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Conserved domains on  [gi|1836039599|gb|QJG51823|]
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type-F conjugative transfer system pilin assembly thiol-disulfide isomerase TrbB (plasmid) [Escherichia coli]

Protein Classification

type-F conjugative transfer system pilin assembly thiol-disulfide isomerase TrbB( domain architecture ID 10014381)

type-F conjugative transfer system pilin assembly thiol-disulfide isomerase TrbB is part of a large group of proteins involved in conjugative transfer of plasmid DNA, specifically the F-type system

CATH:  3.40.30.10
PubMed:  16321931|15558583|10049365|12074972

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK13728 PRK13728
conjugal transfer protein TrbB; Provisional
 1-181 1.80e-112

conjugal transfer protein TrbB; Provisional


:

Pssm-ID: 237484  Cd Length: 181  Bit Score: 317.43  E-value: 1.80e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836039599   1 MSLIKSLLFTLLLAAAAVQASTRDEIERLWNPQGMAAQPAQPAAGTSARTEKPAPRWFRLSNGRQVNLADWKVVLFMQGH 80
Cdd:PRK13728    1 MSLTKLLLVLLLLMATAVQASTRDEIERLWNPKGMAAQPAQPAADTSARTEKPAPRWFRLSNGRQVNLADWKVVLFMQGH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836039599  81 CPYCHQFDPVLKQLAQQYGFSVFPYTLDGQGDTAFPEALPVPPDVMQTFFPNIPVATPTTFLVNVNTLEALPLLQGATDA 160
Cdd:PRK13728   81 CPYCHQFDPVLKQLAQQYGFSVFPYTLDGQGDTAFPEALPAPPDVMQTFFPNIPVATPTTFLVNVNTLEALPLLQGATDA 160

                         170       180
                  ....*....|....*....|.
gi 1836039599 161 AGFMARMDTVLQMYGGKKGAK 181
Cdd:PRK13728  161 AGFMARMDTVLQMYGGKKGAK 181
 
Name Accession Description Interval E-value
PRK13728 PRK13728
conjugal transfer protein TrbB; Provisional
 1-181 1.80e-112

conjugal transfer protein TrbB; Provisional


Pssm-ID: 237484  Cd Length: 181  Bit Score: 317.43  E-value: 1.80e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836039599   1 MSLIKSLLFTLLLAAAAVQASTRDEIERLWNPQGMAAQPAQPAAGTSARTEKPAPRWFRLSNGRQVNLADWKVVLFMQGH 80
Cdd:PRK13728    1 MSLTKLLLVLLLLMATAVQASTRDEIERLWNPKGMAAQPAQPAADTSARTEKPAPRWFRLSNGRQVNLADWKVVLFMQGH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836039599  81 CPYCHQFDPVLKQLAQQYGFSVFPYTLDGQGDTAFPEALPVPPDVMQTFFPNIPVATPTTFLVNVNTLEALPLLQGATDA 160
Cdd:PRK13728   81 CPYCHQFDPVLKQLAQQYGFSVFPYTLDGQGDTAFPEALPAPPDVMQTFFPNIPVATPTTFLVNVNTLEALPLLQGATDA 160

                         170       180
                  ....*....|....*....|.
gi 1836039599 161 AGFMARMDTVLQMYGGKKGAK 181
Cdd:PRK13728  161 AGFMARMDTVLQMYGGKKGAK 181
TrbB TIGR02738
type-F conjugative transfer system pilin assembly thiol-disulfide isomerase TrbB; This protein ...
 21-171 1.25e-64

type-F conjugative transfer system pilin assembly thiol-disulfide isomerase TrbB; This protein is part of a large group of proteins involved in conjugative transfer of plasmid DNA, specifically the F-type system. This protein has been predicted to contain a thioredoxin fold, contains a conserved pair of cysteines and has been shown to function as a thiol disulfide isomerase by complementation of an Ecoli DsbA defect. The protein is believed to be involved in pilin assembly. The protein is closely related to TraF (TIGR02739) which is somewhat longer, lacks the cysteine motif and is apparently not functional as a disulfide bond isomerase.


Pssm-ID: 131785  Cd Length: 153  Bit Score: 195.41  E-value: 1.25e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836039599  21 STRDEIERLWNPQgmaaqpaqpAAGTSARTEKPAprwfrlsnGRQVNLADWKVVLFMQGHCPYCHQFDPVLKQLAQQYGF 100
Cdd:TIGR02738  19 STLDEITNLWAPP---------QGLTAATDNAPQ--------GRHANQDDYALVFFYQSTCPYCHQFAPVLKRFSQQFGL 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1836039599 101 SVFPYTLDGQGDTAFPEALPVPPDVMQTFFPN-IPVATPTTFLVNVNTLEALPLLQGATDAAGFMARMDTVL 171
Cdd:TIGR02738  82 PVYAFSLDGQGLTGFPDPLPATPEVMQTFFPNpRPVVTPATFLVNVNTRKAYPVLQGAVDEAELANRMDEIL 153
TraF pfam13728
F plasmid transfer operon protein; TraF protein undergoes proteolytic processing associated ...
 67-173 1.50e-12

F plasmid transfer operon protein; TraF protein undergoes proteolytic processing associated with export. The 19 amino acids at the amino terminus of the polypeptides appear to constitute a typical membrane leader peptide - not included in this family, while the remainder of the molecule is predicted to be primarily hydrophilic in character. F plasmid TraF and TraH are required for F pilus assembly and F plasmid transfer, and they are both localized to the outer membrane in the presence of the complete F transfer region, especially TraV, the putative anchor.


Pssm-ID: 433436 [Multi-domain]  Cd Length: 224  Bit Score: 63.48  E-value: 1.50e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836039599  67 NLAD-WKVVLFMQGHCPYCHQFDPVLKQLAQQYGFSVFPYTLDGQGDTAFPEAlpvPPDVMQTFFPNIPVaTPTTFLVNV 145
Cdd:pfam13728 126 SLAEeFGLIFFYRGDCPYCEAQAPILQAFADKYGWTVRPVSVDGRPLPGFPNY---RVDNGQAARLGVKR-TPALFLVNP 201

                          90       100
                  ....*....|....*....|....*...
gi 1836039599 146 NTLEALPLlqgatdAAGFMArMDTVLQM 173
Cdd:pfam13728 202 PSGDVVPV------AAGVLS-LDELEER 222
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 52-144 1.10e-07

Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 48.53  E-value: 1.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836039599  52 KPAPRW-FRLSNGRQVNLADW--KVVL--FMQGHCPYCHQFDPVLKQLAQQY-GFSVFPYTLDGQGDTA------FPEAL 119
Cdd:COG0526     6 KPAPDFtLTDLDGKPLSLADLkgKPVLvnFWATWCPPCRAEMPVLKELAEEYgGVVFVGVDVDENPEAVkaflkeLGLPY 85

                          90       100
                  ....*....|....*....|....*.
gi 1836039599 120 PVPPDVMQTFFPNIPV-ATPTTFLVN 144
Cdd:COG0526    86 PVLLDPDGELAKAYGVrGIPTTVLID 111
DsbA_DsbC_DsbG cd03020
DsbA family, DsbC and DsbG subfamily; V-shaped homodimeric proteins containing a redox active ...
 72-114 2.28e-04

DsbA family, DsbC and DsbG subfamily; V-shaped homodimeric proteins containing a redox active CXXC motif imbedded in a TRX fold. They function as protein disulfide isomerases and chaperones in the bacterial periplasm to correct non-native disulfide bonds formed by DsbA and prevent aggregation of incorrectly folded proteins. DsbC and DsbG are kept in their reduced state by the cytoplasmic membrane protein DsbD, which utilizes the TRX/TRX reductase system in the cytosol as a source of reducing equivalents. DsbG differ from DsbC in that it has a more limited substrate specificity, and it may preferentially act later in the folding process to catalyze disulfide rearrangements in folded or partially folded proteins. Also included in the alignment is the predicted protein TrbB, whose gene was sequenced from the enterohemorrhagic E. coli type IV pilus gene cluster, which is required for efficient plasmid transfer.


Pssm-ID: 239318 [Multi-domain]  Cd Length: 197  Bit Score: 39.99  E-value: 2.28e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1836039599  72 KVVLFMQGHCPYCHQFDPVLKQLAQQYGFSVFPYTLDGQGDTA 114
Cdd:cd03020    80 VVYVFTDPDCPYCRKLEKELKPNADGVTVRIFPVPILGLPDST 122
 
Name Accession Description Interval E-value
PRK13728 PRK13728
conjugal transfer protein TrbB; Provisional
 1-181 1.80e-112

conjugal transfer protein TrbB; Provisional


Pssm-ID: 237484  Cd Length: 181  Bit Score: 317.43  E-value: 1.80e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836039599   1 MSLIKSLLFTLLLAAAAVQASTRDEIERLWNPQGMAAQPAQPAAGTSARTEKPAPRWFRLSNGRQVNLADWKVVLFMQGH 80
Cdd:PRK13728    1 MSLTKLLLVLLLLMATAVQASTRDEIERLWNPKGMAAQPAQPAADTSARTEKPAPRWFRLSNGRQVNLADWKVVLFMQGH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836039599  81 CPYCHQFDPVLKQLAQQYGFSVFPYTLDGQGDTAFPEALPVPPDVMQTFFPNIPVATPTTFLVNVNTLEALPLLQGATDA 160
Cdd:PRK13728   81 CPYCHQFDPVLKQLAQQYGFSVFPYTLDGQGDTAFPEALPAPPDVMQTFFPNIPVATPTTFLVNVNTLEALPLLQGATDA 160

                         170       180
                  ....*....|....*....|.
gi 1836039599 161 AGFMARMDTVLQMYGGKKGAK 181
Cdd:PRK13728  161 AGFMARMDTVLQMYGGKKGAK 181
TrbB TIGR02738
type-F conjugative transfer system pilin assembly thiol-disulfide isomerase TrbB; This protein ...
 21-171 1.25e-64

type-F conjugative transfer system pilin assembly thiol-disulfide isomerase TrbB; This protein is part of a large group of proteins involved in conjugative transfer of plasmid DNA, specifically the F-type system. This protein has been predicted to contain a thioredoxin fold, contains a conserved pair of cysteines and has been shown to function as a thiol disulfide isomerase by complementation of an Ecoli DsbA defect. The protein is believed to be involved in pilin assembly. The protein is closely related to TraF (TIGR02739) which is somewhat longer, lacks the cysteine motif and is apparently not functional as a disulfide bond isomerase.


Pssm-ID: 131785  Cd Length: 153  Bit Score: 195.41  E-value: 1.25e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836039599  21 STRDEIERLWNPQgmaaqpaqpAAGTSARTEKPAprwfrlsnGRQVNLADWKVVLFMQGHCPYCHQFDPVLKQLAQQYGF 100
Cdd:TIGR02738  19 STLDEITNLWAPP---------QGLTAATDNAPQ--------GRHANQDDYALVFFYQSTCPYCHQFAPVLKRFSQQFGL 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1836039599 101 SVFPYTLDGQGDTAFPEALPVPPDVMQTFFPN-IPVATPTTFLVNVNTLEALPLLQGATDAAGFMARMDTVL 171
Cdd:TIGR02738  82 PVYAFSLDGQGLTGFPDPLPATPEVMQTFFPNpRPVVTPATFLVNVNTRKAYPVLQGAVDEAELANRMDEIL 153
TraF pfam13728
F plasmid transfer operon protein; TraF protein undergoes proteolytic processing associated ...
 67-173 1.50e-12

F plasmid transfer operon protein; TraF protein undergoes proteolytic processing associated with export. The 19 amino acids at the amino terminus of the polypeptides appear to constitute a typical membrane leader peptide - not included in this family, while the remainder of the molecule is predicted to be primarily hydrophilic in character. F plasmid TraF and TraH are required for F pilus assembly and F plasmid transfer, and they are both localized to the outer membrane in the presence of the complete F transfer region, especially TraV, the putative anchor.


Pssm-ID: 433436 [Multi-domain]  Cd Length: 224  Bit Score: 63.48  E-value: 1.50e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836039599  67 NLAD-WKVVLFMQGHCPYCHQFDPVLKQLAQQYGFSVFPYTLDGQGDTAFPEAlpvPPDVMQTFFPNIPVaTPTTFLVNV 145
Cdd:pfam13728 126 SLAEeFGLIFFYRGDCPYCEAQAPILQAFADKYGWTVRPVSVDGRPLPGFPNY---RVDNGQAARLGVKR-TPALFLVNP 201

                          90       100
                  ....*....|....*....|....*...
gi 1836039599 146 NTLEALPLlqgatdAAGFMArMDTVLQM 173
Cdd:pfam13728 202 PSGDVVPV------AAGVLS-LDELEER 222
TraF-like TIGR02740
TraF-like protein; This protein is related to the F-type conjugation system pilus assembly ...
 76-166 4.06e-11

TraF-like protein; This protein is related to the F-type conjugation system pilus assembly proteins TraF (TIGR02739)and TrbB (TIGR02738) both of which exhibit a thioredoxin fold. The protein represented by this model has the same length and architecture as TraF, but lacks the CXXC-motif found in TrbB and believed to be responsible for the disulfide isomerase activity of that protein.


Pssm-ID: 274275  Cd Length: 271  Bit Score: 59.73  E-value: 4.06e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836039599  76 FMQGHCPYCHQFDPVLKQLAQQYGFSVFPYTLDGQGDTAFPEALpvpPDVMQTFFPNIpVATPTTFLVNVNTLEALPLLQ 155
Cdd:TIGR02740 173 FFKSDCPYCHQQAPILQAFEDRYGIEVLPVSVDGGPLPGFPNAR---PDAGQAQQLKI-RTVPAVFLADPDPNQFTPIGF 248

                          90
                  ....*....|.
gi 1836039599 156 GATDAAGFMAR 166
Cdd:TIGR02740 249 GVMSADELVDR 259
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 52-144 1.10e-07

Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 48.53  E-value: 1.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836039599  52 KPAPRW-FRLSNGRQVNLADW--KVVL--FMQGHCPYCHQFDPVLKQLAQQY-GFSVFPYTLDGQGDTA------FPEAL 119
Cdd:COG0526     6 KPAPDFtLTDLDGKPLSLADLkgKPVLvnFWATWCPPCRAEMPVLKELAEEYgGVVFVGVDVDENPEAVkaflkeLGLPY 85

                          90       100
                  ....*....|....*....|....*.
gi 1836039599 120 PVPPDVMQTFFPNIPV-ATPTTFLVN 144
Cdd:COG0526    86 PVLLDPDGELAKAYGVrGIPTTVLID 111
DsbA_DsbC_DsbG cd03020
DsbA family, DsbC and DsbG subfamily; V-shaped homodimeric proteins containing a redox active ...
 72-114 2.28e-04

DsbA family, DsbC and DsbG subfamily; V-shaped homodimeric proteins containing a redox active CXXC motif imbedded in a TRX fold. They function as protein disulfide isomerases and chaperones in the bacterial periplasm to correct non-native disulfide bonds formed by DsbA and prevent aggregation of incorrectly folded proteins. DsbC and DsbG are kept in their reduced state by the cytoplasmic membrane protein DsbD, which utilizes the TRX/TRX reductase system in the cytosol as a source of reducing equivalents. DsbG differ from DsbC in that it has a more limited substrate specificity, and it may preferentially act later in the folding process to catalyze disulfide rearrangements in folded or partially folded proteins. Also included in the alignment is the predicted protein TrbB, whose gene was sequenced from the enterohemorrhagic E. coli type IV pilus gene cluster, which is required for efficient plasmid transfer.


Pssm-ID: 239318 [Multi-domain]  Cd Length: 197  Bit Score: 39.99  E-value: 2.28e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1836039599  72 KVVLFMQGHCPYCHQFDPVLKQLAQQYGFSVFPYTLDGQGDTA 114
Cdd:cd03020    80 VVYVFTDPDCPYCRKLEKELKPNADGVTVRIFPVPILGLPDST 122
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
62-144 2.48e-04

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 39.08  E-value: 2.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836039599  62 NGRQVNLADWK----VVLFMQGHCPYCHQ-----------------------FDPV--LKQLAQQYGFSvFPYTLDGQGD 112
Cdd:COG1225    10 DGKTVSLSDLRgkpvVLYFYATWCPGCTAelpelrdlyeefkdkgvevlgvsSDSDeaHKKFAEKYGLP-FPLLSDPDGE 88

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1836039599 113 TAfpEALPVPpdvmqtffpnipvATPTTFLVN 144
Cdd:COG1225    89 VA--KAYGVR-------------GTPTTFLID 105
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 62-144 7.34e-04

TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are bacterial protein disulfide reductases with important roles in cytochrome maturation. They are membrane-anchored proteins with a soluble TRX domain containing a CXXC motif located in the periplasm. The TRX domains of this family contain an insert, approximately 25 residues in length, which correspond to an extra alpha helix and a beta strand when compared with TRX. TlpA catalyzes an essential reaction in the biogenesis of cytochrome aa3, while ResA and DsbE are essential proteins in cytochrome c maturation. Also included in this family are proteins containing a TlpA-like TRX domain with domain architectures similar to E. coli DipZ protein, and the N-terminal TRX domain of PilB protein from Neisseria which acts as a disulfide reductase that can recylce methionine sulfoxide reductases.


Pssm-ID: 239264 [Multi-domain]  Cd Length: 116  Bit Score: 37.60  E-value: 7.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836039599  62 NGRQVNLADW--KVVL--FMQGHCPYCHQFDPVLKQLAQQY---GFSVFPYTLDGQGDTAFPEAL-------PVPPDVMQ 127
Cdd:cd02966     8 DGKPVSLSDLkgKVVLvnFWASWCPPCRAEMPELEALAKEYkddGVEVVGVNVDDDDPAAVKAFLkkygitfPVLLDPDG 87

                          90
                  ....*....|....*...
gi 1836039599 128 TFFPNIPV-ATPTTFLVN 144
Cdd:cd02966    88 ELAKAYGVrGLPTTFLID 105
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 73-99 7.69e-04

TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a TRX domain; and Group II, which are composed of fusion proteins of TRX and additional domains. Group I TRX is a small ancient protein that alter the redox state of target proteins via the reversible oxidation of an active site dithiol, present in a CXXC motif, partially exposed at the protein's surface. TRX reduces protein disulfide bonds, resulting in a disulfide bond at its active site. Oxidized TRX is converted to the active form by TRX reductase, using reducing equivalents derived from either NADPH or ferredoxins. By altering their redox state, TRX regulates the functions of at least 30 target proteins, some of which are enzymes and transcription factors. It also plays an important role in the defense against oxidative stress by directly reducing hydrogen peroxide and certain radicals, and by serving as a reductant for peroxiredoxins. At least two major types of functional TRXs have been reported in most organisms; in eukaryotes, they are located in the cytoplasm and the mitochondria. Higher plants contain more types (at least 20 TRX genes have been detected in the genome of Arabidopsis thaliana), two of which (types f amd m) are located in the same compartment, the chloroplast. Also included in the alignment are TRX-like domains which show sequence homology to TRX but do not contain the redox active CXXC motif. Group II proteins, in addition to either a redox active TRX or a TRX-like domain, also contain additional domains, which may or may not possess homology to known proteins.


Pssm-ID: 239245 [Multi-domain]  Cd Length: 93  Bit Score: 37.15  E-value: 7.69e-04
                          10        20
                  ....*....|....*....|....*..
gi 1836039599  73 VVLFMQGHCPYCHQFDPVLKQLAQQYG 99
Cdd:cd02947    14 VVDFWAPWCGPCKAIAPVLEELAEEYP 40
DsbG COG1651
Protein thiol-disulfide isomerase DsbC [Posttranslational modification, protein turnover, ...
 72-114 9.98e-04

Protein thiol-disulfide isomerase DsbC [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441257 [Multi-domain]  Cd Length: 152  Bit Score: 37.67  E-value: 9.98e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1836039599  72 KVVLFMQGHCPYCHQFDPVLKQLAQQYG-----FSVFPYTLDGQGDTA 114
Cdd:COG1651     3 TVVEFFDYQCPYCARFHPELPELLKKYVdgkvrVVYRPFPLLHPDSLR 50
PRX_like1 cd02969
Peroxiredoxin (PRX)-like 1 family; hypothetical proteins that show sequence similarity to PRXs. ...
 53-101 1.94e-03

Peroxiredoxin (PRX)-like 1 family; hypothetical proteins that show sequence similarity to PRXs. Members of this group contain a conserved cysteine that aligns to the first cysteine in the CXXC motif of TRX. This does not correspond to the peroxidatic cysteine found in PRXs, which aligns to the second cysteine in the CXXC motif of TRX. In addition, these proteins do not contain the other two conserved residues of the catalytic triad of PRX. PRXs confer a protective antioxidant role in cells through their peroxidase activity in which hydrogen peroxide, peroxynitrate, and organic hydroperoxides are reduced and detoxified using reducing equivalents derived from either thioredoxin, glutathione, trypanothione and AhpF.


Pssm-ID: 239267 [Multi-domain]  Cd Length: 171  Bit Score: 37.22  E-value: 1.94e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1836039599  53 PAPRwFRL--SNGRQVNLADWK-----VVLFMQGHCPYCHQFDPVLKQLAQQYGFS 101
Cdd:cd02969     3 PAPD-FSLpdTDGKTYSLADFAdgkalVVMFICNHCPYVKAIEDRLNRLAKEYGAK 57
Redoxin pfam08534
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
 61-146 2.24e-03

Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.


Pssm-ID: 400717 [Multi-domain]  Cd Length: 148  Bit Score: 36.58  E-value: 2.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1836039599  61 SNGRQVNLADWK----VVLFMQG-HCPYCHQFDPVLKQLAQQY---GFSV----------------------FPYTLDGQ 110
Cdd:pfam08534  16 TDGNTVSLSDFKgkkvVLNFWPGaFCPTCSAEHPYLEKLNELYkekGVDVvavnsdndaffvkrfwgkeglpFPFLSDGN 95

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1836039599 111 GdtAFPEALpvppDVMQTFFPNIPVATPTTFLVNVN 146
Cdd:pfam08534  96 A--AFTKAL----GLPIEEDASAGLRSPRYAVIDED 125
 
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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