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Conserved domains on  [gi|501457143|ref|WP_012480588|]
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MULTISPECIES: DsbA family protein [Stenotrophomonas]

Protein Classification

DsbA family protein( domain architecture ID 10006587)

DsbA family protein similar to the thiol oxidoreductase FrnE, which is involved in frenolicin biosynthesis

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
FrnE COG2761
Predicted dithiol-disulfide isomerase, DsbA/YjbH family (virulence, stress resistance) ...
14-215 5.52e-39

Predicted dithiol-disulfide isomerase, DsbA/YjbH family (virulence, stress resistance) [Posttranslational modification, protein turnover, chaperones];


:

Pssm-ID: 442047 [Multi-domain]  Cd Length: 205  Bit Score: 133.09  E-value: 5.52e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501457143  14 VDFFHDVVCGWCFVLAPRLQQVSAELG--IQVRHRSFVLQDS-------RAQMVEVFGSMERAKAIiLRHWTDCAAHEDt 84
Cdd:COG2761    4 IDIFSDVVCPWCYIGKRRLEKALAEFGddVEIRWRPFELNPDmppegedRREYLLAKGSPEQAEQM-RAHVEEAAAEEG- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501457143  85 ARIDIEGMRaqdfeYPSGWLGALACQAAGMLGgndAHGAMFDAVQWAHLHQHRNIGDAEVLLDIAESLGHPRGAFADHMR 164
Cdd:COG2761   82 LPFDFDRIK-----PPNTFDAHRLLKAAELQG---KQDALLEALFEAYFTEGRDIGDREVLLDLAAEVGLDAEEFRADLE 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 501457143 165 SDAVRQRVQADRAEAAALGIRSIPT-VIGGNGLRLQTLPLPHLRQALAPLVA 215
Cdd:COG2761  154 SDEAAAAVRADEAEARELGVTGVPTfVFDGKYAVSGAQPYEVFEQALRQALA 205
 
Name Accession Description Interval E-value
FrnE COG2761
Predicted dithiol-disulfide isomerase, DsbA/YjbH family (virulence, stress resistance) ...
14-215 5.52e-39

Predicted dithiol-disulfide isomerase, DsbA/YjbH family (virulence, stress resistance) [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442047 [Multi-domain]  Cd Length: 205  Bit Score: 133.09  E-value: 5.52e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501457143  14 VDFFHDVVCGWCFVLAPRLQQVSAELG--IQVRHRSFVLQDS-------RAQMVEVFGSMERAKAIiLRHWTDCAAHEDt 84
Cdd:COG2761    4 IDIFSDVVCPWCYIGKRRLEKALAEFGddVEIRWRPFELNPDmppegedRREYLLAKGSPEQAEQM-RAHVEEAAAEEG- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501457143  85 ARIDIEGMRaqdfeYPSGWLGALACQAAGMLGgndAHGAMFDAVQWAHLHQHRNIGDAEVLLDIAESLGHPRGAFADHMR 164
Cdd:COG2761   82 LPFDFDRIK-----PPNTFDAHRLLKAAELQG---KQDALLEALFEAYFTEGRDIGDREVLLDLAAEVGLDAEEFRADLE 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 501457143 165 SDAVRQRVQADRAEAAALGIRSIPT-VIGGNGLRLQTLPLPHLRQALAPLVA 215
Cdd:COG2761  154 SDEAAAAVRADEAEARELGVTGVPTfVFDGKYAVSGAQPYEVFEQALRQALA 205
DsbA_FrnE_like cd03025
DsbA family, FrnE-like subfamily; composed of uncharacterized proteins containing a CXXC motif ...
17-191 1.08e-21

DsbA family, FrnE-like subfamily; composed of uncharacterized proteins containing a CXXC motif with similarity to DsbA and FrnE. FrnE is presumed to be a thiol oxidoreductase involved in polyketide biosynthesis, specifically in the production of the aromatic antibiotics frenolicin and nanaomycins.


Pssm-ID: 239323 [Multi-domain]  Cd Length: 193  Bit Score: 88.15  E-value: 1.08e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501457143  17 FHDVVCGWCFVLAPRLQQVSAELGIQVR---HRSFVLQDSRAQMVEvfgsmerAKAIILRHWTDcaahedtARIDIEGM- 92
Cdd:cd03025    6 FIDPLCGWCYGFEPLLEKLKEEYGGGIEvelHLGGLLPGNNARQIT-------KQWRIYVHWHK-------ARIALTGQp 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501457143  93 -----RAQD-FEYPSgwlgALACQA---AGMLGGNDAHgAMFDAVQWAHLHQHRNIGDAEVLLDIAESLGHPRGAFADHM 163
Cdd:cd03025   72 fgedyLELLlFDLDS----APASRAikaARLQGPERLL-EMLKAIQRAHYVEGRDLADTEVLRELAIELGLDVEEFLEDF 146
                        170       180
                 ....*....|....*....|....*...
gi 501457143 164 RSDAVRQRVQADRAEAAALGIRSIPTVI 191
Cdd:cd03025  147 QSDEAKQAIQEDQKLARELGINGFPTLV 174
DSBA pfam01323
DSBA-like thioredoxin domain; This family contains a diverse set of proteins with a ...
13-211 3.85e-14

DSBA-like thioredoxin domain; This family contains a diverse set of proteins with a thioredoxin-like structure pfam00085. This family also includes 2-hydroxychromene-2-carboxylate (HCCA) isomerase enzymes catalyze one step in prokaryotic polyaromatic hydrocarbon (PAH) catabolic pathways. This family also contains members with functions other than HCCA isomerization, such as Kappa family GSTs, whose similarity to HCCA isomerases was not previously recognized. The sequence Swiss:O07298 has been annotated as a dioxygenase but is almost certainly an HCCA isomerase enzyme. Similarly, the sequence Swiss:Q9ZI67 has been annotated as a dehydrogenase, but is most probably also an HCCA isomerase enzyme. In addition, the Rhizobium leguminosarum Swiss:Q52782 protein has been annotated as a putative glycerol-3-phosphate transfer protein, but is also most likely to be an HCCA isomerase enzyme.


Pssm-ID: 426200 [Multi-domain]  Cd Length: 191  Bit Score: 67.84  E-value: 3.85e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501457143   13 VVDFFHDVVCGWCFVLAPRLQQVSAELG-IQVRHRSFVL-QDSRAQMVEVFGSMERAKAIiLRHWTDCAAHEdtaRIDIE 90
Cdd:pfam01323   1 TVDEFFDFLCPFCYLAKERLEKLAARYGdVKVVYRPFPLaGAKKIGNVGPSNLPVKLKYM-MADLERWAALY---GIPLR 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501457143   91 GMRAQDFEYPSGWLGALACQAAGMLggNDAHGAMFDAVqWAhlhQHRNIGDAEVLLDIAESLGHPRGAFADHMRSDAVRQ 170
Cdd:pfam01323  77 FPANFLGNSTRANRLALAAGAEGLA--EKVVRELFNAL-WG---EGAAITDDSVLREVAEKAGLDAEEFDEFLDSPAVKE 150
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 501457143  171 RVQADRAEAAALGIRSIPTVIGGNGLRLQTLPLPHLRQALA 211
Cdd:pfam01323 151 AVRENTAAAISLGVFGVPTFVVGGKMVFGADRLDTLADALA 191
 
Name Accession Description Interval E-value
FrnE COG2761
Predicted dithiol-disulfide isomerase, DsbA/YjbH family (virulence, stress resistance) ...
14-215 5.52e-39

Predicted dithiol-disulfide isomerase, DsbA/YjbH family (virulence, stress resistance) [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442047 [Multi-domain]  Cd Length: 205  Bit Score: 133.09  E-value: 5.52e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501457143  14 VDFFHDVVCGWCFVLAPRLQQVSAELG--IQVRHRSFVLQDS-------RAQMVEVFGSMERAKAIiLRHWTDCAAHEDt 84
Cdd:COG2761    4 IDIFSDVVCPWCYIGKRRLEKALAEFGddVEIRWRPFELNPDmppegedRREYLLAKGSPEQAEQM-RAHVEEAAAEEG- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501457143  85 ARIDIEGMRaqdfeYPSGWLGALACQAAGMLGgndAHGAMFDAVQWAHLHQHRNIGDAEVLLDIAESLGHPRGAFADHMR 164
Cdd:COG2761   82 LPFDFDRIK-----PPNTFDAHRLLKAAELQG---KQDALLEALFEAYFTEGRDIGDREVLLDLAAEVGLDAEEFRADLE 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 501457143 165 SDAVRQRVQADRAEAAALGIRSIPT-VIGGNGLRLQTLPLPHLRQALAPLVA 215
Cdd:COG2761  154 SDEAAAAVRADEAEARELGVTGVPTfVFDGKYAVSGAQPYEVFEQALRQALA 205
DsbA_FrnE_like cd03025
DsbA family, FrnE-like subfamily; composed of uncharacterized proteins containing a CXXC motif ...
17-191 1.08e-21

DsbA family, FrnE-like subfamily; composed of uncharacterized proteins containing a CXXC motif with similarity to DsbA and FrnE. FrnE is presumed to be a thiol oxidoreductase involved in polyketide biosynthesis, specifically in the production of the aromatic antibiotics frenolicin and nanaomycins.


Pssm-ID: 239323 [Multi-domain]  Cd Length: 193  Bit Score: 88.15  E-value: 1.08e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501457143  17 FHDVVCGWCFVLAPRLQQVSAELGIQVR---HRSFVLQDSRAQMVEvfgsmerAKAIILRHWTDcaahedtARIDIEGM- 92
Cdd:cd03025    6 FIDPLCGWCYGFEPLLEKLKEEYGGGIEvelHLGGLLPGNNARQIT-------KQWRIYVHWHK-------ARIALTGQp 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501457143  93 -----RAQD-FEYPSgwlgALACQA---AGMLGGNDAHgAMFDAVQWAHLHQHRNIGDAEVLLDIAESLGHPRGAFADHM 163
Cdd:cd03025   72 fgedyLELLlFDLDS----APASRAikaARLQGPERLL-EMLKAIQRAHYVEGRDLADTEVLRELAIELGLDVEEFLEDF 146
                        170       180
                 ....*....|....*....|....*...
gi 501457143 164 RSDAVRQRVQADRAEAAALGIRSIPTVI 191
Cdd:cd03025  147 QSDEAKQAIQEDQKLARELGINGFPTLV 174
DsbA_FrnE cd03024
DsbA family, FrnE subfamily; FrnE is a DsbA-like protein containing a CXXC motif. It is ...
14-191 7.20e-19

DsbA family, FrnE subfamily; FrnE is a DsbA-like protein containing a CXXC motif. It is presumed to be a thiol oxidoreductase involved in polyketide biosynthesis, specifically in the production of the aromatic antibiotics frenolicin and nanaomycins.


Pssm-ID: 239322 [Multi-domain]  Cd Length: 201  Bit Score: 80.70  E-value: 7.20e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501457143  14 VDFFHDVVCGWCFVLAPRLQQVSAELG----IQVRHRSFVL--------QDSRAQMVEVFGSMERAkAIILRHWTDCAAH 81
Cdd:cd03024    1 IDIWSDVVCPWCYIGKRRLEKALAELGdevdVEIEWRPFELnpdmppegEDRREYLARKYGSTAEQ-AAAMRRVEAAAAA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501457143  82 EDTArIDIEGMRaqdfeYPSGWLGALACQAAGMLGgndAHGAMFDAVQWAHLHQHRNIGDAEVLLDIAESLGHPRGAFAD 161
Cdd:cd03024   80 EGLE-FDFDRVR-----PPNTFDAHRLIHLAKEQG---KQDALVEALFRAYFTEGKDIGDRDVLVDLAEEAGLDAAEARA 150
                        170       180       190
                 ....*....|....*....|....*....|
gi 501457143 162 HMRSDAVRQRVQADRAEAAALGIRSIPTVI 191
Cdd:cd03024  151 VLASDEYADEVRADEARARQLGISGVPFFV 180
COG3531 COG3531
Predicted protein-disulfide isomerase, contains CxxC motif [Posttranslational modification, ...
12-202 1.45e-18

Predicted protein-disulfide isomerase, contains CxxC motif [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442753 [Multi-domain]  Cd Length: 206  Bit Score: 79.91  E-value: 1.45e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501457143  12 PVVDFFHDVVCGWCFVLAPRLQQVSAELGIQVRhrsFVL------QDSRAQMVEvfgsmERAKAIILRHWTDCAA----- 80
Cdd:COG3531    2 PKLHYIYDPLCGWCYGFAPVIEALAEALGDRLD---VELlsgglfPGSNRRPMD-----PEMRAYIQPHWQRIAQltgqp 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501457143  81 ---------HEDTARIDiegmraqdfEYPSgwlgALACQAAGMLGGNDAHgAMFDAVQWAHLHQHRNIGDAEVLLDIAES 151
Cdd:COG3531   74 fgeayndllRDGTFVLD---------SEPA----CRAVLAARELAPEREL-AMLHAIQRAFYVEGRDISDPEVLAELAAE 139
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 501457143 152 LGHPRGAFADHMRSDAVRQRVQADRAEAAALGIRSIPTVIGGNGLRLQTLP 202
Cdd:COG3531  140 LGLDAEAFAAALASEETRQHIQQEFALARQLGVQGFPTLVLEQGGQLYLLP 190
DsbA_HCCA_Iso cd03022
DsbA family, 2-hydroxychromene-2-carboxylate (HCCA) isomerase subfamily; HCCA isomerase is a ...
14-191 4.54e-15

DsbA family, 2-hydroxychromene-2-carboxylate (HCCA) isomerase subfamily; HCCA isomerase is a glutathione (GSH) dependent enzyme involved in the naphthalene catabolic pathway. It converts HCCA, a hemiketal formed spontaneously after ring cleavage of 1,2-dihydroxynapthalene by a dioxygenase, into cis-o-hydroxybenzylidenepyruvate (cHBPA). This is the fourth reaction in a six-step pathway that converts napthalene into salicylate. HCCA isomerase is unique to bacteria that degrade polycyclic aromatic compounds. It is closely related to the eukaryotic protein, GSH transferase kappa (GSTK).


Pssm-ID: 239320 [Multi-domain]  Cd Length: 192  Bit Score: 70.35  E-value: 4.54e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501457143  14 VDFFHDVVCGWCFVLAPRLQQVSAELGIQVRHRSFVLQDSRAQMVEVfGSMERAKAIILRHWTDCAAHEDTARIDIeGMR 93
Cdd:cd03022    1 IDFYFDFSSPYSYLAHERLPALAARHGATVRYRPILLGGVFKATGNV-PPANRPPAKGRYRLRDLERWARRYGIPL-RFP 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501457143  94 AQDFEYPSGWL-GALACQAAGMLGGNDAHgAMFDAVqWAhlhQHRNIGDAEVLLDIAESLGHPRGAFADHMRSDAVRQRV 172
Cdd:cd03022   79 PRFPPNTLRAMrAALAAQAEGDAAEAFAR-AVFRAL-WG---EGLDIADPAVLAAVAAAAGLDADELLAAADDPAVKAAL 153
                        170
                 ....*....|....*....
gi 501457143 173 QADRAEAAALGIRSIPTVI 191
Cdd:cd03022  154 RANTEEAIARGVFGVPTFV 172
DSBA pfam01323
DSBA-like thioredoxin domain; This family contains a diverse set of proteins with a ...
13-211 3.85e-14

DSBA-like thioredoxin domain; This family contains a diverse set of proteins with a thioredoxin-like structure pfam00085. This family also includes 2-hydroxychromene-2-carboxylate (HCCA) isomerase enzymes catalyze one step in prokaryotic polyaromatic hydrocarbon (PAH) catabolic pathways. This family also contains members with functions other than HCCA isomerization, such as Kappa family GSTs, whose similarity to HCCA isomerases was not previously recognized. The sequence Swiss:O07298 has been annotated as a dioxygenase but is almost certainly an HCCA isomerase enzyme. Similarly, the sequence Swiss:Q9ZI67 has been annotated as a dehydrogenase, but is most probably also an HCCA isomerase enzyme. In addition, the Rhizobium leguminosarum Swiss:Q52782 protein has been annotated as a putative glycerol-3-phosphate transfer protein, but is also most likely to be an HCCA isomerase enzyme.


Pssm-ID: 426200 [Multi-domain]  Cd Length: 191  Bit Score: 67.84  E-value: 3.85e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501457143   13 VVDFFHDVVCGWCFVLAPRLQQVSAELG-IQVRHRSFVL-QDSRAQMVEVFGSMERAKAIiLRHWTDCAAHEdtaRIDIE 90
Cdd:pfam01323   1 TVDEFFDFLCPFCYLAKERLEKLAARYGdVKVVYRPFPLaGAKKIGNVGPSNLPVKLKYM-MADLERWAALY---GIPLR 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501457143   91 GMRAQDFEYPSGWLGALACQAAGMLggNDAHGAMFDAVqWAhlhQHRNIGDAEVLLDIAESLGHPRGAFADHMRSDAVRQ 170
Cdd:pfam01323  77 FPANFLGNSTRANRLALAAGAEGLA--EKVVRELFNAL-WG---EGAAITDDSVLREVAEKAGLDAEEFDEFLDSPAVKE 150
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 501457143  171 RVQADRAEAAALGIRSIPTVIGGNGLRLQTLPLPHLRQALA 211
Cdd:pfam01323 151 AVRENTAAAISLGVFGVPTFVVGGKMVFGADRLDTLADALA 191
DsbG COG1651
Protein thiol-disulfide isomerase DsbC [Posttranslational modification, protein turnover, ...
13-191 7.67e-08

Protein thiol-disulfide isomerase DsbC [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441257 [Multi-domain]  Cd Length: 152  Bit Score: 50.00  E-value: 7.67e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501457143  13 VVDFFhDVVCGWCFVLAPRLQQVSAELG---IQVRHRSFVLQDSraqmvevfGSMERAKAIIlrhwtdCAAHEDTARidi 89
Cdd:COG1651    4 VVEFF-DYQCPYCARFHPELPELLKKYVdgkVRVVYRPFPLLHP--------DSLRAARAAL------CAADQGKFW--- 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501457143  90 egmraqdfeypsgwlgalacqaagmlggnDAHGAMFDAvqwahlhqHRNIGDAEvLLDIAESLGHPRGAFADHMRSDAVR 169
Cdd:COG1651   66 -----------------------------AFHDALFAN--------QPALTDDD-LREIAKEAGLDAAKFDACLNSGAVA 107
                        170       180
                 ....*....|....*....|..
gi 501457143 170 QRVQADRAEAAALGIRSIPTVI 191
Cdd:COG1651  108 AKVEADTALAQALGVTGTPTFV 129
DsbA_family cd02972
DsbA family; consists of DsbA and DsbA-like proteins, including DsbC, DsbG, glutathione (GSH) ...
14-50 3.41e-04

DsbA family; consists of DsbA and DsbA-like proteins, including DsbC, DsbG, glutathione (GSH) S-transferase kappa (GSTK), 2-hydroxychromene-2-carboxylate (HCCA) isomerase, an oxidoreductase (FrnE) presumed to be involved in frenolicin biosynthesis, a 27-kDa outer membrane protein, and similar proteins. Members of this family contain a redox active CXXC motif (except GSTK and HCCA isomerase) imbedded in a TRX fold, and an alpha helical insert of about 75 residues (shorter in DsbC and DsbG) relative to TRX. DsbA is involved in the oxidative protein folding pathway in prokaryotes, catalyzing disulfide bond formation of proteins secreted into the bacterial periplasm. DsbC and DsbG function as protein disulfide isomerases and chaperones to correct non-native disulfide bonds formed by DsbA and prevent aggregation of incorrectly folded proteins.


Pssm-ID: 239270 [Multi-domain]  Cd Length: 98  Bit Score: 38.54  E-value: 3.41e-04
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 501457143  14 VDFFHDVVCGWCFVLAPRLQQVSAEL--GIQVRHRSFVL 50
Cdd:cd02972    1 IVEFFDPLCPYCYLFEPELEKLLYADdgGVRVVYRPFPL 39
Thioredoxin_5 pfam13743
Thioredoxin;
17-191 8.81e-04

Thioredoxin;


Pssm-ID: 404608 [Multi-domain]  Cd Length: 176  Bit Score: 38.75  E-value: 8.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501457143   17 FHDVVCGWCFVLAPRLQQVSAELG--IQVRHRSFVLQDSraqmvevfgsmerakaiilrhWTDCAAHedtARIDIEGMRA 94
Cdd:pfam13743   3 FIDPLCPECWAIEPQIKKLKVEYGqkFDIRFIPLGNLQT---------------------LNYNMGR---MPIDGDVLRN 58
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501457143   95 QDFEYPsgWLGALACQAAgMLGGNDAhGAMF-DAVQWAHLHQHRNIGDAEVLLDIAESLGHPRGAFADHMRSDAVRQRVQ 173
Cdd:pfam13743  59 DPFSSP--YLASLAYKAA-ELQGKKK-GRRFlRKLQEAVFLEKQNISDEELLLECAEKAGLDVEEFKEDLHSDLAKKAFQ 134
                         170
                  ....*....|....*...
gi 501457143  174 ADRAEAAALGIRSIPTVI 191
Cdd:pfam13743 135 CDQKLAAEMGVTEHPTLV 152
DsbA_Com1_like cd03023
DsbA family, Com1-like subfamily; composed of proteins similar to Com1, a 27-kDa outer ...
13-211 9.63e-04

DsbA family, Com1-like subfamily; composed of proteins similar to Com1, a 27-kDa outer membrane-associated immunoreactive protein originally found in both acute and chronic disease strains of the pathogenic bacteria Coxiella burnetti. It contains a CXXC motif, assumed to be imbedded in a DsbA-like structure. Its homology to DsbA suggests that the protein is a protein disulfide oxidoreductase. The role of such a protein in pathogenesis is unknown.


Pssm-ID: 239321 [Multi-domain]  Cd Length: 154  Bit Score: 38.34  E-value: 9.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501457143  13 VVDFFhDVVCGWCFVLAPRLQQVSAELGiQVRhrsFVLQDsraqmVEVFGSmERAKAiilrhwtdcaahedtARIdiegm 92
Cdd:cd03023    9 IVEFF-DYNCGYCKKLAPELEKLLKEDP-DVR---VVFKE-----FPILGE-SSVLA---------------ARV----- 57
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501457143  93 raqdfeypsgwlgALACQAAGMLGGNDAHGAMFdavqwahlhQHRNIGDAEVLLDIAESLGHPRGAFADHMRSDAVRQRV 172
Cdd:cd03023   58 -------------ALAVWKNGPGKYLEFHNALM---------ATRGRLNEESLLRIAKKAGLDEAKLKKDMDDPEIEATI 115
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 501457143 173 QADRAEAAALGIRSIPTVIGGNGLRLQTLPLPHLRQALA 211
Cdd:cd03023  116 DKNRQLARALGITGTPAFIIGDTVIPGAVPADTLKEAID 154
 
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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