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Conserved domains on  [gi|22329282|ref|NP_171704|]
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nitroreductase family protein [Arabidopsis thaliana]

Protein Classification

SagB/ThcOx family dehydrogenase( domain architecture ID 10114842)

SagB/ThcOx family dehydrogenase such as Escherichia coli microcin B17-processing protein McbC that is necessary to process the inactive microcin B17 (McbA) precursor into the active peptide

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
McbC_SagB-like_oxidoreductase cd02142
oxidase similar to the microcin B17 processing protein McbC; This family is the oxidase domain ...
 134-296 7.86e-37

oxidase similar to the microcin B17 processing protein McbC; This family is the oxidase domain of NRPS (non-ribosomal peptide synthetase) and other systems that modify polypeptides by cyclizing a thioester to form a ring. These include EpoB, part of the epothilone biosynthesis pathway; TubD, part of the tubulysin biosynthesis pathway, MtsD, part of the myxothiozol biosynthesis pathway; IndC, part of the indigoidine biosynthesis pathway and TfxB, part of the trifitoxin processing pathway. All are FMN-dependent and oxidize the product of the cyclization of thioesters in short polypeptides.


:

Pssm-ID: 380318  Cd Length: 200  Bit Score: 136.40  E-value: 7.86e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329282 134 DSLPPPKPISLPTISHLFYHS--------------LALSAWKTTGSSTWPLRVNPSSGNLHPTEAYLIAPPIPSLSqsAF 199
Cdd:cd02142   8 PNLKPALLATLDLSEALLNRRsrrtfssepltlreLSRLAARGIPGSGYGLRPYPSAGALYPIEVYVIVKNVEGLP--AG 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329282 200 VSHYAPKEHSLEVRAHIP-------SSFFPNFFPENSFLIGISSIFWREAWKYGERAFRYCNHDVGHAIAALSIAAADLG 272
Cdd:cd02142  86 IYHYDPKRHRLVLIREGDfrldlahAAGNQAAFGSAAFSLIIVARFERIAWKYGERAYRYILLEAGHLAQNLYLAATALG 165

                       170       180
                ....*....|....*....|....
gi 22329282 273 WDLKLLDAFGADDLKRLMGLPEFQ 296
Cdd:cd02142 166 LGLCAIGAFDDDALRELLGLDEVE 189
McbC_SagB-like_oxidoreductase cd02142
oxidase similar to the microcin B17 processing protein McbC; This family is the oxidase domain ...
 394-621 8.66e-33

oxidase similar to the microcin B17 processing protein McbC; This family is the oxidase domain of NRPS (non-ribosomal peptide synthetase) and other systems that modify polypeptides by cyclizing a thioester to form a ring. These include EpoB, part of the epothilone biosynthesis pathway; TubD, part of the tubulysin biosynthesis pathway, MtsD, part of the myxothiozol biosynthesis pathway; IndC, part of the indigoidine biosynthesis pathway and TfxB, part of the trifitoxin processing pathway. All are FMN-dependent and oxidize the product of the cyclization of thioesters in short polypeptides.


:

Pssm-ID: 380318  Cd Length: 200  Bit Score: 125.22  E-value: 8.66e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329282 394 SSRALFSHSSYNKLT----VRQVVRTRRSAVDMDAVTCIDM---------SSFYQMLMHCLPSTGESQkeqlalpfralp 460
Cdd:cd02142   1 KSVPLPDPNLKPALLatldLSEALLNRRSRRTFSSEPLTLRelsrlaargIPGSGYGLRPYPSAGALY------------ 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329282 461 wdtaEVHLALFVHRVSGLPKGLYLLVRNeDHlsdlktatrpefewtkpdgcpdnlPLYKLAEGDCQRLAKGLSCHQDIAG 540
Cdd:cd02142  69 ----PIEVYVIVKNVEGLPAGIYHYDPK-RH------------------------RLVLIREGDFRLDLAHAAGNQAAFG 119

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329282 541 DGCFSLGMIARFEPALREKGSWMYPRLFWETGVVGQVLYLEAHAMGISATGIGCYFDDPVHEVLGINDSSFQSLYHFTVG 620
Cdd:cd02142 120 SAAFSLIIVARFERIAWKYGERAYRYILLEAGHLAQNLYLAATALGLGLCAIGAFDDDALRELLGLDEVEEVVLYAFVVG 199


                .
gi 22329282 621 G 621
Cdd:cd02142 200 G 200
 
Name Accession Description Interval E-value
McbC_SagB-like_oxidoreductase cd02142
oxidase similar to the microcin B17 processing protein McbC; This family is the oxidase domain ...
 134-296 7.86e-37

oxidase similar to the microcin B17 processing protein McbC; This family is the oxidase domain of NRPS (non-ribosomal peptide synthetase) and other systems that modify polypeptides by cyclizing a thioester to form a ring. These include EpoB, part of the epothilone biosynthesis pathway; TubD, part of the tubulysin biosynthesis pathway, MtsD, part of the myxothiozol biosynthesis pathway; IndC, part of the indigoidine biosynthesis pathway and TfxB, part of the trifitoxin processing pathway. All are FMN-dependent and oxidize the product of the cyclization of thioesters in short polypeptides.


Pssm-ID: 380318  Cd Length: 200  Bit Score: 136.40  E-value: 7.86e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329282 134 DSLPPPKPISLPTISHLFYHS--------------LALSAWKTTGSSTWPLRVNPSSGNLHPTEAYLIAPPIPSLSqsAF 199
Cdd:cd02142   8 PNLKPALLATLDLSEALLNRRsrrtfssepltlreLSRLAARGIPGSGYGLRPYPSAGALYPIEVYVIVKNVEGLP--AG 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329282 200 VSHYAPKEHSLEVRAHIP-------SSFFPNFFPENSFLIGISSIFWREAWKYGERAFRYCNHDVGHAIAALSIAAADLG 272
Cdd:cd02142  86 IYHYDPKRHRLVLIREGDfrldlahAAGNQAAFGSAAFSLIIVARFERIAWKYGERAYRYILLEAGHLAQNLYLAATALG 165

                       170       180
                ....*....|....*....|....
gi 22329282 273 WDLKLLDAFGADDLKRLMGLPEFQ 296
Cdd:cd02142 166 LGLCAIGAFDDDALRELLGLDEVE 189
McbC_SagB-like_oxidoreductase cd02142
oxidase similar to the microcin B17 processing protein McbC; This family is the oxidase domain ...
 394-621 8.66e-33

oxidase similar to the microcin B17 processing protein McbC; This family is the oxidase domain of NRPS (non-ribosomal peptide synthetase) and other systems that modify polypeptides by cyclizing a thioester to form a ring. These include EpoB, part of the epothilone biosynthesis pathway; TubD, part of the tubulysin biosynthesis pathway, MtsD, part of the myxothiozol biosynthesis pathway; IndC, part of the indigoidine biosynthesis pathway and TfxB, part of the trifitoxin processing pathway. All are FMN-dependent and oxidize the product of the cyclization of thioesters in short polypeptides.


Pssm-ID: 380318  Cd Length: 200  Bit Score: 125.22  E-value: 8.66e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329282 394 SSRALFSHSSYNKLT----VRQVVRTRRSAVDMDAVTCIDM---------SSFYQMLMHCLPSTGESQkeqlalpfralp 460
Cdd:cd02142   1 KSVPLPDPNLKPALLatldLSEALLNRRSRRTFSSEPLTLRelsrlaargIPGSGYGLRPYPSAGALY------------ 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329282 461 wdtaEVHLALFVHRVSGLPKGLYLLVRNeDHlsdlktatrpefewtkpdgcpdnlPLYKLAEGDCQRLAKGLSCHQDIAG 540
Cdd:cd02142  69 ----PIEVYVIVKNVEGLPAGIYHYDPK-RH------------------------RLVLIREGDFRLDLAHAAGNQAAFG 119

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329282 541 DGCFSLGMIARFEPALREKGSWMYPRLFWETGVVGQVLYLEAHAMGISATGIGCYFDDPVHEVLGINDSSFQSLYHFTVG 620
Cdd:cd02142 120 SAAFSLIIVARFERIAWKYGERAYRYILLEAGHLAQNLYLAATALGLGLCAIGAFDDDALRELLGLDEVEEVVLYAFVVG 199


                .
gi 22329282 621 G 621
Cdd:cd02142 200 G 200
antibiot_sagB TIGR03605
SagB-type dehydrogenase domain; SagB of Sterptococcus pyogenes participates in the maturation ...
 143-294 6.56e-17

SagB-type dehydrogenase domain; SagB of Sterptococcus pyogenes participates in the maturation of streptolysin S from a ribosomally produced precursor polypeptide. Chemically similar systems operate on highly diverse sets of bacteriocin precursors in numerous other bacteria. This model describes a domain within SgaB and homologous regions from other proteins, many of which appear to be involved in biosynthesis of secondary metabolites. While some substrates may be intermediates in non-ribosomal peptide syntheses, others are involved in heterocycle-containing bacteriocin biosynthesis, and can be found near SgaC-like (see TIGR03603, cyclodehydratase) and SgaD-like (see TIGR03604, "docking") proteins. Members of this domain family are heterogeneous in length, as many have a partial second copy of the domain represented here. The incomplete second domain scores below the cutoffs to this model in most cases.


Pssm-ID: 188352  Cd Length: 173  Bit Score: 78.88  E-value: 6.56e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329282   143 SLPTISHLFYHSLALSAWKTT-GSSTWPLRVNPSSGNLHPTEAYLIAPPIPSLSQSAFvsHYAPKEHSLEVRAHIPSSF- 220
Cdd:TIGR03605   1 TLEELSQLLWYSAGVRSIKLPyNDGILFRRPYPSGGGLYPLEIYLYVKNIEGLPDGVY--HYDPEEHRLILIRAGEENVd 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329282   221 ----FPNFFPEN----SFLIGISSIFWREAWKYGERAFRYCNHDVGHAIAALSIAAADLGWDLKLLDAFGADDLKRLMGL 292
Cdd:TIGR03605  79 aflvNALLNAENanppPVIIFITARFWKNFWKYGNRAYRLALLDVGIIIQNFYLVATALGLGSCAIGGFDDDYIAELLGL 158


                  ..
gi 22329282   293 PE 294
Cdd:TIGR03605 159 DG 160
antibiot_sagB TIGR03605
SagB-type dehydrogenase domain; SagB of Sterptococcus pyogenes participates in the maturation ...
 465-620 1.33e-07

SagB-type dehydrogenase domain; SagB of Sterptococcus pyogenes participates in the maturation of streptolysin S from a ribosomally produced precursor polypeptide. Chemically similar systems operate on highly diverse sets of bacteriocin precursors in numerous other bacteria. This model describes a domain within SgaB and homologous regions from other proteins, many of which appear to be involved in biosynthesis of secondary metabolites. While some substrates may be intermediates in non-ribosomal peptide syntheses, others are involved in heterocycle-containing bacteriocin biosynthesis, and can be found near SgaC-like (see TIGR03603, cyclodehydratase) and SgaD-like (see TIGR03604, "docking") proteins. Members of this domain family are heterogeneous in length, as many have a partial second copy of the domain represented here. The incomplete second domain scores below the cutoffs to this model in most cases.


Pssm-ID: 188352  Cd Length: 173  Bit Score: 51.92  E-value: 1.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329282   465 EVHLALFVHRVSGLPKGLYllvrnedHLsdlktatrpefewtkpdgCPDNLPLYKLAEGDCQRLAKGLSCHQDI--AGDG 542
Cdd:TIGR03605  40 PLEIYLYVKNIEGLPDGVY-------HY------------------DPEEHRLILIRAGEENVDAFLVNALLNAenANPP 94

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22329282   543 CFSLGMIARFEPALREKGSWMYPRLFWETGVVGQVLYLEAHAMGISATGIGCYFDDPVHEVLGINDSSFQSLYHFTVG 620
Cdd:TIGR03605  95 PVIIFITARFWKNFWKYGNRAYRLALLDVGIIIQNFYLVATALGLGSCAIGGFDDDYIAELLGLDGIEEHVVGVFPVG 172
Nitroreductase pfam00881
Nitroreductase family; The nitroreductase family comprises a group of FMN- or FAD-dependent ...
 483-620 6.33e-05

Nitroreductase family; The nitroreductase family comprises a group of FMN- or FAD-dependent and NAD(P)H-dependent enzymes able to metabolize nitrosubstituted compounds.


Pssm-ID: 425926 [Multi-domain]  Cd Length: 168  Bit Score: 43.92  E-value: 6.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329282   483 YLLVRNEDHLSDLKTATRPEfeWTKPDGCPDNLPLYKLAEGDCqrlakglsCHQDIAGDGCFSLGMIARFEPALREKGSW 562
Cdd:pfam00881  41 FYVVTDGELRYRLAEAALEL--LLVEPAAALLLLLRRDANLKL--------LLQDFLRGAPVLIVITASLSTYLRKAAER 110

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 22329282   563 MYPRLFWETGVVGQVLYLEAHAMGISATGIGCYFDDPVHEVLGInDSSFQSLYHFTVG 620
Cdd:pfam00881 111 AYREALLDAGAAAQNLLLAATSLGLGSCPIGGFDAAAVRELLGL-PDDERLVGLIAVG 167
NfnB COG0778
Nitroreductase [Energy production and conversion]; Nitroreductase is part of the Pathway ...
 555-622 5.27e-04

Nitroreductase [Energy production and conversion]; Nitroreductase is part of the Pathway/BioSystem: Pyrimidine degradation


Pssm-ID: 440541 [Multi-domain]  Cd Length: 163  Bit Score: 40.99  E-value: 5.27e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329282 555 ALREKGSWMYPRLFWE--TGVVGQVLYLEAHAMGISATGIGCYFDDPVHEVLGInDSSFQSLYHFTVGGP 622
Cdd:COG0778  79 CADPDRSEKVPERYALldAGIAAQNLLLAARALGLGTCWIGGFDPEKVRELLGL-PEGEEPVALLALGYP 147
Nitroreductase pfam00881
Nitroreductase family; The nitroreductase family comprises a group of FMN- or FAD-dependent ...
 139-300 7.23e-03

Nitroreductase family; The nitroreductase family comprises a group of FMN- or FAD-dependent and NAD(P)H-dependent enzymes able to metabolize nitrosubstituted compounds.


Pssm-ID: 425926 [Multi-domain]  Cd Length: 168  Bit Score: 37.76  E-value: 7.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329282   139 PKPISLPTISHLFyhSLALSAwkttgsstwplrvnPSSGNLHPTEAYLIAPP--IPSLSQSAF--VSHYAPKEHSLEVRA 214
Cdd:pfam00881  12 PEPVPKEVLEEIL--EAARRA--------------PSAGNLQPWRFYVVTDGelRYRLAEAALelLLVEPAAALLLLLRR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329282   215 HIPSSFFPNFFPENS-FLIGISSIFWREAWKYGERAFRYCNHDVGHAIAALSIAAADLGWDLKLLDAFGADDLKRLMGLP 293
Cdd:pfam00881  76 DANLKLLLQDFLRGApVLIVITASLSTYLRKAAERAYREALLDAGAAAQNLLLAATSLGLGSCPIGGFDAAAVRELLGLP 155


                  ....*..
gi 22329282   294 EFQLPEG 300
Cdd:pfam00881 156 DDERLVG 162
 
Name Accession Description Interval E-value
McbC_SagB-like_oxidoreductase cd02142
oxidase similar to the microcin B17 processing protein McbC; This family is the oxidase domain ...
 134-296 7.86e-37

oxidase similar to the microcin B17 processing protein McbC; This family is the oxidase domain of NRPS (non-ribosomal peptide synthetase) and other systems that modify polypeptides by cyclizing a thioester to form a ring. These include EpoB, part of the epothilone biosynthesis pathway; TubD, part of the tubulysin biosynthesis pathway, MtsD, part of the myxothiozol biosynthesis pathway; IndC, part of the indigoidine biosynthesis pathway and TfxB, part of the trifitoxin processing pathway. All are FMN-dependent and oxidize the product of the cyclization of thioesters in short polypeptides.


Pssm-ID: 380318  Cd Length: 200  Bit Score: 136.40  E-value: 7.86e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329282 134 DSLPPPKPISLPTISHLFYHS--------------LALSAWKTTGSSTWPLRVNPSSGNLHPTEAYLIAPPIPSLSqsAF 199
Cdd:cd02142   8 PNLKPALLATLDLSEALLNRRsrrtfssepltlreLSRLAARGIPGSGYGLRPYPSAGALYPIEVYVIVKNVEGLP--AG 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329282 200 VSHYAPKEHSLEVRAHIP-------SSFFPNFFPENSFLIGISSIFWREAWKYGERAFRYCNHDVGHAIAALSIAAADLG 272
Cdd:cd02142  86 IYHYDPKRHRLVLIREGDfrldlahAAGNQAAFGSAAFSLIIVARFERIAWKYGERAYRYILLEAGHLAQNLYLAATALG 165

                       170       180
                ....*....|....*....|....
gi 22329282 273 WDLKLLDAFGADDLKRLMGLPEFQ 296
Cdd:cd02142 166 LGLCAIGAFDDDALRELLGLDEVE 189
McbC_SagB-like_oxidoreductase cd02142
oxidase similar to the microcin B17 processing protein McbC; This family is the oxidase domain ...
 394-621 8.66e-33

oxidase similar to the microcin B17 processing protein McbC; This family is the oxidase domain of NRPS (non-ribosomal peptide synthetase) and other systems that modify polypeptides by cyclizing a thioester to form a ring. These include EpoB, part of the epothilone biosynthesis pathway; TubD, part of the tubulysin biosynthesis pathway, MtsD, part of the myxothiozol biosynthesis pathway; IndC, part of the indigoidine biosynthesis pathway and TfxB, part of the trifitoxin processing pathway. All are FMN-dependent and oxidize the product of the cyclization of thioesters in short polypeptides.


Pssm-ID: 380318  Cd Length: 200  Bit Score: 125.22  E-value: 8.66e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329282 394 SSRALFSHSSYNKLT----VRQVVRTRRSAVDMDAVTCIDM---------SSFYQMLMHCLPSTGESQkeqlalpfralp 460
Cdd:cd02142   1 KSVPLPDPNLKPALLatldLSEALLNRRSRRTFSSEPLTLRelsrlaargIPGSGYGLRPYPSAGALY------------ 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329282 461 wdtaEVHLALFVHRVSGLPKGLYLLVRNeDHlsdlktatrpefewtkpdgcpdnlPLYKLAEGDCQRLAKGLSCHQDIAG 540
Cdd:cd02142  69 ----PIEVYVIVKNVEGLPAGIYHYDPK-RH------------------------RLVLIREGDFRLDLAHAAGNQAAFG 119

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329282 541 DGCFSLGMIARFEPALREKGSWMYPRLFWETGVVGQVLYLEAHAMGISATGIGCYFDDPVHEVLGINDSSFQSLYHFTVG 620
Cdd:cd02142 120 SAAFSLIIVARFERIAWKYGERAYRYILLEAGHLAQNLYLAATALGLGLCAIGAFDDDALRELLGLDEVEEVVLYAFVVG 199


                .
gi 22329282 621 G 621
Cdd:cd02142 200 G 200
antibiot_sagB TIGR03605
SagB-type dehydrogenase domain; SagB of Sterptococcus pyogenes participates in the maturation ...
 143-294 6.56e-17

SagB-type dehydrogenase domain; SagB of Sterptococcus pyogenes participates in the maturation of streptolysin S from a ribosomally produced precursor polypeptide. Chemically similar systems operate on highly diverse sets of bacteriocin precursors in numerous other bacteria. This model describes a domain within SgaB and homologous regions from other proteins, many of which appear to be involved in biosynthesis of secondary metabolites. While some substrates may be intermediates in non-ribosomal peptide syntheses, others are involved in heterocycle-containing bacteriocin biosynthesis, and can be found near SgaC-like (see TIGR03603, cyclodehydratase) and SgaD-like (see TIGR03604, "docking") proteins. Members of this domain family are heterogeneous in length, as many have a partial second copy of the domain represented here. The incomplete second domain scores below the cutoffs to this model in most cases.


Pssm-ID: 188352  Cd Length: 173  Bit Score: 78.88  E-value: 6.56e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329282   143 SLPTISHLFYHSLALSAWKTT-GSSTWPLRVNPSSGNLHPTEAYLIAPPIPSLSQSAFvsHYAPKEHSLEVRAHIPSSF- 220
Cdd:TIGR03605   1 TLEELSQLLWYSAGVRSIKLPyNDGILFRRPYPSGGGLYPLEIYLYVKNIEGLPDGVY--HYDPEEHRLILIRAGEENVd 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329282   221 ----FPNFFPEN----SFLIGISSIFWREAWKYGERAFRYCNHDVGHAIAALSIAAADLGWDLKLLDAFGADDLKRLMGL 292
Cdd:TIGR03605  79 aflvNALLNAENanppPVIIFITARFWKNFWKYGNRAYRLALLDVGIIIQNFYLVATALGLGSCAIGGFDDDYIAELLGL 158


                  ..
gi 22329282   293 PE 294
Cdd:TIGR03605 159 DG 160
antibiot_sagB TIGR03605
SagB-type dehydrogenase domain; SagB of Sterptococcus pyogenes participates in the maturation ...
 465-620 1.33e-07

SagB-type dehydrogenase domain; SagB of Sterptococcus pyogenes participates in the maturation of streptolysin S from a ribosomally produced precursor polypeptide. Chemically similar systems operate on highly diverse sets of bacteriocin precursors in numerous other bacteria. This model describes a domain within SgaB and homologous regions from other proteins, many of which appear to be involved in biosynthesis of secondary metabolites. While some substrates may be intermediates in non-ribosomal peptide syntheses, others are involved in heterocycle-containing bacteriocin biosynthesis, and can be found near SgaC-like (see TIGR03603, cyclodehydratase) and SgaD-like (see TIGR03604, "docking") proteins. Members of this domain family are heterogeneous in length, as many have a partial second copy of the domain represented here. The incomplete second domain scores below the cutoffs to this model in most cases.


Pssm-ID: 188352  Cd Length: 173  Bit Score: 51.92  E-value: 1.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329282   465 EVHLALFVHRVSGLPKGLYllvrnedHLsdlktatrpefewtkpdgCPDNLPLYKLAEGDCQRLAKGLSCHQDI--AGDG 542
Cdd:TIGR03605  40 PLEIYLYVKNIEGLPDGVY-------HY------------------DPEEHRLILIRAGEENVDAFLVNALLNAenANPP 94

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22329282   543 CFSLGMIARFEPALREKGSWMYPRLFWETGVVGQVLYLEAHAMGISATGIGCYFDDPVHEVLGINDSSFQSLYHFTVG 620
Cdd:TIGR03605  95 PVIIFITARFWKNFWKYGNRAYRLALLDVGIIIQNFYLVATALGLGSCAIGGFDDDYIAELLGLDGIEEHVVGVFPVG 172
Nitroreductase pfam00881
Nitroreductase family; The nitroreductase family comprises a group of FMN- or FAD-dependent ...
 483-620 6.33e-05

Nitroreductase family; The nitroreductase family comprises a group of FMN- or FAD-dependent and NAD(P)H-dependent enzymes able to metabolize nitrosubstituted compounds.


Pssm-ID: 425926 [Multi-domain]  Cd Length: 168  Bit Score: 43.92  E-value: 6.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329282   483 YLLVRNEDHLSDLKTATRPEfeWTKPDGCPDNLPLYKLAEGDCqrlakglsCHQDIAGDGCFSLGMIARFEPALREKGSW 562
Cdd:pfam00881  41 FYVVTDGELRYRLAEAALEL--LLVEPAAALLLLLRRDANLKL--------LLQDFLRGAPVLIVITASLSTYLRKAAER 110

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 22329282   563 MYPRLFWETGVVGQVLYLEAHAMGISATGIGCYFDDPVHEVLGInDSSFQSLYHFTVG 620
Cdd:pfam00881 111 AYREALLDAGAAAQNLLLAATSLGLGSCPIGGFDAAAVRELLGL-PDDERLVGLIAVG 167
NfnB COG0778
Nitroreductase [Energy production and conversion]; Nitroreductase is part of the Pathway ...
 555-622 5.27e-04

Nitroreductase [Energy production and conversion]; Nitroreductase is part of the Pathway/BioSystem: Pyrimidine degradation


Pssm-ID: 440541 [Multi-domain]  Cd Length: 163  Bit Score: 40.99  E-value: 5.27e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329282 555 ALREKGSWMYPRLFWE--TGVVGQVLYLEAHAMGISATGIGCYFDDPVHEVLGInDSSFQSLYHFTVGGP 622
Cdd:COG0778  79 CADPDRSEKVPERYALldAGIAAQNLLLAARALGLGTCWIGGFDPEKVRELLGL-PEGEEPVALLALGYP 147
Nitroreductase pfam00881
Nitroreductase family; The nitroreductase family comprises a group of FMN- or FAD-dependent ...
 139-300 7.23e-03

Nitroreductase family; The nitroreductase family comprises a group of FMN- or FAD-dependent and NAD(P)H-dependent enzymes able to metabolize nitrosubstituted compounds.


Pssm-ID: 425926 [Multi-domain]  Cd Length: 168  Bit Score: 37.76  E-value: 7.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329282   139 PKPISLPTISHLFyhSLALSAwkttgsstwplrvnPSSGNLHPTEAYLIAPP--IPSLSQSAF--VSHYAPKEHSLEVRA 214
Cdd:pfam00881  12 PEPVPKEVLEEIL--EAARRA--------------PSAGNLQPWRFYVVTDGelRYRLAEAALelLLVEPAAALLLLLRR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329282   215 HIPSSFFPNFFPENS-FLIGISSIFWREAWKYGERAFRYCNHDVGHAIAALSIAAADLGWDLKLLDAFGADDLKRLMGLP 293
Cdd:pfam00881  76 DANLKLLLQDFLRGApVLIVITASLSTYLRKAAERAYREALLDAGAAAQNLLLAATSLGLGSCPIGGFDAAAVRELLGLP 155


                  ....*..
gi 22329282   294 EFQLPEG 300
Cdd:pfam00881 156 DDERLVG 162
 
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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