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Conserved domains on  [gi|517340548|ref|WP_018516040|]
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MULTISPECIES: thioredoxin domain-containing protein [Streptomyces]

Protein Classification

DsbA family protein( domain architecture ID 11447254)

DsbA family protein belongs to the thioredoxin superfamily of proteins containing a redox active CXXC motif, similar to DsbA that is involved in the oxidative protein folding pathway in prokaryotes, catalyzing disulfide bond formation of proteins secreted into the bacterial periplasm

CATH:  3.40.30.10
Gene Ontology:  GO:0015036
PubMed:  11967064|9099998|10049365|15558583|12524212
SCOP:  3000031

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DsbG COG1651
Protein thiol-disulfide isomerase DsbC [Posttranslational modification, protein turnover, ...
 62-217 1.14e-47

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


:

Pssm-ID: 441257 [Multi-domain]  Cd Length: 152  Bit Score: 154.00  E-value: 1.14e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517340548  62 TVVEFLDFECEACGAVYPAVEKLREEYGD-RVTFIARYFPMPgHKNAQLAARTVEAAAQQGKFEEMYGKLFTTQAQWGEA 140
Cdd:COG1651    3 TVVEFFDYQCPYCARFHPELPELLKKYVDgKVRVVYRPFPLL-HPDSLRAARAALCAADQGKFWAFHDALFANQPALTDD 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517340548 141 DeskealFRTYAGELGLDMAKFTAVLNDPATTERIEADQRDGLGLGVQGTPTFFVDGLRIPNPGSYEEFRALIEKRL 217
Cdd:COG1651   82 D------LREIAKEAGLDAAKFDACLNSGAVAAKVEADTALAQALGVTGTPTFVVNGKLVSGAVPYEELEAALDAAL 152
 
Name Accession Description Interval E-value
DsbG COG1651
Protein thiol-disulfide isomerase DsbC [Posttranslational modification, protein turnover, ...
 62-217 1.14e-47

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


Pssm-ID: 441257 [Multi-domain]  Cd Length: 152  Bit Score: 154.00  E-value: 1.14e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517340548  62 TVVEFLDFECEACGAVYPAVEKLREEYGD-RVTFIARYFPMPgHKNAQLAARTVEAAAQQGKFEEMYGKLFTTQAQWGEA 140
Cdd:COG1651    3 TVVEFFDYQCPYCARFHPELPELLKKYVDgKVRVVYRPFPLL-HPDSLRAARAALCAADQGKFWAFHDALFANQPALTDD 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517340548 141 DeskealFRTYAGELGLDMAKFTAVLNDPATTERIEADQRDGLGLGVQGTPTFFVDGLRIPNPGSYEEFRALIEKRL 217
Cdd:COG1651   82 D------LREIAKEAGLDAAKFDACLNSGAVAAKVEADTALAQALGVTGTPTFVVNGKLVSGAVPYEELEAALDAAL 152
Thioredoxin_4 pfam13462
Thioredoxin;
62-215 1.92e-30

Thioredoxin;


Pssm-ID: 433227 [Multi-domain]  Cd Length: 164  Bit Score: 110.12  E-value: 1.92e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517340548   62 TVVEFLDFECEACGAVYPAVEKLREEYGD--RVTFIARYFPMPGHKNAQLAARTVEAAAQQG-KFEEMYGKLFTTQAQWG 138
Cdd:pfam13462  15 TVVEYADLRCPHCAKFHEEVLKLLEEYIDtgKVRFIIRDFPLDGEGESLLAAMAARCAGDQSpEYFLVIDKLLYSQQEEW 94

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517340548  139 EADESkealfrtYAGELGLDMAKFTAVLNDPATTERIEADQRDGLGLGVQGTPTFFVDGLRIPNPGSYEEFRALIEK 215
Cdd:pfam13462  95 AQDLE-------LAALAGLKDEEFEACLEEEDFLALVMADVKEARAAGINFTPTFIINGKKVDGPLTYEELKKLIDD 164
DsbA_Com1_like cd03023
DsbA family, Com1-like subfamily; composed of proteins similar to Com1, a 27-kDa outer ...
 56-214 1.03e-25

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: 97.66  E-value: 1.03e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517340548  56 PERSELTVVEFLDFECEACGAVYPAVEKLREEYGDrVTFIARYFPMPGHKNAqLAARTVEAAAQ--QGKFEEMYGKLFTT 133
Cdd:cd03023    2 NPNGDVTIVEFFDYNCGYCKKLAPELEKLLKEDPD-VRVVFKEFPILGESSV-LAARVALAVWKngPGKYLEFHNALMAT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517340548 134 QaqwGEADEskEALFRTyAGELGLDMAKFTAVLNDPATTERIEADQRDGLGLGVQGTPTFFVDGLRIPNPGSYEEFRALI 213
Cdd:cd03023   80 R---GRLNE--ESLLRI-AKKAGLDEAKLKKDMDDPEIEATIDKNRQLARALGITGTPAFIIGDTVIPGAVPADTLKEAI 153


                 .
gi 517340548 214 E 214
Cdd:cd03023  154 D 154
 
Name Accession Description Interval E-value
DsbG COG1651
Protein thiol-disulfide isomerase DsbC [Posttranslational modification, protein turnover, ...
 62-217 1.14e-47

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


Pssm-ID: 441257 [Multi-domain]  Cd Length: 152  Bit Score: 154.00  E-value: 1.14e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517340548  62 TVVEFLDFECEACGAVYPAVEKLREEYGD-RVTFIARYFPMPgHKNAQLAARTVEAAAQQGKFEEMYGKLFTTQAQWGEA 140
Cdd:COG1651    3 TVVEFFDYQCPYCARFHPELPELLKKYVDgKVRVVYRPFPLL-HPDSLRAARAALCAADQGKFWAFHDALFANQPALTDD 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517340548 141 DeskealFRTYAGELGLDMAKFTAVLNDPATTERIEADQRDGLGLGVQGTPTFFVDGLRIPNPGSYEEFRALIEKRL 217
Cdd:COG1651   82 D------LREIAKEAGLDAAKFDACLNSGAVAAKVEADTALAQALGVTGTPTFVVNGKLVSGAVPYEELEAALDAAL 152
Thioredoxin_4 pfam13462
Thioredoxin;
62-215 1.92e-30

Thioredoxin;


Pssm-ID: 433227 [Multi-domain]  Cd Length: 164  Bit Score: 110.12  E-value: 1.92e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517340548   62 TVVEFLDFECEACGAVYPAVEKLREEYGD--RVTFIARYFPMPGHKNAQLAARTVEAAAQQG-KFEEMYGKLFTTQAQWG 138
Cdd:pfam13462  15 TVVEYADLRCPHCAKFHEEVLKLLEEYIDtgKVRFIIRDFPLDGEGESLLAAMAARCAGDQSpEYFLVIDKLLYSQQEEW 94

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 517340548  139 EADESkealfrtYAGELGLDMAKFTAVLNDPATTERIEADQRDGLGLGVQGTPTFFVDGLRIPNPGSYEEFRALIEK 215
Cdd:pfam13462  95 AQDLE-------LAALAGLKDEEFEACLEEEDFLALVMADVKEARAAGINFTPTFIINGKKVDGPLTYEELKKLIDD 164
DsbA_Com1_like cd03023
DsbA family, Com1-like subfamily; composed of proteins similar to Com1, a 27-kDa outer ...
 56-214 1.03e-25

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: 97.66  E-value: 1.03e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517340548  56 PERSELTVVEFLDFECEACGAVYPAVEKLREEYGDrVTFIARYFPMPGHKNAqLAARTVEAAAQ--QGKFEEMYGKLFTT 133
Cdd:cd03023    2 NPNGDVTIVEFFDYNCGYCKKLAPELEKLLKEDPD-VRVVFKEFPILGESSV-LAARVALAVWKngPGKYLEFHNALMAT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517340548 134 QaqwGEADEskEALFRTyAGELGLDMAKFTAVLNDPATTERIEADQRDGLGLGVQGTPTFFVDGLRIPNPGSYEEFRALI 213
Cdd:cd03023   80 R---GRLNE--ESLLRI-AKKAGLDEAKLKKDMDDPEIEATIDKNRQLARALGITGTPAFIIGDTVIPGAVPADTLKEAI 153


                 .
gi 517340548 214 E 214
Cdd:cd03023  154 D 154
FrnE COG2761
Predicted dithiol-disulfide isomerase, DsbA/YjbH family (virulence, stress resistance) ...
 76-218 1.55e-16

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: 74.92  E-value: 1.55e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517340548  76 AVYPAVEKLREEYGdrVTFiarYFPMPGHKNAQLAARTVEAAAQQGKFEEMYGKLFttQAQWGEA-DESKEALFRTYAGE 154
Cdd:COG2761   68 QMRAHVEEAAAEEG--LPF---DFDRIKPPNTFDAHRLLKAAELQGKQDALLEALF--EAYFTEGrDIGDREVLLDLAAE 140

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517340548 155 LGLDMAKFTAVLNDPATTERIEADQRDGLGLGVQGTPTFFVDGlRIPNPG--SYEEFRALIEKRLA 218
Cdd:COG2761  141 VGLDAEEFRADLESDEAAAAVRADEAEARELGVTGVPTFVFDG-KYAVSGaqPYEVFEQALRQALA 205
DsbA_family cd02972
DsbA family; consists of DsbA and DsbA-like proteins, including DsbC, DsbG, glutathione (GSH) ...
 63-204 8.95e-16

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: 70.13  E-value: 8.95e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517340548  63 VVEFLDFECEACGAVYPAVEKLREEYGDRVTFIARYFPMPGH--KNAQLAARTVEAAAQQGKFEEMYGKLfttqaqwgea 140
Cdd:cd02972    1 IVEFFDPLCPYCYLFEPELEKLLYADDGGVRVVYRPFPLLGGmpPNSLAAARAALAAAAQGKFEALHEAL---------- 70

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517340548 141 deskealfrtyagelgldmakftavlndpatterieADQRDGLGLGVQGTPTFFVDGLRIPNPG 204
Cdd:cd02972   71 ------------------------------------ADTALARALGVTGTPTFVVNGEKYSGAG 98
DSBA pfam01323
DSBA-like thioredoxin domain; This family contains a diverse set of proteins with a ...
 62-214 2.82e-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: 68.22  E-value: 2.82e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517340548   62 TVVEFLDFECEACGAVYPAVEKLREEYGDrVTFIARYFPMPGHK------------------------------------ 105
Cdd:pfam01323   1 TVDEFFDFLCPFCYLAKERLEKLAARYGD-VKVVYRPFPLAGAKkignvgpsnlpvklkymmadlerwaalygiplrfpa 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517340548  106 ----NAQLAARTVEAAAQQGKFEEMYGKLFttQAQWGE-ADESKEALFRTYAGELGLDMAKFTAVLNDPATTERIEADQR 180
Cdd:pfam01323  80 nflgNSTRANRLALAAGAEGLAEKVVRELF--NALWGEgAAITDDSVLREVAEKAGLDAEEFDEFLDSPAVKEAVRENTA 157

                         170       180       190
                  ....*....|....*....|....*....|....
gi 517340548  181 DGLGLGVQGTPTFFVDGLRIPNPGSYEEFRALIE 214
Cdd:pfam01323 158 AAISLGVFGVPTFVVGGKMVFGADRLDTLADALA 191
DsbA_DsbA cd03019
DsbA family, DsbA subfamily; DsbA is a monomeric thiol disulfide oxidoreductase protein ...
 63-197 1.30e-10

DsbA family, DsbA subfamily; DsbA is a monomeric thiol disulfide oxidoreductase protein containing a redox active CXXC motif imbedded in a TRX fold. It is involved in the oxidative protein folding pathway in prokaryotes, and is the strongest thiol oxidant known, due to the unusual stability of the thiolate anion form of the first cysteine in the CXXC motif. The highly unstable oxidized form of DsbA directly donates disulfide bonds to reduced proteins secreted into the bacterial periplasm. This rapid and unidirectional process helps to catalyze the folding of newly-synthesized polypeptides. To regain catalytic activity, reduced DsbA is then reoxidized by the membrane protein DsbB, which generates its disulfides from oxidized quinones, which in turn are reoxidized by the electron transport chain.


Pssm-ID: 239317 [Multi-domain]  Cd Length: 178  Bit Score: 58.07  E-value: 1.30e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517340548  63 VVEFLDFECEACGAVYPAVEKLREEYGDRVTFIaRYFPMPGHKNAQLAARTVEAAAQQGKFEEMYGKLFTtQAQWGEADE 142
Cdd:cd03019   19 VIEFFSYGCPHCYNFEPILEAWVKKLPKDVKFE-KVPVVFGGGEGEPLARAFYAAEALGLEDKLHAALFE-AIHEKRKRL 96

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 517340548 143 SKEALFRTYAGELGLDMAKFTAVLNDPATTERIEADQRDGLGLGVQGTPTFFVDG 197
Cdd:cd03019   97 LDPDDIRKIFLSQGVDKKKFDAAYNSFSVKALVAKAEKLAKKYKITGVPAFVVNG 151
DsbA_HCCA_Iso cd03022
DsbA family, 2-hydroxychromene-2-carboxylate (HCCA) isomerase subfamily; HCCA isomerase is a ...
 82-197 4.16e-10

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: 56.87  E-value: 4.16e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517340548  82 EKLREEYGDRVTFIARYFPmpghkNAQLAARTVEAAAQQGKFEEMYGK-LFttQAQWGE-ADESKEALFRTYAGELGLDM 159
Cdd:cd03022   65 ERWARRYGIPLRFPPRFPP-----NTLRAMRAALAAQAEGDAAEAFARaVF--RALWGEgLDIADPAVLAAVAAAAGLDA 137

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 517340548 160 AKFTAVLNDPATTERIEADQRDGLGLGVQGTPTFFVDG 197
Cdd:cd03022  138 DELLAAADDPAVKAALRANTEEAIARGVFGVPTFVVDG 175
NahD COG3917
2-hydroxychromene-2-carboxylate isomerase [Secondary metabolites biosynthesis, transport and ...
 97-197 4.28e-10

2-hydroxychromene-2-carboxylate isomerase [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 443122 [Multi-domain]  Cd Length: 196  Bit Score: 57.10  E-value: 4.28e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517340548  97 RYFPMpghkNAQLAARTVEAAAQQGKFEEMYGKLFttQAQWGE-ADESKEALFRTYAGELGLDMAKFTAVLNDPATTERI 175
Cdd:COG3917   80 PHFPV----NPLLAARAALAAQDAGAAAAFVRAVF--RAVWAEgRDIADPAVLAAIAAAAGLDAAALLAAAQSPAVKARL 153

                         90       100
                 ....*....|....*....|..
gi 517340548 176 EADQRDGLGLGVQGTPTFFVDG 197
Cdd:COG3917  154 RANTEEAVARGVFGAPTFVVDG 175
DsbA_FrnE cd03024
DsbA family, FrnE subfamily; FrnE is a DsbA-like protein containing a CXXC motif. It is ...
 84-197 1.68e-08

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: 52.58  E-value: 1.68e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517340548  84 LREEYGDRVTFIARYFPMPGhKNAQLAARTVEAAAQQG---KFEEMYG-------KLFTTQAQWGEADESKEALFRTY-- 151
Cdd:cd03024   45 MPPEGEDRREYLARKYGSTA-EQAAAMRRVEAAAAAEGlefDFDRVRPpntfdahRLIHLAKEQGKQDALVEALFRAYft 123

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 517340548 152 --------------AGELGLDMAKFTAVLNDPATTERIEADQRDGLGLGVQGTPTFFVDG 197
Cdd:cd03024  124 egkdigdrdvlvdlAEEAGLDAAEARAVLASDEYADEVRADEARARQLGISGVPFFVFNG 183
DsbA_FrnE_like cd03025
DsbA family, FrnE-like subfamily; composed of uncharacterized proteins containing a CXXC motif ...
 71-195 4.17e-07

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: 48.47  E-value: 4.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517340548  71 CEACGAVYPAVEKLREEYGDRVTFIARYFPM-PGHKNAQLAARTVEAAAQQGKFEEMYGKLFTT---------------- 133
Cdd:cd03025   11 CGWCYGFEPLLEKLKEEYGGGIEVELHLGGLlPGNNARQITKQWRIYVHWHKARIALTGQPFGEdylelllfdldsapas 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517340548 134 ------QAQWGEA-----------------DESKEALFRTYAGELGLDMAKFTAVLNDPATTERIEADQRDGLGLGVQGT 190
Cdd:cd03025   91 raikaaRLQGPERllemlkaiqrahyvegrDLADTEVLRELAIELGLDVEEFLEDFQSDEAKQAIQEDQKLARELGINGF 170


                 ....*
gi 517340548 191 PTFFV 195
Cdd:cd03025  171 PTLVL 175
COG3531 COG3531
Predicted protein-disulfide isomerase, contains CxxC motif [Posttranslational modification, ...
 152-216 1.24e-05

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


Pssm-ID: 442753 [Multi-domain]  Cd Length: 206  Bit Score: 44.47  E-value: 1.24e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517340548 152 AGELGLDMAKFTAVLNDPATTERIEADQRDGLGLGVQGTPTFFV--DGLRIPNPGSY---EEFRALIEKR 216
Cdd:COG3531  137 AAELGLDAEAFAAALASEETRQHIQQEFALARQLGVQGFPTLVLeqGGQLYLLPRGYgdpEALLAALEQL 206
TxlA cd02950
TRX-like protein A (TxlA) family; TxlA was originally isolated from the cyanobacterium ...
 62-95 9.36e-05

TRX-like protein A (TxlA) family; TxlA was originally isolated from the cyanobacterium Synechococcus. It is found only in oxygenic photosynthetic organisms. TRX is a small enzyme that participate in redox reactions, via the reversible oxidation of an active site dithiol present in a CXXC motif. Disruption of the txlA gene suggests that the protein is involved in the redox regulation of the structure and function of photosynthetic apparatus. The plant homolog (designated as HCF164) is localized in the chloroplast and is involved in the assembly of the cytochrome b6f complex, which takes a central position in photosynthetic electron transport.


Pssm-ID: 239248 [Multi-domain]  Cd Length: 142  Bit Score: 41.17  E-value: 9.36e-05
                         10        20        30
                 ....*....|....*....|....*....|....
gi 517340548  62 TVVEFLDFECEACGAVYPAVEKLREEYGDRVTFI 95
Cdd:cd02950   23 TLVEFYADWCTVCQEMAPDVAKLKQKYGDQVNFV 56
DsbA_DsbC_DsbG cd03020
DsbA family, DsbC and DsbG subfamily; V-shaped homodimeric proteins containing a redox active ...
 62-201 4.61e-04

DsbA family, DsbC and DsbG subfamily; V-shaped homodimeric proteins containing a redox active CXXC motif imbedded in a TRX fold. They function as protein disulfide isomerases and chaperones in the bacterial periplasm to correct non-native disulfide bonds formed by DsbA and prevent aggregation of incorrectly folded proteins. DsbC and DsbG are kept in their reduced state by the cytoplasmic membrane protein DsbD, which utilizes the TRX/TRX reductase system in the cytosol as a source of reducing equivalents. DsbG differ from DsbC in that it has a more limited substrate specificity, and it may preferentially act later in the folding process to catalyze disulfide rearrangements in folded or partially folded proteins. Also included in the alignment is the predicted protein TrbB, whose gene was sequenced from the enterohemorrhagic E. coli type IV pilus gene cluster, which is required for efficient plasmid transfer.


Pssm-ID: 239318 [Multi-domain]  Cd Length: 197  Bit Score: 39.61  E-value: 4.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517340548  62 TVVEFLDFECEACGAVYPAVEKLReeygDRVTFiaRYFPMP--GHKNAQLAARTVeaaaqqgkfeemygklfttqaqWGE 139
Cdd:cd03020   80 VVYVFTDPDCPYCRKLEKELKPNA----DGVTV--RIFPVPilGLPDSTAKAAAI----------------------WCA 131

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 517340548 140 ADESKeALFRTYAGELgldmakftaVLNDPATTERIEADQRD-GLGLGVQGTPT-FFVDGLRIP 201
Cdd:cd03020  132 KDRAK-AWTDAMSGGK---------VPPPAASCDNPVAANLAlGRQLGVNGTPTiVLADGRVVP 185
Thioredoxin_5 pfam13743
Thioredoxin;
66-209 6.27e-03

Thioredoxin;


Pssm-ID: 404608 [Multi-domain]  Cd Length: 176  Bit Score: 36.06  E-value: 6.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517340548   66 FLDFECEACGAVYPAVEKLREEYGDRVTF-------------IARYFPMPG--HKNAQ-----LAARTVEAAAQQGKFEe 125
Cdd:pfam13743   3 FIDPLCPECWAIEPQIKKLKVEYGQKFDIrfiplgnlqtlnyNMGRMPIDGdvLRNDPfsspyLASLAYKAAELQGKKK- 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517340548  126 myGKLFTTQAQwgEA------DESKEALFRTYAGELGLDMAKFTAVLNDPATTERIEADQRDGLGLGVQGTPTFFV---- 195
Cdd:pfam13743  82 --GRRFLRKLQ--EAvflekqNISDEELLLECAEKAGLDVEEFKEDLHSDLAKKAFQCDQKLAAEMGVTEHPTLVFfnsn 157

                         170
                  ....*....|....*..
gi 517340548  196 ---DGLRIPNPGSYEEF 209
Cdd:pfam13743 158 veeEGLKVEGCYPYDVY 174
 
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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