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Conserved domains on  [gi|392313538|gb|AFM56697|]
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high-molecular-weight protein 2, partial [Lelliottia amnigena]

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 ...
 114-317 4.85e-97

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 cd19535:

Pssm-ID: 394795 [Multi-domain]  Cd Length: 423  Bit Score: 292.85  E-value: 4.85e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392313538 114 PFPLTPVQHAYLTGRMPGQKLGGVGCHLYQEFEGHCLTASQLEQAITTLLQRHPMLHIAFRPDGQQVWLPQPYWNGVTVH 193
Cdd:cd19535    1 PFPLTDVQYAYWIGRQDDQELGGVGCHAYLEFDGEDLDPDRLERAWNKLIARHPMLRAVFLDDGTQQILPEVPWYGITVH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392313538 194 DLRHNDAESRQAYLDALRQRLSHRLLRVEIGETFDFQLTLLPDNHHRLHVNIDLLIMDASSFTLFFDELNALLA--GESL 271
Cdd:cd19535   81 DLRGLSEEEAEAALEELRERLSHRVLDVERGPLFDIRLSLLPEGRTRLHLSIDLLVADALSLQILLRELAALYEdpGEPL 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 392313538 272 PAIDtrYDFRSYLLHQQKINQPLRDDARAYWLAKASTLPPAPVLPL 317
Cdd:cd19535  161 PPLE--LSFRDYLLAEQALRETAYERARAYWQERLPTLPPAPQLPL 204
AcpA COG3433
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ...
 5-95 2.10e-16

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


:

Pssm-ID: 442659 [Multi-domain]  Cd Length: 295  Bit Score: 77.87  E-value: 2.10e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392313538   5 APSQDSLLPDNRHAADYQQLRERLIQELNLTPQQLHEESNLIQAGLDSIRLMRWLHWFRKNGYRLTLRELYAAPTLAAWN 84
Cdd:COG3433  205 LLAAASPAPALETALTEEELRADVAELLGVDPEEIDPDDNLFDLGLDSIRLMQLVERWRKAGLDVSFADLAEHPTLAAWW 284

                         90
                 ....*....|.
gi 392313538  85 QLMLSRSPENA 95
Cdd:COG3433  285 ALLAAAQAAAA 295
 
Name Accession Description Interval E-value
Cyc_NRPS cd19535
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
 114-317 4.85e-97

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: 292.85  E-value: 4.85e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392313538 114 PFPLTPVQHAYLTGRMPGQKLGGVGCHLYQEFEGHCLTASQLEQAITTLLQRHPMLHIAFRPDGQQVWLPQPYWNGVTVH 193
Cdd:cd19535    1 PFPLTDVQYAYWIGRQDDQELGGVGCHAYLEFDGEDLDPDRLERAWNKLIARHPMLRAVFLDDGTQQILPEVPWYGITVH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392313538 194 DLRHNDAESRQAYLDALRQRLSHRLLRVEIGETFDFQLTLLPDNHHRLHVNIDLLIMDASSFTLFFDELNALLA--GESL 271
Cdd:cd19535   81 DLRGLSEEEAEAALEELRERLSHRVLDVERGPLFDIRLSLLPEGRTRLHLSIDLLVADALSLQILLRELAALYEdpGEPL 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 392313538 272 PAIDtrYDFRSYLLHQQKINQPLRDDARAYWLAKASTLPPAPVLPL 317
Cdd:cd19535  161 PPLE--LSFRDYLLAEQALRETAYERARAYWQERLPTLPPAPQLPL 204
AcpA COG3433
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ...
 5-95 2.10e-16

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


Pssm-ID: 442659 [Multi-domain]  Cd Length: 295  Bit Score: 77.87  E-value: 2.10e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392313538   5 APSQDSLLPDNRHAADYQQLRERLIQELNLTPQQLHEESNLIQAGLDSIRLMRWLHWFRKNGYRLTLRELYAAPTLAAWN 84
Cdd:COG3433  205 LLAAASPAPALETALTEEELRADVAELLGVDPEEIDPDDNLFDLGLDSIRLMQLVERWRKAGLDVSFADLAEHPTLAAWW 284

                         90
                 ....*....|.
gi 392313538  85 QLMLSRSPENA 95
Cdd:COG3433  285 ALLAAAQAAAA 295
COG4908 COG4908
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ...
 144-316 6.95e-15

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


Pssm-ID: 443936 [Multi-domain]  Cd Length: 243  Bit Score: 72.76  E-value: 6.95e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392313538 144 EFEGHcLTASQLEQAITTLLQRHPMLHIAFRPDG---QQVWLPQPYWNgVTVHDLRHNDAESRQAYLDALRQRLSHRLLR 220
Cdd:COG4908   25 RLEGP-LDVEALERALRELVRRHPALRTRFVEEDgepVQRIDPDADLP-LEVVDLSALPEPEREAELEELVAEEASRPFD 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392313538 221 VEIGETFDFQLTLLPDNHHRLHVNIDLLIMDASSFTLFFDEL----NALLAGESLPAIDTRYDFRSYLLHQQK-INQPLR 295
Cdd:COG4908  103 LARGPLLRAALIRLGEDEHVLLLTIHHIISDGWSLGILLRELaalyAALLEGEPPPLPELPIQYADYAAWQRAwLQSEAL 182

                        170       180
                 ....*....|....*....|.
gi 392313538 296 DDARAYWLAKASTLPPAPVLP 316
Cdd:COG4908  183 EKQLEYWRQQLAGAPPVLELP 203
Condensation pfam00668
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ...
 155-316 7.77e-10

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: 59.65  E-value: 7.77e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392313538  155 LEQAITTLLQRHPMLHIAFRPDGQQ-VWlpQPYWNGVTVH----DLRHNDAESRQAYLDALRQRLSHRLLRVEIGETFDF 229
Cdd:pfam00668  44 LEKALQELINRHDALRTVFIRQENGePV--QVILEERPFEleiiDISDLSESEEEEAIEAFIQRDLQSPFDLEKGPLFRA 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392313538  230 QLTLLPDNHHRLHVNIDLLIMDASSFTLFFDEL----NALLAGESLPAIDTRyDFRSYLL-HQQKINQPLRDDARAYWLA 304
Cdd:pfam00668 122 GLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLadlyQQLLKGEPLPLPPKT-PYKDYAEwLQQYLQSEDYQKDAAYWLE 200

                         170
                  ....*....|...
gi 392313538  305 K-ASTLPPAPVLP 316
Cdd:pfam00668 201 QlEGELPVLQLPK 213
PRK12316 PRK12316
peptide synthase; Provisional
 6-317 1.21e-09

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 59.59  E-value: 1.21e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392313538    6 PSQDSLLPDNRHAADYQQLRERL--IQELNLTPQQLHEESNLIQAGLDSIRLMRWLHWFRKN-GYRLTLRELYAAPTLAA 82
Cdd:PRK12316 2499 PKPDVSQLRQAYVAPQEGLEQRLaaIWQAVLKVEQVGLDDHFFELGGHSLLATQVVSRVRQDlGLEVPLRILFERPTLAA 2578

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392313538   83 WNQLMLSRSPENAEEETPpdesswpnMTESTPFPLTPVQH--AYLTGRMPGQKLGGVGCHLYQEfegHCLTASQLEQAIT 160
Cdd:PRK12316 2579 FAASLESGQTSRAPVLQK--------VTRVQPLPLSHAQQrqWFLWQLEPESAAYHLPSALHLR---GVLDQAALEQAFD 2647

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392313538  161 TLLQRHPMLHIAFRPDGQQVWlpQPYWNGVTVHDLRHNDAESRQAYLDALRQRLSHRLLRVEIGETFDFQLTLLPDNHHR 240
Cdd:PRK12316 2648 ALVLRHETLRTRFVEVGEQTR--QVILPNMSLRIVLEDCAGVADAAIRQRVAEEIQRPFDLARGPLLRVRLLALDGQEHV 2725

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392313538  241 LHVNIDLLIMDASSFTLFFDELNAL----LAGESLPAIDTRYDFRSYLLHQQK-INQPLRDDARAYWLAKASTLPPAPVL 315
Cdd:PRK12316 2726 LVITQHHIVSDGWSMQVMVDELVQAyagaRRGEQPTLPPLPLQYADYAAWQRAwMDSGEGARQLDYWRERLGGEQPVLEL 2805


                  ..
gi 392313538  316 PL 317
Cdd:PRK12316 2806 PL 2807
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
 22-82 1.05e-08

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: 51.02  E-value: 1.05e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392313538   22 QQLRERLIQELNLTPQQLHEESNLIQAGLDSIRLMRWLHWFRKN-GYRLTLRELYAAPTLAA 82
Cdd:pfam00550   1 ERLRELLAEVLGVPAEEIDPDTDLFDLGLDSLLAVELIARLEEEfGVEIPPSDLFEHPTLAE 62
 
Name Accession Description Interval E-value
Cyc_NRPS cd19535
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
 114-317 4.85e-97

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: 292.85  E-value: 4.85e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392313538 114 PFPLTPVQHAYLTGRMPGQKLGGVGCHLYQEFEGHCLTASQLEQAITTLLQRHPMLHIAFRPDGQQVWLPQPYWNGVTVH 193
Cdd:cd19535    1 PFPLTDVQYAYWIGRQDDQELGGVGCHAYLEFDGEDLDPDRLERAWNKLIARHPMLRAVFLDDGTQQILPEVPWYGITVH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392313538 194 DLRHNDAESRQAYLDALRQRLSHRLLRVEIGETFDFQLTLLPDNHHRLHVNIDLLIMDASSFTLFFDELNALLA--GESL 271
Cdd:cd19535   81 DLRGLSEEEAEAALEELRERLSHRVLDVERGPLFDIRLSLLPEGRTRLHLSIDLLVADALSLQILLRELAALYEdpGEPL 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 392313538 272 PAIDtrYDFRSYLLHQQKINQPLRDDARAYWLAKASTLPPAPVLPL 317
Cdd:cd19535  161 PPLE--LSFRDYLLAEQALRETAYERARAYWQERLPTLPPAPQLPL 204
ArgR-Cyc_NRPS-like cd20480
Cyc (heterocyclization)-like domain of Vibrio anguillarum AngR and similar proteins; belongs ...
 116-317 3.03e-18

Cyc (heterocyclization)-like domain of Vibrio anguillarum AngR and similar proteins; belongs to the Condensation-domain family; Vibrio anguillarum AngR plays a role in regulating the expression of iron transport genes as well as in the production of the siderophore anguibactin. Cyc-domains are a type of Condensation (C) domain. Cyc-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. C-domains typically have a conserved HHxxxD motif at the active site; Cyc-domains have a alternative, conserved DxxxxD active site motif, mutation of the aspartate residues in this motif can abolish or diminish condensation activity. Members of this subfamily have an SxxxD motif at the active site. 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). In addition to Cyc-domains there are various other 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. 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: 380470 [Multi-domain]  Cd Length: 406  Bit Score: 84.48  E-value: 3.03e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392313538 116 PLTPVQHAYLT--GRMPGQKlgGVGCHLYQEFEGHCLTASQLEQAITTLLQRHPMLHIAFRPDgqqVWLPQP---YWNGV 190
Cdd:cd20480    3 PLTSNQNWQLStqRQRSEQQ--SIANFIYQEFDYENISVDTLERCLTVLINHHPMLHALLSDD---FYLHINsknQIDAF 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392313538 191 TVHDLRHNDAESRQAYLDALRQRLSHRLLRVeigeTFDFQLTLLPDNHHRLHVNIDLLIMDASSFTLFFDELNALLAGES 270
Cdd:cd20480   78 AVNDLSSASEQEAAEQLARTRATLTKSRSKA----TISVVLSLLPANKIRLHVRFNSVVVDHPSVNLFFEQLCQLLRGSL 153

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 392313538 271 LPAIDTRYDFRSyllHQQKINQPLR--DDARAYWLAKASTLPPAPVLPL 317
Cdd:cd20480  154 LSFLAQEQVILA---HNQLVISELQstGLSSAFWNEQILQLPSSANLPT 199
AcpA COG3433
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ...
 5-95 2.10e-16

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


Pssm-ID: 442659 [Multi-domain]  Cd Length: 295  Bit Score: 77.87  E-value: 2.10e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392313538   5 APSQDSLLPDNRHAADYQQLRERLIQELNLTPQQLHEESNLIQAGLDSIRLMRWLHWFRKNGYRLTLRELYAAPTLAAWN 84
Cdd:COG3433  205 LLAAASPAPALETALTEEELRADVAELLGVDPEEIDPDDNLFDLGLDSIRLMQLVERWRKAGLDVSFADLAEHPTLAAWW 284

                         90
                 ....*....|.
gi 392313538  85 QLMLSRSPENA 95
Cdd:COG3433  285 ALLAAAQAAAA 295
COG4908 COG4908
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ...
 144-316 6.95e-15

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


Pssm-ID: 443936 [Multi-domain]  Cd Length: 243  Bit Score: 72.76  E-value: 6.95e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392313538 144 EFEGHcLTASQLEQAITTLLQRHPMLHIAFRPDG---QQVWLPQPYWNgVTVHDLRHNDAESRQAYLDALRQRLSHRLLR 220
Cdd:COG4908   25 RLEGP-LDVEALERALRELVRRHPALRTRFVEEDgepVQRIDPDADLP-LEVVDLSALPEPEREAELEELVAEEASRPFD 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392313538 221 VEIGETFDFQLTLLPDNHHRLHVNIDLLIMDASSFTLFFDEL----NALLAGESLPAIDTRYDFRSYLLHQQK-INQPLR 295
Cdd:COG4908  103 LARGPLLRAALIRLGEDEHVLLLTIHHIISDGWSLGILLRELaalyAALLEGEPPPLPELPIQYADYAAWQRAwLQSEAL 182

                        170       180
                 ....*....|....*....|.
gi 392313538 296 DDARAYWLAKASTLPPAPVLP 316
Cdd:COG4908  183 EKQLEYWRQQLAGAPPVLELP 203
C_PKS-NRPS cd20483
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
 155-317 4.52e-14

Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHXXXD motif. 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: 72.29  E-value: 4.52e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392313538 155 LEQAITTLLQRHPMLHIAFR---PDGQQVWLPQPYWNgVTVHDLrhNDAESRQAYLDALRQRLSHRLLRVEIGETFDFQL 231
Cdd:cd20483   41 LQKALSELVRRHEVLRTAYFegdDFGEQQVLDDPSFH-LIVIDL--SEAADPEAALDQLVRNLRRQELDIEEGEVIRGWL 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392313538 232 TLLPDNHHRLHVNIDLLIMDASSFTLFFDEL----NALLAGESLPAID-TRYDFRSYLL-HQQKINQPLRDDARAYWLAK 305
Cdd:cd20483  118 VKLPDEEFALVLASHHIAWDRGSSKSIFEQFtalyDALRAGRDLATVPpPPVQYIDFTLwHNALLQSPLVQPLLDFWKEK 197

                        170
                 ....*....|...
gi 392313538 306 ASTLPPA-PVLPL 317
Cdd:cd20483  198 LEGIPDAsKLLPF 210
C_PKS-NRPS cd19532
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ...
 144-317 4.66e-13

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: 69.02  E-value: 4.66e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392313538 144 EFEGHcLTASQLEQAITTLLQRHPMLHIAFRPDG-----QQVWLPQPywngvtVHDLRHNDAESRQAYLDALrQRLSHRL 218
Cdd:cd19532   31 RLTGP-LDVARLERAVRAVGQRHEALRTCFFTDPedgepMQGVLASS------PLRLEHVQISDEAEVEEEF-ERLKNHV 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392313538 219 LRVEIGETFDFQLTLLPDNHHRLHVNIDLLIMDASSFTLFFDELNALLAGESLPAIDTRYdfRSYLLHQ-QKINQPLRDD 297
Cdd:cd19532  103 YDLESGETMRIVLLSLSPTEHYLIFGYHHIAMDGVSFQIFLRDLERAYNGQPLLPPPLQY--LDFAARQrQDYESGALDE 180

                        170       180
                 ....*....|....*....|.
gi 392313538 298 ARAYWLAKASTLPPA-PVLPL 317
Cdd:cd19532  181 DLAYWKSEFSTLPEPlPLLPF 201
Condensation pfam00668
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ...
 155-316 7.77e-10

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: 59.65  E-value: 7.77e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392313538  155 LEQAITTLLQRHPMLHIAFRPDGQQ-VWlpQPYWNGVTVH----DLRHNDAESRQAYLDALRQRLSHRLLRVEIGETFDF 229
Cdd:pfam00668  44 LEKALQELINRHDALRTVFIRQENGePV--QVILEERPFEleiiDISDLSESEEEEAIEAFIQRDLQSPFDLEKGPLFRA 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392313538  230 QLTLLPDNHHRLHVNIDLLIMDASSFTLFFDEL----NALLAGESLPAIDTRyDFRSYLL-HQQKINQPLRDDARAYWLA 304
Cdd:pfam00668 122 GLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLadlyQQLLKGEPLPLPPKT-PYKDYAEwLQQYLQSEDYQKDAAYWLE 200

                         170
                  ....*....|...
gi 392313538  305 K-ASTLPPAPVLP 316
Cdd:pfam00668 201 QlEGELPVLQLPK 213
PRK12316 PRK12316
peptide synthase; Provisional
 6-317 1.21e-09

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 59.59  E-value: 1.21e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392313538    6 PSQDSLLPDNRHAADYQQLRERL--IQELNLTPQQLHEESNLIQAGLDSIRLMRWLHWFRKN-GYRLTLRELYAAPTLAA 82
Cdd:PRK12316 2499 PKPDVSQLRQAYVAPQEGLEQRLaaIWQAVLKVEQVGLDDHFFELGGHSLLATQVVSRVRQDlGLEVPLRILFERPTLAA 2578

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392313538   83 WNQLMLSRSPENAEEETPpdesswpnMTESTPFPLTPVQH--AYLTGRMPGQKLGGVGCHLYQEfegHCLTASQLEQAIT 160
Cdd:PRK12316 2579 FAASLESGQTSRAPVLQK--------VTRVQPLPLSHAQQrqWFLWQLEPESAAYHLPSALHLR---GVLDQAALEQAFD 2647

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392313538  161 TLLQRHPMLHIAFRPDGQQVWlpQPYWNGVTVHDLRHNDAESRQAYLDALRQRLSHRLLRVEIGETFDFQLTLLPDNHHR 240
Cdd:PRK12316 2648 ALVLRHETLRTRFVEVGEQTR--QVILPNMSLRIVLEDCAGVADAAIRQRVAEEIQRPFDLARGPLLRVRLLALDGQEHV 2725

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392313538  241 LHVNIDLLIMDASSFTLFFDELNAL----LAGESLPAIDTRYDFRSYLLHQQK-INQPLRDDARAYWLAKASTLPPAPVL 315
Cdd:PRK12316 2726 LVITQHHIVSDGWSMQVMVDELVQAyagaRRGEQPTLPPLPLQYADYAAWQRAwMDSGEGARQLDYWRERLGGEQPVLEL 2805


                  ..
gi 392313538  316 PL 317
Cdd:PRK12316 2806 PL 2807
EntF COG1020
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ...
 95-317 5.46e-09

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: 57.56  E-value: 5.46e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392313538   95 AEEETPPDESSWPNMTESTPFPLTPVQHAYLTGRMPGQKLGGVGCHLYQEFEGHCLTASQLEQAITTLLQRHPMLHIAFR 174
Cdd:COG1020     3 AAAAAALPPAAAAAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAGRP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392313538  175 PDGQQVWLPQPYWNGVTVHDLRHNDAESRQAYLDALRQRLSHRLLRVEIGETFDFQLTLLPDNHHRLHVNIDLLIMDASS 254
Cdd:COG1020    83 VQVIQPVVAAPLPVVVLLVDLEALAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDGLL 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 392313538  255 FTLFFDELNALLAGESLPAIDTRYDFRSY-LLHQQKINQPLRDDARAYWLAKASTLPPAPVLPL 317
Cdd:COG1020   163 LAELLRLYLAAYAGAPLPLPPLPIQYADYaLWQREWLQGEELARQLAYWRQQLAGLPPLLELPT 226
LCL_NRPS-like cd19531
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ...
 155-316 9.77e-09

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: 56.21  E-value: 9.77e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392313538 155 LEQAITTLLQRHPMLHIAFRP-DGQ--QVWLPQPYWNgVTVHDLRHNDAESRQAYLDALRQRLSHR--------LLRVEI 223
Cdd:cd19531   41 LERALNELVARHEALRTTFVEvDGEpvQVILPPLPLP-LPVVDLSGLPEAEREAEAQRLAREEARRpfdlargpLLRATL 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392313538 224 getfdFQLTllpDNHHRLHVNIDLLIMDASSFTLFFDELNALLAGES------LPAIDTRY-DF----RSYLlhqqkiNQ 292
Cdd:cd19531  120 -----LRLG---EDEHVLLLTMHHIVSDGWSMGVLLRELAALYAAFLagrpspLPPLPIQYaDYavwqREWL------QG 185

                        170       180
                 ....*....|....*....|....
gi 392313538 293 PLRDDARAYWLAKASTLPPAPVLP 316
Cdd:cd19531  186 EVLERQLAYWREQLAGAPPVLELP 209
PP-binding pfam00550
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ...
 22-82 1.05e-08

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: 51.02  E-value: 1.05e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392313538   22 QQLRERLIQELNLTPQQLHEESNLIQAGLDSIRLMRWLHWFRKN-GYRLTLRELYAAPTLAA 82
Cdd:pfam00550   1 ERLRELLAEVLGVPAEEIDPDTDLFDLGLDSLLAVELIARLEEEfGVEIPPSDLFEHPTLAE 62
E_NRPS cd19534
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ...
 114-314 1.41e-08

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: 55.72  E-value: 1.41e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392313538 114 PFPLTPVQHAYLTGRMPGQklggvgCHLYQEFEGHC---LTASQLEQAITTLLQRHPMLHIAFRPDGQ--QVWLP----Q 184
Cdd:cd19534    1 EVPLTPIQRWFFEQNLAGR------HHFNQSVLLRVpqgLDPDALRQALRALVEHHDALRMRFRREDGgwQQRIRgdveE 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392313538 185 PYwnGVTVHDLRHND-AESRQAYLDALRQRLS---HRLLRVEIgetfdFQLTllpDNHHRLHVNIDLLIMDASSFTLFFD 260
Cdd:cd19534   75 LF--RLEVVDLSSLAqAAAIEALAAEAQSSLDleeGPLLAAAL-----FDGT---DGGDRLLLVIHHLVVDGVSWRILLE 144

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 392313538 261 ELNALLAGES---LPAIDTRYDFRSYLLHQQKINQPLRDDA-RAYWLAKAST----LPPAPV 314
Cdd:cd19534  145 DLEAAYEQALagePIPLPSKTSFQTWAELLAEYAQSPALLEeLAYWRELPAAdywgLPKDPE 206
DCL_NRPS cd19543
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ...
 155-302 2.95e-07

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: 51.43  E-value: 2.95e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392313538 155 LEQAITTLLQRHPMLHIAFRPDG----QQVWLPQPYWNgVTVHDLRHNDAESRQAYLDALRQRlshrllrvEIGETFD-- 228
Cdd:cd19543   41 FRAAWQAVVDRHPILRTSFVWEGlgepLQVVLKDRKLP-WRELDLSHLSEAEQEAELEALAEE--------DRERGFDla 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392313538 229 ----FQLTL--LPDNHHRLHVNIDLLIMDASSFTLFFDEL----NALLAGE--SLPAIDTRYDFRSYLLHQQKinqplrD 296
Cdd:cd19543  112 raplMRLTLirLGDDRYRLVWSFHHILLDGWSLPILLKELfaiyAALGEGQppSLPPVRPYRDYIAWLQRQDK------E 185


                 ....*.
gi 392313538 297 DARAYW 302
Cdd:cd19543  186 AAEAYW 191
CT_NRPS-like cd19542
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ...
 115-311 8.58e-07

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: 50.00  E-value: 8.58e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392313538 115 FPLTPVQHAYLTGRMPGQKLGGVgcHLYQEFEGHClTASQLEQAITTLLQRHPMLHIAFRPDGQQVWLPQPYWNGVT--V 192
Cdd:cd19542    2 YPCTPMQEGMLLSQLRSPGLYFN--HFVFDLDSSV-DVERLRNAWRQLVQRHDILRTVFVESSAEGTFLQVVLKSLDppI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392313538 193 HDLRHNDaESRQAYLDALRQRlshrllRVEIGETFdFQLTLL--PDNHHRLHVNIDLLIMDASSFTLFFDELNALLAGES 270
Cdd:cd19542   79 EEVETDE-DSLDALTRDLLDD------PTLFGQPP-HRLTLLetSSGEVYLVLRISHALYDGVSLPIILRDLAAAYNGQL 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 392313538 271 LPaidTRYDFRSYLLHQQKINQplrDDARAYW---LAKASTLPP 311
Cdd:cd19542  151 LP---PAPPFSDYISYLQSQSQ---EESLQYWrkyLQGASPCAF 188
PRK05691 PRK05691
peptide synthase; Validated
 66-317 3.05e-06

peptide synthase; Validated


Pssm-ID: 235564 [Multi-domain]  Cd Length: 4334  Bit Score: 49.01  E-value: 3.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392313538   66 GYRLTLRELYAAPTLAAWnqlmlSRSPENAEEETPPDESSWPNMTESTPFPLTPVQH-------------AYltgRMPGq 132
Cdd:PRK05691  632 GIDLNLRQLFEAPTLAAF-----SAAVARQLAGGGAAQAAIARLPRGQALPQSLAQNrlwllwqldpqsaAY---NIPG- 702

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392313538  133 klggvGCHLYQEfeghcLTASQLEQAITTLLQRHPMLHIAF-RPDGQ--QVWLPQPYWNgVTVHDLRHNDAESRQAYLDA 209
Cdd:PRK05691  703 -----GLHLRGE-----LDEAALRASFQRLVERHESLRTRFyERDGValQRIDAQGEFA-LQRIDLSDLPEAEREARAAQ 771

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392313538  210 LRQRLSHRLLRVEIGETFDFQLTLLPDNHHRLHVNIDLLIMDASSFTLFFDELNALLAGE------SLPAIDTRY-DFRS 282
Cdd:PRK05691  772 IREEEARQPFDLEKGPLLRVTLVRLDDEEHQLLVTLHHIVADGWSLNILLDEFSRLYAAAcqgqtaELAPLPLGYaDYGA 851

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 392313538  283 YllHQQKINQPLRDDARAYWLAKASTlpPAPVLPL 317
Cdd:PRK05691  852 W--QRQWLAQGEAARQLAYWKAQLGD--EQPVLEL 882
DCL_NRPS-like cd19536
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ...
 115-311 3.29e-06

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: 48.21  E-value: 3.29e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392313538 115 FPLTPVQHAYLTgRMPGQKLGGVGCHLYQEFEGHCLTASQLEQAITTLLQRHPMLHIAFRPDGQ----QVWLPQPYWNgV 190
Cdd:cd19536    2 YPLSSLQEGMLF-HSLLNPGGSVYLHNYTYTVGRRLNLDLLLEALQVLIDRHDILRTSFIEDGLgqpvQVVHRQAQVP-V 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392313538 191 TVHDLRHndAESRQAYLDALRQRLSHRLLRVEIGETFDFQLTLLPDNHH-RLHVNIDLLIMDASSFTLFFDELNALLAG- 268
Cdd:cd19536   80 TELDLTP--LEEQLDPLRAYKEETKIRRFDLGRAPLVRAALVRKDERERfLLVISDHHSILDGWSLYLLVKEILAVYNQl 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 392313538 269 -----ESLPAidtRYDFRSYLLHQQKinQPLRDDARAYWL-----AKASTLPP 311
Cdd:cd19536  158 leykpLSLPP---AQPYRDFVAHERA--SIQQAASERYWReylagATLATLPA 205
entF PRK10252
enterobactin non-ribosomal peptide synthetase EntF;
150-311 5.35e-05

enterobactin non-ribosomal peptide synthetase EntF;


Pssm-ID: 236668 [Multi-domain]  Cd Length: 1296  Bit Score: 45.04  E-value: 5.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392313538  150 LTASQLEQAITTLLQRHPMLHIAFRPDGQQVWL---PQPYWNGVTVHDLRHNDAESRQAYldALRQRLSHRLLRVEIGET 226
Cdd:PRK10252   42 LDAPLLARAVVAGLAEADTLRMRFTEDNGEVWQwvdPALTFPLPEIIDLRTQPDPHAAAQ--ALMQADLQQDLRVDSGKP 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392313538  227 FDFQ-LTLLPDNHHRLHVNIDLLIMDASSFTLFFDEL----NALLAGESLPAIdTRYDFRSYLLHQQKINQ-PLRDDARA 300
Cdd:PRK10252  120 LVFHqLIQLGDNRWYWYQRYHHLLVDGFSFPAITRRIaaiyCAWLRGEPTPAS-PFTPFADVVEEYQRYRAsEAWQRDAA 198

                         170
                  ....*....|.
gi 392313538  301 YWLAKASTLPP 311
Cdd:PRK10252  199 FWAEQRRQLPP 209
PRK12316 PRK12316
peptide synthase; Provisional
 44-310 7.09e-05

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 44.56  E-value: 7.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392313538   44 NLIQAGLDSIRLMRWLHWFRKNGYRLTLRELYAAPTLAAWNQLMLSRSPENAEEETPpdesswpnmteSTPFPLTPVQHA 123
Cdd:PRK12316 3579 NFFELGGDSIISLQVVSRARQAGIRFTPKDLFQHQTIQGLARVARVGGGVAVDQGPV-----------SGETLLLPIQQQ 3647

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392313538  124 YLTGRMPGQKlggvgcHLYQEF---EGHCLTASQLEQAITTLLQRHPMLHIAFRPDGQqvwlpqpYWNGvtvhdlRHNDA 200
Cdd:PRK12316 3648 FFEEPVPERH------HWNQSLllkPREALDAAALEAALQALVEHHDALRLRFVEDAG-------GWTA------EHLPV 3708

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392313538  201 ESRQAYLdaLRQRLSHRLLRVEIGE----TFDFQ--------LTLLPDNHHRLHVNIDLLIMDASSFTLFFDEL----NA 264
Cdd:PRK12316 3709 ELGGALL--WRAELDDAEELERLGEeaqrSLDLAdgpllralLATLADGSQRLLLVIHHLVVDGVSWRILLEDLqqayQQ 3786

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 392313538  265 LLAGE--SLPAIDTRydFRSYLLHQQK-INQPLRDDARAYWLAK----ASTLP 310
Cdd:PRK12316 3787 LLQGEapRLPAKTSS--FKAWAERLQEhARGEALKAELAYWQEQlqgvSSELP 3837
PRK12316 PRK12316
peptide synthase; Provisional
 42-310 1.82e-04

peptide synthase; Provisional


Pssm-ID: 237054 [Multi-domain]  Cd Length: 5163  Bit Score: 43.41  E-value: 1.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392313538   42 ESNLIQAGLDSIRLMRWLHWFRKNGYRLTLRELYAAPTLAAWNQLMlSRSPENAEEETPPdesswpnmteSTPFPLTPVQ 121
Cdd:PRK12316 1039 DDNFFELGGDSIVSIQVVSRARQAGIQLSPRDLFQHQTIRSLALVA-KAGQATAADQGPA----------SGEVALAPVQ 1107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392313538  122 HAYLTGRMPGQKlggvgcHLYQEFeghCLTASQ------LEQAITTLLQRHPMLHIAFRpdGQQVWLPQPYWNGVTVHDL 195
Cdd:PRK12316 1108 RWFFEQAIPQRQ------HWNQSL---LLQARQpldpdrLGRALERLVAHHDALRLRFR--EEDGGWQQAYAAPQAGEVL 1176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392313538  196 RHNDAESrQAYLDALRQRlSHRLLRVEIGETFDFQLTLLPDNHHRLHVNIDLLIMDASSFTLFFDELNALL--AGESLPA 273
Cdd:PRK12316 1177 WQRQAAS-EEELLALCEE-AQRSLDLEQGPLLRALLVDMADGSQRLLLVIHHLVVDGVSWRILLEDLQRAYadLDADLPA 1254

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 392313538  274 IDTRYDFRSYLLHQQKinqPLRDDARAYWLAK----ASTLP 310
Cdd:PRK12316 1255 RTSSYQAWARRLHEHA---GARAEELDYWQAQledaPHELP 1292
starter-C_NRPS cd19533
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ...
 116-311 1.56e-03

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: 40.05  E-value: 1.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392313538 116 PLTPVQHayltGRMPGQKLGGVGCHL----YQEFEGHCLTASqLEQAITTLLQRHPMLHIAF--RPDGQQVWLPQPYWNG 189
Cdd:cd19533    3 PLTSAQR----GVWFAEQLDPEGSIYnlaeYLEITGPVDLAV-LERALRQVIAEAETLRLRFteEEGEPYQWIDPYTPVP 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 392313538 190 VTVHDLR-HNDAESrqAYLDALRQRLSHRLlRVEIGETFDFQLTLLPDNHHRLHVNIDLLIMDASSFTLFFDEL----NA 264
Cdd:cd19533   78 IRHIDLSgDPDPEG--AAQQWMQEDLRKPL-PLDNDPLFRHALFTLGDNRHFWYQRVHHIVMDGFSFALFGQRVaeiyTA 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 392313538 265 LLAGESLPAidtrYDFRSYLLHQQKINQ----PLRDDARAYWLAKASTLPP 311
Cdd:cd19533  155 LLKGRPAPP----APFGSFLDLVEEEQAyrqsERFERDRAFWTEQFEDLPE 201
 
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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