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Conserved domains on  [gi|1002314546|ref|XP_015620642|]
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disease resistance protein RGA5-like isoform X1 [Oryza sativa Japonica Group]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NB-ARC super family cl26397
NB-ARC domain;
211-463 7.03e-26

NB-ARC domain;


The actual alignment was detected with superfamily member pfam00931:

Pssm-ID: 395745 [Multi-domain]  Cd Length: 245  Bit Score: 107.47  E-value: 7.03e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002314546  211 RDISMQKLVRWLaDGEPKLKVASIVGSGGVGKTTLATEFYRlHGRRLDAPFDCRAFVRTPRKPDMTKILTDMLSQLrpqh 290
Cdd:pfam00931    1 REDMVEKVIGKL-SEKDEPGIVGIHGMGGVGKTTLAAQIFN-DFDEVEGHFDSVAWVVVSKTFTISTLQQTILQNL---- 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002314546  291 qHQSSDVW----EVDRLLEtIRTHLQDKRYFIIIEDLWASSMWDIVSRGLPDNNSCSRILITTEIEPVALACCGYNSEHI 366
Cdd:pfam00931   75 -GLSEDDWdnkeEGELARK-IRRALLTKRFLLVLDDVWDEEDWDKIGIPLPDRENGCRVLLTTRSEEVAGRVGGPSDPHE 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002314546  367 IKIdpLGDDvSSQLFFSGVVGQGN-EFPGHLTEVSHDMIKKCGGLPLAI-----TITARHFksqlldgMQQWNHIQKSLT 440
Cdd:pfam00931  153 VEL--LEPD-EAWELFENKVFPKTlGECELLEDVAKEIVEKCRGLPLALkvlggLLSCKKT-------VEEWKHVYDVLQ 222

                          250       260
                   ....*....|....*....|...
gi 1002314546  441 TSNLKKNPTLQGMRQVLNLIYNN 463
Cdd:pfam00931  223 SELKSNSYSLNSVRSILQLSYEN 245
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 933-1022 1.31e-19

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: 84.53  E-value: 1.31e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002314546  933 QAKQSHKLVVIQFTTSRCPASRYIAPAFTEYAKEFAGAVFIKVNVdsDELESVTDWYDIEGIvPTFFFVKDGEKIDKIPG 1012
Cdd:cd02947      5 ELIKSAKPVVVDFWAPWCGPCKAIAPVLEELAEEYPKVKFVKVDV--DENPELAEEYGVRSI-PTFLFFKNGKEVDRVVG 81

                           90
                   ....*....|.
gi 1002314546 1013 AN-KELLRAKI 1022
Cdd:cd02947     82 ADpKEELEEFL 92
Rx_N pfam18052
Rx N-terminal domain; This entry represents the N-terminal domain found in many plant ...
 40-108 9.00e-06

Rx N-terminal domain; This entry represents the N-terminal domain found in many plant resistance proteins. This domain has been predicted to be a coiled-coil, however the structure shows that it adopts a four helical bundle fold.


:

Pssm-ID: 436239  Cd Length: 93  Bit Score: 44.95  E-value: 9.00e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002314546   40 RKGERKKILLLRGDLRHL---LDDyyllVEPPSDTapppDSTAACWAKEVRELSYDVDDFLDELTTQLLHHR 108
Cdd:pfam18052   20 LKGVKDDLEKLKDELESIqafLED----AERKQIT----DEQVKLWLKQLRDVAYDAEDVLDEFLYEALRRK 83
LRR super family cl34836
Leucine-rich repeat (LRR) protein [Transcription];
639-752 1.46e-05

Leucine-rich repeat (LRR) protein [Transcription];


The actual alignment was detected with superfamily member COG4886:

Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 48.78  E-value: 1.46e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002314546  639 SISELLQLRYLKITGN-ITvKLPEKIQGLQHLQTLeadaratavllDIVHTQcllhlrlvlldllphchryiFTSIPKWT 717
Cdd:COG4886    177 ELGNLTNLKELDLSNNqIT-DLPEPLGNLTNLEEL-----------DLSGNQ--------------------LTDLPEPL 224

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1002314546  718 GKLNNLRILNIAVMQISqdDLDTLKGLGSLTALSL 752
Cdd:COG4886    225 ANLTNLETLDLSNNQLT--DLPELGNLTNLEELDL 257
 
Name Accession Description Interval E-value
NB-ARC pfam00931
NB-ARC domain;
211-463 7.03e-26

NB-ARC domain;


Pssm-ID: 395745 [Multi-domain]  Cd Length: 245  Bit Score: 107.47  E-value: 7.03e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002314546  211 RDISMQKLVRWLaDGEPKLKVASIVGSGGVGKTTLATEFYRlHGRRLDAPFDCRAFVRTPRKPDMTKILTDMLSQLrpqh 290
Cdd:pfam00931    1 REDMVEKVIGKL-SEKDEPGIVGIHGMGGVGKTTLAAQIFN-DFDEVEGHFDSVAWVVVSKTFTISTLQQTILQNL---- 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002314546  291 qHQSSDVW----EVDRLLEtIRTHLQDKRYFIIIEDLWASSMWDIVSRGLPDNNSCSRILITTEIEPVALACCGYNSEHI 366
Cdd:pfam00931   75 -GLSEDDWdnkeEGELARK-IRRALLTKRFLLVLDDVWDEEDWDKIGIPLPDRENGCRVLLTTRSEEVAGRVGGPSDPHE 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002314546  367 IKIdpLGDDvSSQLFFSGVVGQGN-EFPGHLTEVSHDMIKKCGGLPLAI-----TITARHFksqlldgMQQWNHIQKSLT 440
Cdd:pfam00931  153 VEL--LEPD-EAWELFENKVFPKTlGECELLEDVAKEIVEKCRGLPLALkvlggLLSCKKT-------VEEWKHVYDVLQ 222

                          250       260
                   ....*....|....*....|...
gi 1002314546  441 TSNLKKNPTLQGMRQVLNLIYNN 463
Cdd:pfam00931  223 SELKSNSYSLNSVRSILQLSYEN 245
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 933-1022 1.31e-19

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: 84.53  E-value: 1.31e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002314546  933 QAKQSHKLVVIQFTTSRCPASRYIAPAFTEYAKEFAGAVFIKVNVdsDELESVTDWYDIEGIvPTFFFVKDGEKIDKIPG 1012
Cdd:cd02947      5 ELIKSAKPVVVDFWAPWCGPCKAIAPVLEELAEEYPKVKFVKVDV--DENPELAEEYGVRSI-PTFLFFKNGKEVDRVVG 81

                           90
                   ....*....|.
gi 1002314546 1013 AN-KELLRAKI 1022
Cdd:cd02947     82 ADpKEELEEFL 92
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 923-1025 6.63e-18

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: 79.86  E-value: 6.63e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002314546  923 TMEQFAlhmSQAKQSHKLVVIQFTTSRCPASRYIAPAFTEYAKEFAGAV-FIKVNVdsDELESVTDWYDIEGIvPTFFFV 1001
Cdd:COG3118      6 TDENFE---EEVLESDKPVLVDFWAPWCGPCKMLAPVLEELAAEYGGKVkFVKVDV--DENPELAAQFGVRSI-PTLLLF 79

                           90       100
                   ....*....|....*....|....*
gi 1002314546 1002 KDGEKIDKIPGA-NKELLRAKIRRH 1025
Cdd:COG3118     80 KDGQPVDRFVGAlPKEQLREFLDKV 104
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 918-1024 6.42e-14

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: 68.41  E-value: 6.42e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002314546  918 VIVPHTMEQFAlhmSQAKQSHKLVVIQFTTSRCPASRYIAPAFTEYAKEFAGAVFIkVNVDSDELESVTDWYDIEGIvPT 997
Cdd:pfam00085    1 VVVVLTDANFD---EVVQKSSKPVLVDFYAPWCGPCKMLAPEYEELAQEYKGNVVF-AKVDVDENPDLASKYGVRGY-PT 75

                           90       100
                   ....*....|....*....|....*...
gi 1002314546  998 FFFVKDGEKIDKIPGAN-KELLRAKIRR 1024
Cdd:pfam00085   76 LIFFKNGQPVDDYVGARpKDALAAFLKA 103
PTZ00051 PTZ00051
thioredoxin; Provisional
 923-1019 1.07e-12

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 64.90  E-value: 1.07e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002314546  923 TMEQFALHMSQakqsHKLVVIQFTTSRCPASRYIAPAFTEYAKEFAGAVFIKVNVdsDELESVTDWYDIEGIvPTFFFVK 1002
Cdd:PTZ00051     7 SQAEFESTLSQ----NELVIVDFYAEWCGPCKRIAPFYEECSKEYTKMVFVKVDV--DELSEVAEKENITSM-PTFKVFK 79

                           90
                   ....*....|....*..
gi 1002314546 1003 DGEKIDKIPGANKELLR 1019
Cdd:PTZ00051    80 NGSVVDTLLGANDEALK 96
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 923-1025 3.08e-09

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: 55.37  E-value: 3.08e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002314546  923 TMEQFAlhmSQAKQSHKLVVIQFTTSRCPASRYIAPAFTEYAKEFAG-AVFIKVNVDsdELESVTDWYDIEGIvPTFFFV 1001
Cdd:TIGR01068    2 TDANFD---ETIASSDKPVLVDFWAPWCGPCKMIAPILEELAKEYEGkVKFVKLNVD--ENPDIAAKYGIRSI-PTLLLF 75

                           90       100
                   ....*....|....*....|....*
gi 1002314546 1002 KDGEKIDKIPGAN-KELLRAKIRRH 1025
Cdd:TIGR01068   76 KNGKEVDRSVGALpKAALKQLINKN 100
COG3903 COG3903
Predicted ATPase [General function prediction only];
48-420 4.32e-06

Predicted ATPase [General function prediction only];


Pssm-ID: 443109 [Multi-domain]  Cd Length: 933  Bit Score: 50.79  E-value: 4.32e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002314546   48 LLLRGDLRHLLDDYYLLVEPPSDTAPPPDSTAACWAKEVRELSYDVDDFLDELTTQLLHHRGGGDGSSTAGAKkMISSMI 127
Cdd:COG3903     10 AAAAAALALLALAAAAAAAAAAAALAAALEALRAALALLLLLLAALALALAALALLLAAAALLLRLLLLLLAA-RLLARL 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002314546  128 ARLRGELNRRRWIADEVTLFSARVkEAIRRQESYHLGRRTSSSRPREEVDDDDREDSAGNERRRFLSLTFGMDDAAVHGQ 207
Cdd:COG3903     89 AAAAAAALARAAAAALALLLRLRL-AARRLLLARALAAAALAAAAAAAAAAAAAPAPPPPAPPPPAPLAALARRAAALAA 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002314546  208 LVGRDISMQKLVrwladgepklkvaSIVGSGGVGKTTLATEFyrlhGRRLDAPF-DCRAFV--RTPRKPDMtkILTDMLS 284
Cdd:COG3903    168 AARALLSAARLV-------------TLTGPGGVGKTRLALEV----AHRLADRFpDGVWFVdlAGVTDPAL--VLAAVAR 228

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002314546  285 QLR-PQHQHQSsdvwevdrLLETIRTHLQDKRYFIII---EDLWASSMwDIVSRGLPDNNSCsRILITTEiEPVALAccg 360
Cdd:COG3903    229 ALGvRDAPGRD--------PAARLRAALADRRLLLVLdncEHVVDAAA-ALVRPLLPAAPGL-RVLATSR-EPLGLP--- 294

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002314546  361 ynSEHIIKIDPLGDDVSS---------QLFFS--GVVGQGNEFPGHLTEVSHDMIKKCGGLPLAITITARH 420
Cdd:COG3903    295 --GERVLPLPPLAVPPPGaealaseavALFVEraGAARPGFALDAAEAAAVAEICRRLDGLPLAIELAAAR 363
Rx_N pfam18052
Rx N-terminal domain; This entry represents the N-terminal domain found in many plant ...
 40-108 9.00e-06

Rx N-terminal domain; This entry represents the N-terminal domain found in many plant resistance proteins. This domain has been predicted to be a coiled-coil, however the structure shows that it adopts a four helical bundle fold.


Pssm-ID: 436239  Cd Length: 93  Bit Score: 44.95  E-value: 9.00e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002314546   40 RKGERKKILLLRGDLRHL---LDDyyllVEPPSDTapppDSTAACWAKEVRELSYDVDDFLDELTTQLLHHR 108
Cdd:pfam18052   20 LKGVKDDLEKLKDELESIqafLED----AERKQIT----DEQVKLWLKQLRDVAYDAEDVLDEFLYEALRRK 83
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
639-752 1.46e-05

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 48.78  E-value: 1.46e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002314546  639 SISELLQLRYLKITGN-ITvKLPEKIQGLQHLQTLeadaratavllDIVHTQcllhlrlvlldllphchryiFTSIPKWT 717
Cdd:COG4886    177 ELGNLTNLKELDLSNNqIT-DLPEPLGNLTNLEEL-----------DLSGNQ--------------------LTDLPEPL 224

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1002314546  718 GKLNNLRILNIAVMQISqdDLDTLKGLGSLTALSL 752
Cdd:COG4886    225 ANLTNLETLDLSNNQLT--DLPELGNLTNLEELDL 257
 
Name Accession Description Interval E-value
NB-ARC pfam00931
NB-ARC domain;
211-463 7.03e-26

NB-ARC domain;


Pssm-ID: 395745 [Multi-domain]  Cd Length: 245  Bit Score: 107.47  E-value: 7.03e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002314546  211 RDISMQKLVRWLaDGEPKLKVASIVGSGGVGKTTLATEFYRlHGRRLDAPFDCRAFVRTPRKPDMTKILTDMLSQLrpqh 290
Cdd:pfam00931    1 REDMVEKVIGKL-SEKDEPGIVGIHGMGGVGKTTLAAQIFN-DFDEVEGHFDSVAWVVVSKTFTISTLQQTILQNL---- 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002314546  291 qHQSSDVW----EVDRLLEtIRTHLQDKRYFIIIEDLWASSMWDIVSRGLPDNNSCSRILITTEIEPVALACCGYNSEHI 366
Cdd:pfam00931   75 -GLSEDDWdnkeEGELARK-IRRALLTKRFLLVLDDVWDEEDWDKIGIPLPDRENGCRVLLTTRSEEVAGRVGGPSDPHE 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002314546  367 IKIdpLGDDvSSQLFFSGVVGQGN-EFPGHLTEVSHDMIKKCGGLPLAI-----TITARHFksqlldgMQQWNHIQKSLT 440
Cdd:pfam00931  153 VEL--LEPD-EAWELFENKVFPKTlGECELLEDVAKEIVEKCRGLPLALkvlggLLSCKKT-------VEEWKHVYDVLQ 222

                          250       260
                   ....*....|....*....|...
gi 1002314546  441 TSNLKKNPTLQGMRQVLNLIYNN 463
Cdd:pfam00931  223 SELKSNSYSLNSVRSILQLSYEN 245
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 933-1022 1.31e-19

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: 84.53  E-value: 1.31e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002314546  933 QAKQSHKLVVIQFTTSRCPASRYIAPAFTEYAKEFAGAVFIKVNVdsDELESVTDWYDIEGIvPTFFFVKDGEKIDKIPG 1012
Cdd:cd02947      5 ELIKSAKPVVVDFWAPWCGPCKAIAPVLEELAEEYPKVKFVKVDV--DENPELAEEYGVRSI-PTFLFFKNGKEVDRVVG 81

                           90
                   ....*....|.
gi 1002314546 1013 AN-KELLRAKI 1022
Cdd:cd02947     82 ADpKEELEEFL 92
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 923-1025 6.63e-18

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: 79.86  E-value: 6.63e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002314546  923 TMEQFAlhmSQAKQSHKLVVIQFTTSRCPASRYIAPAFTEYAKEFAGAV-FIKVNVdsDELESVTDWYDIEGIvPTFFFV 1001
Cdd:COG3118      6 TDENFE---EEVLESDKPVLVDFWAPWCGPCKMLAPVLEELAAEYGGKVkFVKVDV--DENPELAAQFGVRSI-PTLLLF 79

                           90       100
                   ....*....|....*....|....*
gi 1002314546 1002 KDGEKIDKIPGA-NKELLRAKIRRH 1025
Cdd:COG3118     80 KDGQPVDRFVGAlPKEQLREFLDKV 104
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 918-1024 6.42e-14

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: 68.41  E-value: 6.42e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002314546  918 VIVPHTMEQFAlhmSQAKQSHKLVVIQFTTSRCPASRYIAPAFTEYAKEFAGAVFIkVNVDSDELESVTDWYDIEGIvPT 997
Cdd:pfam00085    1 VVVVLTDANFD---EVVQKSSKPVLVDFYAPWCGPCKMLAPEYEELAQEYKGNVVF-AKVDVDENPDLASKYGVRGY-PT 75

                           90       100
                   ....*....|....*....|....*...
gi 1002314546  998 FFFVKDGEKIDKIPGAN-KELLRAKIRR 1024
Cdd:pfam00085   76 LIFFKNGQPVDDYVGARpKDALAAFLKA 103
PTZ00051 PTZ00051
thioredoxin; Provisional
 923-1019 1.07e-12

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 64.90  E-value: 1.07e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002314546  923 TMEQFALHMSQakqsHKLVVIQFTTSRCPASRYIAPAFTEYAKEFAGAVFIKVNVdsDELESVTDWYDIEGIvPTFFFVK 1002
Cdd:PTZ00051     7 SQAEFESTLSQ----NELVIVDFYAEWCGPCKRIAPFYEECSKEYTKMVFVKVDV--DELSEVAEKENITSM-PTFKVFK 79

                           90
                   ....*....|....*..
gi 1002314546 1003 DGEKIDKIPGANKELLR 1019
Cdd:PTZ00051    80 NGSVVDTLLGANDEALK 96
TRX_PICOT cd02984
TRX domain, PICOT (for PKC-interacting cousin of TRX) subfamily; PICOT is a protein that ...
 925-1022 8.03e-11

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: 59.59  E-value: 8.03e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002314546  925 EQFALHMSqaKQSHKLVVIQFTTSRCPASRYIAPAFTEYAKE-FAGAVFikVNVDSDELESVTDWYDIEGiVPTFFFVKD 1003
Cdd:cd02984      3 EEFEELLK--SDASKLLVLHFWAPWAEPCKQMNQVFEELAKEaFPSVLF--LSIEAEELPEISEKFEITA-VPTFVFFRN 77

                           90
                   ....*....|....*....
gi 1002314546 1004 GEKIDKIPGANKELLRAKI 1022
Cdd:cd02984     78 GTIVDRVSGADPKELAKKV 96
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 931-1028 9.65e-11

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 60.86  E-value: 9.65e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002314546  931 MSQAKQSHKLVVIQFTTSRCPASRYIAPAFTEYAKEFAGAVFIKVNVDsDELESVTDWYDIEGI---------------- 994
Cdd:COG0526     21 LSLADLKGKPVLVNFWATWCPPCRAEMPVLKELAEEYGGVVFVGVDVD-ENPEAVKAFLKELGLpypvlldpdgelakay 99

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1002314546  995 ----VPTFFFV-KDGEKIDKIPGA-NKELLRAKIRRHTAS 1028
Cdd:COG0526    100 gvrgIPTTVLIdKDGKIVARHVGPlSPEELEEALEKLLAK 139
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 923-1025 3.08e-09

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: 55.37  E-value: 3.08e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002314546  923 TMEQFAlhmSQAKQSHKLVVIQFTTSRCPASRYIAPAFTEYAKEFAG-AVFIKVNVDsdELESVTDWYDIEGIvPTFFFV 1001
Cdd:TIGR01068    2 TDANFD---ETIASSDKPVLVDFWAPWCGPCKMIAPILEELAKEYEGkVKFVKLNVD--ENPDIAAKYGIRSI-PTLLLF 75

                           90       100
                   ....*....|....*....|....*
gi 1002314546 1002 KDGEKIDKIPGAN-KELLRAKIRRH 1025
Cdd:TIGR01068   76 KNGKEVDRSVGALpKAALKQLINKN 100
TRX_CDSP32 cd02985
TRX family, chloroplastic drought-induced stress protein of 32 kD (CDSP32); CDSP32 is composed ...
 922-1025 3.53e-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: 52.10  E-value: 3.53e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002314546  922 HTMEQFALHMSQAKQshKLVVIQFTTSRCPASRYIAPAFTEYAKEFAGAVFIKVNvdSDELESVTDWYDIEGI--VPTFF 999
Cdd:cd02985      1 HSVEELDEALKKAKG--RLVVLEFALKHSGPSVKIYPTMVKLSRTCNDVVFLLVN--GDENDSTMELCRREKIieVPHFL 76

                           90       100
                   ....*....|....*....|....*.
gi 1002314546 1000 FVKDGEKIDKIPGANKELLRAKIRRH 1025
Cdd:cd02985     77 FYKDGEKIHEEEGIGPDELIGDVLYY 102
COG3903 COG3903
Predicted ATPase [General function prediction only];
48-420 4.32e-06

Predicted ATPase [General function prediction only];


Pssm-ID: 443109 [Multi-domain]  Cd Length: 933  Bit Score: 50.79  E-value: 4.32e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002314546   48 LLLRGDLRHLLDDYYLLVEPPSDTAPPPDSTAACWAKEVRELSYDVDDFLDELTTQLLHHRGGGDGSSTAGAKkMISSMI 127
Cdd:COG3903     10 AAAAAALALLALAAAAAAAAAAAALAAALEALRAALALLLLLLAALALALAALALLLAAAALLLRLLLLLLAA-RLLARL 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002314546  128 ARLRGELNRRRWIADEVTLFSARVkEAIRRQESYHLGRRTSSSRPREEVDDDDREDSAGNERRRFLSLTFGMDDAAVHGQ 207
Cdd:COG3903     89 AAAAAAALARAAAAALALLLRLRL-AARRLLLARALAAAALAAAAAAAAAAAAAPAPPPPAPPPPAPLAALARRAAALAA 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002314546  208 LVGRDISMQKLVrwladgepklkvaSIVGSGGVGKTTLATEFyrlhGRRLDAPF-DCRAFV--RTPRKPDMtkILTDMLS 284
Cdd:COG3903    168 AARALLSAARLV-------------TLTGPGGVGKTRLALEV----AHRLADRFpDGVWFVdlAGVTDPAL--VLAAVAR 228

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002314546  285 QLR-PQHQHQSsdvwevdrLLETIRTHLQDKRYFIII---EDLWASSMwDIVSRGLPDNNSCsRILITTEiEPVALAccg 360
Cdd:COG3903    229 ALGvRDAPGRD--------PAARLRAALADRRLLLVLdncEHVVDAAA-ALVRPLLPAAPGL-RVLATSR-EPLGLP--- 294

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002314546  361 ynSEHIIKIDPLGDDVSS---------QLFFS--GVVGQGNEFPGHLTEVSHDMIKKCGGLPLAITITARH 420
Cdd:COG3903    295 --GERVLPLPPLAVPPPGaealaseavALFVEraGAARPGFALDAAEAAAVAEICRRLDGLPLAIELAAAR 363
Rx_N pfam18052
Rx N-terminal domain; This entry represents the N-terminal domain found in many plant ...
 40-108 9.00e-06

Rx N-terminal domain; This entry represents the N-terminal domain found in many plant resistance proteins. This domain has been predicted to be a coiled-coil, however the structure shows that it adopts a four helical bundle fold.


Pssm-ID: 436239  Cd Length: 93  Bit Score: 44.95  E-value: 9.00e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002314546   40 RKGERKKILLLRGDLRHL---LDDyyllVEPPSDTapppDSTAACWAKEVRELSYDVDDFLDELTTQLLHHR 108
Cdd:pfam18052   20 LKGVKDDLEKLKDELESIqafLED----AERKQIT----DEQVKLWLKQLRDVAYDAEDVLDEFLYEALRRK 83
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
639-752 1.46e-05

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 48.78  E-value: 1.46e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002314546  639 SISELLQLRYLKITGN-ITvKLPEKIQGLQHLQTLeadaratavllDIVHTQcllhlrlvlldllphchryiFTSIPKWT 717
Cdd:COG4886    177 ELGNLTNLKELDLSNNqIT-DLPEPLGNLTNLEEL-----------DLSGNQ--------------------LTDLPEPL 224

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1002314546  718 GKLNNLRILNIAVMQISqdDLDTLKGLGSLTALSL 752
Cdd:COG4886    225 ANLTNLETLDLSNNQLT--DLPELGNLTNLEELDL 257
PRK10996 PRK10996
thioredoxin 2; Provisional
 936-1013 4.85e-05

thioredoxin 2; Provisional


Pssm-ID: 182889 [Multi-domain]  Cd Length: 139  Bit Score: 44.29  E-value: 4.85e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002314546  936 QSHKLVVIQFTTSRCPASRYIAPAFTEYAKEFAGAV-FIKVNVDSDELESVTdwYDIEGIvPTFFFVKDGEKIDKIPGA 1013
Cdd:PRK10996    50 QDDLPVVIDFWAPWCGPCRNFAPIFEDVAAERSGKVrFVKVNTEAERELSAR--FRIRSI-PTIMIFKNGQVVDMLNGA 125
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
939-1024 7.17e-05

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 43.70  E-value: 7.17e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002314546  939 KLVVIQFTTSRCPASRYIAPAFTEYAKEFA--GAVFIKVNVD-------------------SDELESVTDWYDIEGIvPT 997
Cdd:COG1225     22 KPVVLYFYATWCPGCTAELPELRDLYEEFKdkGVEVLGVSSDsdeahkkfaekyglpfpllSDPDGEVAKAYGVRGT-PT 100

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1002314546  998 FFFV-KDGEKIDKIPGANK------ELLRAKIRR 1024
Cdd:COG1225    101 TFLIdPDGKIRYVWVGPVDprphleEVLEALLAE 134
ybbN cd02956
ybbN protein family; ybbN is a hypothetical protein containing a redox-inactive TRX-like ...
 938-1016 8.20e-05

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


Pssm-ID: 239254 [Multi-domain]  Cd Length: 96  Bit Score: 42.64  E-value: 8.20e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002314546  938 HKLVVIQFTTSRCPASRYIAPAFTEYAKEFAGAvFIKVNVDSDELESVTDWYDIEGIvPTFFFVKDGEKIDKIPGANKE 1016
Cdd:cd02956     12 QVPVVVDFWAPRSPPSKELLPLLERLAEEYQGQ-FVLAKVNCDAQPQIAQQFGVQAL-PTVYLFAAGQPVDGFQGAQPE 88
PDI_a_family cd02961
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ...
 920-1006 1.30e-04

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: 42.21  E-value: 1.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002314546  920 VPHTMEQFALHMsqakQSHKLVVIQFTTSRCPASRYIAPAFTEYAKEFAG---AVFIKVNVDSDelESVTDWYDIEGiVP 996
Cdd:cd02961      1 VELTDDNFDELV----KDSKDVLVEFYAPWCGHCKALAPEYEKLAKELKGdgkVVVAKVDCTAN--NDLCSEYGVRG-YP 73

                           90
                   ....*....|
gi 1002314546  997 TFFFVKDGEK 1006
Cdd:cd02961     74 TIKLFPNGSK 83
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 932-1012 1.84e-04

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


Pssm-ID: 239264 [Multi-domain]  Cd Length: 116  Bit Score: 41.84  E-value: 1.84e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002314546  932 SQAKQSHKLVVIQFTTSRCPASRYIAPAFTEYAKEFA--GAVFIKVNVDSDELESVTDWYDIEGI--------------- 994
Cdd:cd02966     13 SLSDLKGKVVLVNFWASWCPPCRAEMPELEALAKEYKddGVEVVGVNVDDDDPAAVKAFLKKYGItfpvlldpdgelaka 92

                           90       100
                   ....*....|....*....|....
gi 1002314546  995 -----VPTFFFV-KDGEKIDKIPG 1012
Cdd:cd02966     93 ygvrgLPTTFLIdRDGRIRARHVG 116
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
639-752 8.43e-04

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 43.00  E-value: 8.43e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002314546  639 SISELLQLRYLKITGN-ITvKLPEKIQGLQHLQTLeadaratavllDIVHTQcllhlrlvlldllphchryiFTSIPKWT 717
Cdd:COG4886    131 ELANLTNLKELDLSNNqLT-DLPEPLGNLTNLKSL-----------DLSNNQ--------------------LTDLPEEL 178

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1002314546  718 GKLNNLRILNIAVMQISqdDL-DTLKGLGSLTALSL 752
Cdd:COG4886    179 GNLTNLKELDLSNNQIT--DLpEPLGNLTNLEELDL 212
SoxW COG2143
Thioredoxin-related protein SoxW [Posttranslational modification, protein turnover, chaperones] ...
 931-1015 2.36e-03

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


Pssm-ID: 441746 [Multi-domain]  Cd Length: 146  Bit Score: 39.50  E-value: 2.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002314546  931 MSQAKQSHKLVVIQFTTSRCPASRYI------APAFTEYAKEfaGAVFIKVNVDSD--------ELESVTDW---YDIEG 993
Cdd:COG2143     33 LALAKAEGKPILLFFESDWCPYCKKLhkevfsDPEVAAYLKE--NFVVVQLDAEGDkevtdfdgETLTEKELarkYGVRG 110

                           90       100
                   ....*....|....*....|...
gi 1002314546  994 iVPTF-FFVKDGEKIDKIPGANK 1015
Cdd:COG2143    111 -TPTLvFFDAEGKEIARIPGYLK 132
TlpA_like_ScsD_MtbDsbE cd03011
TlpA-like family, suppressor for copper sensitivity D protein (ScsD) and actinobacterial DsbE ...
 932-1008 2.80e-03

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: 38.82  E-value: 2.80e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002314546  932 SQAKQSHKLVVIQFTTSRCPASRYIAPAFTEYAKEFAgavFIKVNVDSDELESVTDW-----YDIEGI------------ 994
Cdd:cd03011     14 DLESLSGKPVLVYFWATWCPVCRFTSPTVNQLAADYP---VVSVALRSGDDGAVARFmqkkgYGFPVIndpdgvisarwg 90

                           90
                   ....*....|....*..
gi 1002314546  995 ---VPTFFFVKDGEKID 1008
Cdd:cd03011     91 vsvTPAIVIVDPGGIVF 107
PDI_a_ERp44 cd02996
PDIa family, endoplasmic reticulum protein 44 (ERp44) subfamily; ERp44 is an ER-resident ...
 936-1009 4.02e-03

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: 38.14  E-value: 4.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002314546  936 QSHKLVVIQFTTSRCPASRYIAPAFTEYAKEF------AGAVFIKvNVDSDELESVTDWYDIEGiVPTFFFVKDGEKIDK 1009
Cdd:cd02996     16 QSAELVLVNFYADWCRFSQMLHPIFEEAAAKIkeefpdAGKVVWG-KVDCDKESDIADRYRINK-YPTLKLFRNGMMMKR 93
Thioredoxin_2 pfam13098
Thioredoxin-like domain;
935-1022 4.92e-03

Thioredoxin-like domain;


Pssm-ID: 379034 [Multi-domain]  Cd Length: 103  Bit Score: 37.79  E-value: 4.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002314546  935 KQSHKLVVIQFTTSRCPASRYIA------PAFTEYAKEfaGAVFIKVNVDSDElESVTDWYDIE---------GI--VPT 997
Cdd:pfam13098    1 KGNGKPVLVVFTDPDCPYCKKLKkelledPDVTVYLGP--NFVFIAVNIWCAK-EVAKAFTDILenkelgrkyGVrgTPT 77

                           90       100
                   ....*....|....*....|....*.
gi 1002314546  998 FFFVKDGEKIDKIPGA-NKELLRAKI 1022
Cdd:pfam13098   78 IVFFDGKGELLRLPGYvPAEEFLALL 103
 
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.
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