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Conserved domains on  [gi|2679228985|ref|WP_333519569|]
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condensation domain-containing protein, partial [Bacillus sp. 0102A]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
C_NRPS-like super family cl40425
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ...
 59-202 1.47e-60

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.


The actual alignment was detected with superfamily member cd19531:

Pssm-ID: 394795 [Multi-domain]  Cd Length: 427  Bit Score: 194.50  E-value: 1.47e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2679228985  59 TYPVSSAQKRIYVLQQLEDGGTGYNMPAVLELEGKLDPERLDRAFQELIKRHESLRTSFEQdEGGEPVQRIHDEVPFTLQ 138
Cdd:cd19531     1 PLPLSFAQQRLWFLDQLEPGSAAYNIPGALRLRGPLDVAALERALNELVARHEALRTTFVE-VDGEPVQVILPPLPLPLP 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2679228985 139 ----TAVLGEQTEQEA---AAAFI-QPFDLTQALLFRAQIVQVSDERHLLLVDMHHMISDGVSVNILIREFG 202
Cdd:cd19531    80 vvdlSGLPEAEREAEAqrlAREEArRPFDLARGPLLRATLLRLGEDEHVLLLTMHHIVSDGWSMGVLLRELA 151
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
 1-42 7.42e-08

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


:

Pssm-ID: 440006 [Multi-domain]  Cd Length: 80  Bit Score: 47.93  E-value: 7.42e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2679228985   1 GGHSLKATALVSRIAKEFDVQVPLKDVFAHPTVEGLASVIRE 42
Cdd:COG0236    36 GLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLEE 77
 
Name Accession Description Interval E-value
LCL_NRPS-like cd19531
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ...
 59-202 1.47e-60

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: 194.50  E-value: 1.47e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2679228985  59 TYPVSSAQKRIYVLQQLEDGGTGYNMPAVLELEGKLDPERLDRAFQELIKRHESLRTSFEQdEGGEPVQRIHDEVPFTLQ 138
Cdd:cd19531     1 PLPLSFAQQRLWFLDQLEPGSAAYNIPGALRLRGPLDVAALERALNELVARHEALRTTFVE-VDGEPVQVILPPLPLPLP 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2679228985 139 ----TAVLGEQTEQEA---AAAFI-QPFDLTQALLFRAQIVQVSDERHLLLVDMHHMISDGVSVNILIREFG 202
Cdd:cd19531    80 vvdlSGLPEAEREAEAqrlAREEArRPFDLARGPLLRATLLRLGEDEHVLLLTMHHIVSDGWSMGVLLRELA 151
Condensation pfam00668
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ...
 56-203 6.97e-58

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: 188.31  E-value: 6.97e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2679228985  56 QRETYPVSSAQKRIYVLQQLEDGGTGYNMPAVLELEGKLDPERLDRAFQELIKRHESLRTSFEQDEGGEPVQRIHDEVPF 135
Cdd:pfam00668   1 VQDEYPLSPAQKRMWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIRQENGEPVQVILEERPF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2679228985 136 TLQTAVLG---EQTEQEAAAAFIQ-----PFDLTQALLFRAQIVQVSDERHLLLVDMHHMISDGVSVNILIREFGD 203
Cdd:pfam00668  81 ELEIIDISdlsESEEEEAIEAFIQrdlqsPFDLEKGPLFRAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLAD 156
COG4908 COG4908
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ...
 62-203 2.37e-48

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


Pssm-ID: 443936 [Multi-domain]  Cd Length: 243  Bit Score: 157.89  E-value: 2.37e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2679228985  62 VSSAQKRIYVLqqlEDGGTGYNMPAVLELEGKLDPERLDRAFQELIKRHESLRTSFEQDEGgEPVQRIHDEVPFTLQTAV 141
Cdd:COG4908     1 LSPAQKRFLFL---EPGSNAYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFVEEDG-EPVQRIDPDADLPLEVVD 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2679228985 142 L-------GEQTEQEAAAAFIQ-PFDLTQALLFRAQIVQVSDERHLLLVDMHHMISDGVSVNILIREFGD 203
Cdd:COG4908    77 LsalpepeREAELEELVAEEASrPFDLARGPLLRAALIRLGEDEHVLLLTIHHIISDGWSLGILLRELAA 146
PRK12467 PRK12467
peptide synthase; Provisional
 1-201 8.08e-47

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 164.56  E-value: 8.08e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2679228985    1 GGHSLKATALVSRIAKEFDVQVPLKDVFAHPTVEGLASVIREGTDSPYEAMKPAEQRETYPVSSAQKRIYVLQQLEDGGT 80
Cdd:PRK12467  1058 GGHSLLATQVISRVRQRLGIQVPLRTLFEHQTLAGFAQAVAAQQQGAQPALPDVDRDQPLPLSYAQERQWFLWQLEPGSA 1137

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2679228985   81 GYNMPAVLELEGKLDPERLDRAFQELIKRHESLRTSFEQdEGGEPVQRIHDEVPFTLQTAVLGEQTEQEAA-AAFI---- 155
Cdd:PRK12467  1138 AYHIPQALRLKGPLDIEALERSFDALVARHESLRTTFVQ-EDGRTRQVIHPVGSLTLEEPLLLAADKDEAQlKVYVeaea 1216

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 2679228985  156 -QPFDLTQALLFRAQIVQVSDERHLLLVDMHHMISDGVSVNILIREF 201
Cdd:PRK12467  1217 rQPFDLEQGPLLRVGLLRLAADEHVLVLTLHHIVSDGWSMQVLVDEL 1263
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
 1-42 7.42e-08

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


Pssm-ID: 440006 [Multi-domain]  Cd Length: 80  Bit Score: 47.93  E-value: 7.42e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2679228985   1 GGHSLKATALVSRIAKEFDVQVPLKDVFAHPTVEGLASVIRE 42
Cdd:COG0236    36 GLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLEE 77
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
 1-34 3.69e-06

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: 42.94  E-value: 3.69e-06
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2679228985   1 GGHSLKATALVSRIAKEFDVQVPLKDVFAHPTVE 34
Cdd:pfam00550  28 GLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLA 61
alpha_am_amid TIGR03443
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ...
 1-40 2.14e-05

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


Pssm-ID: 274582 [Multi-domain]  Cd Length: 1389  Bit Score: 44.67  E-value: 2.14e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 2679228985    1 GGHSLKATALVSRIAKEFDVQVPLKDVFAHPTVEGLASVI 40
Cdd:TIGR03443  878 GGHSILATRMIFELRKKLNVELPLGLIFKSPTIKGFAKEV 917
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
1-45 3.62e-05

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 43.88  E-value: 3.62e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 2679228985    1 GGHSLKATALVSRIAKEFDVQVPLKDVFAHPTVEGLASVIREGTD 45
Cdd:PRK10252  1006 GGHSLLAMKLAAQLSRQFARQVTPGQVMVASTVAKLATLLDAEED 1050
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
 1-42 3.68e-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: 38.00  E-value: 3.68e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 2679228985    1 GGHSLKATALVSRIAKEFDVQVPLKDVFAHPTVEGLASVIRE 42
Cdd:smart00823  43 GLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAEHLAA 84
 
Name Accession Description Interval E-value
LCL_NRPS-like cd19531
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ...
 59-202 1.47e-60

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: 194.50  E-value: 1.47e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2679228985  59 TYPVSSAQKRIYVLQQLEDGGTGYNMPAVLELEGKLDPERLDRAFQELIKRHESLRTSFEQdEGGEPVQRIHDEVPFTLQ 138
Cdd:cd19531     1 PLPLSFAQQRLWFLDQLEPGSAAYNIPGALRLRGPLDVAALERALNELVARHEALRTTFVE-VDGEPVQVILPPLPLPLP 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2679228985 139 ----TAVLGEQTEQEA---AAAFI-QPFDLTQALLFRAQIVQVSDERHLLLVDMHHMISDGVSVNILIREFG 202
Cdd:cd19531    80 vvdlSGLPEAEREAEAqrlAREEArRPFDLARGPLLRATLLRLGEDEHVLLLTMHHIVSDGWSMGVLLRELA 151
Condensation pfam00668
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ...
 56-203 6.97e-58

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: 188.31  E-value: 6.97e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2679228985  56 QRETYPVSSAQKRIYVLQQLEDGGTGYNMPAVLELEGKLDPERLDRAFQELIKRHESLRTSFEQDEGGEPVQRIHDEVPF 135
Cdd:pfam00668   1 VQDEYPLSPAQKRMWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIRQENGEPVQVILEERPF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2679228985 136 TLQTAVLG---EQTEQEAAAAFIQ-----PFDLTQALLFRAQIVQVSDERHLLLVDMHHMISDGVSVNILIREFGD 203
Cdd:pfam00668  81 ELEIIDISdlsESEEEEAIEAFIQrdlqsPFDLEKGPLFRAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLAD 156
COG4908 COG4908
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ...
 62-203 2.37e-48

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


Pssm-ID: 443936 [Multi-domain]  Cd Length: 243  Bit Score: 157.89  E-value: 2.37e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2679228985  62 VSSAQKRIYVLqqlEDGGTGYNMPAVLELEGKLDPERLDRAFQELIKRHESLRTSFEQDEGgEPVQRIHDEVPFTLQTAV 141
Cdd:COG4908     1 LSPAQKRFLFL---EPGSNAYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFVEEDG-EPVQRIDPDADLPLEVVD 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2679228985 142 L-------GEQTEQEAAAAFIQ-PFDLTQALLFRAQIVQVSDERHLLLVDMHHMISDGVSVNILIREFGD 203
Cdd:COG4908    77 LsalpepeREAELEELVAEEASrPFDLARGPLLRAALIRLGEDEHVLLLTIHHIISDGWSLGILLRELAA 146
PRK12467 PRK12467
peptide synthase; Provisional
 1-201 8.08e-47

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 164.56  E-value: 8.08e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2679228985    1 GGHSLKATALVSRIAKEFDVQVPLKDVFAHPTVEGLASVIREGTDSPYEAMKPAEQRETYPVSSAQKRIYVLQQLEDGGT 80
Cdd:PRK12467  1058 GGHSLLATQVISRVRQRLGIQVPLRTLFEHQTLAGFAQAVAAQQQGAQPALPDVDRDQPLPLSYAQERQWFLWQLEPGSA 1137

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2679228985   81 GYNMPAVLELEGKLDPERLDRAFQELIKRHESLRTSFEQdEGGEPVQRIHDEVPFTLQTAVLGEQTEQEAA-AAFI---- 155
Cdd:PRK12467  1138 AYHIPQALRLKGPLDIEALERSFDALVARHESLRTTFVQ-EDGRTRQVIHPVGSLTLEEPLLLAADKDEAQlKVYVeaea 1216

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 2679228985  156 -QPFDLTQALLFRAQIVQVSDERHLLLVDMHHMISDGVSVNILIREF 201
Cdd:PRK12467  1217 rQPFDLEQGPLLRVGLLRLAADEHVLVLTLHHIVSDGWSMQVLVDEL 1263
PRK05691 PRK05691
peptide synthase; Validated
 1-201 1.96e-41

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 149.16  E-value: 1.96e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2679228985    1 GGHSLKATALVSRIAKEFDVQVPLKDVFAHPTVEG----LASVIREGTDSPyEAMKPAEQRETYPVSSAQKRIYVLQQLE 76
Cdd:PRK05691   614 GGNSIAATQVVARLRDELGIDLNLRQLFEAPTLAAfsaaVARQLAGGGAAQ-AAIARLPRGQALPQSLAQNRLWLLWQLD 692

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2679228985   77 DGGTGYNMPAVLELEGKLDPERLDRAFQELIKRHESLRTSF-EQDegGEPVQRIHDEVPFTLQTAVLGE--QTEQEAAAA 153
Cdd:PRK05691   693 PQSAAYNIPGGLHLRGELDEAALRASFQRLVERHESLRTRFyERD--GVALQRIDAQGEFALQRIDLSDlpEAEREARAA 770

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2679228985  154 FI------QPFDLTQALLFRAQIVQVSDERHLLLVDMHHMISDGVSVNILIREF 201
Cdd:PRK05691   771 QIreeearQPFDLEKGPLLRVTLVRLDDEEHQLLVTLHHIVADGWSLNILLDEF 824
LCL_NRPS-like cd19540
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ...
 61-199 1.41e-35

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: 129.46  E-value: 1.41e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2679228985  61 PVSSAQKRIYVLQQLEDGGTGYNMPAVLELEGKLDPERLDRAFQELIKRHESLRTSFEQDEGGePVQRIHD--EVPFTLQ 138
Cdd:cd19540     3 PLSFAQQRLWFLNRLDGPSAAYNIPLALRLTGALDVDALRAALADVVARHESLRTVFPEDDGG-PYQVVLPaaEARPDLT 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2679228985 139 TAVLGEQTEQEAAAAFI-QPFDLTQALLFRAQIVQVSDERHLLLVDMHHMISDGVSVNILIR 199
Cdd:cd19540    82 VVDVTEDELAARLAEAArRGFDLTAELPLRARLFRLGPDEHVLVLVVHHIAADGWSMAPLAR 143
PRK12316 PRK12316
peptide synthase; Provisional
 1-200 2.92e-35

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 131.23  E-value: 2.92e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2679228985    1 GGHSLKATALVSRIAKEFDVQVPLKDVFAHPTVEGLASVIREGTDSPYEAMKPAEQRETYPVSSAQKRIYVLQQLEDGGT 80
Cdd:PRK12316  2544 GGHSLLATQVVSRVRQDLGLEVPLRILFERPTLAAFAASLESGQTSRAPVLQKVTRVQPLPLSHAQQRQWFLWQLEPESA 2623

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2679228985   81 GYNMPAVLELEGKLDPERLDRAFQELIKRHESLRTSFEQDeGGEPVQRIHDEVPFT---LQTAVLGEQTEQEAAAAFIQ- 156
Cdd:PRK12316  2624 AYHLPSALHLRGVLDQAALEQAFDALVLRHETLRTRFVEV-GEQTRQVILPNMSLRivlEDCAGVADAAIRQRVAEEIQr 2702

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 2679228985  157 PFDLTQALLFRAQIVQVSDERHLLLVDMHHMISDGVSVNILIRE 200
Cdd:PRK12316  2703 PFDLARGPLLRVRLLALDGQEHVLVITQHHIVSDGWSMQVMVDE 2746
PRK05691 PRK05691
peptide synthase; Validated
 1-202 3.75e-35

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 131.06  E-value: 3.75e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2679228985    1 GGHSLKATALVSRIAKEFDVQVPLKDVFAHPTVEGLASVIR----EGTDSPYEAMKPAEQRETYPVSSAQKRIYVLQQLE 76
Cdd:PRK05691  1666 GGHSLLATQIVSRTRQACDVELPLRALFEASELGAFAEQVAriqaAGERNSQGAIARVDRSQPVPLSYSQQRMWFLWQME 1745

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2679228985   77 DGGTGYNMPAVLELEGKLDPERLDRAFQELIKRHESLRTSFEQDeGGEPVQRIHDEVPF--------TLQTAVLGEQTEQ 148
Cdd:PRK05691  1746 PDSPAYNVGGMARLSGVLDVDRFEAALQALILRHETLRTTFPSV-DGVPVQQVAEDSGLrmdwqdfsALPADARQQRLQQ 1824

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2679228985  149 EAAAAFIQPFDLTQALLFRAQIVQVSDERHLLLVDMHHMISDGVSVNILIREFG 202
Cdd:PRK05691  1825 LADSEAHQPFDLERGPLLRACLVKAAEREHYFVLTLHHIVTEGWAMDIFARELG 1878
PRK12316 PRK12316
peptide synthase; Provisional
 36-201 1.46e-34

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 129.31  E-value: 1.46e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2679228985   36 LASVIREGTDS---PYEAMKPAEQREtyPVSSAQKRIYVLQQLEDGGTGYNMPAVLELEGKLDPERLDRAFQELIKRHES 112
Cdd:PRK12316    25 LATLRGEGVDFslfPIPAGVSSAERD--RLSYAQQRMWFLWQLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHET 102

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2679228985  113 LRTSFEQdEGGEPVQRIHDEVPFTLQ--------TAVLGEQTEQEAAAAFIQPFDLTQALLFRAQIVQVSDERHLLLVDM 184
Cdd:PRK12316   103 LRTVFPR-GADDSLAQVPLDRPLEVEfedcsglpEAEQEARLRDEAQRESLQPFDLCEGPLLRVRLLRLGEEEHVLLLTL 181

                          170
                   ....*....|....*..
gi 2679228985  185 HHMISDGVSVNILIREF 201
Cdd:PRK12316   182 HHIVSDGWSMNVLIEEF 198
LCL_NRPS cd19538
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ...
 61-200 1.70e-32

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: 121.22  E-value: 1.70e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2679228985  61 PVSSAQKRIYVLQQLEDGGTGYNMPAVLELEGKLDPERLDRAFQELIKRHESLRTSFeQDEGGEPVQRIHDEVPFTL--- 137
Cdd:cd19538     3 PLSFAQRRLWFLHQLEGPSATYNIPLVIKLKGKLDVQALQQALYDVVERHESLRTVF-PEEDGVPYQLILEEDEATPkle 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2679228985 138 QTAVLGEQTEQEAAAAFIQPFDLTQALLFRAQIVQVSDERHLLLVDMHHMISDGVSVNILIRE 200
Cdd:cd19538    82 IKEVDEEELESEINEAVRYPFDLSEEPPFRATLFELGENEHVLLLLLHHIAADGWSLAPLTRD 144
C_PKS-NRPS cd19532
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
 59-200 8.24e-32

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: 119.10  E-value: 8.24e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2679228985  59 TYPVSSAQKRIYVLQQLEDGGTGYNMPAVLELEGKLDPERLDRAFQELIKRHESLRTSFEQDEG-GEPVQRIHDEVPFTL 137
Cdd:cd19532     1 TEPMSFGQSRFWFLQQYLEDPTTFNVTFSYRLTGPLDVARLERAVRAVGQRHEALRTCFFTDPEdGEPMQGVLASSPLRL 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2679228985 138 QTavLGEQTEQEAAAAFIQ----PFDLTQALLFRAQIVQVSDERHLLLVDMHHMISDGVSVNILIRE 200
Cdd:cd19532    81 EH--VQISDEAEVEEEFERlknhVYDLESGETMRIVLLSLSPTEHYLIFGYHHIAMDGVSFQIFLRD 145
PRK12467 PRK12467
peptide synthase; Provisional
 58-201 1.44e-31

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 120.65  E-value: 1.44e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2679228985   58 ETYPVSSAQKRIYVLQQLEDGGTGYNMPAVLELEGKLDPERLDRAFQELIKRHESLRTSFEQDEGGEpVQRIHDE----V 133
Cdd:PRK12467    48 ERIPLSYAQERQWFLWQLDPDSAAYNIPTALRLRGELDVSALRRAFDALVARHESLRTRFVQDEEGF-RQVIDASlsltI 126

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2679228985  134 PFTLQTAVLGEQTEQEaAAAFIQ-----PFDLTQALLFRAQIVQVSDERHLLLVDMHHMISDGVSVNILIREF 201
Cdd:PRK12467   127 PLDDLANEQGRARESQ-IEAYINeevarPFDLANGPLLRVRLLRLADDEHVLVVTLHHIISDGWSMRVLVEEL 198
DCL_NRPS cd19543
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ...
 60-201 9.23e-30

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: 113.45  E-value: 9.23e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2679228985  60 YPVSSAQKRIYvLQQLEDGGTG-YNMPAVLELEGKLDPERLDRAFQELIKRHESLRTSFEQDEGGEPVQRIHDEVPFTLQ 138
Cdd:cd19543     2 YPLSPMQEGML-FHSLLDPGSGaYVEQMVITLEGPLDPDRFRAAWQAVVDRHPILRTSFVWEGLGEPLQVVLKDRKLPWR 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2679228985 139 TAVLGEQTEQEAAAAF--------IQPFDLTQALLFRAQIVQVSDERHLLLVDMHHMISDGVSVNILIREF 201
Cdd:cd19543    81 ELDLSHLSEAEQEAELealaeedrERGFDLARAPLMRLTLIRLGDDRYRLVWSFHHILLDGWSLPILLKEL 151
starter-C_NRPS cd19533
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ...
 59-199 2.80e-26

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


Pssm-ID: 380456 [Multi-domain]  Cd Length: 419  Bit Score: 103.99  E-value: 2.80e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2679228985  59 TYPVSSAQKRIYVLQQLEDGGTGYNMPAVLELEGKLDPERLDRAFQELIKRHESLRTSFEQDEgGEPVQRIHDEVPFTLQ 138
Cdd:cd19533     1 RLPLTSAQRGVWFAEQLDPEGSIYNLAEYLEITGPVDLAVLERALRQVIAEAETLRLRFTEEE-GEPYQWIDPYTPVPIR 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2679228985 139 -TAVLGEQTEQEAAAAFIQ-----PFDLTQALLFRAQIVQVSDERHLLLVDMHHMISDGVSVNILIR 199
Cdd:cd19533    80 hIDLSGDPDPEGAAQQWMQedlrkPLPLDNDPLFRHALFTLGDNRHFWYQRVHHIVMDGFSFALFGQ 146
PRK12316 PRK12316
peptide synthase; Provisional
 1-200 4.27e-26

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 105.04  E-value: 4.27e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2679228985    1 GGHSLKATALVSRiAKEFDVQVPLKDVFAHPTVEGLASVIREGT-----DSPYEAMKP--AEQRETYPVSSAQKRIYVLQ 73
Cdd:PRK12316  3584 GGDSIISLQVVSR-ARQAGIRFTPKDLFQHQTIQGLARVARVGGgvavdQGPVSGETLllPIQQQFFEEPVPERHHWNQS 3662

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2679228985   74 QLedggtgynmpavLELEGKLDPERLDRAFQELIKRHESLRTSFEQDEGGEPVQRIHDEVP-FTLQTAVLGEQTEQEAAA 152
Cdd:PRK12316  3663 LL------------LKPREALDAAALEAALQALVEHHDALRLRFVEDAGGWTAEHLPVELGgALLWRAELDDAEELERLG 3730

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 2679228985  153 AFIQ-PFDLTQALLFRAQIVQVSDERHLLLVDMHHMISDGVSVNILIRE 200
Cdd:PRK12316  3731 EEAQrSLDLADGPLLRALLATLADGSQRLLLVIHHLVVDGVSWRILLED 3779
SgcC5_NRPS-like cd19539
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ...
 61-200 1.34e-24

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: 99.38  E-value: 1.34e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2679228985  61 PVSSAQKRIYVLQQLEDGGTGYNMPAVLELEGKLDPERLDRAFQELIKRHESLRTSFEQDEGGEPVQRI----------H 130
Cdd:cd19539     3 PLSFAQERLWFIDQGEDGGPAYNIPGAWRLTGPLDVEALREALRDVVARHEALRTLLVRDDGGVPRQEIlppgpaplevR 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2679228985 131 DEVPFTLQTAVLGEQTEQEAAAafiQPFDLTQALLFRAQIVQVSDERHLLLVDMHHMISDGVSVNILIRE 200
Cdd:cd19539    83 DLSDPDSDRERRLEELLRERES---RGFDLDEEPPIRAVLGRFDPDDHVLVLVAHHTAFDAWSLDVFARD 149
C_NRPS-like cd19066
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ...
 60-201 1.71e-24

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: 99.02  E-value: 1.71e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2679228985  60 YPVSSAQKRIYVLQQLEDGGTGYNMPAVLELEGKLDPERLDRAFQELIKRHESLRTSFEQdEGGEPVQRIHDEVP-FTLQ 138
Cdd:cd19066     2 IPLSPMQRGMWFLKKLATDPSAFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRFCE-EAGRYEQVVLDKTVrFRIE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2679228985 139 TAVLGEQTEQEA------AAAFIQPFDLTQALLFRAQIVQVSDERHLLLVDMHHMISDGVSVNILIREF 201
Cdd:cd19066    81 IIDLRNLADPEArlleliDQIQQTIYDLERGPLVRVALFRLADERDVLVVAIHHIIVDGGSFQILFEDI 149
DCL_NRPS-like cd19536
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ...
 60-201 3.31e-23

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


Pssm-ID: 380459 [Multi-domain]  Cd Length: 419  Bit Score: 95.59  E-value: 3.31e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2679228985  60 YPVSSAQKRIYVLQQLEDGGTGYNMPAVLELEGKLDPERLDRAFQELIKRHESLRTSFEQDEGGEPVQRIH--------- 130
Cdd:cd19536     2 YPLSSLQEGMLFHSLLNPGGSVYLHNYTYTVGRRLNLDLLLEALQVLIDRHDILRTSFIEDGLGQPVQVVHrqaqvpvte 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2679228985 131 -DEVPFTLQTAVLGEQTEQEaaaaFIQPFDLTQALLFRAQIVQVSDERHLLLV-DMHHMISDGVSVNILIREF 201
Cdd:cd19536    82 lDLTPLEEQLDPLRAYKEET----KIRRFDLGRAPLVRAALVRKDERERFLLViSDHHSILDGWSLYLLVKEI 150
CT_NRPS-like cd19542
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ...
 60-201 1.62e-20

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: 87.75  E-value: 1.62e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2679228985  60 YPVSSAQKRIyVLQQLEDGGTGYNmPAVLELEGKLDPERLDRAFQELIKRHESLRTSF-EQDEGGEPVQRIHDEVPftlq 138
Cdd:cd19542     2 YPCTPMQEGM-LLSQLRSPGLYFN-HFVFDLDSSVDVERLRNAWRQLVQRHDILRTVFvESSAEGTFLQVVLKSLD---- 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2679228985 139 TAVLGEQTEQEAAAAFIQPFD----LTQALLFRAQIVQVSDERHLLLVDMHHMISDGVSVNILIREF 201
Cdd:cd19542    76 PPIEEVETDEDSLDALTRDLLddptLFGQPPHRLTLLETSSGEVYLVLRISHALYDGVSLPIILRDL 142
C_PKS-NRPS_PksJ-like cd20484
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
 59-201 4.87e-19

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: 83.90  E-value: 4.87e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2679228985  59 TYPVSSAQKRIYVLQQLEDGGTGYNMPAVLELEGKLDPERLDRAFQELIKRHESLRTSFEQDEGGePVQRIHDEVPFTLQ 138
Cdd:cd20484     1 RSPLSEGQKGLWMLQKMSPEMSAYNVPLCFRFSSKLDVEKFKQACQFVLEQHPILKSVIEEEDGV-PFQKIEPSKPLSFQ 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2679228985 139 TAVLGEQTEQEaAAAFIQ-----PFDLTQALLFRAQIVQVSDERHLLLVDMHHMISDGVSVNILIREF 201
Cdd:cd20484    80 EEDISSLKESE-IIAYLRekakePFVLENGPLMRVHLFSRSEQEHFVLITIHHIIFDGSSSLTLIHSL 146
C_PKS-NRPS cd20483
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
 61-201 5.27e-19

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: 83.85  E-value: 5.27e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2679228985  61 PVSSAQKRIYVLQQLEDGGTGYNMPAVLELEGKLDPERLDRAFQELIKRHESLRTSF-EQDEGGEpvQRIHDEVPFTLQT 139
Cdd:cd20483     3 PMSTFQRRLWFLHNFLEDKTFLNLLLVCHIKGKPDVNLLQKALSELVRRHEVLRTAYfEGDDFGE--QQVLDDPSFHLIV 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2679228985 140 AVLGEQTEQEAA------AAFIQPFDLTQALLFRAQIVQVSDERHLLLVDMHHMISDGVSVNILIREF 201
Cdd:cd20483    81 IDLSEAADPEAAldqlvrNLRRQELDIEEGEVIRGWLVKLPDEEFALVLASHHIAWDRGSSKSIFEQF 148
E-C_NRPS cd19544
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); ...
 60-200 3.17e-18

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: 81.33  E-value: 3.17e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2679228985  60 YPVSSAQKRIYVLQQLEDGGTGYNMPAVLELEgklDPERLDR---AFQELIKRHESLRTSFEQDEGGEPVQRIHDEVPFT 136
Cdd:cd19544     2 YPLAPLQEGILFHHLLAEEGDPYLLRSLLAFD---SRARLDAflaALQQVIDRHDILRTAILWEGLSEPVQVVWRQAELP 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2679228985 137 LQTAVL-GEQTEQEAAAAFIQP----FDLTQALLFRAQIVQVSD-ERHLLLVDMHHMISDGVSVNILIRE 200
Cdd:cd19544    79 VEELTLdPGDDALAQLRARFDPrryrLDLRQAPLLRAHVAEDPAnGRWLLLLLFHHLISDHTSLELLLEE 148
X-Domain_NRPS cd19546
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ...
 61-200 1.76e-17

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: 79.45  E-value: 1.76e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2679228985  61 PVSSAQKRIYVLQQLEDGGTGYNMPAVLELEGKLDPERLDRAFQELIKRHESLRTSFEQDeGGEPVQRIHD----EVPFT 136
Cdd:cd19546     6 PATAGQLRTWLLARLDEETRGRHLSVALRLRGRLDRDALEAALGDVAARHEILRTTFPGD-GGDVHQRILDadaaRPELP 84

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2679228985 137 LQTAVLGEQTEQEAAAAfIQPFDLTQALLFRAQIVQVSDERHLLLVDMHHMISDGVSVNILIRE 200
Cdd:cd19546    85 VVPATEEELPALLADRA-AHLFDLTRETPWRCTLFALSDTEHVLLLVVHRIAADDESLDVLVRD 147
PRK12467 PRK12467
peptide synthase; Provisional
 53-200 1.27e-16

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 77.51  E-value: 1.27e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2679228985   53 PAEQRETYPVSSAQKRIyVLQQLEDGGTG-YNMPAVLELEGkLDPERLDRAFQELIKRHESLRTSF-EQDEGGEPVQRIH 130
Cdd:PRK12467  2640 VGDIEDIYPLSPMQQGM-LFHTLYEGGAGdYINQMRVDVEG-LDVERFRTAWQAVIDRHEILRSGFlWDGELEEPLQVVY 2717

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2679228985  131 D--EVPFTL----QTAVLGEQTEQEAAAAFIQPFDLTQALLFRAQIVQVSDERHLLLVDMHHMISDGVSVNILIRE 200
Cdd:PRK12467  2718 KqaRLPFSRldwrDRADLEQALDALAAADRQQGFDLLSAPLLRLTLVRTGEDRHHLIYTNHHILMDGWSGSQLLGE 2793
E_NRPS cd19534
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
 82-201 5.78e-16

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: 74.98  E-value: 5.78e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2679228985  82 YNMPAVLELEGKLDPERLDRAFQELIKRHESLRTSFEQDEGGEpVQRIHDEV--PFTLQ----TAVLGEQTEQEAAAAFI 155
Cdd:cd19534    22 FNQSVLLRVPQGLDPDALRQALRALVEHHDALRMRFRREDGGW-QQRIRGDVeeLFRLEvvdlSSLAQAAAIEALAAEAQ 100

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2679228985 156 QPFDLTQALLFRAQIVQVSDERHLLLVDMHHMISDGVSVNILIREF 201
Cdd:cd19534   101 SSLDLEEGPLLAAALFDGTDGGDRLLLVIHHLVVDGVSWRILLEDL 146
PRK12467 PRK12467
peptide synthase; Provisional
 1-198 7.98e-16

peptide synthase; Provisional


Pssm-ID: 237108 [Multi-domain]  Cd Length: 3956  Bit Score: 75.20  E-value: 7.98e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2679228985    1 GGHSLKATALVSRiAKEFDVQVPLKDVFAHPTVEGLASVIREGTDSPYEAMKPAEQreTYPVSSAQKRIYVLQQLEDggT 80
Cdd:PRK12467  2125 GGDSIISIQVVSR-ARQAGIRFTPKDLFQHQTVQSLAAVAQEGDGTVSIDQGPVTG--DLPLLPIQQMFFADDIPER--H 2199

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2679228985   81 GYNMPAVLELEGKLDPERLDRAFQELIKRHESLRTSFEQDEGG---EPVQRIHDEVPFTLQTAVL-GEQTEQEAAAAfIQ 156
Cdd:PRK12467  2200 HWNQSVLLEPREALDAELLEAALQALLVHHDALRLGFVQEDGGwsaMHRAPEQERRPLLWQVVVAdKEELEALCEQA-QR 2278

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 2679228985  157 PFDLTQALLFRAQIVQVSDERHLLLVDMHHMISDGVSVNILI 198
Cdd:PRK12467  2279 SLDLEEGPLLRAVLATLPDGSQRLLLVIHHLVVDGVSWRILL 2320
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
51-199 1.00e-15

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 74.70  E-value: 1.00e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2679228985   51 MKPAEQRetYPVSSAQKRIYVLQQLEDGGTGYNMPAVLELEGKLDPERLDRAFQELIKRHESLRTSFEQDEgGEPVQRIH 130
Cdd:PRK10252     1 AEPMSQH--LPLVAAQPGIWMAEKLSPLPSAWSVAHYVELTGELDAPLLARAVVAGLAEADTLRMRFTEDN-GEVWQWVD 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2679228985  131 DEVPF-TLQTAVLGEQTEQEAAA-AFIQPfDLTQAL-------LFRAQIVQVSDERHLLLVDMHHMISDGVSVNILIR 199
Cdd:PRK10252    78 PALTFpLPEIIDLRTQPDPHAAAqALMQA-DLQQDLrvdsgkpLVFHQLIQLGDNRWYWYQRYHHLLVDGFSFPAITR 154
PRK12316 PRK12316
peptide synthase; Provisional
 1-198 1.27e-15

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 74.61  E-value: 1.27e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2679228985    1 GGHSLKATALVSRiAKEFDVQVPLKDVFAHPTVEGLASVIREGTDSPYEAMKPAEQRETYPVssaQKRIYvlQQLEDGGT 80
Cdd:PRK12316  1046 GGDSIVSIQVVSR-ARQAGIQLSPRDLFQHQTIRSLALVAKAGQATAADQGPASGEVALAPV---QRWFF--EQAIPQRQ 1119

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2679228985   81 GYNMPAVLELEGKLDPERLDRAFQELIKRHESLRTSFEQDEGGEPVQRIHDEVPFTLQTAVLGEQTEQEAAAAFIQ-PFD 159
Cdd:PRK12316  1120 HWNQSLLLQARQPLDPDRLGRALERLVAHHDALRLRFREEDGGWQQAYAAPQAGEVLWQRQAASEEELLALCEEAQrSLD 1199

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 2679228985  160 LTQALLFRAQIVQVSDERHLLLVDMHHMISDGVSVNILI 198
Cdd:PRK12316  1200 LEQGPLLRALLVDMADGSQRLLLVIHHLVVDGVSWRILL 1238
PRK12316 PRK12316
peptide synthase; Provisional
 7-200 2.72e-15

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 73.84  E-value: 2.72e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2679228985    7 ATALVSRIAKEFDVQvpLKDVFAH----------PTVEGLASVIREGTDSpyEAMKPAEQRETYPVSSAQKRIYVLQQLE 76
Cdd:PRK12316  1498 AEATVQRLADDYARE--LQALIEHccdernrgvtPSDFPLAGLSQAQLDA--LPLPAGEIADIYPLSPMQQGMLFHSLYE 1573

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2679228985   77 DGGTGYNMPAVLELEGkLDPERLDRAFQELIKRHESLRTSF-EQDEGGEPVQRIHDEV--PFTLQTAVLGEQTEQE---- 149
Cdd:PRK12316  1574 QEAGDYINQLRVDVQG-LDPDRFRAAWQATVDRHEILRSGFlWQDGLEQPLQVIHKQVelPFAELDWRGREDLGQAldal 1652

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2679228985  150 AAAAFIQPFDLTQALLFRAQIVQVSDERHLLLVDMHHMISDGVSVNILIRE 200
Cdd:PRK12316  1653 AQAERQKGFDLTRAPLLRLVLVRTGEGRHHLIYTNHHILMDGWSNAQLLGE 1703
Cyc_NRPS cd19535
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
 86-200 3.62e-15

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: 72.91  E-value: 3.62e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2679228985  86 AVLELEGK-LDPERLDRAFQELIKRHESLRTSFeqDEGGEpvQRIHDEVP-FTLQTAVLGEQTEQEAAAAFI-------- 155
Cdd:cd19535    28 AYLEFDGEdLDPDRLERAWNKLIARHPMLRAVF--LDDGT--QQILPEVPwYGITVHDLRGLSEEEAEAALEelrerlsh 103

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2679228985 156 QPFDLTQALLFRAQIVQVSDERHLLLVDMHHMISDGVSVNILIRE 200
Cdd:cd19535   104 RVLDVERGPLFDIRLSLLPEGRTRLHLSIDLLVADALSLQILLRE 148
PRK05691 PRK05691
peptide synthase; Validated
 1-198 1.81e-14

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 71.35  E-value: 1.81e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2679228985    1 GGHSLKATALVSRiAKEFDVQVPLKDVFAHPTVEGLASVIREgtdspyEAMKPAEQ---RETYPVSSAQKRIYVLQQLED 77
Cdd:PRK05691  2737 GGDSILSIQVVSR-ARQLGIHFSPRDLFQHQTVQTLAAVATH------SEAAQAEQgplQGASGLTPIQHWFFDSPVPQP 2809

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2679228985   78 ggTGYNMPAVLELEGKLDPERLDRAFQELIKRHESLRTSFEQDEGGEPVQRIHDEVPFTLQTAVLGEQTEQEAAAAFIQ- 156
Cdd:PRK05691  2810 --QHWNQALLLEPRQALDPALLEQALQALVEHHDALRLRFSQADGRWQAEYRAVTAQELLWQVTVADFAECAALFADAQr 2887

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 2679228985  157 PFDLTQALLFRAQIVQVSDERHLLLVDMHHMISDGVSVNILI 198
Cdd:PRK05691  2888 SLDLQQGPLLRALLVDGPQGQQRLLLAIHHLVVDGVSWRVLL 2929
PRK12316 PRK12316
peptide synthase; Provisional
 53-200 2.67e-14

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 70.76  E-value: 2.67e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2679228985   53 PAEQRETYPVSSAQKRIYVLQQLEDGGTGYNMPAVLELEGkLDPERLDRAFQELIKRHESLRTSF-EQDEGGEPVQRIHD 131
Cdd:PRK12316  4096 LGEIEDIYPLSPMQQGMLFHSLYEQEAGDYINQMRVDVQG-LDVERFRAAWQAALDRHDVLRSGFvWQGELGRPLQVVHK 4174

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2679228985  132 --EVPFTLQ----TAVLGEQTEQEAAAAFIQPFDLTQALLFRAQIVQVSDERHLLLVDMHHMISDGVSVNILIRE 200
Cdd:PRK12316  4175 qvSLPFAELdwrgRADLQAALDALAAAERERGFDLQRAPLLRLVLVRTAEGRHHLIYTNHHILMDGWSNSQLLGE 4249
C_NRPS-like cd19537
Condensation family domain with an atypical active site motif; Condensation (C) domains of ...
 74-203 7.23e-14

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: 69.14  E-value: 7.23e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2679228985  74 QLEDGGTGYNMPAVLELEGKLDPERLDRAFQELIKRHESLRTSFEQDEGGePVQRIHDEVPFTLQTAVLGEQTEqeaaaa 153
Cdd:cd19537    16 QLSTGTSSFNVSFACRLSGDVDRDRLASAWNTVLARHRILRSRYVPRDGG-LRRSYSSSPPRVQRVDTLDVWKE------ 88

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2679228985 154 FIQPFDLTQALLFRaqiVQVSDeRHLLLVdMHHMISDGVSVNILIREFGD 203
Cdd:cd19537    89 INRPFDLEREDPIR---VFISP-DTLLVV-MSHIICDLTTLQLLLREVSA 133
FUM14_C_NRPS-like cd19545
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ...
 63-201 6.82e-13

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: 66.17  E-value: 6.82e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2679228985  63 SSAQKRIYVLQQledggtgynmpaVLELEGKLDPERLDRAFQELIKRHESLRTSFEQDEGGEPVQRIHDEVPFT------ 136
Cdd:cd19545    15 TARQPGAYVGQR------------VFELPPDIDLARLQAAWEQVVQANPILRTRIVQSDSGGLLQVVVKESPISwtests 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2679228985 137 LQTAVlgEQTEQEaaaafiqPFDLTQAlLFRAQIVQVSDERHLLLVDMHHMISDGVSVNILIREF 201
Cdd:cd19545    83 LDEYL--EEDRAA-------PMGLGGP-LVRLALVEDPDTERYFVWTIHHALYDGWSLPLILRQV 137
PRK05691 PRK05691
peptide synthase; Validated
 53-201 6.27e-12

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 64.03  E-value: 6.27e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2679228985   53 PAEQRE-TYPVSSAQKRIyVLQQLEDGGTG-YNMPAVLELEGKLDPERLDRAFQELIKRHESLRTSFEQDEGGEPVQRIH 130
Cdd:PRK05691  3250 PAAEIEdVYPLTPMQEGL-LLHTLLEPGTGlYYMQDRYRINSALDPERFAQAWQAVVARHEALRASFSWNAGETMLQVIH 3328

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2679228985  131 D--EVPFTLQ--TAVLGEQTEQEAAAAFIQP----FDLTQALLFRAQIVQVSDERHLLLVDMHHMISDGVSVNILIREF 201
Cdd:PRK05691  3329 KpgRTPIDYLdwRGLPEDGQEQRLQALHKQEreagFDLLNQPPFHLRLIRVDEARYWFMMSNHHILIDAWCRSLLMNDF 3407
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
 53-201 1.51e-11

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


Pssm-ID: 440643 [Multi-domain]  Cd Length: 1329  Bit Score: 62.57  E-value: 1.51e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2679228985   53 PAEQRETYPVSSAQKRIYVLQQLEDGGTGYNMPAVLELEGKLDPERLDRAFQELIKRHESLRTSFEQDEGgEPVQRIHDE 132
Cdd:COG1020     11 PAAAAAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAG-RPVQVIQPV 89

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2679228985  133 VPFTLQTAVL--------GEQTEQEAAAAFIQPFDLTQALLFRAQIVQVSDERHLLLVDMHHMISDGVSVNILIREF 201
Cdd:COG1020     90 VAAPLPVVVLlvdlealaEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDGLLLAEL 166
beta-lac_NRPS cd19547
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ...
 60-191 4.58e-09

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: 55.01  E-value: 4.58e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2679228985  60 YPVSSAQKRIYVLQQLEDGGTGYNMPAVLELEGKLDPERLDRAFQELIKRHESLRTSFEQDEGGEPVQRIHDEV--PFTL 137
Cdd:cd19547     2 YPLAPMQEGMLFRGLFWPDSDAYFNQNVLELVGGTDEDVLREAWRRVADRYEILRTGFTWRDRAEPLQYVRDDLapPWAL 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2679228985 138 ---------QTAVLGEQTEQEAAAAFIqpfDLTQALLFRAQIVQVSDERHLLLVDMHHMISDG 191
Cdd:cd19547    82 ldwsgedpdRRAELLERLLADDRAAGL---SLADCPLYRLTLVRLGGGRHYLLWSHHHILLDG 141
AcpP COG0236
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ...
 1-42 7.42e-08

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


Pssm-ID: 440006 [Multi-domain]  Cd Length: 80  Bit Score: 47.93  E-value: 7.42e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2679228985   1 GGHSLKATALVSRIAKEFDVQVPLKDVFAHPTVEGLASVIRE 42
Cdd:COG0236    36 GLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLEE 77
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
 1-34 3.69e-06

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: 42.94  E-value: 3.69e-06
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2679228985   1 GGHSLKATALVSRIAKEFDVQVPLKDVFAHPTVE 34
Cdd:pfam00550  28 GLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLA 61
alpha_am_amid TIGR03443
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ...
 1-40 2.14e-05

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


Pssm-ID: 274582 [Multi-domain]  Cd Length: 1389  Bit Score: 44.67  E-value: 2.14e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 2679228985    1 GGHSLKATALVSRIAKEFDVQVPLKDVFAHPTVEGLASVI 40
Cdd:TIGR03443  878 GGHSILATRMIFELRKKLNVELPLGLIFKSPTIKGFAKEV 917
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
1-45 3.62e-05

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 43.88  E-value: 3.62e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 2679228985    1 GGHSLKATALVSRIAKEFDVQVPLKDVFAHPTVEGLASVIREGTD 45
Cdd:PRK10252  1006 GGHSLLAMKLAAQLSRQFARQVTPGQVMVASTVAKLATLLDAEED 1050
PRK09294 PRK09294
phthiocerol/phthiodiolone dimycocerosyl transferase;
90-191 8.20e-05

phthiocerol/phthiodiolone dimycocerosyl transferase;


Pssm-ID: 181765 [Multi-domain]  Cd Length: 416  Bit Score: 42.39  E-value: 8.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2679228985  90 LEGKLDPERLDRAFQELIKRHESLRTSFEQDEGGEPVQRIHDEVPftlQTAVLGEQTEQEAAAAFiqPFDLTQAlLFRAQ 169
Cdd:PRK09294   30 LRGVLDIDALSDAFDALLRAHPVLAAHLEQDSDGGWELVADDLLH---PGIVVVDGDAARPLPEL--QLDQGVS-LLALD 103

                          90       100
                  ....*....|....*....|..
gi 2679228985 170 IVQVSDERHLLLVdMHHMISDG 191
Cdd:PRK09294  104 VVPDDGGARVTLY-IHHSIADA 124
PRK05691 PRK05691
peptide synthase; Validated
 1-41 8.51e-05

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 42.85  E-value: 8.51e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 2679228985    1 GGHSLKATALVSRIAKEFDVQVPLKDVFAHPTVEGLASVIR 41
Cdd:PRK05691  4269 GGHSLLATQIASRVQKALQRNVPLRAMFECSTVEELAEYIE 4309
PKS_PP smart00823
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ...
 1-42 3.68e-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: 38.00  E-value: 3.68e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 2679228985    1 GGHSLKATALVSRIAKEFDVQVPLKDVFAHPTVEGLASVIRE 42
Cdd:smart00823  43 GLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAEHLAA 84
PRK12316 PRK12316
peptide synthase; Provisional
 1-38 5.26e-04

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 40.33  E-value: 5.26e-04
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 2679228985    1 GGHSLKATALVSRIAKEFDVQVPLKDVFAHPTVEGLAS 38
Cdd:PRK12316  5100 GGHSLLAIQVTSRIQLELGLELPLRELFQTPTLAAFVE 5137
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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