIANTRVYVLDEDGRPVPPGVPGELYVGGDGLALGYL--NRPALTAerFVADP--FGPGE-RLYRTGDLARWLPDG 381

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*....
gi 517718121  404 ELALLGRKDNQVKIRGNRVELGDIEHRLTNMAGIREAVVRMRAKADTPK 452
Cdd:cd12117   382 RLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGDK 430
A_NRPS_VisG_like cd17651
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ...
 9-445 1.41e-100

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: 330.46  E-value: 1.41e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121    9 LARAFAAFPERKAIECGQQTLSYKELDAESDRICELLHAHGAAQYDHIGILMqDRCAS-IAAVIGILKLGGVFVPLDPLH 87
Cdd:cd17651     1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCA-RRSAElVVALLAILKAGAAYVPLDPAY 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   88 PDERLVTMLDTAEVSCLLCDDAQFERAETLQGhegkyFVLRARQAMSVQAGSKEaysHSA--NATDPIYIYFTSGSTGKP 165
Cdd:cd17651    80 PAERLAFMLADAGPVLVLTHPALAGELAVELV-----AVTLLDQPGAAAGADAE---PDPalDADDLAYVIYTSGSTGRP 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  166 KAVVGKNESLLHFMNWEASWLDLTDPMRVSQLTSIGFDAVLRDIFVPICAGGTICIPeSREIILDPLRLVHWLEHSRVHV 245
Cdd:cd17651   152 KGVVMPHRSLANLVAWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVLP-PEEVRTDPPALAAWLDEQRISR 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  246 VHC-TPSLFRFINHLSLTADSYPDLRYVLLAGETIRP-ESLKNWYDNLGNRvRLVNLYGPTETTMIKLFYPIKPEDVHRE 323
Cdd:cd17651   231 VFLpTVALRALAEHGRPLGVRLAALRYLLTGGEQLVLtEDLREFCAGLPGL-RLHNHYGPTETHVVTALSLPGDPAAWPA 309

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  324 SIPIGRPLPDTSVYLLDEQQQPVSGSEAGEICIATRYMTHGYFpsSHPDQTA--FIPDPcrdQSGEIMMYRTGDMGRWLP 401
Cdd:cd17651   310 PPPIGRPIDNTRVYVLDAALRPVPPGVPGELYIGGAGLARGYL--NRPELTAerFVPDP---FVPGARMYRTGDLARWLP 384

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....
gi 517718121  402 EGELALLGRKDNQVKIRGNRVELGDIEHRLTNMAGIREAVVRMR 445
Cdd:cd17651   385 DGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAR 428
Condensation pfam00668
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ...
 948-1372 1.54e-95

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: 315.43  E-value: 1.54e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   948 KQAYYPLTAAQMRVFMDEQLVNTGSGYHITTAFMIYGPIDVTRLERACGQLIERHEALRTSFDI-VDGDPVQRIHEHCDF 1026
Cdd:pfam00668    1 VQDEYPLSPAQKRMWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIRqENGEPVQVILEERPF 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  1027 HL---EIVHLQGQQLHTAVNGCIR-----PFQLERAPLIRSILIPLAEEQHLLVLDMHHIVADGKSVFLLQRDLAALYE- 1097
Cdd:pfam00668   81 ELeiiDISDLSESEEEEAIEAFIQrdlqsPFDLEKGPLFRAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLYQq 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  1098 ---GRELHDLPVQ-YVDFAQWQTSAPVVEDLRRQEQFWQSMFADYRPLPGIPTDHTPEANeRSFAGGHITWEPDPVLSRR 1173
Cdd:pfam00668  161 llkGEPLPLPPKTpYKDYAEWLQQYLQSEDYQKDAAYWLEQLEGELPVLQLPKDYARPAD-RSFKGDRLSFTLDEDTEEL 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  1174 LYAVAAEQQTTLFMVLLAAFHVLYAKYSAREEVTVGTPVEGRRRAEVRQVVGMFVNALAIRSYPEGDKPFSSFLQEIRGT 1253
Cdd:pfam00668  240 LRKLAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPSPDIERMVGMFVNTLPLRIDPKGGKTFSELIKRVQED 319

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  1254 MLQAYEHQDYPLERLAKQLDLHHS-RDHLMFDTVFSMLNYedfavrsdDLQFEYAELPTLSEI-------------YNLR 1319
Cdd:pfam00668  320 LLSAEPHQGYPFGDLVNDLRLPRDlSRHPLFDPMFSFQNY--------LGQDSQEEEFQLSELdlsvssvieeeakYDLS 391

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|...
gi 517718121  1320 VEIVESPERLRGTFKYGQELYEARTVSQLAQDYERILAAVAESPNIKLKDIEI 1372
Cdd:pfam00668  392 LTASERGGGLTIKIDYNTSLFDEETIERFAEHFKELLEQAIAHPSQPLSELDL 444
PRK12316 PRK12316
peptide synthase; Provisional
 783-1376 9.68e-95

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 338.86  E-value: 9.68e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  783 VQLQVEEAQEPLLIAYYLADKMIDD--EQLSVYLRRFLPDYMIPARFIRLDKMPLTPNGKLDYNALPSPfEQDTTARIYK 860
Cdd:PRK12316 2433 VVVAQDGASGKQLVAYVVPDDAAEDllAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALPKP-DVSQLRQAYV 2511

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  861 APNSSTELKLLDIWTHILGIKRISADDHFLQIGVHSLNIMTLIAQVYENFQVELPLEQVFEHDTLEEIAAYIDEQDSQYG 940
Cdd:PRK12316 2512 APQEGLEQRLAAIWQAVLKVEQVGLDDHFFELGGHSLLATQVVSRVRQDLGLEVPLRILFERPTLAAFAASLESGQTSRA 2591

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  941 VRIEPAAKQAYYPLTAAQMRVFMDEQLVNTGSGYHITTAFMIYGPIDVTRLERACGQLIERHEALRTSFDIVDGDPVQRI 1020
Cdd:PRK12316 2592 PVLQKVTRVQPLPLSHAQQRQWFLWQLEPESAAYHLPSALHLRGVLDQAALEQAFDALVLRHETLRTRFVEVGEQTRQVI 2671

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1021 HEHCDFHLEIVHLQ----GQQLHTAVNGCIRPFQLERAPLIRSILIPLAEEQHLLVLDMHHIVADGKSVFLLQRDLAALY 1096
Cdd:PRK12316 2672 LPNMSLRIVLEDCAgvadAAIRQRVAEEIQRPFDLARGPLLRVRLLALDGQEHVLVITQHHIVSDGWSMQVMVDELVQAY 2751

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1097 EGR------ELHDLPVQYVDFAQWQTSAPVVEDLRRQEQFWQSMFADYRPLPGIPTDHtPEANERSFAGGHITWEPDPVL 1170
Cdd:PRK12316 2752 AGArrgeqpTLPPLPLQYADYAAWQRAWMDSGEGARQLDYWRERLGGEQPVLELPLDR-PRPALQSHRGARLDVALDVAL 2830

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1171 SRRLYAVAAEQQTTLFMVLLAAFHVLYAKYSAREEVTVGTPVEGRRRAEVRQVVGMFVNALAIRSYPEGDKPFSSFLQEI 1250
Cdd:PRK12316 2831 SRELLALARREGVTLFMLLLASFQVLLHRYSGQSDIRVGVPIANRNRAETERLIGFFVNTQVLRAQVDAQLAFRDLLGQV 2910

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1251 RGTMLQAYEHQDYPLERLAKQLDLHHSRDH-LMFDTVFSMLNYEDFAVRSDDLQFEYAELPTLSEIYNLRVEIVESPERL 1329
Cdd:PRK12316 2911 KEQALGAQAHQDLPFEQLVEALQPERSLSHsPLFQVMYNHQSGERAAAQLPGLHIESFAWDGAATQFDLALDTWESAEGL 2990

                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....*..
gi 517718121 1330 RGTFKYGQELYEARTVSQLAQDYERILAAVAESPNIKLKDIEIRTPQ 1376
Cdd:PRK12316 2991 GASLTYATDLFDARTVERLARHWQNLLRGMVENPQRSVDELAMLDAE 3037
A_NRPS_Ta1_like cd12116
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ...
 17-445 2.60e-94

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: 312.30  E-value: 2.60e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   17 PERKAIECGQQTLSYKELDAESDRICELLHAHGAAQYDHIGILMQDRCASIAAVIGILKLGGVFVPLDPLHPDERLVTML 96
Cdd:cd12116     1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   97 DTAEVSCLLCDDAQFERaetlqghegkyFVLRARQAMSVQAGSKEAYSHSANATDP---IYIYFTSGSTGKPKAVVGKNE 173
Cdd:cd12116    81 EDAEPALVLTDDALPDR-----------LPAGLPVLLLALAAAAAAPAAPRTPVSPddlAYVIYTSGSTGRPKGVVVSHR 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  174 SLLHFMNWEASWLDLTDPMRVSQLTSIGFDAVLRDIFVPICAGGTICIpESREIILDPLRLVHWLEHSRVHVVHCTPSLF 253
Cdd:cd12116   150 NLVNFLHSMRERLGLGPGDRLLAVTTYAFDISLLELLLPLLAGARVVI-APRETQRDPEALARLIEAHSITVMQATPATW 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  254 RfinhLSLTADSYPDLRYVLLAGETIRPESLKnwyDNLGNRVR-LVNLYGPTETTMIKLFYPIKPEDVHresIPIGRPLP 332
Cdd:cd12116   229 R----MLLDAGWQGRAGLTALCGGEALPPDLA---ARLLSRVGsLWNLYGPTETTIWSTAARVTAAAGP---IPIGRPLA 298

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  333 DTSVYLLDEQQQPVSGSEAGEICIATRYMTHGYFpsSHPDQTA--FIPDPCRDQSGEimMYRTGDMGRWLPEGELALLGR 410
Cdd:cd12116   299 NTQVYVLDAALRPVPPGVPGELYIGGDGVAQGYL--GRPALTAerFVPDPFAGPGSR--LYRTGDLVRRRADGRLEYLGR 374

                         410       420       430
                  ....*....|....*....|....*....|....*
gi 517718121  411 KDNQVKIRGNRVELGDIEHRLTNMAGIREAVVRMR 445
Cdd:cd12116   375 ADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVR 409
A_NRPS_Bac cd17655
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ...
 17-442 9.43e-94

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: 311.57  E-value: 9.43e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   17 PERKAIECGQQTLSYKELDAESDRICELLHAHGAAQYDHIGILMQDRCASIAAVIGILKLGGVFVPLDPLHPDERLVTML 96
Cdd:cd17655    11 PDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEERIQYIL 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   97 DTAEVSCLLCDDAQferaETLQGHEGKYFVLRARQamsVQAGSKEAYSHSANATDPIYIYFTSGSTGKPKAVVGKNESLL 176
Cdd:cd17655    91 EDSGADILLTQSHL----QPPIAFIGLIDLLDEDT---IYHEESENLEPVSKSDDLAYVIYTSGSTGKPKGVMIEHRGVV 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  177 HFMNWEASWLDLTDPMRVSQLTSIGFDAVLRDIFVPICAGGTICIpESREIILDPLRLVHWLEHSRVHVVHCTPSLFRFI 256
Cdd:cd17655   164 NLVEWANKVIYQGEHLRVALFASISFDASVTEIFASLLSGNTLYI-VRKETVLDGQALTQYIRQNRITIIDLTPAHLKLL 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  257 NHLSLTadSYPDLRYVLLAGETIRPESLKNWYDNLGNRVRLVNLYGPTETTMIKLFYPIKPEDVHRESIPIGRPLPDTSV 336
Cdd:cd17655   243 DAADDS--EGLSLKHLIVGGEALSTELAKKIIELFGTNPTITNAYGPTETTVDASIYQYEPETDQQVSVPIGKPLGNTRI 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  337 YLLDEQQQPVSGSEAGEICIATRYMTHGYFpsSHPDQTA--FIPDPCRdqSGEiMMYRTGDMGRWLPEGELALLGRKDNQ 414
Cdd:cd17655   321 YILDQYGRPQPVGVAGELYIGGEGVARGYL--NRPELTAekFVDDPFV--PGE-RMYRTGDLARWLPDGNIEFLGRIDHQ 395

                         410       420
                  ....*....|....*....|....*...
gi 517718121  415 VKIRGNRVELGDIEHRLTNMAGIREAVV 442
Cdd:cd17655   396 VKIRGYRIELGEIEARLLQHPDIKEAVV 423
A_NRPS_AB3403-like cd17646
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ...
 9-449 1.85e-93

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: 310.75  E-value: 1.85e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121    9 LARAFAAFPERKAIECGQQTLSYKELDAESDRICELLHAHGAAQYDHIGILMQDRCASIAAVIGILKLGGVFVPLDPLHP 88
Cdd:cd17646     4 VAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYP 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   89 DERLVTMLDTAEVSCLLCDDAQFERAETLQGHEgkyfVLRARQAMSVQAGSKEAYSHSANatdPIYIYFTSGSTGKPKAV 168
Cdd:cd17646    84 ADRLAYMLADAGPAVVLTTADLAARLPAGGDVA----LLGDEALAAPPATPPLVPPRPDN---LAYVIYTSGSTGRPKGV 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  169 VGKNESLLHFMNWEASWLDLTDPMRVSQLTSIGFDAVLRDIFVPICAGGTICIPES---ReiilDPLRLVHWLEHSRVHV 245
Cdd:cd17646   157 MVTHAGIVNRLLWMQDEYPLGPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVARPgghR----DPAYLAALIREHGVTT 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  246 VHCTPSLFR-FINhlSLTADSYPDLRYVLLAGETIRPESLKNWYDNLGnrVRLVNLYGPTETTMIKLFYPIKPEDVhRES 324
Cdd:cd17646   233 CHFVPSMLRvFLA--EPAAGSCASLRRVFCSGEALPPELAARFLALPG--AELHNLYGPTEAAIDVTHWPVRGPAE-TPS 307

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  325 IPIGRPLPDTSVYLLDEQQQPVSGSEAGEICIATRYMTHGYFpsSHPDQTA--FIPDPCRDQSgeiMMYRTGDMGRWLPE 402
Cdd:cd17646   308 VPIGRPVPNTRLYVLDDALRPVPVGVPGELYLGGVQLARGYL--GRPALTAerFVPDPFGPGS---RMYRTGDLARWRPD 382

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*..
gi 517718121  403 GELALLGRKDNQVKIRGNRVELGDIEHRLTNMAGIREAVVRMRAKAD 449
Cdd:cd17646   383 GALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPA 429
DltA cd05945
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ...
 14-450 1.04e-89

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: 298.78  E-value: 1.04e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   14 AAFPERKAIECGQQTLSYKELDAESDRICELLHAHGAAQYDHIGILMQDRCASIAAVIGILKLGGVFVPLDPLHPDERLV 93
Cdd:cd05945     2 AANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERIR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   94 TMLDTAEVSCLLCDDaqferaetlqghegkyfvlrarqamsvqagskeayshsanaTDPIYIYFTSGSTGKPKAVVGKNE 173
Cdd:cd05945    82 EILDAAKPALLIADG-----------------------------------------DDNAYIIFTSGSTGRPKGVQISHD 120

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  174 SLLHFMNWEASWLDLTDPMRVSQLTSIGFDAVLRDIFVPICAGGTiCIPESREIILDPLRLVHWLEHSRVHVVHCTPSLF 253
Cdd:cd05945   121 NLVSFTNWMLSDFPLGPGDVFLNQAPFSFDLSVMDLYPALASGAT-LVPVPRDATADPKQLFRFLAEHGITVWVSTPSFA 199

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  254 RF-INHLSLTADSYPDLRYVLLAGETIRPESLKNWYDNLGNRvRLVNLYGPTETTMIKLFYPIKPEDVHR-ESIPIGRPL 331
Cdd:cd05945   200 AMcLLSPTFTPESLPSLRHFLFCGEVLPHKTARALQQRFPDA-RIYNTYGPTEATVAVTYIEVTPEVLDGyDRLPIGYAK 278

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  332 PDTSVYLLDEQQQPVSGSEAGEICIATRYMTHGYFPSSHPDQTAFIPDPCRdqsgeiMMYRTGDMGRWLPEGELALLGRK 411
Cdd:cd05945   279 PGAKLVILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDEGQ------RAYRTGDLVRLEADGLLFYRGRL 352

                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 517718121  412 DNQVKIRGNRVELGDIEHRLTNMAGIREAVVRMRAKADT 450
Cdd:cd05945   353 DFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEK 391
A_NRPS_Cytc1-like cd17643
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ...
 17-445 2.43e-89

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: 297.68  E-value: 2.43e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   17 PERKAIECGQQTLSYKELDAESDRICELLHAHGAAQYDHIGILMQDRCASIAAVIGILKLGGVFVPLDPLHPDERLVTML 96
Cdd:cd17643     1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   97 DTAEVSCLLCDdaqferaetlqghegkyfvlrarqamsvqagskeayshsanATDPIYIYFTSGSTGKPKAVVGKNESLL 176
Cdd:cd17643    81 ADSGPSLLLTD-----------------------------------------PDDLAYVIYTSGSTGRPKGVVVSHANVL 119

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  177 HFMNWEASWLDLTDPMRVSQLTSIGFDAVLRDIFVPICAGGTICIPEsREIILDPLRLVHWLEHSRVHVVHCTPSLFR-F 255
Cdd:cd17643   120 ALFAATQRWFGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVP-YEVARSPEDFARLLRDEGVTVLNQTPSAFYqL 198

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  256 INHLSLTADSYPDLRYVLLAGETIRPESLKNWYDNLGN-RVRLVNLYGPTETTMIKLFYPIKPEDVH-RESIPIGRPLPD 333
Cdd:cd17643   199 VEAADRDGRDPLALRYVIFGGEALEAAMLRPWAGRFGLdRPQLVNMYGITETTVHVTFRPLDAADLPaAAASPIGRPLPG 278

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  334 TSVYLLDEQQQPVSGSEAGEICIATRYMTHGYFpsSHPDQTA--FIPDPcrDQSGEIMMYRTGDMGRWLPEGELALLGRK 411
Cdd:cd17643   279 LRVYVLDADGRPVPPGVVGELYVSGAGVARGYL--GRPELTAerFVANP--FGGPGSRMYRTGDLARRLPDGELEYLGRA 354

                         410       420       430
                  ....*....|....*....|....*....|....
gi 517718121  412 DNQVKIRGNRVELGDIEHRLTNMAGIREAVVRMR 445
Cdd:cd17643   355 DEQVKIRGFRIELGEIEAALATHPSVRDAAVIVR 388
A_NRPS_GliP_like cd17653
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ...
 14-444 1.35e-87

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: 292.29  E-value: 1.35e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   14 AAFPERKAIECGQQTLSYKELDAESDRICELLHAHGAAQYDHIGILMQDRCASIAAVIGILKLGGVFVPLDPLHPDERLV 93
Cdd:cd17653     8 AAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLPSARIQ 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   94 TMLDTAEVSCLLCDDAQferaetlqghegkyfvlrarqamsvqagskeayshsanaTDPIYIYFTSGSTGKPKAVVGKNE 173
Cdd:cd17653    88 AILRTSGATLLLTTDSP---------------------------------------DDLAYIIFTSGSTGIPKGVMVPHR 128

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  174 SLLHFMNWEASWLDLTDPMRVSQLTSIGFDAVLRDIFVPICAGGTICIPESREIILDPLRlvhwlehsRVHVVHCTPSLf 253
Cdd:cd17653   129 GVLNYVSQPPARLDVGPGSRVAQVLSIAFDACIGEIFSTLCNGGTLVLADPSDPFAHVAR--------TVDALMSTPSI- 199

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  254 rfinhLS-LTADSYPDLRYVLLAGETIRPESLKNWydnlGNRVRLVNLYGPTETTMIKLFYPIKPEDvhreSIPIGRPLP 332
Cdd:cd17653   200 -----LStLSPQDFPNLKTIFLGGEAVPPSLLDRW----SPGRRLYNAYGPTECTISSTMTELLPGQ----PVTIGKPIP 266

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  333 DTSVYLLDEQQQPVSGSEAGEICIATRYMTHGYFPSshPDQTA--FIPDPcrDQSGEiMMYRTGDMGRWLPEGELALLGR 410
Cdd:cd17653   267 NSTCYILDADLQPVPEGVVGEICISGVQVARGYLGN--PALTAskFVPDP--FWPGS-RMYRTGDYGRWTEDGGLEFLGR 341

                         410       420       430
                  ....*....|....*....|....*....|....*
gi 517718121  411 KDNQVKIRGNRVELGDIEHR-LTNMAGIREAVVRM 444
Cdd:cd17653   342 EDNQVKVRGFRINLEEIEEVvLQSQPEVTQAAAIV 376
PRK05691 PRK05691
peptide synthase; Validated
 838-1372 5.10e-87

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 314.80  E-value: 5.10e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  838 NGKLDYNALpSPFEQDTTARIYKAPNSSTELKLLDIWTHILGIKRISADDHFLQIGVHSLNIMTLIAQVYENFQVELPLE 917
Cdd:PRK05691  560 DGSLDSYAL-FPALQAVEAAQTAASGDELQARIAAIWCEQLKVEQVAADDHFFLLGGNSIAATQVVARLRDELGIDLNLR 638

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  918 QVFEHDTLEEIAAYIDEQDSQYGV---RIEPAAKQAYYPLTAAQMRVFMDEQLVNTGSGYHITTAFMIYGPIDVTRLERA 994
Cdd:PRK05691  639 QLFEAPTLAAFSAAVARQLAGGGAaqaAIARLPRGQALPQSLAQNRLWLLWQLDPQSAAYNIPGGLHLRGELDEAALRAS 718

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  995 CGQLIERHEALRTSFDIVDGDPVQRIHEHCDFHLEIVHLQGQQLH--TAVNGCIR------PFQLERAPLIRSILIPLAE 1066
Cdd:PRK05691  719 FQRLVERHESLRTRFYERDGVALQRIDAQGEFALQRIDLSDLPEAerEARAAQIReeearqPFDLEKGPLLRVTLVRLDD 798

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1067 EQHLLVLDMHHIVADGKSVFLLQRDLAALYEGR------ELHDLPVQYVDFAQWQTSAPVVEDLRRQEQFWQSMFADYRP 1140
Cdd:PRK05691  799 EEHQLLVTLHHIVADGWSLNILLDEFSRLYAAAcqgqtaELAPLPLGYADYGAWQRQWLAQGEAARQLAYWKAQLGDEQP 878

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1141 LPGIPTDHTPEANERSFAGGHiTWEPDPVLSRRLYAVAAEQQTTLFMVLLAAFHVLYAKYSAREEVTVGTPVEGRRRAEV 1220
Cdd:PRK05691  879 VLELATDHPRSARQAHSAARY-SLRVDASLSEALRGLAQAHQATLFMVLLAAFQALLHRYSGQGDIRIGVPNANRPRLET 957

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1221 RQVVGMFVNALAIRSYPEGDKPFSSFLQEIRGTMLQAYEHQDYPLERLAKQLDlhHSRDHLMFDTVFSMLNYEDFAVRS- 1299
Cdd:PRK05691  958 QGLVGFFINTQVLRAQLDGRLPFTALLAQVRQATLGAQAHQDLPFEQLVEALP--QAREQGLFQVMFNHQQRDLSALRRl 1035

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517718121 1300 DDLQFEyaELPTLSE--IYNLRVEIVESPE-RLRGTFKYGQELYEARTVSQLAQDYERILAAVAESPNIKLKDIEI 1372
Cdd:PRK05691 1036 PGLLAE--ELPWHSReaKFDLQLHSEEDRNgRLTLSFDYAAELFDAATIERLAEHFLALLEQVCEDPQRALGDVQL 1109
A_NRPS_Sfm_like cd12115
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ...
 9-442 2.10e-86

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: 289.22  E-value: 2.10e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121    9 LARAFAAFPERKAIECGQQTLSYKELDAESDRICELLHAHGAAQYDHIGILMQDRCASIAAVIGILKLGGVFVPLDPLHP 88
Cdd:cd12115     5 VEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYP 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   89 DERLVTMLDTAEVSCLLCDdaqferaetlqghegkyfvlrarqamsvqagskeayshsanATDPIYIYFTSGSTGKPKAV 168
Cdd:cd12115    85 PERLRFILEDAQARLVLTD-----------------------------------------PDDLAYVIYTSGSTGRPKGV 123

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  169 VGKNESLLHFMNWEASWLDLTDPMRVSQLTSIGFDAVLRDIFVPICAGGTICIPESreiildPLRLVHWLEHSRVHVVHC 248
Cdd:cd12115   124 AIEHRNAAAFLQWAAAAFSAEELAGVLASTSICFDLSVFELFGPLATGGKVVLADN------VLALPDLPAAAEVTLINT 197

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  249 TPSLFRFInhlsLTADSYP-DLRYVLLAGETIRPESLKNWYDNLgNRVRLVNLYGPTETTMIKLFYPIKPEDVhrESIPI 327
Cdd:cd12115   198 VPSAAAEL----LRHDALPaSVRVVNLAGEPLPRDLVQRLYARL-QVERVVNLYGPSEDTTYSTVAPVPPGAS--GEVSI 270

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  328 GRPLPDTSVYLLDEQQQPVSGSEAGEICIATRYMTHGYFpsSHPDQTA--FIPDPCRDQSgeiMMYRTGDMGRWLPEGEL 405
Cdd:cd12115   271 GRPLANTQAYVLDRALQPVPLGVPGELYIGGAGVARGYL--GRPGLTAerFLPDPFGPGA---RLYRTGDLVRWRPDGLL 345

                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 517718121  406 ALLGRKDNQVKIRGNRVELGDIEHRLTNMAGIREAVV 442
Cdd:cd12115   346 EFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVV 382
PRK05691 PRK05691
peptide synthase; Validated
 788-1367 2.21e-86

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 312.87  E-value: 2.21e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  788 EEAQEPLLIAYYLADKMIDDEQLSVY--LRRFLPDYMIPARFIRLDKMPLTPNGKLDYNALPSPFEQdttARIYKAPNSS 865
Cdd:PRK05691 1562 EGAAGAQLVGYYTGEAGQEAEAERLKaaLAAELPEYMVPAQLIRLDQMPLGPSGKLDRRALPEPVWQ---QREHVEPRTE 1638

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  866 TELKLLDIWTHILGIKRISADDHFLQIGVHSLNIMTLIAQVYENFQVELPLEQVFEHDTLEEIAAYIdEQDSQYGVR--- 942
Cdd:PRK05691 1639 LQQQIAAIWREVLGLPRVGLRDDFFALGGHSLLATQIVSRTRQACDVELPLRALFEASELGAFAEQV-ARIQAAGERnsq 1717

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  943 --IEPAAKQAYYPLTAAQMRVFMDEQLVNTGSGYHITTAFMIYGPIDVTRLERACGQLIERHEALRTSFDIVDGDPVQRI 1020
Cdd:PRK05691 1718 gaIARVDRSQPVPLSYSQQRMWFLWQMEPDSPAYNVGGMARLSGVLDVDRFEAALQALILRHETLRTTFPSVDGVPVQQV 1797

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1021 HEHCDFHL---EIVHLQG-------QQLhtAVNGCIRPFQLERAPLIRSILIPLAEEQHLLVLDMHHIVADGKSVFLLQR 1090
Cdd:PRK05691 1798 AEDSGLRMdwqDFSALPAdarqqrlQQL--ADSEAHQPFDLERGPLLRACLVKAAEREHYFVLTLHHIVTEGWAMDIFAR 1875

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1091 DLAALYE----GRE--LHDLPVQYVDFAQWQTSAPVVEDLRRQEQFWQSMFADYRPLPGIPTDHtPEANERSFAGGHITW 1164
Cdd:PRK05691 1876 ELGALYEafldDREspLEPLPVQYLDYSVWQRQWLESGERQRQLDYWKAQLGNEHPLLELPADR-PRPPVQSHRGELYRF 1954

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1165 EPDPVLSRRLYAVAAEQQTTLFMVLLAAFHVLYAKYSAREEVTVGTPVEGRRRAEVRQVVGMFVNALAIRSYPEGDKPFS 1244
Cdd:PRK05691 1955 DLSPELAARVRAFNAQRGLTLFMTMTATLAALLYRYSGQRDLRIGAPVANRIRPESEGLIGAFLNTQVLRCQLDGQMSVS 2034

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1245 SFLQEIRGTMLQAYEHQDYPLERLAKQLDLHHSRDHlmfDTVFS-MLNYEDFAVRSD----DLQFEYAELPTLSEIYNLR 1319
Cdd:PRK05691 2035 ELLEQVRQTVIEGQSHQDLPFDHLVEALQPPRSAAY---NPLFQvMCNVQRWEFQQSrqlaGMTVEYLVNDARATKFDLN 2111

                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....*...
gi 517718121 1320 VEIVESPERLRGTFKYGQELYEARTVSQLAQDYERILAAVAESPNIKL 1367
Cdd:PRK05691 2112 LEVTDLDGRLGCCLTYSRDLFDEPRIARMAEHWQNLLEALLGDPQQRL 2159
A_NRPS_PvdJ-like cd17649
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ...
 17-442 5.10e-86

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: 288.50  E-value: 5.10e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   17 PERKAIECGQQTLSYKELDAESDRICELLHAHGAAQYDHIGILMQDRCASIAAVIGILKLGGVFVPLDPLHPDERLVTML 96
Cdd:cd17649     1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   97 DTAEVSCLLCddaqferaetlqgHEGKyfvlrarqamsvqagskeayshsanatDPIYIYFTSGSTGKPKAVVGKNESLL 176
Cdd:cd17649    81 EDSGAGLLLT-------------HHPR---------------------------QLAYVIYTSGSTGTPKGVAVSHGPLA 120

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  177 HFMNWEASWLDLTDPMRVSQLTSIGFDAVLRDIFVPICAGGTICIPeSREIILDPLRLVHWLEHSRVHVVHCTPS-LFRF 255
Cdd:cd17649   121 AHCQATAERYGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLR-PDELWASADELAEMVRELGVTVLDLPPAyLQQL 199

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  256 INHL-SLTADSYPDLRYVLLAGETIRPESLKNWydnLGNRVRLVNLYGPTETTMIKLFYPIKPEDVHR-ESIPIGRPLPD 333
Cdd:cd17649   200 AEEAdRTGDGRPPSLRLYIFGGEALSPELLRRW---LKAPVRLFNAYGPTEATVTPLVWKCEAGAARAgASMPIGRPLGG 276

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  334 TSVYLLDEQQQPVSGSEAGEICIATRYMTHGYFpsSHPDQTA--FIPDPcrdQSGEIM-MYRTGDMGRWLPEGELALLGR 410
Cdd:cd17649   277 RSAYILDADLNPVPVGVTGELYIGGEGLARGYL--GRPELTAerFVPDP---FGAPGSrLYRTGDLARWRDDGVIEYLGR 351

                         410       420       430
                  ....*....|....*....|....*....|..
gi 517718121  411 KDNQVKIRGNRVELGDIEHRLTNMAGIREAVV 442
Cdd:cd17649   352 VDHQVKIRGFRIELGEIEAALLEHPGVREAAV 383
A_NRPS_CmdD_like cd17652
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ...
 17-445 2.05e-84

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: 283.37  E-value: 2.05e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   17 PERKAIECGQQTLSYKELDAESDRICELLHAHGAAQYDHIGILMqDRCAS-IAAVIGILKLGGVFVPLDPLHPDERLVTM 95
Cdd:cd17652     1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALAL-PRSAElVVAILAVLKAGAAYLPLDPAYPAERIAYM 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   96 LDTAEVSCLLcddaqferaetlqghegkyfvlrarqamsvqagskeayshsANATDPIYIYFTSGSTGKPKAVVGKNESL 175
Cdd:cd17652    80 LADARPALLL-----------------------------------------TTPDNLAYVIYTSGSTGRPKGVVVTHRGL 118

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  176 LHFMNWEASWLDLTDPMRVSQLTSIGFDAVLRDIFVPICAGGTICIPESREIIL-DPLRLVhwLEHSRVHVVHCTPSLFR 254
Cdd:cd17652   119 ANLAAAQIAAFDVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELLPgEPLADL--LREHRITHVTLPPAALA 196

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  255 finhlSLTADSYPDLRYVLLAGETIRPESLKNWydnlGNRVRLVNLYGPTETTMIKLFY-PIKPEDVhresIPIGRPLPD 333
Cdd:cd17652   197 -----ALPPDDLPDLRTLVVAGEACPAELVDRW----APGRRMINAYGPTETTVCATMAgPLPGGGV----PPIGRPVPG 263

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  334 TSVYLLDEQQQPVSGSEAGEICIATRYMTHGYFpsSHPDQTA--FIPDPCRDQSGEimMYRTGDMGRWLPEGELALLGRK 411
Cdd:cd17652   264 TRVYVLDARLRPVPPGVPGELYIAGAGLARGYL--NRPGLTAerFVADPFGAPGSR--MYRTGDLARWRADGQLEFLGRA 339

                         410       420       430
                  ....*....|....*....|....*....|....
gi 517718121  412 DNQVKIRGNRVELGDIEHRLTNMAGIREAVVRMR 445
Cdd:cd17652   340 DDQVKIRGFRIELGEVEAALTEHPGVAEAVVVVR 373
LCL_NRPS-like cd19540
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ...
 953-1363 9.02e-84

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: 281.23  E-value: 9.02e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  953 PLTAAQMRV-FMDeQLVNTGSGYHITTAFMIYGPIDVTRLERACGQLIERHEALRTSFDIVDGDPVQRIH--EHCDFHLE 1029
Cdd:cd19540     3 PLSFAQQRLwFLN-RLDGPSAAYNIPLALRLTGALDVDALRAALADVVARHESLRTVFPEDDGGPYQVVLpaAEARPDLT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1030 IVHLQGQQLHTAVNGCI-RPFQLERAPLIRSILIPLAEEQHLLVLDMHHIVADGKSVFLLQRDLAALYEGR------ELH 1102
Cdd:cd19540    82 VVDVTEDELAARLAEAArRGFDLTAELPLRARLFRLGPDEHVLVLVVHHIAADGWSMAPLARDLATAYAARragrapDWA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1103 DLPVQYVDFAQWQTSAPVVED-----LRRQEQFWQSMFADyrpLPG---IPTDHtPEANERSFAGGHITWEPDPVLSRRL 1174
Cdd:cd19540   162 PLPVQYADYALWQRELLGDEDdpdslAARQLAYWRETLAG---LPEeleLPTDR-PRPAVASYRGGTVEFTIDAELHARL 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1175 YAVAAEQQTTLFMVLLAAFHVLYAKYSAREEVTVGTPVEGRRRAEVRQVVGMFVNALAIRSYPEGDKPFSSFLQEIRGTM 1254
Cdd:cd19540   238 AALAREHGATLFMVLHAALAVLLSRLGAGDDIPIGTPVAGRGDEALDDLVGMFVNTLVLRTDVSGDPTFAELLARVRETD 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1255 LQAYEHQDYPLERLAKQLDLHHSRDH--LmFDTVFSMLNYEDFAVRSDDLQFEYAELPTLSEIYNLRVEIVES------P 1326
Cdd:cd19540   318 LAAFAHQDVPFERLVEALNPPRSTARhpL-FQVMLAFQNTAAATLELPGLTVEPVPVDTGVAKFDLSFTLTERrdadgaP 396

                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 517718121 1327 ERLRGTFKYGQELYEARTVSQLAQDYERILAAVAESP 1363
Cdd:cd19540   397 AGLTGELEYATDLFDRSTAERLADRFVRVLEAVVADP 433
AMP-binding pfam00501
AMP-binding enzyme;
9-418 1.03e-83

AMP-binding enzyme;


Pssm-ID: 459834 [Multi-domain]  Cd Length: 417  Bit Score: 280.74  E-value: 1.03e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121     9 LARAFAAFPERKAIECG-QQTLSYKELDAESDRICELLHAHGAAQYDHIGILMQDRCASIAAVIGILKLGGVFVPLDPLH 87
Cdd:pfam00501    1 LERQAARTPDKTALEVGeGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121    88 PDERLVTMLDTAEVSCLLCDDAQ------------FERAETLQGHEGKYFVLRARQAMSVQAGSKEAYSHSANATDPIYI 155
Cdd:pfam00501   81 PAEELAYILEDSGAKVLITDDALkleellealgklEVVKLVLVLDRDPVLKEEPLPEEAKPADVPPPPPPPPDPDDLAYI 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   156 YFTSGSTGKPKAVVGKNESLLHFM----NWEASWLDLTDPMRVSQLTSIGFDA-VLRDIFVPICAGGTICIPEsREIILD 230
Cdd:pfam00501  161 IYTSGTTGKPKGVMLTHRNLVANVlsikRVRPRGFGLGPDDRVLSTLPLFHDFgLSLGLLGPLLAGATVVLPP-GFPALD 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   231 PLRLVHWLEHSRVHVVHCTPSLFRFI-NHLSLTADSYPDLRYVLLAGETIRPESLKNWYDNLGNRVrlVNLYGPTETTMI 309
Cdd:pfam00501  240 PAALLELIERYKVTVLYGVPTLLNMLlEAGAPKRALLSSLRLVLSGGAPLPPELARRFRELFGGAL--VNGYGLTETTGV 317

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   310 KLFYPikPEDVHRESIP-IGRPLPDTSVYLLDEQ-QQPVSGSEAGEICIATRYMTHGYFpsSHPDQTA--FIPDPcrdqs 385
Cdd:pfam00501  318 VTTPL--PLDEDLRSLGsVGRPLPGTEVKIVDDEtGEPVPPGEPGELCVRGPGVMKGYL--NDPELTAeaFDEDG----- 388

                          410       420       430
                   ....*....|....*....|....*....|...
gi 517718121   386 geimMYRTGDMGRWLPEGELALLGRKDNQVKIR 418
Cdd:pfam00501  389 ----WYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
LCL_NRPS cd19538
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ...
 953-1363 8.71e-82

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: 275.68  E-value: 8.71e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  953 PLTAAQMRVFMDEQLVNTGSGYHITTAFMIYGPIDVTRLERACGQLIERHEALRTSFDIVDGDPVQRIHEHCDFHLEIVH 1032
Cdd:cd19538     3 PLSFAQRRLWFLHQLEGPSATYNIPLVIKLKGKLDVQALQQALYDVVERHESLRTVFPEEDGVPYQLILEEDEATPKLEI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1033 LQ--GQQLHTAVNGCIR-PFQLERAPLIRSILIPLAEEQHLLVLDMHHIVADGKSVFLLQRDLAALYEGR------ELHD 1103
Cdd:cd19538    83 KEvdEEELESEINEAVRyPFDLSEEPPFRATLFELGENEHVLLLLLHHIAADGWSLAPLTRDLSKAYRARckgeapELAP 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1104 LPVQYVDFAQWQ-----TSAPVVEDLRRQEQFWQSMFADYRPLPGIPTDHtPEANERSFAGGHITWEPDPVLSRRLYAVA 1178
Cdd:cd19538   163 LPVQYADYALWQqellgDESDPDSLIARQLAYWKKQLAGLPDEIELPTDY-PRPAESSYEGGTLTFEIDSELHQQLLQLA 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1179 AEQQTTLFMVLLAAFHVLYAKYSAREEVTVGTPVEGRRRAEVRQVVGMFVNALAIRSYPEGDKPFSSFLQEIRGTMLQAY 1258
Cdd:cd19538   242 KDNNVTLFMVLQAGFAALLTRLGAGTDIPIGSPVAGRNDDSLEDLVGFFVNTLVLRTDTSGNPSFRELLERVKETNLEAY 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1259 EHQDYPLERLAKQLDLHHSRD-HLMFDTVFSMLNyedfavrSDDLQFEYAELPTLSEIYN-------LRVEIVE-----S 1325
Cdd:cd19538   322 EHQDIPFERLVEALNPTRSRSrHPLFQIMLALQN-------TPQPSLDLPGLEAKLELRTvgsakfdLTFELREqyndgT 394

                         410       420       430
                  ....*....|....*....|....*....|....*...
gi 517718121 1326 PERLRGTFKYGQELYEARTVSQLAQDYERILAAVAESP 1363
Cdd:cd19538   395 PNGIEGFIEYRTDLFDHETIEALAQRYLLLLESAVENP 432
A_NRPS_SidN3_like cd05918
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ...
 17-442 6.97e-80

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: 272.11  E-value: 6.97e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   17 PERKAIECGQQTLSYKELDAESDRICELLHAHGAAQYDHIGILMqDRCA-SIAAVIGILKLGGVFVPLDPLHPDERLVTM 95
Cdd:cd05918    13 PDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCF-EKSKwAVVAMLAVLKAGGAFVPLDPSHPLQRLQEI 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   96 LDTAEVSCLLCDDAQferaetlqghegkyfvlrarqamsvqagskeayshsanatDPIYIYFTSGSTGKPKAVVGKNESL 175
Cdd:cd05918    92 LQDTGAKVVLTSSPS----------------------------------------DAAYVIFTSGSTGKPKGVVIEHRAL 131

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  176 LHFMNWEASWLDLTDPMRVSQLTSIGFDAVLRDIFVPICAGGTICIPeSREIILDplRLVHWLEHSRVHVVHCTPSLFRF 255
Cdd:cd05918   132 STSALAHGRALGLTSESRVLQFASYTFDVSILEIFTTLAAGGCLCIP-SEEDRLN--DLAGFINRLRVTWAFLTPSVARL 208

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  256 INHLSLtadsyPDLRYVLLAGETIRPESLKNWydnlGNRVRLVNLYGPTETTMIKLFYPIKPEDvhrESIPIGRPLPdTS 335
Cdd:cd05918   209 LDPEDV-----PSLRTLVLGGEALTQSDVDTW----ADRVRLINAYGPAECTIAATVSPVVPST---DPRNIGRPLG-AT 275

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  336 VYLLDEQ--QQPVSGSEAGEICIATRYMTHGYFpsSHPDQTA--FIPDP-----CRDQSGEiMMYRTGDMGRWLPEGELA 406
Cdd:cd05918   276 CWVVDPDnhDRLVPIGAVGELLIEGPILARGYL--NDPEKTAaaFIEDPawlkqEGSGRGR-RLYRTGDLVRYNPDGSLE 352

                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 517718121  407 LLGRKDNQVKIRGNRVELGDIEHRLTN-MAGIREAVV 442
Cdd:cd05918   353 YVGRKDTQVKIRGQRVELGEIEHHLRQsLPGAKEVVV 389
A_NRPS_TlmIV_like cd12114
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ...
 17-442 2.86e-79

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: 270.30  E-value: 2.86e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   17 PERKAIECGQQTLSYKELDAESDRICELLHAHGAAQYDHIGILMQDRCASIAAVIGILKLGGVFVPLDPLHPDERLVTML 96
Cdd:cd12114     1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   97 DTAEVSCLLCDDAQferaetLQGHEGKYFVLRARQamSVQAGSKEAYSHSANATDPIYIYFTSGSTGKPKAVVGKNESLL 176
Cdd:cd12114    81 ADAGARLVLTDGPD------AQLDVAVFDVLILDL--DALAAPAPPPPVDVAPDDLAYVIFTSGSTGTPKGVMISHRAAL 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  177 HFMnweaswLDLTDPMRVSQ------LTSIGFDAVLRDIFVPICAGGTICIP-ESREiiLDPLRLVHWLEHSRVHVVHCT 249
Cdd:cd12114   153 NTI------LDINRRFAVGPddrvlaLSSLSFDLSVYDIFGALSAGATLVLPdEARR--RDPAHWAELIERHGVTLWNSV 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  250 PSLFRFI-NHLSLTADSYPDLRYVLLAGETIrPESLKNWYDNLGNRVRLVNLYGPTETTMIKLFYPIKPEDVHRESIPIG 328
Cdd:cd12114   225 PALLEMLlDVLEAAQALLPSLRLVLLSGDWI-PLDLPARLRALAPDARLISLGGATEASIWSIYHPIDEVPPDWRSIPYG 303

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  329 RPLPDTSVYLLDEQQQPVSGSEAGEICIATRYMTHGYFPSSHPDQTAFIPDPcrdqSGEiMMYRTGDMGRWLPEGELALL 408
Cdd:cd12114   304 RPLANQRYRVLDPRGRDCPDWVPGELWIGGRGVALGYLGDPELTAARFVTHP----DGE-RLYRTGDLGRYRPDGTLEFL 378

                         410       420       430
                  ....*....|....*....|....*....|....
gi 517718121  409 GRKDNQVKIRGNRVELGDIEHRLTNMAGIREAVV 442
Cdd:cd12114   379 GRRDGQVKVRGYRIELGEIEAALQAHPGVARAVV 412
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
 942-1376 1.02e-78

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: 285.98  E-value: 1.02e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  942 RIEPAAKQAYYPLTAAQMRVFMDEQLVNTGSGYHITTAFMIYGPIDVTRLERACGQLIERHEALRTSFDIVDGDPVQRIH 1021
Cdd:COG1020     8 ALPPAAAAAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAGRPVQVIQ 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1022 EHCDFHLEIVHLQ--------GQQLHTAVNGCIRPFQLERAPLIRSILIPLAEEQHLLVLDMHHIVADGKSVFLLQRDLA 1093
Cdd:COG1020    88 PVVAAPLPVVVLLvdlealaeAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDGLLLAELL 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1094 ALY------EGRELHDLPVQYVDFAQWQTSAPVVEDLRRQEQFWQSMFADYRPLPGIPTDHTPEAnERSFAGGHITWEPD 1167
Cdd:COG1020   168 RLYlaayagAPLPLPPLPIQYADYALWQREWLQGEELARQLAYWRQQLAGLPPLLELPTDRPRPA-VQSYRGARVSFRLP 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1168 PVLSRRLYAVAAEQQTTLFMVLLAAFHVLYAKYSAREEVTVGTPVEGRRRAEVRQVVGMFVNALAIRSYPEGDKPFSSFL 1247
Cdd:COG1020   247 AELTAALRALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPRPELEGLVGFFVNTLPLRVDLSGDPSFAELL 326

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1248 QEIRGTMLQAYEHQDYPLERLAKQLDLHHSRDHL-MFDTVFSMLNYEDFAVRSDDLQFEYAELPTLSEIYNLRVEIVESP 1326
Cdd:COG1020   327 ARVRETLLAAYAHQDLPFERLVEELQPERDLSRNpLFQVMFVLQNAPADELELPGLTLEPLELDSGTAKFDLTLTVVETG 406

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 517718121 1327 ERLRGTFKYGQELYEARTVSQLAQDYERILAAVAESPNIKLKDIEIRTPQ 1376
Cdd:COG1020   407 DGLRLTLEYNTDLFDAATIERMAGHLVTLLEALAADPDQPLGDLPLLTAA 456
A_NRPS_ApnA-like cd17644
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ...
 17-445 6.93e-78

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: 265.84  E-value: 6.93e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   17 PERKAIECGQQTLSYKELDAESDRICELLHAHGAAQYDHIGILMQDRCASIAAVIGILKLGGVFVPLDPLHPDERLVTML 96
Cdd:cd17644    14 PDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLDPNYPQERLTYIL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   97 DTAEVSCLLCddaqferaetlQGHegkyfvlrarqamsvqagskeayshsanatDPIYIYFTSGSTGKPKAVVGKNESLL 176
Cdd:cd17644    94 EDAQISVLLT-----------QPE------------------------------NLAYVIYTSGSTGKPKGVMIEHQSLV 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  177 HFMNWEASWLDLTDPMRVSQLTSIGFDAVLRDIFVPICAGGTICI-PEsrEIILDPLRLVHWLEHSRVHVVHCTPSLFR- 254
Cdd:cd17644   133 NLSHGLIKEYGITSSDRVLQFASIAFDVAAEEIYVTLLSGATLVLrPE--EMRSSLEDFVQYIQQWQLTVLSLPPAYWHl 210

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  255 FINHLSLTADSYPD-LRYVLLAGETIRPESLKNWYDNLGNRVRLVNLYGPTETTMIKLFY-PIKPEDVHRESIPIGRPLP 332
Cdd:cd17644   211 LVLELLLSTIDLPSsLRLVIVGGEAVQPELVRQWQKNVGNFIQLINVYGPTEATIAATVCrLTQLTERNITSVPIGRPIA 290

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  333 DTSVYLLDEQQQPVSGSEAGEICIATRYMTHGYFpsSHPDQTA--FIPDPCRDQSGEiMMYRTGDMGRWLPEGELALLGR 410
Cdd:cd17644   291 NTQVYILDENLQPVPVGVPGELHIGGVGLARGYL--NRPELTAekFISHPFNSSESE-RLYKTGDLARYLPDGNIEYLGR 367

                         410       420       430
                  ....*....|....*....|....*....|....*
gi 517718121  411 KDNQVKIRGNRVELGDIEHRLTNMAGIREAVVRMR 445
Cdd:cd17644   368 IDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVR 402
PRK12316 PRK12316
peptide synthase; Provisional
 14-442 6.21e-74

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 273.37  E-value: 6.21e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   14 AAFPERKAIECGQQTLSYKELDAESDRICELLHAHGAAQYDHIGILMQDRCASIAAVIGILKLGGVFVPLDPLHPDERLV 93
Cdd:PRK12316 4562 RMTPDAVAVVFDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLA 4641

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   94 TMLDTAEVSCLLCDDAQFERAETLQGhegkyfvlraRQAMSV-QAGSKEAYSHS--ANATDP---IYIYFTSGSTGKPKA 167
Cdd:PRK12316 4642 YMMEDSGAALLLTQSHLLQRLPIPDG----------LASLALdRDEDWEGFPAHdpAVRLHPdnlAYVIYTSGSTGRPKG 4711

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  168 VVGKNESLLHFMNWEASWLDLTDPMRVSQLTSIGFDAVLRDIFVPICAGGTICIPESReiILDPLRLVHWLEHSRVHVVH 247
Cdd:PRK12316 4712 VAVSHGSLVNHLHATGERYELTPDDRVLQFMSFSFDGSHEGLYHPLINGASVVIRDDS--LWDPERLYAEIHEHRVTVLV 4789

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  248 CTPSLFR-FINHLSLTADsYPDLRYVLLAGETIRPESLKNWYDNLGNrVRLVNLYGPTETTMIKLFYPIKPEDVH-RESI 325
Cdd:PRK12316 4790 FPPVYLQqLAEHAERDGE-PPSLRVYCFGGEAVAQASYDLAWRALKP-VYLFNGYGPTETTVTVLLWKARDGDACgAAYM 4867

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  326 PIGRPLPDTSVYLLDEQQQPVSGSEAGEICIATRYMTHGYFpsSHPDQTA--FIPDPCRDQSGEimMYRTGDMGRWLPEG 403
Cdd:PRK12316 4868 PIGTPLGNRSGYVLDGQLNPLPVGVAGELYLGGEGVARGYL--ERPALTAerFVPDPFGAPGGR--LYRTGDLARYRADG 4943

                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 517718121  404 ELALLGRKDNQVKIRGNRVELGDIEHRLTNMAGIREAVV 442
Cdd:PRK12316 4944 VIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVV 4982
PRK12467 PRK12467
peptide synthase; Provisional
 11-443 6.78e-74

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 273.19  E-value: 6.78e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   11 RAFAAFPERKAIECGQQTLSYKELDAESDRICELLHAHGAAQYDHIGILMQDRCASIAAVIGILKLGGVFVPLDPLHPDE 90
Cdd:PRK12467  520 AQARQHPERPALVFGEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQD 599

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   91 RLVTMLDTAEVSCLLCDDAQFERAETLQGHEgkyfVLRARQAMSVQAGSKEAYSHSANATDPI-YIYFTSGSTGKPKAVV 169
Cdd:PRK12467  600 RLAYMLDDSGVRLLLTQSHLLAQLPVPAGLR----SLCLDEPADLLCGYSGHNPEVALDPDNLaYVIYTSGSTGQPKGVA 675

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  170 GKNESLLHFMNWEASWLDLTDPMRVSQLTSIGFDAVLRDIFVPICAGGTICIpESREIILDPLRLVHWLEHSRVHVVHCT 249
Cdd:PRK12467  676 ISHGALANYVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGATLHL-LPPDCARDAEAFAALMADQGVTVLKIV 754

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  250 PSLFRFINHLSLTADSYPdLRYVLLAGETIRPESLKNWYDnLGNRVRLVNLYGPTETTMIKLFYPIKPEDVHRESIPIGR 329
Cdd:PRK12467  755 PSHLQALLQASRVALPRP-QRALVCGGEALQVDLLARVRA-LGPGARLINHYGPTETTVGVSTYELSDEERDFGNVPIGQ 832

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  330 PLPDTSVYLLDEQQQPVSGSEAGEICIATRYMTHGYFpsSHPDQTA--FIPDPCRDQSGEimMYRTGDMGRWLPEGELAL 407
Cdd:PRK12467  833 PLANLGLYILDHYLNPVPVGVVGELYIGGAGLARGYH--RRPALTAerFVPDPFGADGGR--LYRTGDLARYRADGVIEY 908

                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 517718121  408 LGRKDNQVKIRGNRVELGDIEHRLTNMAGIREAVVR 443
Cdd:PRK12467  909 LGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVL 944
MenE/FadK COG0318
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ...
 9-442 8.23e-74

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: 253.58  E-value: 8.23e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121    9 LARAFAAFPERKAIECGQQTLSYKELDAESDRICELLHAHGAAQYDHIGILMQDRCASIAAVIGILKLGGVFVPLDPLHP 88
Cdd:COG0318     5 LRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRLT 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   89 DERLVTMLDTAEVSCLLCddaqferaetlqghegkyfvlrarqamsvqagskeayshsanatdpIYIYFTSGSTGKPKAV 168
Cdd:COG0318    85 AEELAYILEDSGARALVT----------------------------------------------ALILYTSGTTGRPKGV 118

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  169 VGKNESLLHFMNWEASWLDLTDPMRVSQLTSIGFDAVLR-DIFVPICAGGTICIPESReiilDPLRLVHWLEHSRVHVVH 247
Cdd:COG0318   119 MLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTvGLLAPLLAGATLVLLPRF----DPERVLELIERERVTVLF 194

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  248 CTPSLF-RFINHLSLTADSYPDLRYVLLAGETIRPESLKNWYDNLGnrVRLVNLYGPTETTMIKLFYPIKPEDVHRESIp 326
Cdd:COG0318   195 GVPTMLaRLLRHPEFARYDLSSLRLVVSGGAPLPPELLERFEERFG--VRIVEGYGLTETSPVVTVNPEDPGERRPGSV- 271

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  327 iGRPLPDTSVYLLDEQQQPVSGSEAGEICIATRYMTHGYFpsSHPDQTAfipDPCRDqsGeimMYRTGDMGRWLPEGELA 406
Cdd:COG0318   272 -GRPLPGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYW--NDPEATA---EAFRD--G---WLRTGDLGRLDEDGYLY 340

                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 517718121  407 LLGRKDNQVKIRGNRVELGDIEHRLTNMAGIREAVV 442
Cdd:COG0318   341 IVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAV 376
A_NRPS_PpsD_like cd17650
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ...
 17-455 2.21e-73

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: 252.39  E-value: 2.21e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   17 PERKAIECGQQTLSYKELDAESDRICELLHAHGAAQYDHIGILMQDRCASIAAVIGILKLGGVFVPLDPLHPDERLVTML 96
Cdd:cd17650     1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   97 DTAEVSCLLCDdaqferaetlqghegkyfvlrarqamsvqagskeayshsanATDPIYIYFTSGSTGKPKAVVGKNESLL 176
Cdd:cd17650    81 EDSGAKLLLTQ-----------------------------------------PEDLAYVIYTSGTTGKPKGVMVEHRNVA 119

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  177 H-FMNWEASWLDLTDPMRVSQLTSIGFDAVLRDIFVPICAGGTIcIPESREIILDPLRLVHWLEHSRVHVVHCTPSLFR- 254
Cdd:cd17650   120 HaAHAWRREYELDSFPVRLLQMASFSFDVFAGDFARSLLNGGTL-VICPDEVKLDPAALYDLILKSRITLMESTPALIRp 198

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  255 FINHLSLTADSYPDLRYVLLAGETIRPESLKNWYDNLGNRVRLVNLYGPTETTMIKLFYPIKPEDVHR-ESIPIGRPLPD 333
Cdd:cd17650   199 VMAYVYRNGLDLSAMRLLIVGSDGCKAQDFKTLAARFGQGMRIINSYGVTEATIDSTYYEEGRDPLGDsANVPIGRPLPN 278

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  334 TSVYLLDEQQQPVSGSEAGEICIATRYMTHGYFpsSHPDQTA--FIPDPCrdQSGEiMMYRTGDMGRWLPEGELALLGRK 411
Cdd:cd17650   279 TAMYVLDERLQPQPVGVAGELYIGGAGVARGYL--NRPELTAerFVENPF--APGE-RMYRTGDLARWRADGNVELLGRV 353

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....
gi 517718121  412 DNQVKIRGNRVELGDIEHRLTNMAGIREAVVRMRAKADTPKGMA 455
Cdd:cd17650   354 DHQVKIRGFRIELGEIESQLARHPAIDEAVVAVREDKGGEARLC 397
PRK12467 PRK12467
peptide synthase; Provisional
 14-442 1.51e-70

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 262.40  E-value: 1.51e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   14 AAFPERKAIECGQQTLSYKELDAESDRICELLHAHGAAQYDHIGILMQDRCASIAAVIGILKLGGVFVPLDPLHPDERLV 93
Cdd:PRK12467 1585 AATPEAVALVFGEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLA 1664

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   94 TMLDTAEVSCLLCDDAQFERAETLQGHEGkyFVLRARQAMSvqagskEAYSHS--ANATDP---IYIYFTSGSTGKPKAV 168
Cdd:PRK12467 1665 YMIEDSGIELLLTQSHLQARLPLPDGLRS--LVLDQEDDWL------EGYSDSnpAVNLAPqnlAYVIYTSGSTGRPKGA 1736

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  169 VGKNESLLHFMNWEASWLDLTDPMRVSQLTSIGFDAVLRDIFVPICAGGTICIPESrEIILDPLRLVHWLEHSRVHVVHC 248
Cdd:PRK12467 1737 GNRHGALVNRLCATQEAYQLSAADVVLQFTSFAFDVSVWELFWPLINGARLVIAPP-GAHRDPEQLIQLIERQQVTTLHF 1815

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  249 TPSLFR-FINHLSLTADSyPDLRYVLLAGETIRPESLKNWYDNLGNRvRLVNLYGPTETTMIKLFYPIKPEDVH-RESIP 326
Cdd:PRK12467 1816 VPSMLQqLLQMDEQVEHP-LSLRRVVCGGEALEVEALRPWLERLPDT-GLFNLYGPTETAVDVTHWTCRRKDLEgRDSVP 1893

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  327 IGRPLPDTSVYLLDEQQQPVSGSEAGEICIATRYMTHGYFpsSHPDQTA--FIPDPCRDQSGEimMYRTGDMGRWLPEGE 404
Cdd:PRK12467 1894 IGQPIANLSTYILDASLNPVPIGVAGELYLGGVGLARGYL--NRPALTAerFVADPFGTVGSR--LYRTGDLARYRADGV 1969

                         410       420       430
                  ....*....|....*....|....*....|....*...
gi 517718121  405 LALLGRKDNQVKIRGNRVELGDIEHRLTNMAGIREAVV 442
Cdd:PRK12467 1970 IEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVV 2007
SgcC5_NRPS-like cd19539
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ...
 953-1363 2.32e-69

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: 239.97  E-value: 2.32e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  953 PLTAAQMRVFMDEQLVNTGSGYHITTAFMIYGPIDVTRLERACGQLIERHEALRTSFDIVDGD-PVQRIHEHCDFHLEIV 1031
Cdd:cd19539     3 PLSFAQERLWFIDQGEDGGPAYNIPGAWRLTGPLDVEALREALRDVVARHEALRTLLVRDDGGvPRQEILPPGPAPLEVR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1032 HL---------QGQQLHTAVNGciRPFQLERAPLIRSILIPLAEEQHLLVLDMHHIVADGKSVFLLQRDLAALYEGRE-- 1100
Cdd:cd19539    83 DLsdpdsdrerRLEELLRERES--RGFDLDEEPPIRAVLGRFDPDDHVLVLVAHHTAFDAWSLDVFARDLAALYAARRkg 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1101 ----LHDLPVQYVDFAQWQ---TSAPVVEDLRRqeqFWQSMFADYRPLPgIPTDHtPEANERSFAGGHITWEPDPVLSRR 1173
Cdd:cd19539   161 paapLPELRQQYKEYAAWQreaLAAPRAAELLD---FWRRRLRGAEPTA-LPTDR-PRPAGFPYPGADLRFELDAELVAA 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1174 LYAVAAEQQTTLFMVLLAAFHVLYAKYSAREEVTVGTPVEGRRRAEVRQVVGMFVNALAIRSYPEGDKPFSSFLQEIRGT 1253
Cdd:cd19539   236 LRELAKRARSSLFMVLLAAYCVLLRRYTGQTDIVVGTPVAGRNHPRFESTVGFFVNLLPLRVDVSDCATFRDLIARVRKA 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1254 MLQAYEHQDYPLERLAKQL-DLHHSRDHLMFDTVFSMLN--YEDFAVRSDDLQFEYAELPTLSEiYNLRVEIVESPERLR 1330
Cdd:cd19539   316 LVDAQRHQELPFQQLVAELpVDRDAGRHPLVQIVFQVTNapAGELELAGGLSYTEGSDIPDGAK-FDLNLTVTEEGTGLR 394

                         410       420       430
                  ....*....|....*....|....*....|...
gi 517718121 1331 GTFKYGQELYEARTVSQLAQDYERILAAVAESP 1363
Cdd:cd19539   395 GSLGYATSLFDEETIQGFLADYLQVLRQLLANP 427
PRK12316 PRK12316
peptide synthase; Provisional
 912-1370 7.08e-69

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 257.19  E-value: 7.08e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  912 VELPLE--QVFehdtleeIAAYIDEQDSQYGVRIePAAKQA--YYPLTAAQMRVFMDEQLVNTGSGYHITTAFMIYGPID 987
Cdd:PRK12316   14 IELPLEkrRVF-------LATLRGEGVDFSLFPI-PAGVSSaeRDRLSYAQQRMWFLWQLEPQSGAYNLPSAVRLNGPLD 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  988 VTRLERACGQLIERHEALRTSFDIVDGDPVQRIHEHCDFHLEIVHLQGQ---QLHTAVN-----GCIRPFQLERAPLIRS 1059
Cdd:PRK12316   86 RQALERAFASLVQRHETLRTVFPRGADDSLAQVPLDRPLEVEFEDCSGLpeaEQEARLRdeaqrESLQPFDLCEGPLLRV 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1060 ILIPLAEEQHLLVLDMHHIVADGKSVFLLQRDLAALYEGR------ELHDLPVQYVDFAQWQTSAPVVEDLRRQEQFWQS 1133
Cdd:PRK12316  166 RLLRLGEEEHVLLLTLHHIVSDGWSMNVLIEEFSRFYSAYatgaepGLPALPIQYADYALWQRSWLEAGEQERQLEYWRA 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1134 MFADYRPLPGIPTDHtPEANERSFAGGHITWEPDPVLSRRLYAVAAEQQTTLFMVLLAAFHVLYAKYSAREEVTVGTPVE 1213
Cdd:PRK12316  246 QLGEEHPVLELPTDH-PRPAVPSYRGSRYEFSIDPALAEALRGTARRQGLTLFMLLLGAFNVLLHRYSGQTDIRVGVPIA 324

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1214 GRRRAEVRQVVGMFVNALAIRSYPEGDKPFSSFLQEIRGTMLQAYEHQDYPLERLAKQLDLHHSRDHLMFDTVfsMLNYE 1293
Cdd:PRK12316  325 NRNRAEVEGLIGFFVNTQVLRSVFDGRTRVATLLAGVKDTVLGAQAHQDLPFERLVEALKVERSLSHSPLFQV--MYNHQ 402

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1294 ----DFAVRSD--DLQFEYAELPTLSEIYNLRVEIVESPERLRGTFKYGQELYEARTVSQLAQDYERILAAVAESPNIKL 1367
Cdd:PRK12316  403 plvaDIEALDTvaGLEFGQLEWKSRTTQFDLTLDTYEKGGRLHAALTYATDLFEARTVERMARHWQNLLRGMVENPQARV 482


                  ...
gi 517718121 1368 KDI 1370
Cdd:PRK12316  483 DEL 485
PRK12467 PRK12467
peptide synthase; Provisional
 912-1370 9.72e-69

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 256.63  E-value: 9.72e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  912 VELPLEQvfehdtleeiAAYIDEQDSQYGVRIE----PAAKQAY--YPLTAAQMRVFMDEQLVNTGSGYHITTAFMIYGP 985
Cdd:PRK12467   14 ITLPLEK----------RRLYLEKMQEEGVSFAnlpiPQVRSAFerIPLSYAQERQWFLWQLDPDSAAYNIPTALRLRGE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  986 IDVTRLERACGQLIERHEALRTSFDIVDGDPVQRIHEHCDFHLEIVHL-------QGQQLHTAVNGCI-RPFQLERAPLI 1057
Cdd:PRK12467   84 LDVSALRRAFDALVARHESLRTRFVQDEEGFRQVIDASLSLTIPLDDLaneqgraRESQIEAYINEEVaRPFDLANGPLL 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1058 RSILIPLAEEQHLLVLDMHHIVADGKSVFLLQRDLAALYEGR------ELHDLPVQYVDFAQWQTSAPVVEDLRRQEQFW 1131
Cdd:PRK12467  164 RVRLLRLADDEHVLVVTLHHIISDGWSMRVLVEELVQLYSAYsqgrepSLPALPIQYADYAIWQRSWLEAGERERQLAYW 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1132 QSMFADYRPLPGIPTDHtPEANERSFAGGHITWEPDPVLSRRLYAVAAEQQTTLFMVLLAAFHVLYAKYSAREEVTVGTP 1211
Cdd:PRK12467  244 QEQLGGEHTVLELPTDR-PRPAVPSYRGARLRVDLPQALSAGLKALAQREGVTLFMVLLASFQTLLHRYSGQSDIRIGVP 322

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1212 VEGRRRAEVRQVVGMFVNALAIRSYPEGDKPFSSFLQEIRGTMLQAYEHQDYPLERLAKQLDLHHSRDHL-MFDTVFSML 1290
Cdd:PRK12467  323 NANRNRVETERLIGFFVNTQVLKAEVDPQASFLELLQQVKRTALGAQAHQDLPFEQLVEALQPERSLSHSpLFQVMFNHQ 402

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1291 NyedfaVRSDDLQFEYAELP--TLSEI--------YNLRVEIVESPERLRGTFKYGQELYEARTVSQLAQDYERILAAVA 1360
Cdd:PRK12467  403 N-----TATGGRDREGAQLPglTVEELswarhtaqFDLALDTYESAQGLWAAFTYATDLFEATTIERLATHWRNLLEAIV 477

                         490
                  ....*....|
gi 517718121 1361 ESPNIKLKDI 1370
Cdd:PRK12467  478 AEPRRRLGEL 487
A_NRPS_ProA cd17656
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ...
 17-446 8.36e-68

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: 237.37  E-value: 8.36e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   17 PERKAIECGQQTLSYKELDAESDRICELLHAHGAAQYDHIGILMQDRCASIAAVIGILKLGGVFVPLDPLHPDERLVTML 96
Cdd:cd17656     2 PDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIM 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   97 DTAEVSCLLcddAQFERAETLQgHEGKYFVLrarQAMSVQAGSKEAYSHSANATDPIYIYFTSGSTGKPKAVVGKNESLL 176
Cdd:cd17656    82 LDSGVRVVL---TQRHLKSKLS-FNKSTILL---EDPSISQEDTSNIDYINNSDDLLYIIYTSGTTGKPKGVQLEHKNMV 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  177 HFMNWEASWLDLTDPMRVSQLTSIGFDAVLRDIFVPICAGGTICIPeSREIILDPLRLVHWLEHSRVHVVHCTPSLFRFI 256
Cdd:cd17656   155 NLLHFEREKTNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLYII-REETKRDVEQLFDLVKRHNIEVVFLPVAFLKFI 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  257 NHLSLTADSYPD-LRYVLLAGETIRPESLKNWYDNLGNrVRLVNLYGPTETTMIKLfYPIKPEDVHRESIPIGRPLPDTS 335
Cdd:cd17656   234 FSEREFINRFPTcVKHIITAGEQLVITNEFKEMLHEHN-VHLHNHYGPSETHVVTT-YTINPEAEIPELPPIGKPISNTW 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  336 VYLLDEQQQPVSGSEAGEICIATRYMTHGYFpsSHPDQTA--FIPDPCRDQSgeiMMYRTGDMGRWLPEGELALLGRKDN 413
Cdd:cd17656   312 IYILDQEQQLQPQGIVGELYISGASVARGYL--NRQELTAekFFPDPFDPNE---RMYRTGDLARYLPDGNIEFLGRADH 386

                         410       420       430
                  ....*....|....*....|....*....|...
gi 517718121  414 QVKIRGNRVELGDIEHRLTNMAGIREAVVRMRA 446
Cdd:cd17656   387 QVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKA 419
PRK12316 PRK12316
peptide synthase; Provisional
 14-442 3.63e-67

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 251.80  E-value: 3.63e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   14 AAFPERKAIECGQQTLSYKELDAESDRICELLHAHGAAQYDHIGILMQDRCASIAAVIGILKLGGVFVPLDPLHPDERLV 93
Cdd:PRK12316  522 ERTPEAPALAFGEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLA 601

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   94 TMLDTAEVSCLLcddAQFERAETLQGHEGKYFVLRARQAMSVQAGSKEAYSHSANATDPIYIYFTSGSTGKPKAVVGKNE 173
Cdd:PRK12316  602 YMLEDSGVQLLL---SQSHLGRKLPLAAGVQVLDLDRPAAWLEGYSEENPGTELNPENLAYVIYTSGSTGKPKGAGNRHR 678

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  174 SLLHFMNWEASWLDLTDPMRVSQLTSIGFDAVLRDIFVPICAGGTICIPeSREIILDPLRLVHWLEHSRVHVVHCTPSLF 253
Cdd:PRK12316  679 ALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVA-APGDHRDPAKLVELINREGVDTLHFVPSML 757

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  254 RFINHLSLTADSYPdLRYVLLAGETIRPESLKNWYDNLGNrVRLVNLYGPTETTmIKLFYPIKPEDVHReSIPIGRPLPD 333
Cdd:PRK12316  758 QAFLQDEDVASCTS-LRRIVCSGEALPADAQEQVFAKLPQ-AGLYNLYGPTEAA-IDVTHWTCVEEGGD-SVPIGRPIAN 833

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  334 TSVYLLDEQQQPVSGSEAGEICIATRYMTHGYFpsSHPDQTA--FIPDPCRDqsGEiMMYRTGDMGRWLPEGELALLGRK 411
Cdd:PRK12316  834 LACYILDANLEPVPVGVLGELYLAGRGLARGYH--GRPGLTAerFVPSPFVA--GE-RMYRTGDLARYRADGVIEYAGRI 908

                         410       420       430
                  ....*....|....*....|....*....|.
gi 517718121  412 DNQVKIRGNRVELGDIEHRLTNMAGIREAVV 442
Cdd:PRK12316  909 DHQVKLRGLRIELGEIEARLLEHPWVREAAV 939
A_NRPS_LgrA-like cd17645
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ...
 17-455 9.45e-67

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: 232.83  E-value: 9.45e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   17 PERKAIECGQQTLSYKELDAESDRICELLHAHGAAQYDHIGILMQDRCASIAAVIGILKLGGVFVPLDPLHPDERLVTML 96
Cdd:cd17645    12 PDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYPGERIAYML 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   97 DTAEVSCLLcddaqferaetlqghegkyfvlrarqamsvqagskeayshsANATDPIYIYFTSGSTGKPKAVVGKNESLL 176
Cdd:cd17645    92 ADSSAKILL-----------------------------------------TNPDDLAYVIYTSGSTGLPKGVMIEHHNLV 130

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  177 HFMNWEASWLDLTDPMRVSQLTSIGFDAVLRDIFVPICAGGTICIPESrEIILDPLRLVHWLEHSRVHVVHC-TPSLFRF 255
Cdd:cd17645   131 NLCEWHRPYFGVTPADKSLVYASFSFDASAWEIFPHLTAGAALHVVPS-ERRLDLDALNDYFNQEGITISFLpTGAAEQF 209

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  256 I---NHlsltadsypDLRYVLLAGETIRpESLKNWYdnlgnrvRLVNLYGPTETTMIKLFYPIKPEDvhrESIPIGRPLP 332
Cdd:cd17645   210 MqldNQ---------SLRVLLTGGDKLK-KIERKGY-------KLVNNYGPTENTVVATSFEIDKPY---ANIPIGKPID 269

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  333 DTSVYLLDEQQQPVSGSEAGEICIATRYMTHGYFpsSHPDQTA--FIPDPcrDQSGEiMMYRTGDMGRWLPEGELALLGR 410
Cdd:cd17645   270 NTRVYILDEALQLQPIGVAGELCIAGEGLARGYL--NRPELTAekFIVHP--FVPGE-RMYRTGDLAKFLPDGNIEFLGR 344

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*
gi 517718121  411 KDNQVKIRGNRVELGDIEHRLTNMAGIREAVVRMRAKADTPKGMA 455
Cdd:cd17645   345 LDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLV 389
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
9-452 2.92e-65

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 243.41  E-value: 2.92e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121    9 LARAFAAFPERKAIECGQQTLSYKELDAESDRICELLHAHGAAQYDHIGILMQDRCASIAAVIGILKLGGVFVPLDPLHP 88
Cdd:PRK10252  464 VAQQAAKTPDAPALADARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYP 543

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   89 DERLVTMLDTAEVSCLLCDDAQFERAETLQGHEgkyfVLRARQAMSVQAGSKEAYSHSAnatDPIYIYFTSGSTGKPKAV 168
Cdd:PRK10252  544 DDRLKMMLEDARPSLLITTADQLPRFADVPDLT----SLCYNAPLAPQGAAPLQLSQPH---HTAYIIFTSGSTGRPKGV 616

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  169 VGKNESLLHFMNWEASWLDLTDPMRVSQLTSIGFDAVLRDIFVPICAGGTICI--PESREiilDPLRLVHWLEHSRVHVV 246
Cdd:PRK10252  617 MVGQTAIVNRLLWMQNHYPLTADDVVLQKTPCSFDVSVWEFFWPFIAGAKLVMaePEAHR---DPLAMQQFFAEYGVTTT 693

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  247 HCTPS-LFRFINhlSLTADSYPD----LRYVLLAGETIrPESLKNWYDNLGNrVRLVNLYGPTETTMIKLFYPIKPED-- 319
Cdd:PRK10252  694 HFVPSmLAAFVA--SLTPEGARQscasLRQVFCSGEAL-PADLCREWQQLTG-APLHNLYGPTEAAVDVSWYPAFGEEla 769

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  320 -VHRESIPIGRPLPDTSVYLLDEQQQPVSGSEAGEICIATRYMTHGYFpsSHPDQTA--FIPDPCRdqSGEiMMYRTGDM 396
Cdd:PRK10252  770 aVRGSSVPIGYPVWNTGLRILDARMRPVPPGVAGDLYLTGIQLAQGYL--GRPDLTAsrFIADPFA--PGE-RMYRTGDV 844

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 517718121  397 GRWLPEGELALLGRKDNQVKIRGNRVELGDIEHRLTNMAGIREAVVRMRAKADTPK 452
Cdd:PRK10252  845 ARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVEQAVTHACVINQAAA 900
C_NRPS-like cd19066
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ...
 952-1363 7.66e-65

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: 226.91  E-value: 7.66e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  952 YPLTAAQMRVFMDEQLVNTGSGYHITTAFMIYGPIDVTRLERACGQLIERHEALRTSFDIVDGDPVQRIHEH-CDFHLEI 1030
Cdd:cd19066     2 IPLSPMQRGMWFLKKLATDPSAFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRFCEEAGRYEQVVLDKtVRFRIEI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1031 VHLQGQQLHTAV------NGCIRPFQLERAPLIRSILIPLAEEQHLLVLDMHHIVADGKSVFLLQRDLAALYEG-----R 1099
Cdd:cd19066    82 IDLRNLADPEARllelidQIQQTIYDLERGPLVRVALFRLADERDVLVVAIHHIIVDGGSFQILFEDISSVYDAaerqkP 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1100 ELHDLPVQYVDFAQWQTSAPVVEDLRRQEQFWQSMFADYRPLPGIPTDHTPEANeRSFAGGHITWEPDPVLSRRLYAVAA 1179
Cdd:cd19066   162 TLPPPVGSYADYAAWLEKQLESEAAQADLAYWTSYLHGLPPPLPLPKAKRPSQV-ASYEVLTLEFFLRSEETKRLREVAR 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1180 EQQTTLFMVLLAAFHVLYAKYSAREEVTVGTPVEGRRRAEVRQVVGMFVNALAIRSYPEGDKPFSSFLQEIRGTMLQAYE 1259
Cdd:cd19066   241 ESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRPDEAVEDTIGLFLNLLPLRIDTSPDATFPELLKRTKEQSREAIE 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1260 HQDYPLERLAKQLDLHHSR-DHLMFDTVFSMLNYeDFAVRSDDLQFEYAELPTLSE--IYNLRVEIVESPER-LRGTFKY 1335
Cdd:cd19066   321 HQRVPFIELVRHLGVVPEApKHPLFEPVFTFKNN-QQQLGKTGGFIFTTPVYTSSEgtVFDLDLEASEDPDGdLLLRLEY 399

                         410       420
                  ....*....|....*....|....*...
gi 517718121 1336 GQELYEARTVSQLAQDYERILAAVAESP 1363
Cdd:cd19066   400 SRGVYDERTIDRFAERYMTALRQLIENP 427
PRK12467 PRK12467
peptide synthase; Provisional
 17-442 6.73e-64

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 241.22  E-value: 6.73e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   17 PERKAIECGQQTLSYKELDAESDRICELLHAHGAAQYDHIGILMQDRCASIAAVIGILKLGGVFVPLDPLHPDERLVTML 96
Cdd:PRK12467 3109 PEAPALVFGDQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYMI 3188

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   97 DTAEVSCLLCDDAQFERAEtlqghegkyfVLRARQAMSVQAGSKEAYSHS--ANATDP---IYIYFTSGSTGKPKAVVGK 171
Cdd:PRK12467 3189 EDSGVKLLLTQAHLLEQLP----------APAGDTALTLDRLDLNGYSENnpSTRVMGenlAYVIYTSGSTGKPKGVGVR 3258

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  172 NESLLHFMNWEASWLDLTDPMRVSQLTSIGFDAVLRDIFVPICAGGTICIPESReiILDPLRLVHWLEHSRVHVVHCTPS 251
Cdd:PRK12467 3259 HGALANHLCWIAEAYELDANDRVLLFMSFSFDGAQERFLWTLICGGCLVVRDND--LWDPEELWQAIHAHRISIACFPPA 3336

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  252 LFRFINHLSLTADsYPDLRYVLLAGETIRPESLKNWYDNLGNRvRLVNLYGPTETTMIKLFYPIKPEDVHRES-IPIGRP 330
Cdd:PRK12467 3337 YLQQFAEDAGGAD-CASLDIYVFGGEAVPPAAFEQVKRKLKPR-GLTNGYGPTEAVVTVTLWKCGGDAVCEAPyAPIGRP 3414

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  331 LPDTSVYLLDEQQQPVSGSEAGEICIATRYMTHGYFpsSHPDQTA--FIPDPCRDQSGEimMYRTGDMGRWLPEGELALL 408
Cdd:PRK12467 3415 VAGRSIYVLDGQLNPVPVGVAGELYIGGVGLARGYH--QRPSLTAerFVADPFSGSGGR--LYRTGDLARYRADGVIEYL 3490

                         410       420       430
                  ....*....|....*....|....*....|....
gi 517718121  409 GRKDNQVKIRGNRVELGDIEHRLTNMAGIREAVV 442
Cdd:PRK12467 3491 GRIDHQVKIRGFRIELGEIEARLLQHPSVREAVV 3524
PRK12316 PRK12316
peptide synthase; Provisional
 14-442 1.91e-63

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 239.86  E-value: 1.91e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   14 AAFPERKAIECGQQTLSYKELDAESDRICELLHAHGAAQYDHIGILMQDRCASIAAVIGILKLGGVFVPLDPLHPDERLV 93
Cdd:PRK12316 2014 ARAPEAIAVVFGDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLA 2093

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   94 TMLDTAEVSCLLCDDAQFERAETLQGHEgkyfVLRARQAMSVQAGSKEAYSHSANATDPIYIYFTSGSTGKPKAVVGKNE 173
Cdd:PRK12316 2094 YMLEDSGAALLLTQRHLLERLPLPAGVA----RLPLDRDAEWADYPDTAPAVQLAGENLAYVIYTSGSTGLPKGVAVSHG 2169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  174 SLLHFMNWEASWLDLTDPMRVSQLTSIGFDAVLRDIFVPICAGGTICIPESReiILDPLRLVHWLEHSRVHVVHCTPS-L 252
Cdd:PRK12316 2170 ALVAHCQAAGERYELSPADCELQFMSFSFDGAHEQWFHPLLNGARVLIRDDE--LWDPEQLYDEMERHGVTILDFPPVyL 2247

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  253 FRFINHLSLTADSyPDLRYVLLAGETIRPESLKNWYDNLGNrVRLVNLYGPTETTMIKLFYPIKPEDVH-RESIPIGRPL 331
Cdd:PRK12316 2248 QQLAEHAERDGRP-PAVRVYCFGGEAVPAASLRLAWEALRP-VYLFNGYGPTEAVVTPLLWKCRPQDPCgAAYVPIGRAL 2325

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  332 PDTSVYLLDEQQQPVSGSEAGEICIATRYMTHGYFpsSHPDQTA--FIPDPCrDQSGEiMMYRTGDMGRWLPEGELALLG 409
Cdd:PRK12316 2326 GNRRAYILDADLNLLAPGMAGELYLGGEGLARGYL--NRPGLTAerFVPDPF-SASGE-RLYRTGDLARYRADGVVEYLG 2401

                         410       420       430
                  ....*....|....*....|....*....|...
gi 517718121  410 RKDNQVKIRGNRVELGDIEHRLTNMAGIREAVV 442
Cdd:PRK12316 2402 RIDHQVKIRGFRIELGEIEARLQAHPAVREAVV 2434
A_NRPS_ACVS-like cd17648
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ...
 17-458 4.63e-63

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: 222.66  E-value: 4.63e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   17 PERKAIECGQQTLSYKELDAESDRICELLHAHGAAQYDH-IGILMQDRCASIAAVIGILKLGGVFVPLDPLHPDERLvtm 95
Cdd:cd17648     1 PDRVAVVYGDKRLTYRELNERANRLAHYLLSVAEIRPDDlVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERI--- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   96 ldtaevscllcddaqferaetlqghegkYFVLRARQAMSVQAGSkeayshsanaTDPIYIYFTSGSTGKPKAVVGKNESL 175
Cdd:cd17648    78 ----------------------------QFILEDTGARVVITNS----------TDLAYAIYTSGTTGKPKGVLVEHGSV 119

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  176 LHFMNWEASWLDLTDP--MRVSQLTSIGFDAVLRDIFVPICAGGTICIPESrEIILDPLRLVHWLEHSRVHVVHCTPSLF 253
Cdd:cd17648   120 VNLRTSLSERYFGRDNgdEAVLFFSNYVFDFFVEQMTLALLNGQKLVVPPD-EMRFDPDRFYAYINREKVTYLSGTPSVL 198

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  254 RFINHLSLtadsyPDLRYVLLAGETIRPESlknwYDNLGNRV--RLVNLYGPTETTM--IKLFYPikpeDVHRESIPIGR 329
Cdd:cd17648   199 QQYDLARL-----PHLKRVDAAGEEFTAPV----FEKLRSRFagLIINAYGPTETTVtnHKRFFP----GDQRFDKSLGR 265

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  330 PLPDTSVYLLDEQQQPVSGSEAGEICIATRYMTHGYFpsSHPDQTA--FIPDPC-----RDQSGEIMMYRTGDMGRWLPE 402
Cdd:cd17648   266 PVRNTKCYVLNDAMKRVPVGAVGELYLGGDGVARGYL--NRPELTAerFLPNPFqteqeRARGRNARLYKTGDLVRWLPS 343

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 517718121  403 GELALLGRKDNQVKIRGNRVELGDIEHRLTNMAGIREAVVRMRAKADTPKGMAQQH 458
Cdd:cd17648   344 GELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAKEDASQAQSRIQKY 399
COG4908 COG4908
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ...
 954-1186 2.15e-61

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


Pssm-ID: 443936 [Multi-domain]  Cd Length: 243  Bit Score: 210.28  E-value: 2.15e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  954 LTAAQMRVFMDEQlvnTGSGYHITTAFMIYGPIDVTRLERACGQLIERHEALRTSFDIVDGDPVQRIHEHCDFHLEIVHL 1033
Cdd:COG4908     1 LSPAQKRFLFLEP---GSNAYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFVEEDGEPVQRIDPDADLPLEVVDL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1034 QG-------QQLHTAVNGCI-RPFQLERAPLIRSILIPLAEEQHLLVLDMHHIVADGKSVFLLQRDLAALYEGRE----- 1100
Cdd:COG4908    78 SAlpepereAELEELVAEEAsRPFDLARGPLLRAALIRLGEDEHVLLLTIHHIISDGWSLGILLRELAALYAALLegepp 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1101 -LHDLPVQYVDFAQWQTSAPVVEDLRRQEQFWQSMFADYRPLPGIPTDHtPEANERSFAGGHITWEPDPVLSRRLYAVAA 1179
Cdd:COG4908   158 pLPELPIQYADYAAWQRAWLQSEALEKQLEYWRQQLAGAPPVLELPTDR-PRPAVQTFRGATLSFTLPAELTEALKALAK 236


                  ....*..
gi 517718121 1180 EQQTTLF 1186
Cdd:COG4908   237 AHGATVN 243
DCL_NRPS cd19543
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ...
 952-1363 5.33e-57

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: 203.97  E-value: 5.33e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  952 YPLTAAQ--MrVFmdEQLVNTGSG-YHITTAFMIYGPIDVTRLERACGQLIERHEALRTSFDIV-DGDPVQRIHEHCDFH 1027
Cdd:cd19543     2 YPLSPMQegM-LF--HSLLDPGSGaYVEQMVITLEGPLDPDRFRAAWQAVVDRHPILRTSFVWEgLGEPLQVVLKDRKLP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1028 LEIVHLQG----------QQLHTAVNgcIRPFQLERAPLIRSILIPLAEEQHLLVLDMHHIVADGKSVFLLQRDLAALY- 1096
Cdd:cd19543    79 WRELDLSHlseaeqeaelEALAEEDR--ERGFDLARAPLMRLTLIRLGDDRYRLVWSFHHILLDGWSLPILLKELFAIYa 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1097 ---EGRELHDLPVQ-YVDFAQWqtsapvvedLRRQ-----EQFWQSMFADYRPLPGIPTDhTPEANERSFAGGHITWEPD 1167
Cdd:cd19543   157 algEGQPPSLPPVRpYRDYIAW---------LQRQdkeaaEAYWREYLAGFEEPTPLPKE-LPADADGSYEPGEVSFELS 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1168 PVLSRRLYAVAAEQQTTLFMVLLAAFHVLYAKYSAREEVTVGTPVEGrRRAE---VRQVVGMFVNALAIRSYPEGDKPFS 1244
Cdd:cd19543   227 AELTARLQELARQHGVTLNTVVQGAWALLLSRYSGRDDVVFGTTVSG-RPAElpgIETMVGLFINTLPVRVRLDPDQTVL 305

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1245 SFLQEIRGTMLQAYEHQDYPLERLAKQLDLHHSrdhlMFDTVFSMLNY-EDFAVR----SDDLQFEYAELPTLSEiYNLR 1319
Cdd:cd19543   306 ELLKDLQAQQLELREHEYVPLYEIQAWSEGKQA----LFDHLLVFENYpVDESLEeeqdEDGLRITDVSAEEQTN-YPLT 380

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....
gi 517718121 1320 VEIVESpERLRGTFKYGQELYEARTVSQLAQDYERILAAVAESP 1363
Cdd:cd19543   381 VVAIPG-EELTIKLSYDAEVFDEATIERLLGHLRRVLEQVAANP 423
PRK12316 PRK12316
peptide synthase; Provisional
 14-442 1.16e-56

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 217.90  E-value: 1.16e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   14 AAFPERKAIECGQQTLSYKELDAESDRICELLHAHGAAQYDHIGILMQDRCASIAAVIGILKLGGVFVPLDPLHPDERLV 93
Cdd:PRK12316 3068 ERTPDAVALAFGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLA 3147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   94 TMLDTAEVSCLLCddaqferaetlQGHEgKYFVLRARQAMSVQAGSKEAYSHS-ANATDP---IYIYFTSGSTGKPKAVV 169
Cdd:PRK12316 3148 YMLEDSGAQLLLS-----------QSHL-RLPLAQGVQVLDLDRGDENYAEANpAIRTMPenlAYVIYTSGSTGKPKGVG 3215

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  170 GKNESLLHFMNWEASWLDLTDPMRVSQLTSIGFDAVLRDIFVPICAGGTICIpESREIILDPLRLVHWLEHSRVHVVHCT 249
Cdd:PRK12316 3216 IRHSALSNHLCWMQQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVL-AGPEDWRDPALLVELINSEGVDVLHAY 3294

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  250 PSLFRFINHlSLTADSYPDLRYVLLAGETIRPESLKNWYDNLGnrvrLVNLYGPTETTMIKLFYPIKPEdvHRESIPIGR 329
Cdd:PRK12316 3295 PSMLQAFLE-EEDAHRCTSLKRIVCGGEALPADLQQQVFAGLP----LYNLYGPTEATITVTHWQCVEE--GKDAVPIGR 3367

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  330 PLPDTSVYLLDEQQQPVSGSEAGEICIATRYMTHGYFpsSHPDQTA--FIPDPCrdQSGEiMMYRTGDMGRWLPEGELAL 407
Cdd:PRK12316 3368 PIANRACYILDGSLEPVPVGALGELYLGGEGLARGYH--NRPGLTAerFVPDPF--VPGE-RLYRTGDLARYRADGVIEY 3442

                         410       420       430
                  ....*....|....*....|....*....|....*
gi 517718121  408 LGRKDNQVKIRGNRVELGDIEHRLTNMAGIREAVV 442
Cdd:PRK12316 3443 IGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVV 3477
C_PKS-NRPS cd19532
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
 953-1363 2.78e-55

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: 198.83  E-value: 2.78e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  953 PLTAAQMRV-FMDeQLVNTGSGYHITTAFMIYGPIDVTRLERACGQLIERHEALRTSF--DIVDGDPVQRIHEHCDFHLE 1029
Cdd:cd19532     3 PMSFGQSRFwFLQ-QYLEDPTTFNVTFSYRLTGPLDVARLERAVRAVGQRHEALRTCFftDPEDGEPMQGVLASSPLRLE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1030 IVHLQG--------QQLHTAVngcirpFQLERAPLIRSILIPLAEEQHLLVLDMHHIVADGKSVFLLQRDLAALYEGREL 1101
Cdd:cd19532    82 HVQISDeaeveeefERLKNHV------YDLESGETMRIVLLSLSPTEHYLIFGYHHIAMDGVSFQIFLRDLERAYNGQPL 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1102 HDLPVQYVDFAQWQTSAPVVEDLRRQEQFWQSMFAD-YRPLPGIPTDHTPE-------ANERSFAggHItwepDPVLSRR 1173
Cdd:cd19532   156 LPPPLQYLDFAARQRQDYESGALDEDLAYWKSEFSTlPEPLPLLPFAKVKSrppltryDTHTAER--RL----DAALAAR 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1174 LYAVAAEQQTTLFMVLLAAFHVLYAKYSAREEVTVGTPVEGRRRAEVRQVVGMFVNALAIRSYPEGDKPFSSFLQEIRGT 1253
Cdd:cd19532   230 IKEASRKLRVTPFHFYLAALQVLLARLLDVDDICIGIADANRTDEDFMETIGFFLNLLPLRFRRDPSQTFADVLKETRDK 309

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1254 MLQAYEHQDYPLERLAKQLDLHHSRDHL-MFDTVFsmlNY-----EDFAVRSDDLQFEYAELPTLSeiYNLRVEIVESPE 1327
Cdd:cd19532   310 AYAALAHSRVPFDVLLDELGVPRSATHSpLFQVFI---NYrqgvaESRPFGDCELEGEEFEDARTP--YDLSLDIIDNPD 384

                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 517718121 1328 ---RLrgTFKYGQELYEARTVSQLAQDYERILAAVAESP 1363
Cdd:cd19532   385 gdcLL--TLKVQSSLYSEEDAELLLDSYVNLLEAFARDP 421
C_PKS-NRPS_PksJ-like cd20484
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
 952-1363 1.89e-54

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: 196.77  E-value: 1.89e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  952 YPLTAAQMRVFMDEQLVNTGSGYHITTAFMIYGPIDVTRLERACGQLIERHEALRTSFDIVDGDPVQRIHEHCDFHLE-- 1029
Cdd:cd20484     2 SPLSEGQKGLWMLQKMSPEMSAYNVPLCFRFSSKLDVEKFKQACQFVLEQHPILKSVIEEEDGVPFQKIEPSKPLSFQee 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1030 -IVHLQGQQ----LHTAVNgciRPFQLERAPLIRSILIPLAEEQHLLVLDMHHIVADGKSVFLLQRDL----AALYEGRE 1100
Cdd:cd20484    82 dISSLKESEiiayLREKAK---EPFVLENGPLMRVHLFSRSEQEHFVLITIHHIIFDGSSSLTLIHSLldayQALLQGKQ 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1101 LHDLPV--QYVDFAQWQTSAPVVEDLRRQEQFWQSMFADYRPLPGIPTDHtPEANERSFAGGHITWEPDPVLSRRLYAVA 1178
Cdd:cd20484   159 PTLASSpaSYYDFVAWEQDMLAGAEGEEHRAYWKQQLSGTLPILELPADR-PRSSAPSFEGQTYTRRLPSELSNQIKSFA 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1179 AEQQTTLFMVLLAAFHVLYAKYSAREEVTVGTPVEGRRRAEVRQVVGMFVNALAIRSYPEGDKPFSSFLQEIRGTMLQAY 1258
Cdd:cd20484   238 RSQSINLSTVFLGIFKLLLHRYTGQEDIIVGMPTMGRPEERFDSLIGYFINMLPIRSRILGEETFSDFIRKLQLTVLDGL 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1259 EHQDYPLERLAKQLDLHHSRDHL-MFDTVFSmlnYEDFaVRSDDLQFEYAELPTLSEI-----------YNLRVEIVESP 1326
Cdd:cd20484   318 DHAAYPFPAMVRDLNIPRSQANSpVFQVAFF---YQNF-LQSTSLQQFLAEYQDVLSIefvegihqegeYELVLEVYEQE 393

                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 517718121 1327 ERLRGTFKYGQELYEARTVSQLAQDYERILAAVAESP 1363
Cdd:cd20484   394 DRFTLNIKYNPDLFDASTIERMMEHYVKLAEELIANP 430
PRK05691 PRK05691
peptide synthase; Validated
 9-452 1.64e-52

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 204.25  E-value: 1.64e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121    9 LARAFAAFPERKAIECGQQTLSYKELDAESDRICELLHAHGAAQYDHIGILMQDRCASIAAVIGILKLGGVFVPLDPLHP 88
Cdd:PRK05691 1137 LNEQARQTPERIALVWDGGSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYP 1216

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   89 DERLVTMLDTAEVSCLLCDDAQFERAETLQGhegkyFVLRARQAMSVQAGSKEAYSHSANATDPIYIYFTSGSTGKPKAV 168
Cdd:PRK05691 1217 AERLAYMLADSGVELLLTQSHLLERLPQAEG-----VSAIALDSLHLDSWPSQAPGLHLHGDNLAYVIYTSGSTGQPKGV 1291

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  169 VGKNESLLHFMNWEASWLDLTDPMRVSQLTSIGFDAVLRDIFVPICAGGTICIP---ESReiilDPLRLVHWLEHSRVHV 245
Cdd:PRK05691 1292 GNTHAALAERLQWMQATYALDDSDVLMQKAPISFDVSVWECFWPLITGCRLVLAgpgEHR----DPQRIAELVQQYGVTT 1367

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  246 VHCTPSLFRFINHLSLTADSYpDLRYVLLAGETIRPEsLKNWYDNLGNRVRLVNLYGPTETTMIKLFYPIKPEDVHREsi 325
Cdd:PRK05691 1368 LHFVPPLLQLFIDEPLAAACT-SLRRLFSGGEALPAE-LRNRVLQRLPQVQLHNRYGPTETAINVTHWQCQAEDGERS-- 1443

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  326 PIGRPLPDTSVYLLDEQQQPVSGSEAGEICIATRYMTHGYFPSshPDQTA--FIPDPCRDQSGEimMYRTGDMGRWLPEG 403
Cdd:PRK05691 1444 PIGRPLGNVLCRVLDAELNLLPPGVAGELCIGGAGLARGYLGR--PALTAerFVPDPLGEDGAR--LYRTGDRARWNADG 1519

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*....
gi 517718121  404 ELALLGRKDNQVKIRGNRVELGDIEHRLTNMAGIREAVVRMRAKADTPK 452
Cdd:PRK05691 1520 ALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVLVREGAAGAQ 1568
PRK05691 PRK05691
peptide synthase; Validated
 14-442 1.64e-51

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 200.78  E-value: 1.64e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   14 AAFPERKAIECGQQTLSYKELDAESDRICELLHAHGAAQYDHIGILMQDRCASIAAVIGILKLGGVFVPLDPLHPDERLV 93
Cdd:PRK05691 3731 AAHPQRIAASCLDQQWSYAELNRAANRLGHALRAAGVGVDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGLPAQRLQ 3810

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   94 TMLDTAEVSCLLCDDAQFERAETLQGHEG-----KYFVLRARQAMSVQAGSKEAYSHSANATdpiYIYFTSGSTGKPKAV 168
Cdd:PRK05691 3811 RIIELSRTPVLVCSAACREQARALLDELGcanrpRLLVWEEVQAGEVASHNPGIYSGPDNLA---YVIYTSGSTGLPKGV 3887

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  169 VGKNESLLHFMNWEASWLDLTDPMRVSQLTSIGFD-AVLRDIFVPICAGGTICIPESreIILDPLRLVHWLEHSRVHVVH 247
Cdd:PRK05691 3888 MVEQRGMLNNQLSKVPYLALSEADVIAQTASQSFDiSVWQFLAAPLFGARVEIVPNA--IAHDPQGLLAHVQAQGITVLE 3965

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  248 CTPSLFRFInhLSLTADSYPDLRYVLLAGETIRPESLKNW---YDNLGnrvrLVNLYGPTETTMIKLFYPIKPEDVHRES 324
Cdd:PRK05691 3966 SVPSLIQGM--LAEDRQALDGLRWMLPTGEAMPPELARQWlqrYPQIG----LVNAYGPAECSDDVAFFRVDLASTRGSY 4039

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  325 IPIGRPLPDTSVYLLDEQQQPVSGSEAGEICIATRYMTHGYFpsSHPDQTA--FIPDPcRDQSGEiMMYRTGDMGRWLPE 402
Cdd:PRK05691 4040 LPIGSPTDNNRLYLLDEALELVPLGAVGELCVAGTGVGRGYV--GDPLRTAlaFVPHP-FGAPGE-RLYRTGDLARRRSD 4115

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|
gi 517718121  403 GELALLGRKDNQVKIRGNRVELGDIEHRLTNMAGIREAVV 442
Cdd:PRK05691 4116 GVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAV 4155
starter-C_NRPS cd19533
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ...
 952-1363 1.32e-48

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: 179.49  E-value: 1.32e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  952 YPLTAAQMRVFMDEQLVNTGSGYHITTAFMIYGPIDVTRLERACGQLIERHEALRTSFDIVDGDPVQRIHEHCDFHLEIV 1031
Cdd:cd19533     2 LPLTSAQRGVWFAEQLDPEGSIYNLAEYLEITGPVDLAVLERALRQVIAEAETLRLRFTEEEGEPYQWIDPYTPVPIRHI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1032 HLQGQQL-HTAVNGCIR-----PFQLERAPLIRSILIPLAEEQHLLVLDMHHIVADGKSVFLLQRDLAALY----EGREL 1101
Cdd:cd19533    82 DLSGDPDpEGAAQQWMQedlrkPLPLDNDPLFRHALFTLGDNRHFWYQRVHHIVMDGFSFALFGQRVAEIYtallKGRPA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1102 HDLPV-----------QYVDFAQWQtsapvvedlrRQEQFWQSMFADYRPlpgiPTDHTPEANERSFAGGHITWEPDPVL 1170
Cdd:cd19533   162 PPAPFgsfldlveeeqAYRQSERFE----------RDRAFWTEQFEDLPE----PVSLARRAPGRSLAFLRRTAELPPEL 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1171 SRRLYAVAAEQQTTLFMVLLAAFHVLYAKYSAREEVTVGTPVEGRRRAEVRQVVGMFVNALAIRSYPEGDKPFSSFLQEI 1250
Cdd:cd19533   228 TRTLLEAAEAHGASWPSFFIALVAAYLHRLTGANDVVLGVPVMGRLGAAARQTPGMVANTLPLRLTVDPQQTFAELVAQV 307

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1251 RGTMLQAYEHQDYPLERLAKQLDLHHSRDHLmFDTVfsmLNYE--DFAVRSDDLQFEYAelpTLSEIYNLRVEIVESPER 1328
Cdd:cd19533   308 SRELRSLLRHQRYRYEDLRRDLGLTGELHPL-FGPT---VNYMpfDYGLDFGGVVGLTH---NLSSGPTNDLSIFVYDRD 380

                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 517718121 1329 ----LRGTFKYGQELYEARTVSQLAQDYERILAAVAESP 1363
Cdd:cd19533   381 desgLRIDFDANPALYSGEDLARHQERLLRLLEEAAADP 419
AFD_class_I cd04433
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ...
 151-442 1.69e-48

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: 176.32  E-value: 1.69e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  151 DPIYIYFTSGSTGKPKAVVGKNESLLHFMNWEASWLDLTDPMRVSQLTSIGFDAVLRDIFVPICAGGTICIPESReiilD 230
Cdd:cd04433     1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKF----D 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  231 PLRLVHWLEHSRVHVVHCTPSLFRFINHLSLTAD-SYPDLRYVLLAGETIRPESLKNWYDNLGnrVRLVNLYGPTETTMI 309
Cdd:cd04433    77 PEAALELIEREKVTILLGVPTLLARLLKAPESAGyDLSSLRALVSGGAPLPPELLERFEEAPG--IKLVNGYGLTETGGT 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  310 KLFYPikPEDVHRESIPIGRPLPDTSVYLLDEQQQPVSGSEAGEICIATRYMTHGYFpsSHPDQTAFIpdpcrDQSGeim 389
Cdd:cd04433   155 VATGP--PDDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYW--NNPEATAAV-----DEDG--- 222

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 517718121  390 MYRTGDMGRWLPEGELALLGRKDNQVKIRGNRVELGDIEHRLTNMAGIREAVV 442
Cdd:cd04433   223 WYRTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAV 275
PRK04813 PRK04813
D-alanine--poly(phosphoribitol) ligase subunit DltA;
17-442 2.14e-47

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


Pssm-ID: 235313 [Multi-domain]  Cd Length: 503  Bit Score: 178.17  E-value: 2.14e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   17 PERKAIECGQQTLSYKELDAESDRICELLHAHGAAQ------YDHIGILMqdrcasIAAVIGILKLGGVFVPLDPLHPDE 90
Cdd:PRK04813   16 PDFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLPDkspiivFGHMSPEM------LATFLGAVKAGHAYIPVDVSSPAE 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   91 RLVTMLDTAEVSCLLC-DDAQFERAETLqghegkyfVLRARQ-AMSVQAGSKEAYSHSANATDPIYIYFTSGSTGKPKAV 168
Cdd:PRK04813   90 RIEMIIEVAKPSLIIAtEELPLEILGIP--------VITLDElKDIFATGNPYDFDHAVKGDDNYYIIFTSGTTGKPKGV 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  169 VGKNESLLHFMNWEASWLDL-TDPMRVSQlTSIGFDAVLRDIFVPICAGGT-ICIPesREIILDPLRLVHWLEHSRVHVV 246
Cdd:PRK04813  162 QISHDNLVSFTNWMLEDFALpEGPQFLNQ-APYSFDLSVMDLYPTLASGGTlVALP--KDMTANFKQLFETLPQLPINVW 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  247 HCTPSlFRFINHL--SLTADSYPDLRYVLLAGETIR---PESLKNWYDNlgnrVRLVNLYGPTETTM----IKlfypIKP 317
Cdd:PRK04813  239 VSTPS-FADMCLLdpSFNEEHLPNLTHFLFCGEELPhktAKKLLERFPS----ATIYNTYGPTEATVavtsIE----ITD 309

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  318 EDVHR-ESIPIGRPLPDTSVYLLDEQQQPVSGSEAGEICIATRYMTHGYFpsSHPDQT--AFIpdpcrdQSGEIMMYRTG 394
Cdd:PRK04813  310 EMLDQyKRLPIGYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYL--NNPEKTaeAFF------TFDGQPAYHTG 381

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 517718121  395 DMGRwLPEGELALLGRKDNQVKIRGNRVELGDIEHRLTNMAGIREAVV 442
Cdd:PRK04813  382 DAGY-LEDGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVV 428
PRK05691 PRK05691
peptide synthase; Validated
 1-453 2.24e-47

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 187.30  E-value: 2.24e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121    1 MDNTIQYELARAFAAFPERKAIECGQQTLSYKELDAESDRICELLHAHGAAQYDHIGILMQDRCASIAAVIGILKLGGVF 80
Cdd:PRK05691 2186 LDQTLHGLFAAQAARTPQAPALTFAGQTLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAY 2265

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   81 VPLDPLHPDERLVTMLDTAEVSCLLCDDAQFEraeTLqgheGKYFVLRARQAMSVQAGSKEAYSHS--ANATDP---IYI 155
Cdd:PRK05691 2266 VPLDPEYPLERLHYMIEDSGIGLLLSDRALFE---AL----GELPAGVARWCLEDDAAALAAYSDAplPFLSLPqhqAYL 2338

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  156 YFTSGSTGKPKAV-VGKNESLLHFmnweASWLDLTDpMRVS----QLTSIGFDAVLRDIFVPICAGGTICIpeSREIILD 230
Cdd:PRK05691 2339 IYTSGSTGKPKGVvVSHGEIAMHC----QAVIERFG-MRADdcelHFYSINFDAASERLLVPLLCGARVVL--RAQGQWG 2411

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  231 PLRLVHWLEHSRVHVVHCTPSLFRFINHLSLTADSYPDLRYVLLAGETIRPESLKnwydnlgnRVR-------LVNLYGP 303
Cdd:PRK05691 2412 AEEICQLIREQQVSILGFTPSYGSQLAQWLAGQGEQLPVRMCITGGEALTGEHLQ--------RIRqafapqlFFNAYGP 2483

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  304 TETTMIKLFYPIkPEDVHRE--SIPIGRPLPDTSVYLLDEQQQPVSGSEAGEICIATRYMTHGYfpSSHPDQTA--FIPD 379
Cdd:PRK05691 2484 TETVVMPLACLA-PEQLEEGaaSVPIGRVVGARVAYILDADLALVPQGATGELYVGGAGLAQGY--HDRPGLTAerFVAD 2560

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517718121  380 PCRDQSGEimMYRTGDMGRWLPEGELALLGRKDNQVKIRGNRVELGDIEHRLTNMAGIREAVVrmrAKADTPKG 453
Cdd:PRK05691 2561 PFAADGGR--LYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVV---LALDTPSG 2629
PRK12316 PRK12316
peptide synthase; Provisional
 795-1361 4.31e-47

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 186.70  E-value: 4.31e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  795 LIAYYLADKMIDD--EQLSVYLRRFLPDYMIPARFIRLDKMPLTPNGKLDYNALPSPfEQDTTARIYKAPNSSTELKLLD 872
Cdd:PRK12316 3485 LVAYVVPEDEAGDlrEALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKALPRP-DAALLQQDYVAPVNELERRLAA 3563

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  873 IWTHILGIKRISADDHFLQIGVHSLNIMTLIAQVYEnFQVELPLEQVFEHDTLEEIA-------AYIDEQDSQYGVRIEP 945
Cdd:PRK12316 3564 IWADVLKLEQVGLTDNFFELGGDSIISLQVVSRARQ-AGIRFTPKDLFQHQTIQGLArvarvggGVAVDQGPVSGETLLL 3642

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  946 AAKQAYYPLTAAQMRVFMDEQLVNTGsgyhittafmiyGPIDVTRLERACGQLIERHEALRTSFDIVDGDPVQR---IHE 1022
Cdd:PRK12316 3643 PIQQQFFEEPVPERHHWNQSLLLKPR------------EALDAAALEAALQALVEHHDALRLRFVEDAGGWTAEhlpVEL 3710

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1023 HCDFHLEIVHLQGQQLHTAVNGCIRPFQLERAPLIRSILIPLAEEQHLLVLDMHHIVADGKSVFLLQRDLAALY------ 1096
Cdd:PRK12316 3711 GGALLWRAELDDAEELERLGEEAQRSLDLADGPLLRALLATLADGSQRLLLVIHHLVVDGVSWRILLEDLQQAYqqllqg 3790

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1097 EGRELHDLPVQYVDFAQWQTSAPVVEDLRRQEQFWQSMFADyrpLPG-IPTDHTPEANERSFAgGHITWEPDPVLSRRLY 1175
Cdd:PRK12316 3791 EAPRLPAKTSSFKAWAERLQEHARGEALKAELAYWQEQLQG---VSSeLPCDHPQGALQNRHA-ASVQTRLDRELTRRLL 3866

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1176 AVA-AEQQTTLFMVLLAAFHVLYAKYSAREEVTVGTPVEGRRR----AEVRQVVGMFVNALAIRSYPEGDKPFS--SFLQ 1248
Cdd:PRK12316 3867 QQApAAYRTQVNDLLLTALARVVCRWTGEASALVQLEGHGREDlfadIDLSRTVGWFTSLFPVRLSPVEDLGASikAIKE 3946

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1249 EIR-------GTMLQAYEHQDYPLERLAKQLDLHHSRDHL-MFDTVFSMlNYEDFAVRSDDLQFEYAELPTLSEIYNLRV 1320
Cdd:PRK12316 3947 QLRaipnkgiGFGLLRYLGDEESRRTLAGLPVPRITFNYLgQFDGSFDE-EMALFVPAGESAGAEQSPDAPLDNWLSLNG 4025

                         570       580       590       600
                  ....*....|....*....|....*....|....*....|.
gi 517718121 1321 EIVESPERLRGTFKygQELYEARTVSQLAQDYERILAAVAE 1361
Cdd:PRK12316 4026 RVYGGELSLDWTFS--REMFEEATIQRLADDYAAELTALVE 4064
C_PKS-NRPS cd20483
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
 953-1359 5.20e-47

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: 175.14  E-value: 5.20e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  953 PLTAAQMRVFMDEQLVNTGSGYHITTAFMIYGPIDVTRLERACGQLIERHEALRTSFDIVDGDPVQRIHEHCDFHLEIVH 1032
Cdd:cd20483     3 PMSTFQRRLWFLHNFLEDKTFLNLLLVCHIKGKPDVNLLQKALSELVRRHEVLRTAYFEGDDFGEQQVLDDPSFHLIVID 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1033 LQG-----QQLHTAV-NGCIRPFQLERAPLIRSILIPLAEEQHLLVLDMHHIVADGKSVFLLQRDLAALYE----GRELH 1102
Cdd:cd20483    83 LSEaadpeAALDQLVrNLRRQELDIEEGEVIRGWLVKLPDEEFALVLASHHIAWDRGSSKSIFEQFTALYDalraGRDLA 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1103 DLP---VQYVDFAQWQ----TSAPVVEDLrrqeQFWQSMFADYRP----LPGIPTDHTPEA-NERSFAGGHItwepDPVL 1170
Cdd:cd20483   163 TVPpppVQYIDFTLWHnallQSPLVQPLL----DFWKEKLEGIPDasklLPFAKAERPPVKdYERSTVEATL----DKEL 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1171 SRRLYAVAAEQQTTLFMVLLAAFHVLYAKYSAREEVTVGTpVEGRR-RAEVRQVVGMFVNALAIRSYPEGDKPFSSFLQE 1249
Cdd:cd20483   235 LARMKRICAQHAVTPFMFLLAAFRAFLYRYTEDEDLTIGM-VDGDRpHPDFDDLVGFFVNMLPIRCRMDCDMSFDDLLES 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1250 IRGTMLQAYEHQDYPLERLAKQLDLHHSRDHLmfdTVFSM-LNYE-----------DFAVRSDDLQfeyaELPTLSEIYn 1317
Cdd:cd20483   314 TKTTCLEAYEHSAVPFDYIVDALDVPRSTSHF---PIGQIaVNYQvhgkfpeydtgDFKFTDYDHY----DIPTACDIA- 385

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 517718121 1318 lrVEIVESPER-LRGTFKYGQELYEARTVSQLAQDYERILAAV 1359
Cdd:cd20483   386 --LEAEEDPDGgLDLRLEFSTTLYDSADMERFLDNFVTFLTSV 426
X-Domain_NRPS cd19546
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ...
 953-1363 5.58e-46

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: 172.28  E-value: 5.58e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  953 PLTAAQMRVFMDEQLVNTGSGYHITTAFMIYGPIDVTRLERACGQLIERHEALRTSFDIVDGDPVQRIH--EHCDFHLEI 1030
Cdd:cd19546     6 PATAGQLRTWLLARLDEETRGRHLSVALRLRGRLDRDALEAALGDVAARHEILRTTFPGDGGDVHQRILdaDAARPELPV 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1031 VHLQGQQLHTAV-NGCIRPFQLERAPLIRSILIPLAEEQHLLVLDMHHIVADGKSVFLLQRDLAALY----EGR--ELHD 1103
Cdd:cd19546    86 VPATEEELPALLaDRAAHLFDLTRETPWRCTLFALSDTEHVLLLVVHRIAADDESLDVLVRDLAAAYgarrEGRapERAP 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1104 LPVQYVDFAQWQTSAPVVEDLRR-----QEQFWQSMFADY---------RPLPGIPTDHTPEANERSFAGGHItwepdpv 1169
Cdd:cd19546   166 LPLQFADYALWERELLAGEDDRDsligdQIAYWRDALAGApdelelptdRPRPVLPSRRAGAVPLRLDAEVHA------- 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1170 lsrRLYAVAAEQQTTLFMVLLAAFHVLYAKYSAREEVTVGTpVEGRRRAEV--RQVVGMFVNALAIRSYPEGDKPFSSFL 1247
Cdd:cd19546   239 ---RLMEAAESAGATMFTVVQAALAMLLTRLGAGTDVTVGT-VLPRDDEEGdlEGMVGPFARPLALRTDLSGDPTFRELL 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1248 QEIRGTMLQAYEHQDYPLERLAKQLDLHHSRD-HLMFDTVFSmlnyedfaVRSDDLQ-FEYAELPTLSEI---------- 1315
Cdd:cd19546   315 GRVREAVREARRHQDVPFERLAELLALPPSADrHPVFQVALD--------VRDDDNDpWDAPELPGLRTSpvplgteame 386

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 517718121 1316 YNLRVEIVE------SPERLRGTFKYGQELYEARTVSQLAQDYERILAAVAESP 1363
Cdd:cd19546   387 LDLSLALTErrnddgDPDGLDGSLRYAADLFDRATAAALARRLVRVLEQVAADP 440
A_NRPS_acs4 cd17654
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ...
 28-442 4.98e-45

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: 169.96  E-value: 4.98e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   28 TLSYKELDAESDRICELLHAHGAAQYDHIGILMQDRCASIAAVIGILKLGGVFVPLDPLHPDERLVTMLDTAEVSCLLCD 107
Cdd:cd17654    16 TVSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVMKKCHVSYLLQN 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  108 DaqferaetLQGHEGKYFVLRARQ-AMSVQAGSkeayshsanatdpIYIYFTSGSTGKPKAVVGKNESLLHFMNWEASWL 186
Cdd:cd17654    96 K--------ELDNAPLSFTPEHRHfNIRTDECL-------------AYVIHTSGTTGTPKIVAVPHKCILPNIQHFRSLF 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  187 DLTdPMRVSQLTSIG-FDAVLRDIFVPICAGGTICIPESrEIILDPLRLVHWL-EHSRVHVVHCTPSLFR-----FINHL 259
Cdd:cd17654   155 NIT-SEDILFLTSPLtFDPSVVEIFLSLSSGATLLIVPT-SVKVLPSKLADILfKRHRITVLQATPTLFRrfgsqSIKST 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  260 SLTADSypDLRYVLLAGETIrPES--LKNWYdNLGNRVRLVNLYGPTETTMIKLFYPIKPEDvhrESIPIGRPLPDTSVY 337
Cdd:cd17654   233 VLSATS--SLRVLALGGEPF-PSLviLSSWR-GKGNRTRIFNIYGITEVSCWALAYKVPEED---SPVQLGSPLLGTVIE 305

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  338 LLDEQQQPVSGSEAGE----ICIATRYMThgyfpsshpdqtafIPDPCrdqsgeimMYRTGDMGRwLPEGELALLGRKDN 413
Cdd:cd17654   306 VRDQNGSEGTGQVFLGglnrVCILDDEVT--------------VPKGT--------MRATGDFVT-VKDGELFFLGRKDS 362

                         410       420
                  ....*....|....*....|....*....
gi 517718121  414 QVKIRGNRVELGDIEHRLTNMAGIREAVV 442
Cdd:cd17654   363 QIKRRGKRINLDLIQQVIESCLGVESCAV 391
CT_NRPS-like cd19542
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ...
 952-1363 2.53e-43

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: 163.25  E-value: 2.53e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  952 YPLTAAQMRVFMdEQLVNTGSgYHITTAFMIYGPIDVTRLERACGQLIERHEALRTSFDIVDGDP--VQRIHEHCDFHLE 1029
Cdd:cd19542     2 YPCTPMQEGMLL-SQLRSPGL-YFNHFVFDLDSSVDVERLRNAWRQLVQRHDILRTVFVESSAEGtfLQVVLKSLDPPIE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1030 IVHLQGQQLHTAVNGCIRPFQLERAPLIRSILIPLAEEQHLLVLDMHHIVADGKSVFLLQRDLAALYEGRELHDlPVQYV 1109
Cdd:cd19542    80 EVETDEDSLDALTRDLLDDPTLFGQPPHRLTLLETSSGEVYLVLRISHALYDGVSLPIILRDLAAAYNGQLLPP-APPFS 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1110 DFAQ--WQTSAPvvedlrRQEQFWQSMFADYRPLPgIPTDHTPEANERSfagGHITWEPdpvlSRRLYAVAAEQQTTLFM 1187
Cdd:cd19542   159 DYISylQSQSQE------ESLQYWRKYLQGASPCA-FPSLSPKRPAERS---LSSTRRS----LAKLEAFCASLGVTLAS 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1188 VLLAAFHVLYAKYSAREEVTVGTPVEGR--RRAEVRQVVGMFVNALAIRSYPEGDKPFSSFLQEIRGTMLQAYEHQDYPL 1265
Cdd:cd19542   225 LFQAAWALVLARYTGSRDVVFGYVVSGRdlPVPGIDDIVGPCINTLPVRVKLDPDWTVLDLLRQLQQQYLRSLPHQHLSL 304

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1266 ERLAKQLDLHHSRdhLMFDTVFSMLNYEDFAVRSDDLQFE----YAELPTLseiYNLRVEIVESPERLRGTFKYGQELYE 1341
Cdd:cd19542   305 REIQRALGLWPSG--TLFNTLVSYQNFEASPESELSGSSVfelsAAEDPTE---YPVAVEVEPSGDSLKVSLAYSTSVLS 379

                         410       420
                  ....*....|....*....|..
gi 517718121 1342 ARTVSQLAQDYERILAAVAESP 1363
Cdd:cd19542   380 EEQAEELLEQFDDILEALLANP 401
alpha_am_amid TIGR03443
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ...
 5-449 2.66e-42

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: 169.86  E-value: 2.66e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121     5 IQYELARAFAAFPER------KAIECGQ---QTLSYKELDAESDRICELLHAHGAAQ------YDHIGILMqdrcasIAA 69
Cdd:TIGR03443  238 IHDIFADNAEKHPDRtcvvetPSFLDPSsktRSFTYKQINEASNILAHYLLKTGIKRgdvvmiYAYRGVDL------VVA 311

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121    70 VIGILKLGGVFVPLDPLHPDERLVTMLDTAEVSCLLCddaqFERAETLQGHEGKY----FVLRAR-QAMSVQA-GSKEAY 143
Cdd:TIGR03443  312 VMGVLKAGATFSVIDPAYPPARQTIYLSVAKPRALIV----IEKAGTLDQLVRDYidkeLELRTEiPALALQDdGSLVGG 387

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   144 SHSANATDPIYIY---------------------FTSGSTGKPKAVVGKNESLLHFMNWEASWLDLTDPMRVSQLTSIGF 202
Cdd:TIGR03443  388 SLEGGETDVLAPYqalkdtptgvvvgpdsnptlsFTSGSEGIPKGVLGRHFSLAYYFPWMAKRFGLSENDKFTMLSGIAH 467

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   203 DAVLRDIFVPICAGGTICIPeSREIILDPLRLVHWLEHSRVHVVHCTPSLFRFinhLSLTADS-YPDLRYVLLAGET-IR 280
Cdd:TIGR03443  468 DPIQRDMFTPLFLGAQLLVP-TADDIGTPGRLAEWMAKYGATVTHLTPAMGQL---LSAQATTpIPSLHHAFFVGDIlTK 543

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   281 PESLKnwYDNLGNRVRLVNLYGPTETTMIKLFYPIKP--EDVH-----RESIPIGRPLPDtsVYLL----DEQQQPVSGS 349
Cdd:TIGR03443  544 RDCLR--LQTLAENVCIVNMYGTTETQRAVSYFEIPSrsSDSTflknlKDVMPAGKGMKN--VQLLvvnrNDRTQTCGVG 619

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   350 EAGEICI----------------ATRYMTHGYFPSSH-PDQTAFIPDPC-------RDQsgeimMYRTGDMGRWLPEGEL 405
Cdd:TIGR03443  620 EVGEIYVragglaegylglpelnAEKFVNNWFVDPSHwIDLDKENNKPErefwlgpRDR-----LYRTGDLGRYLPDGNV 694

                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....
gi 517718121   406 ALLGRKDNQVKIRGNRVELGDIEHRLTNMAGIREAVVRMRAKAD 449
Cdd:TIGR03443  695 ECCGRADDQVKIRGFRIELGEIDTHLSQHPLVRENVTLVRRDKD 738
A_NRPS_alphaAR cd17647
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ...
 16-455 4.51e-41

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: 159.61  E-value: 4.51e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   16 FPERKAI-------ECGQQTLSYKELDAESDRICELLHAHGAAQYDHIGILMQDRCASIAAVIGILKLGGVFVPLDPLHP 88
Cdd:cd17647     1 FPERTCVvetpslnSSKTRSFTYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   89 DERLVTMLDTAEVSCLLcddaqferaetlqghegkyfVLRArqaMSVQAGSkeayshSANATdpiyIYFTSGSTGKPKAV 168
Cdd:cd17647    81 PARQNIYLGVAKPRGLI--------------------VIRA---AGVVVGP------DSNPT----LSFTSGSEGIPKGV 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  169 VGKNESLLHFMNWEASWLDLTDPMRVSQLTSIGFDAVLRDIFVPICAGGTICIPeSREIILDPLRLVHWLEHSRVHVVHC 248
Cdd:cd17647   128 LGRHFSLAYYFPWMAKRFNLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLVP-TQDDIGTPGRLAEWMAKYGATVTHL 206

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  249 TPSLFRFinhlsLTADS---YPDLRYVLLAGET-IRPESLKnwYDNLGNRVRLVNLYGPTETTMIKLFY--PIKPEDVH- 321
Cdd:cd17647   207 TPAMGQL-----LTAQAttpFPKLHHAFFVGDIlTKRDCLR--LQTLAENVRIVNMYGTTETQRAVSYFevPSRSSDPTf 279

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  322 ----RESIPIGRPLPDTSVYLLD--EQQQPVSGSEAGEICIATRYMTHGYFPSSHPDQTAFIP----DPC----RDQSGE 387
Cdd:cd17647   280 lknlKDVMPAGRGMLNVQLLVVNrnDRTQICGIGEVGEIYVRAGGLAEGYRGLPELNKEKFVNnwfvEPDhwnyLDKDNN 359

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517718121  388 I-----------MMYRTGDMGRWLPEGELALLGRKDNQVKIRGNRVELGDIEHRLTNMAGIREAVVRMRAKADTPKGMA 455
Cdd:cd17647   360 EpwrqfwlgprdRLYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENITLVRRDKDEEPTLV 438
PRK12316 PRK12316
peptide synthase; Provisional
 795-1240 1.50e-40

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 165.13  E-value: 1.50e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  795 LIAYYLADKMIDD--EQLSVYLRRFLPDYMIPARFIRLDKMPLTPNGKLDYNALPSPfEQDTTARIYKAPNSSTELKLLD 872
Cdd:PRK12316  947 LVGYVVLESEGGDwrEALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKALPAP-EASVAQQGYVAPRNALERTLAA 1025

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  873 IWTHILGIKRISADDHFLQIGVHSLNIMTLIAQVYENfQVELPLEQVFEHDTLEEIAAyIDEQDSQYGVRIEPAAKQAyy 952
Cdd:PRK12316 1026 IWQDVLGVERVGLDDNFFELGGDSIVSIQVVSRARQA-GIQLSPRDLFQHQTIRSLAL-VAKAGQATAADQGPASGEV-- 1101

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  953 PLTAAQMRVFmdEQLVNTGSGYHITTAFMIYGPIDVTRLERACGQLIERHEALRTSFDIVDGDPVQRIHEHCDFH-LEIV 1031
Cdd:PRK12316 1102 ALAPVQRWFF--EQAIPQRQHWNQSLLLQARQPLDPDRLGRALERLVAHHDALRLRFREEDGGWQQAYAAPQAGEvLWQR 1179

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1032 HLQGQQ-LHTAVNGCIRPFQLERAPLIRSILIPLAEEQHLLVLDMHHIVADGKSVFLLQRDLAALYEGRELhDLPVQYVD 1110
Cdd:PRK12316 1180 QAASEEeLLALCEEAQRSLDLEQGPLLRALLVDMADGSQRLLLVIHHLVVDGVSWRILLEDLQRAYADLDA-DLPARTSS 1258

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1111 FAQW----QTSAPVvedLRRQEQFWQsmfadyRPLPGIPTD---HTPEANERSFAGGHITWEPDPVLSRRLYAVA-AEQQ 1182
Cdd:PRK12316 1259 YQAWarrlHEHAGA---RAEELDYWQ------AQLEDAPHElpcENPDGALENRHERKLELRLDAERTRQLLQEApAAYR 1329

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517718121 1183 TTLFMVLLAAFHVLYAKYSAREEVTVgtPVEGRRRA------EVRQVVGMFVNALAIRSYPEGD 1240
Cdd:PRK12316 1330 TQVNDLLLTALARVTCRWSGQASVLV--QLEGHGREdlfediDLSRTVGWFTSLFPVRLTPAAD 1391
DCL_NRPS-like cd19536
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ...
 952-1363 4.17e-40

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: 154.53  E-value: 4.17e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  952 YPLTAAQMRVFMDEQLVNTGSGYHITTAFMIYGPIDVTRLERACGQLIERHEALRTSFDIVD-GDPVQRIHEHCDFHLEI 1030
Cdd:cd19536     2 YPLSSLQEGMLFHSLLNPGGSVYLHNYTYTVGRRLNLDLLLEALQVLIDRHDILRTSFIEDGlGQPVQVVHRQAQVPVTE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1031 VHL-QGQQLHTAVNGCI-----RPFQLERAPLIRSILIPLAEEQH-LLVLDMHHIVADGKSVFLLQRDLAALY----EGR 1099
Cdd:cd19536    82 LDLtPLEEQLDPLRAYKeetkiRRFDLGRAPLVRAALVRKDERERfLLVISDHHSILDGWSLYLLVKEILAVYnqllEYK 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1100 ELHDLPVQ-YVDFAQWQTSApvvEDLRRQEQFWQSMF--ADYRPLPGIPTDHTPEANERSfagghiTWEPDPVLSRRLYA 1176
Cdd:cd19536   162 PLSLPPAQpYRDFVAHERAS---IQQAASERYWREYLagATLATLPALSEAVGGGPEQDS------ELLVSVPLPVRSRS 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1177 VAAEQQTTLFMVLLAAFHVLYAKYSAREEVTVGTPVEGRRR--AEVRQVVGMFVNALAIR-SYPEGdkPFSSFLQEIRGT 1253
Cdd:cd19536   233 LAKRSGIPLSTLLLAAWALVLSRHSGSDDVVFGTVVHGRSEetTGAERLLGLFLNTLPLRvTLSEE--TVEDLLKRAQEQ 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1254 MLQAYEHQDYPLeRLAKQldlhHSRDHLMFDtvfSMLNYEDFavrsdDLQFEyAELPTLSEIY-----------NLRVEI 1322
Cdd:cd19536   311 ELESLSHEQVPL-ADIQR----CSEGEPLFD---SIVNFRHF-----DLDFG-LPEWGSDEGMrrgllfsefksNYDVNL 376

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 517718121 1323 VESPE--RLRGTFKYGQELYEARTVSQLAQDYERILAAVAESP 1363
Cdd:cd19536   377 SVLPKqdRLELKLAYNSQVLDEEQAQRLAAYYKSAIAELATAP 419
Acs COG0365
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
9-442 5.28e-40

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


Pssm-ID: 440134 [Multi-domain]  Cd Length: 565  Bit Score: 157.58  E-value: 5.28e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121    9 LARAFAAFPERKAI----ECG-QQTLSYKELDAESDRICELLHAHGAAQYDHIGILMQDRCASIAAVIGILKLGGVFVPL 83
Cdd:COG0365    15 LDRHAEGRGDKVALiwegEDGeERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSPV 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   84 DP-LHPDErLVTMLDTAEVSCLLCDDAQFERaetlqgheGKYFVLRAR--QAMS-------------------------- 134
Cdd:COG0365    95 FPgFGAEA-LADRIEDAEAKVLITADGGLRG--------GKVIDLKEKvdEALEelpslehvivvgrtgadvpmegdldw 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  135 ---VQAGSKEAYSHSANATDPIYIYFTSGSTGKPKAVVGKNESLLHFMNWEAS-WLDLTDPMRVSQLTSIGFDAVLRDIF 210
Cdd:COG0365   166 delLAAASAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKyVLDLKPGDVFWCTADIGWATGHSYIV 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  211 V-PICAGGTICIPESREIILDPLRLVHWLEHSRVHVVHCTPSLFR-FINHLSLTADSY--PDLRYVLLAGETIRPESLKN 286
Cdd:COG0365   246 YgPLLNGATVVLYEGRPDFPDPGRLWELIEKYGVTVFFTAPTAIRaLMKAGDEPLKKYdlSSLRLLGSAGEPLNPEVWEW 325

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  287 WYDNLGnrVRLVNLYGPTETTMIKL-FYPIKPedVHRESipIGRPLPDTSVYLLDEQQQPVSGSEAGEICIATRY--MTH 363
Cdd:COG0365   326 WYEAVG--VPIVDGWGQTETGGIFIsNLPGLP--VKPGS--MGKPVPGYDVAVVDEDGNPVPPGEEGELVIKGPWpgMFR 399

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  364 GYFpsSHPDQTA-----FIPDpcrdqsgeimMYRTGDMGRWLPEGELALLGRKDNQVKIRGNRVELGDIEHRLTNMAGIR 438
Cdd:COG0365   400 GYW--NDPERYRetyfgRFPG----------WYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVA 467


                  ....
gi 517718121  439 EAVV 442
Cdd:COG0365   468 EAAV 471
PRK12316 PRK12316
peptide synthase; Provisional
 952-1372 5.59e-38

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 156.66  E-value: 5.59e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  952 YPLTAAQMRVFMdEQLVNTGSGYHITTAFMIYGPIDVTRLERACGQLIERHEALRTSFDIVD--GDPVQRIHEHCDFHLE 1029
Cdd:PRK12316 4103 YPLSPMQQGMLF-HSLYEQEAGDYINQMRVDVQGLDVERFRAAWQAALDRHDVLRSGFVWQGelGRPLQVVHKQVSLPFA 4181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1030 IVHLQGQQ------LHTAVNGCIRPFQLERAPLIRSILIPLAEEQHLLVLDMHHIVADGKSVFLLQRDLAALYEGRELHD 1103
Cdd:PRK12316 4182 ELDWRGRAdlqaalDALAAAERERGFDLQRAPLLRLVLVRTAEGRHHLIYTNHHILMDGWSNSQLLGEVLERYSGRPPAQ 4261

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1104 LPVQYVDFAQWQTSapvvEDLRRQEQFWQSMFADYRPlPGIPTDHTPEANERSFAG-GHITWEPDPVLSRRLYAVAAEQQ 1182
Cdd:PRK12316 4262 PGGRYRDYIAWLQR----QDAAASEAFWREQLAALDE-PTRLAQAIARADLRSANGyGEHVRELDATATARLREFARTQR 4336

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1183 TTLFMVLLAAFHVLYAKYSAREEVTVGTPVEGR--RRAEVRQVVGMFVNALAIRSYPEGDKPFSSFLQEIRGTMLQAYEH 1260
Cdd:PRK12316 4337 VTLNTLVQAAWLLLLQRYTGQDTVAFGATVAGRpaELPGIEGQIGLFINTLPVIATPRAQQSVVEWLQQVQRQNLALREH 4416

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1261 QDYPLERLAKQLDLHHSRdhlMFDtvfSMLNYEDFAVrSDDLQFEYAELPTLSEIYN---------LRVEIVESperLRG 1331
Cdd:PRK12316 4417 EHTPLYEIQRWAGQGGEA---LFD---SLLVFENYPV-SEALQQGAPGGLRFGEVTNheqtnypltLAVGLGET---LSL 4486

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|.
gi 517718121 1332 TFKYGQELYEARTVSQLAQDYERILAAVAESPNIKLKDIEI 1372
Cdd:PRK12316 4487 QFSYDRGHFDAATIERLARHLTNLLEAMAEDPQRRLGELQL 4527
MACS_like cd05972
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ...
 29-442 1.95e-37

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: 146.71  E-value: 1.95e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   29 LSYKELDAESDRICELLHAHGAAQYDHIGILMQDRCASIAAVIGILKLGGVFVPLDPLHPDERLVTMLDTAEVSCLLCDd 108
Cdd:cd05972     1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTD- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  109 aqferaetlqghegkyfvlrarqamsvqagskeayshsanATDPIYIYFTSGSTGKPKAVVGKNESLLHFMNWEASWLDL 188
Cdd:cd05972    80 ----------------------------------------AEDPALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLGL 119

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  189 TDPMRVSQLTSIGF-DAVLRDIFVPICAGGTICIPESREiiLDPLRLVHWLEHSRVHVVHCTPSLFRFINHLSLTADSYP 267
Cdd:cd05972   120 RPDDIHWNIADPGWaKGAWSSFFGPWLLGATVFVYEGPR--FDAERILELLERYGVTSFCGPPTAYRMLIKQDLSSYKFS 197

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  268 DLRYVLLAGETIRPESLKNWYDNLGNRVRlvNLYGPTETTMI---KLFYPIKPEDvhresipIGRPLPDTSVYLLDEQQQ 344
Cdd:cd05972   198 HLRLVVSAGEPLNPEVIEWWRAATGLPIR--DGYGQTETGLTvgnFPDMPVKPGS-------MGRPTPGYDVAIIDDDGR 268

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  345 PVSGSEAGEICIatRYMTHGYFpsshpdqTAFIPDPCRDQS---GEImmYRTGDMGRWLPEGELALLGRKDNQVKIRGNR 421
Cdd:cd05972   269 ELPPGEEGDIAI--KLPPPGLF-------LGYVGDPEKTEAsirGDY--YLTGDRAYRDEDGYFWFVGRADDIIKSSGYR 337

                         410       420
                  ....*....|....*....|.
gi 517718121  422 VELGDIEHRLTNMAGIREAVV 442
Cdd:cd05972   338 IGPFEVESALLEHPAVAEAAV 358
PRK05691 PRK05691
peptide synthase; Validated
 808-1237 5.22e-37

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 153.40  E-value: 5.22e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  808 EQLSVYLRRFLPDYMIPARFIRLDKMPLTPNGKLDYNALPSP-FEQDTTAriYKAPNSSTELKLLDIWTHILGIKRISAD 886
Cdd:PRK05691 2653 EALKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRALPAPdPELNRQA--YQAPRSELEQQLAQIWREVLNVERVGLG 2730

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  887 DHFLQIG---VHSLNIMTLIAQVYENFQvelPlEQVFEHDTLEEIAAYIDEQDSqygVRIEPAAKQAYYPLTAAQmRVFM 963
Cdd:PRK05691 2731 DNFFELGgdsILSIQVVSRARQLGIHFS---P-RDLFQHQTVQTLAAVATHSEA---AQAEQGPLQGASGLTPIQ-HWFF 2802

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  964 DEQLVNTgsgYHITTAFMI--YGPIDVTRLERACGQLIERHEALRTSFDIVDGdpvqrihehcDFHLEIVHLQGQQLHTA 1041
Cdd:PRK05691 2803 DSPVPQP---QHWNQALLLepRQALDPALLEQALQALVEHHDALRLRFSQADG----------RWQAEYRAVTAQELLWQ 2869

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1042 VN-----GCI-------RPFQLERAPLIRSILIPLAEEQHLLVLDMHHIVADGKSVFLLQRDLAALYegRELHD-----L 1104
Cdd:PRK05691 2870 VTvadfaECAalfadaqRSLDLQQGPLLRALLVDGPQGQQRLLLAIHHLVVDGVSWRVLLEDLQALY--RQLSAgaepaL 2947

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1105 PVQYVDFAQWQT---SAPVVEDLRRQEQFWQSMFADyrPLPGIPTDHtPEANERSFAGGHITWEPDPVLSRRLYAVA-AE 1180
Cdd:PRK05691 2948 PAKTSAFRDWAArlqAYAGSESLREELGWWQAQLGG--PRAELPCDR-PQGGNLNRHAQTVSVRLDAERTRQLLQQApAA 3024

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517718121 1181 QQTTLFMVLLAAFHVLYAKYSAREEVTVgtPVEGRRRA------EVRQVVGMFVNALAIRSYP 1237
Cdd:PRK05691 3025 YRTQVNDLLLTALARVLCRWSGQPSVLV--QLEGHGREalfddiDLTRSVGWFTSAYPLRLTP 3085
PRK12467 PRK12467
peptide synthase; Provisional
 808-1237 2.66e-35

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 148.00  E-value: 2.66e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  808 EQLSVYLRRFLPDYMIPARFIRLDKMPLTPNGKLDYNALPSPfEQDTTARIYKAPNSSTELKLLDIWTHILGIKRISADD 887
Cdd:PRK12467 2041 AILKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKALPAP-DASELQQAYVAPQSELEQRLAAIWQDVLGLEQVGLHD 2119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  888 HFLQIGVHSLNIMTLIAQVYENfQVELPLEQVFEHDTLEEIAAYIDEQDSqyGVRIEPAAKQAYYPLTAAQmRVFMDEQL 967
Cdd:PRK12467 2120 NFFELGGDSIISIQVVSRARQA-GIRFTPKDLFQHQTVQSLAAVAQEGDG--TVSIDQGPVTGDLPLLPIQ-QMFFADDI 2195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  968 VNTgsgYHITTAFMI--YGPIDVTRLERACGQLIERHEALRTSFDIVDGDpVQRIHEHCDFHLEIVHLQ-----GQQLHT 1040
Cdd:PRK12467 2196 PER---HHWNQSVLLepREALDAELLEAALQALLVHHDALRLGFVQEDGG-WSAMHRAPEQERRPLLWQvvvadKEELEA 2271

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1041 AVNGCIRPFQLERAPLIRSILIPLAEEQHLLVLDMHHIVADGKSVFLLQRDLAA----LYEGRELHdLPVQYVDFAQW-- 1114
Cdd:PRK12467 2272 LCEQAQRSLDLEEGPLLRAVLATLPDGSQRLLLVIHHLVVDGVSWRILLEDLQTayrqLQGGQPVK-LPAKTSAFKAWae 2350

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1115 --QTSAPVVEdLRRQEQFWQSMFADYRplPGIPTDHTPEANERSFAgGHITWEPDPVLSRRLYAVA-AEQQTTLFMVLLA 1191
Cdd:PRK12467 2351 rlQTYAASAA-LADELGYWQAQLQGAS--TELPCDHPQGGLQRRHA-ASVTTHLDSEWTRRLLQEApAAYRTQVNDLLLT 2426

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 517718121 1192 AFHVLYAKYSAREEVTVgtPVEGRRRAE------VRQVVGMFVNALAIRSYP 1237
Cdd:PRK12467 2427 ALARVIARWTGQASTLI--QLEGHGREDlfdeidLTRTVGWFTSLYPVKLSP 2476
FC-FACS_FadD_like cd05936
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ...
 9-442 2.20e-34

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: 138.85  E-value: 2.20e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121    9 LARAFAAFPERKAIECGQQTLSYKELDAESDRICELLHAHGAAQYDHIGILMQDRCASIAAVIGILKLGGVFVPLDPLHP 88
Cdd:cd05936     5 LEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYT 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   89 DERLVTMLDTAEVSCLLCDDAqFERAetlqghegkyfvlrarqamsVQAGSKEAYSHSANATDPIYIYFTSGSTGKPKAV 168
Cdd:cd05936    85 PRELEHILNDSGAKALIVAVS-FTDL--------------------LAAGAPLGERVALTPEDVAVLQYTSGTTGVPKGA 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  169 VgknesLLH---FMNWEASWLDLTDPMRVSQLT--------SIGFDAVLrdiFVPICAGGTIcIPESReiiLDPLRLVHW 237
Cdd:cd05936   144 M-----LTHrnlVANALQIKAWLEDLLEGDDVVlaalplfhVFGLTVAL---LLPLALGATI-VLIPR---FRPIGVLKE 211

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  238 LEHSRVHVVHCTPSLF-RFINHLSLTADSYPDLRYVLLAGETIRPESLKNWYDNLGnrVRLVNLYGPTETTMIKLFYPIk 316
Cdd:cd05936   212 IRKHRVTIFPGVPTMYiALLNAPEFKKRDFSSLRLCISGGAPLPVEVAERFEELTG--VPIVEGYGLTETSPVVAVNPL- 288

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  317 peDVHRESIPIGRPLPDTSVYLLDEQQQPVSGSEAGEICIATRYMTHGYFPssHPDQTAfipdpcrdqsgEIMM---YRT 393
Cdd:cd05936   289 --DGPRKPGSIGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWN--RPEETA-----------EAFVdgwLRT 353

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*....
gi 517718121  394 GDMGRWLPEGELALLGRKDNQVKIRGNRVELGDIEHRLTNMAGIREAVV 442
Cdd:cd05936   354 GDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAV 402
FACL_like_6 cd05922
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 44-442 2.00e-33

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: 135.65  E-value: 2.00e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   44 LLHAHGAAQYDHIGILMQDRCASIAAVIGILKLGG----VFVPLDPLHPDERLVTMLDTAEVSCLLCDdaqferaETLQG 119
Cdd:cd05922     9 ALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGrlglVFVPLNPTLKESVLRYLVADAGGRIVLAD-------AGAAD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  120 HEGKYFVLRARQAMSVQAGSKEAYSHSANA-----TDPIYIYFTSGSTGKPKAVVGKNESLLHFMNWEASWLDLTDPMRV 194
Cdd:cd05922    82 RLRDALPASPDPGTVLDADGIRAARASAPAhevshEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADDRA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  195 SQLTSIGFDAVLRDIFVPICAGGTICIPESREIildPLRLVHWLEHSRVHVVHCTPSLFRFINHLSLTADSYPDLRYVLL 274
Cdd:cd05922   162 LTVLPLSYDYGLSVLNTHLLRGATLVLTNDGVL---DDAFWEDLREHGATGLAGVPSTYAMLTRLGFDPAKLPSLRYLTQ 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  275 AGETIRPESLKNWYDnLGNRVRLVNLYGPTETTMIKLFYPikPEDVHRESIPIGRPLPDTSVYLLDEQQQPVSGSEAGEI 354
Cdd:cd05922   239 AGGRLPQETIARLRE-LLPGAQVYVMYGQTEATRRMTYLP--PERILEKPGSIGLAIPGGEFEILDDDGTPTPPGEPGEI 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  355 CIATRYMTHGYFpsshpDQTAFIPDPcrdqSGEIMMYRTGDMGRWLPEGELALLGRKDNQVKIRGNRVELGDIEHRLTNM 434
Cdd:cd05922   316 VHRGPNVMKGYW-----NDPPYRRKE----GRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSI 386


                  ....*...
gi 517718121  435 AGIREAVV 442
Cdd:cd05922   387 GLIIEAAA 394
PRK12316 PRK12316
peptide synthase; Provisional
 952-1370 2.55e-31

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 134.70  E-value: 2.55e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  952 YPLTAAQMRVFMdEQLVNTGSGYHITTAFMIYGPIDVTRLERACGQLIERHEALRTSFDIVDG--DPVQRIHEHCDFHLE 1029
Cdd:PRK12316 1557 YPLSPMQQGMLF-HSLYEQEAGDYINQLRVDVQGLDPDRFRAAWQATVDRHEILRSGFLWQDGleQPLQVIHKQVELPFA 1635

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1030 IVHLQGQ-QLHTAVNGCI-----RPFQLERAPLIRSILIPLAEEQHLLVLDMHHIVADGKSVFLLQRDLAALYEGRELHD 1103
Cdd:PRK12316 1636 ELDWRGReDLGQALDALAqaerqKGFDLTRAPLLRLVLVRTGEGRHHLIYTNHHILMDGWSNAQLLGEVLQRYAGQPVAA 1715

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1104 LPVQYVDFAQWQTSapvvEDLRRQEQFWQSMFADYRpLPGIPTDHTPEANERSFAGGHITwEPDPVLSRRLYAVAAEQQT 1183
Cdd:PRK12316 1716 PGGRYRDYIAWLQR----QDAAASEAFWKEQLAALE-EPTRLAQAARTEDGQVGYGDHQQ-LLDPAQTRALAEFARAQKV 1789

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1184 TLFMVLLAAFHVLYAKYSAREEVTVGTPVEGrRRAE---VRQVVGMFVNALAIRSYPEGDKPFSSFLQEIRGTMLQAYEH 1260
Cdd:PRK12316 1790 TLNTLVQAAWLLLLQRYTGQETVAFGATVAG-RPAElpgIEQQIGLFINTLPVIAAPRPDQSVADWLQEVQALNLALREH 1868

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1261 QDYPL---ERLAKQldlhhsRDHLMFDtvfSMLNYEDFAVrSDDLQ------FEYAELPTLSEI-YNLRVEiVESPERLR 1330
Cdd:PRK12316 1869 EHTPLydiQRWAGQ------GGEALFD---SLLVFENYPV-AEALKqgapagLVFGRVSNHEQTnYPLTLA-VTLGETLS 1937

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|
gi 517718121 1331 GTFKYGQELYEARTVSQLAQDYERILAAVAESPNIKLKDI 1370
Cdd:PRK12316 1938 LQYSYDRGHFDAAAIERLDRHLLHLLEQMAEDAQAALGEL 1977
FACL_FadD13-like cd17631
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ...
 9-442 3.23e-31

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: 128.50  E-value: 3.23e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121    9 LARAFAAFPERKAIECGQQTLSYKELDAESDRICELLHAHGAAQYDHIGILMQDRCASIAAVIGILKLGGVFVPLDplhp 88
Cdd:cd17631     1 LRRRARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLN---- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   89 derlvTMLDTAEVSCLLCDdaqferaetlqghegkyfvlrarqamsvqAGSKEAYShsanatDPIYIYFTSGSTGKPKAV 168
Cdd:cd17631    77 -----FRLTPPEVAYILAD-----------------------------SGAKVLFD------DLALLMYTSGTTGRPKGA 116

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  169 VGKNESLL-HFMNWEASWLDLTDP--MRVSQLTSIGFDAVLrdIFVPICAGGTICIPESreiiLDPLRLVHWLEHSRVHV 245
Cdd:cd17631   117 MLTHRNLLwNAVNALAALDLGPDDvlLVVAPLFHIGGLGVF--TLPTLLRGGTVVILRK----FDPETVLDLIERHRVTS 190

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  246 VHCTPSLFRF-INHLSLTADSYPDLRYVLLAGEtIRPESLKNWYDNLGnrVRLVNLYGPTETTMIKLFypIKPEDVHRES 324
Cdd:cd17631   191 FFLVPTMIQAlLQHPRFATTDLSSLRAVIYGGA-PMPERLLRALQARG--VKFVQGYGMTETSPGVTF--LSPEDHRRKL 265

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  325 IPIGRPLPDTSVYLLDEQQQPVSGSEAGEICIATRYMTHGYFpsSHPDQTA-FIPDpcrdqsGeimMYRTGDMGRWLPEG 403
Cdd:cd17631   266 GSAGRPVFFVEVRIVDPDGREVPPGEVGEIVVRGPHVMAGYW--NRPEATAaAFRD------G---WFHTGDLGRLDEDG 334

                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 517718121  404 ELALLGRKDNQVKIRGNRVELGDIEHRLTNMAGIREAVV 442
Cdd:cd17631   335 YLYIVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAV 373
PRK12467 PRK12467
peptide synthase; Provisional
 783-1115 2.29e-30

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 131.44  E-value: 2.29e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  783 VQLQVEEAQEPLLIAYYLADKMIDD--EQLSVYLRRFLPDYMIPARFIRLDKMPLTPNGKLDYNALPSPFEQDttARIYK 860
Cdd:PRK12467 3523 VVLARDGAGGKQLVAYVVPADPQGDwrETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDRKALPDPDAKG--SREYV 3600

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  861 APNSSTELKLLDIWTHILGIKRISADDHFLQIGVHSLNIMTLIAQVYENFQVELPLEQVFEHDTLEEIAAYIDEQDsqyg 940
Cdd:PRK12467 3601 APRSEVEQQLAAIWADVLGVEQVGVTDNFFELGGDSLLALQVLSRIRQSLGLKLSLRDLMSAPTIAELAGYSPLGD---- 3676

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  941 VRIEPAakqayypltaaqmrvfmdeqlvntgsgyhittafmiygpIDVTRLERACGQLIERHEALRTSFdivDGDPVQRI 1020
Cdd:PRK12467 3677 VPVNLL---------------------------------------LDLNRLETGFPALFCRHEGLGTVF---DYEPLAVI 3714

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1021 hehcdfhleivhlqgqqlhtavngcirpfqleraplirsilipLAEEQHLLVLDMHHIVADGksvfllqrdlaalYEGRE 1100
Cdd:PRK12467 3715 -------------------------------------------LEGDRHVLGLTCRHLLDDG-------------WQDTS 3738

                         330
                  ....*....|....*
gi 517718121 1101 LHDLPVQYVDFAQWQ 1115
Cdd:PRK12467 3739 LQAMAVQYADYILWQ 3753
PRK12467 PRK12467
peptide synthase; Provisional
 952-1367 7.64e-30

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 129.90  E-value: 7.64e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  952 YPLTAAQMRVFMdEQLVNTGSGYHITTAFMIYGPIDVTRLERACGQLIERHEALRTSFDIVDG--DPVQRIHEHCDfhLE 1029
Cdd:PRK12467 2647 YPLSPMQQGMLF-HTLYEGGAGDYINQMRVDVEGLDVERFRTAWQAVIDRHEILRSGFLWDGEleEPLQVVYKQAR--LP 2723

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1030 IVHLQGQQLHT--------AVNGCIRPFQLERAPLIRSILIPLAEEQHLLVLDMHHIVADGKSVFLLQRDLAALYEGREL 1101
Cdd:PRK12467 2724 FSRLDWRDRADleqaldalAAADRQQGFDLLSAPLLRLTLVRTGEDRHHLIYTNHHILMDGWSGSQLLGEVLQRYFGQPP 2803

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1102 HDLPVQYVDFAQWQTSapvvEDLRRQEQFWQSMFADY----RPLPGIPTDHTPEanersfAGGH----ITWepDPVLSRR 1173
Cdd:PRK12467 2804 PAREGRYRDYIAWLQA----QDAEASEAFWKEQLAALeeptRLARALYPAPAEA------VAGHgahyLHL--DATQTRQ 2871

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1174 LYAVAAEQQTTLFMVLLAAFHVLYAKYSAREEVTVGTPVEGrRRAEVR---QVVGMFVNALAIRSYPEGDKPFSSFLQEI 1250
Cdd:PRK12467 2872 LIEFARRHRVTLNTLVQGAWLLLLQRFTGQDTVCFGATVAG-RPAQLRgaeQQLGLFINTLPVIASPRAEQTVSDWLQQV 2950

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1251 RGTMLQAYEHQDYPL---ERLAKQLdlhhsrDHLMFDtvfSMLNYEDFAVrSDDLQFEYAELPTLSEIYNLRVE------ 1321
Cdd:PRK12467 2951 QAQNLALREFEHTPLadiQRWAGQG------GEALFD---SILVFENYPI-SEALKQGAPSGLRFGAVSSREQTnypltl 3020

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 517718121 1322 IVESPERLRGTFKYGQELYEARTVSQLAQDYERILAAVAESPNIKL 1367
Cdd:PRK12467 3021 AVGLGDTLELEFSYDRQHFDAAAIERLAESFDRLLQAMLNNPAARL 3066
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
953-1376 9.66e-30

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 129.01  E-value: 9.66e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  953 PLTAAQMRVFMDEQLVNTGSGYHITTAFMIYGPIDVTRLERACGQLIERHEALRTSFDIVDGDPVQRIHEHCDF-HLEIV 1031
Cdd:PRK10252    9 PLVAAQPGIWMAEKLSPLPSAWSVAHYVELTGELDAPLLARAVVAGLAEADTLRMRFTEDNGEVWQWVDPALTFpLPEII 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1032 HLQGQ-QLHTAVNGCIR-----PFQLERA-PLIRSILIPLAEEQHLLVLDMHHIVADGKSVFLLQRDLAALYEGRELHD- 1103
Cdd:PRK10252   89 DLRTQpDPHAAAQALMQadlqqDLRVDSGkPLVFHQLIQLGDNRWYWYQRYHHLLVDGFSFPAITRRIAAIYCAWLRGEp 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1104 ------LPVQYV--DFAQWQTSapvvEDLRRQEQFWQSMFADY--------RPLPG-IPTDH----TPEANERSFagghi 1162
Cdd:PRK10252  169 tpaspfTPFADVveEYQRYRAS----EAWQRDAAFWAEQRRQLpppaslspAPLPGrSASADilrlKLEFTDGAF----- 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1163 twepdpvlsRRLYAVAAEQQTTLFMVLLAAFHVlyAKYSAREEVTVGTPVEGRRRAEVRQVVGMFVNALAIRSYPEGDKP 1242
Cdd:PRK10252  240 ---------RQLAAQASGVQRPDLALALVALWL--GRLCGRMDYAAGFIFMRRLGSAALTATGPVLNVLPLRVHIAAQET 308

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1243 FSSFLQEIRGTMLQAYEHQDYPLERLAKQLDLHHSRDHLmFDTVFSMLNYeDFAVRSDDLQfeyAELPTLS-------EI 1315
Cdd:PRK10252  309 LPELATRLAAQLKKMRRHQRYDAEQIVRDSGRAAGDEPL-FGPVLNIKVF-DYQLDFPGVQ---AQTHTLAtgpvndlEL 383

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517718121 1316 Y-------NLRVEIVESPERlrgtfkygqelYEARTVSQLAQDYERILAAVAESPNIKLKDIEIRTPQ 1376
Cdd:PRK10252  384 AlfpdehgGLSIEILANPQR-----------YDEATLIAHAERLKALIAQFAADPALLCGDVDILLPG 440
C_NRPS-like cd19537
Condensation family domain with an atypical active site motif; Condensation (C) domains of ...
 977-1314 6.92e-29

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: 120.75  E-value: 6.92e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  977 TTAF-MIY-----GPIDVTRLERACGQLIERHEALRTSFDIVDGDPVQRIHEHCdfhlEIVHLQGQ-QLHTAVNgciRPF 1049
Cdd:cd19537    21 TSSFnVSFacrlsGDVDRDRLASAWNTVLARHRILRSRYVPRDGGLRRSYSSSP----PRVQRVDTlDVWKEIN---RPF 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1050 QLERAPLIRsILIPlaeeQHLLVLDMHHIVADGKSVFLLQRDLAALYEGRELHDLPVQYVDFAQWQTSAPvvedlRRQEQ 1129
Cdd:cd19537    94 DLEREDPIR-VFIS----PDTLLVVMSHIICDLTTLQLLLREVSAAYNGKLLPPVRREYLDSTAWSRPAS-----PEDLD 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1130 FWQSmfadYrpLPGIPTDHTPE-ANERSFAGGHITWEPDPVLSRRLYAVAAEQQTTLFMVLLAA-FHVLYAKySAREEVT 1207
Cdd:cd19537   164 FWSE----Y--LSGLPLLNLPRrTSSKSYRGTSRVFQLPGSLYRSLLQFSTSSGITLHQLALAAvALALQDL-SDRTDIV 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1208 VGTPVEGRRRAEVRQVVGMFVNALAIR-SYP-EGDKPFSSFLQEIRGTMLQAYEHQdYPLERLAKQLDLH-HSRDHLMFD 1284
Cdd:cd19537   237 LGAPYLNRTSEEDMETVGLFLEPLPIRiRFPsSSDASAADFLRAVRRSSQAALAHA-IPWHQLLEHLGLPpDSPNHPLFD 315

                         330       340       350
                  ....*....|....*....|....*....|.
gi 517718121 1285 TvfsMLNYEDFAVRSDDLQFEYAE-LPTLSE 1314
Cdd:cd19537   316 V---MVTFHDDRGVSLALPIPGVEpLYTWAE 343
FACL_DitJ_like cd05934
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 30-442 2.40e-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. Members of this family include DitJ from Pseudomonas and similar proteins.


Pssm-ID: 341257 [Multi-domain]  Cd Length: 422  Bit Score: 119.70  E-value: 2.40e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   30 SYKELDAESDRICELLHAHGAAQYDHIGILMQDRCASIAAVIGILKLGGVFVPLDPlhpderlvtmldtaevscllcdda 109
Cdd:cd05934     5 TYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINT------------------------ 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  110 qferaeTLQGHEGKYFVLRARQAMSVqagskeayshsanaTDPIYIYFTSGSTGKPKAVVGKNESLLHFMNWEASWLDLT 189
Cdd:cd05934    61 ------ALRGDELAYIIDHSGAQLVV--------------VDPASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLG 120

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  190 DPMRVsqLTSIGF---DAVLRDIFVPICAGGTIcipesreIILDPLRLVHWLEHSRVHVVHCTPSLFRFINHLSLTADSY 266
Cdd:cd05934   121 EDDVY--LTVLPLfhiNAQAVSVLAALSVGATL-------VLLPRFSASRFWSDVRRYGATVTNYLGAMLSYLLAQPPSP 191

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  267 PD----LRYVLLAGETirPESLKNWYDNLGnrVRLVNLYGPTETTmiklFYPIKPEDVHRESIPIGRPLPDTSVYLLDEQ 342
Cdd:cd05934   192 DDrahrLRAAYGAPNP--PELHEEFEERFG--VRLLEGYGMTETI----VGVIGPRDEPRRPGSIGRPAPGYEVRIVDDD 263

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  343 QQPVSGSEAGEICIATRY---MTHGYFpsSHPDQTAfipdpcrdQSGEIMMYRTGDMGRWLPEGELALLGRKDNQVKIRG 419
Cdd:cd05934   264 GQELPAGEPGELVIRGLRgwgFFKGYY--NMPEATA--------EAMRNGWFHTGDLGYRDADGFFYFVDRKKDMIRRRG 333

                         410       420
                  ....*....|....*....|...
gi 517718121  420 NRVELGDIEHRLTNMAGIREAVV 442
Cdd:cd05934   334 ENISSAEVERAILRHPAVREAAV 356
AANH_WbpG-like cd01996
Rhizobium leguminosarum WbpG protein and similar proteins; This subfamily includes Rhizobium ...
 513-626 1.01e-27

Rhizobium leguminosarum WbpG protein and similar proteins; This subfamily includes Rhizobium leguminosarum WbpG and Campylobacter jejuni PseA proteins. They belong to the of adenine nucleotide alpha hydrolase (AANH) superfamily that also includes N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to adenosine group. This subfamily of proteins is predicted to bind ATP. This domain has a strongly conserved motif SGGKD at the N-terminus.


Pssm-ID: 467500 [Multi-domain]  Cd Length: 158  Bit Score: 110.54  E-value: 1.01e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  513 NQPSYDCLLLYSGGKDSTYALYRLVEM-GARVLAYTFDNGYISSAAFRNIDSVVKELGVDHIVGTFDG--MLDIFKEGLK 589
Cdd:cd01996     2 KGKPYDCIIGVSGGKDSTYAAHKAKEKyGLRPLLVTVDAGWNSPEAVKNIEKLVRALGVDLITFVPNWkeMRDLQRLAFK 81

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 517718121  590 QECSVCNGCFKAMRILSTRVAAERGIPYIVTGLSRGQ 626
Cdd:cd01996    82 SNGDQDWPQDHGIFTSLYKMAVKFGIPLIIWGENPAE 118
PRK06188 PRK06188
acyl-CoA synthetase; Validated
 9-411 8.42e-27

acyl-CoA synthetase; Validated


Pssm-ID: 235731 [Multi-domain]  Cd Length: 524  Bit Score: 116.62  E-value: 8.42e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121    9 LARAFAAFPERKAIECGQQTLSYKELDAESDRICELLHAHGAAQYDHIGILMQDRCASIAAVIGILKLGGVFVPLDPLHP 88
Cdd:PRK06188   18 LVSALKRYPDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALHPLGS 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   89 DERLVTMLDTAEVSCLLCDDAQF-ERAETLQGHegkyfVLRARQAMSV--------------QAGSKEAYSHSAnATDPI 153
Cdd:PRK06188   98 LDDHAYVLEDAGISTLIVDPAPFvERALALLAR-----VPSLKHVLTLgpvpdgvdllaaaaKFGPAPLVAAAL-PPDIA 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  154 YIYFTSGSTGKPKAVVGKNESLLHFMNWEASWLDLTDPMRVSQLTSIGFDAVLrdIFVP-ICAGGTICIPESreiiLDPL 232
Cdd:PRK06188  172 GLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTPLSHAGGA--FFLPtLLRGGTVIVLAK----FDPA 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  233 RLVHWLEHSRVHVVHCTPS-LFRFINHLSLTADSYPDLRYVLLAGETIRPESLKNWYDNLGNRvrLVNLYGPTETTMIKL 311
Cdd:PRK06188  246 EVLRAIEEQRITATFLVPTmIYALLDHPDLRTRDLSSLETVYYGASPMSPVRLAEAIERFGPI--FAQYYGQTEAPMVIT 323

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  312 FYPIK---PEDVHRESiPIGRPLPDTSVYLLDEQQQPVSGSEAGEICIATRYMTHGYFpsSHPDQTAfipDPCRDqsGEI 388
Cdd:PRK06188  324 YLRKRdhdPDDPKRLT-SCGRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYW--NRPEETA---EAFRD--GWL 395

                         410       420
                  ....*....|....*....|...
gi 517718121  389 mmyRTGDMGRWLPEGELALLGRK 411
Cdd:PRK06188  396 ---HTGDVAREDEDGFYYIVDRK 415
Firefly_Luc_like cd05911
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ...
 27-442 9.07e-26

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: 113.08  E-value: 9.07e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   27 QTLSYKELDAESDRICELLHAHGAAQYDHIGILMQDRCASIAAVIGILKLGGVFVPLDPLHPDERLVTMLDTAEVSCLLC 106
Cdd:cd05911     9 KELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFT 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  107 DDAQFER---AETLQGHEGKYFVLRAR------QAMSVQAGSKEAYSH-----SANATDPIYIYFTSGSTGKPKAVVGKN 172
Cdd:cd05911    89 DPDGLEKvkeAAKELGPKDKIIVLDDKpdgvlsIEDLLSPTLGEEDEDlppplKDGKDDTAAILYSSGTTGLPKGVCLSH 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  173 ESLL--HFMNWEASWLDLTDPMRVsqLTSIGFD---AVLRDIFVPICaGGTICIpESREIILDPLRLVhwlEHSRVHVVH 247
Cdd:cd05911   169 RNLIanLSQVQTFLYGNDGSNDVI--LGFLPLYhiyGLFTTLASLLN-GATVII-MPKFDSELFLDLI---EKYKITFLY 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  248 CTPSLF-RFINHLSLTADSYPDLRYVLLAGETIRPEsLKNWYDNLGNRVRLVNLYGPTETTMIKLFYPikPEDVHRESIp 326
Cdd:cd05911   242 LVPPIAaALAKSPLLDKYDLSSLRVILSGGAPLSKE-LQELLAKRFPNATIKQGYGMTETGGILTVNP--DGDDKPGSV- 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  327 iGRPLPDTSVYLLDEQQQPVSG-SEAGEICIATRYMTHGYFpsSHPDQTAfipdPCRDQSGeimMYRTGDMGRWLPEGEL 405
Cdd:cd05911   318 -GRLLPNVEAKIVDDDGKDSLGpNEPGEICVRGPQVMKGYY--NNPEATK----ETFDEDG---WLHTGDIGYFDEDGYL 387

                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 517718121  406 ALLGRKDNQVKIRGNRVELGDIEHRLTNMAGIREAVV 442
Cdd:cd05911   388 YIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAV 424
PRK12316 PRK12316
peptide synthase; Provisional
 783-937 1.74e-25

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 115.44  E-value: 1.74e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  783 VQLQVEEAQEPLLIAYYLAD--KMIDDE--------QLSVYLRRFLPDYMIPARFIRLDKMPLTPNGKLDYNALPSPfEQ 852
Cdd:PRK12316 4981 VVIAQEGAVGKQLVGYVVPQdpALADADeaqaelrdELKAALRERLPEYMVPAHLVFLARMPLTPNGKLDRKALPQP-DA 5059

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  853 DTTARIYKAPNSSTELKLLDIWTHILGIKRISADDHFLQIGVHSLNIMTLIAQVYENFQVELPLEQVFEHDTLEEIAAYI 932
Cdd:PRK12316 5060 SLLQQAYVAPRSELEQQVAAIWAEVLQLERVGLDDNFFELGGHSLLAIQVTSRIQLELGLELPLRELFQTPTLAAFVELA 5139


                  ....*
gi 517718121  933 DEQDS 937
Cdd:PRK12316 5140 AAAGS 5144
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
795-936 4.27e-25

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 113.60  E-value: 4.27e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  795 LIAYYLA--DKMIDDEQLSVYLRRFLPDYMIPARFIRLDKMPLTPNGKLDYNALPSPfeqDTTARIY-KAPNSSTELKLL 871
Cdd:PRK10252  908 LVGYLVSqsGLPLDTSALQAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKALPLP---ELKAQVPgRAPKTGTETIIA 984

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517718121  872 DIWTHILGIKRISADDHFLQIGVHSLNIMTLIAQVYENFQVELPLEQVFEHDTLEEIAAYIDEQD 936
Cdd:PRK10252  985 AAFSSLLGCDVVDADADFFALGGHSLLAMKLAAQLSRQFARQVTPGQVMVASTVAKLATLLDAEE 1049
PRK07656 PRK07656
long-chain-fatty-acid--CoA ligase; Validated
 4-442 2.18e-24

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


Pssm-ID: 236072 [Multi-domain]  Cd Length: 513  Bit Score: 109.22  E-value: 2.18e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121    4 TIQYELARAFAAFPERKAIECGQQTLSYKELDAESDRICELLHAHGAAQYDHIGILMQDRCASIAAVIGILKLGGVFVPL 83
Cdd:PRK07656    6 TLPELLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   84 DPLH-PDErLVTMLDTAEVSCLLCDDA---QFERAETLQGHEGKYFVLRARQAMS-----------VQAGSKEAYSHSAN 148
Cdd:PRK07656   86 NTRYtADE-AAYILARGDAKALFVLGLflgVDYSATTRLPALEHVVICETEEDDPhtekmktftdfLAAGDPAERAPEVD 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  149 ATDPIYIYFTSGSTGKPKAVVGKNESLL-HFMNWeASWLDLTD--------PM-RVSQLTsIGFDAvlrdifvPICAGGT 218
Cdd:PRK07656  165 PDDVADILFTSGTTGRPKGAMLTHRQLLsNAADW-AEYLGLTEgdrylaanPFfHVFGYK-AGVNA-------PLMRGAT 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  219 IcIPESReiiLDPLRLVHWLEHSRVHVVHCTPSLFRFI-NHLSLTADSYPDLRYVLLAGETIRPESLKNWYDNLGnrVRL 297
Cdd:PRK07656  236 I-LPLPV---FDPDEVFRLIETERITVLPGPPTMYNSLlQHPDRSAEDLSSLRLAVTGAASMPVALLERFESELG--VDI 309

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  298 V-NLYGPTE----TTMiklfypiKPEDVHRESIP--IGRPLPDTSVYLLDEQQQPVSGSEAGEICIATRYMTHGYFpsSH 370
Cdd:PRK07656  310 VlTGYGLSEasgvTTF-------NRLDDDRKTVAgtIGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGYY--DD 380

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517718121  371 PDQTAFIPDPcrdqSGEImmyRTGDMGRWLPEGELALLGRKDNQVKIRGNRVELGDIEHRLTNMAGIREAVV 442
Cdd:PRK07656  381 PEATAAAIDA----DGWL---HTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAV 445
ACS-like cd17634
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ...
 27-442 2.67e-24

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: 109.59  E-value: 2.67e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   27 QTLSYKELDAESDRICELLHAHGAAQYDHIGILMQDRCASIAAVIGILKLGGVFVPLDPLHPDERLVTMLDTAEVSCLLC 106
Cdd:cd17634    83 RTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLIT 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  107 DDAQFERAETL------------------------------QGHEGKYFVLRARqamsVQAGSKEAYSHSANATDPIYIY 156
Cdd:cd17634   163 ADGGVRAGRSVplkknvddalnpnvtsvehvivlkrtgsdiDWQEGRDLWWRDL----IAKASPEHQPEAMNAEDPLFIL 238

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  157 FTSGSTGKPKAVVGKNESLLHFMNWEAS----------WLDLTDPMRVSQLTSIgfdavlrdIFVPICAGGTICIPESRE 226
Cdd:cd17634   239 YTSGTTGKPKGVLHTTGGYLVYAATTMKyvfdygpgdiYWCTADVGWVTGHSYL--------LYGPLACGATTLLYEGVP 310

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  227 IILDPLRLVHWLEHSRVHVVHCTPSLFRFINHLSLTADSYPD---LRYVLLAGETIRPESLKnWYDNL--GNRVRLVNLY 301
Cdd:cd17634   311 NWPTPARMWQVVDKHGVNILYTAPTAIRALMAAGDDAIEGTDrssLRILGSVGEPINPEAYE-WYWKKigKEKCPVVDTW 389

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  302 GPTETT--MIklfyPIKPEDVHRESIPIGRPLPDTSVYLLDEQQQPVSGSEAGEICIAtrymthgyfpSSHPDQT-AFIP 378
Cdd:cd17634   390 WQTETGgfMI----TPLPGAIELKAGSATRPVFGVQPAVVDNEGHPQPGGTEGNLVIT----------DPWPGQTrTLFG 455

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517718121  379 DPCRDQSGEIM----MYRTGDMGRWLPEGELALLGRKDNQVKIRGNRVELGDIEHRLTNMAGIREAVV 442
Cdd:cd17634   456 DHERFEQTYFStfkgMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAV 523
CBAL cd05923
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ...
 9-442 2.69e-24

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: 108.37  E-value: 2.69e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121    9 LARAFAAFPERKAI--ECGQQTLSYKELDAESDRICELLHAHGAAQYDHIGILMQDRCASIAAVIGILKLGGVFVPLDP- 85
Cdd:cd05923     7 LRRAASRAPDACAIadPARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPr 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   86 LHPDErLVTMLDTAEV-SCLLCDDAQFERAETLQGHEgkyfVLRarqaMSVQAGSKEAYSHSANATDPI-------YIYF 157
Cdd:cd05923    87 LKAAE-LAELIERGEMtAAVIAVDAQVMDAIFQSGVR----VLA----LSDLVGLGEPESAGPLIEDPPrepeqpaFVFY 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  158 TSGSTGKPKAVVGKN---ESLLHFMNWEASwLDLTDPMRVSQLT----SIGFDAVLrdiFVPICAGGTICIPESreiiLD 230
Cdd:cd05923   158 TSGTTGLPKGAVIPQraaESRVLFMSTQAG-LRHGRHNVVLGLMplyhVIGFFAVL---VAALALDGTYVVVEE----FD 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  231 PLRLVHWLEHSRVHVVHCTPSLFR-FINHLSLTADSYPDLRYVLLAGETIRPESLKNWYDNLGNRVrlVNLYGPTEtTMI 309
Cdd:cd05923   230 PADALKLIEQERVTSLFATPTHLDaLAAAAEFAGLKLSSLRHVTFAGATMPDAVLERVNQHLPGEK--VNIYGTTE-AMN 306

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  310 KLFYPikpeDVHRESipIGRPLPDTSVY---LLDEQQQPVSGSEAGEICIA-------TRYMthgyfpsSHPDQTAfipd 379
Cdd:cd05923   307 SLYMR----DARTGT--EMRPGFFSEVRivrIGGSPDEALANGEEGELIVAaaadaafTGYL-------NQPEATA---- 369

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517718121  380 pcrdQSGEIMMYRTGDMGRWLPEGELALLGRKDNQVKIRGNRVELGDIEHRLTNMAGIREAVV 442
Cdd:cd05923   370 ----KKLQDGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVV 428
PRK06187 PRK06187
long-chain-fatty-acid--CoA ligase; Validated
 1-442 2.87e-24

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


Pssm-ID: 235730 [Multi-domain]  Cd Length: 521  Bit Score: 108.74  E-value: 2.87e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121    1 MDNTIqYELARAFAA-FPERKAIECGQQTLSYKELDAESDRICELLHAHGAAQYDHIGILMQDRCASIAAVIGILKLGGV 79
Cdd:PRK06187    4 YPLTI-GRILRHGARkHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   80 FVPLD-PLHPDERLVTMLDtAEVSCLLCDD---AQFERAETLQGHEGKYFVL--RARQAMSVQAGSKEAYSHSANATDP- 152
Cdd:PRK06187   83 LHPINiRLKPEEIAYILND-AEDRVVLVDSefvPLLAAILPQLPTVRTVIVEgdGPAAPLAPEVGEYEELLAAASDTFDf 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  153 ---------IYIYfTSGSTGKPKAVVGKNESL-LHFMNwEASWLDLTD--------PMRVSQLTSIGfdavlrdiFVPIC 214
Cdd:PRK06187  162 pdidendaaAMLY-TSGTTGHPKGVVLSHRNLfLHSLA-VCAWLKLSRddvylvivPMFHVHAWGLP--------YLALM 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  215 AGGTICIPESreiiLDPLRLVHWLEHSRVHVVHCTPSLFRFI-NHLSLTADSYPDLRYVLLAGETIRPESLKNWYDNLGn 293
Cdd:PRK06187  232 AGAKQVIPRR----FDPENLLDLIETERVTFFFAVPTIWQMLlKAPRAYFVDFSSLRLVIYGGAALPPALLREFKEKFG- 306

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  294 rVRLVNLYGPTETTMIKLFYPIKPEDVHRESIPI--GRPLPDTSVYLLDE--QQQPVSGSEAGEICIATRYMTHGYFpsS 369
Cdd:PRK06187  307 -IDLVQGYGMTETSPVVSVLPPEDQLPGQWTKRRsaGRPLPGVEARIVDDdgDELPPDGGEVGEIIVRGPWLMQGYW--N 383

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  370 HPDQTA--FIPDpcrdqsgeimMYRTGDMGRWLPEGELALLGRKDNQVKIRGNRV---ELGDI--EHRltnmaGIREAVV 442
Cdd:PRK06187  384 RPEATAetIDGG----------WLHTGDVGYIDEDGYLYITDRIKDVIISGGENIyprELEDAlyGHP-----AVAEVAV 448
WbuX TIGR03573
N-acetyl sugar amidotransferase; This enzyme has been implicated in the formation of the ...
 456-758 2.99e-24

N-acetyl sugar amidotransferase; This enzyme has been implicated in the formation of the acetamido moiety (sugar-NC(=NH)CH3) which is found on some exopolysaccharides and is positively charged at neutral pH. The reaction involves ligation of ammonia with a sugar N-acetyl group, displacing water. In E. coli (O145 strain) and Pseudomonas aeruginosa (O12 strain) this gene is known as wbuX and ifnA respectively and likely acts on sialic acid. In Campylobacter jejuni, the gene is known as pseA and acts on pseudaminic acid in the process of flagellin glycosylation. In other Pseudomonas strains and various organisms it is unclear what the identity of the sugar substrate is, and in fact, the phylogenetic tree of this family sports a considerably deep branching suggestive of possible major differences in substrate structure. Nevertheless, the family is characterized by a conserved tetracysteine motif (CxxC.....[GN]xCxxC) possibly indicative of a metal binding site, as well as an invariable contextual association with homologs of the HisH and HisF proteins known as WbuY and WbuZ, respectively. These two proteins are believed to supply the enzyme with ammonium by hydrolysis of glutamine and delivery through an ammonium conduit.


Pssm-ID: 274658  Cd Length: 343  Bit Score: 105.85  E-value: 2.99e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   456 QQHCAACGLPSTYPGISFDDMGKCSVCTGQEQyrsaAEQ--YFQGMEQLQSKLQPVEKENQPSYDCLLLYSGGKDSTYAL 533
Cdd:TIGR03573    1 MKFCKRCVMPTTRPGITFDEDGVCSACRNFEE----KSKidWDEREKELEELVDKIKKKGGGRYDCIIGVSGGKDSTYQA 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   534 YRLVE-MGARVLAYTFDNGYISSAAFRNIDSVVKELGVDHIVGTFDG--MLDIFKEGLKQECSVCNGCFKAMRILSTRVA 610
Cdd:TIGR03573   77 HVLKKkLGLNPLLVTVDPGWNTELGVKNLNNLIKKLGFDLHTITINPetFRKLQRAYFKKVGDPEWPQDHAIFASVYQVA 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   611 AERGIPYIVTGLS---------------RGQIYDVRLYDilqqgyrttAEIELKIQEQRVlyhGKKDYVAEAFERDELIN 675
Cdd:TIGR03573  157 LKFNIPLIIWGENiaeeyggdseeelnpDEWKYNKRGID---------AANIKDFSDKGL---SERDLYAYTYPDKEKLQ 224

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   676 RSMLDQVELVDFYRYcdvSKQDILSFlqSKSEC-WSNPEDTG----FCSSNCLINDAGIYVQRTQLGYDNYAFPNSWEVR 750
Cdd:TIGR03573  225 SKGVKVIYLGYYVKW---DKKKNYEF--IKKRGgWREGPHPGtyenYKHIDSIFTIFHDYLKYLKFGFGRATDHASIDIR 299


                   ....*...
gi 517718121   751 TGHITLEQ 758
Cdd:TIGR03573  300 SGRITREE 307
E_NRPS cd19534
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
 953-1361 3.04e-24

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


Pssm-ID: 380457 [Multi-domain]  Cd Length: 428  Bit Score: 107.34  E-value: 3.04e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  953 PLTAAQmRVFMDEQLVNTgsgYHITTAFMIY--GPIDVTRLERACGQLIERHEALRTSFDIVDGDPVQRIHE--HCDFHL 1028
Cdd:cd19534     3 PLTPIQ-RWFFEQNLAGR---HHFNQSVLLRvpQGLDPDALRQALRALVEHHDALRMRFRREDGGWQQRIRGdvEELFRL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1029 EIV----HLQGQQLHTAVNGCIRPFQLERAPLIRSILIPLAEEQHLLVLDMHHIVADGKSVFLLQRDLAALYEGRELHDL 1104
Cdd:cd19534    79 EVVdlssLAQAAAIEALAAEAQSSLDLEEGPLLAAALFDGTDGGDRLLLVIHHLVVDGVSWRILLEDLEAAYEQALAGEP 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1105 PVQ-----YVDFAQWQTSAPVVEDLRRQEQFWQSMFA-DYRPLPGIPTDHtpEANERSFaggHITWEPDPVlSRRLYAVA 1178
Cdd:cd19534   159 IPLpsktsFQTWAELLAEYAQSPALLEELAYWRELPAaDYWGLPKDPEQT--YGDARTV---SFTLDEEET-EALLQEAN 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1179 AEQQTTLFMVLLAAFHVLYAKYSAREEVTVGtpVEGRRR------AEVRQVVGMFVNALAIRSYPEGDKPFSSFLQEIRG 1252
Cdd:cd19534   233 AAYRTEINDLLLAALALAFQDWTGRAPPAIF--LEGHGReeidpgLDLSRTVGWFTSMYPVVLDLEASEDLGDTLKRVKE 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1253 TMLQ------AYEHQDYPLERLAKQLDLHHSRDhLMFdtvfsmlNY-EDF-AVRSDDLQFEYAELPTLSEI-------YN 1317
Cdd:cd19534   311 QLRRipnkgiGYGILRYLTPEGTKRLAFHPQPE-ISF-------NYlGQFdQGERDDALFVSAVGGGGSDIgpdtprfAL 382

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....
gi 517718121 1318 LRVEIVESPERLRGTFKYGQELYEARTVSQLAQDYERILAAVAE 1361
Cdd:cd19534   383 LDINAVVEGGQLVITVSYSRNMYHEETIQQLADSYKEALEALIE 426
FUM14_C_NRPS-like cd19545
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ...
 952-1363 3.50e-24

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: 106.61  E-value: 3.50e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  952 YPLTAAQmRVFMDEQLVNTGSgYHITTAFMIYGPIDVTRLERACGQLIERHEALRTSFDIVD-GDPVQRIHEHCDFHlei 1030
Cdd:cd19545     2 YPCTPLQ-EGLMALTARQPGA-YVGQRVFELPPDIDLARLQAAWEQVVQANPILRTRIVQSDsGGLLQVVVKESPIS--- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1031 vhlqgQQLHTAVNGCIRPFQLER----APLIRSILIPLAEEQHLLVLDMHHIVADGKSVFLLQRDLAALYEGRElhdlPV 1106
Cdd:cd19545    77 -----WTESTSLDEYLEEDRAAPmglgGPLVRLALVEDPDTERYFVWTIHHALYDGWSLPLILRQVLAAYQGEP----VP 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1107 QYVDFAQWqTSAPVVEDLRRQEQFWQSMFADYRPLPGIPtdhTPEANERSfagghitwEPDPVLSRRL-YAVAAEQQTTL 1185
Cdd:cd19545   148 QPPPFSRF-VKYLRQLDDEAAAEFWRSYLAGLDPAVFPP---LPSSRYQP--------RPDATLEHSIsLPSSASSGVTL 215

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1186 FMVLLAAFHVLYAKYSAREEVTVGTPVEGRRR--AEVRQVVGMFVNALAIRSYPEGDKPFSSFLQEIRGTMLQAYEHQDY 1263
Cdd:cd19545   216 ATVLRAAWALVLSRYTGSDDVVFGVTLSGRNApvPGIEQIVGPTIATVPLRVRIDPEQSVEDFLQTVQKDLLDMIPFEHT 295

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1264 PLERLAKQLDlhHSRDHLMFDTVF--------SMLNYEDFAVRSDDLQFEyaELPTlseiYNLRVEIVESPERLRGTFKY 1335
Cdd:cd19545   296 GLQNIRRLGP--DARAACNFQTLLvvqpalpsSTSESLELGIEEESEDLE--DFSS----YGLTLECQLSGSGLRVRARY 367

                         410       420
                  ....*....|....*....|....*...
gi 517718121 1336 GQELYEARTVSQLAQDYERILAAVAESP 1363
Cdd:cd19545   368 DSSVISEEQVERLLDQFEHVLQQLASAP 395
CHC_CoA_lg cd05903
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ...
 28-442 4.44e-24

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: 107.08  E-value: 4.44e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   28 TLSYKELDAESDRICELLHAHGAAQYDHIGILMQDRCASIAAVIGILKLGGVFVPLDPLHPDERLVTMLDTAEVSCLLCD 107
Cdd:cd05903     1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  108 DaqferaetlqghegkyfvlRARQamsvqagskeaYSHSANATDPIYIYFTSGSTGKPKAVVGKNESLLHFMNWEASWLD 187
Cdd:cd05903    81 E-------------------RFRQ-----------FDPAAMPDAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLG 130

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  188 LTDPMRVSQLTSIG-FDAVLRDIFVPICAGGTICIPEsreiILDPLRLVHWLEHSRV-HVVHCTPSLFRFINHLSLTADS 265
Cdd:cd05903   131 LGPGDVFLVASPMAhQTGFVYGFTLPLLLGAPVVLQD----IWDPDKALALMREHGVtFMMGATPFLTDLLNAVEEAGEP 206

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  266 YPDLRYVLLAGETIRPESLKNWYDNLGNRVrlVNLYGPTETTMIklFYPIKPEDVHRESIPIGRPLPDTSVYLLDEQQQP 345
Cdd:cd05903   207 LSRLRTFVCGGATVPRSLARRAAELLGAKV--CSAYGSTECPGA--VTSITPAPEDRRLYTDGRPLPGVEIKVVDDTGAT 282

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  346 VSGSEAGEICIATRYMTHGYFpsSHPDQTA-FIPDpcrdqsgeiMMYRTGDMGRWLPEGELALLGR-KDnqVKIR-GNRV 422
Cdd:cd05903   283 LAPGVEGELLSRGPSVFLGYL--DRPDLTAdAAPE---------GWFRTGDLARLDEDGYLRITGRsKD--IIIRgGENI 349

                         410       420
                  ....*....|....*....|
gi 517718121  423 ELGDIEHRLTNMAGIREAVV 442
Cdd:cd05903   350 PVLEVEDLLLGHPGVIEAAV 369
Cyc_NRPS cd19535
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
 986-1301 7.77e-24

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: 106.03  E-value: 7.77e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  986 IDVTRLERACGQLIERHEALRTsfdIVDGDPVQRIHEH-CDFHLEIVHLQGQQLHTAVNGCI--------RPFQLERAPL 1056
Cdd:cd19535    37 LDPDRLERAWNKLIARHPMLRA---VFLDDGTQQILPEvPWYGITVHDLRGLSEEEAEAALEelrerlshRVLDVERGPL 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1057 IRSILIPLAEEQHLLVLDMHHIVADGKSVFLLQRDLAALYEGRElHDLPVQYVDFAQW--QTSAPVVEDLRRQEQFWQSM 1134
Cdd:cd19535   114 FDIRLSLLPEGRTRLHLSIDLLVADALSLQILLRELAALYEDPG-EPLPPLELSFRDYllAEQALRETAYERARAYWQER 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1135 FADYRPLPGIPTDHTPEA-NERSFAggHITWEPDPVLSRRLYAVAAEQQTTLFMVLLAAF-HVLyAKYSAREEVTVGTPV 1212
Cdd:cd19535   193 LPTLPPAPQLPLAKDPEEiKEPRFT--RREHRLSAEQWQRLKERARQHGVTPSMVLLTAYaEVL-ARWSGQPRFLLNLTL 269

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1213 EGRRR--AEVRQVVGMFVNA--LAIRsyPEGDKPFSSFLQEIRGTMLQAYEHQDYP----LERLAKQldlHHSRDHLMfD 1284
Cdd:cd19535   270 FNRLPlhPDVNDVVGDFTSLllLEVD--GSEGQSFLERARRLQQQLWEDLDHSSYSgvvvVRRLLRR---RGGQPVLA-P 343

                         330
                  ....*....|....*...
gi 517718121 1285 TVF-SMLNYEDFAVRSDD 1301
Cdd:cd19535   344 VVFtSNLGLPLLDEEVRE 361
VL_LC_FACS_like cd05907
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ...
 25-442 8.01e-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: 106.53  E-value: 8.01e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   25 GQQTLSYKELDAESDRICELLHAHGAAQYDHIGILMQDRCASIAAVIGILKLGGVFVPLDPLHPDERLVTMLDTAEVSCL 104
Cdd:cd05907     2 VWQPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKAL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  105 LCDDAqferaetlqghegkyfvlrarqamsvqagskeayshsanaTDPIYIYFTSGSTGKPKAVVGKNESLLhfmnWEAS 184
Cdd:cd05907    82 FVEDP----------------------------------------DDLATIIYTSGTTGRPKGVMLSHRNIL----SNAL 117

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  185 WLDLTDPMRvSQLTSIGF------DAVLRDIFVPICAGGTICIPESREIILDPLRLVhwlehsRVHVVHCTPSLFRFInH 258
Cdd:cd05907   118 ALAERLPAT-EGDRHLSFlplahvFERRAGLYVPLLAGARIYFASSAETLLDDLSEV------RPTVFLAVPRVWEKV-Y 189

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  259 LSLTADSYPDLRYVLLA---GETIR---------PESLKNWYDNLGnrVRLVNLYGPTETTMIKLFYPikPEDVHRESIp 326
Cdd:cd05907   190 AAIKVKAVPGLKRKLFDlavGGRLRfaasggaplPAELLHFFRALG--IPVYEGYGLTETSAVVTLNP--PGDNRIGTV- 264

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  327 iGRPLPDTSVYLldeqqqpvsgSEAGEICIATRYMTHGYFPSshPDQTA--FIPDPcrdqsgeimMYRTGDMGRWLPEGE 404
Cdd:cd05907   265 -GKPLPGVEVRI----------ADDGEILVRGPNVMLGYYKN--PEATAeaLDADG---------WLHTGDLGEIDEDGF 322

                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 517718121  405 LALLGR-KDNQVKIRGNRVELGDIEHRLTNMAGIREAVV 442
Cdd:cd05907   323 LHITGRkKDLIITSGGKNISPEPIENALKASPLISQAVV 361
PRK05691 PRK05691
peptide synthase; Validated
 795-933 5.97e-23

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 107.18  E-value: 5.97e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  795 LIAYYLADKMIDD-----EQLSVYLRRFLPDYMIPARFIRLDKMPLTPNGKLDYNALPSPFEQDTTARIYKAPNSSTELK 869
Cdd:PRK05691 4166 LVGYLVPHQTVLAqgallERIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKALPALDIGQLQSQAYLAPRNELEQT 4245

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517718121  870 LLDIWTHILGIKRISADDHFLQIGVHSLNIMTLIAQVYENFQVELPLEQVFEHDTLEEIAAYID 933
Cdd:PRK05691 4246 LATIWADVLKVERVGVHDNFFELGGHSLLATQIASRVQKALQRNVPLRAMFECSTVEELAEYIE 4309
BCL_4HBCL cd05959
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ...
 17-442 3.37e-22

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: 102.06  E-value: 3.37e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   17 PERKAIECGQQTLSYKELDAESDRICELLHAHGAAQYDHIGILMQDRCASIAAVIGILKLGGVFVPLDPLHPDERLVTML 96
Cdd:cd05959    18 GDKTAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYL 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   97 D-----TAEVSCLLCDdaQFERAETLQGHEgKYFVLRARQAMS----------VQAGSKEAYSHSANATDPIYIYFTSGS 161
Cdd:cd05959    98 EdsrarVVVVSGELAP--VLAAALTKSEHT-LVVLIVSGGAGPeagalllaelVAAEAEQLKPAATHADDPAFWLYSSGS 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  162 TGKPKAVVGKNESLLHFMNWEA-SWLDLTDPMRVSQLTSIGFDAVLRD-IFVPICAGGT-ICIPESREiildPLRLVHWL 238
Cdd:cd05959   175 TGRPKGVVHLHADIYWTAELYArNVLGIREDDVCFSAAKLFFAYGLGNsLTFPLSVGATtVLMPERPT----PAAVFKRI 250

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  239 EHSRVHVVHCTPSLFR-FINHLSLTADSYPDLRYVLLAGETIRPESLKNWYDNLGnrVRLVNLYGPTEttMIKLFYPIKP 317
Cdd:cd05959   251 RRYRPTVFFGVPTLYAaMLAAPNLPSRDLSSLRLCVSAGEALPAEVGERWKARFG--LDILDGIGSTE--MLHIFLSNRP 326

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  318 EDVHRESIpiGRPLPDTSVYLLDEQQQPVSGSEAGEICIATRYMTHGYFPSshpdqtafipdpcRDQSGEIMM---YRTG 394
Cdd:cd05959   327 GRVRYGTT--GKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNN-------------RDKTRDTFQgewTRTG 391

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 517718121  395 DMGRWLPEGELALLGRKDNQVKIRGNRVELGDIEHRLTNMAGIREAVV 442
Cdd:cd05959   392 DKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAV 439
A_NRPS_TubE_like cd05906
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ...
 25-429 3.45e-22

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: 102.36  E-value: 3.45e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   25 GQQTLSYKELDAESDRICELLHAHGAAQYDHIGILMQDRCASIAAVIGILKLGGVFVPLDPLHPD----------ERLVT 94
Cdd:cd05906    36 SEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPLTVPPTYdepnarlrklRHIWQ 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   95 MLDTAEVsclLCDD---AQFERAETLQGHEGkyFVLRARQAMSVQAGSKEAysHSANATDPIYIYFTSGSTGKPKAVVGK 171
Cdd:cd05906   116 LLGSPVV---LTDAelvAEFAGLETLSGLPG--IRVLSIEELLDTAADHDL--PQSRPDDLALLMLTSGSTGFPKAVPLT 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  172 NESLLHfMNWEASWLDLTDPMRVsQLTSIGFDAVLRDIFV---PICAGG-TICIPESrEIILDPLRLVHWLEHSRVHVVH 247
Cdd:cd05906   189 HRNILA-RSAGKIQHNGLTPQDV-FLNWVPLDHVGGLVELhlrAVYLGCqQVHVPTE-EILADPLRWLDLIDRYRVTITW 265

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  248 CTPSLFRFINHLSLTADSYP----DLRYVLLAGE-----TIRP--ESLKnwydNLGNRVR-LVNLYGPTETTMIKLFYPI 315
Cdd:cd05906   266 APNFAFALLNDLLEEIEDGTwdlsSLRYLVNAGEavvakTIRRllRLLE----PYGLPPDaIRPAFGMTETCSGVIYSRS 341

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  316 KPEDVHRESIP---IGRPLPDTSVYLLDEQQQPVSGSEAGEICIATRYMTHGYFPSSHPDQTAFIPDpcrdqsGeimMYR 392
Cdd:cd05906   342 FPTYDHSQALEfvsLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTED------G---WFR 412

                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 517718121  393 TGDMGrWLPEGELALLGRKDNQVKIRGNRVELGDIEH 429
Cdd:cd05906   413 TGDLG-FLDNGNLTITGRTKDTIIVNGVNYYSHEIEA 448
PRK04319 PRK04319
acetyl-CoA synthetase; Provisional
 26-442 4.41e-22

acetyl-CoA synthetase; Provisional


Pssm-ID: 235279 [Multi-domain]  Cd Length: 570  Bit Score: 102.28  E-value: 4.41e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   26 QQTLSYKELDAESDRICELLHAHGAAQYDHIGILMQDRCASIAAVIGILKLGGVFVPLDPLHPDERLVTMLDTAEVSCLL 105
Cdd:PRK04319   71 KEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVLI 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  106 CDDAQFER--AETL------------QGHEGKYFVLRARqamsVQAGSKEAYSHSANATDPIYIYFTSGSTGKPKAVVG- 170
Cdd:PRK04319  151 TTPALLERkpADDLpslkhvllvgedVEEGPGTLDFNAL----MEQASDEFDIEWTDREDGAILHYTSGSTGKPKGVLHv 226

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  171 KNESLLHFMNweASW-LDL---------TDPMRVSQlTSIGfdavlrdIFVPICAGGTICIPESReiiLDPLRLVHWLEH 240
Cdd:PRK04319  227 HNAMLQHYQT--GKYvLDLheddvywctADPGWVTG-TSYG-------IFAPWLNGATNVIDGGR---FSPERWYRILED 293

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  241 SRVHVVHCTPSLFR-FINHLSLTADSY--PDLRYVLLAGETIRPESLKNWYDNLGNRVRlvNLYGPTET--TMIKLFY-- 313
Cdd:PRK04319  294 YKVTVWYTAPTAIRmLMGAGDDLVKKYdlSSLRHILSVGEPLNPEVVRWGMKVFGLPIH--DNWWMTETggIMIANYPam 371

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  314 PIKPEDvhresipIGRPLPDTSVYLLDEQQQPVSGSEAGEICIATRY--MTHGYFPSSHPDQTAFIPDpcrdqsgeimMY 391
Cdd:PRK04319  372 DIKPGS-------MGKPLPGIEAAIVDDQGNELPPNRMGNLAIKKGWpsMMRGIWNNPEKYESYFAGD----------WY 434

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|.
gi 517718121  392 RTGDMGRWLPEGELALLGRKDNQVKIRGNRVELGDIEHRLTNMAGIREAVV 442
Cdd:PRK04319  435 VSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGV 485
PRK06145 PRK06145
acyl-CoA synthetase; Validated
 12-442 5.14e-22

acyl-CoA synthetase; Validated


Pssm-ID: 102207 [Multi-domain]  Cd Length: 497  Bit Score: 101.50  E-value: 5.14e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   12 AFAAF-----PERKAIECGQQTLSYKELDAESDRICELLHAHGAAQYDHIGILMQDRCASIAAVIGILKLGGVFVPLD-P 85
Cdd:PRK06145    6 ASIAFharrtPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINyR 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   86 LHPDErLVTMLDTAEVSCLLCDdaqfERAETLQGHEGKYFVLRARQAMSV----QAGSKEAYSHSANATDPIYIYFTSGS 161
Cdd:PRK06145   86 LAADE-VAYILGDAGAKLLLVD----EEFDAIVALETPKIVIDAAAQADSrrlaQGGLEIPPQAAVAPTDLVRLMYTSGT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  162 TGKPKAVVGKNESLlhfmNWEA----SWLDLTDPMR---VSQLTSIG-FDavLRDIFVpICAGGTICIpeSREiiLDPLR 233
Cdd:PRK06145  161 TDRPKGVMHSYGNL----HWKSidhvIALGLTASERllvVGPLYHVGaFD--LPGIAV-LWVGGTLRI--HRE--FDPEA 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  234 LVHWLEHSRVHVVHCTPSLFRFInhLSL-TADSY--PDLRYVLLAGETIrPESLKNWYDNLGNRVRLVNLYGPTETTMIK 310
Cdd:PRK06145  230 VLAAIERHRLTCAWMAPVMLSRV--LTVpDRDRFdlDSLAWCIGGGEKT-PESRIRDFTRVFTRARYIDAYGLTETCSGD 306

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  311 LFYpikpeDVHRESIPI---GRPLPDTSVYLLDEQQQPVSGSEAGEICIATRYMTHGYFPSSHPDQTAFIPDpcrdqsge 387
Cdd:PRK06145  307 TLM-----EAGREIEKIgstGRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYGD-------- 373

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 517718121  388 imMYRTGDMGRWLPEGELALLGRKDNQVKIRGNRVELGDIEHRLTNMAGIREAVV 442
Cdd:PRK06145  374 --WFRSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAV 426
PRK06178 PRK06178
acyl-CoA synthetase; Validated
 8-453 3.86e-21

acyl-CoA synthetase; Validated


Pssm-ID: 235724 [Multi-domain]  Cd Length: 567  Bit Score: 99.35  E-value: 3.86e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121    8 ELARAFAAF-PERKAIECGQQTLSYKELDAESDRICELLHAHGAAQYDHIGILMQDrCASI-AAVIGILKLGGVFVPLDP 85
Cdd:PRK06178   37 EYLRAWARErPQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPN-CPQFhIVFFGILKLGAVHVPVSP 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   86 LHPDERLVTMLDTAEVSCLLCDDAQFE-----RAET-------------------------LQG----HEGKYFVLRARQ 131
Cdd:PRK06178  116 LFREHELSYELNDAGAEVLLALDQLAPvveqvRAETslrhvivtsladvlpaeptlplpdsLRAprlaAAGAIDLLPALR 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  132 AMSVQAGskeaySHSANATDPIYIYFTSGSTGKPKAVVGKNESLLHFMnweASWLDLTDPMRvSQLTSIGF--------- 202
Cdd:PRK06178  196 ACTAPVP-----LPPPALDALAALNYTGGTTGMPKGCEHTQRDMVYTA---AAAYAVAVVGG-EDSVFLSFlpefwiage 266

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  203 DAvlrDIFVPICAGGTIcipesreIIL---DPLRLVHWLEHSRVhvvhctpslfrfiNHLSLTADSYPDL-------RYV 272
Cdd:PRK06178  267 NF---GLLFPLFSGATL-------VLLarwDAVAFMAAVERYRV-------------TRTVMLVDNAVELmdhprfaEYD 323

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  273 LLAGETIR---------PESLKNWYDNLGNRVRLVNlYGPTETTMIKLF---YPIKPEDVHRESIPIGRPLPDTSVYLLD 340
Cdd:PRK06178  324 LSSLRQVRvvsfvkklnPDYRQRWRALTGSVLAEAA-WGMTETHTCDTFtagFQDDDFDLLSQPVFVGLPVPGTEFKICD 402

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  341 EQQ-QPVSGSEAGEICIATRYMTHGYFpsSHPDQTAfipDPCRDQsgeimMYRTGDMGRWLPEGELALLGRKDNQVKIRG 419
Cdd:PRK06178  403 FETgELLPLGAEGEIVVRTPSLLKGYW--NKPEATA---EALRDG-----WLHTGDIGKIDEQGFLHYLGRRKEMLKVNG 472

                         490       500       510
                  ....*....|....*....|....*....|....*
gi 517718121  420 NRVELGDIEHRLTNMAGI-REAVVrmrAKADTPKG 453
Cdd:PRK06178  473 MSVFPSEVEALLGQHPAVlGSAVV---GRPDPDKG 504
MACS_like_2 cd05973
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
 29-442 4.39e-21

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


Pssm-ID: 341277 [Multi-domain]  Cd Length: 437  Bit Score: 97.97  E-value: 4.39e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   29 LSYKELDAESDRICELLHAHGAAQYDHIGILMQDRCASIAAVIGILKLGGVFVPLDPLHPDERLVTMLDTAEVSCLLCDD 108
Cdd:cd05973     1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTDA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  109 AQFERAetlqghegkyfvlrarqamsvqagskeayshsanATDPIYIYFTSGSTGKPKAVVGKNESLLHFMNWEASWLDL 188
Cdd:cd05973    81 ANRHKL----------------------------------DSDPFVMMFTSGTTGLPKGVPVPLRALAAFGAYLRDAVDL 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  189 TDPMRVSQLTSIGFDAVL-RDIFVPICAG-------GTICIPESREIIldplrlvhwlEHSRVHVVHCTPSLFRFINHLS 260
Cdd:cd05973   127 RPEDSFWNAADPGWAYGLyYAITGPLALGhptilleGGFSVESTWRVI----------ERLGVTNLAGSPTAYRLLMAAG 196

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  261 LTADSYPD--LRYVLLAGETIRPESLKnWYD-NLGNRVRlvNLYGPTETTMIKLFYPIKPEDVHRESIpiGRPLPDTSVY 337
Cdd:cd05973   197 AEVPARPKgrLRRVSSAGEPLTPEVIR-WFDaALGVPIH--DHYGQTELGMVLANHHALEHPVHAGSA--GRAMPGWRVA 271

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  338 LLDEQQQPVSGSEAGEICIATRYMTHGYFPS-SHPDQTAFIPDpcrdqsgeimMYRTGDMGRWLPEGELALLGRKDNQVK 416
Cdd:cd05973   272 VLDDDGDELGPGEPGRLAIDIANSPLMWFRGyQLPDTPAIDGG----------YYLTGDTVEFDPDGSFSFIGRADDVIT 341

                         410       420
                  ....*....|....*....|....*.
gi 517718121  417 IRGNRVELGDIEHRLTNMAGIREAVV 442
Cdd:cd05973   342 MSGYRIGPFDVESALIEHPAVAEAAV 367
BCL_like cd05919
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ...
 19-442 4.73e-21

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: 97.92  E-value: 4.73e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   19 RKAIECGQQTLSYKELDAESDRICELLHAHGAAQYDHIGILMQDRCASIAAVIGILKLGGVFVPLDP-LHPDErLVTMLD 97
Cdd:cd05919     1 KTAFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPlLHPDD-YAYIAR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   98 TAEVSCLLCDDAqferaetlqghegkyfvlrarqamsvqagskeayshsanatDPIYIYFTSGSTGKPKAVVGKNESLLH 177
Cdd:cd05919    80 DCEARLVVTSAD-----------------------------------------DIAYLLYSSGTTGPPKGVMHAHRDPLL 118

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  178 FMN-WEASWLDLTDPMRVSQLTSIGFDAVL-RDIFVPICAGGTICIPESREiilDPLRLVHWLEHSRVHVVHCTPSLF-R 254
Cdd:cd05919   119 FADaMAREALGLTPGDRVFSSAKMFFGYGLgNSLWFPLAVGASAVLNPGWP---TAERVLATLARFRPTVLYGVPTFYaN 195

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  255 FINHLSLTADSYPDLRYVLLAGETIRPESLKNWYDNLGnrVRLVNLYGPTEttMIKLFYPIKPEDVHRESIpiGRPLPDT 334
Cdd:cd05919   196 LLDSCAGSPDALRSLRLCVSAGEALPRGLGERWMEHFG--GPILDGIGATE--VGHIFLSNRPGAWRLGST--GRPVPGY 269

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  335 SVYLLDEQQQPVSGSEAGEICIATRYMTHGYFPSSHPDQTAFipdpcrdqSGEimMYRTGDMGRWLPEGELALLGRKDNQ 414
Cdd:cd05919   270 EIRLVDEEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATF--------NGG--WYRTGDKFCRDADGWYTHAGRADDM 339

                         410       420
                  ....*....|....*....|....*...
gi 517718121  415 VKIRGNRVELGDIEHRLTNMAGIREAVV 442
Cdd:cd05919   340 LKVGGQWVSPVEVESLIIQHPAVAEAAV 367
MACS_AAE_MA_like cd05970
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ...
 7-442 4.95e-21

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: 98.72  E-value: 4.95e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121    7 YELARAFAA-FPERKAI-ECGQQT----LSYKELDAESDRICELLHAHGAAQYDHIGILMQDRCASIAAVIGILKLGGVF 80
Cdd:cd05970    20 YDVVDAMAKeYPDKLALvWCDDAGeeriFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIA 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   81 VPLDPLHPDERLVTMLDTAEVSCLLCDDAQFERAETLQGHEGKYFVLRARQA--------MSVQAGSKEAY--------S 144
Cdd:cd05970   100 IPATHQLTAKDIVYRIESADIKMIVAIAEDNIPEEIEKAAPECPSKPKLVWVgdpvpegwIDFRKLIKNASpdferptaN 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  145 HSANATDPIYIYFTSGSTGKPKAVVGKNESLLHFMNWEASWLDLTDPMRVSQLTSIGF-DAVLRDIFVPICAGGTICIPE 223
Cdd:cd05970   180 SYPCGEDILLVYFSSGTTGMPKMVEHDFTYPLGHIVTAKYWQNVREGGLHLTVADTGWgKAVWGKIYGQWIAGAAVFVYD 259

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  224 SREiiLDPLRLVHWLEHSRVHVVHCTPSLFRFINHLSLTADSYPDLRYVLLAGETIRPESLKNWYDNLGnrVRLVNLYGP 303
Cdd:cd05970   260 YDK--FDPKALLEKLSKYGVTTFCAPPTIYRFLIREDLSRYDLSSLRYCTTAGEALNPEVFNTFKEKTG--IKLMEGFGQ 335

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  304 TETTMIKLFYP---IKPEDvhresipIGRPLPDTSVYLLDEQQQPVSGSEAGEICIATRY-----MTHGYFpsSHPDQTA 375
Cdd:cd05970   336 TETTLTIATFPwmePKPGS-------MGKPAPGYEIDLIDREGRSCEAGEEGEIVIRTSKgkpvgLFGGYY--KDAEKTA 406

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517718121  376 fipdpcrdqsgEIM---MYRTGDMGrWLPE-GELALLGRKDNQVKIRGNRVELGDIEHRLTNMAGIREAVV 442
Cdd:cd05970   407 -----------EVWhdgYYHTGDAA-WMDEdGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAV 465
AACS_like cd05968
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ...
 27-440 7.83e-21

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: 98.72  E-value: 7.83e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   27 QTLSYKELDAESDRICELLHAHGAAQYDHIGILMQDRCASIAAVIGILKLGGVFVPLDPLHPDERLVTMLDTAEVSCLLC 106
Cdd:cd05968    90 RTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKALIT 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  107 DDAQFERAETLQGHEG------------KYFVLRARQAMSVQAGSKEAYSHSANAT-----------DPIYIYFTSGSTG 163
Cdd:cd05968   170 ADGFTRRGREVNLKEEadkacaqcptveKVVVVRHLGNDFTPAKGRDLSYDEEKETagdgaerteseDPLMIIYTSGTTG 249

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  164 KPKAVVGKN--------ESLLHFMnweaswlDLTDPMRVSQLTSIGFDAVLRDIFVPICAGGTICIPESREIILDPLRLV 235
Cdd:cd05968   250 KPKGTVHVHagfplkaaQDMYFQF-------DLKPGDLLTWFTDLGWMMGPWLIFGGLILGATMVLYDGAPDHPKADRLW 322

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  236 HWLEHSRVHVVHCTPSLFR-FINHLS--LTADSYPDLRYVLLAGETIRPESLKNWYDN-LGNRVRLVNLYGPTETT---- 307
Cdd:cd05968   323 RMVEDHEITHLGLSPTLIRaLKPRGDapVNAHDLSSLRVLGSTGEPWNPEPWNWLFETvGKGRNPIINYSGGTEISggil 402

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  308 ---MIKlfyPIKPedvhresIPIGRPLPDTSVYLLDEQQQPVSGsEAGEICIATRY--MTHGYFpsshpdqtafipdpcR 382
Cdd:cd05968   403 gnvLIK---PIKP-------SSFNGPVPGMKADVLDESGKPARP-EVGELVLLAPWpgMTRGFW---------------R 456

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517718121  383 DQSGEIMMYRT--------GDMGRWLPEGELALLGRKDNQVKIRGNRVELGDIEHRLTNMAGIREA 440
Cdd:cd05968   457 DEDRYLETYWSrfdnvwvhGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLES 522
MACS_like_3 cd05971
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
 30-442 1.38e-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: 1.38e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   30 SYKELDAESDRICELLHAHGAAQYDHIGILMQDRCASIAAVIGILKLGGVFVPLDPLHPDERLVTMLDTAEVSCLLCDDA 109
Cdd:cd05971     8 TFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVTDGS 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  110 QferaetlqghegkyfvlrarqamsvqagskeayshsanatDPIYIYFTSGSTGKPKAVVGKNESLL-HFMNWEASWLDL 188
Cdd:cd05971    88 D----------------------------------------DPALIIYTSGTTGPPKGALHAHRVLLgHLPGVQFPFNLF 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  189 TDPMRVSQLTS----IGfdaVLRDIFVPICAGGtICIPESREIILDPLRLVHWLEHSRVHVVHCTPSLFRFINHLSLTAD 264
Cdd:cd05971   128 PRDGDLYWTPAdwawIG---GLLDVLLPSLYFG-VPVLAHRMTKFDPKAALDLMSRYGVTTAFLPPTALKMMRQQGEQLK 203

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  265 SYP-DLRYVLLAGETIRPESLKNWYDNLGnrVRLVNLYGPTETTMI----KLFYPIKPEDvhresipIGRPLPDTSVYLL 339
Cdd:cd05971   204 HAQvKLRAIATGGESLGEELLGWAREQFG--VEVNEFYGQTECNLVigncSALFPIKPGS-------MGKPIPGHRVAIV 274

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  340 DEQQQPVSGSEAGEICIATrymthgyfpsshPDQTAFIPDPCRDQSGEIMM----YRTGDMGRWLPEGELALLGRKDNQV 415
Cdd:cd05971   275 DDNGTPLPPGEVGEIAVEL------------PDPVAFLGYWNNPSATEKKMagdwLLTGDLGRKDSDGYFWYVGRDDDVI 342

                         410       420
                  ....*....|....*....|....*..
gi 517718121  416 KIRGNRVELGDIEHRLTNMAGIREAVV 442
Cdd:cd05971   343 TSSGYRIGPAEIEECLLKHPAVLMAAV 369
MACS_like_4 cd05969
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ...
 29-442 1.56e-20

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: 96.42  E-value: 1.56e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   29 LSYKELDAESDRICELLHAHGAAQYDHIGILMQDRCASIAAVIGILKLGGVFVPLDPLHPDERLVTMLDTAEVSCLLCDD 108
Cdd:cd05969     1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  109 AQFERAETlqghegkyfvlrarqamsvqagskeayshsanaTDPIYIYFTSGSTGKPKAVVGKNESLLHFMNWEASWLDL 188
Cdd:cd05969    81 ELYERTDP---------------------------------EDPTLLHYTSGTTGTPKGVLHVHDAMIFYYFTGKYVLDL 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  189 ---------TDPMRVSQlTSIGfdavlrdIFVPICAGGTICIPESReiiLDPLRLVHWLEHSRVHVVHCTPSLFRFINHL 259
Cdd:cd05969   128 hpddiywctADPGWVTG-TVYG-------IWAPWLNGVTNVVYEGR---FDAESWYGIIERVKVTVWYTAPTAIRMLMKE 196

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  260 SLT-ADSY--PDLRYVLLAGETIRPESLKnWYDNLGNrVRLVNLYGPTETTMIKLF----YPIKPEDvhresipIGRPLP 332
Cdd:cd05969   197 GDElARKYdlSSLRFIHSVGEPLNPEAIR-WGMEVFG-VPIHDTWWQTETGSIMIAnypcMPIKPGS-------MGKPLP 267

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  333 DTSVYLLDEQQQPVSGSEAGEICIATRY--MTHGYFPSSHPDQTAFIpdpcrdqSGeimMYRTGDMGRWLPEGELALLGR 410
Cdd:cd05969   268 GVKAAVVDENGNELPPGTKGILALKPGWpsMFRGIWNDEERYKNSFI-------DG---WYLTGDLAYRDEDGYFWFVGR 337

                         410       420       430
                  ....*....|....*....|....*....|..
gi 517718121  411 KDNQVKIRGNRVELGDIEHRLTNMAGIREAVV 442
Cdd:cd05969   338 ADDIIKTSGHRVGPFEVESALMEHPAVAEAGV 369
alpha_am_amid TIGR03443
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ...
 788-950 5.74e-20

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: 97.06  E-value: 5.74e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   788 EEAQEPL---LIAYYladKMIDDeqLSVYLRRFLPDYMIPARFIRLDKMPLTPNGKLDYNALPSPfeqDTTARIYKAPNS 864
Cdd:TIGR03443  766 EESSDPVvkgLIKYR---KLIKD--IREYLKKKLPSYAIPTVIVPLKKLPLNPNGKVDKPALPFP---DTAQLAAVAKNR 837

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   865 S----------TELKLLDIWTHILGIK--RISADDHFLQIGVHSLNIMTLIAQVYENFQVELPLEQVFEHDTLEEIAAYI 932
Cdd:TIGR03443  838 SasaadeefteTEREIRDLWLELLPNRpaTISPDDSFFDLGGHSILATRMIFELRKKLNVELPLGLIFKSPTIKGFAKEV 917

                          170       180
                   ....*....|....*....|...
gi 517718121   933 D-----EQDSQYGVRIEPAAKQA 950
Cdd:TIGR03443  918 DrlkkgEELADEGDSEIEEEETV 940
PRK03640 PRK03640
o-succinylbenzoate--CoA ligase;
11-442 5.89e-20

o-succinylbenzoate--CoA ligase;


Pssm-ID: 235146 [Multi-domain]  Cd Length: 483  Bit Score: 95.03  E-value: 5.89e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   11 RAFAAfPERKAIECGQQTLSYKELDAESDRICELLHAHGAAQYDHIGILMQDRCASIAAVIGILKLGGVFVPLDP-LHPD 89
Cdd:PRK03640   11 RAFLT-PDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTrLSRE 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   90 ERLVTMLDtAEVSCLLCDDaqferaETLQGHEGKYFVLRArQAMSVQAGS---KEAYSHSANATdpiyIYFTSGSTGKPK 166
Cdd:PRK03640   90 ELLWQLDD-AEVKCLITDD------DFEAKLIPGISVKFA-ELMNGPKEEaeiQEEFDLDEVAT----IMYTSGTTGKPK 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  167 AVVG--KNesllHFMNWEASWLDL--TD--------PM-RVSqltsiGFDAVLRDIFVpicaGGTICIPESreiiLDPLR 233
Cdd:PRK03640  158 GVIQtyGN----HWWSAVGSALNLglTEddcwlaavPIfHIS-----GLSILMRSVIY----GMRVVLVEK----FDAEK 220

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  234 LVHWLEHSRVHVVHCTPS-LFRFINHLSltADSYPD-LRYVLLAGETIRP---ESLKNWydnlgnRVRLVNLYGPTETT- 307
Cdd:PRK03640  221 INKLLQTGGVTIISVVSTmLQRLLERLG--EGTYPSsFRCMLLGGGPAPKpllEQCKEK------GIPVYQSYGMTETAs 292

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  308 -MIKLfypiKPEDVHRESIPIGRPLPDTSVYLLDeQQQPVSGSEAGEICIATRYMTHGYFPSSHPDQTAFipdpcrdQSG 386
Cdd:PRK03640  293 qIVTL----SPEDALTKLGSAGKPLFPCELKIEK-DGVVVPPFEEGEIVVKGPNVTKGYLNREDATRETF-------QDG 360

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 517718121  387 eimMYRTGDMGRWLPEGELALLGRKDNQVKIRGNRVELGDIEHRLTNMAGIREAVV 442
Cdd:PRK03640  361 ---WFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGV 413
MACS_like_1 cd05974
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ...
 29-442 7.49e-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: 341278 [Multi-domain]  Cd Length: 432  Bit Score: 94.17  E-value: 7.49e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   29 LSYKELDAESDRICELLHAHGAAQYDHIGILMQDRCASIAAVIGILKLGGVFVPLdplhpderlVTMLDTAEVScllcdd 108
Cdd:cd05974     1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPA---------TTLLTPDDLR------ 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  109 AQFERaetlqgheGKYFVLRARQAmsvqagskeayshsANATDPIYIYFTSGSTGKPKAVVGKNESL----LHFMNW--- 181
Cdd:cd05974    66 DRVDR--------GGAVYAAVDEN--------------THADDPMLLYFTSGTTSKPKLVEHTHRSYpvghLSTMYWigl 123

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  182 ---EASWlDLTDPMRVSQLTSigfdavlrDIFVPICAGGTI-CIPESReiiLDPLRLVHWLEHSRVHVVHCTPSLFRFIN 257
Cdd:cd05974   124 kpgDVHW-NISSPGWAKHAWS--------CFFAPWNAGATVfLFNYAR---FDAKRVLAALVRYGVTTLCAPPTVWRMLI 191

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  258 HLSLTADSYPdLRYVLLAGETIRPESLKNWYDNLGNRVRlvNLYGPTETTMIKLFYPIKPEDVHResipIGRPLPDTSVY 337
Cdd:cd05974   192 QQDLASFDVK-LREVVGAGEPLNPEVIEQVRRAWGLTIR--DGYGQTETTALVGNSPGQPVKAGS----MGRPLPGYRVA 264

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  338 LLDEQQQPVSgseAGEICI---ATR---YMThGYfpSSHPDQTAfipdpcrdQSGEIMMYRTGDMGRWLPEGELALLGRK 411
Cdd:cd05974   265 LLDPDGAPAT---EGEVALdlgDTRpvgLMK-GY--AGDPDKTA--------HAMRGGYYRTGDIAMRDEDGYLTYVGRA 330

                         410       420       430
                  ....*....|....*....|....*....|.
gi 517718121  412 DNQVKIRGNRVELGDIEHRLTNMAGIREAVV 442
Cdd:cd05974   331 DDVFKSSDYRISPFELESVLIEHPAVAEAAV 361
E-C_NRPS cd19544
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); ...
 990-1234 1.93e-19

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: 92.50  E-value: 1.93e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  990 RLER---ACGQLIERHEALRTSFdIVDG--DPVQRIHEHCDFHLEIVHLQG-----QQLHTAVNGCIRPFQLERAPLIRS 1059
Cdd:cd19544    37 RLDAflaALQQVIDRHDILRTAI-LWEGlsEPVQVVWRQAELPVEELTLDPgddalAQLRARFDPRRYRLDLRQAPLLRA 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1060 ILIP-LAEEQHLLVLDMHHIVADGKSVFLLQRDLAALYEGRElHDL--PVQYVDF-AQWQTSAPVVEdlrrQEQFWQSMF 1135
Cdd:cd19544   116 HVAEdPANGRWLLLLLFHHLISDHTSLELLLEEIQAILAGRA-AALppPVPYRNFvAQARLGASQAE----HEAFFREML 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1136 ADYRPlpgiPTdhTP------EANERSFAGGHITWEPDpvLSRRLYAVAAEQQTTlfmvlLAA-FHVLYA----KYSARE 1204
Cdd:cd19544   191 GDVDE----PT--APfglldvQGDGSDITEARLALDAE--LAQRLRAQARRLGVS-----PASlFHLAWAlvlaRCSGRD 257

                         250       260       270
                  ....*....|....*....|....*....|....
gi 517718121 1205 EVTVGTPVEGR----RRAEvrQVVGMFVNALAIR 1234
Cdd:cd19544   258 DVVFGTVLSGRmqggAGAD--RALGMFINTLPLR 289
PRK06839 PRK06839
o-succinylbenzoate--CoA ligase;
17-442 2.64e-19

o-succinylbenzoate--CoA ligase;


Pssm-ID: 168698 [Multi-domain]  Cd Length: 496  Bit Score: 93.00  E-value: 2.64e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   17 PERKAIECGQQTLSYKELDAESDRICE-LLHAHGAAQYDHIGILMQDRCASIAAVIGILKLGGVFVPLD-PLHPDErLVT 94
Cdd:PRK06839   16 PDRIAIITEEEEMTYKQLHEYVSKVAAyLIYELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNiRLTENE-LIF 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   95 MLDTAEVSCLLCDDAQFERAETLQGHEGKYFVLRArqamsvqAGSKEAYSHS------ANATDPIYIYFTSGSTGKPKAV 168
Cdd:PRK06839   95 QLKDSGTTVLFVEKTFQNMALSMQKVSYVQRVISI-------TSLKEIEDRKidnfveKNESASFIICYTSGTTGKPKGA 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  169 VGKNESllhfMNWEA----SWLDLT-DPMRVSQLTSIGFDAVLRDIFVPICAGGTICIPESreiiLDPLRLVHWLEHSRV 243
Cdd:PRK06839  168 VLTQEN----MFWNAlnntFAIDLTmHDRSIVLLPLFHIGGIGLFAFPTLFAGGVIIVPRK----FEPTKALSMIEKHKV 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  244 HVVHCTPSLFRFINHLSLTADsyPDLRYV--LLAGETIRPESLKNWYDNLGnrVRLVNLYGPTETTmiKLFYPIKPEDVH 321
Cdd:PRK06839  240 TVVMGVPTIHQALINCSKFET--TNLQSVrwFYNGGAPCPEELMREFIDRG--FLFGQGFGMTETS--PTVFMLSEEDAR 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  322 RESIPIGRPLPDTSVYLLDEQQQPVSGSEAGEICIATRYMTHGYFpsSHPDQTAfipDPCRDQsgeimMYRTGDMGRWLP 401
Cdd:PRK06839  314 RKVGSIGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYW--NRPDATE---ETIQDG-----WLCTGDLARVDE 383

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|.
gi 517718121  402 EGELALLGRKDNQVKIRGNRVELGDIEHRLTNMAGIREAVV 442
Cdd:PRK06839  384 DGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAV 424
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
 783-1198 6.37e-19

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: 93.77  E-value: 6.37e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  783 VQLQVEEAQEPLLIAYYLADK--MIDDEQLSVYLRRFLPDYMIPARFIRLDKMPLTPNGKLDynALPSPFEQDTTARIYK 860
Cdd:COG1020   903 VVAREDAPGDKRLVAYVVPEAgaAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLD--RLALPAPAAAAAAAAA 980

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  861 APNSSTELKLLDIWTHILGIKRISADDHFLQIGVHSLNIMTLIAQVYENFQVELPLEQVFEHDTLEEIAAYIDEQDSQYG 940
Cdd:COG1020   981 APPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLLLLLFLAAAAAAAAAAAAAAAAAAA 1060

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  941 VRIEPAAKQAYYPLTAAQMRVFMDEQLVNTGSGYHITTAFMIYGPIDVTRLERACGQLIERHEALRTSFDIVDGDPVQRI 1020
Cdd:COG1020  1061 APLAAAAAPLPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLALLLLLALLLALLAALRARRAVRQEGPRLRL 1140

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1021 HEHC------DFHLEIVHLQGQQLHTAVNGCIRPFQLERAPLIRSILIPLAEEQHLLVLDMHHIVADGKSVFLLQRDLAA 1094
Cdd:COG1020  1141 LVALaaalalAALLALLLAAAAAAAELLAAAALLLLLALLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLL 1220

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1095 LY----EGRELHDLPVQYVDFAQWQTSAPVVEDLRRQEQFWQSMFADYRPLPGIPTDHTPEANERSFAGGHITWEPDPVL 1170
Cdd:COG1020  1221 LLllaaAAAALLALALLLALLALAALLALAALAALAAALLALALALLALALLLLALALLLPALARARAARTARALALLLL 1300

                         410       420
                  ....*....|....*....|....*...
gi 517718121 1171 SRRLYAVAAEQQTTLFMVLLAAFHVLYA 1198
Cdd:COG1020  1301 LALLLLLALALALLLLLLLLLALLLLAL 1328
PRK08316 PRK08316
acyl-CoA synthetase; Validated
 3-422 1.97e-18

acyl-CoA synthetase; Validated


Pssm-ID: 181381 [Multi-domain]  Cd Length: 523  Bit Score: 90.38  E-value: 1.97e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121    3 NTIQYELARAFAAFPERKAIECGQQTLSYKELDAESDRICELLHAHGAAQYDHIGILMQDRCASIAAVIGILKLGGVFVP 82
Cdd:PRK08316   11 QTIGDILRRSARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVP 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   83 LDPLHPDERLVTMLDTAEVSCLLCDDAQFERAETLQGHEGKYFVLRARQ-------------AMSVQAGSKEAYSHSANA 149
Cdd:PRK08316   91 VNFMLTGEELAYILDHSGARAFLVDPALAPTAEAALALLPVDTLILSLVlggreapggwldfADWAEAGSVAEPDVELAD 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  150 TDPIYIYFTSGSTGKPKAVVGKNESLLHfmnweaswldltdpMRVSQLTSIGFDAvlRDIFV---PI--CA--------- 215
Cdd:PRK08316  171 DDLAQILYTSGTESLPKGAMLTHRALIA--------------EYVSCIVAGDMSA--DDIPLhalPLyhCAqldvflgpy 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  216 ---GGTICIPESReiilDPLRLVHWLEHSRVHVVHCTP----SLFRfinhlsltadsYPDLRYVLLA-------GETIRP 281
Cdd:PRK08316  235 lyvGATNVILDAP----DPELILRTIEAERITSFFAPPtvwiSLLR-----------HPDFDTRDLSslrkgyyGASIMP 299

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  282 -ESLKNWYDNLGNrVRLVNLYGPTEttMIKLFYPIKPEDVHRESIPIGRPLPDTSVYLLDEQQQPVSGSEAGEICIATRY 360
Cdd:PRK08316  300 vEVLKELRERLPG-LRFYNCYGQTE--IAPLATVLGPEEHLRRPGSAGRPVLNVETRVVDDDGNDVAPGEVGEIVHRSPQ 376

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517718121  361 MTHGYFpsSHPDQT--AFipdpcrdQSGeimMYRTGDMGRWLPEGELALLGRKDNQVKIRGNRV 422
Cdd:PRK08316  377 LMLGYW--DDPEKTaeAF-------RGG---WFHSGDLGVMDEEGYITVVDRKKDMIKTGGENV 428
PRK13383 PRK13383
acyl-CoA synthetase; Provisional
 9-442 4.38e-18

acyl-CoA synthetase; Provisional


Pssm-ID: 139531 [Multi-domain]  Cd Length: 516  Bit Score: 89.29  E-value: 4.38e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121    9 LARAFAAFPERKAIECGQQTLSYKELDAESDRICELLHAHGAAQYDHIGILMQDRCASIAAVIGILKLGGVFVPLDPLHP 88
Cdd:PRK13383   41 LAVTAARWPGRTAIIDDDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFR 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   89 DERLVTMLDTAEVSCLLCDDaqfERAETLQGHEGKYFVLRarqamSVQAGSKEAYSHSANATDPIYIYFTSGSTGKPKAV 168
Cdd:PRK13383  121 SDALAAALRAHHISTVVADN---EFAERIAGADDAVAVID-----PATAGAEESGGRPAVAAPGRIVLLTSGTTGKPKGV 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  169 ---------VGKNESLLHFMNWE-ASWLDLTDPMrvsqLTSIGFDAVLrdifVPICAGGTICIPE--SREIILDPLRLVH 236
Cdd:PRK13383  193 prapqlrsaVGVWVTILDRTRLRtGSRISVAMPM----FHGLGLGMLM----LTIALGGTVLTHRhfDAEAALAQASLHR 264

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  237 WLEHSRVHVVHCT----PSLFRFINHLsltadsyPDLRYVLLAGETIRPESLKNWYDNLGNrvRLVNLYGPTETTMIKLf 312
Cdd:PRK13383  265 ADAFTAVPVVLARilelPPRVRARNPL-------PQLRVVMSSGDRLDPTLGQRFMDTYGD--ILYNGYGSTEVGIGAL- 334

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  313 ypIKPEDVHRESIPIGRPLPDTSVYLLDEQQQPVSGSEAGEICIATRYMTHGYfpsshpdqtafipdpcRDQSGEIM--- 389
Cdd:PRK13383  335 --ATPADLRDAPETVGKPVAGCPVRILDRNNRPVGPRVTGRIFVGGELAGTRY----------------TDGGGKAVvdg 396

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 517718121  390 MYRTGDMGRWLPEGELALLGRKDNQVKIRGNRVELGDIEHRLTNMAGIREAVV 442
Cdd:PRK13383  397 MTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAV 449
PRK05691 PRK05691
peptide synthase; Validated
 945-1361 5.91e-18

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 90.61  E-value: 5.91e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  945 PAAK-QAYYPLTAAQMRVFMdEQLVNTGSG-YHITTAFMIYGPIDVTRLERACGQLIERHEALRTSFDIVDG-DPVQRIH 1021
Cdd:PRK05691 3250 PAAEiEDVYPLTPMQEGLLL-HTLLEPGTGlYYMQDRYRINSALDPERFAQAWQAVVARHEALRASFSWNAGeTMLQVIH 3328

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1022 EHCDFHLEIVHLQG----------QQLHTAVNGCirPFQLERAPLIRSILIPLAEEQHLLVLDMHHIVADGKSVFLLQRD 1091
Cdd:PRK05691 3329 KPGRTPIDYLDWRGlpedgqeqrlQALHKQEREA--GFDLLNQPPFHLRLIRVDEARYWFMMSNHHILIDAWCRSLLMND 3406

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1092 LAALY----EGRELHdLPV--QYVDFAQWQTSapvvEDLRRQEQFWQSMFADY-RPLPgIPTDHTPEANERSFAGGHITW 1164
Cdd:PRK05691 3407 FFEIYtalgEGREAQ-LPVppRYRDYIGWLQR----QDLAQARQWWQDNLRGFeRPTP-IPSDRPFLREHAGDSGGMVVG 3480

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1165 EP----DPVLSRRLYAVAAEQQTTLFMVLLAAFHVLYAKYSAREEVTVGTPVEGR--RRAEVRQVVGMFVNALAIR-SYP 1237
Cdd:PRK05691 3481 DCytrlDAADGARLRELAQAHQLTVNTFAQAAWALVLRRYSGDRDVLFGVTVAGRpvSMPQMQRTVGLFINSIALRvQLP 3560

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1238 EGDKPFS--SFLQEIRGTMLQAYEHQDYPLERLAKQLDLhhSRDHLMFDTVFSmlnYEDFAVRS---DDLQFEYAELPTL 1312
Cdd:PRK05691 3561 AAGQRCSvrQWLQGLLDSNMELREYEYLPLVAIQECSEL--PKGQPLFDSLFV---FENAPVEVsvlDRAQSLNASSDSG 3635

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 517718121 1313 SEIYNLRVEIVESP-ERLRGTFKYGQELYEARTVSQLAQDYERILAAVAE 1361
Cdd:PRK05691 3636 RTHTNFPLTAVCYPgDDLGLHLSYDQRYFDAPTVERLLGEFKRLLLALVQ 3685
PRK09088 PRK09088
acyl-CoA synthetase; Validated
 25-442 1.39e-17

acyl-CoA synthetase; Validated


Pssm-ID: 181644 [Multi-domain]  Cd Length: 488  Bit Score: 87.55  E-value: 1.39e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   25 GQQTLSYKELDAESDRICELLHAHGAAQYDHIGILMQDRCASIAAVIGILKLGGVFVPLD-PLHPDErLVTMLDTAEVSC 103
Cdd:PRK09088   19 LGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNwRLSASE-LDALLQDAEPRL 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  104 LLCDDAQfeRAETLQGHEGKYFVLRARQAmsvqagsKEAYSHSANATDPIYIYFTSGSTGKPKAV---------VGKNES 174
Cdd:PRK09088   98 LLGDDAV--AAGRTDVEDLAAFIASADAL-------EPADTPSIPPERVSLILFTSGTSGQPKGVmlsernlqqTAHNFG 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  175 LLHFMNWEASWLdLTDPMrvsqLTSIGFDAVLRdifvPICA-GGTICIPESreiiLDPLRLVHWLEHSRVHVVH--CTPS 251
Cdd:PRK09088  169 VLGRVDAHSSFL-CDAPM----FHIIGLITSVR----PVLAvGGSILVSNG----FEPKRTLGRLGDPALGITHyfCVPQ 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  252 LFR-FINHLSLTADSYPDLRYVLLAGETIRPESLKNWydnLGNRVRLVNLYGPTETTMIkLFYPIKPEDVHRESIPIGRP 330
Cdd:PRK09088  236 MAQaFRAQPGFDAAALRHLTALFTGGAPHAAEDILGW---LDDGIPMVDGFGMSEAGTV-FGMSVDCDVIRAKAGAAGIP 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  331 LPDTSVYLLDEQQQPVSGSEAGEICIATRYMTHGYFPSSHPDQTAFipdpcrDQSGeimMYRTGDMGRWLPEGELALLGR 410
Cdd:PRK09088  312 TPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAF------TGDG---WFRTGDIARRDADGFFWVVDR 382

                         410       420       430
                  ....*....|....*....|....*....|..
gi 517718121  411 KDNQVKIRGNRVELGDIEHRLTNMAGIREAVV 442
Cdd:PRK09088  383 KKDMFISGGENVYPAEIEAVLADHPGIRECAV 414
MCS cd05941
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ...
 18-442 1.57e-17

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: 86.96  E-value: 1.57e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   18 ERKAIECGQQTLSYKELDAESDRICELLHAHGA-AQYDHIGILMQDRCASIAAVIGILKLGGVFVPLDPLHPDERLVTML 96
Cdd:cd05941     1 DRIAIVDDGDSITYADLVARAARLANRLLALGKdLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   97 DTAEVSCLLcddaqferaetlqghegkyfvlrarqamsvqagskeayshsanatDPIYIYFTSGSTGKPKAVVGKNESLL 176
Cdd:cd05941    81 TDSEPSLVL---------------------------------------------DPALILYTSGTTGRPKGVVLTHANLA 115

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  177 hfmnweASWLDLTDPMRVSQLTSI----------G-FDAVLrdifVPICAGGTiCIPESReiiLDPLRLVHWLEHSRVHV 245
Cdd:cd05941   116 ------ANVRALVDAWRWTEDDVLlhvlplhhvhGlVNALL----CPLFAGAS-VEFLPK---FDPKEVAISRLMPSITV 181

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  246 VHCTPSLF-RFINHLSLTADSYPDLRYVllAGETIR---------PESLKNWYDNLGNRvRLVNLYGPTETTMIkLFYPI 315
Cdd:cd05941   182 FMGVPTIYtRLLQYYEAHFTDPQFARAA--AAERLRlmvsgsaalPVPTLEEWEAITGH-TLLERYGMTEIGMA-LSNPL 257

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  316 kpedvHRESIP--IGRPLPDTSVYLLDEQ-QQPVSGSEAGEICIATRYMTHGYFpsSHPDQT--AFIPDPcrdqsgeimM 390
Cdd:cd05941   258 -----DGERRPgtVGMPLPGVQARIVDEEtGEPLPRGEVGEIQVRGPSVFKEYW--NKPEATkeEFTDDG---------W 321

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 517718121  391 YRTGDMGRWLPEGELALLGR-KDNQVKIRGNRVELGDIEHRLTNMAGIREAVV 442
Cdd:cd05941   322 FKTGDLGVVDEDGYYWILGRsSVDIIKSGGYKVSALEIERVLLAHPGVSECAV 374
ttLC_FACS_AlkK_like cd12119
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ...
 9-412 1.61e-17

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


Pssm-ID: 341284 [Multi-domain]  Cd Length: 518  Bit Score: 87.69  E-value: 1.61e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121    9 LARAFAAFPERKAI----ECGQQTLSYKELdaeSDRICELLHAhgaaqYDHIGILMQDRCASIA-----------AVIGI 73
Cdd:cd12119     2 LEHAARLHGDREIVsrthEGEVHRYTYAEV---AERARRLANA-----LRRLGVKPGDRVATLAwnthrhlelyyAVPGM 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   74 lklGGVFVPLDPLHPDERLVTMLDTAEVSCLLCDDAQFERAETLQGH---EGKYFVLRARQAMSVQAGSK-EAYSHSANA 149
Cdd:cd12119    74 ---GAVLHTINPRLFPEQIAYIINHAEDRVVFVDRDFLPLLEAIAPRlptVEHVVVMTDDAAMPEPAGVGvLAYEELLAA 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  150 TDPIY------------IYFTSGSTGKPKAVVGKNESL-LHFMNweaswLDLTDPMRVSQltsigFDAVLrdIFVPI--- 213
Cdd:cd12119   151 ESPEYdwpdfdentaaaICYTSGTTGNPKGVVYSHRSLvLHAMA-----ALLTDGLGLSE-----SDVVL--PVVPMfhv 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  214 ----------CAGGTICIPESReiiLDPLRLVHWLEHSRVHVVHCTPSLFR-FINHLSLTADSYPDLRYVLLAGETIrPE 282
Cdd:cd12119   219 nawglpyaaaMVGAKLVLPGPY---LDPASLAELIEREGVTFAAGVPTVWQgLLDHLEANGRDLSSLRRVVIGGSAV-PR 294

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  283 SLKNWYDNLGnrVRLVNLYGPTET----TMIKL---FYPIKPEDVHRESIPIGRPLPDTSVYLLDEQQQ--PVSGSEAGE 353
Cdd:cd12119   295 SLIEAFEERG--VRVIHAWGMTETsplgTVARPpseHSNLSEDEQLALRAKQGRPVPGVELRIVDDDGRelPWDGKAVGE 372

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  354 ICIATRYMTHGYFpssHPDQTAfipdPCRDQSGeimMYRTGDMGRWLPEGELALLGR-KD 412
Cdd:cd12119   373 LQVRGPWVTKSYY---KNDEES----EALTEDG---WLRTGDVATIDEDGYLTITDRsKD 422
MACS_euk cd05928
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ...
 151-442 2.78e-17

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: 87.14  E-value: 2.78e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  151 DPIYIYFTSGSTGKPKAVVGKNESLLH--FMNwEASWLDLTDPMRVSQLTSIGF-DAVLRDIFVPICAGGTICIPESREi 227
Cdd:cd05928   175 EPMAIYFTSGTTGSPKMAEHSHSSLGLglKVN-GRYWLDLTASDIMWNTSDTGWiKSAWSSLFEPWIQGACVFVHHLPR- 252

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  228 iLDPLRLVHWLEHSRVHVVHCTPSLFRFINHLSLTADSYPDLRYVLLAGETIRPESLKNWYDNLGnrVRLVNLYGPTETT 307
Cdd:cd05928   253 -FDPLVILKTLSSYPITTFCGAPTVYRMLVQQDLSSYKFPSLQHCVTGGEPLNPEVLEKWKAQTG--LDIYEGYGQTETG 329

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  308 MIKLFY---PIKPEDvhresipIGRPLPDTSVYLLDEQQQPVSGSEAGEICIATRYMTHGYFPSSH---PDQTAfiPDPC 381
Cdd:cd05928   330 LICANFkgmKIKPGS-------MGKASPPYDVQIIDDNGNVLPPGTEGDIGIRVKPIRPFGLFSGYvdnPEKTA--ATIR 400

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517718121  382 RDqsgeimMYRTGDMGRWLPEGELALLGRKDNQVKIRGNRVELGDIEHRLTNMAGIREAVV 442
Cdd:cd05928   401 GD------FYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAV 455
A_NRPS_Bac cd17655
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ...
 788-849 3.83e-17

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: 86.23  E-value: 3.83e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517718121  788 EEAQEPLLIAYYLADKMIDDEQLSVYLRRFLPDYMIPARFIRLDKMPLTPNGKLDYNALPSP 849
Cdd:cd17655   428 DEQGQNYLCAYIVSEKELPVAQLREFLARELPDYMIPSYFIKLDEIPLTPNGKVDRKALPEP 489
OSB_CoA_lg cd05912
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ...
 28-442 7.06e-17

O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.


Pssm-ID: 341238 [Multi-domain]  Cd Length: 411  Bit Score: 84.71  E-value: 7.06e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   28 TLSYKELDAESDRICELLHAHGAAQYDHIGILMQDRCASIAAVIGILKLGGVFVPLDP-LHPDERLVTMLDTaevscllc 106
Cdd:cd05912     1 SYTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTrLTPNELAFQLKDS-------- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  107 dDAQFERAETlqghegkyfvlrarqamsvqagskeayshsanatdpiyIYFTSGSTGKPKAVVGKNESllHFMNWEASWL 186
Cdd:cd05912    73 -DVKLDDIAT--------------------------------------IMYTSGTTGKPKGVQQTFGN--HWWSAIGSAL 111

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  187 DL--TD--------PM-RVSQLTSI------GFDAVLRDIFvpicaggticipesreiilDPLRLVHWLEHSRVHVVHCT 249
Cdd:cd05912   112 NLglTEddnwlcalPLfHISGLSILmrsviyGMTVYLVDKF-------------------DAEQVLHLINSGKVTIISVV 172

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  250 PSLFRFInhLSLTADSYP-DLRYVLLAGETIrPESLKNWYDNLGnrVRLVNLYGPTETTmiKLFYPIKPEDVHRESIPIG 328
Cdd:cd05912   173 PTMLQRL--LEILGEGYPnNLRCILLGGGPA-PKPLLEQCKEKG--IPVYQSYGMTETC--SQIVTLSPEDALNKIGSAG 245

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  329 RPLPDTSVYLLDEQQQPvsgSEAGEICIATRYMTHGYFPSSHPDQTAFipdpcrdQSGeimMYRTGDMGRWLPEGELALL 408
Cdd:cd05912   246 KPLFPVELKIEDDGQPP---YEVGEILLKGPNVTKGYLNRPDATEESF-------ENG---WFKTGDIGYLDEEGFLYVL 312

                         410       420       430
                  ....*....|....*....|....*....|....
gi 517718121  409 GRKDNQVKIRGNRVELGDIEHRLTNMAGIREAVV 442
Cdd:cd05912   313 DRRSDLIISGGENIYPAEIEEVLLSHPAIKEAGV 346
FAA1 COG1022
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
9-442 8.14e-17

Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];


Pssm-ID: 440645 [Multi-domain]  Cd Length: 603  Bit Score: 85.92  E-value: 8.14e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121    9 LARAFAAFPERKAIEC----GQQTLSYKELDAESDRICELLHAHGAAQYDHIGILMQDRCASIAAVIGILKLGGVFVPLD 84
Cdd:COG1022    17 LRRRAARFPDRVALREkedgIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAVTVPIY 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   85 PLHPDERLVTMLDTAEVSCLLC-DDAQFERAETLQGH------------EGKYFVLRAR-----QAMSVQAGSKEAYSHS 146
Cdd:COG1022    97 PTSSAEEVAYILNDSGAKVLFVeDQEQLDKLLEVRDElpslrhivvldpRGLRDDPRLLsldelLALGREVADPAELEAR 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  147 ANATDP----IYIYfTSGSTGKPKAVVgknesLLH--FMnWEASWLDLTDPMRVSqltsigfDAVLrdIFVPIC------ 214
Cdd:COG1022   177 RAAVKPddlaTIIY-TSGTTGRPKGVM-----LTHrnLL-SNARALLERLPLGPG-------DRTL--SFLPLAhvfert 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  215 -------AGGTICIPESREIILDPLR----------------------------------LVHW-----LEHSRVHVVHC 248
Cdd:COG1022   241 vsyyalaAGATVAFAESPDTLAEDLRevkptfmlavprvwekvyagiqakaeeagglkrkLFRWalavgRRYARARLAGK 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  249 TPSLFRFINHLslTADS--YP--------DLRYVLLAGETIRPEsLKNWYDNLGnrVRLVNLYGPTETTmiklfyPI--- 315
Cdd:COG1022   321 SPSLLLRLKHA--LADKlvFSklrealggRLRFAVSGGAALGPE-LARFFRALG--IPVLEGYGLTETS------PVitv 389

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  316 -KPEDVHRESIpiGRPLPDTSVYLldeqqqpvsgSEAGEICIATRYMTHGYFpsSHPDQTA--FIPDpcrdqsGeimMYR 392
Cdd:COG1022   390 nRPGDNRIGTV--GPPLPGVEVKI----------AEDGEILVRGPNVMKGYY--KNPEATAeaFDAD------G---WLH 446

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|.
gi 517718121  393 TGDMGRWLPEGELALLGRKDNQVKIR-GNRVELGDIEHRLTNMAGIREAVV 442
Cdd:COG1022   447 TGDIGELDEDGFLRITGRKKDLIVTSgGKNVAPQPIENALKASPLIEQAVV 497
AAS_C cd05909
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ...
 54-428 9.97e-17

C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.


Pssm-ID: 341235 [Multi-domain]  Cd Length: 490  Bit Score: 85.08  E-value: 9.97e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   54 DHIGILMQDRCASIAAVIGILKLGGVFVPLDPLHPDERLVTMLDTAEVSCLLCDDAQFERAETLQGHEGKYFV------- 126
Cdd:cd05909    32 ENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTVLTSKQFIEKLKLHHLFDVEYDArivyled 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  127 LRAR-----------QAMSVQAGS-KEAYSHSANATDPIYIYFTSGSTGKPKAVVGKNESLLHfmnweaswldltdpmRV 194
Cdd:cd05909   112 LRAKiskadkckaflAGKFPPKWLlRIFGVAPVQPDDPAVILFTSGSEGLPKGVVLSHKNLLA---------------NV 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  195 SQLTSIgFDAVLRDIF---VPI--CAGGTICI---------------PesreiiLDPLRLVHWLEHSRVHVVHCTPSLFR 254
Cdd:cd05909   177 EQITAI-FDPNPEDVVfgaLPFfhSFGLTGCLwlpllsgikvvfhpnP------LDYKKIPELIYDKKATILLGTPTFLR 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  255 -FINhlSLTADSYPDLRYVLLAGETIRPESLKNWYDNLGnrVRLVNLYGPTET----TMIKLFYPIKPEDVhresipiGR 329
Cdd:cd05909   250 gYAR--AAHPEDFSSLRLVVAGAEKLKDTLRQEFQEKFG--IRILEGYGTTECspviSVNTPQSPNKEGTV-------GR 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  330 PLPDTSVYLLD-EQQQPVSGSEAGEICIATRYMTHGYFPSshPDQTAFIPdpcRDQsgeimMYRTGDMGRWLPEGELALL 408
Cdd:cd05909   319 PLPGMEVKIVSvETHEEVPIGEGGLLLVRGPNVMLGYLNE--PELTSFAF---GDG-----WYDTGDIGKIDGEGFLTIT 388

                         410       420
                  ....*....|....*....|
gi 517718121  409 GRKDNQVKIRGNRVELGDIE 428
Cdd:cd05909   389 GRLSRFAKIAGEMVSLEAIE 408
FACL_like_1 cd05910
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 27-415 1.02e-16

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: 84.82  E-value: 1.02e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   27 QTLSYKELDAESDRICELLHAHGAAQYDHIGILMQDRCASIAAVIGILKLGGVFVPLDPLHPDERLVTMLDTAEvscllc 106
Cdd:cd05910     1 SRLSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQEAE------ 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  107 ddaqferaetlqghegkyfvlrarqamsvqagsKEAYSHSANATDPIYIYFTSGSTGKPKAVVGKNESLlhfmnweASWL 186
Cdd:cd05910    75 ---------------------------------PDAFIGIPKADEPAAILFTSGSTGTPKGVVYRHGTF-------AAQI 114

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  187 DltdpmRVSQLTSIGFDAVLRDIFVPI-----CAGGTICIPE---SREIILDPLRLVHWLEHSRVHVVHCTPSLFRFINH 258
Cdd:cd05910   115 D-----ALRQLYGIRPGEVDLATFPLFalfgpALGLTSVIPDmdpTRPARADPQKLVGAIRQYGVSIVFGSPALLERVAR 189

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  259 LSLTAD-SYPDLRYVLLAGETIRPESLKNWYDNLGNRVRLVNLYGPTETTMIKLfypIKPEDVHRESIP---------IG 328
Cdd:cd05910   190 YCAQHGiTLPSLRRVLSAGAPVPIALAARLRKMLSDEAEILTPYGATEALPVSS---IGSRELLATTTAatsggagtcVG 266

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  329 RPLPDTSVYLLDEQQQPVSG---------SEAGEICIATRYMTHGYFpsSHPDQTAF--IPDPcrdqsGEIMMYRTGDMG 397
Cdd:cd05910   267 RPIPGVRVRIIEIDDEPIAEwddtlelprGEIGEITVTGPTVTPTYV--NRPVATALakIDDN-----SEGFWHRMGDLG 339

                         410
                  ....*....|....*...
gi 517718121  398 RWLPEGELALLGRKDNQV 415
Cdd:cd05910   340 YLDDEGRLWFCGRKAHRV 357
beta-lac_NRPS cd19547
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ...
 952-1363 1.76e-16

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: 83.51  E-value: 1.76e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  952 YPLTAAQMRVFMDEQLVNTGSGYHITTAFMIYGPIDVTRLERACGQLIERHEALRTSFDIVD-GDPVQRIHEHCDFHLEI 1030
Cdd:cd19547     2 YPLAPMQEGMLFRGLFWPDSDAYFNQNVLELVGGTDEDVLREAWRRVADRYEILRTGFTWRDrAEPLQYVRDDLAPPWAL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1031 VHLQGQQLHTAVNGCIRPFQLERA--------PLIRSILIPLAEEQHLLVLDMHHIVADGKSVFLLQRDLAALYE----G 1098
Cdd:cd19547    82 LDWSGEDPDRRAELLERLLADDRAaglsladcPLYRLTLVRLGGGRHYLLWSHHHILLDGWCLSLIWGDVFRVYEelahG 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1099 RELHDLPVQ-YVDFAQWQTSAPVVEDlrRQEQFWQSMFADYRPlpgIPTDHTPEANERSFAGghITWEPDPVLSRRLYAV 1177
Cdd:cd19547   162 REPQLSPCRpYRDYVRWIRARTAQSE--ESERFWREYLRDLTP---SPFSTAPADREGEFDT--VVHEFPEQLTRLVNEA 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1178 AAEQQTTLFMVLLAAFHVLYAKYSAREEVTVGTPVEGR--RRAEVRQVVGMFVNALAIRSYPEGDKPFSSFLQEIRGTML 1255
Cdd:cd19547   235 ARGYGVTTNAISQAAWSMLLALQTGARDVVHGLTIAGRppELEGSEHMVGIFINTIPLRIRLDPDQTVTGLLETIHRDLA 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121 1256 QAYEHQDYPLERLAKQLDLHHSRDHLMFDTVFSMLNYEDFAVRSDDLQFEYAELPTLSEIYNLRVEIVESPERLRGTFKY 1335
Cdd:cd19547   315 TTAAHGHVPLAQIKSWASGERLSGGRVFDNLVAFENYPEDNLPGDDLSIQIIDLHAQEKTEYPIGLIVLPLQKLAFHFNY 394

                         410       420
                  ....*....|....*....|....*...
gi 517718121 1336 GQELYEARTVSQLAQDYERILAAVAESP 1363
Cdd:cd19547   395 DTTHFTRAQVDRFIEVFRLLTEQLCRRP 422
AFD_YhfT-like cd17633
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ...
 151-442 1.93e-16

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: 82.07  E-value: 1.93e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  151 DPIYIYFTSGSTGKPKAVVGKNESLLHFMNWEASWLDLTDPMRVSQLTSIGFDAVLRDIFVPICAGGTICIPESreiiLD 230
Cdd:cd17633     1 NPFYIGFTSGTTGLPKAYYRSERSWIESFVCNEDLFNISGEDAILAPGPLSHSLFLYGAISALYLGGTFIGQRK----FN 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  231 PLRLVHWLEHSRVHVVHCTPSLfrfINHLSLTADSYPDLRYVLLAGETIRPESLKNwYDNLGNRVRLVNLYGPTETTMIK 310
Cdd:cd17633    77 PKSWIRKINQYNATVIYLVPTM---LQALARTLEPESKIKSIFSSGQKLFESTKKK-LKNIFPKANLIEFYGTSELSFIT 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  311 lfYPIKPEDVHRESIpiGRPLPDTSVYLLDEQqqpvsGSEAGEICIATRYMTHGYFP--SSHPDQtafipdpcrdqsgei 388
Cdd:cd17633   153 --YNFNQESRPPNSV--GRPFPNVEIEIRNAD-----GGEIGKIFVKSEMVFSGYVRggFSNPDG--------------- 208

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 517718121  389 mMYRTGDMGRWLPEGELALLGRKDNQVKIRGNRVELGDIEHRLTNMAGIREAVV 442
Cdd:cd17633   209 -WMSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIV 261
PRK07470 PRK07470
acyl-CoA synthetase; Validated
 9-442 3.01e-16

acyl-CoA synthetase; Validated


Pssm-ID: 180988 [Multi-domain]  Cd Length: 528  Bit Score: 83.55  E-value: 3.01e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121    9 LARAFAAFPERKAIECGQQTLSYKELDAESDRICELLHAHGAAQYDHIGILMQDRCASIAAVIGILKLGGVFVPLD-PLH 87
Cdd:PRK07470   13 LRQAARRFPDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNfRQT 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   88 PDErLVTMLDTAEVSCLLCDDAQFERAETLQG---HEGKYFVL-RARQAMSVQAGSKEAYSHS-ANAT----DPIYIYFT 158
Cdd:PRK07470   93 PDE-VAYLAEASGARAMICHADFPEHAAAVRAaspDLTHVVAIgGARAGLDYEALVARHLGARvANAAvdhdDPCWFFFT 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  159 SGSTGKPKAVVgknesLLH----FM--NWEAswlDLTdPMRVSQLTSIgfdavlrdIFVPICAGG-------------TI 219
Cdd:PRK07470  172 SGTTGRPKAAV-----LTHgqmaFVitNHLA---DLM-PGTTEQDASL--------VVAPLSHGAgihqlcqvargaaTV 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  220 CIPESREIILDPLRLVhwlEHSRVHVVHCTPSLFR-FINHLSLTADSYPDLRYVLLAGETIRPESLKNWYDNLGNrvRLV 298
Cdd:PRK07470  235 LLPSERFDPAEVWALV---ERHRVTNLFTVPTILKmLVEHPAVDRYDHSSLRYVIYAGAPMYRADQKRALAKLGK--VLV 309

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  299 NLYGPTETT-MIKLFYPI--KPEDVHRESI-PIGRPLPDTSVYLLDEQQQPVSGSEAGEICIATRYMTHGYFPSSHPDQT 374
Cdd:PRK07470  310 QYFGLGEVTgNITVLPPAlhDAEDGPDARIgTCGFERTGMEVQIQDDEGRELPPGETGEICVIGPAVFAGYYNNPEANAK 389

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517718121  375 AFipdpcRDQsgeimMYRTGDMGRWLPEGELALLGRKDNQVKIRGNRVELGDIEHRLTNMAGIREAVV 442
Cdd:PRK07470  390 AF-----RDG-----WFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAV 447
A_NRPS cd05930
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ...
 783-846 3.13e-16

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: 82.96  E-value: 3.13e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517718121  783 VQLQVEEAQEPLLIAYYLADK--MIDDEQLSVYLRRFLPDYMIPARFIRLDKMPLTPNGKLDYNAL 846
Cdd:cd05930   379 VVAREDGDGEKRLVAYVVPDEggELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
PRK07638 PRK07638
acyl-CoA synthetase; Validated
 17-442 3.43e-16

acyl-CoA synthetase; Validated


Pssm-ID: 236071 [Multi-domain]  Cd Length: 487  Bit Score: 83.29  E-value: 3.43e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   17 PERKAIECGQQTLSYKELDAESDRICELLHAHgAAQYDHIGILMQDRCASIAAVIGILKLGGVFVPLDPLHPDERLVTML 96
Cdd:PRK07638   15 PNKIAIKENDRVLTYKDWFESVCKVANWLNEK-ESKNKTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELKERL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   97 DTAEVSCLLCDDAQFERaetLQGHEGKyfVLRARQAMSVQAGSKEAYSHSANAT-DPIYIYFTSGSTGKPKAVVGKNESL 175
Cdd:PRK07638   94 AISNADMIVTERYKLND---LPDEEGR--VIEIDEWKRMIEKYLPTYAPIENVQnAPFYMGFTSGSTGKPKAFLRAQQSW 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  176 LHFMNWEASWLDLTDPMRV----SQLTSIGFDAVLRDIFVpicaGGTICIPESreiiLDPLRLVHWLEHSRVHVVHCTPS 251
Cdd:PRK07638  169 LHSFDCNVHDFHMKREDSVliagTLVHSLFLYGAISTLYV----GQTVHLMRK----FIPNQVLDKLETENISVMYTVPT 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  252 LF-------RFINHLSLTADSYPDLryvllagETIRPESLKNWYDNLgnrvRLVNLYGPTETTMIKLfypIKPEDVHRES 324
Cdd:PRK07638  241 MLeslykenRVIENKMKIISSGAKW-------EAEAKEKIKNIFPYA----KLYEFYGASELSFVTA---LVDEESERRP 306

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  325 IPIGRPLPDTSVYLLDEQQQPVSGSEAGEICIATRYMTHGYFPSShpdqtafIPDPCRDQSGEIMMYrtgDMGRWLPEGE 404
Cdd:PRK07638  307 NSVGRPFHNVQVRICNEAGEEVQKGEIGTVYVKSPQFFMGYIIGG-------VLARELNADGWMTVR---DVGYEDEEGF 376

                         410       420       430
                  ....*....|....*....|....*....|....*...
gi 517718121  405 LALLGRKDNQVKIRGNRVELGDIEHRLTNMAGIREAVV 442
Cdd:PRK07638  377 IYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVV 414
PRK13382 PRK13382
bile acid CoA ligase;
9-443 4.33e-16

bile acid CoA ligase;


Pssm-ID: 172019 [Multi-domain]  Cd Length: 537  Bit Score: 83.27  E-value: 4.33e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121    9 LARAFAAFPERKAI--ECGqqTLSYKELDAESDRICELLHAHGAAQYDHIGILMQDRCASIAAVIGILKLGGVFVPL--- 83
Cdd:PRK13382   49 FAIAAQRCPDRPGLidELG--TLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLnts 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   84 ---------------DPLHPDERLVTMLDTAEVSCllcDDAQFERAETLQGHEGKYFVLRARQA-MSVQAGSKEAYShsa 147
Cdd:PRK13382  127 fagpalaevvtregvDTVIYDEEFSATVDRALADC---PQATRIVAWTDEDHDLTVEVLIAAHAgQRPEPTGRKGRV--- 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  148 natdpiyIYFTSGSTGKPKavvGKNESLLHFMNWEASWLDLTdPMRVSQLTSI--------GFDAVLrdifvpiCAGGTI 219
Cdd:PRK13382  201 -------ILLTSGTTGTPK---GARRSGPGGIGTLKAILDRT-PWRAEEPTVIvapmfhawGFSQLV-------LAASLA 262

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  220 C-IPESREiiLDPLRLVHWLEHSRVHVVHCTPSLFRFINHL---SLTADSYPDLRYVLLAGETIRPESLKNWYDNLGNRv 295
Cdd:PRK13382  263 CtIVTRRR--FDPEATLDLIDRHRATGLAVVPVMFDRIMDLpaeVRNRYSGRSLRFAAASGSRMRPDVVIAFMDQFGDV- 339

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  296 rLVNLYGPTETTMIKLfypIKPEDVHRESIPIGRPLPDTSVYLLDEQQQPVSGSEAGEICIATRYMTHGYFPSSHPDqta 375
Cdd:PRK13382  340 -IYNNYNATEAGMIAT---ATPADLRAAPDTAGRPAEGTEIRILDQDFREVPTGEVGTIFVRNDTQFDGYTSGSTKD--- 412

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517718121  376 FIpdpcrdqsgEIMMyRTGDMGRWLPEGELALLGRKDNQVKIRGNRVELGDIEHRLTNMAGIREAVVR 443
Cdd:PRK13382  413 FH---------DGFM-ASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVI 470
FADD10 cd17635
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ...
 151-442 5.19e-16

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: 81.15  E-value: 5.19e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  151 DPIYIYFTSGSTGKPKAVVGKNESLL----HFMNWEASWLDLTDPMRVSQLTSIGFDAVLRDIFVpicAGGTICIPESRE 226
Cdd:cd17635     2 DPLAVIFTSGTTGEPKAVLLANKTFFavpdILQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLI---HGGLCVTGGENT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  227 IILDPLRLvhwLEHSRVHVVHCTPSLFRFINHLSLTADSY-PDLRYVLLAGETIRPESLKN--WYDNlgnrVRLVNLYGP 303
Cdd:cd17635    79 TYKSLFKI---LTTNAVTTTCLVPTLLSKLVSELKSANATvPSLRLIGYGGSRAIAADVRFieATGL----TNTAQVYGL 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  304 TETTMIKLFypikpeDVHRESIPI---GRPLPDTSVYLLDEQQQPVSGSEAGEICIATRYMTHGYFPSSHPDQTAFIPDp 380
Cdd:cd17635   152 SETGTALCL------PTDDDSIEInavGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLIDG- 224

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517718121  381 crdqsgeimMYRTGDMGRWLPEGELALLGRKDNQVKIRGNRVELGDIEHRLTNMAGIREAVV 442
Cdd:cd17635   225 ---------WVNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECAC 277
PrpE cd05967
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ...
 26-442 5.65e-16

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: 83.13  E-value: 5.65e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   26 QQTLSYKELDAESDRICELLHAHGAAQYDHIGILM---------QDRCASIAAVIGILkLGGvFVPldplhpdERLVTML 96
Cdd:cd05967    80 ERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMpmipeaaiaMLACARIGAIHSVV-FGG-FAA-------KELASRI 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   97 DTAEVSCLLCDDAQFE------------RAETLQGHEGKYFVLRARQAMSVQAGS-----------KEAYSH---SANAT 150
Cdd:cd05967   151 DDAKPKLIVTASCGIEpgkvvpykplldKALELSGHKPHHVLVLNRPQVPADLTKpgrdldwsellAKAEPVdcvPVAAT 230

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  151 DPIYIYFTSGSTGKPKAVVGKNESLLHFMNWEASWLDLTDPMRVSQLTS-IGFdaVLRDIFV---PICAGGTICIPESRe 226
Cdd:cd05967   231 DPLYILYTSGTTGKPKGVVRDNGGHAVALNWSMRNIYGIKPGDVWWAASdVGW--VVGHSYIvygPLLHGATTVLYEGK- 307

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  227 iildPLRL----VHW--LEHSRVHVVHCTPSLFRFINHLSLTAD-----SYPDLRYVLLAGETIRPESLkNWYDNLGNrV 295
Cdd:cd05967   308 ----PVGTpdpgAFWrvIEKYQVNALFTAPTAIRAIRKEDPDGKyikkyDLSSLRTLFLAGERLDPPTL-EWAENTLG-V 381

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  296 RLVNLYGPTETTmiklfYPIKPEDVHRESIPI-----GRPLPDTSVYLLDEQQQPVSGSEAGEICIAtRYMTHGYFPSSH 370
Cdd:cd05967   382 PVIDHWWQTETG-----WPITANPVGLEPLPIkagspGKPVPGYQVQVLDEDGEPVGPNELGNIVIK-LPLPPGCLLTLW 455

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517718121  371 PDQTAFIPDPCRDQSGeimMYRTGDMGRWLPEGELALLGRKDNQVKIRGNRVELGDIEHRLTNMAGIREAVV 442
Cdd:cd05967   456 KNDERFKKLYLSKFPG---YYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAV 524
PRK07059 PRK07059
Long-chain-fatty-acid--CoA ligase; Validated
 9-470 5.79e-16

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


Pssm-ID: 235923 [Multi-domain]  Cd Length: 557  Bit Score: 82.76  E-value: 5.79e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121    9 LARAFAAFPERKAIECGQQTLSYKELDAESDRICELLHAHGAAQYDHIGILMQDRCASIAAVIGILKLGGVFVPLDPLH- 87
Cdd:PRK07059   29 LEESFRQYADRPAFICMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVNVNPLYt 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   88 PDERLVTMLDT-AEVSCLLcddAQFerAETLQ--------------------GHEGKY--FVLRARQAM----------- 133
Cdd:PRK07059  109 PRELEHQLKDSgAEAIVVL---ENF--ATTVQqvlaktavkhvvvasmgdllGFKGHIvnFVVRRVKKMvpawslpghvr 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  134 ---SVQAGSKEAYSHSANATDPI-YIYFTSGSTGkpkavVGKNESLLH------FMNWEAsWLD--LTDPMRVSQLTSIG 201
Cdd:PRK07059  184 fndALAEGARQTFKPVKLGPDDVaFLQYTGGTTG-----VSKGATLLHrnivanVLQMEA-WLQpaFEKKPRPDQLNFVC 257

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  202 fdAV-LRDIF-------VPICAGGT-ICIPESREIildPlRLVHWLEHSRVHVVHCTPSLFR-FINHLSLTADSYPDLRY 271
Cdd:PRK07059  258 --ALpLYHIFaltvcglLGMRTGGRnILIPNPRDI---P-GFIKELKKYQVHIFPAVNTLYNaLLNNPDFDKLDFSKLIV 331

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  272 VLLAGETIRPESLKNWYDNLGNRVrlVNLYGPTETTmiklfyPI---KPEDVHRESIPIGRPLPDTSVYLLDEQQQPVSG 348
Cdd:PRK07059  332 ANGGGMAVQRPVAERWLEMTGCPI--TEGYGLSETS------PVatcNPVDATEFSGTIGLPLPSTEVSIRDDDGNDLPL 403

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  349 SEAGEICIATRYMTHGYFpsSHPDQTAfipdpcrdqsgEIMM----YRTGDMGRWLPEGELALLGRKDNQVKIRGNRVEL 424
Cdd:PRK07059  404 GEPGEICIRGPQVMAGYW--NRPDETA-----------KVMTadgfFRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYP 470

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*.
gi 517718121  425 GDIEHRLTNMAGIREavvrmrakadtpkgmaqqhCAACGLPSTYPG 470
Cdd:PRK07059  471 NEIEEVVASHPGVLE-------------------VAAVGVPDEHSG 497
PRK07798 PRK07798
acyl-CoA synthetase; Validated
 14-415 5.92e-16

acyl-CoA synthetase; Validated


Pssm-ID: 236100 [Multi-domain]  Cd Length: 533  Bit Score: 82.63  E-value: 5.92e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   14 AAFPERKAIECGQQTLSYKELDAESDRICELLHAHGAAQYDHIGILMQDRCASIAAVIGILKLGGVFVPLDPLHPDERLV 93
Cdd:PRK07798   14 DAVPDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELR 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   94 TMLDTAEVSCLLCDDAQFER-AETLQGHEgkyfvlRARQAMSVQAGSKEAYSH------SANAT------------DPIY 154
Cdd:PRK07798   94 YLLDDSDAVALVYEREFAPRvAEVLPRLP------KLRTLVVVEDGSGNDLLPgavdyeDALAAgsperdfgerspDDLY 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  155 IYFTSGSTGKPKAVVGKNESLlhfmnWEASwLDLTDPMRVSQLTSIgfDAVLRD-------IFVPIC------------- 214
Cdd:PRK07798  168 LLYTGGTTGMPKGVMWRQEDI-----FRVL-LGGRDFATGEPIEDE--EELAKRaaagpgmRRFPAPplmhgagqwaafa 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  215 ---AGGTICIPESREiiLDPLRLVHWLEHSRVHVVHCTPSLF-R-FINHLsLTADSY--PDLRYVLLAGETIRPESLKNW 287
Cdd:PRK07798  240 alfSGQTVVLLPDVR--FDADEVWRTIEREKVNVITIVGDAMaRpLLDAL-EARGPYdlSSLFAIASGGALFSPSVKEAL 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  288 YDNLGNRVrLVNLYGPTET-TMIKLFYPIKPEDVHRESIPIGrplPDTSVylLDEQQQPVS-GSEAGEIcIATR-YMTHG 364
Cdd:PRK07798  317 LELLPNVV-LTDSIGSSETgFGGSGTVAKGAVHTGGPRFTIG---PRTVV--LDEDGNPVEpGSGEIGW-IARRgHIPLG 389

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  365 YFpsSHPDQTAFIpdpcrdqsgeimmYRT---------GDMGRWLPEGELALLGRkDNQV 415
Cdd:PRK07798  390 YY--KDPEKTAET-------------FPTidgvryaipGDRARVEADGTITLLGR-GSVC 433
PRK09274 PRK09274
peptide synthase; Provisional
 9-416 7.25e-16

peptide synthase; Provisional


Pssm-ID: 236443 [Multi-domain]  Cd Length: 552  Bit Score: 82.64  E-value: 7.25e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121    9 LARAFAAFPERKAIECGQ----------QTLSYKELDAESDRICELLHAHGAAQYDHIgILMQDRCAS-IAAVIGILKLG 77
Cdd:PRK09274   12 LPRAAQERPDQLAVAVPGgrgadgklayDELSFAELDARSDAIAHGLNAAGIGRGMRA-VLMVTPSLEfFALTFALFKAG 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   78 GVFVPLDPLHPDERLVTMLDTAE------------VSCLL------------CDDAQFERAETL----QGHEGKYFVLRA 129
Cdd:PRK09274   91 AVPVLVDPGMGIKNLKQCLAEAQpdafigipkahlARRLFgwgkpsvrrlvtVGGRLLWGGTTLatllRDGAAAPFPMAD 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  130 rqamsvqagskeayshsANATDPIYIYFTSGSTGKPKAVVgknesllhfmnweaswldLTDPMRVSQLTSI--------- 200
Cdd:PRK09274  171 -----------------LAPDDMAAILFTSGSTGTPKGVV------------------YTHGMFEAQIEALredygiepg 215

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  201 GFDAVLRDIFV--PICAGGTICIPE---SREIILDPLRLVHWLEHSRVHVVHCTPSLFRFINHLSLTAD-SYPDLRYVLL 274
Cdd:PRK09274  216 EIDLPTFPLFAlfGPALGMTSVIPDmdpTRPATVDPAKLFAAIERYGVTNLFGSPALLERLGRYGEANGiKLPSLRRVIS 295

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  275 AGETIRPESLKNWYDNLGNRVRLVNLYGPTET---TMI----KLFYPIKPEDVHrESIPIGRPLPDTSVYLLD------- 340
Cdd:PRK09274  296 AGAPVPIAVIERFRAMLPPDAEILTPYGATEAlpiSSIesreILFATRAATDNG-AGICVGRPVDGVEVRIIAisdapip 374

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517718121  341 --EQQQPVSGSEAGEICIATRYMTHGYFPSSHPDQTAFIPDPCRDqsgeiMMYRTGDMGRWLPEGELALLGRKDNQVK 416
Cdd:PRK09274  375 ewDDALRLATGEIGEIVVAGPMVTRSYYNRPEATRLAKIPDGQGD-----VWHRMGDLGYLDAQGRLWFCGRKAHRVE 447
PRK06087 PRK06087
medium-chain fatty-acid--CoA ligase;
2-442 1.58e-15

medium-chain fatty-acid--CoA ligase;


Pssm-ID: 180393 [Multi-domain]  Cd Length: 547  Bit Score: 81.33  E-value: 1.58e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121    2 DNTIQYELARAFAAFPERKAIECGQQT-LSYKELDAESDRICELLHAHGAAQYDHIGILMQDRCASIAAVIGILKLGGVF 80
Cdd:PRK06087   22 DASLADYWQQTARAMPDKIAVVDNHGAsYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVS 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   81 VPLDPLHPDERLVTMLDTAEVSCLLC---------DDAQFERAETLQGHEGKYFVLRARQAMS-------VQAGSKEAYS 144
Cdd:PRK06087  102 VPLLPSWREAELVWVLNKCQAKMFFAptlfkqtrpVDLILPLQNQLPQLQQIVGVDKLAPATSslslsqiIADYEPLTTA 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  145 HSANATDPIYIYFTSGSTGKPKAVVGKNESLLHFMNWEASWLDLT--DPMRV-SQLT-SIGFdavLRDIFVPICAGGTIC 220
Cdd:PRK06087  182 ITTHGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTwqDVFMMpAPLGhATGF---LHGVTAPFLIGARSV 258

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  221 IPEsreiILDPLRLVHWLEHSRVHVVH-CTPSLFRFINHLSLTADSYPDLRYVLLAGETIrPESLKNwyDNLGNRVRLVN 299
Cdd:PRK06087  259 LLD----IFTPDACLALLEQQRCTCMLgATPFIYDLLNLLEKQPADLSALRFFLCGGTTI-PKKVAR--ECQQRGIKLLS 331

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  300 LYGPTET---TMIKLFYPIkPEDVHREsipiGRPLPDTSVYLLDEQQQPVSGSEAGEICIATRYMTHGYFpsSHPDQTAF 376
Cdd:PRK06087  332 VYGSTESsphAVVNLDDPL-SRFMHTD----GYAAAGVEIKVVDEARKTLPPGCEGEEASRGPNVFMGYL--DEPELTAR 404

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517718121  377 IPDpcrdqsgEIMMYRTGDMGRWLPEGELALLGRKdNQVKIRGNR-VELGDIEHRLTNMAGIREAVV 442
Cdd:PRK06087  405 ALD-------EEGWYYSGDLCRMDEAGYIKITGRK-KDIIVRGGEnISSREVEDILLQHPKIHDACV 463
A_NRPS_Srf_like cd12117
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ...
 783-846 2.27e-15

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: 80.71  E-value: 2.27e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517718121  783 VQLQVEEAQEPLLIAYYLADKMIDDEQLSVYLRRFLPDYMIPARFIRLDKMPLTPNGKLDYNAL 846
Cdd:cd12117   420 VVVREDAGGDKRLVAYVVAEGALDAAELRAFLRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
PRK12583 PRK12583
acyl-CoA synthetase; Provisional
 2-419 3.04e-15

acyl-CoA synthetase; Provisional


Pssm-ID: 237145 [Multi-domain]  Cd Length: 558  Bit Score: 80.59  E-value: 3.04e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121    2 DNTIQYELARAFAAFPERKAIECGQQTL--SYKELDAESDRICELLHAHGAAQYDHIGILMQDRCASIAAVIGILKLGGV 79
Cdd:PRK12583   17 TQTIGDAFDATVARFPDREALVVRHQALryTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAI 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   80 FVPLDPLHPDERLVTMLDTAEVSCLLCDDAqFERA---ETLQG-----HEGKYFVLR----------------------- 128
Cdd:PRK12583   97 LVNINPAYRASELEYALGQSGVRWVICADA-FKTSdyhAMLQEllpglAEGQPGALAcerlpelrgvvslapapppgfla 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  129 --ARQAM--SVQAGSKEAYSHSANATDPIYIYFTSGSTGKPKAVVGKNESLLHFMNWEASWLDLTDPMRVSQLTSI--GF 202
Cdd:PRK12583  176 whELQARgeTVSREALAERQASLDRDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLCVPVPLyhCF 255

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  203 DAVLRDIfVPICAGGTICIPesrEIILDPLRLVHWLEHSRVHVVHCTPSLF-RFINHLSLTADSYPDLRYVLLAGETIRP 281
Cdd:PRK12583  256 GMVLANL-GCMTVGACLVYP---NEAFDPLATLQAVEEERCTALYGVPTMFiAELDHPQRGNFDLSSLRTGIMAGAPCPI 331

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  282 ESLKNWYDNLgNRVRLVNLYGPTETTMIKLFYPIKpEDVHRESIPIGRPLPDTSVYLLDEQQQPVSGSEAGEICIATRYM 361
Cdd:PRK12583  332 EVMRRVMDEM-HMAEVQIAYGMTETSPVSLQTTAA-DDLERRVETVGRTQPHLEVKVVDPDGATVPRGEIGELCTRGYSV 409

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 517718121  362 THGYFpsSHPDQTAFIPDpcrdqsGEIMMYrTGDMGRWLPEGELALLGRKDNQVkIRG 419
Cdd:PRK12583  410 MKGYW--NNPEATAESID------EDGWMH-TGDLATMDEQGYVRIVGRSKDMI-IRG 457
PRK05857 PRK05857
fatty acid--CoA ligase;
25-440 3.26e-15

fatty acid--CoA ligase;


Pssm-ID: 180293 [Multi-domain]  Cd Length: 540  Bit Score: 80.44  E-value: 3.26e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   25 GQQTLSYKELDAESDRICELLHAHGAAQYDHIGILMQDRCASIAAVIGILKLGGVFVPLDPLHPDErlvtmldTAEVSCL 104
Cdd:PRK05857   38 GTSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLPIA-------AIERFCQ 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  105 LCDDAQFERAETLQ-GHEGKYFVLRARQAMSVQAGSKEAYS-HSAN-----------ATDPIYIYFTSGSTGKPKAVVGK 171
Cdd:PRK05857  111 ITDPAAALVAPGSKmASSAVPEALHSIPVIAVDIAAVTRESeHSLDaaslagnadqgSEDPLAMIFTSGTTGEPKAVLLA 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  172 NESLLHF--------MNWeASWLDLTDPMRVSQLTSIGFdavLRDIFVPICAGGtICIPESREiildPLRLVHWLEHSRV 243
Cdd:PRK05857  191 NRTFFAVpdilqkegLNW-VTWVVGETTYSPLPATHIGG---LWWILTCLMHGG-LCVTGGEN----TTSLLEILTTNAV 261

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  244 HVVHCTPSLF-RFINHLSLTADSYPDLRYVLLAGETIRPESLKnWYDNLGnrVRLVNLYGPTETTMIKLFYPIKPEDVHR 322
Cdd:PRK05857  262 ATTCLVPTLLsKLVSELKSANATVPSLRLVGYGGSRAIAADVR-FIEATG--VRTAQVYGLSETGCTALCLPTDDGSIVK 338

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  323 -ESIPIGRPLPDTSVYLLDEQ----QQPVSGSEA--GEICIATRYMTHGYFpsSHPDQTafipdpcrdqsGEIMM---YR 392
Cdd:PRK05857  339 iEAGAVGRPYPGVDVYLAATDgigpTAPGAGPSAsfGTLWIKSPANMLGYW--NNPERT-----------AEVLIdgwVN 405

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 517718121  393 TGDMGRWLPEGELALLGRKDNQVKIRGNRVELGDIEHRLTNMAGIREA 440
Cdd:PRK05857  406 TGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREA 453
23DHB-AMP_lg cd05920
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ...
 9-442 7.93e-15

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: 78.91  E-value: 7.93e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121    9 LARAFAAFPERKAIECGQQTLSYKELDAESDRICELLHAHGAAQYDHIGILMQDRCASIAAVIGILKLGGVFVPLDPLHP 88
Cdd:cd05920    21 LARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPVLALPSHR 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   89 DERLVTMLDTAEVSCLLCDDAqferaetlqgHEGKYFVLRARQAMSVQAgskeayshsanatDPIYIYFTSGSTGKPKAV 168
Cdd:cd05920   101 RSELSAFCAHAEAVAYIVPDR----------HAGFDHRALARELAESIP-------------EVALFLLSGGTTGTPKLI 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  169 VGKNESLLHFMNWEASWLDLTDPMRVSQLTSIGFDAVLR--DIFVPICAGGTICIPESReiilDPLRLVHWLEHSRVHVV 246
Cdd:cd05920   158 PRTHNDYAYNVRASAEVCGLDQDTVYLAVLPAAHNFPLAcpGVLGTLLAGGRVVLAPDP----SPDAAFPLIEREGVTVT 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  247 HCTPSLF-RFINHLSLTADSYPDLRYVLLAGETIRPESLKNWYDNLGNRVRLVnlYGPTETtMIKLFYPIKPEDV--HRE 323
Cdd:cd05920   234 ALVPALVsLWLDAAASRRADLSSLRLLQVGGARLSPALARRVPPVLGCTLQQV--FGMAEG-LLNYTRLDDPDEViiHTQ 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  324 sipiGRPL-PDTSVYLLDEQQQPVSGSEAGEIciATR--YMTHGYFPSSHPDQTAFIPDPcrdqsgeimMYRTGDMGRWL 400
Cdd:cd05920   311 ----GRPMsPDDEIRVVDEEGNPVPPGEEGEL--LTRgpYTIRGYYRAPEHNARAFTPDG---------FYRTGDLVRRT 375

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 517718121  401 PEGELALLGRKDNQVKIRGNRVELGDIEHRLTNMAGIREAVV 442
Cdd:cd05920   376 PDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAV 417
FACL_fum10p_like cd05926
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ...
 17-442 2.09e-14

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: 77.74  E-value: 2.09e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   17 PERKAIECGQQT--LSYKELDAESDRICELLHAHGAAQYDHIGILMQDRCASIAAVIGILKLGGVFVPLDPLHPDERLVT 94
Cdd:cd05926     1 PDAPALVVPGSTpaLTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   95 MLDTAEVSCLLCDD---------AQFERAETLQ-GHE--GKYFVLRARQAMSVQAGSKEAYSHS-ANATDPIYIYFTSGS 161
Cdd:cd05926    81 YLADLGSKLVLTPKgelgpasraASKLGLAILElALDvgVLIRAPSAESLSNLLADKKNAKSEGvPLPDDLALILHTSGT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  162 TGKPKAVVGKNESLLHFMNWEASWLDLTDPMR---VSQLTSI-GFDAVLrdiFVPICAGGTICIPESreiiLDPLRLVHW 237
Cdd:cd05926   161 TGRPKGVPLTHRNLAASATNITNTYKLTPDDRtlvVMPLFHVhGLVASL---LSTLAAGGSVVLPPR----FSASTFWPD 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  238 LEHSRVHVVHCTPSLFRFI--NHLSLTADSYPDLRYVLLAGETIRPESLKNWYDNLGnrVRLVNLYGPTETTMIKLFYPI 315
Cdd:cd05926   234 VRDYNATWYTAVPTIHQILlnRPEPNPESPPPKLRFIRSCSASLPPAVLEALEATFG--APVLEAYGMTEAAHQMTSNPL 311

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  316 KPEDVHRESIPIGRplpDTSVYLLDEQQQPVSGSEAGEICIATRYMTHGYFPSSHPDQTAFIPDPcrdqsgeimMYRTGD 395
Cdd:cd05926   312 PPGPRKPGSVGKPV---GVEVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDG---------WFRTGD 379

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*..
gi 517718121  396 MGRWLPEGELALLGRKDNQVKIRGNRVELGDIEHRLTNMAGIREAVV 442
Cdd:cd05926   380 LGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVA 426
FAAL cd05931
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ...
 9-429 2.96e-14

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: 77.28  E-value: 2.96e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121    9 LARAFAAFPERkaiecGQQTLSYKELDAESDRICELLHAHGAAQyDHIGILMQDRCASIAAVIGILKLGGVFVPL---DP 85
Cdd:cd05931    10 PAYTFLDDEGG-----REETLTYAELDRRARAIAARLQAVGKPG-DRVLLLAPPGLDFVAAFLGCLYAGAIAVPLpppTP 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   86 LHPDERLVTMLDTAEVSCLLCDDAqFERAETLQGHEGKYFVLRARQAMSVQAGSKEAYSH--SANATDPIYIYFTSGSTG 163
Cdd:cd05931    84 GRHAERLAAILADAGPRVVLTTAA-ALAAVRAFAASRPAAGTPRLLVVDLLPDTSAADWPppSPDPDDIAYLQYTSGSTG 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  164 KPKAVVGKNESLLH---------FMNWE---ASWLDLTDPMRVsqltsIGFdavlrdIFVPICAGGTICIPESREIILDP 231
Cdd:cd05931   163 TPKGVVVTHRNLLAnvrqirrayGLDPGdvvVSWLPLYHDMGL-----IGG------LLTPLYSGGPSVLMSPAAFLRRP 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  232 LRlvhWLEH-SRVHVVHcT--PSlFRFinhlSLTADSYPD----------LRYVLLAGETIRPESLKNWYDnlgnRVRLV 298
Cdd:cd05931   232 LR---WLRLiSRYRATI-SaaPN-FAY----DLCVRRVRDedlegldlssWRVALNGAEPVRPATLRRFAE----AFAPF 298

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  299 NL--------YGPTETTMI---------------------KLFYPIKPEDVH-RESIPIGRPLPDTSVYLLDEQ-QQPVS 347
Cdd:cd05931   299 GFrpeafrpsYGLAEATLFvsggppgtgpvvlrvdrdalaGRAVAVAADDPAaRELVSCGRPLPDQEVRIVDPEtGRELP 378

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  348 GSEAGEICIATRYMTHGYFpsSHPDQTAFIPDPCRDQSGEIMMyRTGDMGRwLPEGELALLGRKDNQVKIRGNRVELGDI 427
Cdd:cd05931   379 DGEVGEIWVRGPSVASGYW--GRPEATAETFGALAATDEGGWL-RTGDLGF-LHDGELYITGRLKDLIIVRGRNHYPQDI 454


                  ..
gi 517718121  428 EH 429
Cdd:cd05931   455 EA 456
PRK05605 PRK05605
long-chain-fatty-acid--CoA ligase; Validated
 2-449 8.36e-14

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


Pssm-ID: 235531 [Multi-domain]  Cd Length: 573  Bit Score: 76.19  E-value: 8.36e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121    2 DNTIQYELARAFAAFPERKAIECGQQTLSYKELDAESDRICELLHAHGAAQYDHIGILMQDRCASIAAVIGILKLGGVFV 81
Cdd:PRK05605   31 DTTLVDLYDNAVARFGDRPALDFFGATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVV 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   82 PLDPL-------HPDE----RLVTMLD-TAEVSCLLCDDAQFERAETLQGHEG----KYFVLR--------ARQAMSVQA 137
Cdd:PRK05605  111 EHNPLytaheleHPFEdhgaRVAIVWDkVAPTVERLRRTTPLETIVSVNMIAAmpllQRLALRlpipalrkARAALTGPA 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  138 ---------------GSKEAYSH-SANATDPIYIYFTSGSTGKPKAVVgknesLLHfMNWEA------SWL-DLTD---- 190
Cdd:PRK05605  191 pgtvpwetlvdaaigGDGSDVSHpRPTPDDVALILYTSGTTGKPKGAQ-----LTH-RNLFAnaaqgkAWVpGLGDgper 264

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  191 -----PM-RVSQLTSIGFDAVLrdifvpicAGGTICIPESREI--ILDPLRlvhwleHSRVHVVHCTPSLFRFI------ 256
Cdd:PRK05605  265 vlaalPMfHAYGLTLCLTLAVS--------IGGELVLLPAPDIdlILDAMK------KHPPTWLPGVPPLYEKIaeaaee 330

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  257 NHLSLTAdsypdLRYVLLAGETIRPESLKNWYDNLGNRvrLVNLYGPTETTMIKLFYPIKPedvHRESIPIGRPLPDTSV 336
Cdd:PRK05605  331 RGVDLSG-----VRNAFSGAMALPVSTVELWEKLTGGL--LVEGYGLTETSPIIVGNPMSD---DRRPGYVGVPFPDTEV 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  337 YL-----LDEQQQPvsgSEAGEICIATRYMTHGYFpsSHPDQTA--FIPDpcrdqsgeimMYRTGDMGRWLPEGELALLG 409
Cdd:PRK05605  401 RIvdpedPDETMPD---GEEGELLVRGPQVFKGYW--NRPEETAksFLDG----------WFRTGDVVVMEEDGFIRIVD 465

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|
gi 517718121  410 RKDNQVKIRGNRVELGDIEHRLTNMAGIREAVVRMRAKAD 449
Cdd:PRK05605  466 RIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPRED 505
OSB_MenE-like cd17630
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ...
 157-442 1.47e-13

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: 73.52  E-value: 1.47e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  157 FTSGSTGKPKAVV-----------GKNeSLLHFmNWEASWLDLTDPMRVSqltsiGFDAVLRDIFvpicAGGTICIPESR 225
Cdd:cd17630     7 LTSGSTGTPKAVVhtaanllasaaGLH-SRLGF-GGGDSWLLSLPLYHVG-----GLAILVRSLL----AGAELVLLERN 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  226 eiilDPLRLVHwlEHSRVHVVHCTPSLFRFINHLSLTADSYPDLRYVLLAGETIRPESLKNWYDNlgnRVRLVNLYGPTE 305
Cdd:cd17630    76 ----QALAEDL--APPGVTHVSLVPTQLQRLLDSGQGPAALKSLRAVLLGGAPIPPELLERAADR---GIPLYTTYGMTE 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  306 T-TMIKLfypiKPEDVHRESIpIGRPLPDTSVYLldeqqqpvsgSEAGEICIATRYMTHGYFpsshpdqTAFIPDPCRDQ 384
Cdd:cd17630   147 TaSQVAT----KRPDGFGRGG-VGVLLPGRELRI----------VEDGEIWVGGASLAMGYL-------RGQLVPEFNED 204

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 517718121  385 SgeimMYRTGDMGRWLPEGELALLGRKDNQVKIRGNRVELGDIEHRLTNMAGIREAVV 442
Cdd:cd17630   205 G----WFTTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFV 258
A_NRPS_Ta1_like cd12116
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ...
 788-846 1.93e-13

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: 74.64  E-value: 1.93e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517718121  788 EEAQEPLLIAYYLAD--KMIDDEQLSVYLRRFLPDYMIPARFIRLDKMPLTPNGKLDYNAL 846
Cdd:cd12116   410 EDGGDRRLVAYVVLKagAAPDAAALRAHLRATLPAYMVPSAFVRLDALPLTANGKLDRKAL 470
PRK13295 PRK13295
cyclohexanecarboxylate-CoA ligase; Reviewed
 2-419 4.77e-13

cyclohexanecarboxylate-CoA ligase; Reviewed


Pssm-ID: 171961 [Multi-domain]  Cd Length: 547  Bit Score: 73.55  E-value: 4.77e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121    2 DNTIQYELARAFAAFPERKAI-----ECGQ-QTLSYKELDAESDRICELLHAHGAAQYDHIGILMQDRCASIAAVIGILK 75
Cdd:PRK13295   23 DRTINDDLDACVASCPDKTAVtavrlGTGApRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSR 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   76 LGGVFVPLDPLHPDERLVTMLDTAEVSCLLC-------DDAQFerAETLQ------------GHEG-----KYFVLRAR- 130
Cdd:PRK13295  103 IGAVLNPLMPIFRERELSFMLKHAESKVLVVpktfrgfDHAAM--ARRLRpelpalrhvvvvGGDGadsfeALLITPAWe 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  131 QAMSVQAGSKeaySHSANATDPIYIYFTSGSTGKPKAVVGKNESLLHFMNWEASWLDLT--------DPMrvSQLTsiGF 202
Cdd:PRK13295  181 QEPDAPAILA---RLRPGPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGaddvilmaSPM--AHQT--GF 253

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  203 DAVLRdifVPICAGGTICIPEsreiILDPLRLVHWLEHSRV-HVVHCTPSLFRFINHLSLTADSYPDLRYVLLAGETIRP 281
Cdd:PRK13295  254 MYGLM---MPVMLGATAVLQD----IWDPARAAELIRTEGVtFTMASTPFLTDLTRAVKESGRPVSSLRTFLCAGAPIPG 326

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  282 ESLKNWYDNLGNRVrlVNLYGPTETTMIKLFYPIKPEDVHRESipIGRPLPDTSVYLLDEQQQPVSGSEAGEICIATRYM 361
Cdd:PRK13295  327 ALVERARAALGAKI--VSAWGMTENGAVTLTKLDDPDERASTT--DGCPLPGVEVRVVDADGAPLPAGQIGRLQVRGCSN 402

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 517718121  362 THGYFpsSHPDQTAfipdpcRDQSGeimMYRTGDMGRWLPEGELALLGR-KDnqVKIRG 419
Cdd:PRK13295  403 FGGYL--KRPQLNG------TDADG---WFDTGDLARIDADGYIRISGRsKD--VIIRG 448
PRK08751 PRK08751
long-chain fatty acid--CoA ligase;
4-439 7.20e-13

long-chain fatty acid--CoA ligase;


Pssm-ID: 181546 [Multi-domain]  Cd Length: 560  Bit Score: 72.99  E-value: 7.20e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121    4 TIQYELARAFAAFPERKAIECGQQTLSYKELDAESDRICE-LLHAHGAAQYDHIGILMQDRCASIAAVIGILKLGGVFVP 82
Cdd:PRK08751   26 TVAEVFATSVAKFADRPAYHSFGKTITYREADQLVEQFAAyLLGELQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVN 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   83 LDPLHPDERLVTMLDTAEVSCLL-----CDDAQFERAET------------LQGHEGKYFV------------------- 126
Cdd:PRK08751  106 VNPLYTPRELKHQLIDSGASVLVvidnfGTTVQQVIADTpvkqvittglgdMLGFPKAALVnfvvkyvkklvpeyringa 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  127 LRARQAMSVqaGSKEAYSHSANATDPI-YIYFTSGSTGKPKAVVGKNESLLHFMNWEASWLDLTDPMRVSQLTSIgfDAV 205
Cdd:PRK08751  186 IRFREALAL--GRKHSMPTLQIEPDDIaFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQWLAGTGKLEEGCEVVI--TAL 261

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  206 -LRDIFVpICAGGTIC--IPESREIILDPLRL---VHWLEHSRVHVVHCTPSLFR-FINHLSLTADSYPDLRYVLLAGET 278
Cdd:PRK08751  262 pLYHIFA-LTANGLVFmkIGGCNHLISNPRDMpgfVKELKKTRFTAFTGVNTLFNgLLNTPGFDQIDFSSLKMTLGGGMA 340

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  279 IRPESLKNWYDNLGnrVRLVNLYGPTETTMIKLfypIKPEDVHRESIPIGRPLPDTSVYLLDEQQQPVSGSEAGEICIAT 358
Cdd:PRK08751  341 VQRSVAERWKQVTG--LTLVEAYGLTETSPAAC---INPLTLKEYNGSIGLPIPSTDACIKDDAGTVLAIGEIGELCIKG 415

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  359 RYMTHGYFpsSHPDQTAFIpdpcRDQSGeimMYRTGDMGRWLPEGELALLGRKDNQVKIRGNRVELGDIEHRLTNMAGIR 438
Cdd:PRK08751  416 PQVMKGYW--KRPEETAKV----MDADG---WLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVL 486


                  .
gi 517718121  439 E 439
Cdd:PRK08751  487 E 487
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
 861-935 7.27e-13

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: 65.26  E-value: 7.27e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517718121  861 APNSSTELKLLDIWTHILGIK--RISADDHFLQ-IGVHSLNIMTLIAQVYENFQVELPLEQVFEHDTLEEIAAYIDEQ 935
Cdd:COG0236     1 MPREELEERLAEIIAEVLGVDpeEITPDDSFFEdLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLEEK 78
A_NRPS_PvdJ-like cd17649
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ...
 792-847 7.85e-13

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: 72.40  E-value: 7.85e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  792 EPLLIAYY-LADKMI---DDEQLSVYLRRFLPDYMIPARFIRLDKMPLTPNGKLDYNALP 847
Cdd:cd17649   391 GKQLVAYVvLRAAAAqpeLRAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLDRKALP 450
A_NRPS_ProA cd17656
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ...
 788-847 1.10e-12

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: 72.12  E-value: 1.10e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  788 EEAQEPLLIAYYLADKMIDDEQLSVYLRRFLPDYMIPARFIRLDKMPLTPNGKLDYNALP 847
Cdd:cd17656   420 DDKGEKYLCAYFVMEQELNISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKALP 479
ABCL cd05958
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ...
 19-442 1.14e-12

2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.


Pssm-ID: 341268 [Multi-domain]  Cd Length: 439  Bit Score: 71.74  E-value: 1.14e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   19 RKAIECGQQTLSYKELDAESDRICELLHAHGAAQYDH-IGILMQDRCASIAAVIGILKLGGVFVPLDPLHPDERLVTMLD 97
Cdd:cd05958     1 RTCLRSPEREWTYRDLLALANRIANVLVGELGIVPGNrVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   98 TAEVSCLLCDDAQferaetlqghegkyfvlrarqamsvqagskeayshsaNATDPIYIY-FTSGSTGKPKAVVGKNESLL 176
Cdd:cd05958    81 KARITVALCAHAL-------------------------------------TASDDICILaFTSGTTGAPKATMHFHRDPL 123

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  177 H-FMNWEASWLDLTDPMRVSQLTSI----GFDAVLrdIFVPICAGGTICIPESreiilDPLRLVHWLEHSRVHVVHCTPS 251
Cdd:cd05958   124 AsADRYAVNVLRLREDDRFVGSPPLaftfGLGGVL--LFPFGVGASGVLLEEA-----TPDLLLSAIARYKPTVLFTAPT 196

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  252 LFRFInhLSLTADSYPD---LRYVLLAGETIRPESLKNWYDNLGnrVRLVNLYGPTEttMIKLFYPIKPEDVHRESipIG 328
Cdd:cd05958   197 AYRAM--LAHPDAAGPDlssLRKCVSAGEALPAALHRAWKEATG--IPIIDGIGSTE--MFHIFISARPGDARPGA--TG 268

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  329 RPLPDTSVYLLDEQQQPVSGSEAGEICIATRYMTHGYFPSSHpdQTAFipdpcrdQSGEIMmyrTGDMGRWLPEGELALL 408
Cdd:cd05958   269 KPVPGYEAKVVDDEGNPVPDGTIGRLAVRGPTGCRYLADKRQ--RTYV-------QGGWNI---TGDTYSRDPDGYFRHQ 336

                         410       420       430
                  ....*....|....*....|....*....|....*
gi 517718121  409 GRKDNQVKIRGNRVELGDIEHRLTNMAGIRE-AVV 442
Cdd:cd05958   337 GRSDDMIVSGGYNIAPPEVEDVLLQHPAVAEcAVV 371
LC_FACS_like cd05935
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ...
 29-442 1.32e-12

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: 71.74  E-value: 1.32e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   29 LSYKELDAESDRICELLHAHGAAQYDHIGILMQDRCASIAAVIGILKLGGVFVPLDPlhpderlvtMLDTAEVSCLLCDd 108
Cdd:cd05935     2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINP---------MLKERELEYILND- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  109 aqferaetlqghegkyfvlrarqamsvqAGSKEAYSHSaNATDPIYIYFTSGSTGKPKAVVGKNESLLHFMNWEASWLDL 188
Cdd:cd05935    72 ----------------------------SGAKVAVVGS-ELDDLALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGL 122

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  189 TdPMRVSQLT-----SIGFDAVLRdifVPICAGGTICIPE--SREIILDPLRlvhwlEHSRVHVVHCTPSLFRFINHLSL 261
Cdd:cd05935   123 T-PSDVILAClplfhVTGFVGSLN---TAVYVGGTYVLMArwDRETALELIE-----KYKVTFWTNIPTMLVDLLATPEF 193

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  262 TADSYPDLRYVLLAGETIRPESLKNWYDNLGnrVRLVNLYGPTET-TMIKLFYPIKPedvhrESIPIGRPLPDTSVYLLD 340
Cdd:cd05935   194 KTRDLSSLKVLTGGGAPMPPAVAEKLLKLTG--LRFVEGYGLTETmSQTHTNPPLRP-----KLQCLGIP*FGVDARVID 266

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  341 -EQQQPVSGSEAGEICIATRYMTHGYFPSSHPDQTAFIPDPCRDqsgeimMYRTGDMGRWLPEGELALLGRKDNQVKIRG 419
Cdd:cd05935   267 iETGRELPPNEVGEIVVRGPQIFKGYWNRPEETEESFIEIKGRR------FFRTGDLGYMDEEGYFFFVDRVKRMINVSG 340

                         410       420
                  ....*....|....*....|...
gi 517718121  420 NRVELGDIEHRLTNMAGIREAVV 442
Cdd:cd05935   341 FKVWPAEVEAKLYKHPAI*EVCV 363
PRK06164 PRK06164
acyl-CoA synthetase; Validated
 14-442 2.34e-12

acyl-CoA synthetase; Validated


Pssm-ID: 235722 [Multi-domain]  Cd Length: 540  Bit Score: 71.31  E-value: 2.34e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   14 AAFPERKAIECGQQTLSYKELDAESDRICELLHAHGAAQYDHIGILMQDRCASIAAVIGILKLGGVFVPLDplhpderlv 93
Cdd:PRK06164   21 RARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVN--------- 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   94 TMLDTAEVSCLL----------------------CDDAQFERAETLQGhegkYFVL-------------RARQAMSV--Q 136
Cdd:PRK06164   92 TRYRSHEVAHILgrgrarwlvvwpgfkgidfaaiLAAVPPDALPPLRA----IAVVddaadatpapapgARVQLFALpdP 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  137 AGSKEAYSHSANATDPIYIYFTSGSTGKPKAVVGKNESLLHFMNWEASWLDLTDPMRVsqLTSIGFDAV--LRDIFVPIC 214
Cdd:PRK06164  168 APPAAAGERAADPDAGALLFTTSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVL--LAALPFCGVfgFSTLLGALA 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  215 AGGTI-CIPesreiILDPLRLVHWLEHSRVHVVHCTPSLFRFINHLSLTADSYPDLRYVLLAGETIRPESLKNWYDNLGn 293
Cdd:PRK06164  246 GGAPLvCEP-----VFDAARTARALRRHRVTHTFGNDEMLRRILDTAGERADFPSARLFGFASFAPALGELAALARARG- 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  294 rVRLVNLYGPTETTMIKLFYPIKPEDVHReSIPIGRPL-PDTSVYLLDEQQQPV-SGSEAGEICIATRYMTHGYFpsSHP 371
Cdd:PRK06164  320 -VPLTGLYGSSEVQALVALQPATDPVSVR-IEGGGRPAsPEARVRARDPQDGALlPDGESGEIEIRAPSLMRGYL--DNP 395

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517718121  372 DQT--AFIPDPcrdqsgeimMYRTGDMGRWLPEGELALLGRKDNQVKIRGNRVELGDIEHRLTNMAGIREAVV 442
Cdd:PRK06164  396 DATarALTDDG---------YFRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQV 459
A_NRPS_VisG_like cd17651
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ...
 792-847 5.50e-12

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: 70.07  E-value: 5.50e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 517718121  792 EPLLIAYYLADKMIDD--EQLSVYLRRFLPDYMIPARFIRLDKMPLTPNGKLDYNALP 847
Cdd:cd17651   434 EKRLVAYVVGDPEAPVdaAELRAALATHLPEYMVPSAFVLLDALPLTPNGKLDRRALP 491
PRK07788 PRK07788
acyl-CoA synthetase; Validated
 12-446 6.02e-12

acyl-CoA synthetase; Validated


Pssm-ID: 236097 [Multi-domain]  Cd Length: 549  Bit Score: 69.96  E-value: 6.02e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   12 AFAAF--PERKAI--ECGqqTLSYKELDAESDRICELLHAHGAAQYDHIGILMQDRCASIAAVIGILKLGGVFVPLDPLH 87
Cdd:PRK07788   56 AHAARraPDRAALidERG--TLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGF 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   88 PDERLVTMLDTAEVSCLLCDDAQFERAETLQGHEGKYFVLRA-RQAMSVQAGSKEAYSHSANATDPI----------YIY 156
Cdd:PRK07788  134 SGPQLAEVAAREGVKALVYDDEFTDLLSALPPDLGRLRAWGGnPDDDEPSGSTDETLDDLIAGSSTAplpkppkpggIVI 213

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  157 FTSGSTGKPKAVVGKNESLLhfmnweASWLDLTD--PMRVSQLTSIG---FDAVLRDIFVPICA-GGTICIPEsreiILD 230
Cdd:PRK07788  214 LTSGTTGTPKGAPRPEPSPL------APLAGLLSrvPFRAGETTLLPapmFHATGWAHLTLAMAlGSTVVLRR----RFD 283

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  231 PLRLVHWLEHSRVHVVHCTPSLFRFINHLSLTADSYPD---LRYVLLAGETIRPESLKNWYDNLGNRvrLVNLYGPTETT 307
Cdd:PRK07788  284 PEATLEDIAKHKATALVVVPVMLSRILDLGPEVLAKYDtssLKIIFVSGSALSPELATRALEAFGPV--LYNLYGSTEVA 361

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  308 miklFYPI-KPEDVHRESIPIGRPLPDTSVYLLDEQQQPVSGSEAGEICIATRYMTHGYFPSSHPDqtafIPDpcrdqsG 386
Cdd:PRK07788  362 ----FATIaTPEDLAEAPGTVGRPPKGVTVKILDENGNEVPRGVVGRIFVGNGFPFEGYTDGRDKQ----IID------G 427

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  387 eimMYRTGDMGRWLPEGELALLGRKDNQVKIRGNRVELGDIEHRLTNMAGIREAVV----------RMRA 446
Cdd:PRK07788  428 ---LLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVigvddeefgqRLRA 494
PRK06334 PRK06334
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
 29-440 6.83e-12

long chain fatty acid--[acyl-carrier-protein] ligase; Validated


Pssm-ID: 180533 [Multi-domain]  Cd Length: 539  Bit Score: 69.84  E-value: 6.83e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   29 LSYKELdaeSDRICELlhAHGAAQY--DHIGILMQDRCASIAAVIGILKLGGVFVPLDPLHPDERLVTMLDTAEVSCLLC 106
Cdd:PRK06334   46 LSYNQV---RKAVIAL--ATKVSKYpdQHIGIMMPASAGAYIAYFATLLSGKIPVMINWSQGLREVTACANLVGVTHVLT 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  107 DDAQFERAETLQGHEGKY-----FVLRARQAMSVQAGSKEAY--------------SHSANATDPIYIYFTSGSTGKPKA 167
Cdd:PRK06334  121 SKQLMQHLAQTHGEDAEYpfsliYMEEVRKELSFWEKCRIGIymsipfewlmrwfgVSDKDPEDVAVILFTSGTEKLPKG 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  168 VVGKNESLLHfmNWEASwLDLTDPMRVSQLTSI-------GFDAVlrdIFVPICAGgtICIPESREIiLDPLRLVHWLEH 240
Cdd:PRK06334  201 VPLTHANLLA--NQRAC-LKFFSPKEDDVMMSFlppfhayGFNSC---TLFPLLSG--VPVVFAYNP-LYPKKIVEMIDE 271

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  241 SRVHVVHCTPSLFRFI-NHLSLTADSYPDLRYVLLAGETIRpESLKNWYDNLGNRVRLVNLYGPTETTMIklfYPIKPED 319
Cdd:PRK06334  272 AKVTFLGSTPVFFDYIlKTAKKQESCLPSLRFVVIGGDAFK-DSLYQEALKTFPHIQLRQGYGTTECSPV---ITINTVN 347

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  320 VHRESIPIGRPLPDTSVYLLDEQQQ-PVSGSEAGEICIATRYMTHGYFpSSHPDQtAFIpdpcrdQSGEIMMYRTGDMGR 398
Cdd:PRK06334  348 SPKHESCVGMPIRGMDVLIVSEETKvPVSSGETGLVLTRGTSLFSGYL-GEDFGQ-GFV------ELGGETWYVTGDLGY 419

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|..
gi 517718121  399 WLPEGELALLGRKDNQVKIRGNRVELGDIEHRLTNMAGIREA 440
Cdd:PRK06334  420 VDRHGELFLKGRLSRFVKIGAEMVSLEALESILMEGFGQNAA 461
LC_FACS_like cd17640
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ...
 27-442 7.48e-12

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: 69.31  E-value: 7.48e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   27 QTLSYKELDAESDRICELLHAHGAAQYDHIGILMQDRCASIAAVIGILKLGGVFVPLDPLHPDERLVTMLDTAEVSCLLc 106
Cdd:cd17640     4 KRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALV- 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  107 ddaqferaetlqghegkyfvlrarqamsVQAGSKEAyshsanATdpiyIYFTSGSTGKPKAVVGKNESLLHfmnweaswl 186
Cdd:cd17640    83 ----------------------------VENDSDDL------AT----IIYTSGTTGNPKGVMLTHANLLH--------- 115

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  187 dltdpmRVSQLTSIgFDAVLRDIFVPIC---------------AGGTICIPESREIILDPLRLVhwlehsRVHVVHCTPS 251
Cdd:cd17640   116 ------QIRSLSDI-VPPQPGDRFLSILpiwhsyersaeyfifACGCSQAYTSIRTLKDDLKRV------KPHYIVSVPR 182

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  252 LF---------------RFINHLSLTADSYPDLRYVLLAGETIrPESLKNWYDNLGnrVRLVNLYGPTETTmiklfyPIK 316
Cdd:cd17640   183 LWeslysgiqkqvskssPIKQFLFLFFLSGGIFKFGISGGGAL-PPHVDTFFEAIG--IEVLNGYGLTETS------PVV 253

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  317 PEDVHRESI--PIGRPLPDTSVYLLDEQ-QQPVSGSEAGEICIATRYMTHGYFpsSHPDQTAFIpdpcRDQSGeimMYRT 393
Cdd:cd17640   254 SARRLKCNVrgSVGRPLPGTEIKIVDPEgNVVLPPGEKGIVWVRGPQVMKGYY--KNPEATSKV----LDSDG---WFNT 324

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 517718121  394 GDMGRWLPEGELALLGR-KDNQVKIRGNRVELGDIEHRLTNMAGIREAVV 442
Cdd:cd17640   325 GDLGWLTCGGELVLTGRaKDTIVLSNGENVEPQPIEEALMRSPFIEQIMV 374
FadD3 cd17638
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ...
 155-442 9.58e-12

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: 67.91  E-value: 9.58e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  155 IYFTSGSTGKPKAVVGKN-ESLLHFMNWeASWLDLTDPMRVSQLT----SIGFDAvlrDIFVPICAGGTIcIPESreiIL 229
Cdd:cd17638     5 IMFTSGTTGRSKGVMCAHrQTLRAAAAW-ADCADLTEDDRYLIINpffhTFGYKA---GIVACLLTGATV-VPVA---VF 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  230 DPLRLVHWLEHSRVHVVHCTPSLFR-FINHLSLTADSYPDLRYVLLAGETIRPESLKNWYDNLGNRVRLVNlYGPTETTM 308
Cdd:cd17638    77 DVDAILEAIERERITVLPGPPTLFQsLLDHPGRKKFDLSSLRAAVTGAATVPVELVRRMRSELGFETVLTA-YGLTEAGV 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  309 IKLFYPikPEDVHRESIPIGRPLPDTSVYLLDeqqqpvsgseAGEICIATRYMTHGYFpsSHPDQTAfipdPCRDQSGEI 388
Cdd:cd17638   156 ATMCRP--GDDAETVATTCGRACPGFEVRIAD----------DGEVLVRGYNVMQGYL--DDPEATA----EAIDADGWL 217

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 517718121  389 mmyRTGDMGRWLPEGELALLGRKDNQVKIRGNRVELGDIEHRLTNMAGIREAVV 442
Cdd:cd17638   218 ---HTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAV 268
PRK08279 PRK08279
long-chain-acyl-CoA synthetase; Validated
 9-189 1.06e-11

long-chain-acyl-CoA synthetase; Validated


Pssm-ID: 236217 [Multi-domain]  Cd Length: 600  Bit Score: 69.52  E-value: 1.06e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121    9 LARAFAAFPERKAIECGQQTLSYKELDAESDRICELLHAHGAAQYDHIGILMQDRCASIAAVIGILKLGGVFVPLDPLHP 88
Cdd:PRK08279   43 FEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVALLNTQQR 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   89 DERLVTMLDTAEVSCLLCDDAQFERAETLQGH---EGKYFVLRARQAMSVQA-GSKEAYSHSANATDP------------ 152
Cdd:PRK08279  123 GAVLAHSLNLVDAKHLIVGEELVEAFEEARADlarPPRLWVAGGDTLDDPEGyEDLAAAAAGAPTTNPasrsgvtakdta 202

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 517718121  153 IYIYfTSGSTGKPKAVVGKNESLLHFMNWEASWLDLT 189
Cdd:PRK08279  203 FYIY-TSGTTGLPKAAVMSHMRWLKAMGGFGGLLRLT 238
A_NRPS_AB3403-like cd17646
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ...
 783-846 1.12e-11

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: 68.84  E-value: 1.12e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517718121  783 VQLQVEEAQEPLLIAYYLADKM---IDDEQLSVYLRRFLPDYMIPARFIRLDKMPLTPNGKLDYNAL 846
Cdd:cd17646   422 VVARAAPAGAARLVGYVVPAAGaagPDTAALRAHLAERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
A_NRPS_PpsD_like cd17650
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ...
 783-846 1.82e-11

similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341305 [Multi-domain]  Cd Length: 447  Bit Score: 68.26  E-value: 1.82e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517718121  783 VQLQVEEAQEPLLIAYYLADKMIDDEQLSVYLRRFLPDYMIPARFIRLDKMPLTPNGKLDYNAL 846
Cdd:cd17650   384 VAVREDKGGEARLCAYVVAAATLNTAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
 869-927 1.99e-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: 60.65  E-value: 1.99e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517718121   869 KLLDIWTHILGI--KRISADDHFLQIGVHSLNIMTLIAQVYENFQVELPLEQVFEHDTLEE 927
Cdd:pfam00550    2 RLRELLAEVLGVpaEEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLAE 62
A_NRPS_Cytc1-like cd17643
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ...
 795-846 2.00e-11

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: 68.10  E-value: 2.00e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 517718121  795 LIAYYLAD--KMIDDEQLSVYLRRFLPDYMIPARFIRLDKMPLTPNGKLDYNAL 846
Cdd:cd17643   397 LVAYVVADdgAAADIAELRALLKELLPDYMVPARYVPLDALPLTVNGKLDRAAL 450
A_NRPS_LgrA-like cd17645
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ...
 792-847 2.60e-11

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: 67.58  E-value: 2.60e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 517718121  792 EPLLIAYYLADKMIDDEQLSVYLRRFLPDYMIPARFIRLDKMPLTPNGKLDYNALP 847
Cdd:cd17645   385 RKYLVAYVTAPEEIPHEELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKALP 440
EntE COG1021
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ...
 2-419 3.06e-11

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: 67.86  E-value: 3.06e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121    2 DNTIQYELARAFAAFPERKAIECGQQTLSYKELDAESDRICELLHAHGAAQYDHIGILMQDRCASIAAVIGILKLGGVFV 81
Cdd:COG1021    24 GETLGDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAIPV 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   82 PLDPLHPDERLVTMLDTAEVSCLLCDDAQ--F---ERAETLQ-GHEG-KYFVL--RARQAMSVQAGSKEAYSHSANATDP 152
Cdd:COG1021   104 FALPAHRRAEISHFAEQSEAVAYIIPDRHrgFdyrALARELQaEVPSlRHVLVvgDAGEFTSLDALLAAPADLSEPRPDP 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  153 IYIYF---TSGSTGKPKavvgkneslL----H---FMNWEASwldlTDPMRVSQ---------------LTSIGFDAVLr 207
Cdd:COG1021   184 DDVAFfqlSGGTTGLPK---------LiprtHddyLYSVRAS----AEICGLDAdtvylaalpaahnfpLSSPGVLGVL- 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  208 difvpiCAGGTICIPESreiiLDPLRLVHWLEHSRVHVVHCTPSLF-RFINHLSLTADSYPDLRYVLLAG--------ET 278
Cdd:COG1021   250 ------YAGGTVVLAPD----PSPDTAFPLIERERVTVTALVPPLAlLWLDAAERSRYDLSSLRVLQVGGaklspelaRR 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  279 IRPEslknwydnLGnrVRLVNLYGPTE----TTMIKlfypiKPEDVHRESIpiGRPL-PDTSVYLLDEQQQPVSGSEAGE 353
Cdd:COG1021   320 VRPA--------LG--CTLQQVFGMAEglvnYTRLD-----DPEEVILTTQ--GRPIsPDDEVRIVDEDGNPVPPGEVGE 382

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517718121  354 ICiaTR--YMTHGYFPSSHPDQTAFIPDpcrdqsGeimMYRTGDMGRWLPEGELALLGRKDNQVkIRG 419
Cdd:COG1021   383 LL--TRgpYTIRGYYRAPEHNARAFTPD------G---FYRTGDLVRRTPDGYLVVEGRAKDQI-NRG 438
PRK07786 PRK07786
long-chain-fatty-acid--CoA ligase; Validated
 8-446 6.25e-11

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


Pssm-ID: 169098 [Multi-domain]  Cd Length: 542  Bit Score: 66.72  E-value: 6.25e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121    8 ELARAFAAFPERKAIECGQQTLSYKELDAESDRICELLHAHGAAQYDHIGILMQDRCASIAAVIGILKLGGVFVPLD-PL 86
Cdd:PRK07786   22 QLARHALMQPDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNfRL 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   87 HPDE-----------RLVTMLDTAEVSCLLCDDAQFERAETLQGHEGKYFVLRARQAMSvQAGSKEAYSHSANATdPIYI 155
Cdd:PRK07786  102 TPPEiaflvsdcgahVVVTEAALAPVATAVRDIVPLLSTVVVAGGSSDDSVLGYEDLLA-EAGPAHAPVDIPNDS-PALI 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  156 YFTSGSTGKPKAVVgknesLLHfMNWEASWLDLTDPMRVSQLTSIGFDAV-------LRDIFVPICAGGTICI-PESrei 227
Cdd:PRK07786  180 MYTSGTTGRPKGAV-----LTH-ANLTGQAMTCLRTNGADINSDVGFVGVplfhiagIGSMLPGLLLGAPTVIyPLG--- 250

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  228 ILDPLRLVHWLEHSRVHVVHCTPSLFRFInhlsltadsypdlryvlLAGETIRPESLK----NW-----YDNLGNRV--- 295
Cdd:PRK07786  251 AFDPGQLLDVLEAEKVTGIFLVPAQWQAV-----------------CAEQQARPRDLAlrvlSWgaapaSDTLLRQMaat 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  296 ----RLVNLYGPTETTMIKLFypIKPEDVHRESIPIGRPLPDTSVYLLDEQQQPVSGSEAGEICIATRYMTHGYFpsSHP 371
Cdd:PRK07786  314 fpeaQILAAFGQTEMSPVTCM--LLGEDAIRKLGSVGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYW--NNP 389

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 517718121  372 DQTAfipdpcrdQSGEIMMYRTGDMGRWLPEGELALLGRKDNQVKIRGNRVELGDIEHRLTNMAGIREAVVRMRA 446
Cdd:PRK07786  390 EATA--------EAFAGGWFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRA 456
PRK09029 PRK09029
O-succinylbenzoic acid--CoA ligase; Provisional
 16-414 7.11e-11

O-succinylbenzoic acid--CoA ligase; Provisional


Pssm-ID: 236363 [Multi-domain]  Cd Length: 458  Bit Score: 66.43  E-value: 7.11e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   16 FPERKAIECGQQTLSYKELDAESDRICELLHAHGAAQ--------YDHIGILmqdrCASIAAvigiLKLGGVFVPLDPLH 87
Cdd:PRK09029   16 RPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEgsgvalrgKNSPETL----LAYLAL----LQCGARVLPLNPQL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   88 PDERLVTMLDTAEVSCLLCDDaqferaetlqgHEGKYFVLRARQAMSVQAGSKEAYSHSANATdpiyIYFTSGSTGKPKA 167
Cdd:PRK09029   88 PQPLLEELLPSLTLDFALVLE-----------GENTFSALTSLHLQLVEGAHAVAWQPQRLAT----MTLTSGSTGLPKA 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  168 VV-------GKNESLLHFMNWEA--SWLdLTDPM-RVSqltsiGFDAVLRDIFvpicAGGTICIPESreiildplrlvHW 237
Cdd:PRK09029  153 AVhtaqahlASAEGVLSLMPFTAqdSWL-LSLPLfHVS-----GQGIVWRWLY----AGATLVVRDK-----------QP 211

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  238 LEHSRVHVVHCT--PS-LFRFINHLSLTAdsypDLRYVLLAGETIrPESL---------KNWydnLGnrvrlvnlYGPTE 305
Cdd:PRK09029  212 LEQALAGCTHASlvPTqLWRLLDNRSEPL----SLKAVLLGGAAI-PVELteqaeqqgiRCW---CG--------YGLTE 275

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  306 ---TTMIKLFypikpedvhrESIP-IGRPLPDTSVYLLDeqqqpvsgseaGEICIATRYMTHGYFpsshpdqtafipdpc 381
Cdd:PRK09029  276 masTVCAKRA----------DGLAgVGSPLPGREVKLVD-----------GEIWLRGASLALGYW--------------- 319

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|
gi 517718121  382 rdQSGEIM-------MYRTGDMGRWLpEGELALLGRKDNQ 414
Cdd:PRK09029  320 --RQGQLVplvndegWFATRDRGEWQ-NGELTILGRLDNL 356
caiC PRK08008
putative crotonobetaine/carnitine-CoA ligase; Validated
 27-442 7.28e-11

putative crotonobetaine/carnitine-CoA ligase; Validated


Pssm-ID: 181195 [Multi-domain]  Cd Length: 517  Bit Score: 66.63  E-value: 7.28e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   27 QTLSYKELDAESDRICELLHAHGAAQYDHIGILMqDRCAS-IAAVIGILKLGGVFVPLDPLHPDERLVTMLDTAEVSCLL 105
Cdd:PRK08008   36 RRYSYLELNEEINRTANLFYSLGIRKGDKVALHL-DNCPEfIFCWFGLAKIGAIMVPINARLLREESAWILQNSQASLLV 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  106 CDDA--------QFERAETLQGhegkyfVLRARQAMSVQAGSKEAYSHSA------------NATDPIYIYFTSGSTGKP 165
Cdd:PRK08008  115 TSAQfypmyrqiQQEDATPLRH------ICLTRVALPADDGVSSFTQLKAqqpatlcyapplSTDDTAEILFTSGTTSRP 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  166 KAVVGKNESLL---HFMNWEASWLDltDPMRVSQLTSIGFDAVLRDIFVPICAGGTICIPE--SREIILDPLRLVhwleh 240
Cdd:PRK08008  189 KGVVITHYNLRfagYYSAWQCALRD--DDVYLTVMPAFHIDCQCTAAMAAFSAGATFVLLEkySARAFWGQVCKY----- 261

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  241 sRVHVVHCTPSLFRFINHLSLTA-DSYPDLRYVLlagetirpeslknWYDNLGNR----------VRLVNLYGPTETtmi 309
Cdd:PRK08008  262 -RATITECIPMMIRTLMVQPPSAnDRQHCLREVM-------------FYLNLSDQekdafeerfgVRLLTSYGMTET--- 324

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  310 kLFYPI--KPEDvHRESIPIGRPLPDTSVYLLDEQQQPVSGSEAGEICI---ATRYMTHGYFpsSHPDQTAfipdpcRDQ 384
Cdd:PRK08008  325 -IVGIIgdRPGD-KRRWPSIGRPGFCYEAEIRDDHNRPLPAGEIGEICIkgvPGKTIFKEYY--LDPKATA------KVL 394

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 517718121  385 SGEIMMYrTGDMGRWLPEGELALLGRKDNQVKIRGNRVELGDIEHRLTNMAGIREAVV 442
Cdd:PRK08008  395 EADGWLH-TGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVV 451
A_NRPS_ACVS-like cd17648
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ...
 795-847 1.06e-10

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: 65.50  E-value: 1.06e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 517718121  795 LIAYYLADK-MIDDEQLSVYLRRFLPDYMIPARFIRLDKMPLTPNGKLDYNALP 847
Cdd:cd17648   400 LVGYYLPEPgHVPESDLLSFLRAKLPRYMVPARLVRLEGIPVTINGKLDVRALP 453
A_NRPS_CmdD_like cd17652
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ...
 795-847 1.50e-10

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: 64.97  E-value: 1.50e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 517718121  795 LIAYYLA--DKMIDDEQLSVYLRRFLPDYMIPARFIRLDKMPLTPNGKLDYNALP 847
Cdd:cd17652   382 LVAYVVPapGAAPTAAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRALP 436
A_NRPS_ApnA-like cd17644
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ...
 795-847 7.06e-10

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: 63.22  E-value: 7.06e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 517718121  795 LIAYYLADK--MIDDEQLSVYLRRFLPDYMIPARFIRLDKMPLTPNGKLDYNALP 847
Cdd:cd17644   411 LVAYIVPHYeeSPSTVELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDRRALP 465
A_NRPS_Sfm_like cd12115
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ...
 783-846 7.08e-10

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: 63.11  E-value: 7.08e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517718121  783 VQLQVEEAQEPLLIAYYLAD--KMIDDEQLSVYLRRFLPDYMIPARFIRLDKMPLTPNGKLDYNAL 846
Cdd:cd12115   382 VVAIGDAAGERRLVAYIVAEpgAAGLVEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
LC_FACL_like cd05914
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ...
 25-442 9.55e-10

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: 62.84  E-value: 9.55e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   25 GQQTLSYKELDAESDRICELLHAHGAAQYDHIGILMQDRCASIAAVIGILKLGGVFVPLDP-LHPDErLVTMLDTAEVSC 103
Cdd:cd05914     4 GGEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAeFTADE-VHHILNHSEAKA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  104 LLCDDAQferaetlqghegkyfvlrarqamsvqagskeayshsanatDPIYIYFTSGSTGKPKAVVGKNESLLhfmnWEA 183
Cdd:cd05914    83 IFVSDED----------------------------------------DVALINYTSGTTGNSKGVMLTYRNIV----SNV 118

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  184 SWLDLTDPMR-----VSQLTSIGFDAVLRDIFVPICAGGTIC----IPESREIILDPLRLVHWLEHSRVHVVhctpsLFR 254
Cdd:cd05914   119 DGVKEVVLLGkgdkiLSILPLHHIYPLTFTLLLPLLNGAHVVfldkIPSAKIIALAFAQVTPTLGVPVPLVI-----EKI 193

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  255 FINHL--SLTADSYPDLRYVLLAGETIRPESLKNWYDNLGNRVRL-------VNL----------------YGPTETTMI 309
Cdd:cd05914   194 FKMDIipKLTLKKFKFKLAKKINNRKIRKLAFKKVHEAFGGNIKEfviggakINPdveeflrtigfpytigYGMTETAPI 273

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  310 KLFYPikPEDVHRESIpiGRPLPDTSVYLLDeqqqPVSGSEAGEICIATRYMTHGYFPSSHPDQTAFIPDPcrdqsgeim 389
Cdd:cd05914   274 ISYSP--PNRIRLGSA--GKVIDGVEVRIDS----PDPATGEGEIIVRGPNVMKGYYKNPEATAEAFDKDG--------- 336

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 517718121  390 MYRTGDMGRWLPEGELALLGRKDNQ-VKIRGNRVELGDIEHRLTNMAGIREAVV 442
Cdd:cd05914   337 WFHTGDLGKIDAEGYLYIRGRKKEMiVLSSGKNIYPEEIEAKINNMPFVLESLV 390
PTZ00237 PTZ00237
acetyl-CoA synthetase; Provisional
 152-428 1.16e-09

acetyl-CoA synthetase; Provisional


Pssm-ID: 240325 [Multi-domain]  Cd Length: 647  Bit Score: 62.84  E-value: 1.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  152 PIYIYFTSGSTGKPKAVVGKNESLLHFMNWEASWLDLTD-PMRVSQLTSIGFDAVLRDIFVPICAGGTICIPESReiILD 230
Cdd:PTZ00237  256 PLYILYTSGTTGNSKAVVRSNGPHLVGLKYYWRSIIEKDiPTVVFSHSSIGWVSFHGFLYGSLSLGNTFVMFEGG--IIK 333

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  231 PLRLVH--W--LEHSRVHVVHCTPSLFRFINHLSLTAD------SYPDLRYVLLAGETIRpESLKNWYDNlGNRVRLVNL 300
Cdd:PTZ00237  334 NKHIEDdlWntIEKHKVTHTLTLPKTIRYLIKTDPEATiirskyDLSNLKEIWCGGEVIE-ESIPEYIEN-KLKIKSSRG 411

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  301 YGPTETTMIKLFypikpeDVHRESIPI---GRPLPDTSVYLLDEQQQPVSGSEAGEICI---------ATRYMTHGYFP- 367
Cdd:PTZ00237  412 YGQTEIGITYLY------CYGHINIPYnatGVPSIFIKPSILSEDGKELNVNEIGEVAFklpmppsfaTTFYKNDEKFKq 485

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 517718121  368 --SSHPDqtafipdpcrdqsgeimMYRTGDMGRWLPEGELALLGRKDNQVKIRGNRVELGDIE 428
Cdd:PTZ00237  486 lfSKFPG-----------------YYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIE 531
PRK05620 PRK05620
long-chain fatty-acid--CoA ligase;
25-442 2.45e-09

long-chain fatty-acid--CoA ligase;


Pssm-ID: 180167 [Multi-domain]  Cd Length: 576  Bit Score: 61.72  E-value: 2.45e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   25 GQQTLSYKELDAESDRICELLHAH-GAAQYDHIGILMQDRCASIAAVIGILKLGGVFVPLDPLHPDERLVTMLDTAEVSC 103
Cdd:PRK05620   35 EQEQTTFAAIGARAAALAHALHDElGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEV 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  104 LLCDDAQFERAETLQGH----EGKYFVLR--ARQAMSVQAGSKEAYSHSA--------------NATDPIYIYFTSGSTG 163
Cdd:PRK05620  115 IVADPRLAEQLGEILKEcpcvRAVVFIGPsdADSAAAHMPEGIKVYSYEAlldgrstvydwpelDETTAAAICYSTGTTG 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  164 KPKAVVGKNESL-LHFMNweaswLDLTDPMRVSQLTSIGFDAVLRDIF---VPICA---GGTICIPESReiiLDPLRLVH 236
Cdd:PRK05620  195 APKGVVYSHRSLyLQSLS-----LRTTDSLAVTHGESFLCCVPIYHVLswgVPLAAfmsGTPLVFPGPD---LSAPTLAK 266

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  237 WLEHSRVHVVHCTPSLF-RFINHLSLTADSYPDLRYVLLAGETIRPESLKNWYDNLGnrVRLVNLYGPTETTMI-KLFYP 314
Cdd:PRK05620  267 IIATAMPRVAHGVPTLWiQLMVHYLKNPPERMSLQEIYVGGSAVPPILIKAWEERYG--VDVVHVWGMTETSPVgTVARP 344

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  315 ikPEDVHRES-----IPIGRpLPDTSVYLLDEQQQPVSGSE--AGEICIATRYMTHGYF--PSSHPDQTA--FIPDPCRD 383
Cdd:PRK05620  345 --PSGVSGEArwayrVSQGR-FPASLEYRIVNDGQVMESTDrnEGEIQVRGNWVTASYYhsPTEEGGGAAstFRGEDVED 421

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517718121  384 QSGEIMM---YRTGDMGRWLPEGELALLGRKDNQVKIRGNRVELGDIEHRLTNMAGIREAVV 442
Cdd:PRK05620  422 ANDRFTAdgwLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAV 483
DltA cd05945
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ...
 795-846 3.01e-09

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: 61.11  E-value: 3.01e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 517718121  795 LIAYYLADKMIDDEQLSV---YLRRFLPDYMIPARFIRLDKMPLTPNGKLDYNAL 846
Cdd:cd05945   395 LIAFVVPKPGAEAGLTKAikaELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
PRK06710 PRK06710
long-chain-fatty-acid--CoA ligase; Validated
 16-442 3.06e-09

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


Pssm-ID: 180666 [Multi-domain]  Cd Length: 563  Bit Score: 61.20  E-value: 3.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   16 FPERKAIECGQQTLSYKELDAESDRICELLHAHGAAQYDHIGILMQDRCASIAAVIGILKLGGVFVPLDPLHPDERLVTM 95
Cdd:PRK06710   37 YPEKKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQ 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   96 LDTAEVSCLLCDDAQFERAETLQGHEGKY--------------------FVLRARQAMSVQAGSKEAYsHSANAT----- 150
Cdd:PRK06710  117 LHDSGAKVILCLDLVFPRVTNVQSATKIEhvivtriadflpfpknllypFVQKKQSNLVVKVSESETI-HLWNSVekevn 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  151 -------DP----IYIYFTSGSTGKPKAVVGKNESLLHFMNWEASWLDLTDPMRVSQLTSIGFDAVLrdifvPICAGGTI 219
Cdd:PRK06710  196 tgvevpcDPendlALLQYTGGTTGFPKGVMLTHKNLVSNTLMGVQWLYNCKEGEEVVLGVLPFFHVY-----GMTAVMNL 270

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  220 CIPESREIILDP---LRLV-HWLEHSRVHVVHCTPSLF-RFINHLSLTADSYPDLRyVLLAGETIRPESLKNWYDNLGNR 294
Cdd:PRK06710  271 SIMQGYKMVLIPkfdMKMVfEAIKKHKVTLFPGAPTIYiALLNSPLLKEYDISSIR-ACISGSAPLPVEVQEKFETVTGG 349

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  295 vRLVNLYGPTETTmiklfyPIKPEDVHRES-IP--IGRPLPDTSVYLLD-EQQQPVSGSEAGEICIATRYMTHGYFpsSH 370
Cdd:PRK06710  350 -KLVEGYGLTESS------PVTHSNFLWEKrVPgsIGVPWPDTEAMIMSlETGEALPPGEIGEIVVKGPQIMKGYW--NK 420

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517718121  371 PDQTAFIPdpcrdQSGEImmyRTGDMGRWLPEGELALLGRKDNQVKIRGNRVELGDIEHRLTNMAGIREAVV 442
Cdd:PRK06710  421 PEETAAVL-----QDGWL---HTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVT 484
PLN02330 PLN02330
4-coumarate--CoA ligase-like 1
 27-442 4.25e-09

4-coumarate--CoA ligase-like 1


Pssm-ID: 215189 [Multi-domain]  Cd Length: 546  Bit Score: 60.76  E-value: 4.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   27 QTLSYKELDAESDRICELLHAHGAAQyDHIGILMQDRCASIAAV-IGILKLGGVFVPLDPLHPDERLVTMLDTAEVSCLL 105
Cdd:PLN02330   54 KAVTYGEVVRDTRRFAKALRSLGLRK-GQVVVVVLPNVAEYGIVaLGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIV 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  106 CDDAQFERAETLQ------GHEGKYFVLRARQAMSV--QAGSKEAYsHSANATDPIYIYFTSGSTGKPKAVVGKNESLLH 177
Cdd:PLN02330  133 TNDTNYGKVKGLGlpvivlGEEKIEGAVNWKELLEAadRAGDTSDN-EEILQTDLCALPFSSGTTGISKGVMLTHRNLVA 211

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  178 FMnweASWLDLTDPMRVSQLTSIGFDAvlrdiFVPICAGGTICIPESRE----IILDPLRLVHWLEHSRVHVVHCTPSLF 253
Cdd:PLN02330  212 NL---CSSLFSVGPEMIGQVVTLGLIP-----FFHIYGITGICCATLRNkgkvVVMSRFELRTFLNALITQEVSFAPIVP 283

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  254 RFInhLSLTADSYPD--------LRYVLLAGETIRPESLKNWYDNLGNrVRLVNLYGPTETTMIKLFY--PIKPEDVHRE 323
Cdd:PLN02330  284 PII--LNLVKNPIVEefdlsklkLQAIMTAAAPLAPELLTAFEAKFPG-VQVQEAYGLTEHSCITLTHgdPEKGHGIAKK 360

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  324 SiPIGRPLPDTSVYLLD-EQQQPVSGSEAGEICIATRYMTHGYFpsSHPDQTafipDPCRDQSGEImmyRTGDMGRWLPE 402
Cdd:PLN02330  361 N-SVGFILPNLEVKFIDpDTGRSLPKNTPGELCVRSQCVMQGYY--NNKEET----DRTIDEDGWL---HTGDIGYIDDD 430

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|
gi 517718121  403 GELALLGRKDNQVKIRGNRVELGDIEHRLTNMAGIREAVV 442
Cdd:PLN02330  431 GDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAV 470
AcpA COG3433
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ...
 726-936 4.75e-09

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


Pssm-ID: 442659 [Multi-domain]  Cd Length: 295  Bit Score: 59.38  E-value: 4.75e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  726 DAGIYVQRTQLGYDNYAFPNSWEVRTGHITLEQSRNELESPVNEERVHVILKELGY----DVQLQVEEAQEP------LL 795
Cdd:COG3433    67 APFIPVPYPAQPGRQADDLRLLLRRGLGPGGGLERLVQQVVIRAERGEEEELLLVLraaaVVRVAVLAALRGagvgllLI 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  796 IAYYLADKMIDDEQLSVYLRRFLPDYMIPARFIRLDKMPLTPNGKLDYNALPSPFEQDTTARIYKAPNSSTELK---LLD 872
Cdd:COG3433   147 VGAVAALDGLAAAAALAALDKVPPDVVAASAVVALDALLLLALKVVARAAPALAAAEALLAAASPAPALETALTeeeLRA 226

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517718121  873 IWTHILGIK--RISADDHFLQIGVHSLNIMTLIAQVyENFQVELPLEQVFEHDTLEEIAAYIDEQD 936
Cdd:COG3433   227 DVAELLGVDpeEIDPDDNLFDLGLDSIRLMQLVERW-RKAGLDVSFADLAEHPTLAAWWALLAAAQ 291
A_NRPS_MycA_like cd05908
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ...
 148-428 4.85e-09

The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341234 [Multi-domain]  Cd Length: 499  Bit Score: 60.58  E-value: 4.85e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  148 NATDPIYIYFTSGSTGKPKAVVGKNESLLHFM-------NWEA-----SWLDLTDPMRVsqltsIGFDavlrdiFVPICA 215
Cdd:cd05908   104 LADELAFIQFSSGSTGDPKGVMLTHENLVHNMfailnstEWKTkdrilSWMPLTHDMGL-----IAFH------LAPLIA 172

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  216 GGTICIPESREIILDPlrlVHWLEHSRVHVVH--CTPSLFR--FINHLSLTADSYPDL---RYVLLAGETIRPESLKNWY 288
Cdd:cd05908   173 GMNQYLMPTRLFIRRP---ILWLKKASEHKATivSSPNFGYkyFLKTLKPEKANDWDLssiRMILNGAEPIDYELCHEFL 249

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  289 DNLG----NRVRLVNLYGPTETT----MIKLFYPIKPEDVHRESIPIGRPLPD--------------------TSVYLLD 340
Cdd:cd05908   250 DHMSkyglKRNAILPVYGLAEASvgasLPKAQSPFKTITLGRRHVTHGEPEPEvdkkdsecltfvevgkpideTDIRICD 329

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  341 EQQQPVSGSEAGEICIATRYMTHGYFPSSHPDQTAFIPDpcrdqsGEImmyRTGDMGrWLPEGELALLGRKDNQVKIRGN 420
Cdd:cd05908   330 EDNKILPDGYIGHIQIRGKNVTPGYYNNPEATAKVFTDD------GWL---KTGDLG-FIRNGRLVITGREKDIIFVNGQ 399


                  ....*...
gi 517718121  421 RVELGDIE 428
Cdd:cd05908   400 NVYPHDIE 407
ACS cd05966
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ...
 148-442 5.39e-09

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: 60.65  E-value: 5.39e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  148 NATDPIYIYFTSGSTGKPKAVVgknesllH----FMNWEASWLDLTdpmrvsqltsigFDAVLRDIFV------------ 211
Cdd:cd05966   229 DSEDPLFILYTSGSTGKPKGVV-------HttggYLLYAATTFKYV------------FDYHPDDIYWctadigwitghs 289

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  212 -----PICAGGTICIPESREIILDPLRLVHWLEHSRVHVVHCTPSLFRfinhlSLTA--DSYPD------LRyvLLA--G 276
Cdd:cd05966   290 yivygPLANGATTVMFEGTPTYPDPGRYWDIVEKHKVTIFYTAPTAIR-----ALMKfgDEWVKkhdlssLR--VLGsvG 362

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  277 ETIRPESLKNWYDNLGN-RVRLVNLYGPTETTMIKL-----FYPIKPEDVhresipiGRPLPDTSVYLLDEQQQPVSGSE 350
Cdd:cd05966   363 EPINPEAWMWYYEVIGKeRCPIVDTWWQTETGGIMItplpgATPLKPGSA-------TRPFFGIEPAILDEEGNEVEGEV 435

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  351 AGEICIA--------TRYMTHGYFpsshpDQTAFIPDPcrdqsGeimMYRTGDMGRWLPEGELALLGRKDNQVKIRGNRV 422
Cdd:cd05966   436 EGYLVIKrpwpgmarTIYGDHERY-----EDTYFSKFP-----G---YYFTGDGARRDEDGYYWITGRVDDVINVSGHRL 502

                         330       340
                  ....*....|....*....|
gi 517718121  423 ELGDIEHRLTNMAGIREAVV 442
Cdd:cd05966   503 GTAEVESALVAHPAVAEAAV 522
PRK07514 PRK07514
malonyl-CoA synthase; Validated
 7-412 8.40e-09

malonyl-CoA synthase; Validated


Pssm-ID: 181011 [Multi-domain]  Cd Length: 504  Bit Score: 59.89  E-value: 8.40e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121    7 YELARAFAAFPERKAIECGQ-QTLSYKELDAESDRICELLHAHGAAQYDHIGILMQDRCASIAAVIGILKLGGVFVPLDP 85
Cdd:PRK07514    6 FDALRAAFADRDAPFIETPDgLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNT 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   86 LHPDERLVTMLDTAEVSCLLCDDAQFE------------RAETLQGHEGKYFVLRARQAmsvqagSKEAYSHSANATDPI 153
Cdd:PRK07514   86 AYTLAELDYFIGDAEPALVVCDPANFAwlskiaaaagapHVETLDADGTGSLLEAAAAA------PDDFETVPRGADDLA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  154 YIYFTSGSTGKPKAVVGKNESLLhfmnweASWLDLTDPMRVSQltsigfDAVL---------RDIFVpicAGGTICIPES 224
Cdd:PRK07514  160 AILYTSGTTGRSKGAMLSHGNLL------SNALTLVDYWRFTP------DDVLihalpifhtHGLFV---ATNVALLAGA 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  225 REIIL---DPLRLVHWLEhsRVHVVHCTPSLF-RFINHLSLTADSYPDLR-YV-----LLAgETIRpeslkNWYDNLGNR 294
Cdd:PRK07514  225 SMIFLpkfDPDAVLALMP--RATVMMGVPTFYtRLLQEPRLTREAAAHMRlFIsgsapLLA-ETHR-----EFQERTGHA 296

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  295 V--RlvnlYGPTETTMIKlfypIKPEDVHRESIPIGRPLPDTSVYLLD-EQQQPVSGSEAGEICIATRYMTHGYFpsSHP 371
Cdd:PRK07514  297 IleR----YGMTETNMNT----SNPYDGERRAGTVGFPLPGVSLRVTDpETGAELPPGEIGMIEVKGPNVFKGYW--RMP 366

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....
gi 517718121  372 DQTA--FIPDpcrdqsGeimMYRTGDMGRWLPEGELALLGR-KD 412
Cdd:PRK07514  367 EKTAeeFRAD------G---FFITGDLGKIDERGYVHIVGRgKD 401
PaaK COG1541
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ...
 151-437 1.64e-08

Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];


Pssm-ID: 441150 [Multi-domain]  Cd Length: 423  Bit Score: 58.62  E-value: 1.64e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  151 DPIYIYFTSGSTGKPKaVVGknesllhfmnweASWLDLTDPMRVSQ--LTSIGFDAvlRDIFVpICAG------------ 216
Cdd:COG1541    84 EIVRIHASSGTTGKPT-VVG------------YTRKDLDRWAELFArsLRAAGVRP--GDRVQ-NAFGyglftgglglhy 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  217 -----GTICIPESreiILDPLRLVHWLEHSRVHVVHCTPSlfrFINHLSLTAD----SYPD--LRYVLLAGETIrPESLK 285
Cdd:COG1541   148 gaerlGATVIPAG---GGNTERQLRLMQDFGPTVLVGTPS---YLLYLAEVAEeegiDPRDlsLKKGIFGGEPW-SEEMR 220

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  286 NWY-DNLGnrVRLVNLYGPTETTMI---------------KLFYP--IKPEDvhresipiGRPLPDTsvylldeqqqpvs 347
Cdd:COG1541   221 KEIeERWG--IKAYDIYGLTEVGPGvayeceaqdglhiweDHFLVeiIDPET--------GEPVPEG------------- 277

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  348 gsEAGEICIAT---------RYMTHgyfpsshpDQTAFIPDPCRDqsGEIMMyRtgdMGRWlpegelalLGRKDNQVKIR 418
Cdd:COG1541   278 --EEGELVVTTltkeampliRYRTG--------DLTRLLPEPCPC--GRTHP-R---IGRI--------LGRADDMLIIR 333

                         330
                  ....*....|....*....
gi 517718121  419 GNRVELGDIEHRLTNMAGI 437
Cdd:COG1541   334 GVNVFPSQIEEVLLRIPEV 352
PRK07768 PRK07768
long-chain-fatty-acid--CoA ligase; Validated
 151-455 4.23e-08

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


Pssm-ID: 236091 [Multi-domain]  Cd Length: 545  Bit Score: 57.70  E-value: 4.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  151 DPIYIYFTSGSTGKPKAVVGKNESLlhFMNWEA---------------SWLDLTDPMRVsqltsIGFdavlrdIFVPICA 215
Cdd:PRK07768  153 DLALMQLTSGSTGSPKAVQITHGNL--YANAEAmfvaaefdvetdvmvSWLPLFHDMGM-----VGF------LTVPMYF 219

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  216 GGTICIPESREIILDPLRlvhWLE--HSRVHVVHCTPS---------LFRFINHLSLTADSypdLRYVLLAGETIRPESL 284
Cdd:PRK07768  220 GAELVKVTPMDFLRDPLL---WAEliSKYRGTMTAAPNfayallarrLRRQAKPGAFDLSS---LRFALNGAEPIDPADV 293

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  285 KNWYDNLG----NRVRLVNLYGPTETT----MIKLFYPIKPEDVH-------RESIP-----------IGRPLPDTSVYL 338
Cdd:PRK07768  294 EDLLDAGArfglRPEAILPAYGMAEATlavsFSPCGAGLVVDEVDadllaalRRAVPatkgntrrlatLGPPLPGLEVRV 373

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  339 LDEQQQPVSGSEAGEICIATRYMTHGYFpsshpdqTAFIPDPCRDQSGeimMYRTGDMGRWLPEGELALLGRKDNQVKIR 418
Cdd:PRK07768  374 VDEDGQVLPPRGVGVIELRGESVTPGYL-------TMDGFIPAQDADG---WLDTGDLGYLTEEGEVVVCGRVKDVIIMA 443

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 517718121  419 GNRVELGDIEHRLTNMAGIREA-VVRMRAKADTPK-GMA 455
Cdd:PRK07768  444 GRNIYPTDIERAAARVEGVRPGnAVAVRLDAGHSReGFA 482
PRK08633 PRK08633
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
 140-431 4.98e-08

2-acyl-glycerophospho-ethanolamine acyltransferase; Validated


Pssm-ID: 236315 [Multi-domain]  Cd Length: 1146  Bit Score: 58.01  E-value: 4.98e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  140 KEAYSHSANATDPIYIYFTSGSTGKPKAVV--GKN-----ESLLHFMNweaswLDLTDPMrVSQLT---SIGFDAVLrdi 209
Cdd:PRK08633  772 KRLYGPTFKPDDTATIIFSSGSEGEPKGVMlsHHNilsniEQISDVFN-----LRNDDVI-LSSLPffhSFGLTVTL--- 842

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  210 FVPICAG-GTICIPesreiilDPL------RLVHwlEHsRVHVVHCTPSLFR-FINHLSLTADSYPDLRYVLLAGETIRP 281
Cdd:PRK08633  843 WLPLLEGiKVVYHP-------DPTdalgiaKLVA--KH-RATILLGTPTFLRlYLRNKKLHPLMFASLRLVVAGAEKLKP 912

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  282 EsLKNWY-DNLGnrVRLVNLYGPTETT-MIKLFYP-IKPEDVHRESI----PIGRPLPDTSVYLLD-EQQQPVSGSEAGE 353
Cdd:PRK08633  913 E-VADAFeEKFG--IRILEGYGATETSpVASVNLPdVLAADFKRQTGskegSVGMPLPGVAVRIVDpETFEELPPGEDGL 989

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517718121  354 ICIATRYMTHGYFpsSHPDQTAfipDPCRDQSGeIMMYRTGDMGRWLPEGELALLGRKDNQVKIRGNRVELGDIEHRL 431
Cdd:PRK08633  990 ILIGGPQVMKGYL--GDPEKTA---EVIKDIDG-IGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEEL 1061
PRK04813 PRK04813
D-alanine--poly(phosphoribitol) ligase subunit DltA;
803-846 8.25e-08

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


Pssm-ID: 235313 [Multi-domain]  Cd Length: 503  Bit Score: 56.44  E-value: 8.25e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 517718121  803 KMIDDEqlsvyLRRFLPDYMIPARFIRLDKMPLTPNGKLDYNAL 846
Cdd:PRK04813  459 KAIKKE-----LKERLMEYMIPRKFIYRDSLPLTPNGKIDRKAL 497
LC_FACS_bac1 cd17641
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ...
 27-442 8.33e-08

bacterial long-chain fatty acid CoA synthetase; 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: 341296 [Multi-domain]  Cd Length: 569  Bit Score: 56.66  E-value: 8.33e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   27 QTLSYKELDAESDRICELLHAHGAAQYDHIGILMQDRCASIAAVIGILKLGGVFVPL--DPLHpdERLVTMLDTAEVSCL 104
Cdd:cd17641    10 QEFTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIyqDSMA--EEVAYLLNYTGARVV 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  105 LCDDA-QFERAETLQGH------------EG--KYFVLRARQAMSVQAGSKEA-------YSHSANATDP---IYIYFTS 159
Cdd:cd17641    88 IAEDEeQVDKLLEIADRipsvryviycdpRGmrKYDDPRLISFEDVVALGRALdrrdpglYEREVAAGKGedvAVLCTTS 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  160 GSTGKPKAVVGKNESLLHFmnwEASWLDLtDPMR-----VSQLTsigFDAVLRDIFV---PICAGGTICIPES------- 224
Cdd:cd17641   168 GTTGKPKLAMLSHGNFLGH---CAAYLAA-DPLGpgdeyVSVLP---LPWIGEQMYSvgqALVCGFIVNFPEEpetmmed 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  225 -REI----ILDPLRLvhW---LEHSRVHVVHCTP---SLFRFINHLSLTA----------DSYPDLRYVL---------- 273
Cdd:cd17641   241 lREIgptfVLLPPRV--WegiAADVRARMMDATPfkrFMFELGMKLGLRAldrgkrgrpvSLWLRLASWLadallfrplr 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  274 ------------LAGETIRPESLKnWYDNLGnrVRLVNLYGPTETTMiklFYPIKPE-DVHRESIpiGRPLPDTSVYLld 340
Cdd:cd17641   319 drlgfsrlrsaaTGGAALGPDTFR-FFHAIG--VPLKQLYGQTELAG---AYTVHRDgDVDPDTV--GVPFPGTEVRI-- 388

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  341 eqqqpvsgSEAGEICIATRYMTHGYFpsSHPDQTAfipdpcRDQSGEIMMyRTGDMGRWLPEGELALLGR-KDNQVKIRG 419
Cdd:cd17641   389 --------DEVGEILVRSPGVFVGYY--KNPEATA------EDFDEDGWL-HTGDAGYFKENGHLVVIDRaKDVGTTSDG 451

                         490       500
                  ....*....|....*....|...
gi 517718121  420 NRVELGDIEHRLTNMAGIREAVV 442
Cdd:cd17641   452 TRFSPQFIENKLKFSPYIAEAVV 474
FATP_FACS cd05940
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ...
 27-442 8.51e-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: 56.21  E-value: 8.51e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   27 QTLSYKELDAESDRICELLHAHGAAQYDHIGILMQDRCASIAAVIGILKLGGVfvpldplhpderlVTMLDTaevscllc 106
Cdd:cd05940     2 EALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAV-------------AALINY-------- 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  107 ddaqferaeTLQGhegkyfvlrarqamsvqagskEAYSHSANATDP--------IYIYfTSGSTGKPKAVVGKNESLLHF 178
Cdd:cd05940    61 ---------NLRG---------------------ESLAHCLNVSSAkhlvvdaaLYIY-TSGTTGLPKAAIISHRRAWRG 109

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  179 MNWEASW--------LDLTDPMRVSQLTSIGFDAVLRdifvpicAGGTICIPES-------REIIldplrlvhwlEHsrv 243
Cdd:cd05940   110 GAFFAGSggalpsdvLYTCLPLYHSTALIVGWSACLA-------SGATLVIRKKfsasnfwDDIR----------KY--- 169

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  244 hvvHCTpsLFRFINHLsltadsypdLRYVL---------------LAGETIRPESlknWyDNLGNR---VRLVNLYGPTE 305
Cdd:cd05940   170 ---QAT--IFQYIGEL---------CRYLLnqppkpterkhkvrmIFGNGLRPDI---W-EEFKERfgvPRIAEFYAATE 231

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  306 TTMIKLFYPIKPEDVHRESIPIGRPLPDTSVYLLDEQQQPVSGS----------EAGE-IC-IATRYMTHGYFpsshpDQ 373
Cdd:cd05940   232 GNSGFINFFGKPGAIGRNPSLLRKVAPLALVKYDLESGEPIRDAegrcikvprgEPGLlISrINPLEPFDGYT-----DP 306

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 517718121  374 TAFIPDPCRD--QSGEImMYRTGDMGRWLPEGELALLGRKDNQVKIRGNRVELGDIEHRLTNMAGIREAVV 442
Cdd:cd05940   307 AATEKKILRDvfKKGDA-WFNTGDLMRLDGEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANV 376
A_NRPS_GliP_like cd17653
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ...
 795-846 1.23e-07

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: 55.78  E-value: 1.23e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 517718121  795 LIAYYlADKMIDDEQLSVYLRRFLPDYMIPARFIRLDKMPLTPNGKLDYNAL 846
Cdd:cd17653   381 LVAFV-TPETVDVDGLRSELAKHLPSYAVPDRIIALDSFPLTANGKVDRKAL 431
ACLS-CaiC cd17637
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ...
 250-442 2.48e-07

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: 54.20  E-value: 2.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  250 PSLFRFINHLSLTADSYPDLRYVLlaG-ETirPESLKNWYDNlgNRVRLVNLYGPTETTMIKLFYPI--KPEDVhresip 326
Cdd:cd17637    97 PILSNLLDAAEKSGVDLSSLRHVL--GlDA--PETIQRFEET--TGATFWSLYGQTETSGLVTLSPYreRPGSA------ 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  327 iGRPLPDTSVYLLDEQQQPVSGSEAGEICIATRYMTHGYFPSSHPDQTAFipdpcRDQsgeimMYRTGDMGRWLPEGELA 406
Cdd:cd17637   165 -GRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTF-----RNG-----WHHTGDLGRFDEDGYLW 233

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 517718121  407 LLGRKDNQ--VKIRGNRVELGDIEHRLTNMAGIREAVV 442
Cdd:cd17637   234 YAGRKPEKelIKPGGENVYPAEVEKVILEHPAIAEVCV 271
A_NRPS_alphaAR cd17647
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ...
 775-849 3.04e-07

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: 54.83  E-value: 3.04e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517718121  775 ILKELGYDVQLQVEEAQEPL---LIAYYladKMIDDeqLSVYLRRFLPDYMIPARFIRLDKMPLTPNGKLDYNALPSP 849
Cdd:cd17647   448 PDDESFAQEDVPKEVSTDPIvkgLIGYR---KLIKD--IREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKLQFP 520
ttLC_FACS_AEE21_like cd12118
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ...
 9-169 3.41e-07

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: 54.61  E-value: 3.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121    9 LARAFAAFPERKAIECGQQTLSYKELDAESDRICELLHAHGAAQYDHIGILMQDRCASIAAVIGILKLGGVFVPLDPLHP 88
Cdd:cd12118    10 LERAAAVYPDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLD 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   89 DERLVTMLDTAEVSCLLCDdAQFERAETLQGHEGKYFVLRArqamsvqagskeayshsANATDPIYIYFTSGSTGKPKAV 168
Cdd:cd12118    90 AEEIAFILRHSEAKVLFVD-REFEYEDLLAEGDPDFEWIPP-----------------ADEWDPIALNYTSGTTGRPKGV 151


                  .
gi 517718121  169 V 169
Cdd:cd12118   152 V 152
PtmA cd17636
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ...
 328-442 4.08e-07

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: 53.84  E-value: 4.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  328 GRPLPDTSVYLLDEQQQPVSGSEAGEICIATRYMTHGYFpsSHPDQTAfipdpCRDQSGeimMYRTGDMGRWLPEGELAL 407
Cdd:cd17636   166 GRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYW--NRPEVNA-----RRTRGG---WHHTNDLGRREPDGSLSF 235

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 517718121  408 LGRKDNQVKIRGNRVELGDIEHRLTNMAGIREAVV 442
Cdd:cd17636   236 VGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAV 270
PRK05691 PRK05691
peptide synthase; Validated
 1-428 4.24e-07

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 55.17  E-value: 4.24e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121    1 MDNTIQYELARAFAAFPERKAI------ECGQQTLSYKELDAESDRICELLHAHgAAQYDHIGILMQDRCASIAAVIGIL 74
Cdd:PRK05691    7 LPLTLVQALQRRAAQTPDRLALrfladdPGEGVVLSYRDLDLRARTIAAALQAR-ASFGDRAVLLFPSGPDYVAAFFGCL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   75 KLGGVFVPLDP-----LHPDERLVTMLDTAEVSCLLCDDAQferAETLQGHEGkyfvLRARQAM------SVQAGSKEAY 143
Cdd:PRK05691   86 YAGVIAVPAYPpesarRHHQERLLSIIADAEPRLLLTVADL---RDSLLQMEE----LAAANAPellcvdTLDPALAEAW 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  144 SHSANATDPI-YIYFTSGSTGKPKAV------VGKNESLLH-----FMNWE---ASWLDLTDPMRVsqltsIGfdAVLRD 208
Cdd:PRK05691  159 QEPALQPDDIaFLQYTSGSTALPKGVqvshgnLVANEQLIRhgfgiDLNPDdviVSWLPLYHDMGL-----IG--GLLQP 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  209 IFvpicaGGTICIPESREIILDplRLVHWLEHsrvhvvhctpslfrfINHLSLTADSYPDLRYVL---------LAG--- 276
Cdd:PRK05691  232 IF-----SGVPCVLMSPAYFLE--RPLRWLEA---------------ISEYGGTISGGPDFAYRLcservsesaLERldl 289

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  277 ----------ETIRPESLKNWYDNLG----NRVRLVNLYGPTETTmikLFYP-------IKPEDVHRESIP--------- 326
Cdd:PRK05691  290 srwrvaysgsEPIRQDSLERFAEKFAacgfDPDSFFASYGLAEAT---LFVSggrrgqgIPALELDAEALArnraepgtg 366

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  327 -----IGRPLPDTSVYLLDEQQQPVSGSEA-GEICIATRYMTHGYFPSSHPDQTAFIpdpcrDQSGEIMMyRTGDMGrWL 400
Cdd:PRK05691  367 svlmsCGRSQPGHAVLIVDPQSLEVLGDNRvGEIWASGPSIAHGYWRNPEASAKTFV-----EHDGRTWL-RTGDLG-FL 439

                         490       500
                  ....*....|....*....|....*...
gi 517718121  401 PEGELALLGRKDNQVKIRGNRVELGDIE 428
Cdd:PRK05691  440 RDGELFVTGRLKDMLIVRGHNLYPQDIE 467
PRK08314 PRK08314
long-chain-fatty-acid--CoA ligase; Validated
 4-189 4.36e-07

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


Pssm-ID: 236235 [Multi-domain]  Cd Length: 546  Bit Score: 54.20  E-value: 4.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121    4 TIQYELARAFAAFPERKAIECGQQTLSYKELDAESDRICELLHAH-GAAQYDHIGILMQDRCASIAAVIGILKLGGVFVP 82
Cdd:PRK08314   11 SLFHNLEVSARRYPDKTAIVFYGRAISYRELLEEAERLAGYLQQEcGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVP 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   83 LDPLHPDERLVTMLDTAEVSCLLCDDAQFERAETLQGHEGKYFVLRA------------------RQAMSVQAGSKEAY- 143
Cdd:PRK08314   91 VNPMNREEELAHYVTDSGARVAIVGSELAPKVAPAVGNLRLRHVIVAqysdylpaepeiavpawlRAEPPLQALAPGGVv 170

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 517718121  144 -------------SHSANATDPIYIYFTSGSTGKPKAVVGKNESLLHFMNWEASWLDLT 189
Cdd:PRK08314  171 awkealaaglappPHTAGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNST 229
COG1606 COG1606
ATP-utilizing enzyme, PP-loop superfamily [General function prediction only];
500-621 4.83e-07

ATP-utilizing enzyme, PP-loop superfamily [General function prediction only];


Pssm-ID: 441214 [Multi-domain]  Cd Length: 265  Bit Score: 52.81  E-value: 4.83e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  500 EQLQSKLQPVEKenqpsydCLLLYSGGKDSTYALYRLVE-MGARVLAYTFDNGYISSAAFRNIDSVVKELGVDHIVGTFD 578
Cdd:COG1606     6 ERLKAILKELGS-------VLVAFSGGVDSTLLAKVAHDvLGDRVLAVTADSPSLPERELEEAKELAKEIGIRHEVIETD 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 517718121  579 gMLDI--FKEGLKQECSVCngcfKAMRILS-TRVAAERGIPYIVTG 621
Cdd:COG1606    79 -ELEDpeFVANPPDRCYHC----KKELFSKlKELAKELGYAVVADG 119
PRK08043 PRK08043
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
149-455 5.24e-07

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


Pssm-ID: 181207 [Multi-domain]  Cd Length: 718  Bit Score: 54.33  E-value: 5.24e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  149 ATDPIYIYFTSGSTGKPKAVVGKNESLLhfmnweaswldltdpMRVSQLTSIGfDAVLRD-----------------IFV 211
Cdd:PRK08043  364 PEDAALILFTSGSEGHPKGVVHSHKSLL---------------ANVEQIKTIA-DFTPNDrfmsalplfhsfgltvgLFT 427

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  212 PICAGGTICIPESreiildPL--RLVHWLEHSRvhvvHCTpSLF---RFINHLSLTADSY--PDLRYVLLAGETIRPESL 284
Cdd:PRK08043  428 PLLTGAEVFLYPS------PLhyRIVPELVYDR----NCT-VLFgtsTFLGNYARFANPYdfARLRYVVAGAEKLQESTK 496

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  285 KNWYDNLGnrVRLVNLYGPTE---TTMIKLFYPIKPEDVhresipiGRPLPDTSVYLLdeqqqPVSG-SEAGEICIATRY 360
Cdd:PRK08043  497 QLWQDKFG--LRILEGYGVTEcapVVSINVPMAAKPGTV-------GRILPGMDARLL-----SVPGiEQGGRLQLKGPN 562

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  361 MTHGYFPSSHPDQtaFIPDPCRDQSGEIMM--YRTGDMGRWLPEGELALLGRKDNQVKIRGNRVELGDIEHrLTNMAGiR 438
Cdd:PRK08043  563 IMNGYLRVEKPGV--LEVPTAENARGEMERgwYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQ-LALGVS-P 638

                         330
                  ....*....|....*..
gi 517718121  439 EAVVRMRAKADTPKGMA 455
Cdd:PRK08043  639 DKQHATAIKSDASKGEA 655
D-ala-DACP-lig TIGR01734
D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also ...
 814-846 6.49e-07

D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also called D-alanine-D-alanyl carrier protein ligase) which activates D-alanine as an adenylate via the reaction D-ala + ATP -> D-ala-AMP + PPi, and further catalyzes the condensation of the amino acid adenylate with the D-alanyl carrier protein (D-ala-ACP). The D-alanine is then further transferred to teichoic acid in the biosynthesis of lipoteichoic acid (LTA) and wall teichoic acid (WTA) in gram positive bacteria, both polysacchatides. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]


Pssm-ID: 273780 [Multi-domain]  Cd Length: 502  Bit Score: 53.61  E-value: 6.49e-07
                           10        20        30
                   ....*....|....*....|....*....|...
gi 517718121   814 LRRFLPDYMIPARFIRLDKMPLTPNGKLDYNAL 846
Cdd:TIGR01734  464 LKKSLPAYMIPRKFIYRDQLPLTANGKIDRKAL 496
PRK05677 PRK05677
long-chain-fatty-acid--CoA ligase; Validated
 301-465 1.04e-06

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


Pssm-ID: 168170 [Multi-domain]  Cd Length: 562  Bit Score: 53.23  E-value: 1.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  301 YGPTETTMIKLFYPIKpedvHRESIPIGRPLPDTSVYLLDEQQQPVSGSEAGEICIATRYMTHGYFpsSHPDQTAFIpdp 380
Cdd:PRK05677  358 YGMTETSPVVSVNPSQ----AIQVGTIGIPVPSTLCKVIDDDGNELPLGEVGELCVKGPQVMKGYW--QRPEATDEI--- 428

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  381 cRDQSGEImmyRTGDMGRWLPEGELALLGRKDNQVKIRGNRVELGDIEHRLTNMAGIREavvrmrakadtpkgmaqqhCA 460
Cdd:PRK05677  429 -LDSDGWL---KTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQ-------------------CA 485


                  ....*
gi 517718121  461 ACGLP 465
Cdd:PRK05677  486 AIGVP 490
MenE/FadK COG0318
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ...
 805-857 1.45e-06

O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis


Pssm-ID: 440087 [Multi-domain]  Cd Length: 452  Bit Score: 52.51  E-value: 1.45e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 517718121  805 IDDEQLSVYLRRFLPDYMIPARFIRLDKMPLTPNGKLDYNALPSPFEQDTTAR 857
Cdd:COG0318   400 LDAEELRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRERYAAGALEA 452
PRK08308 PRK08308
acyl-CoA synthetase; Validated
 328-442 3.17e-06

acyl-CoA synthetase; Validated


Pssm-ID: 236231 [Multi-domain]  Cd Length: 414  Bit Score: 51.19  E-value: 3.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  328 GRPLPDTSVYLLDEQQQPV----SGSEAGEICIATRYMTH---GYfPSSHPDQTAfipDPCRDQSGEIMMY------RTG 394
Cdd:PRK08308  221 GTPLPEAWFYKLRERTTYMmqqyGCSEAGCVSICPDMKSHldlGN-PLPHVSVSA---GSDENAPEEIVVKmgdkeiFTK 296

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 517718121  395 DMGRWLPEGELALLGRKDNQVKIRGNRVELGDIEHRLTNMAGIREAVV 442
Cdd:PRK08308  297 DLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVV 344
PRK08276 PRK08276
long-chain-fatty-acid--CoA ligase; Validated
 26-411 4.24e-06

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


Pssm-ID: 236215 [Multi-domain]  Cd Length: 502  Bit Score: 51.06  E-value: 4.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   26 QQTLSYKELDAESDRICELLHAHGAAQYDHIGILMQDRCASIAAVIGILKLGGVFVPLD-PLHPDErLVTMLDTAEVSCL 104
Cdd:PRK08276    9 GEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINwHLTAAE-IAYIVDDSGAKVL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  105 LCDDAQFERAETLQGHEGKYfvLRARQAMSVQAGSKEAYSH--SANATDPI-------YIYFTSGSTGKPKAV------V 169
Cdd:PRK08276   88 IVSAALADTAAELAAELPAG--VPLLLVVAGPVPGFRSYEEalAAQPDTPIadetagaDMLYSSGTTGRPKGIkrplpgL 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  170 GKNESLLHFMNWEASWLDLTDPMRVSQLTSIGFDAVLRDIFVPICAGGTICIPESreiiLDP---LRLVhwlEHSRVHVV 246
Cdd:PRK08276  166 DPDEAPGMMLALLGFGMYGGPDSVYLSPAPLYHTAPLRFGMSALALGGTVVVMEK----FDAeeaLALI---ERYRVTHS 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  247 HCTPSLfrFINHLSLtadsypdlryvllagetirPESLKNWYDNLGNRV--------------RLVNLYGP--------T 304
Cdd:PRK08276  239 QLVPTM--FVRMLKL-------------------PEEVRARYDVSSLRVaihaaapcpvevkrAMIDWWGPiiheyyasS 297

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  305 ETTMIKLfypIKPED--VHRESipIGRPLpDTSVYLLDEQQQPVSGSEAGEIciatrYMTHGYFPSSH---PDQTAFIPD 379
Cdd:PRK08276  298 EGGGVTV---ITSEDwlAHPGS--VGKAV-LGEVRILDEDGNELPPGEIGTV-----YFEMDGYPFEYhndPEKTAAARN 366

                         410       420       430
                  ....*....|....*....|....*....|...
gi 517718121  380 PCRdqsgeimMYRTGDMGrWLPE-GELALLGRK 411
Cdd:PRK08276  367 PHG-------WVTVGDVG-YLDEdGYLYLTDRK 391
FACL_like_4 cd05944
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 151-419 7.02e-06

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


Pssm-ID: 341266 [Multi-domain]  Cd Length: 359  Bit Score: 49.79  E-value: 7.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  151 DPIYIYF-TSGSTGKPKaVVGKNESLLHFMNWEASWLDLTDPMRV--SQLTSIGFDAVLRDIFVPICAGGTICIP----- 222
Cdd:cd05944     2 DDVAAYFhTGGTTGTPK-LAQHTHSNEVYNAWMLALNSLFDPDDVllCGLPLFHVNGSVVTLLTPLASGAHVVLAgpagy 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  223 ESREIILDPLRLVhwlEHSRVHVVHCTPSLFRFINHLSLTADsYPDLRYVLLAGETIRPESLKNWYDNLGnrVRLVNLYG 302
Cdd:cd05944    81 RNPGLFDNFWKLV---ERYRITSLSTVPTVYAALLQVPVNAD-ISSLRFAMSGAAPLPVELRARFEDATG--LPVVEGYG 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  303 PTETT-MIKLFYPIKPedvhRESIPIGRPLPDTSVYLLDEQ-----QQPVSGSEAGEICIATRYMTHGYFPSSHpDQTAF 376
Cdd:cd05944   155 LTEATcLVAVNPPDGP----KRPGSVGLRLPYARVRIKVLDgvgrlLRDCAPDEVGEICVAGPGVFGGYLYTEG-NKNAF 229

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 517718121  377 IPDpcrdqsgeiMMYRTGDMGRWLPEGELALLGRKDNQVkIRG 419
Cdd:cd05944   230 VAD---------GWLNTGDLGRLDADGYLFITGRAKDLI-IRG 262
AANH_PF0828-like cd01994
putative ATP pyrophosphatase PF0828 and similar proteins; This subfamily includes Pyrococcus ...
 519-621 7.77e-06

putative ATP pyrophosphatase PF0828 and similar proteins; This subfamily includes Pyrococcus furiosus putative ATP pyrophosphatase PF0828 and Pyrococcus horikoshii PH1257. They belong to the adenine nucleotide alpha hydrolase (AANH) superfamily that also includes other N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group. This subfamily of proteins is predicted to bind ATP. This domain has a strongly conserved motif SGGKD at the N-terminus.


Pssm-ID: 467498  Cd Length: 211  Bit Score: 48.43  E-value: 7.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  519 CLLLYSGGKDSTYALYRLVEMGARV--LAYTFDNGYIS----SAAFRNIDSVVKELGVDHIVGTFDGMLDIFKEGLKQEC 592
Cdd:cd01994     2 VVALISGGKDSIYALLHAIRNGHEVvaLANLRPEDKDSymfqTVGHELLELQAEALGLPLIRREIRGKSVTQELGYEGEE 81

                          90       100
                  ....*....|....*....|....*....
gi 517718121  593 SVcngCFKAMRILSTRVAAERGIPYIVTG 621
Cdd:cd01994    82 ED---EVEDLYELLKKVKERPEVEAVVSG 107
PRK07787 PRK07787
acyl-CoA synthetase; Validated
 296-442 1.01e-05

acyl-CoA synthetase; Validated


Pssm-ID: 236096 [Multi-domain]  Cd Length: 471  Bit Score: 49.60  E-value: 1.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  296 RLVNLYGPTETtMIKLFYPIkpeDVHRESIPIGRPLPDTSVYLLDEQQQPVS--GSEAGEICIATRYMTHGYFpsSHPDQ 373
Cdd:PRK07787  268 RPVERYGMTET-LITLSTRA---DGERRPGWVGLPLAGVETRLVDEDGGPVPhdGETVGELQVRGPTLFDGYL--NRPDA 341

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  374 TAfipdPCRDQSGeimMYRTGDMGRWLPEGELALLGRKD-NQVKIRGNRVELGDIEHRLTNMAGIREAVV 442
Cdd:PRK07787  342 TA----AAFTADG---WFRTGDVAVVDPDGMHRIVGREStDLIKSGGYRIGAGEIETALLGHPGVREAAV 404
PRK12406 PRK12406
long-chain-fatty-acid--CoA ligase; Provisional
 25-442 1.07e-05

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


Pssm-ID: 183506 [Multi-domain]  Cd Length: 509  Bit Score: 49.70  E-value: 1.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   25 GQQTLSYKELDAESDRICELLHAHGAAQYDHIGILMQDRCASIAAVIGILKLGGVFVPLDpLH--PDERLVTMLDTAevs 102
Cdd:PRK12406    8 GDRRRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVN-WHfkPEEIAYILEDSG--- 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  103 cllcddaqferAETLQGHEGkyfvLRARQAMSVQAGSK-----------EAYSHS-------ANATD------------- 151
Cdd:PRK12406   84 -----------ARVLIAHAD----LLHGLASALPAGVTvlsvptppeiaAAYRISpalltppAGAIDwegwlaqqepydg 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  152 -----PIYIYFTSGSTGKPKAVVGKNESLLHFMNWEA-----------SWLDLTDPMRVSQLTSIGFDAvlrdifvpICA 215
Cdd:PRK12406  149 ppvpqPQSMIYTSGTTGHPKGVRRAAPTPEQAAAAEQmraliyglkpgIRALLTGPLYHSAPNAYGLRA--------GRL 220

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  216 GGTIcIPESReiiLDPLRLVHWLEHSRVHVVHCTPSLFrfINHLSLTAD-----SYPDLRYVLLAGETIRPE---SLKNW 287
Cdd:PRK12406  221 GGVL-VLQPR---FDPEELLQLIERHRITHMHMVPTMF--IRLLKLPEEvrakyDVSSLRHVIHAAAPCPADvkrAMIEW 294

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  288 YDNLGNRvrlvnLYGPTETTMIKLfypIKPEDVHRESIPIGRPLPDTSVYLLDEQQQPVSGSEAGEICIATRYMT----H 363
Cdd:PRK12406  295 WGPVIYE-----YYGSTESGAVTF---ATSEDALSHPGTVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAGNPdftyH 366

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517718121  364 GyfpssHPDQTAFIpdpcrDQSGEIMmyrTGDMGRWLPEGELALLGRKDNQVKIRGNRVELGDIEHRLTNMAGIREAVV 442
Cdd:PRK12406  367 N-----KPEKRAEI-----DRGGFIT---SGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAV 432
PPase_ThiI cd01712
pyrophosphatase domain of thiamine biosynthesis protein ThiI; ThiI is required for thiazole ...
 519-626 1.22e-05

pyrophosphatase domain of thiamine biosynthesis protein ThiI; ThiI is required for thiazole synthesis in the thiamine biosynthesis pathway. ThiI is also responsible for the 4-thiouridine (S4U) modification at position 8 in some prokaryotic tRNAs. ThiI contains a PP-loop pyrophosphatase domain which binds ATP and activates tRNA by adenylation. The PP-loop pyrophosphatase catalytic domain of ThiI proteins is always accompanied by a THUMP domain towards the N terminus. THUMP domains are predicted to bind RNA and are widespread in bacteria, archaea, and eukaryotes. The acronym was derived from the names of RNA-modifying enzymes in which this domain is found, namely, thiouridine synthases (ThiI), methylases, and archaeal pseudouridine synthases. ThiI proteins from gamma-proteobacteria and from archaea of the genus Thermoplasma also contain a C-terminal extension of approximately 100 amino acid residues which accepts sulfur in the form of a persulfide on a cysteine residue. This persulfide is responsible for a nucleophilic attack of the adenylated tRNA substrate, completing the sulfur insertion forming a disulfide-bridge between the rhodanese-like domain and a second cysteine residue located in the PP-loop domain. The reaction releases AMP and modified tRNA, and leaves the enzyme in an oxidized state. The disulfide is then reductively cleaved to complete the enzymatic cycle. The pyrophosphatase domain of ThiI belongs to the adenine nucleotide hydrolase (AANH) superfamily and it binds to adenosine nucleotide.


Pssm-ID: 467485 [Multi-domain]  Cd Length: 185  Bit Score: 47.55  E-value: 1.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  519 CLLLYSGGKDSTYALYRLVEMGARVLAYTFDNG-YISSAAFRNIDSVVKELG------VDHIVGTFDGMLDIFKEGLKQE 591
Cdd:cd01712     7 VLVLLSGGIDSPVAAWMMMKRGVEVDFLHFHSGpYTSEKAVEKVKDLARVLSeyqggvKLYLVPFTDKIQKEILEKVPES 86

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 517718121  592 --CSVCNGCFkaMRIlSTRVAAERGIPYIVTGLSRGQ 626
Cdd:cd01712    87 yrIVLMRRMM--YRI-AEKIAERLGADALVTGESLGQ 120
PRK07867 PRK07867
acyl-CoA synthetase; Validated
 18-168 1.54e-05

acyl-CoA synthetase; Validated


Pssm-ID: 236120 [Multi-domain]  Cd Length: 529  Bit Score: 49.29  E-value: 1.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   18 ERKAIECGQQTLSYKELDAESDRICELLHAHGAAQYD-HIGILMqDRCASIAAVIGILKLGG-VFVPLDPLHPDERLVTM 95
Cdd:PRK07867   18 DDRGLYFEDSFTSWREHIRGSAARAAALRARLDPTRPpHVGVLL-DNTPEFSLLLGAAALSGiVPVGLNPTRRGAALARD 96

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 517718121   96 LDTAEVSCLLCDDAQferAETLQGHEGKYFVLRA-----RQAMSVQAGSkEAYSHSANATDPIYIYFTSGSTGKPKAV 168
Cdd:PRK07867   97 IAHADCQLVLTESAH---AELLDGLDPGVRVINVdspawADELAAHRDA-EPPFRVADPDDLFMLIFTSGTSGDPKAV 170
LC-FACS_euk cd05927
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ...
 29-413 1.91e-05

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: 49.14  E-value: 1.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   29 LSYKELDAESDRICELLHAHGA--AQYDHIGILMQDRCASIAAVIGILKLGGVFVPL-DPLHPdERLVTMLDTAEVSCLL 105
Cdd:cd05927     6 ISYKEVAERADNIGSALRSLGGkpAPASFVGIYSINRPEWIISELACYAYSLVTVPLyDTLGP-EAIEYILNHAEISIVF 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  106 CDDA----QFERAETLqghegkyfvlrarqamsvqaGSKEAYSHSANATDPIY-IYFTSGSTGKPKAVVGKNE---SLLH 177
Cdd:cd05927    85 CDAGvkvySLEEFEKL--------------------GKKNKVPPPPPKPEDLAtICYTSGTTGNPKGVMLTHGnivSNVA 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  178 FMNW---EASWLDLTD------PM-----RVSQLT------SIGF----DAVLRD--------IF--VPicaggticipe 223
Cdd:cd05927   145 GVFKileILNKINPTDvyisylPLahifeRVVEALflyhgaKIGFysgdIRLLLDdikalkptVFpgVP----------- 213

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  224 sreiildplRLVHWLeHSRVH-VVHCTPSLFRFI---------NHLS---LTADSYPD--------------LRYVLLAG 276
Cdd:cd05927   214 ---------RVLNRI-YDKIFnKVQAKGPLKRKLfnfalnyklAELRsgvVRASPFWDklvfnkikqalggnVRLMLTGS 283

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  277 ETIRPESLKNWYDNLGnrVRLVNLYGPTETTMIKLFypikpeDVHRESIP--IGRPLPDTSVYLLD--EQQQPVSGSE-A 351
Cdd:cd05927   284 APLSPEVLEFLRVALG--CPVLEGYGQTECTAGATL------TLPGDTSVghVGGPLPCAEVKLVDvpEMNYDAKDPNpR 355

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517718121  352 GEICIATRYMTHGYFpsSHPDQTA--FipdpcrDQSGeimMYRTGDMGRWLPEGELALLGRKDN 413
Cdd:cd05927   356 GEVCIRGPNVFSGYY--KDPEKTAeaL------DEDG---WLHTGDIGEWLPNGTLKIIDRKKN 408
A_NRPS_SidN3_like cd05918
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ...
 809-846 1.94e-05

The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.


Pssm-ID: 341242 [Multi-domain]  Cd Length: 481  Bit Score: 49.08  E-value: 1.94e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 517718121  809 QLSVYLRRFLPDYMIPARFIRLDKMPLTPNGKLDYNAL 846
Cdd:cd05918   436 ELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRAL 473
PRK13391 PRK13391
acyl-CoA synthetase; Provisional
 28-170 4.31e-05

acyl-CoA synthetase; Provisional


Pssm-ID: 184022 [Multi-domain]  Cd Length: 511  Bit Score: 47.76  E-value: 4.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   28 TLSYKELDAESDRICELLHAHGAAQYDHIGILMQDRCASIAAVIGILKLGGVFVPLDP-LHPDErLVTMLDTAEVSCLLC 106
Cdd:PRK13391   24 VVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNShLTPAE-AAYIVDDSGARALIT 102

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517718121  107 DDAQFERAETLQGHegkyfVLRARQAMSVQA-GSKEAYSHSANATD-----PI-------YIYFTSGSTGKPKAVVG 170
Cdd:PRK13391  103 SAAKLDVARALLKQ-----CPGVRHRLVLDGdGELEGFVGYAEAVAglpatPIadeslgtDMLYSSGTTGRPKGIKR 174
PRK06155 PRK06155
crotonobetaine/carnitine-CoA ligase; Provisional
 9-169 5.26e-05

crotonobetaine/carnitine-CoA ligase; Provisional


Pssm-ID: 235719 [Multi-domain]  Cd Length: 542  Bit Score: 47.45  E-value: 5.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121    9 LARAFAAFPERKAIECGQQTLSYKELDAESDRICELLHAHGAAQYDHIGILMQDRCASIAAVIGILKLGGVFVPLDPLHP 88
Cdd:PRK06155   27 LARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALR 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   89 DERLVTMLDTAEVSCLLCDDAQFERAETLQ------------GHEGKYFVLRARQAMSVQAGSKEAYSHSANATDPIYIY 156
Cdd:PRK06155  107 GPQLEHILRNSGARLLVVEAALLAALEAADpgdlplpavwllDAPASVSVPAGWSTAPLPPLDAPAPAAAVQPGDTAAIL 186

                         170
                  ....*....|...
gi 517718121  157 FTSGSTGKPKAVV 169
Cdd:PRK06155  187 YTSGTTGPSKGVC 199
Dph6 COG2102
Diphthamide synthase (EF-2-diphthine--ammonia ligase) [Translation, ribosomal structure and ...
 520-543 5.41e-05

Diphthamide synthase (EF-2-diphthine--ammonia ligase) [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441705  Cd Length: 213  Bit Score: 45.88  E-value: 5.41e-05
                          10        20
                  ....*....|....*....|....
gi 517718121  520 LLLYSGGKDSTYALYRLVEMGARV 543
Cdd:COG2102     2 VVSWSGGKDSALALYRALQEGYEV 25
CTU1-like cd01713
cytoplasmic tRNA 2-thiolation protein 1 and similar proteins; This subfamily includes human ...
 524-621 6.56e-05

cytoplasmic tRNA 2-thiolation protein 1 and similar proteins; This subfamily includes human cytoplasmic tRNA 2-thiolation protein 1, also called cytosolic thiouridylase subunit 1 (CTU1), ATP-binding domain-containing protein 3 (ATPBD3), cancer-associated gene protein, or cytoplasmic tRNA adenylyltransferase 1. CTU1 plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of tRNA(Lys), tRNA(Glu) and tRNA(Gln). It directly binds tRNAs and probably acts by catalyzing adenylation of tRNAs, an intermediate required for 2-thiolation. The CTU1-like subfamily belongs to the nucleotide alpha hydrolase (AANH) superfamily that includes N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group.


Pssm-ID: 467486  Cd Length: 208  Bit Score: 45.66  E-value: 6.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  524 SGGKDST---YALYRLVE---MGARVLAYTFDNGyISsaAFRN--IDSVVK---ELGVDHIVGTFDgmlDIF-------- 584
Cdd:cd01713    26 SGGKDSTvllYVLKELNKrhdYGVELIAVTIDEG-IK--GYRDdsLEAARKlaeEYGIPLEIVSFE---DEFgftldeli 99

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 517718121  585 --KEGLKQECSVCnGCFKaMRILStRVAAERGIPYIVTG 621
Cdd:cd01713   100 vgKGGKKNACTYC-GVFR-RRALN-RGARELGADKLATG 135
LC_FACS_euk1 cd17639
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ...
 269-428 7.09e-05

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: 47.21  E-value: 7.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  269 LRYVLLAGETIRPESlKNWYDNLGNRVrlVNLYGPTETT--MIKLFypikPEDVhrESIPIGRPLPDTSVYLLDEQQ--- 343
Cdd:cd17639   252 LRYMLSGGAPLSADT-QEFLNIVLCPV--IQGYGLTETCagGTVQD----PGDL--ETGRVGPPLPCCEIKLVDWEEggy 322

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  344 QPVSGSEAGEICIATRYMTHGYFpsSHPDQT--AFIPDpcrdqsgeiMMYRTGDMGRWLPEGELALLGRKDNQVKIR-GN 420
Cdd:cd17639   323 STDKPPPRGEILIRGPNVFKGYY--KNPEKTkeAFDGD---------GWFHTGDIGEFHPDGTLKIIDRKKDLVKLQnGE 391


                  ....*...
gi 517718121  421 RVELGDIE 428
Cdd:cd17639   392 YIALEKLE 399
LarE-like cd01990
Lactate racemization operon protein LarE and similar proteins; This subfamily includes ...
 523-621 8.57e-05

Lactate racemization operon protein LarE and similar proteins; This subfamily includes Lactiplantibacillus plantarum LarE, a sacrificial sulfur insertase of the N-type ATP pyrophosphatase family. LarE is part of the lar operon, encoding five Lar proteins (LarA-E) that collaboratively synthesize and incorporate a niacin-derived Ni-containing cofactor into LarA, an Ni-dependent lactate racemase. It catalyzes successive thiolation reactions by donating the sulfur atom of their exclusive cysteine residues to the substrate. The LarE-like subfamily belongs to the nucleotide alpha hydrolase (AANH) superfamily that includes N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group. Proteins from this subfamily probably binds ATP. This domain is about 200 amino acids long with a strongly conserved motif SGGxDS at the N-terminus.


Pssm-ID: 467494 [Multi-domain]  Cd Length: 222  Bit Score: 45.33  E-value: 8.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  523 YSGGKDSTYALYRLVE-MGARVLAYTFDNGYISSAAFRNIDSVVKELGVDHIVGTFDGMLD-IFKEGLKQECSVCngcfK 600
Cdd:cd01990     6 FSGGVDSSLLAKLAKEvLGDNVVAVTADSPLVPREELEEAKRIAEEIGIRHEIIKTDELDDeEYVANDPDRCYHC----K 81

                          90       100
                  ....*....|....*....|...
gi 517718121  601 AMrILST--RVAAERGIPYIVTG 621
Cdd:cd01990    82 KA-LYSTlkEIAKERGYDVVLDG 103
PRK08349 PRK08349
hypothetical protein; Validated
 522-627 1.06e-04

hypothetical protein; Validated


Pssm-ID: 169396  Cd Length: 198  Bit Score: 44.73  E-value: 1.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  522 LYSGGKDSTYALYRLVEMGARVLAYTFDNGYISSAAFRNIDSVVKELGVD-----HIVGTFDGMLDIFkEGLKQECS--- 593
Cdd:PRK08349    6 LLSSGIDSPVAIYLMLRRGVEVYPVHFRQDEKKEEKVRELVERLQELHGGklkdpVVVDAFEEQGPVF-EKLRELKKekw 84

                          90       100       110
                  ....*....|....*....|....*....|....
gi 517718121  594 VCNGCFKAMRILSTRVAAERGIPYIVTGLSRGQI 627
Cdd:PRK08349   85 TCIFCKYTMYRKAERIAHEIGASAIITGDSLGQV 118
TilS COG0037
tRNA(Ile)-lysidine synthase TilS/MesJ [Translation, ribosomal structure and biogenesis]; tRNA ...
 514-621 1.13e-04

tRNA(Ile)-lysidine synthase TilS/MesJ [Translation, ribosomal structure and biogenesis]; tRNA(Ile)-lysidine synthase TilS/MesJ is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 439807 [Multi-domain]  Cd Length: 235  Bit Score: 45.21  E-value: 1.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  514 QPSYDCLLLYSGGKDST---YALYRLV-EMGARVLAYTFDNGYISSAAF--RNIDSVVKELGVDHIVGTFDGMLDIFKEG 587
Cdd:COG0037    13 EPGDRILVAVSGGKDSLallHLLAKLRrRLGFELVAVHVDHGLREESDEdaEFVAELCEELGIPLHVVRVDVPAIAKKEG 92

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 517718121  588 LkqecSVCNGC----FKAMRilstRVAAERGIPYIVTG 621
Cdd:COG0037    93 K----SPEAAArrarYGALY----ELARELGADKIATG 122
PRK08162 PRK08162
acyl-CoA synthetase; Validated
 9-169 1.41e-04

acyl-CoA synthetase; Validated


Pssm-ID: 236169 [Multi-domain]  Cd Length: 545  Bit Score: 46.09  E-value: 1.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121    9 LARAFAAFPERKAIECGQQTLSYKELDAESDRICELLHAHGAAQYDHIGILMQDRCASIAAVIGILKLGGVF----VPLD 84
Cdd:PRK08162   24 LERAAEVYPDRPAVIHGDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLntlnTRLD 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   85 PlhpdERLVTMLDTAEVSCLLCD-------------------------DAQFERAETLQGHEGKYFVlrarqamsvQAGS 139
Cdd:PRK08162  104 A----ASIAFMLRHGEAKVLIVDtefaevarealallpgpkplvidvdDPEYPGGRFIGALDYEAFL---------ASGD 170

                         170       180       190
                  ....*....|....*....|....*....|.
gi 517718121  140 KE-AYSHSANATDPIYIYFTSGSTGKPKAVV 169
Cdd:PRK08162  171 PDfAWTLPADEWDAIALNYTSGTTGNPKGVV 201
entE PRK10946
(2,3-dihydroxybenzoyl)adenylate synthase;
328-431 1.43e-04

(2,3-dihydroxybenzoyl)adenylate synthase;


Pssm-ID: 236803 [Multi-domain]  Cd Length: 536  Bit Score: 46.14  E-value: 1.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  328 GRPL-PDTSVYLLDEQQQPVSGSEAGEicIATR--YMTHGYFPSSHPDQTAFipdpcrDQSGeimMYRTGDMGRWLPEGE 404
Cdd:PRK10946  356 GRPMsPDDEVWVADADGNPLPQGEVGR--LMTRgpYTFRGYYKSPQHNASAF------DANG---FYCSGDLVSIDPDGY 424

                          90       100
                  ....*....|....*....|....*..
gi 517718121  405 LALLGRKDNQVKIRGNRVELGDIEHRL 431
Cdd:PRK10946  425 ITVVGREKDQINRGGEKIAAEEIENLL 451
PLN02614 PLN02614
long-chain acyl-CoA synthetase
 327-509 1.44e-04

long-chain acyl-CoA synthetase


Pssm-ID: 166255 [Multi-domain]  Cd Length: 666  Bit Score: 46.17  E-value: 1.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  327 IGRPLPDTSVYL--LDEQQQPVSGSEA-GEICIATRYMTHGYFPSSHPDQTAFIPDpcrdqsgeimMYRTGDMGRWLPEG 403
Cdd:PLN02614  441 VGPPVPNVDIRLesVPEMEYDALASTPrGEICIRGKTLFSGYYKREDLTKEVLIDG----------WLHTGDVGEWQPNG 510

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  404 ELALLGRKDNQVKI-RGNRVELGDIEHRLTNMAGIREAVVR-------MRAKADTPKGMAQQHCAACGLPSTYPGISFDD 475
Cdd:PLN02614  511 SMKIIDRKKNIFKLsQGEYVAVENIENIYGEVQAVDSVWVYgnsfesfLVAIANPNQQILERWAAENGVSGDYNALCQNE 590

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 517718121  476 MGKCSVCTgqEQYRSAAEQYFQGMEQLQS-KLQPV 509
Cdd:PLN02614  591 KAKEFILG--ELVKMAKEKKMKGFEIIKAiHLDPV 623
A_NRPS_TlmIV_like cd12114
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ...
 783-846 1.77e-04

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: 45.72  E-value: 1.77e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517718121  783 VQLQVEEAQEPLLIAYYLADKMID-DEQLSVYLRR--FLPDYMIPARFIRLDKMPLTPNGKLDYNAL 846
Cdd:cd12114   411 VVVVLGDPGGKRLAAFVVPDNDGTpIAPDALRAFLaqTLPAYMIPSRVIALEALPLTANGKVDRAAL 477
QueC pfam06508
Queuosine biosynthesis protein QueC; This family of proteins participate in the biosynthesis ...
 519-574 2.16e-04

Queuosine biosynthesis protein QueC; This family of proteins participate in the biosynthesis of 7-carboxy-7-deazaguanine. They catalyze the conversion of 7-deaza-7-carboxyguanine to preQ0.


Pssm-ID: 428982 [Multi-domain]  Cd Length: 210  Bit Score: 44.15  E-value: 2.16e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 517718121   519 CLLLYSGGKDSTYALYRLVEMGARVLAYTFDNGYISSAAFRNIDSVVKELGVDHIV 574
Cdd:pfam06508    2 AVVLLSGGLDSTTCLAWAKKEGYEVYALSFDYGQRHRKELECAKKIAKALGVEHKI 57
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
 870-935 2.16e-04

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: 41.47  E-value: 2.16e-04
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517718121    870 LLDIWTHILGI---KRISADDHFLQIGVHSLNIMTLIAQVYENFQVELPLEQVFEHDTLEEIAAYIDEQ 935
Cdd:smart00823   17 VREQVAAVLGHaaaEAIDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAEHLAAE 85
FACL_like_6 cd05922
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ...
 795-846 4.15e-04

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: 44.74  E-value: 4.15e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 517718121  795 LIAYYLADKMIDDEQLSVYLRRFLPDYMIPARFIRLDKMPLTPNGKLDYNAL 846
Cdd:cd05922   405 LALFVTAPDKIDPKDVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAAL 456
PRK12492 PRK12492
long-chain-fatty-acid--CoA ligase; Provisional
 296-428 5.11e-04

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


Pssm-ID: 171539 [Multi-domain]  Cd Length: 562  Bit Score: 44.43  E-value: 5.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  296 RLVNLYGPTETTMIKlfyPIKPEDVHRESIPIGRPLPDTSVYLLDEQQQPVSGSEAGEICIATRYMTHGYFpsSHPDQTA 375
Cdd:PRK12492  360 TIVEGYGLTETSPVA---STNPYGELARLGTVGIPVPGTALKVIDDDGNELPLGERGELCIKGPQVMKGYW--QQPEATA 434

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 517718121  376 fipdPCRDQSGeimMYRTGDMGRWLPEGELALLGRKDNQVKIRGNRVELGDIE 428
Cdd:PRK12492  435 ----EALDAEG---WFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIE 480
OSB_CoA_lg cd05912
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ...
 796-846 5.64e-04

O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.


Pssm-ID: 341238 [Multi-domain]  Cd Length: 411  Bit Score: 43.87  E-value: 5.64e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 517718121  796 IAYYLADKMIDDEQLSVYLRRFLPDYMIPARFIRLDKMPLTPNGKLDYNAL 846
Cdd:cd05912   359 VAFVVSERPISEEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHEL 409
AANH-like cd01986
adenine nucleotide alpha hydrolase (AANH)-like proteins; This group of adenine nucleotide ...
 519-577 6.22e-04

adenine nucleotide alpha hydrolase (AANH)-like proteins; This group of adenine nucleotide alpha hydrolase (AANH)-like proteins includes N-type ATP PPases and ATP sulfurylases. The domain forms an alpha/beta/alpha fold which binds to adenosine nucleotide.


Pssm-ID: 467490 [Multi-domain]  Cd Length: 74  Bit Score: 39.74  E-value: 6.22e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 517718121  519 CLLLYSGGKDSTYALYRLVE--MGARVLAYTFDNGY--------ISSAAFRNIDSVVKELGVDHIVGTF 577
Cdd:cd01986     1 VVVGYSGGKDSSVALHLASRlgRKAEVAVVHIDHGIgfkeeaesVASIARRSILKKLAEKGARAIATGV 69
ThiI pfam02568
Thiamine biosynthesis protein (ThiI); ThiI is required for thiazole synthesis, required for ...
 518-627 1.09e-03

Thiamine biosynthesis protein (ThiI); ThiI is required for thiazole synthesis, required for thiamine biosynthesis.


Pssm-ID: 280691 [Multi-domain]  Cd Length: 197  Bit Score: 41.65  E-value: 1.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   518 DCLLLYSGGKDSTYALYRLVEMGARVLAYTFDNGYISSAAFRN----IDSVVKELGVDH----IVGTFDGMLDIFKEGL- 588
Cdd:pfam02568    5 KVLALISGGIDSPVAAYMMMRRGCRVVALHFINNPGTSAEAIGkvqkLAELLARYGTSHevrlVVFDFTDVQKEILEKAp 84

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 517718121   589 -KQECSVCNGCFkaMRILStRVAAERGIPYIVTGLSRGQI 627
Cdd:pfam02568   85 eGYRCVLLKRCM--YRIAE-KVAEEEGADALVTGESLGQV 121
PRK07868 PRK07868
acyl-CoA synthetase; Validated
 30-120 1.22e-03

acyl-CoA synthetase; Validated


Pssm-ID: 236121 [Multi-domain]  Cd Length: 994  Bit Score: 43.55  E-value: 1.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   30 SYKELDAESDRICELLHAHGAAQYDHIGILMQDRCASIAAVIGILKLGGVFVpldPLHPDERLVTMLDTAEVSCLLCDDA 109
Cdd:PRK07868  474 TYEAVNRRINNVVRGLIAVGVRQGDRVGVLMETRPSALVAIAALSRLGAVAV---LMPPDTDLAAAVRLGGVTEIITDPT 550

                          90
                  ....*....|.
gi 517718121  110 QFERAETLQGH 120
Cdd:PRK07868  551 NLEAARQLPGR 561
LC_FACS_bac cd05932
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ...
 272-458 1.28e-03

Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.


Pssm-ID: 341255 [Multi-domain]  Cd Length: 508  Bit Score: 43.23  E-value: 1.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  272 VLLAGETIRPESLKNWYDNLGnrVRLVNLYGPTETTMIK-LFYPIKpedvhRESIPIGRPLPDTSVYLldeqqqpvsgSE 350
Cdd:cd05932   279 LAGCGSAPVPPALLEWYRSLG--LNILEAYGMTENFAYShLNYPGR-----DKIGTVGNAGPGVEVRI----------SE 341

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  351 AGEICIATRYMTHGYFpsSHPDQTA--FIPDPcrdqsgeimMYRTGDMGRWLPEGELALLGR-KDNQVKIRGNRVELGDI 427
Cdd:cd05932   342 DGEILVRSPALMMGYY--KDPEATAeaFTADG---------FLRTGDKGELDADGNLTITGRvKDIFKTSKGKYVAPAPI 410

                         170       180       190
                  ....*....|....*....|....*....|.
gi 517718121  428 EHRLTNMAGIrEAVVRMRAKADTPKGMAQQH 458
Cdd:cd05932   411 ENKLAEHDRV-EMVCVIGSGLPAPLALVVLS 440
COG1365 COG1365
Predicted ATPase, PP-loop superfamily [General function prediction only];
523-625 1.41e-03

Predicted ATPase, PP-loop superfamily [General function prediction only];


Pssm-ID: 440976  Cd Length: 256  Bit Score: 41.96  E-value: 1.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  523 YSGGKDSTYALYRLVEMGARVLAYTFDNGYISSAAFR-NIDSVVKELGVDHIVGTFDgMLDIFKEGLKQECSVCNGCFKA 601
Cdd:COG1365    67 FSGGVDSSASLIIAKWIGFDVEAVTVKSTIILPQMFKkNIKELCKKLNVKHEFIEID-LGEIIEDALKGKFHPCGRCHSL 145

                          90       100
                  ....*....|....*....|....*.
gi 517718121  602 MRILSTRVAAERGIPYIVTG--LSRG 625
Cdd:COG1365   146 IEEAVEDYAKKNGIKIVIFGdlLSVG 171
PRK08315 PRK08315
AMP-binding domain protein; Validated
 4-168 1.55e-03

AMP-binding domain protein; Validated


Pssm-ID: 236236 [Multi-domain]  Cd Length: 559  Bit Score: 42.88  E-value: 1.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121    4 TIQYELARAFAAFPERKAI-ECGQQT-LSYKELDAESDRICELLHAHGAAQYDHIGI---------LMQDRCAsiaavig 72
Cdd:PRK08315   17 TIGQLLDRTAARYPDREALvYRDQGLrWTYREFNEEVDALAKGLLALGIEKGDRVGIwapnvpewvLTQFATA------- 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121   73 ilKLGGVFVPLDPLHPDERLVTMLDTAEVSCLLCDDA-------------------------QFERAETL--------QG 119
Cdd:PRK08315   90 --KIGAILVTINPAYRLSELEYALNQSGCKALIAADGfkdsdyvamlyelapelatcepgqlQSARLPELrrviflgdEK 167

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 517718121  120 HEGKYFV--LRARqAMSVQAGSKEAYSHSANATDPIYIYFTSGSTGKPKAV 168
Cdd:PRK08315  168 HPGMLNFdeLLAL-GRAVDDAELAARQATLDPDDPINIQYTSGTTGFPKGA 217
PLN02387 PLN02387
long-chain-fatty-acid-CoA ligase family protein
 301-432 1.55e-03

long-chain-fatty-acid-CoA ligase family protein


Pssm-ID: 215217 [Multi-domain]  Cd Length: 696  Bit Score: 42.80  E-value: 1.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  301 YGPTETTMIKLFYPIKPEDVHResipIGRPLPDTSVYLLDEQQQPVSGSEA----GEICIATRYMTHGYFPSSHPDQTAF 376
Cdd:PLN02387  452 YGLTETCAGATFSEWDDTSVGR----VGPPLPCCYVKLVSWEEGGYLISDKpmprGEIVIGGPSVTLGYFKNQEKTDEVY 527

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 517718121  377 IPDpcrdQSGEIMMYrTGDMGRWLPEGELALLGRKDNQVKIR-GNRVELGDIEHRLT 432
Cdd:PLN02387  528 KVD----ERGMRWFY-TGDIGQFHPDGCLEIIDRKKDIVKLQhGEYVSLGKVEAALS 579
PRK00174 PRK00174
acetyl-CoA synthetase; Provisional
 148-169 1.62e-03

acetyl-CoA synthetase; Provisional


Pssm-ID: 234677 [Multi-domain]  Cd Length: 637  Bit Score: 42.82  E-value: 1.62e-03
                          10        20
                  ....*....|....*....|..
gi 517718121  148 NATDPIYIYFTSGSTGKPKAVV 169
Cdd:PRK00174  243 DAEDPLFILYTSGSTGKPKGVL 264
PRK08576 PRK08576
hypothetical protein; Provisional
 491-588 2.96e-03

hypothetical protein; Provisional


Pssm-ID: 236300 [Multi-domain]  Cd Length: 438  Bit Score: 41.60  E-value: 2.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  491 AAEQYFQGMEQLQSKLQPVEKEnqpsYDCLLLYSGGKDSTYALYRLVEMGARVLAYTFDNGYISSAAFRNIDSVVKELGV 570
Cdd:PRK08576  213 ANREVLEAFEKASIKFLRKFEE----WTVIVPWSGGKDSTAALLLAKKAFGDVTAVYVDTGYEMPLTDEYVEKVAEKLGV 288

                          90
                  ....*....|....*...
gi 517718121  571 DHIVGTFDGMLDIFKEGL 588
Cdd:PRK08576  289 DLIRAGVDVPMPIEKYGM 306
QueC-like cd01995
7-cyano-7-deazaguanine synthase QueC and similar proteins; 7-cyano-7-deazaguanine synthase (EC ...
 519-588 3.13e-03

7-cyano-7-deazaguanine synthase QueC and similar proteins; 7-cyano-7-deazaguanine synthase (EC 6.3.4.20) is also called 7-cyano-7-carbaguanine synthase, preQ(0) synthase, or queuosine biosynthesis protein QueC. It catalyzes the ATP-dependent conversion of 7-carboxy-7-deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)), as part of the biosynthesis pathway of queuosine (Q). Q is one of the most complex modifications occurring at the wobble position of tRNAs with GUN anticodons, and is implicated in a number of biological activities, including accuracy of decoding, virulence, and cellular differentiation. This subfamily belongs to the adenine nucleotide alpha hydrolase (AANH) superfamily that also includes other N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group.


Pssm-ID: 467499 [Multi-domain]  Cd Length: 208  Bit Score: 40.67  E-value: 3.13e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517718121  519 CLLLYSGGKDSTYALYRLVEMGARVLAYTFDNGYISSA----AFRNIDsvvKELGVDHIVGTFDGMLDIFKEGL 588
Cdd:cd01995     3 AVVLLSGGLDSTTLLYWALKEGYEVHALTFDYGQRHAKeeleAAKLIA---KLLGIEHKVIDLSFLGELGGSSL 73
mnmA PRK14665
tRNA-specific 2-thiouridylase MnmA; Provisional
 520-621 3.17e-03

tRNA-specific 2-thiouridylase MnmA; Provisional


Pssm-ID: 173128 [Multi-domain]  Cd Length: 360  Bit Score: 41.46  E-value: 3.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  520 LLLYSGGKDSTYALYRLVEMGARVLAYTF-------DNGYISSAAfrnidSVVKELGVDHIvgTFDGMlDIFKEGLKQ-- 590
Cdd:PRK14665    9 LLGMSGGTDSSVAAMLLLEAGYEVTGVTFrfyefngSTEYLEDAR-----ALAERLGIGHI--TYDAR-KVFRKQIIDyf 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 517718121  591 -----------ECSVCNGCFKAMriLSTRVAAERGIPYIVTG 621
Cdd:PRK14665   81 ideymsghtpvPCTLCNNYLKWP--LLAKIADEMGIFYLATG 120
TIGR00364 TIGR00364
queuosine biosynthesis protein QueC; Members of this protein family are QueC, involved in ...
 519-574 3.80e-03

queuosine biosynthesis protein QueC; Members of this protein family are QueC, involved in synthesizing pre-Q0 from GTP en route to tRNA modification with queuosine. This protein family is represented by a single member in nearly every completed large (> 1000 genes) prokaryotic genome. In Rhizobium meliloti, the gene was designated exsB, possibly because of polar effects on exsA expression in a shared polycistronic mRNA. In Arthrobacter viscosus, the homologous gene was designated ALU1 and was associated with an aluminum tolerance phenotype. [Unknown function, General]


Pssm-ID: 129461 [Multi-domain]  Cd Length: 201  Bit Score: 40.07  E-value: 3.80e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 517718121   519 CLLLYSGGKDSTYALYRLVEMGARVLAYTFDNGYISSAAFRNIDSVVKELGVDHIV 574
Cdd:TIGR00364    1 AIVVLSGGQDSTTCLLWAKDEGYEVHAVTFDYGQRHSRELESARKIAEALGIEHHL 56
FACL_fum10p_like cd05926
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ...
 801-846 4.82e-03

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: 41.14  E-value: 4.82e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 517718121  801 ADKMIDDEQLSVYLRRFLPDYMIPARFIRLDKMPLTPNGKLDYNAL 846
Cdd:cd05926   446 EGASVTEEELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKV 491
PRK09192 PRK09192
fatty acyl-AMP ligase;
328-428 5.15e-03

fatty acyl-AMP ligase;


Pssm-ID: 236403 [Multi-domain]  Cd Length: 579  Bit Score: 41.14  E-value: 5.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  328 GRPLPDTSVYLLDEQQQPVSGSEAGEICIATRYMTHGYFpsshpdqtafipdpcRDQ-SGEIMM----YRTGDMGrWLPE 402
Cdd:PRK09192  388 GKALPGHEIEIRNEAGMPLPERVVGHICVRGPSLMSGYF---------------RDEeSQDVLAadgwLDTGDLG-YLLD 451

                          90       100
                  ....*....|....*....|....*.
gi 517718121  403 GELALLGRKDNQVKIRGNRVELGDIE 428
Cdd:PRK09192  452 GYLYITGRAKDLIIINGRNIWPQDIE 477
PRK07529 PRK07529
AMP-binding domain protein; Validated
 295-470 5.88e-03

AMP-binding domain protein; Validated


Pssm-ID: 236043 [Multi-domain]  Cd Length: 632  Bit Score: 41.09  E-value: 5.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  295 VRLVNLYGPTETTMIKlfyPIKPEDVHRESIPIGRPLP--DTSVYLLDEQ---QQPVSGSEAGEICIATRYMTHGYFPSS 369
Cdd:PRK07529  359 VRIVEGYGLTEATCVS---SVNPPDGERRIGSVGLRLPyqRVRVVILDDAgryLRDCAVDEVGVLCIAGPNVFSGYLEAA 435

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517718121  370 HpDQTAFIPDpcrdqsgeiMMYRTGDMGRWLPEGELALLGR-KDnqVKIRGNrvelgdieHrltNM--AGIREAVVRMra 446
Cdd:PRK07529  436 H-NKGLWLED---------GWLNTGDLGRIDADGYFWLTGRaKD--LIIRGG--------H---NIdpAAIEEALLRH-- 490

                         170       180
                  ....*....|....*....|....
gi 517718121  447 kadtPkgmAQQHCAACGLPSTYPG 470
Cdd:PRK07529  491 ----P---AVALAAAVGRPDAHAG 507
AMP-binding_C pfam13193
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ...
 808-840 6.00e-03

AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.


Pssm-ID: 463804 [Multi-domain]  Cd Length: 76  Bit Score: 37.14  E-value: 6.00e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 517718121   808 EQLSVYLRRFLPDYMIPARFIRLDKMPLTPNGK 840
Cdd:pfam13193   44 EELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
OSB_MenE-like cd17630
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ...
 795-846 6.87e-03

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: 40.39  E-value: 6.87e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 517718121  795 LIAYYLADKMIDDEQLSVYLRRFLPDYMIPARFIRLDKMPLTPNGKLDYNAL 846
Cdd:cd17630   270 PVAVIVGRGPADPAELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRAL 321
QueC COG0603
7-cyano-7-deazaguanine synthase (queuosine biosynthesis) [Translation, ribosomal structure and ...
 520-583 9.44e-03

7-cyano-7-deazaguanine synthase (queuosine biosynthesis) [Translation, ribosomal structure and biogenesis]; 7-cyano-7-deazaguanine synthase (queuosine biosynthesis) is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440368 [Multi-domain]  Cd Length: 223  Bit Score: 39.37  E-value: 9.44e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 517718121  520 LLLYSGGKDSTYALYRLVEMGARVLAYTFDngY-------ISSAAfrnidSVVKELGV-DHIVGTFDGMLDI 583
Cdd:COG0603     6 VVLLSGGLDSTTCLAWALARGYEVYALSFD--YgqrhrkeLEAAR-----RIAKALGVgEHKVIDLDFLGEI 70
AFD_YhfT-like cd17633
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ...
 794-842 9.53e-03

fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain


Pssm-ID: 341288 [Multi-domain]  Cd Length: 320  Bit Score: 39.70  E-value: 9.53e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 517718121  794 LLIAYYLADKmIDDEQLSVYLRRFLPDYMIPARFIRLDKMPLTPNGKLD 842
Cdd:cd17633   272 IAVALYSGDK-LTYKQLKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKIA 319
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH