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Conserved domains on  [gi|504695724|ref|WP_014882826|]
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MULTISPECIES: co-chaperone YbbN [Enterobacter]

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 3.36e-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: 140.10  E-value: 3.36e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695724  12 ANLQQILEQSMAKPVLFYFWSERSQHCLQLTPVLESLAAQYNGQFILAKLDCDAEPMVASQFGLRAIPTVYLFQNGQPVD 91
Cdd:cd02956    1 QNFQQVLQESTQVPVVVDFWAPRSPPSKELLPLLERLAEEYQGQFVLAKVNCDAQPQIAQQFGVQALPTVYLFAAGQPVD 80

                         90
                 ....*....|....*.
gi 504695724  92 GFQGPQPEEAIRALLD 107
Cdd:cd02956   81 GFQGAQPEEQLRQMLD 96
TPR_20 pfam14561
Tetratricopeptide repeat;
195-284 1.32e-33

Tetratricopeptide repeat;


:

Pssm-ID: 434039 [Multi-domain]  Cd Length: 90  Bit Score: 117.61  E-value: 1.32e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695724  195 QAADTPEIQQLQQQVADNPADAALASQLALQLHQVGRNEEALELLFSHLQKDLAAADGQARKMFQEILAALGTGDALASK 274
Cdd:pfam14561   1 QAADAPELAALEARLAADPDDLDARLDLALALHAAGRNEEALELLLEILRRDRNWNDGAARKQLLDIFEALGPGDPLVAK 80

                          90
                  ....*....|
gi 504695724  275 YRRQLYALLY 284
Cdd:pfam14561  81 YRRKLSSLLF 90
TPR_19 pfam14559
Tetratricopeptide repeat;
127-190 1.34e-09

Tetratricopeptide repeat;


:

Pssm-ID: 434038 [Multi-domain]  Cd Length: 65  Bit Score: 53.36  E-value: 1.34e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504695724  127 EGKYDEALPLLKDAWQLSNQNSQIGLLLAETQIALHRSEDAEAVLKTVPLQDQDT-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 3.36e-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: 140.10  E-value: 3.36e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695724  12 ANLQQILEQSMAKPVLFYFWSERSQHCLQLTPVLESLAAQYNGQFILAKLDCDAEPMVASQFGLRAIPTVYLFQNGQPVD 91
Cdd:cd02956    1 QNFQQVLQESTQVPVVVDFWAPRSPPSKELLPLLERLAEEYQGQFVLAKVNCDAQPQIAQQFGVQALPTVYLFAAGQPVD 80

                         90
                 ....*....|....*.
gi 504695724  92 GFQGPQPEEAIRALLD 107
Cdd:cd02956   81 GFQGAQPEEQLRQMLD 96
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 5-110 6.05e-42

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: 139.57  E-value: 6.05e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695724   5 NIVNITEANLQQILEQSmAKPVLFYFWSERSQHCLQLTPVLESLAAQYNGQFILAKLDCDAEPMVASQFGLRAIPTVYLF 84
Cdd:COG3118    1 AVVELTDENFEEEVLES-DKPVLVDFWAPWCGPCKMLAPVLEELAAEYGGKVKFVKVDVDENPELAAQFGVRSIPTLLLF 79

                         90       100
                 ....*....|....*....|....*.
gi 504695724  85 QNGQPVDGFQGPQPEEAIRALLDKVL 110
Cdd:COG3118   80 KDGQPVDRFVGALPKEQLREFLDKVL 105
TPR_20 pfam14561
Tetratricopeptide repeat;
195-284 1.32e-33

Tetratricopeptide repeat;


Pssm-ID: 434039 [Multi-domain]  Cd Length: 90  Bit Score: 117.61  E-value: 1.32e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695724  195 QAADTPEIQQLQQQVADNPADAALASQLALQLHQVGRNEEALELLFSHLQKDLAAADGQARKMFQEILAALGTGDALASK 274
Cdd:pfam14561   1 QAADAPELAALEARLAADPDDLDARLDLALALHAAGRNEEALELLLEILRRDRNWNDGAARKQLLDIFEALGPGDPLVAK 80

                          90
                  ....*....|
gi 504695724  275 YRRQLYALLY 284
Cdd:pfam14561  81 YRRKLSSLLF 90
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 5-108 2.27e-27

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: 101.93  E-value: 2.27e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695724    5 NIVNITEANLQQILeQSMAKPVLFYFWSERSQHCLQLTPVLESLAAQYNGQFILAKLDCDAEPMVASQFGLRAIPTVYLF 84
Cdd:pfam00085   1 VVVVLTDANFDEVV-QKSSKPVLVDFYAPWCGPCKMLAPEYEELAQEYKGNVVFAKVDVDENPDLASKYGVRGYPTLIFF 79

                          90       100
                  ....*....|....*....|....
gi 504695724   85 QNGQPVDGFQGPQPEEAIRALLDK 108
Cdd:pfam00085  80 KNGQPVDDYVGARPKDALAAFLKA 103
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 9-110 1.02e-23

thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of a domain closely related to thioredoxin. This model is designed to recognize authentic thioredoxin, a small protein that should be hit exactly once by this model. Any protein that hits once with a score greater than the second (per domain) trusted cutoff may be taken as thioredoxin. [Energy metabolism, Electron transport]


Pssm-ID: 200072 [Multi-domain]  Cd Length: 101  Bit Score: 92.35  E-value: 1.02e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695724    9 ITEANLQQILEQSmAKPVLFYFWSERSQHCLQLTPVLESLAAQYNGQFILAKLDCDAEPMVASQFGLRAIPTVYLFQNGQ 88
Cdd:TIGR01068   1 LTDANFDETIASS-DKPVLVDFWAPWCGPCKMIAPILEELAKEYEGKVKFVKLNVDENPDIAAKYGIRSIPTLLLFKNGK 79

                          90       100
                  ....*....|....*....|..
gi 504695724   89 PVDGFQGPQPEEAIRALLDKVL 110
Cdd:TIGR01068  80 EVDRSVGALPKAALKQLINKNL 101
PRK10996 PRK10996
thioredoxin 2; Provisional
 6-110 2.25e-19

thioredoxin 2; Provisional


Pssm-ID: 182889 [Multi-domain]  Cd Length: 139  Bit Score: 82.04  E-value: 2.25e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695724   6 IVNITEANLQQILEQSmaKPVLFYFWSERSQHCLQLTPVLESLAAQYNGQFILAKLDCDAEPMVASQFGLRAIPTVYLFQ 85
Cdd:PRK10996  37 VINATGETLDKLLQDD--LPVVIDFWAPWCGPCRNFAPIFEDVAAERSGKVRFVKVNTEAERELSARFRIRSIPTIMIFK 114

                         90       100
                 ....*....|....*....|....*
gi 504695724  86 NGQPVDGFQGPQPEEAIRALLDKVL 110
Cdd:PRK10996 115 NGQVVDMLNGAVPKAPFDSWLNEAL 139
TPR_19 pfam14559
Tetratricopeptide repeat;
127-190 1.34e-09

Tetratricopeptide repeat;


Pssm-ID: 434038 [Multi-domain]  Cd Length: 65  Bit Score: 53.36  E-value: 1.34e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504695724  127 EGKYDEALPLLKDAWQLSNQNSQIGLLLAETQIALHRSEDAEAVLKTVPLQDQDT-RYQGLVAQI 190
Cdd:pfam14559   1 EGDYAEALELLEQALAEDPDNAEARLGLAEALLALGRLDEAEALLAALPAADPDDpRYAALLAKL 65
PRK11788 PRK11788
tetratricopeptide repeat protein; Provisional
 121-245 1.89e-03

tetratricopeptide repeat protein; Provisional


Pssm-ID: 236983 [Multi-domain]  Cd Length: 389  Bit Score: 39.41  E-value: 1.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695724 121 AMALMQEGKYDEALPLLKDAWQLSNQNSQIGLLLAETQIALHRSEDAEAVLKTVPlqDQDTRYQGLVAqiELLKQAA--- 197
Cdd:PRK11788 187 AQQALARGDLDAARALLKKALAADPQCVRASILLGDLALAQGDYAAAIEALERVE--EQDPEYLSEVL--PKLMECYqal 262

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 504695724 198 -DTPEIQQLQQQVADNPADAALASQLALQLHQVGRNEEALELLFSHLQK 245
Cdd:PRK11788 263 gDEAEGLEFLRRALEEYPGADLLLALAQLLEEQEGPEAAQALLREQLRR 311
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 97-215 1.96e-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: 37.86  E-value: 1.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695724  97 QPEEAIRAL--LDKVLPREEELKAQEAMALMQEGKYDEALPLLKDAWQLSNQNSQIGLLLAETQIALHRSEDAEAVLKTV 174
Cdd:COG4783   19 DYDEAEALLekALELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNLGLALLKAGDYDEALALLEKA 98

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 504695724 175 pLQDQDTRYQGLVAQIELLKQAADTPE-IQQLQQQVADNPAD 215
Cdd:COG4783   99 -LKLDPEHPEAYLRLARAYRALGRPDEaIAALEKALELDPDD 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 3.36e-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: 140.10  E-value: 3.36e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695724  12 ANLQQILEQSMAKPVLFYFWSERSQHCLQLTPVLESLAAQYNGQFILAKLDCDAEPMVASQFGLRAIPTVYLFQNGQPVD 91
Cdd:cd02956    1 QNFQQVLQESTQVPVVVDFWAPRSPPSKELLPLLERLAEEYQGQFVLAKVNCDAQPQIAQQFGVQALPTVYLFAAGQPVD 80

                         90
                 ....*....|....*.
gi 504695724  92 GFQGPQPEEAIRALLD 107
Cdd:cd02956   81 GFQGAQPEEQLRQMLD 96
CnoX COG3118
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ...
 5-110 6.05e-42

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: 139.57  E-value: 6.05e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695724   5 NIVNITEANLQQILEQSmAKPVLFYFWSERSQHCLQLTPVLESLAAQYNGQFILAKLDCDAEPMVASQFGLRAIPTVYLF 84
Cdd:COG3118    1 AVVELTDENFEEEVLES-DKPVLVDFWAPWCGPCKMLAPVLEELAAEYGGKVKFVKVDVDENPELAAQFGVRSIPTLLLF 79

                         90       100
                 ....*....|....*....|....*.
gi 504695724  85 QNGQPVDGFQGPQPEEAIRALLDKVL 110
Cdd:COG3118   80 KDGQPVDRFVGALPKEQLREFLDKVL 105
TPR_20 pfam14561
Tetratricopeptide repeat;
195-284 1.32e-33

Tetratricopeptide repeat;


Pssm-ID: 434039 [Multi-domain]  Cd Length: 90  Bit Score: 117.61  E-value: 1.32e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695724  195 QAADTPEIQQLQQQVADNPADAALASQLALQLHQVGRNEEALELLFSHLQKDLAAADGQARKMFQEILAALGTGDALASK 274
Cdd:pfam14561   1 QAADAPELAALEARLAADPDDLDARLDLALALHAAGRNEEALELLLEILRRDRNWNDGAARKQLLDIFEALGPGDPLVAK 80

                          90
                  ....*....|
gi 504695724  275 YRRQLYALLY 284
Cdd:pfam14561  81 YRRKLSSLLF 90
Thioredoxin pfam00085
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 5-108 2.27e-27

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: 101.93  E-value: 2.27e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695724    5 NIVNITEANLQQILeQSMAKPVLFYFWSERSQHCLQLTPVLESLAAQYNGQFILAKLDCDAEPMVASQFGLRAIPTVYLF 84
Cdd:pfam00085   1 VVVVLTDANFDEVV-QKSSKPVLVDFYAPWCGPCKMLAPEYEELAQEYKGNVVFAKVDVDENPDLASKYGVRGYPTLIFF 79

                          90       100
                  ....*....|....*....|....
gi 504695724   85 QNGQPVDGFQGPQPEEAIRALLDK 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 8.04e-25

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: 94.93  E-value: 8.04e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695724  12 ANLQQILEQSmaKPVLFYFWSERSQHCLQLTPVLESLAAQYnGQFILAKLDCDAEPMVASQFGLRAIPTVYLFQNGQPVD 91
Cdd:cd02947    1 EEFEELIKSA--KPVVVDFWAPWCGPCKAIAPVLEELAEEY-PKVKFVKVDVDENPELAEEYGVRSIPTFLFFKNGKEVD 77

                         90
                 ....*....|....*.
gi 504695724  92 GFQGPQPEEAIRALLD 107
Cdd:cd02947   78 RVVGADPKEELEEFLE 93
thioredoxin TIGR01068
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ...
 9-110 1.02e-23

thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of a domain closely related to thioredoxin. This model is designed to recognize authentic thioredoxin, a small protein that should be hit exactly once by this model. Any protein that hits once with a score greater than the second (per domain) trusted cutoff may be taken as thioredoxin. [Energy metabolism, Electron transport]


Pssm-ID: 200072 [Multi-domain]  Cd Length: 101  Bit Score: 92.35  E-value: 1.02e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695724    9 ITEANLQQILEQSmAKPVLFYFWSERSQHCLQLTPVLESLAAQYNGQFILAKLDCDAEPMVASQFGLRAIPTVYLFQNGQ 88
Cdd:TIGR01068   1 LTDANFDETIASS-DKPVLVDFWAPWCGPCKMIAPILEELAKEYEGKVKFVKLNVDENPDIAAKYGIRSIPTLLLFKNGK 79

                          90       100
                  ....*....|....*....|..
gi 504695724   89 PVDGFQGPQPEEAIRALLDKVL 110
Cdd:TIGR01068  80 EVDRSVGALPKAALKQLINKNL 101
PRK10996 PRK10996
thioredoxin 2; Provisional
 6-110 2.25e-19

thioredoxin 2; Provisional


Pssm-ID: 182889 [Multi-domain]  Cd Length: 139  Bit Score: 82.04  E-value: 2.25e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695724   6 IVNITEANLQQILEQSmaKPVLFYFWSERSQHCLQLTPVLESLAAQYNGQFILAKLDCDAEPMVASQFGLRAIPTVYLFQ 85
Cdd:PRK10996  37 VINATGETLDKLLQDD--LPVVIDFWAPWCGPCRNFAPIFEDVAAERSGKVRFVKVNTEAERELSARFRIRSIPTIMIFK 114

                         90       100
                 ....*....|....*....|....*
gi 504695724  86 NGQPVDGFQGPQPEEAIRALLDKVL 110
Cdd:PRK10996 115 NGQVVDMLNGAVPKAPFDSWLNEAL 139
PDI_a_family cd02961
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ...
 7-104 7.79e-13

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: 63.40  E-value: 7.79e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695724   7 VNITEANLQQILEQSmaKPVLFYFWSERSQHCLQLTPVLESLAAQY--NGQFILAKLDCDAEPMVASQFGLRAIPTVYLF 84
Cdd:cd02961    1 VELTDDNFDELVKDS--KDVLVEFYAPWCGHCKALAPEYEKLAKELkgDGKVVVAKVDCTANNDLCSEYGVRGYPTIKLF 78

                         90       100
                 ....*....|....*....|..
gi 504695724  85 QNG--QPVDgFQGPQPEEAIRA 104
Cdd:cd02961   79 PNGskEPVK-YEGPRTLESLVE 99
trxA PRK09381
thioredoxin TrxA;
30-110 4.79e-12

thioredoxin TrxA;


Pssm-ID: 181812 [Multi-domain]  Cd Length: 109  Bit Score: 61.23  E-value: 4.79e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695724  30 FWSERSQHCLQLTPVLESLAAQYNGQFILAKLDCDAEPMVASQFGLRAIPTVYLFQNGQPVDGFQGPQPEEAIRALLDKV 109
Cdd:PRK09381  28 FWAEWCGPCKMIAPILDEIADEYQGKLTVAKLNIDQNPGTAPKYGIRGIPTLLLFKNGEVAATKVGALSKGQLKEFLDAN 107


                 .
gi 504695724 110 L 110
Cdd:PRK09381 108 L 108
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 18-110 1.76e-11

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 60.47  E-value: 1.76e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695724  18 LEQSMAKPVLFYFWSERSQHCLQLTPVLESLAAQYNG-QFILAKLD--------------------CDAEPMVASQFGLR 76
Cdd:COG0526   23 LADLKGKPVLVNFWATWCPPCRAEMPVLKELAEEYGGvVFVGVDVDenpeavkaflkelglpypvlLDPDGELAKAYGVR 102

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 504695724  77 AIPTVYLF-QNGQPVDGFQGPQPEEAIRALLDKVL 110
Cdd:COG0526  103 GIPTTVLIdKDGKIVARHVGPLSPEELEEALEKLL 137
TRX_PICOT cd02984
TRX domain, PICOT (for PKC-interacting cousin of TRX) subfamily; PICOT is a protein that ...
 10-100 1.16e-10

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: 57.28  E-value: 1.16e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695724  10 TEANLQQILEQSMAKPVLFYFWSERSQHCLQLTPVLESLAAQYNGQFILAKLDCDAEPMVASQFGLRAIPTVYLFQNGQP 89
Cdd:cd02984    1 SEEEFEELLKSDASKLLVLHFWAPWAEPCKQMNQVFEELAKEAFPSVLFLSIEAEELPEISEKFEITAVPTFVFFRNGTI 80

                         90
                 ....*....|.
gi 504695724  90 VDGFQGPQPEE 100
Cdd:cd02984   81 VDRVSGADPKE 91
PDI_a_P5 cd03001
PDIa family, P5 subfamily; composed of eukaryotic proteins similar to human P5, a PDI-related ...
 5-102 4.49e-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: 55.76  E-value: 4.49e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695724   5 NIVNITEANLQQILEQSMAkPVLFYFWSERSQHCLQLTPVLESLAAQYNGQFILAKLDCDAEPMVASQFGLRAIPTVYLF 84
Cdd:cd03001    1 DVVELTDSNFDKKVLNSDD-VWLVEFYAPWCGHCKNLAPEWKKAAKALKGIVKVGAVDADVHQSLAQQYGVRGFPTIKVF 79

                         90       100
                 ....*....|....*....|
gi 504695724  85 QNGQ--PVDgFQGPQPEEAI 102
Cdd:cd03001   80 GAGKnsPQD-YQGGRTAKAI 98
PDI_a_ERp46 cd03005
PDIa family, endoplasmic reticulum protein 46 (ERp46) subfamily; ERp46 is an ER-resident ...
 37-104 7.15e-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: 54.98  E-value: 7.15e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504695724  37 HCLQLTPVLESLAAQY---NGQFILAKLDCDAEPMVASQFGLRAIPTVYLFQNGQPVDGFQGPQPEEAIRA 104
Cdd:cd03005   30 HCKRLAPTWEQLAKKFnneNPSVKIAKVDCTQHRELCSEFQVRGYPTLLLFKDGEKVDKYKGTRDLDSLKE 100
TPR_19 pfam14559
Tetratricopeptide repeat;
127-190 1.34e-09

Tetratricopeptide repeat;


Pssm-ID: 434038 [Multi-domain]  Cd Length: 65  Bit Score: 53.36  E-value: 1.34e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504695724  127 EGKYDEALPLLKDAWQLSNQNSQIGLLLAETQIALHRSEDAEAVLKTVPLQDQDT-RYQGLVAQI 190
Cdd:pfam14559   1 EGDYAEALELLEQALAEDPDNAEARLGLAEALLALGRLDEAEALLAALPAADPDDpRYAALLAKL 65
PDI_a_ERp44 cd02996
PDIa family, endoplasmic reticulum protein 44 (ERp44) subfamily; ERp44 is an ER-resident ...
 5-88 1.81e-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: 54.32  E-value: 1.81e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695724   5 NIVNITEANLQQILEQSMAKPVLFYF-WSERSQhclQLTPVLESLAAQYN------GQFILAKLDCDAEPMVASQFGLRA 77
Cdd:cd02996    2 EIVSLTSGNIDDILQSAELVLVNFYAdWCRFSQ---MLHPIFEEAAAKIKeefpdaGKVVWGKVDCDKESDIADRYRINK 78

                         90
                 ....*....|.
gi 504695724  78 IPTVYLFQNGQ 88
Cdd:cd02996   79 YPTLKLFRNGM 89
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 37-239 2.25e-09

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 57.70  E-value: 2.25e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695724  37 HCLQLTPVLESLAAQYNGQFILAKLDCDAEPMVASQFGLRAiptvYLFQNGQPVDGFQGPQPEEAIRALLDKVLPREEEL 116
Cdd:COG3914    5 ALLALAALAAAALLAAAAAAELALAAELEAAALAAALGLAL----LLLAALAEAAAAALLALAAGEAAAAAAALLLLAAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695724 117 KAQEAMALMQEGKYDEALPLLKDAWQLSNQNSQIGLLLAETQIALHRSEDAEAVLKTVpLQDQDTRYQGLVAQIELLKQA 196
Cdd:COG3914   81 LELAALLLQALGRYEEALALYRRALALNPDNAEALFNLGNLLLALGRLEEALAALRRA-LALNPDFAEAYLNLGEALRRL 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 504695724 197 ADTPE-IQQLQQQVADNPADAALASQLALQLHQVGRNEEALELL 239
Cdd:COG3914  160 GRLEEaIAALRRALELDPDNAEALNNLGNALQDLGRLEEAIAAY 203
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 6-102 1.07e-08

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 55.53  E-value: 1.07e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695724   6 IVNITEANLQQILEQSmaKPVLFYFWSERSQHCLQLTPVLESLAAQYN---GQFILAKLDCDAEPMVASQFGLRAIPTVY 82
Cdd:PTZ00102  34 VTVLTDSTFDKFITEN--EIVLVKFYAPWCGHCKRLAPEYKKAAKMLKekkSEIVLASVDATEEMELAQEFGVRGYPTIK 111

                         90       100
                 ....*....|....*....|
gi 504695724  83 LFQNGQPVDgFQGPQPEEAI 102
Cdd:PTZ00102 112 FFNKGNPVN-YSGGRTADGI 130
PTZ00443 PTZ00443
Thioredoxin domain-containing protein; Provisional
 6-88 2.49e-08

Thioredoxin domain-containing protein; Provisional


Pssm-ID: 185622 [Multi-domain]  Cd Length: 224  Bit Score: 53.48  E-value: 2.49e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695724   6 IVNITEANLQQILEQSMAK---PVLFYFWSERSQHCLQLTPVLESLAAQYNGQFILAKLDCDAEPMVASQFGLRAIPTVY 82
Cdd:PTZ00443  32 LVLLNDKNFEKLTQASTGAttgPWFVKFYAPWCSHCRKMAPAWERLAKALKGQVNVADLDATRALNLAKRFAIKGYPTLL 111


                 ....*.
gi 504695724  83 LFQNGQ 88
Cdd:PTZ00443 112 LFDKGK 117
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 97-279 3.75e-07

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: 50.11  E-value: 3.75e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695724  97 QPEEAIRALLDKVLPREEELKAQE--AMALMQEGKYDEALPLLKDAWQLSNQNSQIGLLLAETQIALHRSEDAEAVLKT- 173
Cdd:COG2956   57 EYDRAIRIHQKLLERDPDRAEALLelAQDYLKAGLLDRAEELLEKLLELDPDDAEALRLLAEIYEQEGDWEKAIEVLERl 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695724 174 VPLQDQDTRYQGLVAQIELLKQAADTpEIQQLQQQVADNPADAALASQLALQLHQVGRNEEALELLFSHLQKDlaAADGQ 253
Cdd:COG2956  137 LKLGPENAHAYCELAELYLEQGDYDE-AIEALEKALKLDPDCARALLLLAELYLEQGDYEEAIAALERALEQD--PDYLP 213

                        170       180
                 ....*....|....*....|....*.
gi 504695724 254 ARKMFQEILAALGTGDALASKYRRQL 279
Cdd:COG2956  214 ALPRLAELYEKLGDPEEALELLRKAL 239
TRX_superfamily cd01659
Thioredoxin (TRX) superfamily; a large, diverse group of proteins containing a TRX-fold. Many ...
 27-90 2.52e-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: 44.23  E-value: 2.52e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504695724  27 LFYFWSERSQHCLQLTPVLESLAAqYNGQFILAKLDCDAEP---MVASQFGLRAIPTVYLFQNGQPV 90
Cdd:cd01659    1 LVLFYAPWCPFCQALRPVLAELAL-LNKGVKFEAVDVDEDPaleKELKRYGVGGVPTLVVFGPGIGV 66
PDI_a_TMX3 cd03000
PDIa family, TMX3 subfamily; composed of eukaryotic proteins similar to human TMX3, a TRX ...
 30-102 2.54e-06

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: 45.14  E-value: 2.54e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504695724  30 FWSERSQHCLQLTPVLESLAAQ---YNGQFILAKLDCDAEPMVASQFGLRAIPTVYLFQNGQPVDgFQGPQPEEAI 102
Cdd:cd03000   22 FYAPWCGHCKKLEPVWNEVGAElksSGSPVRVGKLDATAYSSIASEFGVRGYPTIKLLKGDLAYN-YRGPRTKDDI 96
PDI_a_MPD1_like cd03002
PDI family, MPD1-like subfamily; composed of eukaryotic proteins similar to Saccharomyces ...
 5-104 3.92e-06

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: 44.66  E-value: 3.92e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695724   5 NIVNITEANLQQILEQSMAKP-VLFYF-WSersQHCLQLTPVLESLAAQYNGQFILAKLDCDAEP--MVASQFGLRAIPT 80
Cdd:cd03002    1 PVYELTPKNFDKVVHNTNYTTlVEFYApWC---GHCKNLKPEYAKAAKELDGLVQVAAVDCDEDKnkPLCGKYGVQGFPT 77

                         90       100
                 ....*....|....*....|....*....
gi 504695724  81 VYLFQNGQP-----VDGFQGPQPEEAIRA 104
Cdd:cd03002   78 LKVFRPPKKaskhaVEDYNGERSAKAIVD 106
PTZ00051 PTZ00051
thioredoxin; Provisional
 10-99 4.02e-06

thioredoxin; Provisional


Pssm-ID: 173347 [Multi-domain]  Cd Length: 98  Bit Score: 44.48  E-value: 4.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695724  10 TEANLQQILEQSmaKPVLFYFWSERSQHCLQLTPVLESLAAQYNgQFILAKLDCDAEPMVASQFGLRAIPTVYLFQNGQP 89
Cdd:PTZ00051   7 SQAEFESTLSQN--ELVIVDFYAEWCGPCKRIAPFYEECSKEYT-KMVFVKVDVDELSEVAEKENITSMPTFKVFKNGSV 83

                         90
                 ....*....|
gi 504695724  90 VDGFQGPQPE 99
Cdd:PTZ00051  84 VDTLLGANDE 93
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 97-246 4.25e-06

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


Pssm-ID: 442196 [Multi-domain]  Cd Length: 275  Bit Score: 47.03  E-value: 4.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695724  97 QPEEAIRAL--LDKVLPREEELKAQEAMALMQEGKYDEALPLLKDAWQLSNQNSQIGLLLAETQIALHRSEDAEAVLKTV 174
Cdd:COG2956  125 DWEKAIEVLerLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKALKLDPDCARALLLLAELYLEQGDYEEAIAALERA 204

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504695724 175 PLQDQDtRYQGLVAQIELLKQAADTPEIQQLQQQVADNPADAALASQLALQLHQVGRNEEALELLFSHLQKD 246
Cdd:COG2956  205 LEQDPD-YLPALPRLAELYEKLGDPEEALELLRKALELDPSDDLLLALADLLERKEGLEAALALLERQLRRH 275
TRX_NTR cd02949
TRX domain, novel NADPH thioredoxin reductase (NTR) family; composed of fusion proteins found ...
 24-107 8.86e-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: 43.64  E-value: 8.86e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695724  24 KPVLFYFWSERSQHCLQLTPVLESLAAQYNGQFILAKLDCDAEPMVASQFGLRAIPTVYLFQNGQPVDGFQGPQPEEAIR 103
Cdd:cd02949   14 RLILVLYTSPTCGPCRTLKPILNKVIDEFDGAVHFVEIDIDEDQEIAEAAGIMGTPTVQFFKDKELVKEISGVKMKSEYR 93


                 ....
gi 504695724 104 ALLD 107
Cdd:cd02949   94 EFIE 97
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 13-108 2.16e-05

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 45.51  E-value: 2.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695724  13 NLQQILEQSmAKPVLFYFWSERSQHCLQLTPVLESLAAQY--NGQFILAKLDCDAEPMVASQFGLRAIPTVYLFQNGQ-- 88
Cdd:PTZ00102 366 TFEEIVFKS-DKDVLLEIYAPWCGHCKNLEPVYNELGEKYkdNDSIIVAKMNGTANETPLEEFSWSAFPTILFVKAGErt 444

                         90       100
                 ....*....|....*....|
gi 504695724  89 PVDgFQGPQPEEAIRALLDK 108
Cdd:PTZ00102 445 PIP-YEGERTVEGFKEFVNK 463
LapB COG2956
Lipopolysaccharide biosynthesis regulator YciM/LapB, contains six TPR domains and a C-terminal ...
 97-279 3.21e-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: 3.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695724  97 QPEEAIRALLDKVLPREEELKAQEAMA--LMQEGKYDEALPLLKDAWQLSNQNSQIGLLLAETQIALHRSEDAEAVLKTV 174
Cdd:COG2956   23 QPDKAIDLLEEALELDPETVEAHLALGnlYRRRGEYDRAIRIHQKLLERDPDRAEALLELAQDYLKAGLLDRAEELLEKL 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695724 175 pLQDQDTRYQGLVAQIELLKQAADTPE-IQQLQQQVADNPADAALASQLALQLHQVGRNEEALELLFSHLQKDLAAADgq 253
Cdd:COG2956  103 -LELDPDDAEALRLLAEIYEQEGDWEKaIEVLERLLKLGPENAHAYCELAELYLEQGDYDEAIEALEKALKLDPDCAR-- 179

                        170       180
                 ....*....|....*....|....*.
gi 504695724 254 ARKMFQEILAALGTGDALASKYRRQL 279
Cdd:COG2956  180 ALLLLAELYLEQGDYEEAIAALERAL 205
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 112-246 3.30e-05

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: 42.87  E-value: 3.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695724 112 REEELKAQEAMALMQEGKYDEALPLLKDAWQLSNQNSQIGLLLAETQIALHRSEDAEAVLKT-VPLQDQDTRYQGLVAQI 190
Cdd:COG4783    2 ACAEALYALAQALLLAGDYDEAEALLEKALELDPDNPEAFALLGEILLQLGDLDEAIVLLHEaLELDPDEPEARLNLGLA 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 504695724 191 ELLKQAADTpEIQQLQQQVADNPADAALASQLALQLHQVGRNEEALELLFSHLQKD 246
Cdd:COG4783   82 LLKAGDYDE-ALALLEKALKLDPEHPEAYLRLARAYRALGRPDEAIAALEKALELD 136
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 5-120 5.61e-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: 44.28  E-value: 5.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695724    5 NIVNITEANLQQILEQSMAKPVLFYF-WSersQHCLQLTPVLESLAAQY--NGQFI-LAKLDCDAEPMVASQFGLRAIPT 80
Cdd:TIGR01130   2 DVLVLTKDNFDDFIKSHEFVLVEFYApWC---GHCKSLAPEYEKAADELkkKGPPIkLAKVDATEEKDLAQKYGVSGYPT 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 504695724   81 VYLFQNGQPVDG-FQGPQPEEAIRA-LLDKVLPREEELKAQE 120
Cdd:TIGR01130  79 LKIFRNGEDSVSdYNGPRDADGIVKyMKKQSGPAVKEIETVA 120
PDI_a_ERdj5_C cd03004
PDIa family, C-terminal ERdj5 subfamily; ERdj5, also known as JPDI and macrothioredoxin, is a ...
 37-84 1.16e-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: 40.35  E-value: 1.16e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 504695724  37 HCLQLTPVLESLAAQYNGQFILAKLDCDAEPMVASQFGLRAIPTVYLF 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 ...
 30-102 1.39e-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: 40.20  E-value: 1.39e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504695724  30 FWSERSQHCLQLTPVLESLAAQYNGQFILAKLDCDAEPMVASQFGLRAIPTVYLFQNGQPVDGFQGPQPEEAI 102
Cdd:cd03003   25 FYSPRCSHCHDLAPTWREFAKEMDGVIRIGAVNCGDDRMLCRSQGVNSYPSLYVFPSGMNPEKYYGDRSKESL 97
TPR COG0457
Tetratricopeptide (TPR) repeat [General function prediction only];
97-284 1.93e-04

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


Pssm-ID: 440225 [Multi-domain]  Cd Length: 245  Bit Score: 41.92  E-value: 1.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695724  97 QPEEAIrALLDKVL---PREEELKAQEAMALMQEGKYDEALPLLKDAWQLSNQNSQIGLLLAETQIALHRSEDAEAVLKT 173
Cdd:COG0457   23 RYEEAI-EDYEKALeldPDDAEALYNLGLAYLRLGRYEEALADYEQALELDPDDAEALNNLGLALQALGRYEEALEDYDK 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695724 174 VpLQDQDTRYQGLVAQIELLKQAADTPE-IQQLQQQVADNPADAALASQLALQLHQVGRNEEALELLFSHLQKDLAAADG 252
Cdd:COG0457  102 A-LELDPDDAEALYNLGLALLELGRYDEaIEAYERALELDPDDADALYNLGIALEKLGRYEEALELLEKLEAAALAALLA 180

                        170       180       190
                 ....*....|....*....|....*....|..
gi 504695724 253 QARKMFQEILAALGTGDALASKYRRQLYALLY 284
Cdd:COG0457  181 AALGEAALALAAAEVLLALLLALEQALRKKLA 212
PRK11447 PRK11447
cellulose synthase subunit BcsC; Provisional
 97-246 4.99e-04

cellulose synthase subunit BcsC; Provisional


Pssm-ID: 183140 [Multi-domain]  Cd Length: 1157  Bit Score: 41.61  E-value: 4.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695724   97 QPEEAIRAL--LDKVLPREEELKAQEAMALMQEGKYDEALPLLKdawQLSNQN-----------SQIGLLLAETQ--IAL 161
Cdd:PRK11447  162 QRPEAINQLqrLNADYPGNTGLRNTLALLLFSSGRRDEGFAVLE---QMAKSPagrdaaaqlwyGQIKDMPVSDAsvAAL 238

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695724  162 HR-----SEDAEAVLKTVPLQDQ-----DTRYQGLVAQIELLKQAADTPEIQQLQQQVADNPADAALASQLALQLHQVGR 231
Cdd:PRK11447  239 QKylqvfSDGDSVAAARSQLAEQqkqlaDPAFRARAQGLAAVDSGQGGKAIPELQQAVRANPKDSEALGALGQAYSQQGD 318

                         170
                  ....*....|....*
gi 504695724  232 NEEALELLFSHLQKD 246
Cdd:PRK11447  319 RARAVAQFEKALALD 333
ER_PDI_fam TIGR01130
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ...
 24-108 8.40e-04

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


Pssm-ID: 273457 [Multi-domain]  Cd Length: 462  Bit Score: 40.43  E-value: 8.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695724   24 KPVLFYFWSERSQHCLQLTPVLESLAAQYNGQ---FILAKLDC---DAEPmvasqFGLRAIPTVYLFQNG---QPVDgFQ 94
Cdd:TIGR01130 365 KDVLVEFYAPWCGHCKNLAPIYEELAEKYKDAesdVVIAKMDAtanDVPP-----FEVEGFPTIKFVPAGkksEPVP-YD 438

                          90
                  ....*....|....
gi 504695724   95 GPQPEEAIRALLDK 108
Cdd:TIGR01130 439 GDRTLEDFSKFIAK 452
Spy COG3914
Predicted O-linked N-acetylglucosamine transferase, SPINDLY family [Posttranslational ...
 110-277 9.99e-04

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


Pssm-ID: 443119 [Multi-domain]  Cd Length: 658  Bit Score: 40.36  E-value: 9.99e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695724 110 LPREEELKAQEAMALMQEGKYDEALPLLKDAWQLSNQNSQIGLLLAETQIALHRSEDAEAVLKTVPLQDQDTRYQGLVAQ 189
Cdd:COG3914    6 LLALAALAAAALLAAAAAAELALAAELEAAALAAALGLALLLLAALAEAAAAALLALAAGEAAAAAAALLLLAALLELAA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695724 190 IELLKQAADTPEIQQLQQQVADNPADAALASQLALQLHQVGRNEEALEllfsHLQK--DLAAADGQARKMFQEILAALGT 267
Cdd:COG3914   86 LLLQALGRYEEALALYRRALALNPDNAEALFNLGNLLLALGRLEEALA----ALRRalALNPDFAEAYLNLGEALRRLGR 161

                        170
                 ....*....|
gi 504695724 268 GDALASKYRR 277
Cdd:COG3914  162 LEEAIAALRR 171
PDI_a_TMX cd02994
PDIa family, TMX subfamily; composed of proteins similar to the TRX-related human ...
 5-87 1.12e-03

PDIa family, TMX subfamily; composed of proteins similar to the TRX-related human transmembrane protein, TMX. TMX is a type I integral membrane protein; the N-terminal redox active TRX domain is present in the endoplasmic reticulum (ER) lumen while the C-terminus is oriented towards the cytoplasm. It is expressed in many cell types and its active site motif (CPAC) is unique. In vitro, TMX reduces interchain disulfides of insulin and renatures inactive RNase containing incorrect disulfide bonds. The C. elegans homolog, DPY-11, is expressed only in the hypodermis and resides in the cytoplasm. It is required for body and sensory organ morphogeneis. Another uncharacterized TRX-related transmembrane protein, human TMX4, is included in the alignment. The active site sequence of TMX4 is CPSC.


Pssm-ID: 239292 [Multi-domain]  Cd Length: 101  Bit Score: 37.74  E-value: 1.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695724   5 NIVNITEANLQQILE-QSMAKpvlfyFWSERSQHCLQLTPVLESLAAQYNG-QFILAKLDCDAEPMVASQFGLRAIPTVY 82
Cdd:cd02994    2 NVVELTDSNWTLVLEgEWMIE-----FYAPWCPACQQLQPEWEEFADWSDDlGINVAKVDVTQEPGLSGRFFVTALPTIY 76


                 ....*
gi 504695724  83 LFQNG 87
Cdd:cd02994   77 HAKDG 81
TRX_DnaJ cd02963
TRX domain, DnaJ domain containing protein family; composed of uncharacterized proteins of ...
 9-109 1.62e-03

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: 37.35  E-value: 1.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695724   9 ITEANLQ-QILEQSMAKPVLFYFWSERSQHCLQLTPV-------LESLAAQYngqfilAKLDCDAEPMVASQFGLRAIPT 80
Cdd:cd02963    9 LTFSQYEnEIVPKSFKKPYLIKITSDWCFSCIHIEPVwkeviqeLEPLGVGI------ATVNAGHERRLARKLGAHSVPA 82

                         90       100
                 ....*....|....*....|....*....
gi 504695724  81 VYLFQNGQPVDGFQGPQPEEAIRALLDKV 109
Cdd:cd02963   83 IVGIINGQVTFYHDSSFTKQHVVDFVRKL 111
PRK11788 PRK11788
tetratricopeptide repeat protein; Provisional
 121-245 1.89e-03

tetratricopeptide repeat protein; Provisional


Pssm-ID: 236983 [Multi-domain]  Cd Length: 389  Bit Score: 39.41  E-value: 1.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695724 121 AMALMQEGKYDEALPLLKDAWQLSNQNSQIGLLLAETQIALHRSEDAEAVLKTVPlqDQDTRYQGLVAqiELLKQAA--- 197
Cdd:PRK11788 187 AQQALARGDLDAARALLKKALAADPQCVRASILLGDLALAQGDYAAAIEALERVE--EQDPEYLSEVL--PKLMECYqal 262

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 504695724 198 -DTPEIQQLQQQVADNPADAALASQLALQLHQVGRNEEALELLFSHLQK 245
Cdd:PRK11788 263 gDEAEGLEFLRRALEEYPGADLLLALAQLLEEQEGPEAAQALLREQLRR 311
BepA COG4783
Outer membrane protein chaperone/metalloprotease BepA/YfgC, contains M48 and TPR domains [Cell ...
 97-215 1.96e-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: 37.86  E-value: 1.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695724  97 QPEEAIRAL--LDKVLPREEELKAQEAMALMQEGKYDEALPLLKDAWQLSNQNSQIGLLLAETQIALHRSEDAEAVLKTV 174
Cdd:COG4783   19 DYDEAEALLekALELDPDNPEAFALLGEILLQLGDLDEAIVLLHEALELDPDEPEARLNLGLALLKAGDYDEALALLEKA 98

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 504695724 175 pLQDQDTRYQGLVAQIELLKQAADTPE-IQQLQQQVADNPAD 215
Cdd:COG4783   99 -LKLDPEHPEAYLRLARAYRALGRPDEaIAALEKALELDPDD 139
COG4700 COG4700
Uncharacterized conserved protein ECs_4300, contains TPR-like domain [Function unknown];
81-262 2.03e-03

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


Pssm-ID: 443735 [Multi-domain]  Cd Length: 249  Bit Score: 38.71  E-value: 2.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695724  81 VYLFQNGQPvDGFQGPQPEEAIRALLDKVLPREEELKAQE--------------AMALMQEGKYDEALPLLKDAWQLSNQ 146
Cdd:COG4700   43 IYFFAEVLP-ELRNSRDARRVQRAARNALDPGRELRELEKalefadtvqnrvrlADALLELGRYDEAIELYEEALTGIFA 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695724 147 NSQIGLL-LAETQIALHRSEDAEAVLKTVPLQDQDTR---YQGLVAQIelLKQAADTPEIQQLQQQVADNPADAALASQL 222
Cdd:COG4700  122 DDPHILLgLAQALFELGRYAEALETLEKLIAKNPDFKssdAHLLYARA--LEALGDLEAAEAELEALARRYSGPEARYRY 199

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 504695724 223 ALQLHQVGRNEEALElLFSHLQKDLAAADGQARKMFQEIL 262
Cdd:COG4700  200 AKFLARQGRTAEAKE-LLEEILDEAKHMPKHYRRLNREWI 238
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 24-95 4.09e-03

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


Pssm-ID: 239264 [Multi-domain]  Cd Length: 116  Bit Score: 36.45  E-value: 4.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695724  24 KPVLFYFWSERSQHCLQLTPVLESLAAQYNG---QFI---------------LAKLDC------DAEPMVASQFGLRAIP 79
Cdd:cd02966   20 KVVLVNFWASWCPPCRAEMPELEALAKEYKDdgvEVVgvnvddddpaavkafLKKYGItfpvllDPDGELAKAYGVRGLP 99

                         90
                 ....*....|....*..
gi 504695724  80 TVYLF-QNGQPVDGFQG 95
Cdd:cd02966  100 TTFLIdRDGRIRARHVG 116
NrfG COG4235
Cytochrome c-type biogenesis protein CcmH/NrfG [Energy production and conversion, ...
 111-219 4.67e-03

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: 36.52  E-value: 4.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695724 111 PREEELKAQEAMALMQEGKYDEALPLLKDAWQLSNQNSQIGLLLAETQIALHRSEDAEAVLKTV-PLQDQDTRYQGLVAQ 189
Cdd:COG4235   14 PNDAEGWLLLGRAYLRLGRYDEALAAYEKALRLDPDNADALLDLAEALLAAGDTEEAEELLERAlALDPDNPEALYLLGL 93

                         90       100       110
                 ....*....|....*....|....*....|.
gi 504695724 190 IelLKQAADTPE-IQQLQQQVADNPADAALA 219
Cdd:COG4235   94 A--AFQQGDYAEaIAAWQKLLALLPADAPAR 122
Phd_like_TxnDC9 cd02989
Phosducin (Phd)-like family, Thioredoxin (TRX) domain containing protein 9 (TxnDC9) subfamily; ...
 45-95 6.04e-03

Phosducin (Phd)-like family, Thioredoxin (TRX) domain containing protein 9 (TxnDC9) subfamily; composed of predominantly uncharacterized eukaryotic proteins, containing a TRX-like domain without the redox active CXXC motif. The gene name for the human protein is TxnDC9. The two characterized members are described as Phd-like proteins, PLP1 of Saccharomyces cerevisiae and PhLP3 of Dictyostelium discoideum. Gene disruption experiments show that both PLP1 and PhLP3 are non-essential proteins. Unlike Phd and most Phd-like proteins, members of this group do not contain the Phd N-terminal helical domain which is implicated in binding to the G protein betagamma subunit.


Pssm-ID: 239287  Cd Length: 113  Bit Score: 35.63  E-value: 6.04e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 504695724  45 LESLAAQY-NGQFIlaKLDCDAEPMVASQFGLRAIPTVYLFQNGQPVD---GFQG 95
Cdd:cd02989   44 LEILAKKHlETKFI--KVNAEKAPFLVEKLNIKVLPTVILFKNGKTVDrivGFEE 96
 
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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