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Conserved domains on  [gi|489111990|ref|WP_003021844|]
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MULTISPECIES: co-chaperone YbbN [Enterobacterales]

Protein Classification

co-chaperone YbbN( domain architecture ID 18945263)

YbbN is a co-chaperone in heat stress response and DNA synthesis

CATH:  3.40.30.10|1.25.40.10
Gene Ontology:  GO:0061077|GO:0051082|GO:0034599|GO:0005515
PubMed:  21498507|15558583|10517866|30708253
SCOP:  3001345

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 1.54e-42

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: 140.87  E-value: 1.54e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489111990  12 SNLQQTLEQSMTTPVLFYFWSERSQHCLQLTPVLESLAAQYNGQFILAKLDCDAEQMIASQFGLRAIPTVYLFQNGQPVD 91
Cdd:cd02956    1 QNFQQVLQESTQVPVVVDFWAPRSPPSKELLPLLERLAEEYQGQFVLAKVNCDAQPQIAQQFGVQALPTVYLFAAGQPVD 80

                         90
                 ....*....|....*.
gi 489111990  92 GFQGPQPEEVIRALLE 107
Cdd:cd02956   81 GFQGAQPEEQLRQMLD 96
TPR_20 pfam14561
Tetratricopeptide repeat;
195-284 6.51e-34

Tetratricopeptide repeat;


:

Pssm-ID: 434039 [Multi-domain]  Cd Length: 90  Bit Score: 118.38  E-value: 6.51e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489111990  195 QAADTPEIQQLQQQVASNPQDAVLATQLAIQLHQVGRNEESLELLFSHLKKDLTAADGQARKTFQEILAALGTGDALASK 274
Cdd:pfam14561   1 QAADAPELAALEARLAADPDDLDARLDLALALHAAGRNEEALELLLEILRRDRNWNDGAARKQLLDIFEALGPGDPLVAK 80

                          90
                  ....*....|
gi 489111990  275 YRRQLYALLY 284
Cdd:pfam14561  81 YRRKLSSLLF 90
TPR_19 pfam14559
Tetratricopeptide repeat;
127-190 1.10e-11

Tetratricopeptide repeat;


:

Pssm-ID: 434038 [Multi-domain]  Cd Length: 65  Bit Score: 59.13  E-value: 1.10e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489111990  127 AGNHADALPLLKEAWQISNQSSEIGLLLAETQIALNRSDDAEAVLKTIPLQDQDT-RYQGLVAQI 190
Cdd:pfam14559   1 EGDYAEALELLEQALAEDPDNAEARLGLAEALLALGRLDEAEALLAALPAADPDDpRYAALLAKL 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 1.54e-42

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: 140.87  E-value: 1.54e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489111990  12 SNLQQTLEQSMTTPVLFYFWSERSQHCLQLTPVLESLAAQYNGQFILAKLDCDAEQMIASQFGLRAIPTVYLFQNGQPVD 91
Cdd:cd02956    1 QNFQQVLQESTQVPVVVDFWAPRSPPSKELLPLLERLAEEYQGQFVLAKVNCDAQPQIAQQFGVQALPTVYLFAAGQPVD 80

                         90
                 ....*....|....*.
gi 489111990  92 GFQGPQPEEVIRALLE 107
Cdd:cd02956   81 GFQGAQPEEQLRQMLD 96
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 5-110 4.31e-41

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: 137.64  E-value: 4.31e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489111990   5 NIVNINESNLQQTLEQSmTTPVLFYFWSERSQHCLQLTPVLESLAAQYNGQFILAKLDCDAEQMIASQFGLRAIPTVYLF 84
Cdd:COG3118    1 AVVELTDENFEEEVLES-DKPVLVDFWAPWCGPCKMLAPVLEELAAEYGGKVKFVKVDVDENPELAAQFGVRSIPTLLLF 79

                         90       100
                 ....*....|....*....|....*.
gi 489111990  85 QNGQPVDGFQGPQPEEVIRALLEKVL 110
Cdd:COG3118   80 KDGQPVDRFVGALPKEQLREFLDKVL 105
TPR_20 pfam14561
Tetratricopeptide repeat;
195-284 6.51e-34

Tetratricopeptide repeat;


Pssm-ID: 434039 [Multi-domain]  Cd Length: 90  Bit Score: 118.38  E-value: 6.51e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489111990  195 QAADTPEIQQLQQQVASNPQDAVLATQLAIQLHQVGRNEESLELLFSHLKKDLTAADGQARKTFQEILAALGTGDALASK 274
Cdd:pfam14561   1 QAADAPELAALEARLAADPDDLDARLDLALALHAAGRNEEALELLLEILRRDRNWNDGAARKQLLDIFEALGPGDPLVAK 80

                          90
                  ....*....|
gi 489111990  275 YRRQLYALLY 284
Cdd:pfam14561  81 YRRKLSSLLF 90
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 5-108 1.01e-23

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


Pssm-ID: 395038 [Multi-domain]  Cd Length: 103  Bit Score: 92.30  E-value: 1.01e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489111990    5 NIVNINESNLQQTLeQSMTTPVLFYFWSERSQHCLQLTPVLESLAAQYNGQFILAKLDCDAEQMIASQFGLRAIPTVYLF 84
Cdd:pfam00085   1 VVVVLTDANFDEVV-QKSSKPVLVDFYAPWCGPCKMLAPEYEELAQEYKGNVVFAKVDVDENPDLASKYGVRGYPTLIFF 79

                          90       100
                  ....*....|....*....|....
gi 489111990   85 QNGQPVDGFQGPQPEEVIRALLEK 108
Cdd:pfam00085  80 KNGQPVDDYVGARPKDALAAFLKA 103
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 9-110 1.77e-22

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: 89.27  E-value: 1.77e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489111990    9 INESNLQQTLEQSmTTPVLFYFWSERSQHCLQLTPVLESLAAQYNGQFILAKLDCDAEQMIASQFGLRAIPTVYLFQNGQ 88
Cdd:TIGR01068   1 LTDANFDETIASS-DKPVLVDFWAPWCGPCKMIAPILEELAKEYEGKVKFVKLNVDENPDIAAKYGIRSIPTLLLFKNGK 79

                          90       100
                  ....*....|....*....|..
gi 489111990   89 PVDGFQGPQPEEVIRALLEKVL 110
Cdd:TIGR01068  80 EVDRSVGALPKAALKQLINKNL 101
PRK10996 PRK10996
thioredoxin 2; Provisional
 6-98 3.66e-17

thioredoxin 2; Provisional


Pssm-ID: 182889 [Multi-domain]  Cd Length: 139  Bit Score: 76.26  E-value: 3.66e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489111990   6 IVNINESNLQQTLEQSmtTPVLFYFWSERSQHCLQLTPVLESLAAQYNGQFILAKLDCDAEQMIASQFGLRAIPTVYLFQ 85
Cdd:PRK10996  37 VINATGETLDKLLQDD--LPVVIDFWAPWCGPCRNFAPIFEDVAAERSGKVRFVKVNTEAERELSARFRIRSIPTIMIFK 114

                         90
                 ....*....|...
gi 489111990  86 NGQPVDGFQGPQP 98
Cdd:PRK10996 115 NGQVVDMLNGAVP 127
TPR_19 pfam14559
Tetratricopeptide repeat;
127-190 1.10e-11

Tetratricopeptide repeat;


Pssm-ID: 434038 [Multi-domain]  Cd Length: 65  Bit Score: 59.13  E-value: 1.10e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489111990  127 AGNHADALPLLKEAWQISNQSSEIGLLLAETQIALNRSDDAEAVLKTIPLQDQDT-RYQGLVAQI 190
Cdd:pfam14559   1 EGDYAEALELLEQALAEDPDNAEARLGLAEALLALGRLDEAEALLAALPAADPDDpRYAALLAKL 65
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 103-215 3.87e-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: 36.71  E-value: 3.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489111990 103 RALLEKVL---PSEEELKARQAIEFIEAGNHADALPLLKEAWQISNQSSEIGLLLAETQIALNRSDDAEAVLKTIpLQDQ 179
Cdd:COG4783   24 EALLEKALeldPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNLGLALLKAGDYDEALALLEKA-LKLD 102

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 489111990 180 DTRYQGLVAQIELLKQAADTPE-IQQLQQQVASNPQD 215
Cdd:COG4783  103 PEHPEAYLRLARAYRALGRPDEaIAALEKALELDPDD 139
 
Name Accession Description Interval E-value
ybbN cd02956
ybbN protein family; ybbN is a hypothetical protein containing a redox-inactive TRX-like ...
 12-107 1.54e-42

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: 140.87  E-value: 1.54e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489111990  12 SNLQQTLEQSMTTPVLFYFWSERSQHCLQLTPVLESLAAQYNGQFILAKLDCDAEQMIASQFGLRAIPTVYLFQNGQPVD 91
Cdd:cd02956    1 QNFQQVLQESTQVPVVVDFWAPRSPPSKELLPLLERLAEEYQGQFVLAKVNCDAQPQIAQQFGVQALPTVYLFAAGQPVD 80

                         90
                 ....*....|....*.
gi 489111990  92 GFQGPQPEEVIRALLE 107
Cdd:cd02956   81 GFQGAQPEEQLRQMLD 96
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 5-110 4.31e-41

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: 137.64  E-value: 4.31e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489111990   5 NIVNINESNLQQTLEQSmTTPVLFYFWSERSQHCLQLTPVLESLAAQYNGQFILAKLDCDAEQMIASQFGLRAIPTVYLF 84
Cdd:COG3118    1 AVVELTDENFEEEVLES-DKPVLVDFWAPWCGPCKMLAPVLEELAAEYGGKVKFVKVDVDENPELAAQFGVRSIPTLLLF 79

                         90       100
                 ....*....|....*....|....*.
gi 489111990  85 QNGQPVDGFQGPQPEEVIRALLEKVL 110
Cdd:COG3118   80 KDGQPVDRFVGALPKEQLREFLDKVL 105
TPR_20 pfam14561
Tetratricopeptide repeat;
195-284 6.51e-34

Tetratricopeptide repeat;


Pssm-ID: 434039 [Multi-domain]  Cd Length: 90  Bit Score: 118.38  E-value: 6.51e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489111990  195 QAADTPEIQQLQQQVASNPQDAVLATQLAIQLHQVGRNEESLELLFSHLKKDLTAADGQARKTFQEILAALGTGDALASK 274
Cdd:pfam14561   1 QAADAPELAALEARLAADPDDLDARLDLALALHAAGRNEEALELLLEILRRDRNWNDGAARKQLLDIFEALGPGDPLVAK 80

                          90
                  ....*....|
gi 489111990  275 YRRQLYALLY 284
Cdd:pfam14561  81 YRRKLSSLLF 90
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 5-108 1.01e-23

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


Pssm-ID: 395038 [Multi-domain]  Cd Length: 103  Bit Score: 92.30  E-value: 1.01e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489111990    5 NIVNINESNLQQTLeQSMTTPVLFYFWSERSQHCLQLTPVLESLAAQYNGQFILAKLDCDAEQMIASQFGLRAIPTVYLF 84
Cdd:pfam00085   1 VVVVLTDANFDEVV-QKSSKPVLVDFYAPWCGPCKMLAPEYEELAQEYKGNVVFAKVDVDENPDLASKYGVRGYPTLIFF 79

                          90       100
                  ....*....|....*....|....
gi 489111990   85 QNGQPVDGFQGPQPEEVIRALLEK 108
Cdd:pfam00085  80 KNGQPVDDYVGARPKDALAAFLKA 103
TRX_family cd02947
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ...
 12-107 2.01e-23

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: 91.47  E-value: 2.01e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489111990  12 SNLQQTLEQSmtTPVLFYFWSERSQHCLQLTPVLESLAAQYnGQFILAKLDCDAEQMIASQFGLRAIPTVYLFQNGQPVD 91
Cdd:cd02947    1 EEFEELIKSA--KPVVVDFWAPWCGPCKAIAPVLEELAEEY-PKVKFVKVDVDENPELAEEYGVRSIPTFLFFKNGKEVD 77

                         90
                 ....*....|....*.
gi 489111990  92 GFQGPQPEEVIRALLE 107
Cdd:cd02947   78 RVVGADPKEELEEFLE 93
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 9-110 1.77e-22

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: 89.27  E-value: 1.77e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489111990    9 INESNLQQTLEQSmTTPVLFYFWSERSQHCLQLTPVLESLAAQYNGQFILAKLDCDAEQMIASQFGLRAIPTVYLFQNGQ 88
Cdd:TIGR01068   1 LTDANFDETIASS-DKPVLVDFWAPWCGPCKMIAPILEELAKEYEGKVKFVKLNVDENPDIAAKYGIRSIPTLLLFKNGK 79

                          90       100
                  ....*....|....*....|..
gi 489111990   89 PVDGFQGPQPEEVIRALLEKVL 110
Cdd:TIGR01068  80 EVDRSVGALPKAALKQLINKNL 101
PRK10996 PRK10996
thioredoxin 2; Provisional
 6-98 3.66e-17

thioredoxin 2; Provisional


Pssm-ID: 182889 [Multi-domain]  Cd Length: 139  Bit Score: 76.26  E-value: 3.66e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489111990   6 IVNINESNLQQTLEQSmtTPVLFYFWSERSQHCLQLTPVLESLAAQYNGQFILAKLDCDAEQMIASQFGLRAIPTVYLFQ 85
Cdd:PRK10996  37 VINATGETLDKLLQDD--LPVVIDFWAPWCGPCRNFAPIFEDVAAERSGKVRFVKVNTEAERELSARFRIRSIPTIMIFK 114

                         90
                 ....*....|...
gi 489111990  86 NGQPVDGFQGPQP 98
Cdd:PRK10996 115 NGQVVDMLNGAVP 127
PDI_a_family cd02961
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ...
 7-104 2.93e-12

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


Pssm-ID: 239259 [Multi-domain]  Cd Length: 101  Bit Score: 61.86  E-value: 2.93e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489111990   7 VNINESNLQQTLEQSMTTPVLFYF-WSErsqHCLQLTPVLESLAAQY--NGQFILAKLDCDAEQMIASQFGLRAIPTVYL 83
Cdd:cd02961    1 VELTDDNFDELVKDSKDVLVEFYApWCG---HCKALAPEYEKLAKELkgDGKVVVAKVDCTANNDLCSEYGVRGYPTIKL 77

                         90       100
                 ....*....|....*....|...
gi 489111990  84 FQNG--QPVDgFQGPQPEEVIRA 104
Cdd:cd02961   78 FPNGskEPVK-YEGPRTLESLVE 99
TPR_19 pfam14559
Tetratricopeptide repeat;
127-190 1.10e-11

Tetratricopeptide repeat;


Pssm-ID: 434038 [Multi-domain]  Cd Length: 65  Bit Score: 59.13  E-value: 1.10e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489111990  127 AGNHADALPLLKEAWQISNQSSEIGLLLAETQIALNRSDDAEAVLKTIPLQDQDT-RYQGLVAQI 190
Cdd:pfam14559   1 EGDYAEALELLEQALAEDPDNAEARLGLAEALLALGRLDEAEALLAALPAADPDDpRYAALLAKL 65
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 25-110 3.64e-11

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 59.70  E-value: 3.64e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489111990  25 PVLFYFWSERSQHCLQLTPVLESLAAQYNG-QFILAKLD--------------------CDAEQMIASQFGLRAIPTVYL 83
Cdd:COG0526   30 PVLVNFWATWCPPCRAEMPVLKELAEEYGGvVFVGVDVDenpeavkaflkelglpypvlLDPDGELAKAYGVRGIPTTVL 109

                         90       100
                 ....*....|....*....|....*...
gi 489111990  84 F-QNGQPVDGFQGPQPEEVIRALLEKVL 110
Cdd:COG0526  110 IdKDGKIVARHVGPLSPEELEEALEKLL 137
trxA PRK09381
thioredoxin TrxA;
30-88 1.29e-10

thioredoxin TrxA;


Pssm-ID: 181812 [Multi-domain]  Cd Length: 109  Bit Score: 57.38  E-value: 1.29e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 489111990  30 FWSERSQHCLQLTPVLESLAAQYNGQFILAKLDCDAEQMIASQFGLRAIPTVYLFQNGQ 88
Cdd:PRK09381  28 FWAEWCGPCKMIAPILDEIADEYQGKLTVAKLNIDQNPGTAPKYGIRGIPTLLLFKNGE 86
PDI_a_ERp46 cd03005
PDIa family, endoplasmic reticulum protein 46 (ERp46) subfamily; ERp46 is an ER-resident ...
 37-96 2.51e-10

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


Pssm-ID: 239303 [Multi-domain]  Cd Length: 102  Bit Score: 56.52  E-value: 2.51e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489111990  37 HCLQLTPVLESLAAQY---NGQFILAKLDCDAEQMIASQFGLRAIPTVYLFQNGQPVDGFQGP 96
Cdd:cd03005   30 HCKRLAPTWEQLAKKFnneNPSVKIAKVDCTQHRELCSEFQVRGYPTLLLFKDGEKVDKYKGT 92
PDI_a_P5 cd03001
PDIa family, P5 subfamily; composed of eukaryotic proteins similar to human P5, a PDI-related ...
 5-96 7.03e-10

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: 54.99  E-value: 7.03e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489111990   5 NIVNINESNLQQTLEQSmTTPVLFYFWSERSQHCLQLTPVLESLAAQYNGQFILAKLDCDAEQMIASQFGLRAIPTVYLF 84
Cdd:cd03001    1 DVVELTDSNFDKKVLNS-DDVWLVEFYAPWCGHCKNLAPEWKKAAKALKGIVKVGAVDADVHQSLAQQYGVRGFPTIKVF 79

                         90
                 ....*....|....
gi 489111990  85 QNGQ--PVDgFQGP 96
Cdd:cd03001   80 GAGKnsPQD-YQGG 92
TRX_PICOT cd02984
TRX domain, PICOT (for PKC-interacting cousin of TRX) subfamily; PICOT is a protein that ...
 11-105 1.60e-09

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: 53.81  E-value: 1.60e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489111990  11 ESNLQQTLEQSMTTPVLFYFWSERSQHCLQLTPVLESLAAQYNGQFILAKLDCDAEQMIASQFGLRAIPTVYLFQNGQPV 90
Cdd:cd02984    2 EEEFEELLKSDASKLLVLHFWAPWAEPCKQMNQVFEELAKEAFPSVLFLSIEAEELPEISEKFEITAVPTFVFFRNGTIV 81

                         90
                 ....*....|....*
gi 489111990  91 DGFQGPQPEEVIRAL 105
Cdd:cd02984   82 DRVSGADPKELAKKV 96
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 6-151 7.24e-09

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 56.30  E-value: 7.24e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489111990   6 IVNINESNLQQTLEQSMTTPVLFYF-WSersQHCLQLTPVLESLAAQYN---GQFILAKLDCDAEQMIASQFGLRAIPTV 81
Cdd:PTZ00102  34 VTVLTDSTFDKFITENEIVLVKFYApWC---GHCKRLAPEYKKAAKMLKekkSEIVLASVDATEEMELAQEFGVRGYPTI 110

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489111990  82 YLFQNGQPVDGFQGPQPEEVIRALLEKVLP------SEEELKARQAIEFIEAGNH--ADALPLLKEAWQISNQSSEIG 151
Cdd:PTZ00102 111 KFFNKGNPVNYSGGRTADGIVSWIKKLTGPavteveSASEIKLIAKKIFVAFYGEytSKDSELYKKFEEVADKHREHA 188
PDI_a_ERp44 cd02996
PDIa family, endoplasmic reticulum protein 44 (ERp44) subfamily; ERp44 is an ER-resident ...
 5-88 8.59e-09

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: 52.39  E-value: 8.59e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489111990   5 NIVNINESNLQQTLEQSMTTPVLFYF-WSERSQhclQLTPVLESLAAQYN------GQFILAKLDCDAEQMIASQFGLRA 77
Cdd:cd02996    2 EIVSLTSGNIDDILQSAELVLVNFYAdWCRFSQ---MLHPIFEEAAAKIKeefpdaGKVVWGKVDCDKESDIADRYRINK 78

                         90
                 ....*....|.
gi 489111990  78 IPTVYLFQNGQ 88
Cdd:cd02996   79 YPTLKLFRNGM 89
PDI_a_MPD1_like cd03002
PDI family, MPD1-like subfamily; composed of eukaryotic proteins similar to Saccharomyces ...
 5-90 2.60e-08

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: 50.82  E-value: 2.60e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489111990   5 NIVNINESNLQQTLEQS-MTTPVLFYF-WSersQHCLQLTPVLESLAAQYNGQFILAKLDCDAEQ--MIASQFGLRAIPT 80
Cdd:cd03002    1 PVYELTPKNFDKVVHNTnYTTLVEFYApWC---GHCKNLKPEYAKAAKELDGLVQVAAVDCDEDKnkPLCGKYGVQGFPT 77

                         90
                 ....*....|
gi 489111990  81 VYLFQNGQPV 90
Cdd:cd03002   78 LKVFRPPKKA 87
PTZ00443 PTZ00443
Thioredoxin domain-containing protein; Provisional
 6-88 7.10e-08

Thioredoxin domain-containing protein; Provisional


Pssm-ID: 185622 [Multi-domain]  Cd Length: 224  Bit Score: 51.93  E-value: 7.10e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489111990   6 IVNINESNLQQTLEQSM---TTPVLFYFWSERSQHCLQLTPVLESLAAQYNGQFILAKLDCDAEQMIASQFGLRAIPTVY 82
Cdd:PTZ00443  32 LVLLNDKNFEKLTQASTgatTGPWFVKFYAPWCSHCRKMAPAWERLAKALKGQVNVADLDATRALNLAKRFAIKGYPTLL 111


                 ....*.
gi 489111990  83 LFQNGQ 88
Cdd:PTZ00443 112 LFDKGK 117
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 5-129 2.97e-07

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: 51.21  E-value: 2.97e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489111990    5 NIVNINESNLQQTLEQSMTTPVLFYF-WSersQHCLQLTPVLESLAAQY--NGQFI-LAKLDCDAEQMIASQFGLRAIPT 80
Cdd:TIGR01130   2 DVLVLTKDNFDDFIKSHEFVLVEFYApWC---GHCKSLAPEYEKAADELkkKGPPIkLAKVDATEEKDLAQKYGVSGYPT 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 489111990   81 VYLFQNGQPVDG-FQGPQ-PEEVIRALLEKVLPSEEELKARQAIEFIEAGN 129
Cdd:TIGR01130  79 LKIFRNGEDSVSdYNGPRdADGIVKYMKKQSGPAVKEIETVADLEAFLADD 129
TRX_NTR cd02949
TRX domain, novel NADPH thioredoxin reductase (NTR) family; composed of fusion proteins found ...
 25-107 3.81e-06

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: 44.41  E-value: 3.81e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489111990  25 PVLFYFWSERSQHCLQLTPVLESLAAQYNGQFILAKLDCDAEQMIASQFGLRAIPTVYLFQNGQPVDGFQGPQPEEVIRA 104
Cdd:cd02949   15 LILVLYTSPTCGPCRTLKPILNKVIDEFDGAVHFVEIDIDEDQEIAEAAGIMGTPTVQFFKDKELVKEISGVKMKSEYRE 94


                 ...
gi 489111990 105 LLE 107
Cdd:cd02949   95 FIE 97
TRX_superfamily cd01659
Thioredoxin (TRX) superfamily; a large, diverse group of proteins containing a TRX-fold. Many ...
 27-90 6.11e-06

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


Pssm-ID: 238829 [Multi-domain]  Cd Length: 69  Bit Score: 43.07  E-value: 6.11e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489111990  27 LFYFWSERSQHCLQLTPVLESLAAqYNGQFILAKLDCD---AEQMIASQFGLRAIPTVYLFQNGQPV 90
Cdd:cd01659    1 LVLFYAPWCPFCQALRPVLAELAL-LNKGVKFEAVDVDedpALEKELKRYGVGGVPTLVVFGPGIGV 66
PTZ00051 PTZ00051
thioredoxin; Provisional
 11-101 6.63e-06

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 44.10  E-value: 6.63e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489111990  11 ESNLQQTLEQSMTTPVLFYfwSERSQHCLQLTPVLESLAAQYNgQFILAKLDCDAEQMIASQFGLRAIPTVYLFQNGQPV 90
Cdd:PTZ00051   8 QAEFESTLSQNELVIVDFY--AEWCGPCKRIAPFYEECSKEYT-KMVFVKVDVDELSEVAEKENITSMPTFKVFKNGSVV 84

                         90
                 ....*....|.
gi 489111990  91 DGFQGPQPEEV 101
Cdd:PTZ00051  85 DTLLGANDEAL 95
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 97-279 2.03e-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: 2.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489111990  97 QPEEVIRALLEKVLPSEEELKARQAI--EFIEAGNHADALPLLKEAWQISNQSSEIGLLLAETQIALNRSDDAEAVLKT- 173
Cdd:COG2956   57 EYDRAIRIHQKLLERDPDRAEALLELaqDYLKAGLLDRAEELLEKLLELDPDDAEALRLLAEIYEQEGDWEKAIEVLERl 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489111990 174 IPLQDQDTRYQGLVAQIELLKQAADTpEIQQLQQQVASNPQDAVLATQLAIQLHQVGRNEESLELLFSHLKKDltAADGQ 253
Cdd:COG2956  137 LKLGPENAHAYCELAELYLEQGDYDE-AIEALEKALKLDPDCARALLLLAELYLEQGDYEEAIAALERALEQD--PDYLP 213

                        170       180
                 ....*....|....*....|....*.
gi 489111990 254 ARKTFQEILAALGTGDALASKYRRQL 279
Cdd:COG2956  214 ALPRLAELYEKLGDPEEALELLRKAL 239
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 106-246 3.09e-05

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


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 44.33  E-value: 3.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489111990 106 LEKVLPSEEELKARQAIEFIEAGNHADALPLLKEAWQISNQSSEIGLLLAETQIALNRSDDAEAVLKTIPLQDQDtRYQG 185
Cdd:COG2956  136 LLKLGPENAHAYCELAELYLEQGDYDEAIEALEKALKLDPDCARALLLLAELYLEQGDYEEAIAALERALEQDPD-YLPA 214

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489111990 186 LVAQIELLKQAADTPE-IQQLQQQVASNPQDAVLATqLAIQLHQVGRNEESLELLFSHLKKD 246
Cdd:COG2956  215 LPRLAELYEKLGDPEEaLELLRKALELDPSDDLLLA-LADLLERKEGLEAALALLERQLRRH 275
PDI_a_TMX3 cd03000
PDIa family, TMX3 subfamily; composed of eukaryotic proteins similar to human TMX3, a TRX ...
 30-102 5.91e-05

PDIa family, TMX3 subfamily; composed of eukaryotic proteins similar to human TMX3, a TRX related transmembrane protein containing one redox active TRX domain at the N-terminus and a classical ER retrieval sequence for type I transmembrane proteins at the C-terminus. The TMX3 transcript is found in a variety of tissues with the highest levels detected in skeletal muscle and the heart. In vitro, TMX3 showed oxidase activity albeit slightly lower than that of protein disulfide isomerase.


Pssm-ID: 239298 [Multi-domain]  Cd Length: 104  Bit Score: 41.29  E-value: 5.91e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489111990  30 FWSERSQHCLQLTPVLESLAAQ---YNGQFILAKLDCDAEQMIASQFGLRAIPTVYLFQNGQPVDgFQGPQPEEVI 102
Cdd:cd03000   22 FYAPWCGHCKKLEPVWNEVGAElksSGSPVRVGKLDATAYSSIASEFGVRGYPTIKLLKGDLAYN-YRGPRTKDDI 96
PDI_a_ERdj5_C cd03004
PDIa family, C-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 37-84 1.02e-04

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: 40.74  E-value: 1.02e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 489111990  37 HCLQLTPVLESLAAQYNGQFILAKLDCDAEQMIASQFGLRAIPTVYLF 84
Cdd:cd03004   33 PCQALLPELRKAARALKGKVKVGSVDCQKYESLCQQANIRAYPTIRLY 80
PDI_a_ERdj5_N cd03003
PDIa family, N-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 4-100 1.10e-04

PDIa family, N-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 comprised of the first TRX domain of ERdj5 located after the DnaJ domain at the N-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.


Pssm-ID: 239301 [Multi-domain]  Cd Length: 101  Bit Score: 40.59  E-value: 1.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489111990   4 QNIVNINESNLQQTLEQSMTTPVLFYfwSERSQHCLQLTPVLESLAAQYNGQFILAKLDCDAEQMIASQFGLRAIPTVYL 83
Cdd:cd03003    1 PEIVTLDRGDFDAAVNSGEIWFVNFY--SPRCSHCHDLAPTWREFAKEMDGVIRIGAVNCGDDRMLCRSQGVNSYPSLYV 78

                         90
                 ....*....|....*..
gi 489111990  84 FQNGQPVDGFQGPQPEE 100
Cdd:cd03003   79 FPSGMNPEKYYGDRSKE 95
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 115-246 2.32e-04

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: 40.56  E-value: 2.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489111990 115 ELKARQAIEFIEAGNHADALPLLKEAWQISNQSSEIGLLLAETQIALNRSDDAEAVLKT-IPLQDQDTRYQGLVAQIelL 193
Cdd:COG4783    5 EALYALAQALLLAGDYDEAEALLEKALELDPDNPEAFALLGEILLQLGDLDEAIVLLHEaLELDPDEPEARLNLGLA--L 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 489111990 194 KQAADTPE-IQQLQQQVASNPQDAVLATQLAIQLHQVGRNEESLELLFSHLKKD 246
Cdd:COG4783   83 LKAGDYDEaLALLEKALKLDPEHPEAYLRLARAYRALGRPDEAIAALEKALELD 136
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 25-108 2.72e-04

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 42.05  E-value: 2.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489111990  25 PVLFYFWSERSQHCLQLTPVLESLAAQY--NGQFILAKLDCDAEQMIASQFGLRAIPTVYLFQNGQ--PVDgFQGPQPEE 100
Cdd:PTZ00102 377 DVLLEIYAPWCGHCKNLEPVYNELGEKYkdNDSIIVAKMNGTANETPLEEFSWSAFPTILFVKAGErtPIP-YEGERTVE 455


                 ....*...
gi 489111990 101 VIRALLEK 108
Cdd:PTZ00102 456 GFKEFVNK 463
Thioredoxin_8 pfam13905
Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 25-88 9.15e-04

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


Pssm-ID: 464033 [Multi-domain]  Cd Length: 95  Bit Score: 37.67  E-value: 9.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489111990   25 PVLFYFWSERSQHCLQLTPVLESLAAQYNGQ----FILAKLDCDAEQM-----------------------IASQFGLRA 77
Cdd:pfam13905   3 VVLLYFGASWCKPCRRFTPLLKELYEKLKKKknveIVFVSLDRDLEEFkdylkkmpkdwlsvpfddderneLKRKYGVNA 82

                          90
                  ....*....|..
gi 489111990   78 IPTVYLF-QNGQ 88
Cdd:pfam13905  83 IPTLVLLdPNGE 94
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 13-284 1.21e-03

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 39.98  E-value: 1.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489111990  13 NLQQTLEQSMTTPVLFYFWSERSQHCLQLTPVLESLAAQYNGQFILAKLDCDAEQMIASQFGLRAIPtvYLFQNGQPvdg 92
Cdd:COG3914   20 AAAAAELALAAELEAAALAAALGLALLLLAALAEAAAAALLALAAGEAAAAAAALLLLAALLELAAL--LLQALGRY--- 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489111990  93 fqgPQPEEVIRALLEKVlPSEEELKARQAIEFIEAGNHADALPLLKEAWQISNQSSEIGLLLAETQIALNRSDDAEAVLK 172
Cdd:COG3914   95 ---EEALALYRRALALN-PDNAEALFNLGNLLLALGRLEEALAALRRALALNPDFAEAYLNLGEALRRLGRLEEAIAALR 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489111990 173 T-IPLQDQDTRYQGLVAQieLLKQAADTPE-IQQLQQQVASNPQDAVLATQLaiqLHQVGRNEESLELLFSHLKKDLTAA 250
Cdd:COG3914  171 RaLELDPDNAEALNNLGN--ALQDLGRLEEaIAAYRRALELDPDNADAHSNL---LFALRQACDWEVYDRFEELLAALAR 245

                        250       260       270
                 ....*....|....*....|....*....|....
gi 489111990 251 DGQARKTFqeILAALGTGDALASKYRRQLYALLY 284
Cdd:COG3914  246 GPSELSPF--ALLYLPDDDPAELLALARAWAQLV 277
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 37-95 3.71e-03

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


Pssm-ID: 273457 [Multi-domain]  Cd Length: 462  Bit Score: 38.50  E-value: 3.71e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489111990   37 HCLQLTPVLESLAAQYNGQ---FILAKLdcDAEQMIASQFGLRAIPTVYLFQNG---QPVDgFQG 95
Cdd:TIGR01130 378 HCKNLAPIYEELAEKYKDAesdVVIAKM--DATANDVPPFEVEGFPTIKFVPAGkksEPVP-YDG 439
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 103-215 3.87e-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: 36.71  E-value: 3.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489111990 103 RALLEKVL---PSEEELKARQAIEFIEAGNHADALPLLKEAWQISNQSSEIGLLLAETQIALNRSDDAEAVLKTIpLQDQ 179
Cdd:COG4783   24 EALLEKALeldPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNLGLALLKAGDYDEALALLEKA-LKLD 102

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 489111990 180 DTRYQGLVAQIELLKQAADTPE-IQQLQQQVASNPQD 215
Cdd:COG4783  103 PEHPEAYLRLARAYRALGRPDEaIAALEKALELDPDD 139
HyaE cd02965
HyaE family; HyaE is also called HupG and HoxO. They are proteins serving a critical role in ...
 44-98 5.59e-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: 35.75  E-value: 5.59e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 489111990  44 VLESLAAQYNGQFILAKLDCDAEQMIASQFGLRAIPTVYLFQNGQPVDGFQGPQP 98
Cdd:cd02965   50 VLPELLKAFPGRFRAAVVGRADEQALAARFGVLRTPALLFFRDGRYVGVLAGIRD 104
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
25-108 8.26e-03

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 36.00  E-value: 8.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489111990  25 PVLFYFWSERSQHCLQLTPVLESLAAQYNGQ-----------------FIlAKLD------CDAEQMIASQFGLRAIPTV 81
Cdd:COG1225   23 PVVLYFYATWCPGCTAELPELRDLYEEFKDKgvevlgvssdsdeahkkFA-EKYGlpfpllSDPDGEVAKAYGVRGTPTT 101

                         90       100       110
                 ....*....|....*....|....*....|...
gi 489111990  82 YLF-QNGQPVDGFQG-----PQPEEVIRALLEK 108
Cdd:COG1225  102 FLIdPDGKIRYVWVGpvdprPHLEEVLEALLAE 134
 
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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