NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|410894475|gb|EKS42265|]
View 

hypothetical protein HMPREF9695_01357 [Afipia broomeae ATCC 49717]

Protein Classification

peroxiredoxin-like family protein( domain architecture ID 10121943)

peroxiredoxin (PRX)-like family protein containing a CXXC motif, with the second cysteine in the motif corresponding to the peroxidatic cysteine of PRX, however, it does not contain the other two residues of the catalytic triad of PRXs; similar to vertebrate peroxiredoxin-like 2A, 2B (prostamide/prostaglandin F synthase) and 2C

CATH:  3.40.30.10
PubMed:  15518547|12517450|10049365
SCOP:  3000031

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PRX_like2 cd02970
Peroxiredoxin (PRX)-like 2 family; hypothetical proteins that show sequence similarity to PRXs. ...
 68-214 1.47e-28

Peroxiredoxin (PRX)-like 2 family; hypothetical proteins that show sequence similarity to PRXs. Members of this group contain a CXXC motif, similar to TRX. The second cysteine in the motif corresponds to the peroxidatic cysteine of PRX, however, these proteins do not contain the other two 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. TRXs alter the redox state of target proteins by catalyzing the reduction of their disulfide bonds via the CXXC motif using reducing equivalents derived from either NADPH or ferredoxins.


:

Pssm-ID: 239268 [Multi-domain]  Cd Length: 149  Bit Score: 105.13  E-value: 1.47e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410894475  68 PMPPFVLPDETGALVSLESYLSRGPVAVMFHRGHWCPYCRINVNSLVKAQDKITAAGGQVVIITPER----QQFAQEFKL 143
Cdd:cd02970    1 TAPDFELPDAGGETVTLSALLGEGPVVVVFYRGFGCPFCREYLRALSKLLPELDALGVELVAVGPESpeklEAFDKGKFL 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 410894475 144 NadalFPILTDLDNGYALMLNLAI-WLSPDLQKILSGRDIPNYHGNNA-WMLPIPATFVVGTDGLVKARFVDP 214
Cdd:cd02970   81 P----FPVYADPDRKLYRALGLVRsLPWSNTPRALWKNAAIGFRGNDEgDGLQLPGVFVIGPDGTILFAHVDR 149
 
Name Accession Description Interval E-value
PRX_like2 cd02970
Peroxiredoxin (PRX)-like 2 family; hypothetical proteins that show sequence similarity to PRXs. ...
 68-214 1.47e-28

Peroxiredoxin (PRX)-like 2 family; hypothetical proteins that show sequence similarity to PRXs. Members of this group contain a CXXC motif, similar to TRX. The second cysteine in the motif corresponds to the peroxidatic cysteine of PRX, however, these proteins do not contain the other two 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. TRXs alter the redox state of target proteins by catalyzing the reduction of their disulfide bonds via the CXXC motif using reducing equivalents derived from either NADPH or ferredoxins.


Pssm-ID: 239268 [Multi-domain]  Cd Length: 149  Bit Score: 105.13  E-value: 1.47e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410894475  68 PMPPFVLPDETGALVSLESYLSRGPVAVMFHRGHWCPYCRINVNSLVKAQDKITAAGGQVVIITPER----QQFAQEFKL 143
Cdd:cd02970    1 TAPDFELPDAGGETVTLSALLGEGPVVVVFYRGFGCPFCREYLRALSKLLPELDALGVELVAVGPESpeklEAFDKGKFL 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 410894475 144 NadalFPILTDLDNGYALMLNLAI-WLSPDLQKILSGRDIPNYHGNNA-WMLPIPATFVVGTDGLVKARFVDP 214
Cdd:cd02970   81 P----FPVYADPDRKLYRALGLVRsLPWSNTPRALWKNAAIGFRGNDEgDGLQLPGVFVIGPDGTILFAHVDR 149
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
69-228 4.67e-20

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 82.61  E-value: 4.67e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410894475  69 MPPFVLPDETGALVSLESYLSRgPVAVMFHrGHWCPYCRINVNSLVKAQDKITAAGGQVVIITPER----QQFAQEFKLN 144
Cdd:COG1225    1 APDFTLPDLDGKTVSLSDLRGK-PVVLYFY-ATWCPGCTAELPELRDLYEEFKDKGVEVLGVSSDSdeahKKFAEKYGLP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410894475 145 adalFPILTDLDNGYALMLNLAIwlspdlqkilsgrdipnyhgnnawmlpIPATFVVGTDGLVKARFVDPdFRNRMDIDD 224
Cdd:COG1225   79 ----FPLLSDPDGEVAKAYGVRG---------------------------TPTTFLIDPDGKIRYVWVGP-VDPRPHLEE 126


                 ....
gi 410894475 225 LIKA 228
Cdd:COG1225  127 VLEA 130
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 65-210 5.49e-19

AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) and thiol specific antioxidant (TSA).


Pssm-ID: 425763 [Multi-domain]  Cd Length: 124  Bit Score: 79.58  E-value: 5.49e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410894475   65 PGEPMPPFVLPDETGALVSLESYlsRG-PVAVMFHRGHWCPYCRINVNSLVKAQDKITAAGGQVVIITPER----QQFAQ 139
Cdd:pfam00578   1 VGDKAPDFELPDGDGGTVSLSDY--RGkWVVLFFYPADWTPVCTTELPALADLYEEFKKLGVEVLGVSVDSpeshKAFAE 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 410894475  140 EFKLNadalFPILTDLDNGYALMLNLaiwlspdlqkilsgrdipnyhGNNAWMLPIPATFVVGTDGLVKAR 210
Cdd:pfam00578  79 KYGLP----FPLLSDPDGEVARAYGV---------------------LNEEEGGALRATFVIDPDGKVRYI 124
SelL_rel_redox NF040769
SelL-related redox protein; Members of this family are related to the C-terminal region of ...
 67-228 4.61e-11

SelL-related redox protein; Members of this family are related to the C-terminal region of selenoprotein L (SelL), found in many non-mammalian animals. But while SelL itself has a pair of selenocysteine (U) residues (e.g. XP_029705782.1), typically in the motif ULPU, this family is defined more broadly. Most members of the seed alignment for this HMM are bacterial proteins that have one or zero selenocysteine residues, and are shorter than SelU, although SelU members are also included.


Pssm-ID: 468728  Cd Length: 172  Bit Score: 59.63  E-value: 4.61e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410894475  67 EPMPPFVLPDETGALVSLESYLSRGPVAVMFHRGHWCPYCRINVNSLVKAQDKITAAGGQVVIITPERQQFAQEFKLNAD 146
Cdd:NF040769   1 KTAPEVELLDPDGTLVRLLEFLPQGPLLLVFLRHLGUIPCREHLAQLREHQEEFAARGCRVLVVSFASPEFAEKYLERTW 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410894475 147 -ALFPILTD----------LDNGYALML-NLAIWLSpDLQKILSGRDIPNYHGNNAWMLpiPATFVVGTDGLVKARFVDP 214
Cdd:NF040769  81 lSWPLVVSDpdrklyrafgLKRATFLELwGPKVLVG-YLRALLKGGNFYGKPGGDILQL--GGDFILDRDGRILFAHRSR 157

                        170
                 ....*....|....
gi 410894475 215 DFRNRMDIDDLIKA 228
Cdd:NF040769 158 DPADRPSVADLLAA 171
bcp PRK09437
thioredoxin-dependent thiol peroxidase; Reviewed
 65-157 1.95e-03

thioredoxin-dependent thiol peroxidase; Reviewed


Pssm-ID: 181857  Cd Length: 154  Bit Score: 37.61  E-value: 1.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410894475  65 PGEPMPPFVLPDETGALVSLESYLsRGPVAVMFHRGHWCPYCRINVNSLVKAQDKITAAGGQVVIITPER----QQFAQE 140
Cdd:PRK09437   6 AGDIAPKFSLPDQDGEQVSLTDFQ-GQRVLVYFYPKAMTPGCTVQACGLRDNMDELKKAGVVVLGISTDKpeklSRFAEK 84

                         90
                 ....*....|....*..
gi 410894475 141 FKLNadalFPILTDLDN 157
Cdd:PRK09437  85 ELLN----FTLLSDEDH 97
 
Name Accession Description Interval E-value
PRX_like2 cd02970
Peroxiredoxin (PRX)-like 2 family; hypothetical proteins that show sequence similarity to PRXs. ...
 68-214 1.47e-28

Peroxiredoxin (PRX)-like 2 family; hypothetical proteins that show sequence similarity to PRXs. Members of this group contain a CXXC motif, similar to TRX. The second cysteine in the motif corresponds to the peroxidatic cysteine of PRX, however, these proteins do not contain the other two 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. TRXs alter the redox state of target proteins by catalyzing the reduction of their disulfide bonds via the CXXC motif using reducing equivalents derived from either NADPH or ferredoxins.


Pssm-ID: 239268 [Multi-domain]  Cd Length: 149  Bit Score: 105.13  E-value: 1.47e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410894475  68 PMPPFVLPDETGALVSLESYLSRGPVAVMFHRGHWCPYCRINVNSLVKAQDKITAAGGQVVIITPER----QQFAQEFKL 143
Cdd:cd02970    1 TAPDFELPDAGGETVTLSALLGEGPVVVVFYRGFGCPFCREYLRALSKLLPELDALGVELVAVGPESpeklEAFDKGKFL 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 410894475 144 NadalFPILTDLDNGYALMLNLAI-WLSPDLQKILSGRDIPNYHGNNA-WMLPIPATFVVGTDGLVKARFVDP 214
Cdd:cd02970   81 P----FPVYADPDRKLYRALGLVRsLPWSNTPRALWKNAAIGFRGNDEgDGLQLPGVFVIGPDGTILFAHVDR 149
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
69-228 4.67e-20

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 82.61  E-value: 4.67e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410894475  69 MPPFVLPDETGALVSLESYLSRgPVAVMFHrGHWCPYCRINVNSLVKAQDKITAAGGQVVIITPER----QQFAQEFKLN 144
Cdd:COG1225    1 APDFTLPDLDGKTVSLSDLRGK-PVVLYFY-ATWCPGCTAELPELRDLYEEFKDKGVEVLGVSSDSdeahKKFAEKYGLP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410894475 145 adalFPILTDLDNGYALMLNLAIwlspdlqkilsgrdipnyhgnnawmlpIPATFVVGTDGLVKARFVDPdFRNRMDIDD 224
Cdd:COG1225   79 ----FPLLSDPDGEVAKAYGVRG---------------------------TPTTFLIDPDGKIRYVWVGP-VDPRPHLEE 126


                 ....
gi 410894475 225 LIKA 228
Cdd:COG1225  127 VLEA 130
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 65-210 5.49e-19

AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) and thiol specific antioxidant (TSA).


Pssm-ID: 425763 [Multi-domain]  Cd Length: 124  Bit Score: 79.58  E-value: 5.49e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410894475   65 PGEPMPPFVLPDETGALVSLESYlsRG-PVAVMFHRGHWCPYCRINVNSLVKAQDKITAAGGQVVIITPER----QQFAQ 139
Cdd:pfam00578   1 VGDKAPDFELPDGDGGTVSLSDY--RGkWVVLFFYPADWTPVCTTELPALADLYEEFKKLGVEVLGVSVDSpeshKAFAE 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 410894475  140 EFKLNadalFPILTDLDNGYALMLNLaiwlspdlqkilsgrdipnyhGNNAWMLPIPATFVVGTDGLVKAR 210
Cdd:pfam00578  79 KYGLP----FPLLSDPDGEVARAYGV---------------------LNEEEGGALRATFVIDPDGKVRYI 124
Redoxin pfam08534
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
 65-215 4.64e-12

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


Pssm-ID: 400717 [Multi-domain]  Cd Length: 148  Bit Score: 61.62  E-value: 4.64e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410894475   65 PGEPMPPFVLPDET--GALVSLESYLSRgPVAVMFHRGHWCPYCRINVNSLVKAQDKITAAG-GQVVIITPERQQFAQEF 141
Cdd:pfam08534   2 AGDKAPDFTLPDAAtdGNTVSLSDFKGK-KVVLNFWPGAFCPTCSAEHPYLEKLNELYKEKGvDVVAVNSDNDAFFVKRF 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 410894475  142 KLNADALFPILTDLDNGYALMLNLAIWLSPDLqkilsgrdipnyhgnnawMLPIPATFVVGTDGLVKARFVDPD 215
Cdd:pfam08534  81 WGKEGLPFPFLSDGNAAFTKALGLPIEEDASA------------------GLRSPRYAVIDEDGKVVYLFVGPE 136
PRX_AhpE_like cd03018
Peroxiredoxin (PRX) family, AhpE-like subfamily; composed of proteins similar to Mycobacterium ...
 63-228 6.73e-12

Peroxiredoxin (PRX) family, AhpE-like subfamily; composed of proteins similar to Mycobacterium tuberculosis AhpE. AhpE is described as a 1-cys PRX because of the absence of a resolving cysteine. The structure and sequence of AhpE, however, show greater similarity to 2-cys PRXs than 1-cys PRXs. PRXs are thiol-specific antioxidant (TSA) proteins that confer a protective 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. The first step of catalysis is the nucleophilic attack by the peroxidatic cysteine on the peroxide leading to the formation of a cysteine sulfenic acid intermediate. The absence of a resolving cysteine suggests that functional AhpE is regenerated by an external reductant. The solution behavior and crystal structure of AhpE show that it forms dimers and octamers.


Pssm-ID: 239316 [Multi-domain]  Cd Length: 149  Bit Score: 61.14  E-value: 6.73e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410894475  63 PRPGEPMPPFVLPDETGALVSLESYLSRGPVAVMFHRGHWCPYCRINVNSLVKAQDKITAAGGQVVII----TPERQQFA 138
Cdd:cd03018    1 LEVGDKAPDFELPDQNGQEVRLSEFRGRKPVVLVFFPLAFTPVCTKELCALRDSLELFEAAGAEVLGIsvdsPFSLRAWA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410894475 139 QEFKLNadalFPILTDLdngyalmlnlaiwlspdlqkilsgrdipNYHGNNA---------WMLPIPATFVVGTDGLVKA 209
Cdd:cd03018   81 EENGLT----FPLLSDF----------------------------WPHGEVAkaygvfdedLGVAERAVFVIDRDGIIRY 128

                        170       180
                 ....*....|....*....|.
gi 410894475 210 RFVDPDF--RNRMDIDDLIKA 228
Cdd:cd03018  129 AWVSDDGepRDLPDYDEALDA 149
SelL_rel_redox NF040769
SelL-related redox protein; Members of this family are related to the C-terminal region of ...
 67-228 4.61e-11

SelL-related redox protein; Members of this family are related to the C-terminal region of selenoprotein L (SelL), found in many non-mammalian animals. But while SelL itself has a pair of selenocysteine (U) residues (e.g. XP_029705782.1), typically in the motif ULPU, this family is defined more broadly. Most members of the seed alignment for this HMM are bacterial proteins that have one or zero selenocysteine residues, and are shorter than SelU, although SelU members are also included.


Pssm-ID: 468728  Cd Length: 172  Bit Score: 59.63  E-value: 4.61e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410894475  67 EPMPPFVLPDETGALVSLESYLSRGPVAVMFHRGHWCPYCRINVNSLVKAQDKITAAGGQVVIITPERQQFAQEFKLNAD 146
Cdd:NF040769   1 KTAPEVELLDPDGTLVRLLEFLPQGPLLLVFLRHLGUIPCREHLAQLREHQEEFAARGCRVLVVSFASPEFAEKYLERTW 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410894475 147 -ALFPILTD----------LDNGYALML-NLAIWLSpDLQKILSGRDIPNYHGNNAWMLpiPATFVVGTDGLVKARFVDP 214
Cdd:NF040769  81 lSWPLVVSDpdrklyrafgLKRATFLELwGPKVLVG-YLRALLKGGNFYGKPGGDILQL--GGDFILDRDGRILFAHRSR 157

                        170
                 ....*....|....
gi 410894475 215 DFRNRMDIDDLIKA 228
Cdd:NF040769 158 DPADRPSVADLLAA 171
PRX_like1 cd02969
Peroxiredoxin (PRX)-like 1 family; hypothetical proteins that show sequence similarity to PRXs. ...
 66-161 1.93e-08

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: 52.24  E-value: 1.93e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410894475  66 GEPMPPFVLPDETGALVSLESYLSRGPVAVMFHRGHwCPYCRINVNSLVKAQDKITAAGGQVVII-----------TPER 134
Cdd:cd02969    1 GSPAPDFSLPDTDGKTYSLADFADGKALVVMFICNH-CPYVKAIEDRLNRLAKEYGAKGVAVVAInsndieaypedSPEN 79

                         90       100
                 ....*....|....*....|....*...
gi 410894475 135 -QQFAQEFKLNadalFPILTDLDNGYAL 161
Cdd:cd02969   80 mKAKAKEHGYP----FPYLLDETQEVAK 103
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 65-231 5.37e-08

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 50.46  E-value: 5.37e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410894475  65 PGEPMPPFVLPDETGALVSLESYLSRgPVAVMFHrGHWCPYCRINVNSLVKAQDKitAAGGQVVIITPER-----QQFAQ 139
Cdd:COG0526    4 VGKPAPDFTLTDLDGKPLSLADLKGK-PVLVNFW-ATWCPPCRAEMPVLKELAEE--YGGVVFVGVDVDEnpeavKAFLK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410894475 140 EFKLNadalFPILTDLDNGYALMLnlaiwlspdlqkilsgrdipnyhGNNAWmlpiPATFVVGTDGLVKARFVDPdfrnr 219
Cdd:COG0526   80 ELGLP----YPVLLDPDGELAKAY-----------------------GVRGI----PTTVLIDKDGKIVARHVGP----- 123

                        170
                 ....*....|..
gi 410894475 220 MDIDDLIKAFKS 231
Cdd:COG0526  124 LSPEELEEALEK 135
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 71-212 9.02e-08

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: 49.16  E-value: 9.02e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410894475  71 PFVLPDETGALVSLESYlsRGPVAVMFHRGHWCPYCRINVNSLVKAQDKITAAGGQVV-IITPER-----QQFAQEFKLN 144
Cdd:cd02966    1 DFSLPDLDGKPVSLSDL--KGKVVLVNFWASWCPPCRAEMPELEALAKEYKDDGVEVVgVNVDDDdpaavKAFLKKYGIT 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 410894475 145 adalFPILtdLDNGYALMLNLaiwlspdlqkilsgrdipnyhGNNAWmlpiPATFVVGTDGLVKARFV 212
Cdd:cd02966   79 ----FPVL--LDPDGELAKAY---------------------GVRGL----PTTFLIDRDGRIRARHV 115
SCO cd02968
SCO (an acronym for Synthesis of Cytochrome c Oxidase) family; composed of proteins similar to ...
 68-148 2.99e-05

SCO (an acronym for Synthesis of Cytochrome c Oxidase) family; composed of proteins similar to Sco1, a membrane-anchored protein possessing a soluble domain with a TRX fold. Members of this family are required for the proper assembly of cytochrome c oxidase (COX). They contain a metal binding motif, typically CXXXC, which is located in a flexible loop. COX, the terminal enzyme in the respiratory chain, is imbedded in the inner mitochondrial membrane of all eukaryotes and in the plasma membrane of some prokaryotes. It is composed of two subunits, COX I and COX II. It has been proposed that Sco1 specifically delivers copper to the CuA site, a dinuclear copper center, of the COX II subunit. Mutations in human Sco1 and Sco2 cause fatal infantile hepatoencephalomyopathy and cardioencephalomyopathy, respectively. Both disorders are associated with severe COX deficiency in affected tissues. More recently, it has been argued that the redox sensitivity of the copper binding properties of Sco1 implies that it participates in signaling events rather than functioning as a chaperone that transfers copper to COX II.


Pssm-ID: 239266  Cd Length: 142  Bit Score: 42.59  E-value: 2.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410894475  68 PMPPFVLPDETGALVSLESYLSRgPVAVMF---HrghwCPY-CRINVNSLVKAQDKITAAGG---QVVIIT--PER---- 134
Cdd:cd02968    1 IGPDFTLTDQDGRPVTLSDLKGK-PVLVYFgytH----CPDvCPTTLANLAQALKQLGADGGddvQVVFISvdPERdtpe 75

                         90
                 ....*....|....*.
gi 410894475 135 --QQFAQEFKLNADAL 148
Cdd:cd02968   76 vlKAYAKAFGPGWIGL 91
bcp PRK09437
thioredoxin-dependent thiol peroxidase; Reviewed
 65-157 1.95e-03

thioredoxin-dependent thiol peroxidase; Reviewed


Pssm-ID: 181857  Cd Length: 154  Bit Score: 37.61  E-value: 1.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 410894475  65 PGEPMPPFVLPDETGALVSLESYLsRGPVAVMFHRGHWCPYCRINVNSLVKAQDKITAAGGQVVIITPER----QQFAQE 140
Cdd:PRK09437   6 AGDIAPKFSLPDQDGEQVSLTDFQ-GQRVLVYFYPKAMTPGCTVQACGLRDNMDELKKAGVVVLGISTDKpeklSRFAEK 84

                         90
                 ....*....|....*..
gi 410894475 141 FKLNadalFPILTDLDN 157
Cdd:PRK09437  85 ELLN----FTLLSDEDH 97
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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