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Conserved domains on  [gi|1589196069|gb|TCU59227|]
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cytochrome c-type biogenesis protein [Longicatena caecimuris]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CcdA COG0785
Cytochrome c biogenesis protein CcdA [Energy production and conversion, Posttranslational ...
 11-208 1.55e-58

Cytochrome c biogenesis protein CcdA [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


:

Pssm-ID: 440548 [Multi-domain]  Cd Length: 193  Bit Score: 189.67  E-value: 1.55e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589196069  11 ISILMVFMEGVLSFLSPCVLPLLPVYMGYLIGSDVnnkqiRKKRFVIFFTLSFIFGIFTAILLMNISITLISSFFRDHMS 90
Cdd:COG0785     3 LSLLLAFLAGLLSFLSPCVLPLLPGYLSYLTGLSR-----ASRRRALLRALLFVLGFSLVFVLLGALASALGSLLGQYQD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589196069  91 VFIKVGGILIIVLGLFQLGFFKSNFLGKTRRLPFtlKKEMNLLLAFLMGFTFSFAWTPCIGPALSSILLLANSSQNLWMS 170
Cdd:COG0785    78 LLRIVAGVLLILFGLVLLGLLKIPFLQREARINL--RRKAGLLGAFLLGLAFGLGWTPCIGPILGAILALAATSGSVLRG 155

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1589196069 171 NFLMVIYALGLTIPFLLIGIFTDSILNWLSNHKSIMNY 208
Cdd:COG0785   156 ALLLLAYALGLGLPFLLLALFAGRLLGRLRRLRRHLRW 193
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 269-412 1.62e-37

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


:

Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 132.89  E-value: 1.62e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589196069 269 KALLQQLGSYELKDQHDKIIKLEDYKGKVVFLNFWATWCPPCRGELPNIQKLYEKYrsdKHVAILTIVYpggqEKGKSDL 348
Cdd:COG0526     2 KAVGKPAPDFTLTDLDGKPLSLADLKGKPVLVNFWATWCPPCRAEMPVLKELAEEY---GGVVFVGVDV----DENPEAV 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1589196069 349 KEFISDNALTVPVLFD-DGFIYSTFGIGSMPTTFMLDKEGKPYGYIEGALTMEMMENMILKTLNA 412
Cdd:COG0526    75 KAFLKELGLPYPVLLDpDGELAKAYGVRGIPTTVLIDKDGKIVARHVGPLSPEELEEALEKLLAK 139
 
Name Accession Description Interval E-value
CcdA COG0785
Cytochrome c biogenesis protein CcdA [Energy production and conversion, Posttranslational ...
 11-208 1.55e-58

Cytochrome c biogenesis protein CcdA [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440548 [Multi-domain]  Cd Length: 193  Bit Score: 189.67  E-value: 1.55e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589196069  11 ISILMVFMEGVLSFLSPCVLPLLPVYMGYLIGSDVnnkqiRKKRFVIFFTLSFIFGIFTAILLMNISITLISSFFRDHMS 90
Cdd:COG0785     3 LSLLLAFLAGLLSFLSPCVLPLLPGYLSYLTGLSR-----ASRRRALLRALLFVLGFSLVFVLLGALASALGSLLGQYQD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589196069  91 VFIKVGGILIIVLGLFQLGFFKSNFLGKTRRLPFtlKKEMNLLLAFLMGFTFSFAWTPCIGPALSSILLLANSSQNLWMS 170
Cdd:COG0785    78 LLRIVAGVLLILFGLVLLGLLKIPFLQREARINL--RRKAGLLGAFLLGLAFGLGWTPCIGPILGAILALAATSGSVLRG 155

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1589196069 171 NFLMVIYALGLTIPFLLIGIFTDSILNWLSNHKSIMNY 208
Cdd:COG0785   156 ALLLLAYALGLGLPFLLLALFAGRLLGRLRRLRRHLRW 193
DsbD pfam02683
Cytochrome C biogenesis protein transmembrane region; This family consists of the ...
 16-224 1.21e-46

Cytochrome C biogenesis protein transmembrane region; This family consists of the transmembrane (i.e. non-catalytic) region of Cytochrome C biogenesis proteins also known as disulphide interchange proteins. These proteins posses a protein disulphide isomerase like domain that is not found within the aligned region of this family.


Pssm-ID: 280792 [Multi-domain]  Cd Length: 213  Bit Score: 159.49  E-value: 1.21e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589196069  16 VFMEGVLSFLSPCVLPLLPVYMGYLIGSDVNN-KQIRKKRFVIFFTLSFIFGIFTAILLMNISITLISSFFRDHMSVFIK 94
Cdd:pfam02683   1 AFLAGLLSFLSPCILPLIPAYLSYISGVSVGDrKQGKKRVRVLLKSLLFVLGLSLVFVLLGLSAAFLGQLFGDFKGWVRI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589196069  95 VGGILIIVLGLFQLGFFKSNFLGKTRRLPFTLKK-EMNLLLAFLMGFTFSFAWTPCIGPALSSILLLANSSQNLWMSNFL 173
Cdd:pfam02683  81 IAGLIVILFGLHFLGVFRIPFLYKLRLVHKTKKKiSLPVLGAFLLGMTFALGWTPCIGPILASVLALAASTGSLLLGAGL 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1589196069 174 MVIYALGLTIPFLLIGIFTDSILNWLSNHKSIMNYTVKLGAIILIFFGVSM 224
Cdd:pfam02683 161 MVVYVLGLAAPFLLASLFFGSLLLRLKWLRKNSHWVKIAGGVLLILFGVLL 211
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 269-412 1.62e-37

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 132.89  E-value: 1.62e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589196069 269 KALLQQLGSYELKDQHDKIIKLEDYKGKVVFLNFWATWCPPCRGELPNIQKLYEKYrsdKHVAILTIVYpggqEKGKSDL 348
Cdd:COG0526     2 KAVGKPAPDFTLTDLDGKPLSLADLKGKPVLVNFWATWCPPCRAEMPVLKELAEEY---GGVVFVGVDV----DENPEAV 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1589196069 349 KEFISDNALTVPVLFD-DGFIYSTFGIGSMPTTFMLDKEGKPYGYIEGALTMEMMENMILKTLNA 412
Cdd:COG0526    75 KAFLKELGLPYPVLLDpDGELAKAYGVRGIPTTVLIDKDGKIVARHVGPLSPEELEEALEKLLAK 139
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 279-395 1.79e-34

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: 123.89  E-value: 1.79e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589196069 279 ELKDQHDKIIKLEDYKGKVVFLNFWATWCPPCRGELPNIQKLYEKYRSDKhVAILTIVYPggqEKGKSDLKEFISDNALT 358
Cdd:cd02966     3 SLPDLDGKPVSLSDLKGKVVLVNFWASWCPPCRAEMPELEALAKEYKDDG-VEVVGVNVD---DDDPAAVKAFLKKYGIT 78

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1589196069 359 VPVLFD-DGFIYSTFGIGSMPTTFMLDKEGKPYGYIEG 395
Cdd:cd02966    79 FPVLLDpDGELAKAYGVRGLPTTFLIDRDGRIRARHVG 116
PRK03147 PRK03147
thiol-disulfide oxidoreductase ResA;
280-403 1.69e-29

thiol-disulfide oxidoreductase ResA;


Pssm-ID: 179545 [Multi-domain]  Cd Length: 173  Bit Score: 112.79  E-value: 1.69e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589196069 280 LKDQHDKIIKLEDYKGKVVFLNFWATWCPPCRGELPNIQKLYEKYRsDKHVAILTIvypggqEKGKSDL--KEFISDNAL 357
Cdd:PRK03147   46 LTDLEGKKIELKDLKGKGVFLNFWGTWCKPCEKEMPYMNELYPKYK-EKGVEIIAV------NVDETELavKNFVNRYGL 118

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1589196069 358 TVPVLFD-DGFIYSTFGIGSMPTTFMLDKEGKPYGYIEGALTMEMME 403
Cdd:PRK03147  119 TFPVAIDkGRQVIDAYGVGPLPTTFLIDKDGKVVKVITGEMTEEQLE 165
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 277-388 4.25e-22

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


Pssm-ID: 425763 [Multi-domain]  Cd Length: 124  Bit Score: 90.75  E-value: 4.25e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589196069 277 SYELKDQHDKIIKLEDYKGKVVFLNFWAT-WCPPCRGELPNIQKLYEKYRsDKHVAILtIVYPGGQEKgksdLKEFISDN 355
Cdd:pfam00578   7 DFELPDGDGGTVSLSDYRGKWVVLFFYPAdWTPVCTTELPALADLYEEFK-KLGVEVL-GVSVDSPES----HKAFAEKY 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1589196069 356 ALTVPVLFD-DGFIYSTFGI------GSMPTTFMLDKEGK 388
Cdd:pfam00578  81 GLPFPLLSDpDGEVARAYGVlneeegGALRATFVIDPDGK 120
dsbE TIGR00385
periplasmic protein thiol:disulfide oxidoreductases, DsbE subfamily; Involved in the ...
 294-407 2.06e-09

periplasmic protein thiol:disulfide oxidoreductases, DsbE subfamily; Involved in the biogenesis of c-type cytochromes as well as in disulfide bond formation in some periplasmic proteins. [Protein fate, Protein folding and stabilization]


Pssm-ID: 129481 [Multi-domain]  Cd Length: 173  Bit Score: 56.32  E-value: 2.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589196069 294 KGKVVFLNFWATWCPPCRGELPNIQKLyekyrSDKHVAILTIVYPGGQEKGKSDLKEFISDNALTvpvLFD-DGFIYSTF 372
Cdd:TIGR00385  62 QGKPVLLNVWASWCPPCRAEHPYLNEL-----AKQGLPIVGVDYKDDRQNAIKFLKELGNPYQLS---LFDpDGMLGLDL 133

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1589196069 373 GIGSMPTTFMLDKEGKPYGYIEGALTMEMMENMIL 407
Cdd:TIGR00385 134 GVYGAPETFLVDGNGVIRYRHAGPLNPEVWTEEFL 168
dipZ PRK00293
thiol:disulfide interchange protein precursor; Provisional
 12-196 1.44e-05

thiol:disulfide interchange protein precursor; Provisional


Pssm-ID: 234717 [Multi-domain]  Cd Length: 571  Bit Score: 47.13  E-value: 1.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589196069  12 SILMVFMEGV-LSFlSPCVLPLLPVYMGYLIGsdvNNKQIRKKRFvifFTLSFIFgiftaILLMNISITL----ISSF-- 84
Cdd:PRK00293  168 SLLWFFLIGIgLAF-TPCVLPMYPILSGIVLG---GKQRLSTARA---LLLSFVY-----VQGMALTYTLlglvVAAAgl 235

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589196069  85 -FR---DHMSVFIkVGGILIIVLGLFQLGFFksnflgkTRRLPFTLKKEMNLLL----------AFLMGFTFSFAWTPCI 150
Cdd:PRK00293  236 qFQaalQHPYVLI-GLSILFVLLALSMFGLF-------TLQLPSSLQTRLTLLSnrqqggslggVFVMGAISGLICSPCT 307

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1589196069 151 GPALSSILLLANSSQNLWMSNFLMVIYALGLTIPFLLIGIFTDSIL 196
Cdd:PRK00293  308 TAPLSGALLYIAQSGDLLLGGLTLYLLALGMGLPLILITTFGNKLL 353
 
Name Accession Description Interval E-value
CcdA COG0785
Cytochrome c biogenesis protein CcdA [Energy production and conversion, Posttranslational ...
 11-208 1.55e-58

Cytochrome c biogenesis protein CcdA [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440548 [Multi-domain]  Cd Length: 193  Bit Score: 189.67  E-value: 1.55e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589196069  11 ISILMVFMEGVLSFLSPCVLPLLPVYMGYLIGSDVnnkqiRKKRFVIFFTLSFIFGIFTAILLMNISITLISSFFRDHMS 90
Cdd:COG0785     3 LSLLLAFLAGLLSFLSPCVLPLLPGYLSYLTGLSR-----ASRRRALLRALLFVLGFSLVFVLLGALASALGSLLGQYQD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589196069  91 VFIKVGGILIIVLGLFQLGFFKSNFLGKTRRLPFtlKKEMNLLLAFLMGFTFSFAWTPCIGPALSSILLLANSSQNLWMS 170
Cdd:COG0785    78 LLRIVAGVLLILFGLVLLGLLKIPFLQREARINL--RRKAGLLGAFLLGLAFGLGWTPCIGPILGAILALAATSGSVLRG 155

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1589196069 171 NFLMVIYALGLTIPFLLIGIFTDSILNWLSNHKSIMNY 208
Cdd:COG0785   156 ALLLLAYALGLGLPFLLLALFAGRLLGRLRRLRRHLRW 193
DsbD pfam02683
Cytochrome C biogenesis protein transmembrane region; This family consists of the ...
 16-224 1.21e-46

Cytochrome C biogenesis protein transmembrane region; This family consists of the transmembrane (i.e. non-catalytic) region of Cytochrome C biogenesis proteins also known as disulphide interchange proteins. These proteins posses a protein disulphide isomerase like domain that is not found within the aligned region of this family.


Pssm-ID: 280792 [Multi-domain]  Cd Length: 213  Bit Score: 159.49  E-value: 1.21e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589196069  16 VFMEGVLSFLSPCVLPLLPVYMGYLIGSDVNN-KQIRKKRFVIFFTLSFIFGIFTAILLMNISITLISSFFRDHMSVFIK 94
Cdd:pfam02683   1 AFLAGLLSFLSPCILPLIPAYLSYISGVSVGDrKQGKKRVRVLLKSLLFVLGLSLVFVLLGLSAAFLGQLFGDFKGWVRI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589196069  95 VGGILIIVLGLFQLGFFKSNFLGKTRRLPFTLKK-EMNLLLAFLMGFTFSFAWTPCIGPALSSILLLANSSQNLWMSNFL 173
Cdd:pfam02683  81 IAGLIVILFGLHFLGVFRIPFLYKLRLVHKTKKKiSLPVLGAFLLGMTFALGWTPCIGPILASVLALAASTGSLLLGAGL 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1589196069 174 MVIYALGLTIPFLLIGIFTDSILNWLSNHKSIMNYTVKLGAIILIFFGVSM 224
Cdd:pfam02683 161 MVVYVLGLAAPFLLASLFFGSLLLRLKWLRKNSHWVKIAGGVLLILFGVLL 211
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 269-412 1.62e-37

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 132.89  E-value: 1.62e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589196069 269 KALLQQLGSYELKDQHDKIIKLEDYKGKVVFLNFWATWCPPCRGELPNIQKLYEKYrsdKHVAILTIVYpggqEKGKSDL 348
Cdd:COG0526     2 KAVGKPAPDFTLTDLDGKPLSLADLKGKPVLVNFWATWCPPCRAEMPVLKELAEEY---GGVVFVGVDV----DENPEAV 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1589196069 349 KEFISDNALTVPVLFD-DGFIYSTFGIGSMPTTFMLDKEGKPYGYIEGALTMEMMENMILKTLNA 412
Cdd:COG0526    75 KAFLKELGLPYPVLLDpDGELAKAYGVRGIPTTVLIDKDGKIVARHVGPLSPEELEEALEKLLAK 139
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 279-395 1.79e-34

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: 123.89  E-value: 1.79e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589196069 279 ELKDQHDKIIKLEDYKGKVVFLNFWATWCPPCRGELPNIQKLYEKYRSDKhVAILTIVYPggqEKGKSDLKEFISDNALT 358
Cdd:cd02966     3 SLPDLDGKPVSLSDLKGKVVLVNFWASWCPPCRAEMPELEALAKEYKDDG-VEVVGVNVD---DDDPAAVKAFLKKYGIT 78

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1589196069 359 VPVLFD-DGFIYSTFGIGSMPTTFMLDKEGKPYGYIEG 395
Cdd:cd02966    79 FPVLLDpDGELAKAYGVRGLPTTFLIDRDGRIRARHVG 116
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
279-388 6.39e-32

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 117.66  E-value: 6.39e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589196069 279 ELKDQHDKIIKLEDYKGKVVFLNFWATWCPPCRGELPNIQKLYEKYRsDKHVAILTIVyPGGQEKgksdLKEFISDNALT 358
Cdd:COG1225     5 TLPDLDGKTVSLSDLRGKPVVLYFYATWCPGCTAELPELRDLYEEFK-DKGVEVLGVS-SDSDEA----HKKFAEKYGLP 78

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1589196069 359 VPVLFD-DGFIYSTFGIGSMPTTFMLDKEGK 388
Cdd:COG1225    79 FPLLSDpDGEVAKAYGVRGTPTTFLIDPDGK 109
PRK03147 PRK03147
thiol-disulfide oxidoreductase ResA;
280-403 1.69e-29

thiol-disulfide oxidoreductase ResA;


Pssm-ID: 179545 [Multi-domain]  Cd Length: 173  Bit Score: 112.79  E-value: 1.69e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589196069 280 LKDQHDKIIKLEDYKGKVVFLNFWATWCPPCRGELPNIQKLYEKYRsDKHVAILTIvypggqEKGKSDL--KEFISDNAL 357
Cdd:PRK03147   46 LTDLEGKKIELKDLKGKGVFLNFWGTWCKPCEKEMPYMNELYPKYK-EKGVEIIAV------NVDETELavKNFVNRYGL 118

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1589196069 358 TVPVLFD-DGFIYSTFGIGSMPTTFMLDKEGKPYGYIEGALTMEMME 403
Cdd:PRK03147  119 TFPVAIDkGRQVIDAYGVGPLPTTFLIDKDGKVVKVITGEMTEEQLE 165
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 277-388 4.25e-22

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


Pssm-ID: 425763 [Multi-domain]  Cd Length: 124  Bit Score: 90.75  E-value: 4.25e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589196069 277 SYELKDQHDKIIKLEDYKGKVVFLNFWAT-WCPPCRGELPNIQKLYEKYRsDKHVAILtIVYPGGQEKgksdLKEFISDN 355
Cdd:pfam00578   7 DFELPDGDGGTVSLSDYRGKWVVLFFYPAdWTPVCTTELPALADLYEEFK-KLGVEVL-GVSVDSPES----HKAFAEKY 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1589196069 356 ALTVPVLFD-DGFIYSTFGI------GSMPTTFMLDKEGK 388
Cdd:pfam00578  81 GLPFPLLSDpDGEVARAYGVlneeegGALRATFVIDPDGK 120
TlpA_like_DsbE cd03010
TlpA-like family, DsbE (also known as CcmG and CycY) subfamily; DsbE is a membrane-anchored, ...
 282-388 2.63e-14

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: 69.14  E-value: 2.63e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589196069 282 DQHDKIIKLEDYKGKVVFLNFWATWCPPCRGELPNIQKLYEkyrsDKHVAILTIVYPGGQEKGKSDLKEFisDNALTVpV 361
Cdd:cd03010    12 PGPDKTLTSADLKGKPYLLNVWASWCAPCREEHPVLMALAR----QGRVPIYGINYKDNPENALAWLARH--GNPYAA-V 84

                          90       100
                  ....*....|....*....|....*...
gi 1589196069 362 LFD-DGFIYSTFGIGSMPTTFMLDKEGK 388
Cdd:cd03010    85 GFDpDGRVGIDLGVYGVPETFLIDGDGI 112
DsbD COG4232
Thiol:disulfide interchange protein DsbD [Posttranslational modification, protein turnover, ...
 13-311 3.67e-14

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


Pssm-ID: 443376 [Multi-domain]  Cd Length: 416  Bit Score: 73.69  E-value: 3.67e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589196069  13 ILMVFMEGVLSFLSPCVLPLLPVYMGYLIGSDVNNkqiRKKRFV--IFFTLS--FIFGIFTAILLMNISITLISSFFRDh 88
Cdd:COG4232     6 LLLAFLGGLLLNLTPCVLPMLPIKSSIIVGQGGKS---RRRAFLlsLAYVLGmaLTYTLLGLLAALLGGAVGWGFQLQS- 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589196069  89 mSVFIKVGGILIIVLGLFQLGFFksnflgkTRRLPFTLKKEMN-------LLLAFLMGFTFSFAWTPCIGPALSSILLLA 161
Cdd:COG4232    82 -PWVLGALALLFVLLALSMFGLF-------ELQLPSSLQNRLAalsngggLLGAFFMGVLAALVATPCTAPFLGGALGYA 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589196069 162 NSSQNLWMSNFLMVIYALGLTIPFLLIGIFTdSILNWL-----------------------------SNHKSIMNYTVKL 212
Cdd:COG4232   154 LQTGDALLGLLALFALGLGMALPLLLLGLFP-GLLKLLpkpgawmetvkqvfgflllataiwllsvlLPQAGLDAVALLL 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589196069 213 GAIILIFFGVSMVsGKMNFISNYMTQSSN------------------NAMIKDKNEDKKEDGGENKDEKNSEQEKALLQQ 274
Cdd:COG4232   233 WALLLLALALWLL-GALRLPHDSSGRRLSvrkglglllllaglalllGALSGADPLQPLAAGAAAAAAAAGLAWQADLEA 311

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1589196069 275 lgsyelkdqhdkiiKLEDYK--GKVVFLNFWATWCPPCR 311
Cdd:COG4232   312 --------------ALAEARaeGKPVFVDFTADWCVTCK 336
Redoxin pfam08534
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
 277-388 3.55e-13

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


Pssm-ID: 400717 [Multi-domain]  Cd Length: 148  Bit Score: 66.62  E-value: 3.55e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589196069 277 SYELKDQHDKIIKLEDYKGKVVFLNFWAT-WCPPCRGELPNIQKLYEKYRsDKHVAILTIVYPggqekgkSDL---KEFI 352
Cdd:pfam08534  10 TLPDAATDGNTVSLSDFKGKKVVLNFWPGaFCPTCSAEHPYLEKLNELYK-EKGVDVVAVNSD-------NDAffvKRFW 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1589196069 353 SDNALTVPVLFD----------DGFIYSTFGIGSMPTTFMLDKEGK 388
Cdd:pfam08534  82 GKEGLPFPFLSDgnaaftkalgLPIEEDASAGLRSPRYAVIDEDGK 127
PRK15412 PRK15412
thiol:disulfide interchange protein DsbE; Provisional
 294-387 1.10e-10

thiol:disulfide interchange protein DsbE; Provisional


Pssm-ID: 185310 [Multi-domain]  Cd Length: 185  Bit Score: 60.39  E-value: 1.10e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589196069 294 KGKVVFLNFWATWCPPCRGELPNIQKLyekyrSDKHVAILTIVYPGGQEKGKSDLKEFISDNALTvpvLFD-DGFIYSTF 372
Cdd:PRK15412   67 QGKPVLLNVWATWCPTCRAEHQYLNQL-----SAQGIRVVGMNYKDDRQKAISWLKELGNPYALS---LFDgDGMLGLDL 138

                          90
                  ....*....|....*
gi 1589196069 373 GIGSMPTTFMLDKEG 387
Cdd:PRK15412  139 GVYGAPETFLIDGNG 153
PRK14018 PRK14018
bifunctional peptide-methionine (S)-S-oxide reductase MsrA/peptide-methionine (R)-S-oxide ...
 257-400 2.85e-10

bifunctional peptide-methionine (S)-S-oxide reductase MsrA/peptide-methionine (R)-S-oxide reductase MsrB;


Pssm-ID: 184456 [Multi-domain]  Cd Length: 521  Bit Score: 61.81  E-value: 2.85e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589196069 257 GENKDEKNSEQEKALLQQLgSYELKDQHDKIIKledyKGKVVFLNFWATWCPPCRGELPNIqklyEKYRSDKHVA---IL 333
Cdd:PRK14018   23 SPKILDAGTATVPHTLSTL-KTADNRPASVYLK----KDKPTLIKFWASWCPLCLSELGET----EKWAQDAKFSsanLI 93

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589196069 334 TIVYPG-GQEKGKSDLKEFISD-NALTVPVLFD-DGFIYSTFGIGSMPTTFMLDKEGKPYGYIEGALTME 400
Cdd:PRK14018   94 TVASPGfLHEKKDGDFQKWYAGlDYPKLPVLTDnGGTLAQSLNISVYPSWAIIGKDGDVQRIVKGSISEA 163
TlpA_like_DipZ_like cd03012
TlpA-like family, DipZ-like subfamily; composed uncharacterized proteins containing a ...
 285-395 3.58e-10

TlpA-like family, DipZ-like subfamily; composed uncharacterized proteins containing a TlpA-like TRX domain. Some members show domain architectures similar to that of E. coli DipZ protein (also known as DsbD). The only eukaryotic members of the TlpA family belong to this subfamily. TlpA is a disulfide reductase known to have a crucial role in the biogenesis of cytochrome aa3.


Pssm-ID: 239310 [Multi-domain]  Cd Length: 126  Bit Score: 57.32  E-value: 3.58e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589196069 285 DKIIKLEDYKGKVVFLNFWATWCPPCRGELPNIQKLYEKYRSDKHVAI--LTIVYPggQEKGKSDLKEFISDNALTVPVL 362
Cdd:cd03012    13 DKPLSLAQLRGKVVLLDFWTYCCINCLHTLPYLTDLEQKYKDDGLVVIgvHSPEFA--FERDLANVKSAVLRYGITYPVA 90

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1589196069 363 FDDGF-IYSTFGIGSMPTTFMLDKEGKPYGYIEG 395
Cdd:cd03012    91 NDNDYaTWRAYGNQYWPALYLIDPTGNVRHVHFG 124
TlpA_like_ScsD_MtbDsbE cd03011
TlpA-like family, suppressor for copper sensitivity D protein (ScsD) and actinobacterial DsbE ...
 288-388 6.50e-10

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: 56.54  E-value: 6.50e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589196069 288 IKLEDYKGKVVFLNFWATWCPPCRGELPNIQKLyekyrsDKHVAILTIVYPGGQEkgkSDLKEFISDNALTVPVLFD-DG 366
Cdd:cd03011    13 FDLESLSGKPVLVYFWATWCPVCRFTSPTVNQL------AADYPVVSVALRSGDD---GAVARFMQKKGYGFPVINDpDG 83

                          90       100
                  ....*....|....*....|..
gi 1589196069 367 FIYSTFGIGSMPTTFMLDKEGK 388
Cdd:cd03011    84 VISARWGVSVTPAIVIVDPGGI 105
TryX_like_TryX_NRX cd03009
Tryparedoxin (TryX)-like family, TryX and nucleoredoxin (NRX) subfamily; TryX and NRX are ...
 288-388 1.46e-09

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


Pssm-ID: 239307 [Multi-domain]  Cd Length: 131  Bit Score: 55.75  E-value: 1.46e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589196069 288 IKLEDYKGKVVFLNFWATWCPPCRGELPNIQKLYEKYR-SDKHVAILTIvypgGQEKGKSDLKEFISDNA-LTVPvlFDD 365
Cdd:cd03009    11 VPVSSLEGKTVGLYFSASWCPPCRAFTPKLVEFYEKLKeSGKNFEIVFI----SWDRDEESFNDYFSKMPwLAVP--FSD 84

                          90       100
                  ....*....|....*....|....*..
gi 1589196069 366 G----FIYSTFGIGSMPTTFMLDKEGK 388
Cdd:cd03009    85 RerrsRLNRTFKIEGIPTLIILDADGE 111
dsbE TIGR00385
periplasmic protein thiol:disulfide oxidoreductases, DsbE subfamily; Involved in the ...
 294-407 2.06e-09

periplasmic protein thiol:disulfide oxidoreductases, DsbE subfamily; Involved in the biogenesis of c-type cytochromes as well as in disulfide bond formation in some periplasmic proteins. [Protein fate, Protein folding and stabilization]


Pssm-ID: 129481 [Multi-domain]  Cd Length: 173  Bit Score: 56.32  E-value: 2.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589196069 294 KGKVVFLNFWATWCPPCRGELPNIQKLyekyrSDKHVAILTIVYPGGQEKGKSDLKEFISDNALTvpvLFD-DGFIYSTF 372
Cdd:TIGR00385  62 QGKPVLLNVWASWCPPCRAEHPYLNEL-----AKQGLPIVGVDYKDDRQNAIKFLKELGNPYQLS---LFDpDGMLGLDL 133

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1589196069 373 GIGSMPTTFMLDKEGKPYGYIEGALTMEMMENMIL 407
Cdd:TIGR00385 134 GVYGAPETFLVDGNGVIRYRHAGPLNPEVWTEEFL 168
Thioredoxin_8 pfam13905
Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 295-388 3.01e-09

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: 53.85  E-value: 3.01e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589196069 295 GKVVFLNFWATWCPPCRGELPNIQKLYEKYRSDKHVAILTIvypgGQEKGKSDLKEFISDNALTVPVL-FDDGF---IYS 370
Cdd:pfam13905   1 GKVVLLYFGASWCKPCRRFTPLLKELYEKLKKKKNVEIVFV----SLDRDLEEFKDYLKKMPKDWLSVpFDDDErneLKR 76

                          90
                  ....*....|....*...
gi 1589196069 371 TFGIGSMPTTFMLDKEGK 388
Cdd:pfam13905  77 KYGVNAIPTLVLLDPNGE 94
TryX_like_family cd02964
Tryparedoxin (TryX)-like family; composed of TryX and related proteins including nucleoredoxin ...
 284-388 3.33e-09

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


Pssm-ID: 239262 [Multi-domain]  Cd Length: 132  Bit Score: 54.93  E-value: 3.33e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589196069 284 HDKIIKLEDYKGKVVFLNFWATWCPPCRGELPNIQKLYEKYR-SDKHVAILTIvypgGQEKGKSDLKEFISDNA--LTVP 360
Cdd:cd02964     6 GEGVVPVSALEGKTVGLYFSASWCPPCRAFTPKLVEFYEKLKeEGKNFEIVFV----SRDRSEESFNEYFSEMPpwLAVP 81

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1589196069 361 vlFDDGFIYS----TFGIGSMPTTFMLDKEGK 388
Cdd:cd02964    82 --FEDEELREllekQFKVEGIPTLVVLKPDGD 111
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 294-406 1.10e-07

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: 49.48  E-value: 1.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589196069 294 KGKVVFLNFWATWCPPCRGELPNIQKLYEKYrsdKHVAILTIvypggqekgksdlkefisdNALTVPVLFDDgfiystFG 373
Cdd:cd02947     9 SAKPVVVDFWAPWCGPCKAIAPVLEELAEEY---PKVKFVKV-------------------DVDENPELAEE------YG 60

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1589196069 374 IGSMPtTFMLDKEGKPYGYIEGALTMEMMENMI 406
Cdd:cd02947    61 VRSIP-TFLFFKNGKEVDRVVGADPKEELEEFL 92
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 295-406 1.31e-07

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: 49.43  E-value: 1.31e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589196069 295 GKVVFLNFWATWCPPCRGELPNIQKLYEKYRSDkhvaiLTIVypggqekgKSDLKEFISdnaltvpvlfddgfIYSTFGI 374
Cdd:COG3118    18 DKPVLVDFWAPWCGPCKMLAPVLEELAAEYGGK-----VKFV--------KVDVDENPE--------------LAAQFGV 70

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1589196069 375 GSMPtTFMLDKEGKPYGYIEGALTMEMMENMI 406
Cdd:COG3118    71 RSIP-TLLLFKDGQPVDRFVGALPKEQLREFL 101
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 281-400 2.75e-07

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: 48.38  E-value: 2.75e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589196069 281 KDQHDKIIKLEDykgKVVFLNFWATWCPPCRGELPNIQKLYEKYRSDKHVAiltivypggqekgKSDLKEfisdNALTVp 360
Cdd:pfam00085   7 DANFDEVVQKSS---KPVLVDFYAPWCGPCKMLAPEYEELAQEYKGNVVFA-------------KVDVDE----NPDLA- 65

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1589196069 361 vlfddgfiySTFGIGSMPTtFMLDKEGKPYGYIEGALTME 400
Cdd:pfam00085  66 ---------SKYGVRGYPT-LIFFKNGQPVDDYVGARPKD 95
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 296-410 3.68e-07

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: 48.05  E-value: 3.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589196069 296 KVVFLNFWATWCPPCRGELPNIQKLYEKYRSDkhVAIltivypggqekGKSDLKEfisdnaltvpvlfdDGFIYSTFGIG 375
Cdd:TIGR01068  15 KPVLVDFWAPWCGPCKMIAPILEELAKEYEGK--VKF-----------VKLNVDE--------------NPDIAAKYGIR 67

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1589196069 376 SMPtTFMLDKEGKPYGYIEGALTMEMMENMILKTL 410
Cdd:TIGR01068  68 SIP-TLLLFKNGKEVDRSVGALPKAALKQLINKNL 101
DsbD_2 pfam13386
Cytochrome C biogenesis protein transmembrane region;
76-222 1.65e-06

Cytochrome C biogenesis protein transmembrane region;


Pssm-ID: 463866  Cd Length: 199  Bit Score: 48.38  E-value: 1.65e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589196069  76 ISITLISSFFRDHMSVFIkvgGILIIVLGLFQLGFFKSNFLGKT-----RRLPFTLKKEMNLLLAFLMGFtfSFAWTPCi 150
Cdd:pfam13386  60 LSLAGQLAGLRGVLGVLL---GLLLLLLGLYLLGLPGLLKLERLgkglwRLLSPLAKRLKSPGGAFLLGL--LWGLLPC- 133

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1589196069 151 gPALSSILLLANSSQNLWMSNFLMVIYALGlTIPFLLIGIFtdsILNWLSnhKSIMNYTVKLGAIILIFFGV 222
Cdd:pfam13386 134 -GLVYSALLYAAATGSALEGALVMLAFGLG-TLPALLLFGL---LAGFLS--KKLRKRLQRLAGVLLILLGI 198
Thioredoxin_2 pfam13098
Thioredoxin-like domain;
294-406 3.70e-06

Thioredoxin-like domain;


Pssm-ID: 379034 [Multi-domain]  Cd Length: 103  Bit Score: 45.11  E-value: 3.70e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589196069 294 KGKVVFLNFWATWCPPCRG------ELPNIQKLYEKYRSDKHVAILTIVYPGGQEKGKSDLKEFisdnaltvpvlfddgf 367
Cdd:pfam13098   3 NGKPVLVVFTDPDCPYCKKlkkellEDPDVTVYLGPNFVFIAVNIWCAKEVAKAFTDILENKEL---------------- 66

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1589196069 368 iYSTFGIGSMPTTFMLDKEGKpYGYIEGALTMEMMENMI 406
Cdd:pfam13098  67 -GRKYGVRGTPTIVFFDGKGE-LLRLPGYVPAEEFLALL 103
dipZ PRK00293
thiol:disulfide interchange protein precursor; Provisional
 12-196 1.44e-05

thiol:disulfide interchange protein precursor; Provisional


Pssm-ID: 234717 [Multi-domain]  Cd Length: 571  Bit Score: 47.13  E-value: 1.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589196069  12 SILMVFMEGV-LSFlSPCVLPLLPVYMGYLIGsdvNNKQIRKKRFvifFTLSFIFgiftaILLMNISITL----ISSF-- 84
Cdd:PRK00293  168 SLLWFFLIGIgLAF-TPCVLPMYPILSGIVLG---GKQRLSTARA---LLLSFVY-----VQGMALTYTLlglvVAAAgl 235

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589196069  85 -FR---DHMSVFIkVGGILIIVLGLFQLGFFksnflgkTRRLPFTLKKEMNLLL----------AFLMGFTFSFAWTPCI 150
Cdd:PRK00293  236 qFQaalQHPYVLI-GLSILFVLLALSMFGLF-------TLQLPSSLQTRLTLLSnrqqggslggVFVMGAISGLICSPCT 307

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1589196069 151 GPALSSILLLANSSQNLWMSNFLMVIYALGLTIPFLLIGIFTDSIL 196
Cdd:PRK00293  308 TAPLSGALLYIAQSGDLLLGGLTLYLLALGMGLPLILITTFGNKLL 353
CcdA COG0785
Cytochrome c biogenesis protein CcdA [Energy production and conversion, Posttranslational ...
 129-225 3.45e-05

Cytochrome c biogenesis protein CcdA [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440548 [Multi-domain]  Cd Length: 193  Bit Score: 44.45  E-value: 3.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589196069 129 EMNLLLAFLMGFtFSFAwTPCIGPALSSIL--LLANSSQNLWMSNFLMVIYALGLTIPFLLIGIFTDSILNWLSNHKSIM 206
Cdd:COG0785     2 LLSLLLAFLAGL-LSFL-SPCVLPLLPGYLsyLTGLSRASRRRALLRALLFVLGFSLVFVLLGALASALGSLLGQYQDLL 79

                          90
                  ....*....|....*....
gi 1589196069 207 NYtvkLGAIILIFFGVSMV 225
Cdd:COG0785    80 RI---VAGVLLILFGLVLL 95
Sco1 COG1999
Cytochrome oxidase Cu insertion factor, SCO1/SenC/PrrC family [Posttranslational modification, ...
 279-335 3.73e-05

Cytochrome oxidase Cu insertion factor, SCO1/SenC/PrrC family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441602  Cd Length: 156  Bit Score: 43.74  E-value: 3.73e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589196069 279 ELKDQHDKIIKLEDYKGKVVFLNFWATWCP-PCRGELPNIQKLYEKYRSD--KHVAILTI 335
Cdd:COG1999     4 TLTDQDGKPVTLADLRGKPVLVFFGYTSCPdVCPTTLANLAQVQEALGEDggDDVQVLFI 63
PRX_like2 cd02970
Peroxiredoxin (PRX)-like 2 family; hypothetical proteins that show sequence similarity to PRXs. ...
 278-400 6.27e-05

Peroxiredoxin (PRX)-like 2 family; hypothetical proteins that show sequence similarity to PRXs. Members of this group contain a CXXC motif, similar to TRX. The second cysteine in the motif corresponds to the peroxidatic cysteine of PRX, however, these proteins do not contain the other two residues of the catalytic triad of PRX. PRXs confer a protective antioxidant role in cells through their peroxidase activity in which hydrogen peroxide, peroxynitrate, and organic hydroperoxides are reduced and detoxified using reducing equivalents derived from either thioredoxin, glutathione, trypanothione and AhpF. TRXs alter the redox state of target proteins by catalyzing the reduction of their disulfide bonds via the CXXC motif using reducing equivalents derived from either NADPH or ferredoxins.


Pssm-ID: 239268 [Multi-domain]  Cd Length: 149  Bit Score: 42.73  E-value: 6.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589196069 278 YELKDQHDKIIKLEDYKGK----VVFLNFWatWCPPCRGELPNIQKLYEKYRsDKHVAILtIVYPGGQEKgksdLKEFIS 353
Cdd:cd02970     5 FELPDAGGETVTLSALLGEgpvvVVFYRGF--GCPFCREYLRALSKLLPELD-ALGVELV-AVGPESPEK----LEAFDK 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1589196069 354 DNALTVPVLFD-DGFIYSTFGIGSMPTT------FMLDKEGKPYGYIEGALTME 400
Cdd:cd02970    77 GKFLPFPVYADpDRKLYRALGLVRSLPWsntpraLWKNAAIGFRGNDEGDGLQL 130
PLN02919 PLN02919
haloacid dehalogenase-like hydrolase family protein
 292-395 1.30e-04

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215497 [Multi-domain]  Cd Length: 1057  Bit Score: 44.46  E-value: 1.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589196069  292 DYKGKVVFLNFWATWCPPCRGELPNIQKLYEKYRSdkhvAILTIVypgGQEKGKSDLK---EFISDNAL----TVPVLFD 364
Cdd:PLN02919   417 DLKGKVVILDFWTYCCINCMHVLPDLEFLEKKYKD----QPFTVV---GVHSAKFDNEkdlEAIRNAVLryniSHPVVND 489

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1589196069  365 -DGFIYSTFGIGSMPTTFMLDKEGKPYGYIEG 395
Cdd:PLN02919   490 gDMYLWRELGVSSWPTFAVVSPNGKLIAQLSG 521
GSH_Peroxidase cd00340
Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a ...
 277-355 2.26e-04

Glutathione (GSH) peroxidase family; tetrameric selenoenzymes that catalyze the reduction of a variety of hydroperoxides including lipid peroxidases, using GSH as a specific electron donor substrate. GSH peroxidase contains one selenocysteine residue per subunit, which is involved in catalysis. Different isoenzymes are known in mammals,which are involved in protection against reactive oxygen species, redox regulation of many metabolic processes, peroxinitrite scavenging, and modulation of inflammatory processes.


Pssm-ID: 238207 [Multi-domain]  Cd Length: 152  Bit Score: 41.35  E-value: 2.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589196069 277 SYELKDQHDKIIKLEDYKGKVVFL-NFwATWCppcrGELPNI---QKLYEKYRsDKHVAILtiVYP----GGQEKGKS-D 347
Cdd:cd00340     4 DFSVKDIDGEPVSLSKYKGKVLLIvNV-ASKC----GFTPQYeglEALYEKYK-DRGLVVL--GFPcnqfGGQEPGSNeE 75


                  ....*...
gi 1589196069 348 LKEFISDN 355
Cdd:cd00340    76 IKEFCETN 83
PDI_a_family cd02961
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ...
 281-335 4.15e-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: 39.52  E-value: 4.15e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1589196069 281 KDQHDKIIKledyKGKVVFLNFWATWCPPCRGELPNIQKLYEKYRSDKHVAILTI 335
Cdd:cd02961     5 DDNFDELVK----DSKDVLVEFYAPWCGHCKALAPEYEKLAKELKGDGKVVVAKV 55
PRX_AhpE_like cd03018
Peroxiredoxin (PRX) family, AhpE-like subfamily; composed of proteins similar to Mycobacterium ...
 278-364 9.57e-04

Peroxiredoxin (PRX) family, AhpE-like subfamily; composed of proteins similar to Mycobacterium tuberculosis AhpE. AhpE is described as a 1-cys PRX because of the absence of a resolving cysteine. The structure and sequence of AhpE, however, show greater similarity to 2-cys PRXs than 1-cys PRXs. PRXs are thiol-specific antioxidant (TSA) proteins that confer a protective role in cells through their peroxidase activity in which hydrogen peroxide, peroxynitrate, and organic hydroperoxides are reduced and detoxified using reducing equivalents derived from either thioredoxin, glutathione, trypanothione and AhpF. The first step of catalysis is the nucleophilic attack by the peroxidatic cysteine on the peroxide leading to the formation of a cysteine sulfenic acid intermediate. The absence of a resolving cysteine suggests that functional AhpE is regenerated by an external reductant. The solution behavior and crystal structure of AhpE show that it forms dimers and octamers.


Pssm-ID: 239316 [Multi-domain]  Cd Length: 149  Bit Score: 39.56  E-value: 9.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589196069 278 YELKDQHDKIIKLEDYKG--KVVFLNFWATWCPPCRGELPNIQKLYEKYrSDKHVAILTI-VYPggqekgKSDLKEFISD 354
Cdd:cd03018    10 FELPDQNGQEVRLSEFRGrkPVVLVFFPLAFTPVCTKELCALRDSLELF-EAAGAEVLGIsVDS------PFSLRAWAEE 82

                          90
                  ....*....|
gi 1589196069 355 NALTVPVLFD 364
Cdd:cd03018    83 NGLTFPLLSD 92
trxA PRK09381
thioredoxin TrxA;
285-335 2.33e-03

thioredoxin TrxA;


Pssm-ID: 181812 [Multi-domain]  Cd Length: 109  Bit Score: 37.35  E-value: 2.33e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1589196069 285 DKIIKLED--------YKGKVVFLNFWATWCPPCRGELPNIQKLYEKYRSDKHVAILTI 335
Cdd:PRK09381    3 DKIIHLTDdsfdtdvlKADGAILVDFWAEWCGPCKMIAPILDEIADEYQGKLTVAKLNI 61
SCO cd02968
SCO (an acronym for Synthesis of Cytochrome c Oxidase) family; composed of proteins similar to ...
 276-323 4.58e-03

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


Pssm-ID: 239266  Cd Length: 142  Bit Score: 37.20  E-value: 4.58e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1589196069 276 GSYELKDQHDKIIKLEDYKGKVVFLNFWATWCP-PCRGELPNIQKLYEK 323
Cdd:cd02968     3 PDFTLTDQDGRPVTLSDLKGKPVLVYFGYTHCPdVCPTTLANLAQALKQ 51
 
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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