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Conserved domains on  [gi|145332619|ref|NP_001078175|]
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tetraticopeptide domain-containing thioredoxin [Arabidopsis thaliana]

Protein Classification

Graphical summary

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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 ...
 285-367 1.10e-31

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: 114.96  E-value: 1.10e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332619 285 SRLLILYFTATWCGPCRYMSPLYSNLATQHSRVVFLKVDIDKANDVAASWNISSVPTFCFIRDGKEVDKVVGAD-KGSLE 363
Cdd:cd02947   10 AKPVVVDFWAPWCGPCKAIAPVLEELAEEYPKVKFVKVDVDENPELAEEYGVRSIPTFLFFKNGKEVDRVVGADpKEELE 89


                 ....
gi 145332619 364 QKIA 367
Cdd:cd02947   90 EFLE 93
Hip_N cd14438
N-terminal dimerization domain of the Hsp70-interacting protein (Hip) and similar proteins; ...
 6-44 3.16e-15

N-terminal dimerization domain of the Hsp70-interacting protein (Hip) and similar proteins; The Hsc70/Hsp70-interacting protein (Hip, also p48 or suppressor of tumorigenicity ST13) functions as a regulator of the cyclic action of Hsp70. Hip forms homodimers, and this model characterizes the N-terminal dimerization domain, which may not be directly involved in its regulatory function. A central domain of Hip that contains TPR repeats binds the ATPase domain of Hsp70 and slows the release of ADP.


:

Pssm-ID: 271228  Cd Length: 41  Bit Score: 68.73  E-value: 3.16e-15
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 145332619   6 QVAELRRFVEQLKLNPSILHDPSLVFFKEYLRSLGAQVP 44
Cdd:cd14438    3 KLKELKAFVELCKQNPSILHTPELSFFKEYLESLGAKIP 41
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
101-260 8.98e-14

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


:

Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 70.42  E-value: 8.98e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332619 101 NRDDAQSEKSKAMEAISDGRFDEAIEHLTKAVMLNPTSAILYATRASVFLKVKKPNAAIRDANVALQFNSDSAKGYKSRG 180
Cdd:COG0457   72 DPDDAEALNNLGLALQALGRYEEALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYERALELDPDDADALYNLG 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332619 181 MAKAMLGQWEEAAADLHVASKLDYDEEIGTMLKKVEPNAKRIEEHRRKYQRLRKEKELQRAERERRKQQEAQEREAQAAL 260
Cdd:COG0457  152 IALEKLGRYEEALELLEKLEAAALAALLAAALGEAALALAAAEVLLALLLALEQALRKKLAILTLAALAELLLLALALLL 231
 
Name Accession Description Interval E-value
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 285-367 1.10e-31

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: 114.96  E-value: 1.10e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332619 285 SRLLILYFTATWCGPCRYMSPLYSNLATQHSRVVFLKVDIDKANDVAASWNISSVPTFCFIRDGKEVDKVVGAD-KGSLE 363
Cdd:cd02947   10 AKPVVVDFWAPWCGPCKAIAPVLEELAEEYPKVKFVKVDVDENPELAEEYGVRSIPTFLFFKNGKEVDRVVGADpKEELE 89


                 ....
gi 145332619 364 QKIA 367
Cdd:cd02947   90 EFLE 93
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 289-369 9.90e-27

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: 102.21  E-value: 9.90e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332619 289 ILYFTATWCGPCRYMSPLYSNLATQHS-RVVFLKVDIDKANDVAASWNISSVPTFCFIRDGKEVDKVVGA-DKGSLEQKI 366
Cdd:COG3118   22 LVDFWAPWCGPCKMLAPVLEELAAEYGgKVKFVKVDVDENPELAAQFGVRSIPTLLLFKDGQPVDRFVGAlPKEQLREFL 101


                 ...
gi 145332619 367 AQH 369
Cdd:COG3118  102 DKV 104
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 285-367 7.65e-24

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: 94.61  E-value: 7.65e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332619  285 SRLLILYFTATWCGPCRYMSPLYSNLATQHS-RVVFLKVDIDKANDVAASWNISSVPTFCFIRDGKEVDKVVGA-DKGSL 362
Cdd:pfam00085  18 SKPVLVDFYAPWCGPCKMLAPEYEELAQEYKgNVVFAKVDVDENPDLASKYGVRGYPTLIFFKNGQPVDDYVGArPKDAL 97


                  ....*
gi 145332619  363 EQKIA 367
Cdd:pfam00085  98 AAFLK 102
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 286-369 1.22e-23

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: 93.89  E-value: 1.22e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332619  286 RLLILYFTATWCGPCRYMSPLYSNLATQ-HSRVVFLKVDIDKANDVAASWNISSVPTFCFIRDGKEVDKVVGA-DKGSLE 363
Cdd:TIGR01068  15 KPVLVDFWAPWCGPCKMIAPILEELAKEyEGKVKFVKLNVDENPDIAAKYGIRSIPTLLLFKNGKEVDRSVGAlPKAALK 94


                  ....*.
gi 145332619  364 QKIAQH 369
Cdd:TIGR01068  95 QLINKN 100
PTZ00051 PTZ00051
thioredoxin; Provisional
 287-364 3.14e-21

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 87.24  E-value: 3.14e-21
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145332619 287 LLILYFTATWCGPCRYMSPLYSNLATQHSRVVFLKVDIDKANDVAASWNISSVPTFCFIRDGKEVDKVVGADKGSLEQ 364
Cdd:PTZ00051  20 LVIVDFYAEWCGPCKRIAPFYEECSKEYTKMVFVKVDVDELSEVAEKENITSMPTFKVFKNGSVVDTLLGANDEALKQ 97
Hip_N cd14438
N-terminal dimerization domain of the Hsp70-interacting protein (Hip) and similar proteins; ...
 6-44 3.16e-15

N-terminal dimerization domain of the Hsp70-interacting protein (Hip) and similar proteins; The Hsc70/Hsp70-interacting protein (Hip, also p48 or suppressor of tumorigenicity ST13) functions as a regulator of the cyclic action of Hsp70. Hip forms homodimers, and this model characterizes the N-terminal dimerization domain, which may not be directly involved in its regulatory function. A central domain of Hip that contains TPR repeats binds the ATPase domain of Hsp70 and slows the release of ADP.


Pssm-ID: 271228  Cd Length: 41  Bit Score: 68.73  E-value: 3.16e-15
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 145332619   6 QVAELRRFVEQLKLNPSILHDPSLVFFKEYLRSLGAQVP 44
Cdd:cd14438    3 KLKELKAFVELCKQNPSILHTPELSFFKEYLESLGAKIP 41
HipN pfam18253
Hsp70-interacting protein N N-terminal domain; This is the N-terminal domain, known as HipN, ...
 3-44 4.51e-14

Hsp70-interacting protein N N-terminal domain; This is the N-terminal domain, known as HipN, found in Hsp70-interacting protein (Hip) present in Rattus norvegicus. Hip cooperates with the chaperone Hsp70 in protein folding and prevention of aggregation and may delay substrate release by slowing ADP dissociation from Hsp70. HipN is responsible for N-terminal homo-dimerization which is necessary so that the Hip dimer can interact with Hsp70 molecules.


Pssm-ID: 408069  Cd Length: 42  Bit Score: 65.76  E-value: 4.51e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 145332619    3 DAIQVAELRRFVEQLKLNPSILHDPSLVFFKEYLRSLGAQVP 44
Cdd:pfam18253   1 DPAHLSLLKQFVDLCKANPSILHLPELAFFKEFLESLGATVP 42
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
101-260 8.98e-14

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 70.42  E-value: 8.98e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332619 101 NRDDAQSEKSKAMEAISDGRFDEAIEHLTKAVMLNPTSAILYATRASVFLKVKKPNAAIRDANVALQFNSDSAKGYKSRG 180
Cdd:COG0457   72 DPDDAEALNNLGLALQALGRYEEALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYERALELDPDDADALYNLG 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332619 181 MAKAMLGQWEEAAADLHVASKLDYDEEIGTMLKKVEPNAKRIEEHRRKYQRLRKEKELQRAERERRKQQEAQEREAQAAL 260
Cdd:COG0457  152 IALEKLGRYEEALELLEKLEAAALAALLAAALGEAALALAAAEVLLALLLALEQALRKKLAILTLAALAELLLLALALLL 231
PLN03088 PLN03088
SGT1, suppressor of G2 allele of SKP1; Provisional
 110-206 5.12e-12

SGT1, suppressor of G2 allele of SKP1; Provisional


Pssm-ID: 215568 [Multi-domain]  Cd Length: 356  Bit Score: 66.35  E-value: 5.12e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332619 110 SKAMEAISDGRFDEAIEHLTKAVMLNPTSAILYATRASVFLKVKKPNAAIRDANVALQFNSDSAKGYKSRGMAKAMLGQW 189
Cdd:PLN03088   7 DKAKEAFVDDDFALAVDLYTQAIDLDPNNAELYADRAQANIKLGNFTEAVADANKAIELDPSLAKAYLRKGTACMKLEEY 86

                         90
                 ....*....|....*..
gi 145332619 190 EEAAADLHVASKLDYDE 206
Cdd:PLN03088  87 QTAKAALEKGASLAPGD 103
3a0801s09 TIGR00990
mitochondrial precursor proteins import receptor (72 kDa mitochondrial outermembrane protein) ...
 42-228 3.18e-08

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: 55.38  E-value: 3.18e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332619   42 QVPKIEKTAETKPSFSPKHDDDDDDimESDVELDNSDVVEPDNEPPQPMGDPTAEVTDENRDD-AQSEKSKAMEAISDGR 120
Cdd:TIGR00990  65 SKPKISKKERRKRKQAEKETEGKTE--EKKSTAPKNAPVEPADELPEIDESSVANLSEEERKKyAAKLKEKGNKAYRNKD 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332619  121 FDEAIEHLTKAVMLNPtSAILYATRASVFLKVKKPNAAIRDANVALQFNSDSAKGYKSRGMAKAMLGQWEEAAADLHVAS 200
Cdd:TIGR00990 143 FNKAIKLYSKAIECKP-DPVYYSNRAACHNALGDWEKVVEDTTAALELDPDYSKALNRRANAYDGLGKYADALLDLTASC 221

                         170       180       190
                  ....*....|....*....|....*....|
gi 145332619  201 KLD--YDEEIGTMlkkVEPNAKRIEEHRRK 228
Cdd:TIGR00990 222 IIDgfRNEQSAQA---VERLLKKFAESKAK 248
 
Name Accession Description Interval E-value
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 285-367 1.10e-31

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: 114.96  E-value: 1.10e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332619 285 SRLLILYFTATWCGPCRYMSPLYSNLATQHSRVVFLKVDIDKANDVAASWNISSVPTFCFIRDGKEVDKVVGAD-KGSLE 363
Cdd:cd02947   10 AKPVVVDFWAPWCGPCKAIAPVLEELAEEYPKVKFVKVDVDENPELAEEYGVRSIPTFLFFKNGKEVDRVVGADpKEELE 89


                 ....
gi 145332619 364 QKIA 367
Cdd:cd02947   90 EFLE 93
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 289-369 9.90e-27

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: 102.21  E-value: 9.90e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332619 289 ILYFTATWCGPCRYMSPLYSNLATQHS-RVVFLKVDIDKANDVAASWNISSVPTFCFIRDGKEVDKVVGA-DKGSLEQKI 366
Cdd:COG3118   22 LVDFWAPWCGPCKMLAPVLEELAAEYGgKVKFVKVDVDENPELAAQFGVRSIPTLLLFKDGQPVDRFVGAlPKEQLREFL 101


                 ...
gi 145332619 367 AQH 369
Cdd:COG3118  102 DKV 104
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 285-367 7.65e-24

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: 94.61  E-value: 7.65e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332619  285 SRLLILYFTATWCGPCRYMSPLYSNLATQHS-RVVFLKVDIDKANDVAASWNISSVPTFCFIRDGKEVDKVVGA-DKGSL 362
Cdd:pfam00085  18 SKPVLVDFYAPWCGPCKMLAPEYEELAQEYKgNVVFAKVDVDENPDLASKYGVRGYPTLIFFKNGQPVDDYVGArPKDAL 97


                  ....*
gi 145332619  363 EQKIA 367
Cdd:pfam00085  98 AAFLK 102
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 286-369 1.22e-23

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: 93.89  E-value: 1.22e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332619  286 RLLILYFTATWCGPCRYMSPLYSNLATQ-HSRVVFLKVDIDKANDVAASWNISSVPTFCFIRDGKEVDKVVGA-DKGSLE 363
Cdd:TIGR01068  15 KPVLVDFWAPWCGPCKMIAPILEELAKEyEGKVKFVKLNVDENPDIAAKYGIRSIPTLLLFKNGKEVDRSVGAlPKAALK 94


                  ....*.
gi 145332619  364 QKIAQH 369
Cdd:TIGR01068  95 QLINKN 100
PTZ00051 PTZ00051
thioredoxin; Provisional
 287-364 3.14e-21

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 87.24  E-value: 3.14e-21
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145332619 287 LLILYFTATWCGPCRYMSPLYSNLATQHSRVVFLKVDIDKANDVAASWNISSVPTFCFIRDGKEVDKVVGADKGSLEQ 364
Cdd:PTZ00051  20 LVIVDFYAEWCGPCKRIAPFYEECSKEYTKMVFVKVDVDELSEVAEKENITSMPTFKVFKNGSVVDTLLGANDEALKQ 97
TRX_PICOT cd02984
TRX domain, PICOT (for PKC-interacting cousin of TRX) subfamily; PICOT is a protein that ...
 285-367 1.22e-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: 82.70  E-value: 1.22e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332619 285 SRLLILYFTATWCGPCRYMSPLYSNLATQ-HSRVVFLKVDIDKANDVAASWNISSVPTFCFIRDGKEVDKVVGADKGSLE 363
Cdd:cd02984   14 SKLLVLHFWAPWAEPCKQMNQVFEELAKEaFPSVLFLSIEAEELPEISEKFEITAVPTFVFFRNGTIVDRVSGADPKELA 93


                 ....
gi 145332619 364 QKIA 367
Cdd:cd02984   94 KKVE 97
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 286-369 1.32e-16

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 75.88  E-value: 1.32e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332619 286 RLLILYFTATWCGPCRYMSPLYSNLATQHSRVVFLKVDI----------------------DKANDVAASWNISSVPTFC 343
Cdd:COG0526   29 KPVLVNFWATWCPPCRAEMPVLKELAEEYGGVVFVGVDVdenpeavkaflkelglpypvllDPDGELAKAYGVRGIPTTV 108

                         90       100
                 ....*....|....*....|....*...
gi 145332619 344 FI-RDGKEVDKVVGA-DKGSLEQKIAQH 369
Cdd:COG0526  109 LIdKDGKIVARHVGPlSPEELEEALEKL 136
Hip_N cd14438
N-terminal dimerization domain of the Hsp70-interacting protein (Hip) and similar proteins; ...
 6-44 3.16e-15

N-terminal dimerization domain of the Hsp70-interacting protein (Hip) and similar proteins; The Hsc70/Hsp70-interacting protein (Hip, also p48 or suppressor of tumorigenicity ST13) functions as a regulator of the cyclic action of Hsp70. Hip forms homodimers, and this model characterizes the N-terminal dimerization domain, which may not be directly involved in its regulatory function. A central domain of Hip that contains TPR repeats binds the ATPase domain of Hsp70 and slows the release of ADP.


Pssm-ID: 271228  Cd Length: 41  Bit Score: 68.73  E-value: 3.16e-15
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 145332619   6 QVAELRRFVEQLKLNPSILHDPSLVFFKEYLRSLGAQVP 44
Cdd:cd14438    3 KLKELKAFVELCKQNPSILHTPELSFFKEYLESLGAKIP 41
HipN pfam18253
Hsp70-interacting protein N N-terminal domain; This is the N-terminal domain, known as HipN, ...
 3-44 4.51e-14

Hsp70-interacting protein N N-terminal domain; This is the N-terminal domain, known as HipN, found in Hsp70-interacting protein (Hip) present in Rattus norvegicus. Hip cooperates with the chaperone Hsp70 in protein folding and prevention of aggregation and may delay substrate release by slowing ADP dissociation from Hsp70. HipN is responsible for N-terminal homo-dimerization which is necessary so that the Hip dimer can interact with Hsp70 molecules.


Pssm-ID: 408069  Cd Length: 42  Bit Score: 65.76  E-value: 4.51e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 145332619    3 DAIQVAELRRFVEQLKLNPSILHDPSLVFFKEYLRSLGAQVP 44
Cdd:pfam18253   1 DPAHLSLLKQFVDLCKANPSILHLPELAFFKEFLESLGATVP 42
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
101-260 8.98e-14

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 70.42  E-value: 8.98e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332619 101 NRDDAQSEKSKAMEAISDGRFDEAIEHLTKAVMLNPTSAILYATRASVFLKVKKPNAAIRDANVALQFNSDSAKGYKSRG 180
Cdd:COG0457   72 DPDDAEALNNLGLALQALGRYEEALEDYDKALELDPDDAEALYNLGLALLELGRYDEAIEAYERALELDPDDADALYNLG 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332619 181 MAKAMLGQWEEAAADLHVASKLDYDEEIGTMLKKVEPNAKRIEEHRRKYQRLRKEKELQRAERERRKQQEAQEREAQAAL 260
Cdd:COG0457  152 IALEKLGRYEEALELLEKLEAAALAALLAAALGEAALALAAAEVLLALLLALEQALRKKLAILTLAALAELLLLALALLL 231
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
101-258 1.85e-13

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


Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 69.17  E-value: 1.85e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332619 101 NRDDAQSEKSKAMEAISDGRFDEAIEHLTKAVMLNPTSAILYATRASVFLKVKKPNAAIRDANVALQFNSDSAKGYKSRG 180
Cdd:COG4785   69 LPDLAQLYYERGVAYDSLGDYDLAIADFDQALELDPDLAEAYNNRGLAYLLLGDYDAALEDFDRALELDPDYAYAYLNRG 148

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145332619 181 MAKAMLGQWEEAAADLHVASKLDYDeeigtmlkkvepNAKRIEEHRRKYQRLRKEKELQRAERERRKQQEAQEREAQA 258
Cdd:COG4785  149 IALYYLGRYELAIADLEKALELDPN------------DPERALWLYLAERKLDPEKALALLLEDWATAYLLQGDTEEA 214
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
101-205 1.92e-12

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 66.57  E-value: 1.92e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332619 101 NRDDAQSEKSKAMEAISDGRFDEAIEHLTKAVMLNPTSAILYATRASVFLKVKKPNAAIRDANVALQFNSDSAKGYKSRG 180
Cdd:COG0457    4 DPDDAEAYNNLGLAYRRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPDDAEALNNLG 83

                         90       100
                 ....*....|....*....|....*
gi 145332619 181 MAKAMLGQWEEAAADLHVASKLDYD 205
Cdd:COG0457   84 LALQALGRYEEALEDYDKALELDPD 108
PLN03088 PLN03088
SGT1, suppressor of G2 allele of SKP1; Provisional
 110-206 5.12e-12

SGT1, suppressor of G2 allele of SKP1; Provisional


Pssm-ID: 215568 [Multi-domain]  Cd Length: 356  Bit Score: 66.35  E-value: 5.12e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332619 110 SKAMEAISDGRFDEAIEHLTKAVMLNPTSAILYATRASVFLKVKKPNAAIRDANVALQFNSDSAKGYKSRGMAKAMLGQW 189
Cdd:PLN03088   7 DKAKEAFVDDDFALAVDLYTQAIDLDPNNAELYADRAQANIKLGNFTEAVADANKAIELDPSLAKAYLRKGTACMKLEEY 86

                         90
                 ....*....|....*..
gi 145332619 190 EEAAADLHVASKLDYDE 206
Cdd:PLN03088  87 QTAKAALEKGASLAPGD 103
PDI_a_family cd02961
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ...
 285-350 9.36e-12

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: 61.09  E-value: 9.36e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 145332619 285 SRLLILYFTATWCGPCRYMSPLYSNLATQ---HSRVVFLKVDIDKANDVAASWNISSVPTFCFIRDGKE 350
Cdd:cd02961   15 SKDVLVEFYAPWCGHCKALAPEYEKLAKElkgDGKVVVAKVDCTANNDLCSEYGVRGYPTIKLFPNGSK 83
TlpA_like_ScsD_MtbDsbE cd03011
TlpA-like family, suppressor for copper sensitivity D protein (ScsD) and actinobacterial DsbE ...
 289-356 6.96e-11

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: 59.23  E-value: 6.96e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332619 289 ILYFTATWCGPCRYMSPLYSNLAtQHSRVV--------------FLK---VDIDKAND----VAASWNISSVPTFCFIRD 347
Cdd:cd03011   24 LVYFWATWCPVCRFTSPTVNQLA-ADYPVVsvalrsgddgavarFMQkkgYGFPVINDpdgvISARWGVSVTPAIVIVDP 102


                 ....*....
gi 145332619 348 GKEVDKVVG 356
Cdd:cd03011  103 GGIVFVTTG 111
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 96-206 1.25e-10

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: 59.05  E-value: 1.25e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332619  96 EVTDENRDDAQSEKSKAMEAISDGRFDEAIEHLTKAVMLNPTSAILYATRASVFLKVKKPNAAIRDANVALQFNSDSAKG 175
Cdd:COG4783   29 KALELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNLGLALLKAGDYDEALALLEKALKLDPEHPEA 108

                         90       100       110
                 ....*....|....*....|....*....|.
gi 145332619 176 YKSRGMAKAMLGQWEEAAADLHVASKLDYDE 206
Cdd:COG4783  109 YLRLARAYRALGRPDEAIAALEKALELDPDD 139
PRK10996 PRK10996
thioredoxin 2; Provisional
 292-357 1.31e-10

thioredoxin 2; Provisional


Pssm-ID: 182889 [Multi-domain]  Cd Length: 139  Bit Score: 58.93  E-value: 1.31e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 145332619 292 FTATWCGPCRYMSPLYSNLATQHS-RVVFLKVDIDKANDVAASWNISSVPTFCFIRDGKEVDKVVGA 357
Cdd:PRK10996  59 FWAPWCGPCRNFAPIFEDVAAERSgKVRFVKVNTEAERELSARFRIRSIPTIMIFKNGQVVDMLNGA 125
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 119-231 1.71e-10

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 62.32  E-value: 1.71e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332619 119 GRFDEAIEHLTKAVMLNPTSAILYATRASVFLKVKKPNAAIRDANVALQFNSDSAKGYKSRGMAKAMLGQWEEAAADLHV 198
Cdd:COG3914   92 GRYEEALALYRRALALNPDNAEALFNLGNLLLALGRLEEALAALRRALALNPDFAEAYLNLGEALRRLGRLEEAIAALRR 171

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 145332619 199 ASKLDYDE-----EIGTMLKKvepnAKRIEEHRRKYQR 231
Cdd:COG3914  172 ALELDPDNaealnNLGNALQD----LGRLEEAIAAYRR 205
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 104-236 3.15e-10

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: 57.89  E-value: 3.15e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332619 104 DAQSEKSKAMEAISDGRFDEAIEHLTKAVMLNPTSAILYATRASVFLKVKKPNAAIRDANVALQFNSDSAKGYKSRGMAK 183
Cdd:COG4783    3 CAEALYALAQALLLAGDYDEAEALLEKALELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNLGLAL 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 145332619 184 AMLGQWEEAAADLHVASKLD-YDEEIGTMLKKVEPNAKRIEEHRRKYQRLRKEK 236
Cdd:COG4783   83 LKAGDYDEALALLEKALKLDpEHPEAYLRLARAYRALGRPDEAIAALEKALELD 136
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 119-203 9.09e-10

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: 56.89  E-value: 9.09e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332619 119 GRFDEAIEHLTKAVMLNPTSAILYATRASVFLKVKKPNAAIRDANVALQFNSDSAKGYKSRGMAKAMLGQWEEAAADLHV 198
Cdd:COG5010   68 GDFEESLALLEQALQLDPNNPELYYNLALLYSRSGDKDEAKEYYEKALALSPDNPNAYSNLAALLLSLGQDDEAKAALQR 147


                 ....*
gi 145332619 199 ASKLD 203
Cdd:COG5010  148 ALGTS 152
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 119-203 2.80e-09

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 58.47  E-value: 2.80e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332619 119 GRFDEAIEHLTKAVMLNPTSAILYATRASVFLKVKKPNAAIRDANVALQFNSDSAKGYKSRGMAKAMLGQWEEAAADLHV 198
Cdd:COG3914  126 GRLEEALAALRRALALNPDFAEAYLNLGEALRRLGRLEEAIAALRRALELDPDNAEALNNLGNALQDLGRLEEAIAAYRR 205


                 ....*
gi 145332619 199 ASKLD 203
Cdd:COG3914  206 ALELD 210
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 286-356 5.94e-09

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: 53.39  E-value: 5.94e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332619 286 RLLILYFTATWCGPCRYMSPLYSNLATQHS--RVVFLKVDI-----------------------DKANDVAASWNISSVP 340
Cdd:cd02966   20 KVVLVNFWASWCPPCRAEMPELEALAKEYKddGVEVVGVNVddddpaavkaflkkygitfpvllDPDGELAKAYGVRGLP 99

                         90
                 ....*....|....*..
gi 145332619 341 TFCFI-RDGKEVDKVVG 356
Cdd:cd02966  100 TTFLIdRDGRIRARHVG 116
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 119-196 6.70e-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: 53.86  E-value: 6.70e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145332619 119 GRFDEAIEHLTKAVMLNPTSAILYATRASVFLKVKKPNAAIRDANVALQFNSDSAKGYKSRGMAKAMLGQWEEAAADL 196
Cdd:COG4235   31 GRYDEALAAYEKALRLDPDNADALLDLAEALLAAGDTEEAEELLERALALDPDNPEALYLLGLAAFQQGDYAEAIAAW 108
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 96-259 6.97e-09

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: 56.28  E-value: 6.97e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332619  96 EVTDENRDDAQSEKSKAMEAISDGRFDEAIEHLTKAVMLNPTSAILYATRASVFLKVKKPNAAIRDANVALQFNSDSAKG 175
Cdd:COG2956  101 KLLELDPDDAEALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKALKLDPDCARA 180

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332619 176 YKSRGMAKAMLGQWEEAAADLHVASKLDYD-EEIGTMLKKVEPNAKRIEEHRRKYQRLRKEKELQRAERERRKQQEAQER 254
Cdd:COG2956  181 LLLLAELYLEQGDYEEAIAALERALEQDPDyLPALPRLAELYEKLGDPEEALELLRKALELDPSDDLLLALADLLERKEG 260


                 ....*
gi 145332619 255 EAQAA 259
Cdd:COG2956  261 LEAAL 265
ybbN cd02956
ybbN protein family; ybbN is a hypothetical protein containing a redox-inactive TRX-like ...
 288-357 1.46e-08

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: 51.89  E-value: 1.46e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 145332619 288 LILYFTATWCGPCRYMSPLYSNLATQHS-RVVFLKVDIDKANDVAASWNISSVPTFCFIRDGKEVDKVVGA 357
Cdd:cd02956   15 VVVDFWAPRSPPSKELLPLLERLAEEYQgQFVLAKVNCDAQPQIAQQFGVQALPTVYLFAAGQPVDGFQGA 85
NlpI COG4785
Lipoprotein NlpI, contains TPR repeats [Cell wall/membrane/envelope biogenesis];
92-203 1.66e-08

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


Pssm-ID: 443815 [Multi-domain]  Cd Length: 223  Bit Score: 54.54  E-value: 1.66e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332619  92 DPTAEVTDENRDDAQSEkskAMEAISDGRFDEAIEHLTKAVMLNPTSAILYATRASVFLKVKKPNAAIRDANVALQFNSD 171
Cdd:COG4785   29 LLFAAVLALAIALADLA---LALAAAALAAAALAAERIDRALALPDLAQLYYERGVAYDSLGDYDLAIADFDQALELDPD 105

                         90       100       110
                 ....*....|....*....|....*....|..
gi 145332619 172 SAKGYKSRGMAKAMLGQWEEAAADLHVASKLD 203
Cdd:COG4785  106 LAEAYNNRGLAYLLLGDYDAALEDFDRALELD 137
TRX_NTR cd02949
TRX domain, novel NADPH thioredoxin reductase (NTR) family; composed of fusion proteins found ...
 286-356 2.46e-08

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: 51.35  E-value: 2.46e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 145332619 286 RLLILYFTATWCGPCRYMSPLYSNLATQHS-RVVFLKVDIDKANDVAASWNISSVPTFCFIRDGKEVDKVVG 356
Cdd:cd02949   14 RLILVLYTSPTCGPCRTLKPILNKVIDEFDgAVHFVEIDIDEDQEIAEAAGIMGTPTVQFFKDKELVKEISG 85
3a0801s09 TIGR00990
mitochondrial precursor proteins import receptor (72 kDa mitochondrial outermembrane protein) ...
 42-228 3.18e-08

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: 55.38  E-value: 3.18e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332619   42 QVPKIEKTAETKPSFSPKHDDDDDDimESDVELDNSDVVEPDNEPPQPMGDPTAEVTDENRDD-AQSEKSKAMEAISDGR 120
Cdd:TIGR00990  65 SKPKISKKERRKRKQAEKETEGKTE--EKKSTAPKNAPVEPADELPEIDESSVANLSEEERKKyAAKLKEKGNKAYRNKD 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332619  121 FDEAIEHLTKAVMLNPtSAILYATRASVFLKVKKPNAAIRDANVALQFNSDSAKGYKSRGMAKAMLGQWEEAAADLHVAS 200
Cdd:TIGR00990 143 FNKAIKLYSKAIECKP-DPVYYSNRAACHNALGDWEKVVEDTTAALELDPDYSKALNRRANAYDGLGKYADALLDLTASC 221

                         170       180       190
                  ....*....|....*....|....*....|
gi 145332619  201 KLD--YDEEIGTMlkkVEPNAKRIEEHRRK 228
Cdd:TIGR00990 222 IIDgfRNEQSAQA---VERLLKKFAESKAK 248
PilF COG3063
Type IV pilus assembly protein PilF/PilW [Cell motility, Extracellular structures];
119-205 5.71e-08

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


Pssm-ID: 442297 [Multi-domain]  Cd Length: 94  Bit Score: 50.17  E-value: 5.71e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332619 119 GRFDEAIEHLTKAVMLNPTSAILYATRASVFLKVKKPNAAIRdANVALQFNSDSAKGYKSRGMAKAMLGQWEEAAADLHV 198
Cdd:COG3063    6 GDLEEAEEYYEKALELDPDNADALNNLGLLLLEQGRYDEAIA-LEKALKLDPNNAEALLNLAELLLELGDYDEALAYLER 84


                 ....*..
gi 145332619 199 ASKLDYD 205
Cdd:COG3063   85 ALELDPS 91
trxA PRK09381
thioredoxin TrxA;
287-364 6.93e-08

thioredoxin TrxA;


Pssm-ID: 181812 [Multi-domain]  Cd Length: 109  Bit Score: 50.45  E-value: 6.93e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332619 287 LLILYFTATWCGPCRYMSPLYSNLATQHS-RVVFLKVDIDKANDVAASWNISSVPTFCFIRDGKEVDKVVGA-DKGSLEQ 364
Cdd:PRK09381  23 AILVDFWAEWCGPCKMIAPILDEIADEYQgKLTVAKLNIDQNPGTAPKYGIRGIPTLLLFKNGEVAATKVGAlSKGQLKE 102
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 96-232 7.36e-08

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: 53.19  E-value: 7.36e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332619  96 EVTDENRDDAQSEKSKAMEAISDGRFDEAIEHLTKAVMLNPTSAILYATRASVFLKVKKPNAAIRDANVALQFNSDSAKG 175
Cdd:COG2956  135 RLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKALKLDPDCARALLLLAELYLEQGDYEEAIAALERALEQDPDYLPA 214

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 145332619 176 YKSRGMAKAMLGQWEEAAADLHVASKLDYDEEIGTMLKKVEPNAKRIEEHRRKYQRL 232
Cdd:COG2956  215 LPRLAELYEKLGDPEEALELLRKALELDPSDDLLLALADLLERKEGLEAALALLERQ 271
TRX_CDSP32 cd02985
TRX family, chloroplastic drought-induced stress protein of 32 kD (CDSP32); CDSP32 is composed ...
 285-362 8.21e-08

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: 49.79  E-value: 8.21e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332619 285 SRLLILYFTATWCGPCRYMSPLYSNLATQHSRVVFLKV---DIDKANDVAASWNISSVPTFCFIRDGKEVDKVVGADKGS 361
Cdd:cd02985   15 GRLVVLEFALKHSGPSVKIYPTMVKLSRTCNDVVFLLVngdENDSTMELCRREKIIEVPHFLFYKDGEKIHEEEGIGPDE 94


                 .
gi 145332619 362 L 362
Cdd:cd02985   95 L 95
PDI_a_ERp38 cd02998
PDIa family, endoplasmic reticulum protein 38 (ERp38) subfamily; composed of proteins similar ...
 292-350 9.82e-08

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: 49.56  E-value: 9.82e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 145332619 292 FTATWCGPCRYMSPLYSNLAT---QHSRVVFLKVDIDKAN-DVAASWNISSVPTFCFIRDGKE 350
Cdd:cd02998   25 FYAPWCGHCKNLAPEYEKLAAvfaNEDDVVIAKVDADEANkDLAKKYGVSGFPTLKFFPKGST 87
TMX2 cd02962
TMX2 family; composed of proteins similar to human TMX2, a 372-amino acid TRX-related ...
 286-353 1.19e-07

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: 50.46  E-value: 1.19e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145332619 286 RLLILYFTATWCGPCRYMSPLYSNLAT--QHSRVVFLKVDIDKANDVAASWNISS------VPTFCFIRDGKEVDK 353
Cdd:cd02962   48 VTWLVEFFTTWSPECVNFAPVFAELSLkyNNNNLKFGKIDIGRFPNVAEKFRVSTsplskqLPTIILFQGGKEVAR 123
TRX_superfamily cd01659
Thioredoxin (TRX) superfamily; a large, diverse group of proteins containing a TRX-fold. Many ...
 289-355 2.40e-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: 47.69  E-value: 2.40e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332619 289 ILYFTATWCGPCRYMSPLYSNLATQHSRVVFLKVDIDKANDVAASW---NISSVPTFcFIRDGKEVDKVV 355
Cdd:cd01659    1 LVLFYAPWCPFCQALRPVLAELALLNKGVKFEAVDVDEDPALEKELkryGVGGVPTL-VVFGPGIGVKYG 69
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 287-352 3.37e-07

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 52.06  E-value: 3.37e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332619 287 LLILYFTATWCGPCRYMSPLYSN----LATQHSRVVFLKVDIDKANDVAASWNISSVPTFCFIRDGKEVD 352
Cdd:PTZ00102  51 IVLVKFYAPWCGHCKRLAPEYKKaakmLKEKKSEIVLASVDATEEMELAQEFGVRGYPTIKFFNKGNPVN 120
Phd_like_TxnDC9 cd02989
Phosducin (Phd)-like family, Thioredoxin (TRX) domain containing protein 9 (TxnDC9) subfamily; ...
 299-359 3.97e-07

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: 48.34  E-value: 3.97e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 145332619 299 PCRYMSPLYSNLATQHSRVVFLKVDIDKANDVAASWNISSVPTFCFIRDGKEVDKVVGADK 359
Cdd:cd02989   36 RCKIMDKHLEILAKKHLETKFIKVNAEKAPFLVEKLNIKVLPTVILFKNGKTVDRIVGFEE 96
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
134-205 6.07e-07

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 50.01  E-value: 6.07e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 145332619 134 LNPTSAILYATRASVFLKVKKPNAAIRDANVALQFNSDSAKGYKSRGMAKAMLGQWEEAAADLHVASKLDYD 205
Cdd:COG0457    3 LDPDDAEAYNNLGLAYRRLGRYEEAIEDYEKALELDPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPD 74
SoxW COG2143
Thioredoxin-related protein SoxW [Posttranslational modification, protein turnover, chaperones] ...
 286-359 6.10e-07

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


Pssm-ID: 441746 [Multi-domain]  Cd Length: 146  Bit Score: 48.36  E-value: 6.10e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332619 286 RLLILYFTATWCGPCRYM------SPLYSNLATQHsrVVFLKVDIDKANDV-------------AASWNISSVPTFCFI- 345
Cdd:COG2143   41 KPILLFFESDWCPYCKKLhkevfsDPEVAAYLKEN--FVVVQLDAEGDKEVtdfdgetltekelARKYGVRGTPTLVFFd 118

                         90
                 ....*....|....
gi 145332619 346 RDGKEVDKVVGADK 359
Cdd:COG2143  119 AEGKEIARIPGYLK 132
PDI_a_PDI_a'_C cd02995
PDIa family, C-terminal TRX domain (a') subfamily; composed of the C-terminal redox active a' ...
 288-363 2.20e-06

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: 45.63  E-value: 2.20e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 145332619 288 LILYFtATWCGPCRYMSPLYSNLAT---QHSRVVFLKVDIDkANDVAASWNISSVPTFCFIRDGKEVDKVVGADKGSLE 363
Cdd:cd02995   22 LVEFY-APWCGHCKALAPIYEELAEklkGDDNVVIAKMDAT-ANDVPSEFVVDGFPTILFFPAGDKSNPIKYEGDRTLE 98
PDI_a_PDIR cd02997
PDIa family, PDIR subfamily; composed of proteins similar to human PDIR (for Protein Disulfide ...
 292-366 2.39e-06

PDIa family, PDIR subfamily; composed of proteins similar to human PDIR (for Protein Disulfide Isomerase Related). PDIR is composed of three redox active TRX (a) domains and an N-terminal redox inactive TRX-like (b) domain. Similar to PDI, it is involved in oxidative protein folding in the endoplasmic reticulum (ER) through its isomerase and chaperone activities. These activities are lower compared to PDI, probably due to PDIR acting only on a subset of proteins. PDIR is preferentially expressed in cells actively secreting proteins and its expression is induced by stress. Similar to PDI, the isomerase and chaperone activities of PDIR are independent; CXXC mutants lacking isomerase activity retain chaperone activity.


Pssm-ID: 239295 [Multi-domain]  Cd Length: 104  Bit Score: 45.77  E-value: 2.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332619 292 FTATWCGPCRYMSPLYSNLAT---QHSRVVFLKVDIDKAND--VAASWNISSVPTFCFIRDGKEVDKVvgaDKGSLEQKI 366
Cdd:cd02997   24 FYAPWCGHCKKMKPEFTKAATelkEDGKGVLAAVDCTKPEHdaLKEEYNVKGFPTFKYFENGKFVEKY---EGERTAEDI 100
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 99-259 3.08e-06

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: 48.19  E-value: 3.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332619  99 DENRDDAQSEKskAMEAISDGRFDEAIEHLTKAVMLNPTSAILYATRASVFLKVKKPNAAIRDANVALQFNSDSAKGYKS 178
Cdd:COG2956   72 DPDRAEALLEL--AQDYLKAGLLDRAEELLEKLLELDPDDAEALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCE 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332619 179 RGMAKAMLGQWEEAAADLHVASKLD-YDEEIGTMLKKVEPNAKRIEEHRRKYQR-LRKEKELQRAERERRKQQEAQEREA 256
Cdd:COG2956  150 LAELYLEQGDYDEAIEALEKALKLDpDCARALLLLAELYLEQGDYEEAIAALERaLEQDPDYLPALPRLAELYEKLGDPE 229


                 ...
gi 145332619 257 QAA 259
Cdd:COG2956  230 EAL 232
PDI_a_ERp46 cd03005
PDIa family, endoplasmic reticulum protein 46 (ERp46) subfamily; ERp46 is an ER-resident ...
 292-357 4.40e-06

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: 44.97  E-value: 4.40e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332619 292 FTATWCGPCRYMSPLYSNLA----TQHSRVVFLKVDIDKANDVAASWNISSVPTFCFIRDGKEVDKVVGA 357
Cdd:cd03005   23 FFAPWCGHCKRLAPTWEQLAkkfnNENPSVKIAKVDCTQHRELCSEFQVRGYPTLLLFKDGEKVDKYKGT 92
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 119-207 6.16e-06

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 48.07  E-value: 6.16e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332619 119 GRFDEAIEHLTKAVMLNPTSAILYATRASVFLKVKKPNAAIRDANVALQFNSDSAKGYKSRGMAKAMLGQWEEAAADLHV 198
Cdd:COG3914  160 GRLEEAIAALRRALELDPDNAEALNNLGNALQDLGRLEEAIAAYRRALELDPDNADAHSNLLFALRQACDWEVYDRFEEL 239


                 ....*....
gi 145332619 199 ASKLDYDEE 207
Cdd:COG3914  240 LAALARGPS 248
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 119-258 8.36e-06

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: 47.03  E-value: 8.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332619 119 GRFDEAIEHLTKAVMLNPTSAILYATRASVFLKVKKPNAAIRDANVALQFNSDSAKGYKSRGMAKAMLGQWEEAAADLHV 198
Cdd:COG2956   56 GEYDRAIRIHQKLLERDPDRAEALLELAQDYLKAGLLDRAEELLEKLLELDPDDAEALRLLAEIYEQEGDWEKAIEVLER 135

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 145332619 199 ASKLD-YDEEIGTMLKKVEPNAKRIEEHRRKYQR-LRKEKELQRAERERRKQQEAQEREAQA 258
Cdd:COG2956  136 LLKLGpENAHAYCELAELYLEQGDYDEAIEALEKaLKLDPDCARALLLLAELYLEQGDYEEA 197
3a0801s09 TIGR00990
mitochondrial precursor proteins import receptor (72 kDa mitochondrial outermembrane protein) ...
 119-205 1.34e-05

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: 46.90  E-value: 1.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332619  119 GRFDEAIEHLTKAVMLNPTSAILYATRASVFLKVKKPNAAIRDANVALQFNSDSAKGYKSRGMAKAMLGQWEEAAADLHV 198
Cdd:TIGR00990 345 GKHLEALADLSKSIELDPRVTQSYIKRASMNLELGDPDKAEEDFDKALKLNSEDPDIYYHRAQLHFIKGEFAQAGKDYQK 424


                  ....*..
gi 145332619  199 ASKLDYD 205
Cdd:TIGR00990 425 SIDLDPD 431
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
288-368 1.66e-05

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 44.09  E-value: 1.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332619 288 LILYFTATWCGPCRYMSP----LYSNLATQHSRVVFLKVD-------------------IDKANDVAASWNISSVPTFcF 344
Cdd:COG1225   24 VVLYFYATWCPGCTAELPelrdLYEEFKDKGVEVLGVSSDsdeahkkfaekyglpfpllSDPDGEVAKAYGVRGTPTT-F 102

                         90       100
                 ....*....|....*....|....*...
gi 145332619 345 I--RDGKEVDKVVGA--DKGSLEQKIAQ 368
Cdd:COG1225  103 LidPDGKIRYVWVGPvdPRPHLEEVLEA 130
TRX_NDPK cd02948
TRX domain, TRX and NDP-kinase (NDPK) fusion protein family; most members of this group are ...
 287-369 2.10e-05

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: 43.09  E-value: 2.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332619 287 LLILYFTATWCGPCRYMSPLysnlatqhsrvvFLKVDIDKAND-----VAASWNISSV--------PTFCFIRDGKEVDK 353
Cdd:cd02948   19 LTVVDVYQEWCGPCKAVVSL------------FKKIKNELGDDllhfaTAEADTIDTLkryrgkcePTFLFYKNGELVAV 86

                         90
                 ....*....|....*.
gi 145332619 354 VVGADKGSLEQKIAQH 369
Cdd:cd02948   87 IRGANAPLLNKTITEL 102
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 103-205 2.13e-05

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: 46.62  E-value: 2.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332619  103 DDAQSEKSKAMEAISDGRFDEAIEHLTKAVMLNPTSAILYATRASVFLKVKKPNAAIRDANVALQFNSDSAKGYKSRGMA 182
Cdd:TIGR02917 327 NSHQARRLLASIQLRLGRVDEAIATLSPALGLDPDDPAALSLLGEAYLALGDFEKAAEYLAKATELDPENAAARTQLGIS 406

                          90       100
                  ....*....|....*....|...
gi 145332619  183 KAMLGQWEEAAADLHVASKLDYD 205
Cdd:TIGR02917 407 KLSQGDPSEAIADLETAAQLDPE 429
PDI_a_MPD1_like cd03002
PDI family, MPD1-like subfamily; composed of eukaryotic proteins similar to Saccharomyces ...
 289-353 4.04e-05

PDI family, MPD1-like subfamily; composed of eukaryotic proteins similar to Saccharomyces cerevisiae MPD1 protein, which contains a single redox active TRX domain located at the N-terminus, and an ER retention signal at the C-terminus indicative of an ER-resident protein. MPD1 has been shown to suppress the maturation defect of carboxypeptidase Y caused by deletion of the yeast PDI1 gene. Other characterized members of this subfamily include the Aspergillus niger prpA protein and Giardia PDI-1. PrpA is non-essential to strain viability, however, its transcript level is induced by heterologous protein expression suggesting a possible role in oxidative protein folding during high protein production. Giardia PDI-1 has the ability to refold scrambled RNase and exhibits transglutaminase activity.


Pssm-ID: 239300 [Multi-domain]  Cd Length: 109  Bit Score: 42.35  E-value: 4.04e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145332619 289 ILYFTATWCGPCRYMSPLYSNLATQ-HSRVVFLKVDIDKAN--DVAASWNISSVPTFCFIRDGKEVDK 353
Cdd:cd03002   22 LVEFYAPWCGHCKNLKPEYAKAAKElDGLVQVAAVDCDEDKnkPLCGKYGVQGFPTLKVFRPPKKASK 89
PDI_a_ERp44 cd02996
PDIa family, endoplasmic reticulum protein 44 (ERp44) subfamily; ERp44 is an ER-resident ...
 285-348 4.11e-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: 42.38  E-value: 4.11e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 145332619 285 SRLLILYFTATWCGPCRYMSPLYSNLAT-------QHSRVVFLKVDIDKANDVAASWNISSVPTFCFIRDG 348
Cdd:cd02996   18 AELVLVNFYADWCRFSQMLHPIFEEAAAkikeefpDAGKVVWGKVDCDKESDIADRYRINKYPTLKLFRNG 88
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 111-265 5.28e-05

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: 44.33  E-value: 5.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332619 111 KAMEAISDGRFDEAIEHLTKAVMLNPTSAILYATRASVFLKVKKPNAAIRDANVALQFNSDSAKGYKSRGMAKAMLGQWE 190
Cdd:COG2956   14 KGLNYLLNGQPDKAIDLLEEALELDPETVEAHLALGNLYRRRGEYDRAIRIHQKLLERDPDRAEALLELAQDYLKAGLLD 93

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 145332619 191 EAAADLHVASKLDydeeigtmlkkvepnAKRIEEHRRKYQRLRKEKELQRAERERRKQQEAQEREAQAALNDGEV 265
Cdd:COG2956   94 RAEELLEKLLELD---------------PDDAEALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAEL 153
DsbDgamma cd02953
DsbD gamma family; DsbD gamma is the C-terminal periplasmic domain of the bacterial protein ...
 289-355 1.51e-04

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: 40.66  E-value: 1.51e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 145332619 289 ILYFTATWCGPCRYMSPL-YSNLATQH---SRVVFLKVDIDKANDVAA----SWNISSVPTFCFIRDGKEVDKVV 355
Cdd:cd02953   15 FVDFTADWCVTCKVNEKVvFSDPEVQAalkKDVVLLRADWTKNDPEITallkRFGVFGPPTYLFYGPGGEPEPLR 89
Thioredoxin_2 pfam13098
Thioredoxin-like domain;
286-357 1.59e-04

Thioredoxin-like domain;


Pssm-ID: 379034 [Multi-domain]  Cd Length: 103  Bit Score: 40.49  E-value: 1.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332619  286 RLLILYFTATWCGPCRYM----SPLYSNLATQHSRVVFLKVDIDKANDVAASW-------------NISSVPTFCFIrDG 348
Cdd:pfam13098   5 KPVLVVFTDPDCPYCKKLkkelLEDPDVTVYLGPNFVFIAVNIWCAKEVAKAFtdilenkelgrkyGVRGTPTIVFF-DG 83

                          90
                  ....*....|
gi 145332619  349 K-EVDKVVGA 357
Cdd:pfam13098  84 KgELLRLPGY 93
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
119-239 1.76e-04

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 42.69  E-value: 1.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332619 119 GRFDEAIEHLTKAVMLNPTSAILYATRASVFLKVKKPNAAIRDANVALQFNSDSAKGYKSRGMAKAMLGQWEEAAADLHV 198
Cdd:COG0457  124 GRYDEAIEAYERALELDPDDADALYNLGIALEKLGRYEEALELLEKLEAAALAALLAAALGEAALALAAAEVLLALLLAL 203

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 145332619 199 ASKLDYDEEIGTMLKKVEPNAKRIEEHRRKYQRLRKEKELQ 239
Cdd:COG0457  204 EQALRKKLAILTLAALAELLLLALALLLALRLAALALYQYR 244
COG4700 COG4700
Uncharacterized conserved protein ECs_4300, contains TPR-like domain [Function unknown];
119-261 2.22e-04

Uncharacterized conserved protein ECs_4300, contains TPR-like domain [Function unknown];


Pssm-ID: 443735 [Multi-domain]  Cd Length: 249  Bit Score: 42.18  E-value: 2.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332619 119 GRFDEAIEH----LTKAVMLNPtsAILYaTRASVFLKVKKPNAAIRDANVALQFNSD--SAKGYKSRGMAKAMLGQWEEA 192
Cdd:COG4700  103 GRYDEAIELyeeaLTGIFADDP--HILL-GLAQALFELGRYAEALETLEKLIAKNPDfkSSDAHLLYARALEALGDLEAA 179

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 145332619 193 AADLHVASKL--DYDE--EIGTMLKKvepnAKRIEEHRRKYQRLRkeKELQRAERERRKQQEAQEREAQAALN 261
Cdd:COG4700  180 EAELEALARRysGPEAryRYAKFLAR----QGRTAEAKELLEEIL--DEAKHMPKHYRRLNREWIREAKKLLK 246
Phd_like cd02957
Phosducin (Phd)-like family; composed of Phd and Phd-like proteins (PhLP), characterized as ...
 300-356 2.41e-04

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: 40.23  E-value: 2.41e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 145332619 300 CRYMSPLYSNLATQHSRVVFLKVDIDKAnDVAASWNISSVPTFCFIRDGKEVDKVVG 356
Cdd:cd02957   39 CKILDSHLEELAAKYPETKFVKINAEKA-FLVNYLDIKVLPTLLVYKNGELIDNIVG 94
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 123-206 2.72e-04

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: 40.37  E-value: 2.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332619 123 EAIEHLTKAVMLNPTSAILYATRASVFLKVKKPNAAIRDANVALQFNSDSAKGYKSRGMAKAMLGQWEEAAADLHVASKL 202
Cdd:COG4235    1 EAIARLRQALAANPNDAEGWLLLGRAYLRLGRYDEALAAYEKALRLDPDNADALLDLAEALLAAGDTEEAEELLERALAL 80


                 ....
gi 145332619 203 DYDE 206
Cdd:COG4235   81 DPDN 84
OST3_OST6 pfam04756
OST3 / OST6 family, transporter family; The proteins in this family are part of a complex of ...
 288-345 3.05e-04

OST3 / OST6 family, transporter family; The proteins in this family are part of a complex of eight ER proteins that transfers core oligosaccharide from dolichol carrier to Asn-X-Ser/Thr motifs. This family includes both OST3 and OST6, each of which contains four predicted transmembrane helices. Disruption of OST3 and OST6 leads to a defect in the assembly of the complex. Hence, the function of these genes seems to be essential for recruiting a fully active complex necessary for efficient N-glycosylation. These proteins are also thought to be novel Mg2+ transporters.


Pssm-ID: 461420  Cd Length: 294  Bit Score: 42.23  E-value: 3.05e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332619  288 LILYFTATW----CGPCRYMSPLYSNLA--------TQHSRVVFLKVDIDKANDVAASWNISSVPTFCFI 345
Cdd:pfam04756  33 VVVLLTALDprfgCQLCREFQPEFELVAkswfkdhkAGSSKLFFATLDFDDGKDVFQSLGLQTAPHLLLF 102
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 292-349 3.14e-04

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: 42.35  E-value: 3.14e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 145332619  292 FTATWCGPCRYMSPLYSNLAT----QHSRVVFLKVDIDKANDVAASWNISSVPTFCFIRDGK 349
Cdd:TIGR01130  25 FYAPWCGHCKSLAPEYEKAADelkkKGPPIKLAKVDATEEKDLAQKYGVSGYPTLKIFRNGE 86
PTZ00443 PTZ00443
Thioredoxin domain-containing protein; Provisional
 292-349 4.88e-04

Thioredoxin domain-containing protein; Provisional


Pssm-ID: 185622 [Multi-domain]  Cd Length: 224  Bit Score: 41.15  E-value: 4.88e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 145332619 292 FTATWCGPCRYMSPLYSNLATQHSRVVFL-KVDIDKANDVAASWNISSVPTFCFIRDGK 349
Cdd:PTZ00443  59 FYAPWCSHCRKMAPAWERLAKALKGQVNVaDLDATRALNLAKRFAIKGYPTLLLFDKGK 117
TadD COG5010
Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking, secretion, ...
 103-239 1.20e-03

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: 39.17  E-value: 1.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332619 103 DDAQSEKSKAMEAISDGRFDEAIEHLTKAVMLNPTSAILYATRASVFLKVKKPNAAIRDANVALQFNSDSAKGYKSRGMA 182
Cdd:COG5010   18 TKLRTLVEKYEAALAGANNTKEDELAAAGRDKLAKAFAIESPSDNLYNKLGDFEESLALLEQALQLDPNNPELYYNLALL 97

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 145332619 183 KAMLGQWEEAAADLHVASKLD-YDEEIGTMLKKVEPNAKRIEEHRRKYQRLRKEKELQ 239
Cdd:COG5010   98 YSRSGDKDEAKEYYEKALALSpDNPNAYSNLAALLLSLGQDDEAKAALQRALGTSPLK 155
PRK03147 PRK03147
thiol-disulfide oxidoreductase ResA;
290-357 1.50e-03

thiol-disulfide oxidoreductase ResA;


Pssm-ID: 179545 [Multi-domain]  Cd Length: 173  Bit Score: 39.22  E-value: 1.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332619 290 LYFTATWCGPCR----YMSPLYSNLATQHSRVVFLKVD--------------------IDKANDVAASWNISSVPTFCFI 345
Cdd:PRK03147  66 LNFWGTWCKPCEkempYMNELYPKYKEKGVEIIAVNVDetelavknfvnrygltfpvaIDKGRQVIDAYGVGPLPTTFLI 145

                         90
                 ....*....|...
gi 145332619 346 -RDGKEVDKVVGA 357
Cdd:PRK03147 146 dKDGKVVKVITGE 158
PDI_a_ERdj5_C cd03004
PDIa family, C-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 292-341 2.27e-03

PDIa family, C-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a protein containing an N-terminal DnaJ domain and four redox active TRX domains. This subfamily is composed of the three TRX domains located at the C-terminal half of the protein. ERdj5 is a ubiquitous protein localized in the endoplasmic reticulum (ER) and is abundant in secretory cells. It's transcription is induced during ER stress. It interacts with BiP through its DnaJ domain in an ATP-dependent manner. BiP, an ER-resident member of the Hsp70 chaperone family, functions in ER-associated degradation and protein translocation. Also included in the alignment is the single complete TRX domain of an uncharacterized protein from Tetraodon nigroviridis, which also contains a DnaJ domain at its N-terminus.


Pssm-ID: 239302 [Multi-domain]  Cd Length: 104  Bit Score: 37.27  E-value: 2.27e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 145332619 292 FTATWCGPCRYMSPLYSNLATQHS-RVVFLKVDIDKANDVAASWNISSVPT 341
Cdd:cd03004   26 FYAPWCGPCQALLPELRKAARALKgKVKVGSVDCQKYESLCQQANIRAYPT 76
DsbD COG4232
Thiol:disulfide interchange protein DsbD [Posttranslational modification, protein turnover, ...
 286-354 3.12e-03

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


Pssm-ID: 443376 [Multi-domain]  Cd Length: 416  Bit Score: 39.40  E-value: 3.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332619 286 RLLILYFTATWCGPCRYM-------SPLYSNLAtqhSRVVFLKVDIDKANDVA----ASWNISSVPTFCFI-RDGKEVDK 353
Cdd:COG4232  321 KPVFVDFTADWCVTCKENertvfsdPEVQAALA---DDVVLLKADVTDNDPEItallKRFGRFGVPTYVFYdPDGEELPR 397


                 .
gi 145332619 354 V 354
Cdd:COG4232  398 L 398
PEP_TPR_lipo TIGR02917
putative PEP-CTERM system TPR-repeat lipoprotein; This protein family occurs in strictly ...
 111-203 3.24e-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: 3.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332619  111 KAMEAISDGRFDEAIEHLTKAVMLNPT--------SAILYATR--------------------------ASVFLKVKKPN 156
Cdd:TIGR02917 267 KALVDFQKKNYEDARETLQDALKSAPEylpalllaGASEYQLGnleqayqylnqilkyapnshqarrllASIQLRLGRVD 346

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 145332619  157 AAIRDANVALQFNSDSAKGYKSRGMAKAMLGQWEEAAADLHVASKLD 203
Cdd:TIGR02917 347 EAIATLSPALGLDPDDPAALSLLGEAYLALGDFEKAAEYLAKATELD 393
Thioredoxin_8 pfam13905
Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 286-351 3.81e-03

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: 36.52  E-value: 3.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332619  286 RLLILYFTATWCGPCRYMSPLYSNLATQHS-----RVVFLKVDID-----------------------KANDVAASWNIS 337
Cdd:pfam13905   2 KVVLLYFGASWCKPCRRFTPLLKELYEKLKkkknvEIVFVSLDRDleefkdylkkmpkdwlsvpfdddERNELKRKYGVN 81

                          90
                  ....*....|....
gi 145332619  338 SVPTFCFIRDGKEV 351
Cdd:pfam13905  82 AIPTLVLLDPNGEV 95
PRK14552 PRK14552
C/D box methylation guide ribonucleoprotein complex aNOP56 subunit; Provisional
 193-249 4.97e-03

C/D box methylation guide ribonucleoprotein complex aNOP56 subunit; Provisional


Pssm-ID: 237753 [Multi-domain]  Cd Length: 414  Bit Score: 38.80  E-value: 4.97e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 145332619 193 AADLHVASKLDY--DEEIGTMLKKvEPNaKRIEEHRRKYQRLRKEKELQRAERERRKQQ 249
Cdd:PRK14552 343 AAKLAIAARVDYfsGRYIGDELKE-ELN-KRIEEIKEKYPKPPKKKREEKKPQKRKKKK 399
TxlA cd02950
TRX-like protein A (TxlA) family; TxlA was originally isolated from the cyanobacterium ...
 289-356 5.05e-03

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: 36.93  E-value: 5.05e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 145332619 289 ILYFTATWCGPCRYMSPLYSNLATQHSR---VVFLKVDIDKANDVAASWNISSVPTFCFI-RDGKEVDKVVG 356
Cdd:cd02950   24 LVEFYADWCTVCQEMAPDVAKLKQKYGDqvnFVMLNVDNPKWLPEIDRYRVDGIPHFVFLdREGNEEGQSIG 95
PHA02125 PHA02125
thioredoxin-like protein
 288-365 5.47e-03

thioredoxin-like protein


Pssm-ID: 133998 [Multi-domain]  Cd Length: 75  Bit Score: 35.34  E-value: 5.47e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145332619 288 LILYFTATWCGPCRYMSPLYSNLATQhsrvvFLKVDIDKANDVAASWNISSVPTFCfirDGKEVDKVVGADKGSLEQK 365
Cdd:PHA02125   1 MIYLFGAEWCANCKMVKPMLANVEYT-----YVDVDTDEGVELTAKHHIRSLPTLV---NTSTLDRFTGVPRNVAELK 70
TlpA_like_DsbE cd03010
TlpA-like family, DsbE (also known as CcmG and CycY) subfamily; DsbE is a membrane-anchored, ...
 289-357 7.84e-03

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: 36.02  E-value: 7.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145332619 289 ILYFTATWCGPCRYMSPLYSNLATQHS-RVV-------------FLK--------VDIDKANDVAASWNISSVP-TFCFI 345
Cdd:cd03010   29 LLNVWASWCAPCREEHPVLMALARQGRvPIYginykdnpenalaWLArhgnpyaaVGFDPDGRVGIDLGVYGVPeTFLID 108

                         90
                 ....*....|..
gi 145332619 346 RDGKEVDKVVGA 357
Cdd:cd03010  109 GDGIIRYKHVGP 120
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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