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Conserved domains on  [gi|1228053264|ref|WP_094147287|]
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MULTISPECIES: co-chaperone YbbN [unclassified Vibrio]

Protein Classification

thioredoxin family protein( domain architecture ID 11459707)

thioredoxin family protein may function as a thiol disulfide reductase that catalyzes the reduction of protein disulfide bonds using an active site dithiol, present in a CXXC motif

CATH:  3.40.30.10
EC:  1.8.-.-
Gene Ontology:  GO:0015035
PubMed:  11441809|15558583|12074972|30367780

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ybbN cd02956
ybbN protein family; ybbN is a hypothetical protein containing a redox-inactive TRX-like ...
 12-107 1.65e-32

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: 115.06  E-value: 1.65e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228053264  12 HNFREVFERSVETPILFYFWAPMNQESVQLIPELQSVAQQHSGAFTLAILNCQQEQQVAAQFGVQALPTIALFINGQAVD 91
Cdd:cd02956     1 QNFQQVLQESTQVPVVVDFWAPRSPPSKELLPLLERLAEEYQGQFVLAKVNCDAQPQIAQQFGVQALPTVYLFAAGQPVD 80

                          90
                  ....*....|....*.
gi 1228053264  92 GLAGAQTIETVNTMLN 107
Cdd:cd02956    81 GFQGAQPEEQLRQMLD 96
TPR_20 pfam14561
Tetratricopeptide repeat;
195-284 2.01e-29

Tetratricopeptide repeat;


:

Pssm-ID: 434039 [Multi-domain]  Cd Length: 90  Bit Score: 106.82  E-value: 2.01e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228053264 195 QAADSPEIQALEEIFSAEPNNAHIASELALQYHQVNRNEEALELLWSFLQSDLNCLDGGLKKVFMDILSALGQGNSVASL 274
Cdd:pfam14561   1 QAADAPELAALEARLAADPDDLDARLDLALALHAAGRNEEALELLLEILRRDRNWNDGAARKQLLDIFEALGPGDPLVAK 80

                          90
                  ....*....|
gi 1228053264 275 YRRKLYSLLY 284
Cdd:pfam14561  81 YRRKLSSLLF 90
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 111-246 2.17e-05

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


:

Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 45.11  E-value: 2.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228053264 111 PSHDEVSLQQALTLIEQTQHSQALPLLLSLPDDMKAKAEVKLALADVFLETQQYEAAETELERIpLEYQDGYYKGLIAKL 190
Cdd:COG2956   107 PDDAEALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKA-LKLDPDCARALLLLA 185

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1228053264 191 ELHKQAADSPE-IQALEEIFSAEPNNAHIASELALQYHQVNRNEEALELLWSFLQSD 246
Cdd:COG2956   186 ELYLEQGDYEEaIAALERALEQDPDYLPALPRLAELYEKLGDPEEALELLRKALELD 242
 
Name Accession Description Interval E-value
ybbN cd02956
ybbN protein family; ybbN is a hypothetical protein containing a redox-inactive TRX-like ...
 12-107 1.65e-32

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: 115.06  E-value: 1.65e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228053264  12 HNFREVFERSVETPILFYFWAPMNQESVQLIPELQSVAQQHSGAFTLAILNCQQEQQVAAQFGVQALPTIALFINGQAVD 91
Cdd:cd02956     1 QNFQQVLQESTQVPVVVDFWAPRSPPSKELLPLLERLAEEYQGQFVLAKVNCDAQPQIAQQFGVQALPTVYLFAAGQPVD 80

                          90
                  ....*....|....*.
gi 1228053264  92 GLAGAQTIETVNTMLN 107
Cdd:cd02956    81 GFQGAQPEEQLRQMLD 96
TPR_20 pfam14561
Tetratricopeptide repeat;
195-284 2.01e-29

Tetratricopeptide repeat;


Pssm-ID: 434039 [Multi-domain]  Cd Length: 90  Bit Score: 106.82  E-value: 2.01e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228053264 195 QAADSPEIQALEEIFSAEPNNAHIASELALQYHQVNRNEEALELLWSFLQSDLNCLDGGLKKVFMDILSALGQGNSVASL 274
Cdd:pfam14561   1 QAADAPELAALEARLAADPDDLDARLDLALALHAAGRNEEALELLLEILRRDRNWNDGAARKQLLDIFEALGPGDPLVAK 80

                          90
                  ....*....|
gi 1228053264 275 YRRKLYSLLY 284
Cdd:pfam14561  81 YRRKLSSLLF 90
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 5-110 6.15e-28

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: 103.36  E-value: 6.15e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228053264   5 YIVEVNQHNFREVFERSvETPILFYFWAPMNQESVQLIPELQSVAQQHSGAFTLAILNCQQEQQVAAQFGVQALPTIALF 84
Cdd:COG3118     1 AVVELTDENFEEEVLES-DKPVLVDFWAPWCGPCKMLAPVLEELAAEYGGKVKFVKVDVDENPELAAQFGVRSIPTLLLF 79

                          90       100
                  ....*....|....*....|....*.
gi 1228053264  85 INGQAVDGLAGAQTIETVNTMLNKHL 110
Cdd:COG3118    80 KDGQPVDRFVGALPKEQLREFLDKVL 105
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 9-110 5.29e-17

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: 74.63  E-value: 5.29e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228053264   9 VNQHNFREVFERSvETPILFYFWAP------MnqesvqLIPELQSVAQQHSGAFTLAILNCQQEQQVAAQFGVQALPTIA 82
Cdd:TIGR01068   1 LTDANFDETIASS-DKPVLVDFWAPwcgpckM------IAPILEELAKEYEGKVKFVKLNVDENPDIAAKYGIRSIPTLL 73

                          90       100
                  ....*....|....*....|....*...
gi 1228053264  83 LFINGQAVDGLAGAQTIETVNTMLNKHL 110
Cdd:TIGR01068  74 LFKNGKEVDRSVGALPKAALKQLINKNL 101
PRK10996 PRK10996
thioredoxin 2; Provisional
 6-96 9.14e-14

thioredoxin 2; Provisional


Pssm-ID: 182889 [Multi-domain]  Cd Length: 139  Bit Score: 67.02  E-value: 9.14e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228053264   6 IVEVNQHNFREVFERsvETPILFYFWAPMNQESVQLIPELQSVAQQHSGAFTLAILNCQQEQQVAAQFGVQALPTIALFI 85
Cdd:PRK10996   37 VINATGETLDKLLQD--DLPVVIDFWAPWCGPCRNFAPIFEDVAAERSGKVRFVKVNTEAERELSARFRIRSIPTIMIFK 114

                          90
                  ....*....|.
gi 1228053264  86 NGQAVDGLAGA 96
Cdd:PRK10996  115 NGQVVDMLNGA 125
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 6-102 1.17e-11

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: 59.94  E-value: 1.17e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228053264   6 IVEVNQHNFREVFeRSVETPILFYFWAPMNQESVQLIPELQSVAQQHSGAFTLAILNCQQEQQVAAQFGVQALPTIALFI 85
Cdd:pfam00085   2 VVVLTDANFDEVV-QKSSKPVLVDFYAPWCGPCKMLAPEYEELAQEYKGNVVFAKVDVDENPDLASKYGVRGYPTLIFFK 80

                          90
                  ....*....|....*..
gi 1228053264  86 NGQAVDGLAGAQTIETV 102
Cdd:pfam00085  81 NGQPVDDYVGARPKDAL 97
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 147-279 1.88e-06

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


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 48.19  E-value: 1.88e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228053264 147 KAEVKLALADVFLETQQYEAAETELERIpLEYQDGYYKGLIAKLELHKQAADSPE-IQALEEIFSAEPNNAHIASELALQ 225
Cdd:COG2956    75 RAEALLELAQDYLKAGLLDRAEELLEKL-LELDPDDAEALRLLAEIYEQEGDWEKaIEVLERLLKLGPENAHAYCELAEL 153

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1228053264 226 YHQVNRNEEALELLWSFLQSDLNCLDGGLKKVfmDILSALGQGNSVASLYRRKL 279
Cdd:COG2956   154 YLEQGDYDEAIEALEKALKLDPDCARALLLLA--ELYLEQGDYEEAIAALERAL 205
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 111-246 2.17e-05

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


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 45.11  E-value: 2.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228053264 111 PSHDEVSLQQALTLIEQTQHSQALPLLLSLPDDMKAKAEVKLALADVFLETQQYEAAETELERIpLEYQDGYYKGLIAKL 190
Cdd:COG2956   107 PDDAEALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKA-LKLDPDCARALLLLA 185

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1228053264 191 ELHKQAADSPE-IQALEEIFSAEPNNAHIASELALQYHQVNRNEEALELLWSFLQSD 246
Cdd:COG2956   186 ELYLEQGDYEEaIAALERALEQDPDYLPALPRLAELYEKLGDPEEALELLRKALELD 242
TPR_19 pfam14559
Tetratricopeptide repeat;
148-190 7.57e-04

Tetratricopeptide repeat;


Pssm-ID: 434038 [Multi-domain]  Cd Length: 65  Bit Score: 37.18  E-value: 7.57e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1228053264 148 AEVKLALADVFLETQQYEAAETELERIPLEYQ-DGYYKGLIAKL 190
Cdd:pfam14559  22 AEARLGLAEALLALGRLDEAEALLAALPAADPdDPRYAALLAKL 65
 
Name Accession Description Interval E-value
ybbN cd02956
ybbN protein family; ybbN is a hypothetical protein containing a redox-inactive TRX-like ...
 12-107 1.65e-32

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: 115.06  E-value: 1.65e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228053264  12 HNFREVFERSVETPILFYFWAPMNQESVQLIPELQSVAQQHSGAFTLAILNCQQEQQVAAQFGVQALPTIALFINGQAVD 91
Cdd:cd02956     1 QNFQQVLQESTQVPVVVDFWAPRSPPSKELLPLLERLAEEYQGQFVLAKVNCDAQPQIAQQFGVQALPTVYLFAAGQPVD 80

                          90
                  ....*....|....*.
gi 1228053264  92 GLAGAQTIETVNTMLN 107
Cdd:cd02956    81 GFQGAQPEEQLRQMLD 96
TPR_20 pfam14561
Tetratricopeptide repeat;
195-284 2.01e-29

Tetratricopeptide repeat;


Pssm-ID: 434039 [Multi-domain]  Cd Length: 90  Bit Score: 106.82  E-value: 2.01e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228053264 195 QAADSPEIQALEEIFSAEPNNAHIASELALQYHQVNRNEEALELLWSFLQSDLNCLDGGLKKVFMDILSALGQGNSVASL 274
Cdd:pfam14561   1 QAADAPELAALEARLAADPDDLDARLDLALALHAAGRNEEALELLLEILRRDRNWNDGAARKQLLDIFEALGPGDPLVAK 80

                          90
                  ....*....|
gi 1228053264 275 YRRKLYSLLY 284
Cdd:pfam14561  81 YRRKLSSLLF 90
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 5-110 6.15e-28

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: 103.36  E-value: 6.15e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228053264   5 YIVEVNQHNFREVFERSvETPILFYFWAPMNQESVQLIPELQSVAQQHSGAFTLAILNCQQEQQVAAQFGVQALPTIALF 84
Cdd:COG3118     1 AVVELTDENFEEEVLES-DKPVLVDFWAPWCGPCKMLAPVLEELAAEYGGKVKFVKVDVDENPELAAQFGVRSIPTLLLF 79

                          90       100
                  ....*....|....*....|....*.
gi 1228053264  85 INGQAVDGLAGAQTIETVNTMLNKHL 110
Cdd:COG3118    80 KDGQPVDRFVGALPKEQLREFLDKVL 105
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 9-110 5.29e-17

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: 74.63  E-value: 5.29e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228053264   9 VNQHNFREVFERSvETPILFYFWAP------MnqesvqLIPELQSVAQQHSGAFTLAILNCQQEQQVAAQFGVQALPTIA 82
Cdd:TIGR01068   1 LTDANFDETIASS-DKPVLVDFWAPwcgpckM------IAPILEELAKEYEGKVKFVKLNVDENPDIAAKYGIRSIPTLL 73

                          90       100
                  ....*....|....*....|....*...
gi 1228053264  83 LFINGQAVDGLAGAQTIETVNTMLNKHL 110
Cdd:TIGR01068  74 LFKNGKEVDRSVGALPKAALKQLINKNL 101
PRK10996 PRK10996
thioredoxin 2; Provisional
 6-96 9.14e-14

thioredoxin 2; Provisional


Pssm-ID: 182889 [Multi-domain]  Cd Length: 139  Bit Score: 67.02  E-value: 9.14e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228053264   6 IVEVNQHNFREVFERsvETPILFYFWAPMNQESVQLIPELQSVAQQHSGAFTLAILNCQQEQQVAAQFGVQALPTIALFI 85
Cdd:PRK10996   37 VINATGETLDKLLQD--DLPVVIDFWAPWCGPCRNFAPIFEDVAAERSGKVRFVKVNTEAERELSARFRIRSIPTIMIFK 114

                          90
                  ....*....|.
gi 1228053264  86 NGQAVDGLAGA 96
Cdd:PRK10996  115 NGQVVDMLNGA 125
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 13-107 2.57e-12

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: 61.42  E-value: 2.57e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228053264  13 NFREVFERSveTPILFYFWAPMNQESVQLIPELQSVAQQHsGAFTLAILNCQQEQQVAAQFGVQALPTIALFINGQAVDG 92
Cdd:cd02947     2 EFEELIKSA--KPVVVDFWAPWCGPCKAIAPVLEELAEEY-PKVKFVKVDVDENPELAEEYGVRSIPTFLFFKNGKEVDR 78

                          90
                  ....*....|....*
gi 1228053264  93 LAGAQTIETVNTMLN 107
Cdd:cd02947    79 VVGADPKEELEEFLE 93
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 6-102 1.17e-11

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: 59.94  E-value: 1.17e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228053264   6 IVEVNQHNFREVFeRSVETPILFYFWAPMNQESVQLIPELQSVAQQHSGAFTLAILNCQQEQQVAAQFGVQALPTIALFI 85
Cdd:pfam00085   2 VVVLTDANFDEVV-QKSSKPVLVDFYAPWCGPCKMLAPEYEELAQEYKGNVVFAKVDVDENPDLASKYGVRGYPTLIFFK 80

                          90
                  ....*....|....*..
gi 1228053264  86 NGQAVDGLAGAQTIETV 102
Cdd:pfam00085  81 NGQPVDDYVGARPKDAL 97
PDI_a_MPD1_like cd03002
PDI family, MPD1-like subfamily; composed of eukaryotic proteins similar to Saccharomyces ...
 6-84 2.95e-10

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


Pssm-ID: 239300 [Multi-domain]  Cd Length: 109  Bit Score: 56.22  E-value: 2.95e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228053264   6 IVEVNQHNFREVFERSvETPILFYFWAPMNQESVQLIPELQSVAQQHSGAFTLAILNCQQEQ--QVAAQFGVQALPTIAL 83
Cdd:cd03002     2 VYELTPKNFDKVVHNT-NYTTLVEFYAPWCGHCKNLKPEYAKAAKELDGLVQVAAVDCDEDKnkPLCGKYGVQGFPTLKV 80


                  .
gi 1228053264  84 F 84
Cdd:cd03002    81 F 81
PDI_a_family cd02961
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ...
 7-87 4.40e-09

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: 53.00  E-value: 4.40e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228053264   7 VEVNQHNFREVFERSVETPILFYfwAPMNQESVQLIPELQSVAQ--QHSGAFTLAILNCQQEQQVAAQFGVQALPTIALF 84
Cdd:cd02961     1 VELTDDNFDELVKDSKDVLVEFY--APWCGHCKALAPEYEKLAKelKGDGKVVVAKVDCTANNDLCSEYGVRGYPTIKLF 78


                  ...
gi 1228053264  85 ING 87
Cdd:cd02961    79 PNG 81
trxA PRK09381
thioredoxin TrxA;
30-110 1.87e-07

thioredoxin TrxA;


Pssm-ID: 181812 [Multi-domain]  Cd Length: 109  Bit Score: 48.52  E-value: 1.87e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228053264  30 FWAPMNQESVQLIPELQSVAQQHSGAFTLAILNCQQEQQVAAQFGVQALPTIALFINGQAVDGLAGAQTIETVNTMLNKH 109
Cdd:PRK09381   28 FWAEWCGPCKMIAPILDEIADEYQGKLTVAKLNIDQNPGTAPKYGIRGIPTLLLFKNGEVAATKVGALSKGQLKEFLDAN 107


                  .
gi 1228053264 110 L 110
Cdd:PRK09381  108 L 108
PDI_a_P5 cd03001
PDIa family, P5 subfamily; composed of eukaryotic proteins similar to human P5, a PDI-related ...
 6-84 3.02e-07

PDIa family, P5 subfamily; composed of eukaryotic proteins similar to human P5, a PDI-related protein with a domain structure of aa'b (where a and a' are redox active TRX domains and b is a redox inactive TRX-like domain). Like PDI, P5 is located in the endoplasmic reticulum (ER) and displays both isomerase and chaperone activities, which are independent of each other. Compared to PDI, the isomerase and chaperone activities of P5 are lower. The first cysteine in the CXXC motif of both redox active domains in P5 is necessary for isomerase activity. The P5 gene was first isolated as an amplified gene from a hydroxyurea-resistant hamster cell line. The zebrafish P5 homolog has been implicated to play a critical role in establishing left/right asymmetries in the embryonic midline. Some members of this subfamily are P5-like proteins containing only one redox active TRX domain.


Pssm-ID: 239299 [Multi-domain]  Cd Length: 103  Bit Score: 47.67  E-value: 3.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228053264   6 IVEVNQHNF-REVFERSVETPILFYfwAPMNQESVQLIPELQSVAQQHSGAFTLAILNCQQEQQVAAQFGVQALPTIALF 84
Cdd:cd03001     2 VVELTDSNFdKKVLNSDDVWLVEFY--APWCGHCKNLAPEWKKAAKALKGIVKVGAVDADVHQSLAQQYGVRGFPTIKVF 79
PDI_a_ERdj5_C cd03004
PDIa family, C-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 4-84 3.23e-07

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


Pssm-ID: 239302 [Multi-domain]  Cd Length: 104  Bit Score: 47.67  E-value: 3.23e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228053264   4 PYIVEVNQHNFREVFERSVETPILFYF--WAPMNQesvQLIPELQSVAQQHSGAFTLAILNCQQEQQVAAQFGVQALPTI 81
Cdd:cd03004     1 PSVITLTPEDFPELVLNRKEPWLVDFYapWCGPCQ---ALLPELRKAARALKGKVKVGSVDCQKYESLCQQANIRAYPTI 77


                  ...
gi 1228053264  82 ALF 84
Cdd:cd03004    78 RLY 80
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 147-279 1.88e-06

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


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 48.19  E-value: 1.88e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228053264 147 KAEVKLALADVFLETQQYEAAETELERIpLEYQDGYYKGLIAKLELHKQAADSPE-IQALEEIFSAEPNNAHIASELALQ 225
Cdd:COG2956    75 RAEALLELAQDYLKAGLLDRAEELLEKL-LELDPDDAEALRLLAEIYEQEGDWEKaIEVLERLLKLGPENAHAYCELAEL 153

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1228053264 226 YHQVNRNEEALELLWSFLQSDLNCLDGGLKKVfmDILSALGQGNSVASLYRRKL 279
Cdd:COG2956   154 YLEQGDYDEAIEALEKALKLDPDCARALLLLA--ELYLEQGDYEEAIAALERAL 205
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 49-267 5.15e-06

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 47.68  E-value: 5.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228053264  49 AQQHSGAFTLAILNCQQEQQVAAQFGVQALPTIALFINGQAVDGLAGAQTIETVNTMLN-----------KHLPSHDEVS 117
Cdd:COG3914     2 AAAALLALAALAAAALLAAAAAAELALAAELEAAALAAALGLALLLLAALAEAAAAALLalaageaaaaaAALLLLAALL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228053264 118 LQQALTLIEQTQHSQALPLLLSLPDDMKAKAEVKLALADVFLETQQYEAAETELERIpLEYQDGYYKGLIAKLELHKQAA 197
Cdd:COG3914    82 ELAALLLQALGRYEEALALYRRALALNPDNAEALFNLGNLLLALGRLEEALAALRRA-LALNPDFAEAYLNLGEALRRLG 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1228053264 198 DSPE-IQALEEIFSAEPNNAHIASELALQYHQVNRNEEALELLWSFLQsdlncLDGGLKKVFMDILSALGQ 267
Cdd:COG3914   161 RLEEaIAALRRALELDPDNAEALNNLGNALQDLGRLEEAIAAYRRALE-----LDPDNADAHSNLLFALRQ 226
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 111-246 2.17e-05

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


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 45.11  E-value: 2.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228053264 111 PSHDEVSLQQALTLIEQTQHSQALPLLLSLPDDMKAKAEVKLALADVFLETQQYEAAETELERIpLEYQDGYYKGLIAKL 190
Cdd:COG2956   107 PDDAEALRLLAEIYEQEGDWEKAIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKA-LKLDPDCARALLLLA 185

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1228053264 191 ELHKQAADSPE-IQALEEIFSAEPNNAHIASELALQYHQVNRNEEALELLWSFLQSD 246
Cdd:COG2956   186 ELYLEQGDYEEaIAALERALEQDPDYLPALPRLAELYEKLGDPEEALELLRKALELD 242
Thioredoxin_6 pfam13848
Thioredoxin-like domain;
4-84 2.20e-05

Thioredoxin-like domain;


Pssm-ID: 463999 [Multi-domain]  Cd Length: 184  Bit Score: 44.27  E-value: 2.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228053264   4 PYIVEVNQHNFREVFERSVETPILFYFwaPMNQESV-QLIPELQSVAQQHSGAFTLAILNCQQEQQVAAQFGVQ--ALPT 80
Cdd:pfam13848  77 PLVREFTPENAEELFEEGIPPLLLLFL--KKDDESTeEFKKALEKVAKKFRGKINFALVDAKSFGRPLEYFGLSesDLPV 154


                  ....
gi 1228053264  81 IALF 84
Cdd:pfam13848 155 IVIV 158
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 6-87 6.70e-05

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


Pssm-ID: 273457 [Multi-domain]  Cd Length: 462  Bit Score: 43.89  E-value: 6.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228053264   6 IVEVNQHNFREVFeRSVETpILFYFWAPMNQESVQLIPELQSVAQ---QHSGAFTLAILNCQQEQQVAAQFGVQALPTIA 82
Cdd:TIGR01130   3 VLVLTKDNFDDFI-KSHEF-VLVEFYAPWCGHCKSLAPEYEKAADelkKKGPPIKLAKVDATEEKDLAQKYGVSGYPTLK 80


                  ....*
gi 1228053264  83 LFING 87
Cdd:TIGR01130  81 IFRNG 85
PDI_a_ERp44 cd02996
PDIa family, endoplasmic reticulum protein 44 (ERp44) subfamily; ERp44 is an ER-resident ...
 6-90 8.62e-05

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


Pssm-ID: 239294 [Multi-domain]  Cd Length: 108  Bit Score: 40.84  E-value: 8.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228053264   6 IVEVNQHNFREVFERSVETPILFYF-WAPMNQESVQLIPELQSVAQQ---HSGAFTLAILNCQQEQQVAAQFGVQALPTI 81
Cdd:cd02996     3 IVSLTSGNIDDILQSAELVLVNFYAdWCRFSQMLHPIFEEAAAKIKEefpDAGKVVWGKVDCDKESDIADRYRINKYPTL 82


                  ....*....
gi 1228053264  82 ALFINGQAV 90
Cdd:cd02996    83 KLFRNGMMM 91
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 148-239 1.32e-04

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


Pssm-ID: 443378 [Multi-domain]  Cd Length: 131  Bit Score: 40.76  E-value: 1.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228053264 148 AEVKLALADVFLETQQYEAAETELERIpLEYQDGYYKGLIAKLELHKQAADSPE-IQALEEIFSAEPNNAHIASELALQY 226
Cdd:COG4235    17 AEGWLLLGRAYLRLGRYDEALAAYEKA-LRLDPDNADALLDLAEALLAAGDTEEaEELLERALALDPDNPEALYLLGLAA 95

                          90
                  ....*....|...
gi 1228053264 227 HQVNRNEEALELL 239
Cdd:COG4235    96 FQQGDYAEAIAAW 108
TRX_PICOT cd02984
TRX domain, PICOT (for PKC-interacting cousin of TRX) subfamily; PICOT is a protein that ...
 14-96 1.70e-04

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: 39.95  E-value: 1.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228053264  14 FREVFERSVETPILFYFWAPMNQESVQLIPELQSVAQQHSGAFTLAILNCQQEQQVAAQFGVQALPTIALFINGQAVDGL 93
Cdd:cd02984     5 FEELLKSDASKLLVLHFWAPWAEPCKQMNQVFEELAKEAFPSVLFLSIEAEELPEISEKFEITAVPTFVFFRNGTIVDRV 84


                  ...
gi 1228053264  94 AGA 96
Cdd:cd02984    85 SGA 87
PTZ00443 PTZ00443
Thioredoxin domain-containing protein; Provisional
 5-100 5.29e-04

Thioredoxin domain-containing protein; Provisional


Pssm-ID: 185622 [Multi-domain]  Cd Length: 224  Bit Score: 40.38  E-value: 5.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228053264   5 YIVEVNQHNFREVFERSVET---PILFYFWAPMNQESVQLIPELQSVAQQHSGAFTLAILNCQQEQQVAAQFGVQALPTI 81
Cdd:PTZ00443   31 ALVLLNDKNFEKLTQASTGAttgPWFVKFYAPWCSHCRKMAPAWERLAKALKGQVNVADLDATRALNLAKRFAIKGYPTL 110

                          90
                  ....*....|....*....
gi 1228053264  82 ALFINGQAVDGLAGAQTIE 100
Cdd:PTZ00443  111 LLFDKGKMYQYEGGDRSTE 129
TRX_DnaJ cd02963
TRX domain, DnaJ domain containing protein family; composed of uncharacterized proteins of ...
 3-102 5.85e-04

TRX domain, DnaJ domain containing protein family; composed of uncharacterized proteins of about 500-800 amino acids, containing an N-terminal DnaJ domain followed by one redox active TRX domain. DnaJ is a member of the 40 kDa heat-shock protein (Hsp40) family of molecular chaperones, which regulate the activity of Hsp70s. TRX is involved in the redox regulation of many protein substrates through the reduction of disulfide bonds. TRX has been implicated to catalyse the reduction of Hsp33, a chaperone holdase that binds to unfolded protein intermediates. The presence of DnaJ and TRX domains in members of this family suggests that they could be involved in a redox-regulated chaperone network.


Pssm-ID: 239261 [Multi-domain]  Cd Length: 111  Bit Score: 38.51  E-value: 5.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228053264   3 SPYIVEVNQHNFrEVFERSVETPILFYF---W--APMNQESV--QLIPELQSVAqqhsgaFTLAILNCQQEQQVAAQFGV 75
Cdd:cd02963     5 YKYSLTFSQYEN-EIVPKSFKKPYLIKItsdWcfSCIHIEPVwkEVIQELEPLG------VGIATVNAGHERRLARKLGA 77

                          90       100
                  ....*....|....*....|....*..
gi 1228053264  76 QALPTIALFINGQAVDGLAGAQTIETV 102
Cdd:cd02963    78 HSVPAIVGIINGQVTFYHDSSFTKQHV 104
TPR_19 pfam14559
Tetratricopeptide repeat;
148-190 7.57e-04

Tetratricopeptide repeat;


Pssm-ID: 434038 [Multi-domain]  Cd Length: 65  Bit Score: 37.18  E-value: 7.57e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1228053264 148 AEVKLALADVFLETQQYEAAETELERIPLEYQ-DGYYKGLIAKL 190
Cdd:pfam14559  22 AEARLGLAEALLALGRLDEAEALLAALPAADPdDPRYAALLAKL 65
HyaE cd02965
HyaE family; HyaE is also called HupG and HoxO. They are proteins serving a critical role in ...
 42-98 1.12e-03

HyaE family; HyaE is also called HupG and HoxO. They are proteins serving a critical role in the assembly of multimeric [NiFe] hydrogenases, the enzymes that catalyze the oxidation of molecular hydrogen to enable microorganisms to utilize hydrogen as the sole energy source. The E. coli HyaE protein is a chaperone that specifically interacts with the twin-arginine translocation (Tat) signal peptide of the [NiFe] hydrogenase-1 beta subunit precursor. Tat signal peptides target precursor proteins to the Tat protein export system, which facilitates the transport of fully folded proteins across the inner membrane. HyaE may be involved in regulating the traffic of [NiFe] hydrogenase-1 on the Tat transport pathway.


Pssm-ID: 239263  Cd Length: 111  Bit Score: 37.67  E-value: 1.12e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1228053264  42 IPELQSVAQqhsGAFTLAILNCQQEQQVAAQFGVQALPTIALFINGQAVDGLAGAQT 98
Cdd:cd02965    51 LPELLKAFP---GRFRAAVVGRADEQALAARFGVLRTPALLFFRDGRYVGVLAGIRD 104
TRX_NTR cd02949
TRX domain, novel NADPH thioredoxin reductase (NTR) family; composed of fusion proteins found ...
 11-97 2.15e-03

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


Pssm-ID: 239247 [Multi-domain]  Cd Length: 97  Bit Score: 36.71  E-value: 2.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228053264  11 QHNFREVFERSvETPILFYFWAPMNQESVQLIPELQSVAQQHSGAFTLAILNCQQEQQVAAQFGVQALPTIALFINGQAV 90
Cdd:cd02949     2 SYALRKLYHES-DRLILVLYTSPTCGPCRTLKPILNKVIDEFDGAVHFVEIDIDEDQEIAEAAGIMGTPTVQFFKDKELV 80


                  ....*..
gi 1228053264  91 DGLAGAQ 97
Cdd:cd02949    81 KEISGVK 87
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 3-99 2.52e-03

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 38.96  E-value: 2.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228053264   3 SPYIVEVNQHNFrEVFERSVETpILFYFWAPMNQESVQLIPELQSVAQQ---HSGAFTLAILNCQQEQQVAAQFGVQALP 79
Cdd:PTZ00102   31 SEHVTVLTDSTF-DKFITENEI-VLVKFYAPWCGHCKRLAPEYKKAAKMlkeKKSEIVLASVDATEEMELAQEFGVRGYP 108

                          90       100
                  ....*....|....*....|..
gi 1228053264  80 TIALFINGQAV--DGLAGAQTI 99
Cdd:PTZ00102  109 TIKFFNKGNPVnySGGRTADGI 130
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 115-246 6.00e-03

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


Pssm-ID: 443813 [Multi-domain]  Cd Length: 139  Bit Score: 36.32  E-value: 6.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228053264 115 EVSLQQALTLIEQTQHSQALPLLLSLPDDMKAKAEVKLALADVFLETQQYEAAETELERIpLEYQDGYYKGLIAKLELHK 194
Cdd:COG4783     5 EALYALAQALLLAGDYDEAEALLEKALELDPDNPEAFALLGEILLQLGDLDEAIVLLHEA-LELDPDEPEARLNLGLALL 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1228053264 195 QAADSPE-IQALEEIFSAEPNNAHIASELALQYHQVNRNEEALELLWSFLQSD 246
Cdd:COG4783    84 KAGDYDEaLALLEKALKLDPEHPEAYLRLARAYRALGRPDEAIAALEKALELD 136
PDI_a_ERp38 cd02998
PDIa family, endoplasmic reticulum protein 38 (ERp38) subfamily; composed of proteins similar ...
 5-84 8.09e-03

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


Pssm-ID: 239296 [Multi-domain]  Cd Length: 105  Bit Score: 35.30  E-value: 8.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1228053264   5 YIVEVNQHNFREVFERSVEtPILFYFWAPMNQESVQLIPELQSVAQ--QHSGAFTLAILNCQQEQQ-VAAQFGVQALPTI 81
Cdd:cd02998     1 NVVELTDSNFDKVVGDDKK-DVLVEFYAPWCGHCKNLAPEYEKLAAvfANEDDVVIAKVDADEANKdLAKKYGVSGFPTL 79


                  ...
gi 1228053264  82 ALF 84
Cdd:cd02998    80 KFF 82
PTZ00051 PTZ00051
thioredoxin; Provisional
 40-96 9.84e-03

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 34.85  E-value: 9.84e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1228053264  40 QLIPELQSVAQQHSGAFTLAIlNCQQEQQVAAQFGVQALPTIALFINGQAVDGLAGA 96
Cdd:PTZ00051   35 RIAPFYEECSKEYTKMVFVKV-DVDELSEVAEKENITSMPTFKVFKNGSVVDTLLGA 90
 
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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