NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1002298403|ref|XP_015612620|]
View 

TPR repeat-containing thioredoxin TDX [Oryza sativa Japonica Group]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 217-312 1.40e-29

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: 108.41  E-value: 1.40e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002298403 217 SELDTKLKAasslSRLVVLYFTAAWCGPCRFIGPVCKSLAEKHRNVVFLKVDIDELNSVAYRWNVSSVPSFFFVRNGKEI 296
Cdd:cd02947     1 EEFEELIKS----AKPVVVDFWAPWCGPCKAIAPVLEELAEEYPKVKFVKVDVDENPELAEEYGVRSIPTFLFFKNGKEV 76

                          90
                  ....*....|....*..
gi 1002298403 297 DKVVGAD-KNGLERKVA 312
Cdd:cd02947    77 DRVVGADpKEELEEFLE 93
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
48-148 2.69e-20

Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];


:

Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 87.66  E-value: 2.69e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002298403  48 DQAQLCKNKGVDAFSEGKLDEAIEHLTEAIVLNPTSAIAYATRAVIFVKSKKPNAAIRDADAALKINPDSAKGYKSRGMA 127
Cdd:COG4785    71 DLAQLYYERGVAYDSLGDYDLAIADFDQALELDPDLAEAYNNRGLAYLLLGDYDAALEDFDRALELDPDYAYAYLNRGIA 150

                          90       100
                  ....*....|....*....|.
gi 1002298403 128 KAMLGKWEEAAQDLRMAAKLD 148
Cdd:COG4785   151 LYYLGRYELAIADLEKALELD 171
 
Name Accession Description Interval E-value
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 217-312 1.40e-29

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: 108.41  E-value: 1.40e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002298403 217 SELDTKLKAasslSRLVVLYFTAAWCGPCRFIGPVCKSLAEKHRNVVFLKVDIDELNSVAYRWNVSSVPSFFFVRNGKEI 296
Cdd:cd02947     1 EEFEELIKS----AKPVVVDFWAPWCGPCKAIAPVLEELAEEYPKVKFVKVDVDENPELAEEYGVRSIPTFLFFKNGKEV 76

                          90
                  ....*....|....*..
gi 1002298403 297 DKVVGAD-KNGLERKVA 312
Cdd:cd02947    77 DRVVGADpKEELEEFLE 93
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 230-314 8.76e-24

Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442352 [Multi-domain]  Cd Length: 105  Bit Score: 93.35  E-value: 8.76e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002298403 230 SRLVVLYFTAAWCGPCRFIGPVCKSLAEKHRN-VVFLKVDIDELNSVAYRWNVSSVPSFFFVRNGKEIDKVVGA-DKNGL 307
Cdd:COG3118    18 DKPVLVDFWAPWCGPCKMLAPVLEELAAEYGGkVKFVKVDVDENPELAAQFGVRSIPTLLLFKDGQPVDRFVGAlPKEQL 97


                  ....*..
gi 1002298403 308 ERKVAQH 314
Cdd:COG3118    98 REFLDKV 104
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 210-312 1.53e-23

Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the reversible oxidation of an active centre disulfide bond. Some members with only the active site are not separated from the noise.


Pssm-ID: 395038 [Multi-domain]  Cd Length: 103  Bit Score: 92.68  E-value: 1.53e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002298403 210 VIAIHSSSELDTKLKAASslsRLVVLYFTAAWCGPCRFIGPVCKSLAEKHR-NVVFLKVDIDELNSVAYRWNVSSVPSFF 288
Cdd:pfam00085   1 VVVVLTDANFDEVVQKSS---KPVLVDFYAPWCGPCKMLAPEYEELAQEYKgNVVFAKVDVDENPDLASKYGVRGYPTLI 77

                          90       100
                  ....*....|....*....|....*
gi 1002298403 289 FVRNGKEIDKVVGA-DKNGLERKVA 312
Cdd:pfam00085  78 FFKNGQPVDDYVGArPKDALAAFLK 102
PTZ00051 PTZ00051
thioredoxin; Provisional
 222-308 1.44e-21

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 87.24  E-value: 1.44e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002298403 222 KLKAASSLSRLVVLYFTAAWCGPCRFIGPVCKSLAEKHRNVVFLKVDIDELNSVAYRWNVSSVPSFFFVRNGKEIDKVVG 301
Cdd:PTZ00051   10 EFESTLSQNELVIVDFYAEWCGPCKRIAPFYEECSKEYTKMVFVKVDVDELSEVAEKENITSMPTFKVFKNGSVVDTLLG 89


                  ....*..
gi 1002298403 302 ADKNGLE 308
Cdd:PTZ00051   90 ANDEALK 96
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
48-148 2.69e-20

Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 87.66  E-value: 2.69e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002298403  48 DQAQLCKNKGVDAFSEGKLDEAIEHLTEAIVLNPTSAIAYATRAVIFVKSKKPNAAIRDADAALKINPDSAKGYKSRGMA 127
Cdd:COG4785    71 DLAQLYYERGVAYDSLGDYDLAIADFDQALELDPDLAEAYNNRGLAYLLLGDYDAALEDFDRALELDPDYAYAYLNRGIA 150

                          90       100
                  ....*....|....*....|.
gi 1002298403 128 KAMLGKWEEAAQDLRMAAKLD 148
Cdd:COG4785   151 LYYLGRYELAIADLEKALELD 171
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 215-314 2.31e-19

thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of a domain closely related to thioredoxin. This model is designed to recognize authentic thioredoxin, a small protein that should be hit exactly once by this model. Any protein that hits once with a score greater than the second (per domain) trusted cutoff may be taken as thioredoxin. [Energy metabolism, Electron transport]


Pssm-ID: 200072 [Multi-domain]  Cd Length: 101  Bit Score: 81.57  E-value: 2.31e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002298403 215 SSSELDTKLKAASslsRLVVLYFTAAWCGPCRFIGPVCKSLA-EKHRNVVFLKVDIDELNSVAYRWNVSSVPSFFFVRNG 293
Cdd:TIGR01068   2 TDANFDETIASSD---KPVLVDFWAPWCGPCKMIAPILEELAkEYEGKVKFVKLNVDENPDIAAKYGIRSIPTLLLFKNG 78

                          90       100
                  ....*....|....*....|..
gi 1002298403 294 KEIDKVVGA-DKNGLERKVAQH 314
Cdd:TIGR01068  79 KEVDRSVGAlPKAALKQLINKN 100
PLN03088 PLN03088
SGT1, suppressor of G2 allele of SKP1; Provisional
 56-191 7.92e-09

SGT1, suppressor of G2 allele of SKP1; Provisional


Pssm-ID: 215568 [Multi-domain]  Cd Length: 356  Bit Score: 55.95  E-value: 7.92e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002298403  56 KGVDAFSEGKLDEAIEHLTEAIVLNPTSAIAYATRAVIFVKSKKPNAAIRDADAALKINPDSAKGYKSRGMAKAMLGKWE 135
Cdd:PLN03088    8 KAKEAFVDDDFALAVDLYTQAIDLDPNNAELYADRAQANIKLGNFTEAVADANKAIELDPSLAKAYLRKGTACMKLEEYQ 87

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1002298403 136 EAAQDLrmaakldydeEIGAELKKVEPnvlkieehrkKYERLRKERDIKKAEMEKQ 191
Cdd:PLN03088   88 TAKAAL----------EKGASLAPGDS----------RFTKLIKECDEKIAEEEKD 123
3a0801s09 TIGR00990
mitochondrial precursor proteins import receptor (72 kDa mitochondrial outermembrane protein) ...
 56-150 2.00e-07

mitochondrial precursor proteins import receptor (72 kDa mitochondrial outermembrane protein) (mitochondrial import receptor for the ADP/ATP carrier) (translocase of outermembrane tom70); [Transport and binding proteins, Amino acids, peptides and amines]


Pssm-ID: 273380 [Multi-domain]  Cd Length: 615  Bit Score: 52.29  E-value: 2.00e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002298403  56 KGVDAFSEGKLDEAIEHLTEAIVLNPTSAIAYATRAVIFVKSKKPNAAIRDADAALKINPDSAKGYKSRGMAKAMLGKWE 135
Cdd:TIGR00990 337 RGTFKCLKGKHLEALADLSKSIELDPRVTQSYIKRASMNLELGDPDKAEEDFDKALKLNSEDPDIYYHRAQLHFIKGEFA 416

                          90
                  ....*....|....*
gi 1002298403 136 EAAQDLRMAAKLDYD 150
Cdd:TIGR00990 417 QAGKDYQKSIDLDPD 431
TPR_11 pfam13414
TPR repeat;
61-96 2.37e-04

TPR repeat;


Pssm-ID: 315977 [Multi-domain]  Cd Length: 42  Bit Score: 38.22  E-value: 2.37e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1002298403  61 FSEGKLDEAIEHLTEAIVLNPTSAIAYATRAVIFVK 96
Cdd:pfam13414   5 YEQGKYEEAIEAYKKALKLDPDNPEAYYNLGLAYYK 40
TPR smart00028
Tetratricopeptide repeats; Repeats present in 4 or more copies in proteins. Contain a minimum ...
 50-82 2.93e-03

Tetratricopeptide repeats; Repeats present in 4 or more copies in proteins. Contain a minimum of 34 amino acids each and self-associate via a "knobs and holes" mechanism.


Pssm-ID: 197478 [Multi-domain]  Cd Length: 34  Bit Score: 34.73  E-value: 2.93e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1002298403   50 AQLCKNKGVDAFSEGKLDEAIEHLTEAIVLNPT 82
Cdd:smart00028   1 AEALYNLGNAYLKLGDYDEALEYYEKALELDPN 33
 
Name Accession Description Interval E-value
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 217-312 1.40e-29

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: 108.41  E-value: 1.40e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002298403 217 SELDTKLKAasslSRLVVLYFTAAWCGPCRFIGPVCKSLAEKHRNVVFLKVDIDELNSVAYRWNVSSVPSFFFVRNGKEI 296
Cdd:cd02947     1 EEFEELIKS----AKPVVVDFWAPWCGPCKAIAPVLEELAEEYPKVKFVKVDVDENPELAEEYGVRSIPTFLFFKNGKEV 76

                          90
                  ....*....|....*..
gi 1002298403 297 DKVVGAD-KNGLERKVA 312
Cdd:cd02947    77 DRVVGADpKEELEEFLE 93
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 230-314 8.76e-24

Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442352 [Multi-domain]  Cd Length: 105  Bit Score: 93.35  E-value: 8.76e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002298403 230 SRLVVLYFTAAWCGPCRFIGPVCKSLAEKHRN-VVFLKVDIDELNSVAYRWNVSSVPSFFFVRNGKEIDKVVGA-DKNGL 307
Cdd:COG3118    18 DKPVLVDFWAPWCGPCKMLAPVLEELAAEYGGkVKFVKVDVDENPELAAQFGVRSIPTLLLFKDGQPVDRFVGAlPKEQL 97


                  ....*..
gi 1002298403 308 ERKVAQH 314
Cdd:COG3118    98 REFLDKV 104
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 210-312 1.53e-23

Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the reversible oxidation of an active centre disulfide bond. Some members with only the active site are not separated from the noise.


Pssm-ID: 395038 [Multi-domain]  Cd Length: 103  Bit Score: 92.68  E-value: 1.53e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002298403 210 VIAIHSSSELDTKLKAASslsRLVVLYFTAAWCGPCRFIGPVCKSLAEKHR-NVVFLKVDIDELNSVAYRWNVSSVPSFF 288
Cdd:pfam00085   1 VVVVLTDANFDEVVQKSS---KPVLVDFYAPWCGPCKMLAPEYEELAQEYKgNVVFAKVDVDENPDLASKYGVRGYPTLI 77

                          90       100
                  ....*....|....*....|....*
gi 1002298403 289 FVRNGKEIDKVVGA-DKNGLERKVA 312
Cdd:pfam00085  78 FFKNGQPVDDYVGArPKDALAAFLK 102
PTZ00051 PTZ00051
thioredoxin; Provisional
 222-308 1.44e-21

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 87.24  E-value: 1.44e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002298403 222 KLKAASSLSRLVVLYFTAAWCGPCRFIGPVCKSLAEKHRNVVFLKVDIDELNSVAYRWNVSSVPSFFFVRNGKEIDKVVG 301
Cdd:PTZ00051   10 EFESTLSQNELVIVDFYAEWCGPCKRIAPFYEECSKEYTKMVFVKVDVDELSEVAEKENITSMPTFKVFKNGSVVDTLLG 89


                  ....*..
gi 1002298403 302 ADKNGLE 308
Cdd:PTZ00051   90 ANDEALK 96
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
48-148 2.69e-20

Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 87.66  E-value: 2.69e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002298403  48 DQAQLCKNKGVDAFSEGKLDEAIEHLTEAIVLNPTSAIAYATRAVIFVKSKKPNAAIRDADAALKINPDSAKGYKSRGMA 127
Cdd:COG4785    71 DLAQLYYERGVAYDSLGDYDLAIADFDQALELDPDLAEAYNNRGLAYLLLGDYDAALEDFDRALELDPDYAYAYLNRGIA 150

                          90       100
                  ....*....|....*....|.
gi 1002298403 128 KAMLGKWEEAAQDLRMAAKLD 148
Cdd:COG4785   151 LYYLGRYELAIADLEKALELD 171
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 215-314 2.31e-19

thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of a domain closely related to thioredoxin. This model is designed to recognize authentic thioredoxin, a small protein that should be hit exactly once by this model. Any protein that hits once with a score greater than the second (per domain) trusted cutoff may be taken as thioredoxin. [Energy metabolism, Electron transport]


Pssm-ID: 200072 [Multi-domain]  Cd Length: 101  Bit Score: 81.57  E-value: 2.31e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002298403 215 SSSELDTKLKAASslsRLVVLYFTAAWCGPCRFIGPVCKSLA-EKHRNVVFLKVDIDELNSVAYRWNVSSVPSFFFVRNG 293
Cdd:TIGR01068   2 TDANFDETIASSD---KPVLVDFWAPWCGPCKMIAPILEELAkEYEGKVKFVKLNVDENPDIAAKYGIRSIPTLLLFKNG 78

                          90       100
                  ....*....|....*....|..
gi 1002298403 294 KEIDKVVGA-DKNGLERKVAQH 314
Cdd:TIGR01068  79 KEVDRSVGAlPKAALKQLINKN 100
TRX_PICOT cd02984
TRX domain, PICOT (for PKC-interacting cousin of TRX) subfamily; PICOT is a protein that ...
 227-312 4.50e-19

TRX domain, PICOT (for PKC-interacting cousin of TRX) subfamily; PICOT is a protein that interacts with protein kinase C (PKC) theta, a calcium independent PKC isoform selectively expressed in skeletal muscle and T lymphocytes. PICOT contains an N-terminal TRX-like domain, which does not contain the catalytic CXXC motif, followed by one to three glutaredoxin domains. The TRX-like domain is required for interaction with PKC theta. PICOT inhibits the activation of c-Jun N-terminal kinase and the transcription factors, AP-1 and NF-kB, induced by PKC theta or T-cell activating stimuli.


Pssm-ID: 239282 [Multi-domain]  Cd Length: 97  Bit Score: 80.39  E-value: 4.50e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002298403 227 SSLSRLVVLYFTAAWCGPCRFIGPVCKSLA-EKHRNVVFLKVDIDELNSVAYRWNVSSVPSFFFVRNGKEIDKVVGADKN 305
Cdd:cd02984    11 SDASKLLVLHFWAPWAEPCKQMNQVFEELAkEAFPSVLFLSIEAEELPEISEKFEITAVPTFVFFRNGTIVDRVSGADPK 90


                  ....*..
gi 1002298403 306 GLERKVA 312
Cdd:cd02984    91 ELAKKVE 97
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
46-187 9.81e-18

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 80.82  E-value: 9.81e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002298403  46 KRDQAQLCKNKGVDAFSEGKLDEAIEHLTEAIVLNPTSAIAYATRAVIFVKSKKPNAAIRDADAALKINPDSAKGYKSRG 125
Cdd:COG0457    38 DPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPDDAEALNNLGLALQALGRYEEALEDYDKALELDPDDAEALYNLG 117

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002298403 126 MAKAMLGKWEEAAQDLRMAAKLD-YDEEIGAELKKVEPNVLKIEEHRKKYERLRKERDIKKAE 187
Cdd:COG0457   118 LALLELGRYDEAIEAYERALELDpDDADALYNLGIALEKLGRYEEALELLEKLEAAALAALLA 180
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
48-150 1.53e-17

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 80.44  E-value: 1.53e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002298403  48 DQAQLCKNKGVDAFSEGKLDEAIEHLTEAIVLNPTSAIAYATRAVIFVKSKKPNAAIRDADAALKINPDSAKGYKSRGMA 127
Cdd:COG0457     6 DDAEAYNNLGLAYRRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPDDAEALNNLGLA 85

                          90       100
                  ....*....|....*....|...
gi 1002298403 128 KAMLGKWEEAAQDLRMAAKLDYD 150
Cdd:COG0457    86 LQALGRYEEALEDYDKALELDPD 108
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 219-314 2.19e-15

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 71.64  E-value: 2.19e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002298403 219 LDTKLKAASSLS-RLVVLYFTAAWCGPCRFIGPVCKSLAEKHRNVVFLKVDIDE----------------------LNSV 275
Cdd:COG0526    16 LDGKPLSLADLKgKPVLVNFWATWCPPCRAEMPVLKELAEEYGGVVFVGVDVDEnpeavkaflkelglpypvlldpDGEL 95

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1002298403 276 AYRWNVSSVPSFFFV-RNGKEIDKVVGA-DKNGLERKVAQH 314
Cdd:COG0526    96 AKAYGVRGIPTTVLIdKDGKIVARHVGPlSPEELEEALEKL 136
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
48-192 4.89e-15

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 73.50  E-value: 4.89e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002298403  48 DQAQLCKNKGVDAFSEGKLDEAIEHLTEAIVLNPTSAIAYATRAVIFVKSKKPNAAIRDADAALKINPDSAKGYKSRGMA 127
Cdd:COG0457    74 DDAEALNNLGLALQALGRYEEALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYERALELDPDDADALYNLGIA 153

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002298403 128 KAMLGKWEEAAQDLRMAAKLDYDEEIGAELKKVEPNVLKIEEHRKKYERLRKERDIKKAEMEKQR 192
Cdd:COG0457   154 LEKLGRYEEALELLEKLEAAALAALLAAALGEAALALAAAEVLLALLLALEQALRKKLAILTLAA 218
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 41-151 5.37e-15

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 70.61  E-value: 5.37e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002298403  41 EVSDEKRDQAQLCKNKGVDAFSEGKLDEAIEHLTEAIVLNPTSAIAYATRAVIFVKSKKPNAAIRDADAALKINPDSAKG 120
Cdd:COG4783    29 KALELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNLGLALLKAGDYDEALALLEKALKLDPEHPEA 108

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1002298403 121 YKSRGMAKAMLGKWEEAAQDLRMAAKLDYDE 151
Cdd:COG4783   109 YLRLARAYRALGRPDEAIAALEKALELDPDD 139
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 49-148 9.51e-15

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 70.22  E-value: 9.51e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002298403  49 QAQLCKNKGVDAFSEGKLDEAIEHLTEAIVLNPTSAIAYATRAVIFVKSKKPNAAIRDADAALKINPDSAKGYKSRGMAK 128
Cdd:COG4783     3 CAEALYALAQALLLAGDYDEAEALLEKALELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNLGLAL 82

                          90       100
                  ....*....|....*....|
gi 1002298403 129 AMLGKWEEAAQDLRMAAKLD 148
Cdd:COG4783    83 LKAGDYDEALALLEKALKLD 102
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 48-148 8.39e-14

Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 71.95  E-value: 8.39e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002298403  48 DQAQLCKNKGVDAFSEGKLDEAIEHLTEAIVLNPTSAIAYATRAVIFVKSKKPNAAIRDADAALKINPDSAKGYKSRGMA 127
Cdd:COG3914   110 DNAEALFNLGNLLLALGRLEEALAALRRALALNPDFAEAYLNLGEALRRLGRLEEAIAALRRALELDPDNAEALNNLGNA 189

                          90       100
                  ....*....|....*....|.
gi 1002298403 128 KAMLGKWEEAAQDLRMAAKLD 148
Cdd:COG3914   190 LQDLGRLEEAIAAYRRALELD 210
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 64-148 7.20e-13

Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 68.87  E-value: 7.20e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002298403  64 GKLDEAIEHLTEAIVLNPTSAIAYATRAVIFVKSKKPNAAIRDADAALKINPDSAKGYKSRGMAKAMLGKWEEAAQDLRM 143
Cdd:COG3914    92 GRYEEALALYRRALALNPDNAEALFNLGNLLLALGRLEEALAALRRALALNPDFAEAYLNLGEALRRLGRLEEAIAALRR 171


                  ....*
gi 1002298403 144 AAKLD 148
Cdd:COG3914   172 ALELD 176
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 61-148 1.23e-12

Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443378 [Multi-domain]  Cd Length: 131  Bit Score: 63.87  E-value: 1.23e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002298403  61 FSEGKLDEAIEHLTEAIVLNPTSAIAYATRAVIFVKSKKPNAAIRDADAALKINPDSAKGYKSRGMAKAMLGKWEEAAQD 140
Cdd:COG4235    28 LRLGRYDEALAAYEKALRLDPDNADALLDLAEALLAAGDTEEAEELLERALALDPDNPEALYLLGLAAFQQGDYAEAIAA 107


                  ....*...
gi 1002298403 141 LRMAAKLD 148
Cdd:COG4235   108 WQKLLALL 115
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 64-148 1.41e-12

Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 444034 [Multi-domain]  Cd Length: 155  Bit Score: 64.60  E-value: 1.41e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002298403  64 GKLDEAIEHLTEAIVLNPTSAIAYATRAVIFVKSKKPNAAIRDADAALKINPDSAKGYKSRGMAKAMLGKWEEAAQDLRM 143
Cdd:COG5010    68 GDFEESLALLEQALQLDPNNPELYYNLALLYSRSGDKDEAKEYYEKALALSPDNPNAYSNLAALLLSLGQDDEAKAALQR 147


                  ....*
gi 1002298403 144 AAKLD 148
Cdd:COG5010   148 ALGTS 152
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
75-148 1.11e-11

Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 63.40  E-value: 1.11e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002298403  75 EAIVLNPTSAIAYATRAVIFVKSKKPNAAIRDADAALKINPDSAKGYKSRGMAKAMLGKWEEAAQDLRMAAKLD 148
Cdd:COG4785    64 DRALALPDLAQLYYERGVAYDSLGDYDLAIADFDQALELDPDLAEAYNNRGLAYLLLGDYDAALEDFDRALELD 137
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
60-150 2.13e-11

Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 59.41  E-value: 2.13e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002298403  60 AFSEGKLDEAIEHLTEAIVLNPTSAIAYATRAVIFVKSKKPNAAIRdADAALKINPDSAKGYKSRGMAKAMLGKWEEAAQ 139
Cdd:COG3063     2 YLKLGDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEAIA-LEKALKLDPNNAEALLNLAELLLELGDYDEALA 80

                          90
                  ....*....|.
gi 1002298403 140 DLRMAAKLDYD 150
Cdd:COG3063    81 YLERALELDPS 91
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
77-150 2.31e-11

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 62.72  E-value: 2.31e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002298403  77 IVLNPTSAIAYATRAVIFVKSKKPNAAIRDADAALKINPDSAKGYKSRGMAKAMLGKWEEAAQDLRMAAKLDYD 150
Cdd:COG0457     1 LELDPDDAEAYNNLGLAYRRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPD 74
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 63-150 4.91e-11

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 62.05  E-value: 4.91e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002298403  63 EGKLDEAIEHLTEAIVLNPTSAIAYATRAVIFVKSKKPNAAIRDADAALKINPDSAKGYKSRGMAKAMLGKWEEAAQDLR 142
Cdd:COG2956   123 EGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKALKLDPDCARALLLLAELYLEQGDYEEAIAALE 202


                  ....*...
gi 1002298403 143 MAAKLDYD 150
Cdd:COG2956   203 RALEQDPD 210
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 41-177 6.45e-11

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 61.67  E-value: 6.45e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002298403  41 EVSDEKRDQAQLCKNKGVDAFSEGKLDEAIEHLTEAIVLNPTSAIAYATRAVIFVKSKKPNAAIRDADAALKINPDSAKG 120
Cdd:COG2956   135 RLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKALKLDPDCARALLLLAELYLEQGDYEEAIAALERALEQDPDYLPA 214

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1002298403 121 YKSRGMAKAMLGKWEEAAQDLRMAAKLDYDEEIGAELKKVEPNVLKIEEHRKKYERL 177
Cdd:COG2956   215 LPRLAELYEKLGDPEEALELLRKALELDPSDDLLLALADLLERKEGLEAALALLERQ 271
PRK10996 PRK10996
thioredoxin 2; Provisional
 205-302 7.97e-11

thioredoxin 2; Provisional


Pssm-ID: 182889 [Multi-domain]  Cd Length: 139  Bit Score: 58.93  E-value: 7.97e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002298403 205 LKDGDVIAiHSSSELDTKLKaaSSLSrlVVLYFTAAWCGPCRFIGPVCKSLA-EKHRNVVFLKVDIDELNSVAYRWNVSS 283
Cdd:PRK10996   32 LFDGEVIN-ATGETLDKLLQ--DDLP--VVIDFWAPWCGPCRNFAPIFEDVAaERSGKVRFVKVNTEAERELSARFRIRS 106

                          90
                  ....*....|....*....
gi 1002298403 284 VPSFFFVRNGKEIDKVVGA 302
Cdd:PRK10996  107 IPTIMIFKNGQVVDMLNGA 125
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 43-148 1.21e-10

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 60.90  E-value: 1.21e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002298403  43 SDEKRDQAQLckNKGVDAFSEGKLDEAIEHLTEAIVLNPTSAIAYATRAVIFVKSKKPNAAIRDADAALKINPDSAKGYK 122
Cdd:COG2956    71 RDPDRAEALL--ELAQDYLKAGLLDRAEELLEKLLELDPDDAEALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYC 148

                          90       100
                  ....*....|....*....|....*.
gi 1002298403 123 SRGMAKAMLGKWEEAAQDLRMAAKLD 148
Cdd:COG2956   149 ELAELYLEQGDYDEAIEALEKALKLD 174
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 48-152 2.33e-10

Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 61.16  E-value: 2.33e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002298403  48 DQAQLCKNKGVDAFSEGKLDEAIEHLTEAIVLNPTSAIAYATRAVIFVKSKKPNAAIRDADAALKINPDSAKGYKSRGMA 127
Cdd:COG3914   144 DFAEAYLNLGEALRRLGRLEEAIAALRRALELDPDNAEALNNLGNALQDLGRLEEAIAAYRRALELDPDNADAHSNLLFA 223

                          90       100
                  ....*....|....*....|....*
gi 1002298403 128 KAMLGKWEEAAQDLRMAAKLDYDEE 152
Cdd:COG3914   224 LRQACDWEVYDRFEELLAALARGPS 248
PDI_a_family cd02961
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ...
 230-295 2.82e-10

Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic proteins involved in oxidative protein folding in the endoplasmic reticulum (ER) by acting as catalysts and folding assistants. Members of this family include PDI and PDI-related proteins like ERp72, ERp57 (or ERp60), ERp44, P5, PDIR, ERp46 and the transmembrane PDIs. PDI, ERp57, ERp72, P5, PDIR and ERp46 are all oxidases, catalyzing the formation of disulfide bonds of newly synthesized polypeptides in the ER. They also exhibit reductase activity in acting as isomerases to correct any non-native disulfide bonds, as well as chaperone activity to prevent protein aggregation and facilitate the folding of newly synthesized proteins. These proteins usually contain multiple copies of a redox active TRX (a) domain containing a CXXC motif, and may also contain one or more redox inactive TRX-like (b) domains. Only one a domain is required for the oxidase function but multiple copies are necessary for the isomerase function. The different types of PDIs may show different substrate specificities and tissue-specific expression, or may be induced by stress. PDIs are in their reduced form at steady state and are oxidized to the active form by Ero1, which is localized in the ER through ERp44. Some members of this family also contain a DnaJ domain in addition to the redox active a domains; examples are ERdj5 and Pfj2. Also included in the family is the redox inactive N-terminal TRX-like domain of ERp29.


Pssm-ID: 239259 [Multi-domain]  Cd Length: 101  Bit Score: 56.46  E-value: 2.82e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002298403 230 SRLVVLYFTAAWCGPCRFIGPVCKSLAEK---HRNVVFLKVDIDELNSVAYRWNVSSVPSFFFVRNGKE 295
Cdd:cd02961    15 SKDVLVEFYAPWCGHCKALAPEYEKLAKElkgDGKVVVAKVDCTANNDLCSEYGVRGYPTIKLFPNGSK 83
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
48-144 1.06e-09

Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 57.62  E-value: 1.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002298403  48 DQAQLCKNKGVDAFSEGKLDEAIEHLTEAIVLNPTSAIAYATRAVIFVKSKKPNAAIRDADAALKINPDSAKGYKSRGMA 127
Cdd:COG4785   105 DLAEAYNNRGLAYLLLGDYDAALEDFDRALELDPDYAYAYLNRGIALYYLGRYELAIADLEKALELDPNDPERALWLYLA 184

                          90
                  ....*....|....*..
gi 1002298403 128 KAMLGKwEEAAQDLRMA 144
Cdd:COG4785   185 ERKLDP-EKALALLLED 200
TlpA_like_ScsD_MtbDsbE cd03011
TlpA-like family, suppressor for copper sensitivity D protein (ScsD) and actinobacterial DsbE ...
 220-301 1.20e-09

TlpA-like family, suppressor for copper sensitivity D protein (ScsD) and actinobacterial DsbE homolog subfamily; composed of ScsD, the DsbE homolog of Mycobacterium tuberculosis (MtbDsbE) and similar proteins, all containing a redox-active CXXC motif. The Salmonella typhimurium ScsD is a thioredoxin-like protein which confers copper tolerance to copper-sensitive mutants of E. coli. MtbDsbE has been characterized as an oxidase in vitro, catalyzing the disulfide bond formation of substrates like hirudin. The reduced form of MtbDsbE is more stable than its oxidized form, consistent with an oxidase function. This is in contrast to the function of DsbE from gram-negative bacteria which is a specific reductase of apocytochrome c.


Pssm-ID: 239309 [Multi-domain]  Cd Length: 123  Bit Score: 55.38  E-value: 1.20e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002298403 220 DTKLKAASSLSRLVVLYFTAAWCGPCRFIGPVCKSLAE---------------------KHRNVVFLKVDiDELNSVAYR 278
Cdd:cd03011    10 GEQFDLESLSGKPVLVYFWATWCPVCRFTSPTVNQLAAdypvvsvalrsgddgavarfmQKKGYGFPVIN-DPDGVISAR 88

                          90       100
                  ....*....|....*....|...
gi 1002298403 279 WNVSSVPSFFFVRNGKEIDKVVG 301
Cdd:cd03011    89 WGVSVTPAIVIVDPGGIVFVTTG 111
TRX_CDSP32 cd02985
TRX family, chloroplastic drought-induced stress protein of 32 kD (CDSP32); CDSP32 is composed ...
 214-315 3.60e-09

TRX family, chloroplastic drought-induced stress protein of 32 kD (CDSP32); CDSP32 is composed of two TRX domains, a C-terminal TRX domain which contains a redox active CXXC motif and an N-terminal TRX-like domain which contains an SXXS sequence instead of the redox active motif. CDSP32 is a stress-inducible TRX, i.e., it acts as a TRX by reducing protein disulfides and is induced by environmental and oxidative stress conditions. It plays a critical role in plastid defense against oxidative damage, a role related to its function as a physiological electron donor to BAS1, a plastidic 2-cys peroxiredoxin. Plants lacking CDSP32 exhibit decreased photosystem II photochemical efficiencies and chlorophyll retention compared to WT controls, as well as an increased proportion of BAS1 in its overoxidized monomeric form.


Pssm-ID: 239283  Cd Length: 103  Bit Score: 53.64  E-value: 3.60e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002298403 214 HSSSELDTKLKAASSlsRLVVLYFTAAWCGPCRFIGPVCKSLAEKHRNVVFLKVDIDELNS---VAYRWNVSSVPSFFFV 290
Cdd:cd02985     1 HSVEELDEALKKAKG--RLVVLEFALKHSGPSVKIYPTMVKLSRTCNDVVFLLVNGDENDStmeLCRREKIIEVPHFLFY 78

                          90       100
                  ....*....|....*....|....*
gi 1002298403 291 RNGKEIDKVVGADKNGLERKVAQHG 315
Cdd:cd02985    79 KDGEKIHEEEGIGPDELIGDVLYYG 103
PLN03088 PLN03088
SGT1, suppressor of G2 allele of SKP1; Provisional
 56-191 7.92e-09

SGT1, suppressor of G2 allele of SKP1; Provisional


Pssm-ID: 215568 [Multi-domain]  Cd Length: 356  Bit Score: 55.95  E-value: 7.92e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002298403  56 KGVDAFSEGKLDEAIEHLTEAIVLNPTSAIAYATRAVIFVKSKKPNAAIRDADAALKINPDSAKGYKSRGMAKAMLGKWE 135
Cdd:PLN03088    8 KAKEAFVDDDFALAVDLYTQAIDLDPNNAELYADRAQANIKLGNFTEAVADANKAIELDPSLAKAYLRKGTACMKLEEYQ 87

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1002298403 136 EAAQDLrmaakldydeEIGAELKKVEPnvlkieehrkKYERLRKERDIKKAEMEKQ 191
Cdd:PLN03088   88 TAKAAL----------EKGASLAPGDS----------RFTKLIKECDEKIAEEEKD 123
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 68-151 9.12e-09

Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443378 [Multi-domain]  Cd Length: 131  Bit Score: 53.09  E-value: 9.12e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002298403  68 EAIEHLTEAIVLNPTSAIAYATRAVIFVKSKKPNAAIRDADAALKINPDSAKGYKSRGMAKAMLGKWEEAAQDLRMAAKL 147
Cdd:COG4235     1 EAIARLRQALAANPNDAEGWLLLGRAYLRLGRYDEALAAYEKALRLDPDNADALLDLAEALLAAGDTEEAEELLERALAL 80


                  ....
gi 1002298403 148 DYDE 151
Cdd:COG4235    81 DPDN 84
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 228-301 1.40e-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: 52.24  E-value: 1.40e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002298403 228 SLSRL----VVLYFTAAWCGPCRFIGPVCKSLAEKHR--NVVFLKVDI-----------------------DELNSVAYR 278
Cdd:cd02966    13 SLSDLkgkvVLVNFWASWCPPCRAEMPELEALAKEYKddGVEVVGVNVddddpaavkaflkkygitfpvllDPDGELAKA 92

                          90       100
                  ....*....|....*....|....
gi 1002298403 279 WNVSSVPSFFFV-RNGKEIDKVVG 301
Cdd:cd02966    93 YGVRGLPTTFLIdRDGRIRARHVG 116
trxA PRK09381
thioredoxin TrxA;
232-306 3.85e-08

thioredoxin TrxA;


Pssm-ID: 181812 [Multi-domain]  Cd Length: 109  Bit Score: 50.83  E-value: 3.85e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002298403 232 LVVLYFTAAWCGPCRFIGPVCKSLAEKHR-NVVFLKVDIDELNSVAYRWNVSSVPSFFFVRNGKEIDKVVGADKNG 306
Cdd:PRK09381   23 AILVDFWAEWCGPCKMIAPILDEIADEYQgKLTVAKLNIDQNPGTAPKYGIRGIPTLLLFKNGEVAATKVGALSKG 98
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 232-307 6.01e-08

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 53.60  E-value: 6.01e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002298403 232 LVVLYFTAAWCGPCRFIGP----VCKSLAEKHRNVVFLKVDIDELNSVAYRWNVSSVPSFFFVRNGKEIDKVVGADKNGL 307
Cdd:PTZ00102   51 IVLVKFYAPWCGHCKRLAPeykkAAKMLKEKKSEIVLASVDATEEMELAQEFGVRGYPTIKFFNKGNPVNYSGGRTADGI 130
3a0801s09 TIGR00990
mitochondrial precursor proteins import receptor (72 kDa mitochondrial outermembrane protein) ...
 56-150 2.00e-07

mitochondrial precursor proteins import receptor (72 kDa mitochondrial outermembrane protein) (mitochondrial import receptor for the ADP/ATP carrier) (translocase of outermembrane tom70); [Transport and binding proteins, Amino acids, peptides and amines]


Pssm-ID: 273380 [Multi-domain]  Cd Length: 615  Bit Score: 52.29  E-value: 2.00e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002298403  56 KGVDAFSEGKLDEAIEHLTEAIVLNPTSAIAYATRAVIFVKSKKPNAAIRDADAALKINPDSAKGYKSRGMAKAMLGKWE 135
Cdd:TIGR00990 337 RGTFKCLKGKHLEALADLSKSIELDPRVTQSYIKRASMNLELGDPDKAEEDFDKALKLNSEDPDIYYHRAQLHFIKGEFA 416

                          90
                  ....*....|....*
gi 1002298403 136 EAAQDLRMAAKLDYD 150
Cdd:TIGR00990 417 QAGKDYQKSIDLDPD 431
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 56-176 2.24e-07

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 51.27  E-value: 2.24e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002298403  56 KGVDAFSEGKLDEAIEHLTEAIVLNPTSAIAYATRAVIFVKSKKPNAAIRDADAALKINPDSAKGYKSRGMAKAMLGKWE 135
Cdd:COG2956    14 KGLNYLLNGQPDKAIDLLEEALELDPETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAEALLELAQDYLKAGLLD 93

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1002298403 136 EAAQDLRMAAKLD-YDEEIGAELkkvepnvLKIEEHRKKYER 176
Cdd:COG2956    94 RAEELLEKLLELDpDDAEALRLL-------AEIYEQEGDWEK 128
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 62-148 2.66e-07

Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal metal-binding domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 50.88  E-value: 2.66e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002298403  62 SEGKLDEAIEHLTEAIVLNPTSAIAYATRAVIFVKSKKPNAAIRDADAALKINPDSAKGYKSRGMAKAMLGKWEEAAQDL 141
Cdd:COG2956    54 RRGEYDRAIRIHQKLLERDPDRAEALLELAQDYLKAGLLDRAEELLEKLLELDPDDAEALRLLAEIYEQEGDWEKAIEVL 133


                  ....*..
gi 1002298403 142 RMAAKLD 148
Cdd:COG2956   134 ERLLKLG 140
3a0801s09 TIGR00990
mitochondrial precursor proteins import receptor (72 kDa mitochondrial outermembrane protein) ...
 24-173 3.81e-07

mitochondrial precursor proteins import receptor (72 kDa mitochondrial outermembrane protein) (mitochondrial import receptor for the ADP/ATP carrier) (translocase of outermembrane tom70); [Transport and binding proteins, Amino acids, peptides and amines]


Pssm-ID: 273380 [Multi-domain]  Cd Length: 615  Bit Score: 51.52  E-value: 3.81e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002298403  24 AVEPDNDPPQKMGDPSVEVSDEKRDQ-AQLCKNKGVDAFSEGKLDEAIEHLTEAIVLNPtSAIAYATRAVIFVKSKKPNA 102
Cdd:TIGR00990 100 PVEPADELPEIDESSVANLSEEERKKyAAKLKEKGNKAYRNKDFNKAIKLYSKAIECKP-DPVYYSNRAACHNALGDWEK 178

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002298403 103 AIRDADAALKINPDSAKGYKSRGMAKAMLGKWEEAAQDLRMAAKLD-YDEEIGAELkkVEPNVLKIEEHRKK 173
Cdd:TIGR00990 179 VVEDTTAALELDPDYSKALNRRANAYDGLGKYADALLDLTASCIIDgFRNEQSAQA--VERLLKKFAESKAK 248
DsbD COG4232
Thiol:disulfide interchange protein DsbD [Posttranslational modification, protein turnover, ...
 212-299 3.99e-07

Thiol:disulfide interchange protein DsbD [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443376 [Multi-domain]  Cd Length: 416  Bit Score: 50.96  E-value: 3.99e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002298403 212 AIHSSSELDTKLKAASSLSRLVVLYFTAAWCGPCRFI-------GPVCKSLAEkhrNVVFLKVDIDELNSV--AY--RWN 280
Cdd:COG4232   302 GLAWQADLEAALAEARAEGKPVFVDFTADWCVTCKENertvfsdPEVQAALAD---DVVLLKADVTDNDPEitALlkRFG 378

                          90       100
                  ....*....|....*....|
gi 1002298403 281 VSSVPSF-FFVRNGKEIDKV 299
Cdd:COG4232   379 RFGVPTYvFYDPDGEELPRL 398
TRX_superfamily cd01659
Thioredoxin (TRX) superfamily; a large, diverse group of proteins containing a TRX-fold. Many ...
 234-296 4.02e-07

Thioredoxin (TRX) superfamily; a large, diverse group of proteins containing a TRX-fold. Many members contain a classic TRX domain with a redox active CXXC motif. They function as protein disulfide oxidoreductases (PDOs), altering the redox state of target proteins via the reversible oxidation of their active site dithiol. The PDO members of this superfamily include TRX, protein disulfide isomerase (PDI), tlpA-like, glutaredoxin, NrdH redoxin, and the bacterial Dsb (DsbA, DsbC, DsbG, DsbE, DsbDgamma) protein families. Members of the superfamily that do not function as PDOs but contain a TRX-fold domain include phosducins, peroxiredoxins and glutathione (GSH) peroxidases, SCO proteins, GSH transferases (GST, N-terminal domain), arsenic reductases, TRX-like ferredoxins and calsequestrin, among others.


Pssm-ID: 238829 [Multi-domain]  Cd Length: 69  Bit Score: 46.54  E-value: 4.02e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002298403 234 VLYFTAAWCGPCRFIGPVCKSLAEKHRNVVFLKVDIDE---LNSVAYRWNVSSVPSFFFVRNGKEI 296
Cdd:cd01659     1 LVLFYAPWCPFCQALRPVLAELALLNKGVKFEAVDVDEdpaLEKELKRYGVGGVPTLVVFGPGIGV 66
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 84-151 1.08e-06

Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell wall/membrane/envelope biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 47.49  E-value: 1.08e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1002298403  84 AIAYATRAVIFVKSKKPNAAIRDADAALKINPDSAKGYKSRGMAKAMLGKWEEAAQDLRMAAKLDYDE 151
Cdd:COG4783     4 AEALYALAQALLLAGDYDEAEALLEKALELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDE 71
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 63-150 1.20e-06

putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 50.08  E-value: 1.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002298403  63 EGKLDEAIEHLTEAIVLNPTSAIAYATRAVIFVKSKKPNAAIRDADAALKINPDSAKGYKSRGMAKAMLGKWEEAAQDLR 142
Cdd:TIGR02917 342 LGRVDEAIATLSPALGLDPDDPAALSLLGEAYLALGDFEKAAEYLAKATELDPENAAARTQLGISKLSQGDPSEAIADLE 421


                  ....*...
gi 1002298403 143 MAAKLDYD 150
Cdd:TIGR02917 422 TAAQLDPE 429
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 59-184 1.40e-06

Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 444034 [Multi-domain]  Cd Length: 155  Bit Score: 47.26  E-value: 1.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002298403  59 DAFSEGKLDEAIEHLTEAIVLNPTSAIAYATRAVIFVKSKKPNAAIRDADAALKINPDSAKGYKSRGMAKAMLGKWEEAA 138
Cdd:COG5010    29 AALAGANNTKEDELAAAGRDKLAKAFAIESPSDNLYNKLGDFEESLALLEQALQLDPNNPELYYNLALLYSRSGDKDEAK 108

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1002298403 139 QDLRMAAKLD-YDEEIGAELKKVEPNVLKIEEHRKKYERLRKERDIK 184
Cdd:COG5010   109 EYYEKALALSpDNPNAYSNLAALLLSLGQDDEAKAALQRALGTSPLK 155
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 43-148 1.48e-06

putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 49.70  E-value: 1.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002298403  43 SDEKRDQAQLCKNKGVDAFSEGKLDEAIEHLTEAIVLNPTSAIAYATRAVIFVKSKKPNAAIRDADAALKINPDSAKGYK 122
Cdd:TIGR02917 118 LLDDEGAAELLALRGLAYLGLGQLELAQKSYEQALAIDPRSLYAKLGLAQLALAENRFDEARALIDEVLTADPGNVDALL 197

                          90       100
                  ....*....|....*....|....*.
gi 1002298403 123 SRGMAKAMLGKWEEAAQDLRMAAKLD 148
Cdd:TIGR02917 198 LKGDLLLSLGNIELALAAYRKAIALR 223
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
48-184 2.41e-06

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 48.08  E-value: 2.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002298403  48 DQAQLCKNKGVDAFSEGKLDEAIEHLTEAIVLNPTSAIAYATRAVIFVKSKKPNAAIRDADAALKINPDSAKGYKSRGMA 127
Cdd:COG0457   108 DDAEALYNLGLALLELGRYDEAIEAYERALELDPDDADALYNLGIALEKLGRYEEALELLEKLEAAALAALLAAALGEAA 187

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1002298403 128 KAMLGKWEEAAQDLRMAAKLDYDEEIGAELKKVEPNVLKIEEHRKKYERLRKERDIK 184
Cdd:COG0457   188 LALAAAEVLLALLLALEQALRKKLAILTLAALAELLLLALALLLALRLAALALYQYR 244
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 66-150 3.65e-06

Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 48.45  E-value: 3.65e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002298403  66 LDEAIEHLTEAIVLNPTSAIAYATRAVIFVKSKKPNAAIRDADAALKINPDSAKGYKSRGMAKAMLGKWEEAAQDLRMAA 145
Cdd:COG3914    60 LALAAGEAAAAAAALLLLAALLELAALLLQALGRYEEALALYRRALALNPDNAEALFNLGNLLLALGRLEEALAALRRAL 139


                  ....*
gi 1002298403 146 KLDYD 150
Cdd:COG3914   140 ALNPD 144
TryX_like_family cd02964
Tryparedoxin (TryX)-like family; composed of TryX and related proteins including nucleoredoxin ...
 225-271 3.85e-06

Tryparedoxin (TryX)-like family; composed of TryX and related proteins including nucleoredoxin (NRX), rod-derived cone viability factor (RdCVF) and the nematode homolog described as a 16-kD class of TRX. Most members of this family, except RdCVF, are protein disulfide oxidoreductases containing an active site CXXC motif, similar to TRX.


Pssm-ID: 239262 [Multi-domain]  Cd Length: 132  Bit Score: 45.68  E-value: 3.85e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1002298403 225 AASSLS-RLVVLYFTAAWCGPCRFIGPVCKSLAEKHRN------VVFLKVDIDE 271
Cdd:cd02964    11 PVSALEgKTVGLYFSASWCPPCRAFTPKLVEFYEKLKEegknfeIVFVSRDRSE 64
TRX_NDPK cd02948
TRX domain, TRX and NDP-kinase (NDPK) fusion protein family; most members of this group are ...
 232-314 3.90e-06

TRX domain, TRX and NDP-kinase (NDPK) fusion protein family; most members of this group are fusion proteins which contain one redox active TRX domain containing a CXXC motif and three NDPK domains, and are characterized as intermediate chains (ICs) of axonemal outer arm dynein. Dyneins are molecular motors that generate force against microtubules to produce cellular movement, and are divided into two classes: axonemal and cytoplasmic. They are supramolecular complexes consisting of three protein groups classified according to size: dynein heavy, intermediate and light chains. Axonemal dyneins form two structures, the inner and outer arms, which are attached to doublet microtubules throughout the cilia and flagella. The human homolog is the sperm-specific Sptrx-2, presumed to be a component of the human sperm axoneme architecture. Included in this group is another human protein, TRX-like protein 2, a smaller fusion protein containing one TRX and one NDPK domain, which is also associated with microtubular structures. The other members of this group are hypothetical insect proteins containing a TRX domain and outer arm dynein light chains (14 and 16kDa) of Chlamydomonas reinhardtii. Using standard assays, the fusion proteins have shown no TRX enzymatic activity.


Pssm-ID: 239246 [Multi-domain]  Cd Length: 102  Bit Score: 44.63  E-value: 3.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002298403 232 LVVLYFTAAWCGPCRFIGPVCKSLAEK--HRNVVFLKVDIDELnSVAYRWNVSSVPSFFFVRNGKEIDKVVGADKNGLER 309
Cdd:cd02948    19 LTVVDVYQEWCGPCKAVVSLFKKIKNElgDDLLHFATAEADTI-DTLKRYRGKCEPTFLFYKNGELVAVIRGANAPLLNK 97


                  ....*
gi 1002298403 310 KVAQH 314
Cdd:cd02948    98 TITEL 102
DsbDgamma cd02953
DsbD gamma family; DsbD gamma is the C-terminal periplasmic domain of the bacterial protein ...
 222-300 6.10e-06

DsbD gamma family; DsbD gamma is the C-terminal periplasmic domain of the bacterial protein DsbD. It contains a CXXC motif in a TRX fold and shuttles the reducing potential from the membrane domain (DsbD beta) to the N-terminal periplasmic domain (DsbD alpha). DsbD beta, a transmembrane domain comprising of eight helices, acquires its reducing potential from the cytoplasmic thioredoxin. DsbD alpha transfers the acquired reducing potential from DsbD gamma to target proteins such as the periplasmic protein disulphide isomerases, DsbC and DsbG. This flow of reducing potential from the cytoplasm through DsbD allows DsbC and DsbG to act as isomerases in the oxidizing environment of the bacterial periplasm. DsbD also transfers reducing potential from the cytoplasm to specific reductases in the periplasm which are involved in the maturation of cytochromes.


Pssm-ID: 239251 [Multi-domain]  Cd Length: 104  Bit Score: 44.13  E-value: 6.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002298403 222 KLKAASSLSRLVVLYFTAAWCGPCR------FIGPVCKSLAEKhrNVVFLKVDIDELNSV--AY--RWNVSSVPSFFFVR 291
Cdd:cd02953     3 ALAQALAQGKPVFVDFTADWCVTCKvnekvvFSDPEVQAALKK--DVVLLRADWTKNDPEitALlkRFGVFGPPTYLFYG 80


                  ....*....
gi 1002298403 292 NGKEIDKVV 300
Cdd:cd02953    81 PGGEPEPLR 89
SoxW COG2143
Thioredoxin-related protein SoxW [Posttranslational modification, protein turnover, chaperones] ...
 219-304 6.80e-06

Thioredoxin-related protein SoxW [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441746 [Multi-domain]  Cd Length: 146  Bit Score: 45.28  E-value: 6.80e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002298403 219 LDTKLKAASSLSRLVVLYFTAAWCGPCR------FIGPVCKSLAEKHrnVVFLKVDIDELNSV-------------AYRW 279
Cdd:COG2143    29 LEEDLALAKAEGKPILLFFESDWCPYCKklhkevFSDPEVAAYLKEN--FVVVQLDAEGDKEVtdfdgetltekelARKY 106

                          90       100
                  ....*....|....*....|....*.
gi 1002298403 280 NVSSVPSF-FFVRNGKEIDKVVGADK 304
Cdd:COG2143   107 GVRGTPTLvFFDAEGKEIARIPGYLK 132
TryX_like_TryX_NRX cd03009
Tryparedoxin (TryX)-like family, TryX and nucleoredoxin (NRX) subfamily; TryX and NRX are ...
 227-271 1.08e-05

Tryparedoxin (TryX)-like family, TryX and nucleoredoxin (NRX) subfamily; TryX and NRX are thioredoxin (TRX)-like protein disulfide oxidoreductases that alter the redox state of target proteins via the reversible oxidation of an active center CXXC motif. TryX is involved in the regulation of oxidative stress in parasitic trypanosomatids by reducing TryX peroxidase, which in turn catalyzes the reduction of hydrogen peroxide and organic hydroperoxides. TryX derives reducing equivalents from reduced trypanothione, a polyamine peptide conjugate unique to trypanosomatids, which is regenerated by the NADPH-dependent flavoprotein trypanothione reductase. Vertebrate NRX is a 400-amino acid nuclear protein with one redox active TRX domain containing a CPPC active site motif followed by one redox inactive TRX-like domain. Mouse NRX transcripts are expressed in all adult tissues but is restricted to the nervous system and limb buds in embryos. Plant NRX, longer than the vertebrate NRX by about 100-200 amino acids, is a nuclear protein containing a redox inactive TRX-like domain between two redox active TRX domains. Both vertebrate and plant NRXs show thiol oxidoreductase activity in vitro. Their localization in the nucleus suggests a role in the redox regulation of nuclear proteins such as transcription factors.


Pssm-ID: 239307 [Multi-domain]  Cd Length: 131  Bit Score: 44.20  E-value: 1.08e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1002298403 227 SSLS-RLVVLYFTAAWCGPCRFIGPVCKSLAEKHRN------VVFLKVDIDE 271
Cdd:cd03009    14 SSLEgKTVGLYFSASWCPPCRAFTPKLVEFYEKLKEsgknfeIVFISWDRDE 65
PDI_a_ERp46 cd03005
PDIa family, endoplasmic reticulum protein 46 (ERp46) subfamily; ERp46 is an ER-resident ...
 237-302 1.28e-05

PDIa family, endoplasmic reticulum protein 46 (ERp46) subfamily; ERp46 is an ER-resident protein containing three redox active TRX domains. Yeast complementation studies show that ERp46 can substitute for protein disulfide isomerase (PDI) function in vivo. It has been detected in many tissues, however, transcript and protein levels do not correlate in all tissues, suggesting regulation at a posttranscriptional level. An identical protein, named endoPDI, has been identified as an endothelial PDI that is highly expressed in the endothelium of tumors and hypoxic lesions. It has a protective effect on cells exposed to hypoxia.


Pssm-ID: 239303 [Multi-domain]  Cd Length: 102  Bit Score: 43.43  E-value: 1.28e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002298403 237 FTAAWCGPCRFIGPVCKSLAEKHRN----VVFLKVDIDELNSVAYRWNVSSVPSFFFVRNGKEIDKVVGA 302
Cdd:cd03005    23 FFAPWCGHCKRLAPTWEQLAKKFNNenpsVKIAKVDCTQHRELCSEFQVRGYPTLLLFKDGEKVDKYKGT 92
PDI_a_PDI_a'_C cd02995
PDIa family, C-terminal TRX domain (a') subfamily; composed of the C-terminal redox active a' ...
 233-294 1.62e-05

PDIa family, C-terminal TRX domain (a') subfamily; composed of the C-terminal redox active a' domains of PDI, ERp72, ERp57 (or ERp60) and EFP1. PDI, ERp72 and ERp57 are endoplasmic reticulum (ER)-resident eukaryotic proteins involved in oxidative protein folding. They are oxidases, catalyzing the formation of disulfide bonds of newly synthesized polypeptides in the ER. They also exhibit reductase activity in acting as isomerases to correct any non-native disulfide bonds, as well as chaperone activity to prevent protein aggregation and facilitate the folding of newly synthesized proteins. PDI and ERp57 have the abb'a' domain structure (where a and a' are redox active TRX domains while b and b' are redox inactive TRX-like domains). PDI also contains an acidic region (c domain) after the a' domain that is absent in ERp57. ERp72 has an additional a domain at the N-terminus (a"abb'a' domain structure). ERp57 interacts with the lectin chaperones, calnexin and calreticulin, and specifically promotes the oxidative folding of glycoproteins, while PDI shows a wider substrate specificity. ERp72 associates with several ER chaperones and folding factors to form complexes in the ER that bind nascent proteins. EFP1 is a binding partner protein of thyroid oxidase, which is responsible for the generation of hydrogen peroxide, a crucial substrate of thyroperoxidase, which functions to iodinate thyroglobulin and synthesize thyroid hormones.


Pssm-ID: 239293 [Multi-domain]  Cd Length: 104  Bit Score: 42.93  E-value: 1.62e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1002298403 233 VVLYFTAAWCGPCRFIGPVCKSLAEK---HRNVVFLKVDIDElNSVAYRWNVSSVPSFFFVRNGK 294
Cdd:cd02995    21 VLVEFYAPWCGHCKALAPIYEELAEKlkgDDNVVIAKMDATA-NDVPSEFVVDGFPTILFFPAGD 84
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
228-302 1.89e-05

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 43.70  E-value: 1.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002298403 228 SLSRL----VVLYFTAAWCGPCRFIGPVCKSLAEKH--RNVVFLKVDIDEL---------------------NSVAYRWN 280
Cdd:COG1225    15 SLSDLrgkpVVLYFYATWCPGCTAELPELRDLYEEFkdKGVEVLGVSSDSDeahkkfaekyglpfpllsdpdGEVAKAYG 94

                          90       100
                  ....*....|....*....|...
gi 1002298403 281 VSSVPSFFFV-RNGKEIDKVVGA 302
Cdd:COG1225    95 VRGTPTTFLIdPDGKIRYVWVGP 117
ybbN cd02956
ybbN protein family; ybbN is a hypothetical protein containing a redox-inactive TRX-like ...
 228-302 1.90e-05

ybbN protein family; ybbN is a hypothetical protein containing a redox-inactive TRX-like domain. Its gene has been sequenced from several gammaproteobacteria and actinobacteria.


Pssm-ID: 239254 [Multi-domain]  Cd Length: 96  Bit Score: 42.64  E-value: 1.90e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002298403 228 SLSRLVVLYFTAAWCGPCRFIGPVCKSLAEKHR-NVVFLKVDIDELNSVAYRWNVSSVPSFFFVRNGKEIDKVVGA 302
Cdd:cd02956    10 STQVPVVVDFWAPRSPPSKELLPLLERLAEEYQgQFVLAKVNCDAQPQIAQQFGVQALPTVYLFAAGQPVDGFQGA 85
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 55-115 2.30e-05

Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 444034 [Multi-domain]  Cd Length: 155  Bit Score: 43.80  E-value: 2.30e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002298403  55 NKGVDAFSEGKLDEAIEHLTEAIVLNPTSAIAYATRAVIFVKSKKPNAAIRDADAALKINP 115
Cdd:COG5010    93 NLALLYSRSGDKDEAKEYYEKALALSPDNPNAYSNLAALLLSLGQDDEAKAALQRALGTSP 153
PDI_a_ERp38 cd02998
PDIa family, endoplasmic reticulum protein 38 (ERp38) subfamily; composed of proteins similar ...
 237-295 4.15e-05

PDIa family, endoplasmic reticulum protein 38 (ERp38) subfamily; composed of proteins similar to the P5-like protein first isolated from alfalfa, which contains two redox active TRX (a) domains at the N-terminus, like human P5, and a C-terminal domain with homology to the C-terminal domain of ERp29, unlike human P5. The cDNA clone of this protein (named G1) was isolated from an alfalfa cDNA library by screening with human protein disulfide isomerase (PDI) cDNA. The G1 protein is constitutively expressed in all major organs of the plant and its expression is induced by treatment with tunicamycin, indicating that it may be a glucose-regulated protein. The G1 homolog in the eukaryotic social amoeba Dictyostelium discoideum is also described as a P5-like protein, which is located in the endoplasmic reticulum (ER) despite the absence of an ER-retrieval signal. G1 homologs from Aspergillus niger and Neurospora crassa have also been characterized, and are named TIGA and ERp38, respectively. Also included in the alignment is an atypical PDI from Leishmania donovani containing a single a domain, and the C-terminal a domain of a P5-like protein from Entamoeba histolytica.


Pssm-ID: 239296 [Multi-domain]  Cd Length: 105  Bit Score: 41.85  E-value: 4.15e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002298403 237 FTAAWCGPCRFIGPVCKSLA---EKHRNVVFLKVDIDELNS-VAYRWNVSSVPSF-FFVRNGKE 295
Cdd:cd02998    25 FYAPWCGHCKNLAPEYEKLAavfANEDDVVIAKVDADEANKdLAKKYGVSGFPTLkFFPKGSTE 88
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
93-179 4.52e-05

Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 41.69  E-value: 4.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002298403  93 IFVKSKKPNAAIRDADAALKINPDSAKGYKSRGMAKAMLGKWEEAAQdLRMAAKLDYDE-EIGAELKKVEPNVLKIEEHR 171
Cdd:COG3063     1 LYLKLGDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEAIA-LEKALKLDPNNaEALLNLAELLLELGDYDEAL 79


                  ....*...
gi 1002298403 172 KKYERLRK 179
Cdd:COG3063    80 AYLERALE 87
TRX_NTR cd02949
TRX domain, novel NADPH thioredoxin reductase (NTR) family; composed of fusion proteins found ...
 231-301 4.66e-05

TRX domain, novel NADPH thioredoxin reductase (NTR) family; composed of fusion proteins found only in oxygenic photosynthetic organisms containing both TRX and NTR domains. The TRX domain functions as a protein disulfide reductase via the reversible oxidation of an active center dithiol present in a CXXC motif, while the NTR domain functions as a reductant to oxidized TRX. The fusion protein is bifunctional, showing both TRX and NTR activities, but it is not an independent NTR/TRX system. In plants, the protein is found exclusively in shoots and mature leaves and is localized in the chloroplast. It is involved in plant protection against oxidative stress.


Pssm-ID: 239247 [Multi-domain]  Cd Length: 97  Bit Score: 41.72  E-value: 4.66e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002298403 231 RLVVLYFTAAWCGPCRFIGPVCKSLAEKHRNVV-FLKVDIDELNSVAYRWNVSSVPSFFFVRNGKEIDKVVG 301
Cdd:cd02949    14 RLILVLYTSPTCGPCRTLKPILNKVIDEFDGAVhFVEIDIDEDQEIAEAAGIMGTPTVQFFKDKELVKEISG 85
CpoB COG1729
Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane ...
 58-146 7.28e-05

Cell division protein CpoB, coordinates peptidoglycan biosynthesis and outer membrane constriction [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 441335 [Multi-domain]  Cd Length: 113  Bit Score: 41.52  E-value: 7.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002298403  58 VDAFSEGKLDEAIEHLTEAIVLNPTSAI---AYATRAVIFVKSKKPNAAIRDADAALKINPDSAKGYKS---RGMAKAML 131
Cdd:COG1729     1 KALLKAGDYDEAIAAFKAFLKRYPNSPLapdALYWLGEAYYALGDYDEAAEAFEKLLKRYPDSPKAPDAllkLGLSYLEL 80

                          90
                  ....*....|....*
gi 1002298403 132 GKWEEAAQDLRMAAK 146
Cdd:COG1729    81 GDYDKARATLEELIK 95
PDI_a_ERp44 cd02996
PDIa family, endoplasmic reticulum protein 44 (ERp44) subfamily; ERp44 is an ER-resident ...
 208-293 7.67e-05

PDIa family, endoplasmic reticulum protein 44 (ERp44) subfamily; ERp44 is an ER-resident protein, induced during stress, involved in thiol-mediated ER retention. It contains an N-terminal TRX domain, similar to that of PDIa, with a CXFS motif followed by two redox inactive TRX-like domains, homologous to the b and b' domains of PDI. The CXFS motif in the N-terminal domain allows ERp44 to form stable reversible mixed disulfides with its substrates. Through this activity, ERp44 mediates the ER localization of Ero1alpha, a protein that oxidizes protein disulfide isomerases into their active form. ERp44 also prevents the secretion of unassembled cargo protein with unpaired cysteines. It also modulates the activity of inositol 1,4,5-triphosphate type I receptor (IP3R1), an intracellular channel protein that mediates calcium release from the ER to the cytosol.


Pssm-ID: 239294 [Multi-domain]  Cd Length: 108  Bit Score: 41.22  E-value: 7.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002298403 208 GDVIAIhSSSELDTKLKAAsslsRLVVLYFTAAWCGPCRFIGPVCKSLAEKHRN-------VVFLKVDIDELNSVAYRWN 280
Cdd:cd02996     1 SEIVSL-TSGNIDDILQSA----ELVLVNFYADWCRFSQMLHPIFEEAAAKIKEefpdagkVVWGKVDCDKESDIADRYR 75

                          90
                  ....*....|...
gi 1002298403 281 VSSVPSFFFVRNG 293
Cdd:cd02996    76 INKYPTLKLFRNG 88
Thioredoxin_8 pfam13905
Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 231-296 1.02e-04

Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the reversible oxidation of an active centre disulfide bond.


Pssm-ID: 464033 [Multi-domain]  Cd Length: 95  Bit Score: 40.75  E-value: 1.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002298403 231 RLVVLYFTAAWCGPCRFIGPVCKSLAEKHR-----NVVFLKVDIDELNSVAY-----------------------RWNVS 282
Cdd:pfam13905   2 KVVLLYFGASWCKPCRRFTPLLKELYEKLKkkknvEIVFVSLDRDLEEFKDYlkkmpkdwlsvpfdddernelkrKYGVN 81

                          90
                  ....*....|....
gi 1002298403 283 SVPSFFFVRNGKEI 296
Cdd:pfam13905  82 AIPTLVLLDPNGEV 95
TxlA cd02950
TRX-like protein A (TxlA) family; TxlA was originally isolated from the cyanobacterium ...
 234-301 1.12e-04

TRX-like protein A (TxlA) family; TxlA was originally isolated from the cyanobacterium Synechococcus. It is found only in oxygenic photosynthetic organisms. TRX is a small enzyme that participate in redox reactions, via the reversible oxidation of an active site dithiol present in a CXXC motif. Disruption of the txlA gene suggests that the protein is involved in the redox regulation of the structure and function of photosynthetic apparatus. The plant homolog (designated as HCF164) is localized in the chloroplast and is involved in the assembly of the cytochrome b6f complex, which takes a central position in photosynthetic electron transport.


Pssm-ID: 239248 [Multi-domain]  Cd Length: 142  Bit Score: 41.55  E-value: 1.12e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002298403 234 VLYFTAAWCGPCRFIGPVCKSLAEKHR---NVVFLKVD----IDELNsvayRWNVSSVPSF-FFVRNGKEIDKVVG 301
Cdd:cd02950    24 LVEFYADWCTVCQEMAPDVAKLKQKYGdqvNFVMLNVDnpkwLPEID----RYRVDGIPHFvFLDREGNEEGQSIG 95
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
60-148 1.59e-04

Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 42.21  E-value: 1.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002298403  60 AFSEGKLDEAIEHLTEAIVLNPTSAIA-YATRAVIFVKSKKPNAAIRDADAALKI--------NPDSAKGYKSRGMAKAM 130
Cdd:COG4785     6 LALLLALALAAAAASKAAILLAALLFAaVLALAIALADLALALAAAALAAAALAAeridralaLPDLAQLYYERGVAYDS 85

                          90
                  ....*....|....*...
gi 1002298403 131 LGKWEEAAQDLRMAAKLD 148
Cdd:COG4785    86 LGDYDLAIADFDQALELD 103
Phd_like_TxnDC9 cd02989
Phosducin (Phd)-like family, Thioredoxin (TRX) domain containing protein 9 (TxnDC9) subfamily; ...
 255-306 2.05e-04

Phosducin (Phd)-like family, Thioredoxin (TRX) domain containing protein 9 (TxnDC9) subfamily; composed of predominantly uncharacterized eukaryotic proteins, containing a TRX-like domain without the redox active CXXC motif. The gene name for the human protein is TxnDC9. The two characterized members are described as Phd-like proteins, PLP1 of Saccharomyces cerevisiae and PhLP3 of Dictyostelium discoideum. Gene disruption experiments show that both PLP1 and PhLP3 are non-essential proteins. Unlike Phd and most Phd-like proteins, members of this group do not contain the Phd N-terminal helical domain which is implicated in binding to the G protein betagamma subunit.


Pssm-ID: 239287  Cd Length: 113  Bit Score: 40.25  E-value: 2.05e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1002298403 255 LAEKHRNVVFLKVDIDELNSVAYRWNVSSVPSFFFVRNGKEIDKVVGADKNG 306
Cdd:cd02989    47 LAKKHLETKFIKVNAEKAPFLVEKLNIKVLPTVILFKNGKTVDRIVGFEELG 98
TPR_11 pfam13414
TPR repeat;
61-96 2.37e-04

TPR repeat;


Pssm-ID: 315977 [Multi-domain]  Cd Length: 42  Bit Score: 38.22  E-value: 2.37e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1002298403  61 FSEGKLDEAIEHLTEAIVLNPTSAIAYATRAVIFVK 96
Cdd:pfam13414   5 YEQGKYEEAIEAYKKALKLDPDNPEAYYNLGLAYYK 40
TlpA_like_DsbE cd03010
TlpA-like family, DsbE (also known as CcmG and CycY) subfamily; DsbE is a membrane-anchored, ...
 231-302 3.91e-04

TlpA-like family, DsbE (also known as CcmG and CycY) subfamily; DsbE is a membrane-anchored, periplasmic TRX-like reductase containing a CXXC motif that specifically donates reducing equivalents to apocytochrome c via CcmH, another cytochrome c maturation (Ccm) factor with a redox active CXXC motif. Assembly of cytochrome c requires the ligation of heme to reduced thiols of the apocytochrome. In bacteria, this assembly occurs in the periplasm. The reductase activity of DsbE in the oxidizing environment of the periplasm is crucial in the maturation of cytochrome c.


Pssm-ID: 239308 [Multi-domain]  Cd Length: 127  Bit Score: 39.48  E-value: 3.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002298403 231 RLVVLYFTAAWCGPCRFIGPVCKSLAEKHRNVV--------------FLK--------VDIDELNSVAYRWNVSSVPSFF 288
Cdd:cd03010    26 KPYLLNVWASWCAPCREEHPVLMALARQGRVPIyginykdnpenalaWLArhgnpyaaVGFDPDGRVGIDLGVYGVPETF 105

                          90
                  ....*....|....*
gi 1002298403 289 FV-RNGKEIDKVVGA 302
Cdd:cd03010   106 LIdGDGIIRYKHVGP 120
PDI_a_TMX cd02994
PDIa family, TMX subfamily; composed of proteins similar to the TRX-related human ...
 237-293 4.18e-04

PDIa family, TMX subfamily; composed of proteins similar to the TRX-related human transmembrane protein, TMX. TMX is a type I integral membrane protein; the N-terminal redox active TRX domain is present in the endoplasmic reticulum (ER) lumen while the C-terminus is oriented towards the cytoplasm. It is expressed in many cell types and its active site motif (CPAC) is unique. In vitro, TMX reduces interchain disulfides of insulin and renatures inactive RNase containing incorrect disulfide bonds. The C. elegans homolog, DPY-11, is expressed only in the hypodermis and resides in the cytoplasm. It is required for body and sensory organ morphogeneis. Another uncharacterized TRX-related transmembrane protein, human TMX4, is included in the alignment. The active site sequence of TMX4 is CPSC.


Pssm-ID: 239292 [Multi-domain]  Cd Length: 101  Bit Score: 38.90  E-value: 4.18e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1002298403 237 FTAAWCGPCRFIGPVCKSLAEKHR--NVVFLKVDIDELNSVAYRWNVSSVPSFFFVRNG 293
Cdd:cd02994    23 FYAPWCPACQQLQPEWEEFADWSDdlGINVAKVDVTQEPGLSGRFFVTALPTIYHAKDG 81
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 56-148 4.54e-04

putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 41.99  E-value: 4.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002298403  56 KGVDAFSEGKLDEAIEHLTEAIVLNPTSAIAYATRAVIFVKSKKPNAAIRDADAALKINPDSAKGYKSRGMAKAMLGKWE 135
Cdd:TIGR02917 199 KGDLLLSLGNIELALAAYRKAIALRPNNIAVLLALATILIEAGEFEEAEKHADALLKKAPNSPLAHYLKALVDFQKKNYE 278

                          90
                  ....*....|...
gi 1002298403 136 EAAQDLRMAAKLD 148
Cdd:TIGR02917 279 DARETLQDALKSA 291
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 57-148 4.66e-04

putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 41.99  E-value: 4.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002298403  57 GVDAFSEGKLDEAIEHLTEAIVLNPTSAIAYATRAVIFVKSKKPNAAIRDADAALKINPDSAKGYKSRGMAKAMLGKWEE 136
Cdd:TIGR02917 302 GASEYQLGNLEQAYQYLNQILKYAPNSHQARRLLASIQLRLGRVDEAIATLSPALGLDPDDPAALSLLGEAYLALGDFEK 381

                          90
                  ....*....|..
gi 1002298403 137 AAQDLRMAAKLD 148
Cdd:TIGR02917 382 AAEYLAKATELD 393
TPR_1 pfam00515
Tetratricopeptide repeat;
50-82 6.17e-04

Tetratricopeptide repeat;


Pssm-ID: 459840 [Multi-domain]  Cd Length: 34  Bit Score: 36.63  E-value: 6.17e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1002298403  50 AQLCKNKGVDAFSEGKLDEAIEHLTEAIVLNPT 82
Cdd:pfam00515   1 AKALYNLGNAYFKLGKYDEALEYYEKALELNPN 33
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 64-118 1.19e-03

Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443378 [Multi-domain]  Cd Length: 131  Bit Score: 38.45  E-value: 1.19e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1002298403  64 GKLDEAIEHLTEAIVLNPTSAIAYATRAVIFVKSKKPNAAIRDADAALKINPDSA 118
Cdd:COG4235    65 GDTEEAEELLERALALDPDNPEALYLLGLAAFQQGDYAEAIAAWQKLLALLPADA 119
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 232-294 1.44e-03

protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide isomerases retained in the endoplasmic reticulum (ER) and closely related forms. Some members have been assigned alternative or additional functions such as prolyl 4-hydroxylase and dolichyl-diphosphooligosaccharide-protein glycotransferase. Members of this family have at least two protein-disulfide domains, each similar to thioredoxin but with the redox-active disulfide in the motif PWCGHCK, and an ER retention signal at the extreme C-terminus (KDEL, HDEL, and similar motifs).


Pssm-ID: 273457 [Multi-domain]  Cd Length: 462  Bit Score: 40.04  E-value: 1.44e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1002298403 232 LVVLYFTAAWCGPCRFIGP----VCKSLAEKHRNVVFLKVDIDELNSVAYRWNVSSVPSFFFVRNGK 294
Cdd:TIGR01130  20 FVLVEFYAPWCGHCKSLAPeyekAADELKKKGPPIKLAKVDATEEKDLAQKYGVSGYPTLKIFRNGE 86
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 56-150 1.48e-03

putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 40.45  E-value: 1.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002298403  56 KGVDAFSEGKLDEAIEHLTEAIVLNPTSAIAYATRAVIFVKSKKPNAAIRDADAALKINPDSAKGYKSRGMAKAMLGKWE 135
Cdd:TIGR02917 403 LGISKLSQGDPSEAIADLETAAQLDPELGRADLLLILSYLRSGQFDKALAAAKKLEKKQPDNASLHNLLGAIYLGKGDLA 482

                          90
                  ....*....|....*
gi 1002298403 136 EAAQDLRMAAKLDYD 150
Cdd:TIGR02917 483 KAREAFEKALSIEPD 497
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 48-155 2.11e-03

putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 39.68  E-value: 2.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002298403  48 DQAQLCKNKGVDAFSEGKLDEAIEHLTEAIVLNPTSAIAYATRAVIFVKSKKPNAAIRDADAALKINPDSAKGYKSRGMA 127
Cdd:TIGR02917 463 DNASLHNLLGAIYLGKGDLAKAREAFEKALSIEPDFFPAAANLARIDIQEGNPDDAIQRFEKVLTIDPKNLRAILALAGL 542

                          90       100
                  ....*....|....*....|....*...
gi 1002298403 128 KAMLGKWEEAAQDLRMAAKLDYDEEIGA 155
Cdd:TIGR02917 543 YLRTGNEEEAVAWLEKAAELNPQEIEPA 570
Phd_like cd02957
Phosducin (Phd)-like family; composed of Phd and Phd-like proteins (PhLP), characterized as ...
 253-306 2.17e-03

Phosducin (Phd)-like family; composed of Phd and Phd-like proteins (PhLP), characterized as cytosolic regulators of G protein functions. Phd and PhLPs specifically bind G protein betagamma (Gbg)-subunits with high affinity, resulting in the solubilization of Gbg from the plasma membrane and impeding G protein-mediated signal transduction by inhibiting the formation of a functional G protein trimer (G protein alphabetagamma). Phd also inhibits the GTPase activity of G protein alpha. Phd can be phosphorylated by protein kinase A and G protein-coupled receptor kinase 2, leading to its inactivation. Phd was originally isolated from the retina, where it is highly expressed and has been implicated to play an important role in light adaptation. It is also found in the pineal gland, liver, spleen, striated muscle and the brain. The C-terminal domain of Phd adopts a thioredoxin fold, but it does not contain a CXXC motif. Phd interacts with G protein beta mostly through the N-terminal helical domain. Also included in this family is a PhLP characterized as a viral inhibitor of apoptosis (IAP)-associated factor, named VIAF, that functions in caspase activation during apoptosis.


Pssm-ID: 239255 [Multi-domain]  Cd Length: 113  Bit Score: 37.15  E-value: 2.17e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1002298403 253 KSLAEKHRNVVFLKVDIdELNSVAYRWNVSSVPSFFFVRNGKEIDKVVGADKNG 306
Cdd:cd02957    47 EELAAKYPETKFVKINA-EKAFLVNYLDIKVLPTLLVYKNGELIDNIVGFEELG 99
TMX2 cd02962
TMX2 family; composed of proteins similar to human TMX2, a 372-amino acid TRX-related ...
 237-298 2.42e-03

TMX2 family; composed of proteins similar to human TMX2, a 372-amino acid TRX-related transmembrane protein, identified and characterized through the cloning of its cDNA from a human fetal library. It contains a TRX domain but the redox active CXXC motif is replaced with SXXC. Sequence analysis predicts that TMX2 may be a Type I membrane protein, with its C-terminal half protruding on the luminal side of the endoplasmic reticulum (ER). In addition to the TRX domain, transmembrane region and ER-retention signal, TMX2 also contains a Myb DNA-binding domain repeat signature and a dileucine motif in the tail.


Pssm-ID: 239260 [Multi-domain]  Cd Length: 152  Bit Score: 37.75  E-value: 2.42e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002298403 237 FTAAWCGPCRFIGPVCKSLAEK--HRNVVFLKVDIDELNSVAYRWNVSS------VPSFFFVRNGKEIDK 298
Cdd:cd02962    54 FFTTWSPECVNFAPVFAELSLKynNNNLKFGKIDIGRFPNVAEKFRVSTsplskqLPTIILFQGGKEVAR 123
TPR_9 pfam13371
Tetratricopeptide repeat;
93-141 2.65e-03

Tetratricopeptide repeat;


Pssm-ID: 463860 [Multi-domain]  Cd Length: 73  Bit Score: 36.04  E-value: 2.65e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1002298403  93 IFVKSKKPNAAIRDADAALKINPDSAKGYKSRGMAKAMLGKWEEAAQDL 141
Cdd:pfam13371   4 IYLREEDWERALAVVERLLLLAPDDPEERRDRGLLYAQLGCFQAALEDL 52
TPR smart00028
Tetratricopeptide repeats; Repeats present in 4 or more copies in proteins. Contain a minimum ...
 50-82 2.93e-03

Tetratricopeptide repeats; Repeats present in 4 or more copies in proteins. Contain a minimum of 34 amino acids each and self-associate via a "knobs and holes" mechanism.


Pssm-ID: 197478 [Multi-domain]  Cd Length: 34  Bit Score: 34.73  E-value: 2.93e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1002298403   50 AQLCKNKGVDAFSEGKLDEAIEHLTEAIVLNPT 82
Cdd:smart00028   1 AEALYNLGNAYLKLGDYDEALEYYEKALELDPN 33
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 40-147 3.66e-03

putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 38.91  E-value: 3.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002298403  40 VEVSDEKRDQAQLCKNKGVDAFSEGKLDEAIEHLTEAIVLNPTSAIAYATRAVIFVKSKKPNAAIRDADAALKINPDSAK 119
Cdd:TIGR02917 591 NEAADAAPDSPEAWLMLGRAQLAAGDLNKAVSSFKKLLALQPDSALALLLLADAYAVMKNYAKAITSLKRALELKPDNTE 670

                          90       100
                  ....*....|....*....|....*...
gi 1002298403 120 gyksrgmAKAMLGKWEEAAQDLRMAAKL 147
Cdd:TIGR02917 671 -------AQIGLAQLLLAAKRTESAKKI 691
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 55-152 4.03e-03

putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly within a subset of Gram-negative bacterial species with the proposed PEP-CTERM/exosortase system, analogous to the LPXTG/sortase system common in Gram-positive bacteria. This protein occurs in a species if and only if a transmembrane histidine kinase (TIGR02916) and a DNA-binding response regulator (TIGR02915) also occur. The present of tetratricopeptide repeats (TPR) suggests protein-protein interaction, possibly for the regulation of PEP-CTERM protein expression, since many PEP-CTERM proteins in these genomes are preceded by a proposed DNA binding site for the response regulator.


Pssm-ID: 274350 [Multi-domain]  Cd Length: 899  Bit Score: 38.91  E-value: 4.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002298403  55 NKGVDAFSEGKLDEAIEHLTEAIVLNPTSAIAYATRAVIFVKSKKPNAAIRDADAALKINPDSAKGYKSRGMAKAMLGKW 134
Cdd:TIGR02917 232 ALATILIEAGEFEEAEKHADALLKKAPNSPLAHYLKALVDFQKKNYEDARETLQDALKSAPEYLPALLLAGASEYQLGNL 311

                          90
                  ....*....|....*...
gi 1002298403 135 EEAAQDLRMAakLDYDEE 152
Cdd:TIGR02917 312 EQAYQYLNQI--LKYAPN 327
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
111-151 4.12e-03

Tetratricopeptide (TPR) repeat [General function prediction only];


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 38.06  E-value: 4.12e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1002298403 111 LKINPDSAKGYKSRGMAKAMLGKWEEAAQDLRMAAKLDYDE 151
Cdd:COG0457     1 LELDPDDAEAYNNLGLAYRRLGRYEEAIEDYEKALELDPDD 41
PTZ00121 PTZ00121
MAEBL; Provisional
 95-192 4.48e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 38.97  E-value: 4.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002298403   95 VKSKKPNAAIRDADAAL-KINPDSAKGYKSRGMAKAMLGKWEEAAQDLRMAAKLDYDEEIGAELKKVEPNVLKIEEHRKK 173
Cdd:PTZ00121  1347 AAKAEAEAAADEAEAAEeKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKK 1426

                           90
                   ....*....|....*....
gi 1002298403  174 YERLRKERDIKKAEMEKQR 192
Cdd:PTZ00121  1427 AEEKKKADEAKKKAEEAKK 1445
Thioredoxin_2 pfam13098
Thioredoxin-like domain;
231-302 5.83e-03

Thioredoxin-like domain;


Pssm-ID: 379034 [Multi-domain]  Cd Length: 103  Bit Score: 35.86  E-value: 5.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002298403 231 RLVVLYFTAAWCGPCR--------------FIGPVCKSLAE---KHRNVVFLKVDIDELNSVAYRWNVSSVPSFFFVRNG 293
Cdd:pfam13098   5 KPVLVVFTDPDCPYCKklkkelledpdvtvYLGPNFVFIAVniwCAKEVAKAFTDILENKELGRKYGVRGTPTIVFFDGK 84


                  ....*....
gi 1002298403 294 KEIDKVVGA 302
Cdd:pfam13098  85 GELLRLPGY 93
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 233-294 8.19e-03

protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide isomerases retained in the endoplasmic reticulum (ER) and closely related forms. Some members have been assigned alternative or additional functions such as prolyl 4-hydroxylase and dolichyl-diphosphooligosaccharide-protein glycotransferase. Members of this family have at least two protein-disulfide domains, each similar to thioredoxin but with the redox-active disulfide in the motif PWCGHCK, and an ER retention signal at the extreme C-terminus (KDEL, HDEL, and similar motifs).


Pssm-ID: 273457 [Multi-domain]  Cd Length: 462  Bit Score: 37.73  E-value: 8.19e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002298403 233 VVLYFTAAWCGPCRFIGPVCKSLAEKHR----NVVFLKVDIDElNSVAYrWNVSSVPSFFFVRNGK 294
Cdd:TIGR01130 367 VLVEFYAPWCGHCKNLAPIYEELAEKYKdaesDVVIAKMDATA-NDVPP-FEVEGFPTIKFVPAGK 430
SirB1 COG2912
Regulator of sirC expression, contains transglutaminase-like and TPR domains [Signal ...
 93-142 8.67e-03

Regulator of sirC expression, contains transglutaminase-like and TPR domains [Signal transduction mechanisms];


Pssm-ID: 442156 [Multi-domain]  Cd Length: 264  Bit Score: 37.11  E-value: 8.67e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1002298403  93 IFVKSKKPNAAIRDADAALKINPDSAKGYKSRGMAKAMLGKWEEAAQDLR 142
Cdd:COG2912   188 AYLREKDWERALRVVERLLLLDPDDPYEIRDRGLLYAQLGCYQAALEDLE 237
TPR_2 pfam07719
Tetratricopeptide repeat; This Pfam entry includes outlying Tetratricopeptide-like repeats ...
 50-82 8.71e-03

Tetratricopeptide repeat; This Pfam entry includes outlying Tetratricopeptide-like repeats (TPR) that are not matched by pfam00515.


Pssm-ID: 429619 [Multi-domain]  Cd Length: 33  Bit Score: 33.27  E-value: 8.71e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1002298403  50 AQLCKNKGVDAFSEGKLDEAIEHLTEAIVLNPT 82
Cdd:pfam07719   1 AEALYNLGLAYYKLGDYEEALEAYEKALELDPN 33
 
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