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Conserved domains on  [gi|446668268|ref|WP_000745614|]
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MULTISPECIES: bifunctional protein-disulfide isomerase/oxidoreductase DsbC [Salmonella]

Protein Classification

bifunctional protein-disulfide isomerase/oxidoreductase DsbC( domain architecture ID 11485053)

bifunctional protein-disulfide isomerase/oxidoreductase DsbC is required for disulfide bond formation in some periplasmic proteins; also acts as a disulfide isomerase

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK10877 PRK10877
protein disulfide isomerase II DsbC; Provisional
 1-232 0e+00

protein disulfide isomerase II DsbC; Provisional


:

Pssm-ID: 182802 [Multi-domain]  Cd Length: 232  Bit Score: 507.32  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446668268   1 MKKRFMMFTLLAAAFSGVAHADDAAIRQSLAKLGVQSTEIQASPVAGMKTVLTHSGVLYVTDDGKHIIQGPMYDVSGAHP 80
Cdd:PRK10877   1 MKKGFLLFTLLAAAFSGFAHADDAAIQQTLAKLGIQSADIQPSPVAGMKTVLTESGVLYITDDGKHIIQGPMYDVSGTAP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446668268  81 VNVTNKLLMSQLNALEKEMIVYKAPDEKHVITVFTDITCGYCHKLHEEMKDYNALGITVRYLAFPRQGLESQAEQDMKSI 160
Cdd:PRK10877  81 VNVTNQLLLKKLNALEKEMIVYKAPQEKHVITVFTDITCGYCHKLHEQMKDYNALGITVRYLAFPRQGLDSQAEKDMKSI 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446668268 161 WCAKDKNKAFDDAMAGKGVKPASCDVNIADHYALGVQLGVSGTPAIVLSNGYVVPGYQGPKEMKAFLDEHQK 232
Cdd:PRK10877 161 WCAADRNKAFDDAMKGKDVSPASCDVDIADHYALGVQFGVQGTPAIVLSNGTLVPGYQGPKEMKAFLDEHQK 232
 
Name Accession Description Interval E-value
PRK10877 PRK10877
protein disulfide isomerase II DsbC; Provisional
 1-232 0e+00

protein disulfide isomerase II DsbC; Provisional


Pssm-ID: 182802 [Multi-domain]  Cd Length: 232  Bit Score: 507.32  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446668268   1 MKKRFMMFTLLAAAFSGVAHADDAAIRQSLAKLGVQSTEIQASPVAGMKTVLTHSGVLYVTDDGKHIIQGPMYDVSGAHP 80
Cdd:PRK10877   1 MKKGFLLFTLLAAAFSGFAHADDAAIQQTLAKLGIQSADIQPSPVAGMKTVLTESGVLYITDDGKHIIQGPMYDVSGTAP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446668268  81 VNVTNKLLMSQLNALEKEMIVYKAPDEKHVITVFTDITCGYCHKLHEEMKDYNALGITVRYLAFPRQGLESQAEQDMKSI 160
Cdd:PRK10877  81 VNVTNQLLLKKLNALEKEMIVYKAPQEKHVITVFTDITCGYCHKLHEQMKDYNALGITVRYLAFPRQGLDSQAEKDMKSI 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446668268 161 WCAKDKNKAFDDAMAGKGVKPASCDVNIADHYALGVQLGVSGTPAIVLSNGYVVPGYQGPKEMKAFLDEHQK 232
Cdd:PRK10877 161 WCAADRNKAFDDAMKGKDVSPASCDVDIADHYALGVQFGVQGTPAIVLSNGTLVPGYQGPKEMKAFLDEHQK 232
DsbA_DsbC_DsbG cd03020
DsbA family, DsbC and DsbG subfamily; V-shaped homodimeric proteins containing a redox active ...
 38-227 2.00e-79

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: 236.83  E-value: 2.00e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446668268  38 TEIQASPVAGMKTVLTHSGVLYVTDDGKHIIQGPMYDVSG---AHPVNVTNKLLMSQLNALE-KEMIVYKAPDEKHVITV 113
Cdd:cd03020    4 DSVFKTPVAGLYEVVTGGGVLYTDDDGRYLIQGNLYDAKGrkdDLTEARLAQLNAIDLSALPlDDAIVYGKGNGKRVVYV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446668268 114 FTDITCGYCHKLHEEMKDyNALGITVRYLAFPRQGLeSQAEQDMKSIWCAKDKNKAFDDAMAGKGVKP--ASCDVNIADH 191
Cdd:cd03020   84 FTDPDCPYCRKLEKELKP-NADGVTVRIFPVPILGL-PDSTAKAAAIWCAKDRAKAWTDAMSGGKVPPpaASCDNPVAAN 161

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 446668268 192 YALGVQLGVSGTPAIVLSNGYVVPGYQGPKEMKAFL 227
Cdd:cd03020  162 LALGRQLGVNGTPTIVLADGRVVPGAPPAAQLEALL 197
Thioredoxin_2 pfam13098
Thioredoxin-like domain;
104-227 5.18e-27

Thioredoxin-like domain;


Pssm-ID: 379034 [Multi-domain]  Cd Length: 103  Bit Score: 99.81  E-value: 5.18e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446668268  104 APDEKHVITVFTDITCGYCHKLHEEMKDYNalGITVRYlafprqglESQAEQDMKSIWCAKDKNKAFDDamagkgvkpas 183
Cdd:pfam13098   1 KGNGKPVLVVFTDPDCPYCKKLKKELLEDP--DVTVYL--------GPNFVFIAVNIWCAKEVAKAFTD----------- 59

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 446668268  184 cdvnIADHYALGVQLGVSGTPAIVLSNG----YVVPGYQGPKEMKAFL 227
Cdd:pfam13098  60 ----ILENKELGRKYGVRGTPTIVFFDGkgelLRLPGYVPAEEFLALL 103
DsbG COG1651
Protein thiol-disulfide isomerase DsbC [Posttranslational modification, protein turnover, ...
 108-229 3.44e-25

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


Pssm-ID: 441257 [Multi-domain]  Cd Length: 152  Bit Score: 96.61  E-value: 3.44e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446668268 108 KHVITVFTDITCGYCHKLHEEMKDYNAL----GITVRYLAFPRqgLESQAEQDMKSIWCAKDKNK--AFDDAM------- 174
Cdd:COG1651    1 KVTVVEFFDYQCPYCARFHPELPELLKKyvdgKVRVVYRPFPL--LHPDSLRAARAALCAADQGKfwAFHDALfanqpal 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446668268 175 ---------AGKGVKPA---SC------DVNIADHYALGVQLGVSGTPAIVLsNGYVVPGYQGPKEMKAFLDE 229
Cdd:COG1651   79 tdddlreiaKEAGLDAAkfdAClnsgavAAKVEADTALAQALGVTGTPTFVV-NGKLVSGAVPYEELEAALDA 150
 
Name Accession Description Interval E-value
PRK10877 PRK10877
protein disulfide isomerase II DsbC; Provisional
 1-232 0e+00

protein disulfide isomerase II DsbC; Provisional


Pssm-ID: 182802 [Multi-domain]  Cd Length: 232  Bit Score: 507.32  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446668268   1 MKKRFMMFTLLAAAFSGVAHADDAAIRQSLAKLGVQSTEIQASPVAGMKTVLTHSGVLYVTDDGKHIIQGPMYDVSGAHP 80
Cdd:PRK10877   1 MKKGFLLFTLLAAAFSGFAHADDAAIQQTLAKLGIQSADIQPSPVAGMKTVLTESGVLYITDDGKHIIQGPMYDVSGTAP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446668268  81 VNVTNKLLMSQLNALEKEMIVYKAPDEKHVITVFTDITCGYCHKLHEEMKDYNALGITVRYLAFPRQGLESQAEQDMKSI 160
Cdd:PRK10877  81 VNVTNQLLLKKLNALEKEMIVYKAPQEKHVITVFTDITCGYCHKLHEQMKDYNALGITVRYLAFPRQGLDSQAEKDMKSI 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446668268 161 WCAKDKNKAFDDAMAGKGVKPASCDVNIADHYALGVQLGVSGTPAIVLSNGYVVPGYQGPKEMKAFLDEHQK 232
Cdd:PRK10877 161 WCAADRNKAFDDAMKGKDVSPASCDVDIADHYALGVQFGVQGTPAIVLSNGTLVPGYQGPKEMKAFLDEHQK 232
DsbA_DsbC_DsbG cd03020
DsbA family, DsbC and DsbG subfamily; V-shaped homodimeric proteins containing a redox active ...
 38-227 2.00e-79

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: 236.83  E-value: 2.00e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446668268  38 TEIQASPVAGMKTVLTHSGVLYVTDDGKHIIQGPMYDVSG---AHPVNVTNKLLMSQLNALE-KEMIVYKAPDEKHVITV 113
Cdd:cd03020    4 DSVFKTPVAGLYEVVTGGGVLYTDDDGRYLIQGNLYDAKGrkdDLTEARLAQLNAIDLSALPlDDAIVYGKGNGKRVVYV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446668268 114 FTDITCGYCHKLHEEMKDyNALGITVRYLAFPRQGLeSQAEQDMKSIWCAKDKNKAFDDAMAGKGVKP--ASCDVNIADH 191
Cdd:cd03020   84 FTDPDCPYCRKLEKELKP-NADGVTVRIFPVPILGL-PDSTAKAAAIWCAKDRAKAWTDAMSGGKVPPpaASCDNPVAAN 161

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 446668268 192 YALGVQLGVSGTPAIVLSNGYVVPGYQGPKEMKAFL 227
Cdd:cd03020  162 LALGRQLGVNGTPTIVLADGRVVPGAPPAAQLEALL 197
Thioredoxin_2 pfam13098
Thioredoxin-like domain;
104-227 5.18e-27

Thioredoxin-like domain;


Pssm-ID: 379034 [Multi-domain]  Cd Length: 103  Bit Score: 99.81  E-value: 5.18e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446668268  104 APDEKHVITVFTDITCGYCHKLHEEMKDYNalGITVRYlafprqglESQAEQDMKSIWCAKDKNKAFDDamagkgvkpas 183
Cdd:pfam13098   1 KGNGKPVLVVFTDPDCPYCKKLKKELLEDP--DVTVYL--------GPNFVFIAVNIWCAKEVAKAFTD----------- 59

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 446668268  184 cdvnIADHYALGVQLGVSGTPAIVLSNG----YVVPGYQGPKEMKAFL 227
Cdd:pfam13098  60 ----ILENKELGRKYGVRGTPTIVFFDGkgelLRLPGYVPAEEFLALL 103
DsbG COG1651
Protein thiol-disulfide isomerase DsbC [Posttranslational modification, protein turnover, ...
 108-229 3.44e-25

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


Pssm-ID: 441257 [Multi-domain]  Cd Length: 152  Bit Score: 96.61  E-value: 3.44e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446668268 108 KHVITVFTDITCGYCHKLHEEMKDYNAL----GITVRYLAFPRqgLESQAEQDMKSIWCAKDKNK--AFDDAM------- 174
Cdd:COG1651    1 KVTVVEFFDYQCPYCARFHPELPELLKKyvdgKVRVVYRPFPL--LHPDSLRAARAALCAADQGKfwAFHDALfanqpal 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446668268 175 ---------AGKGVKPA---SC------DVNIADHYALGVQLGVSGTPAIVLsNGYVVPGYQGPKEMKAFLDE 229
Cdd:COG1651   79 tdddlreiaKEAGLDAAkfdAClnsgavAAKVEADTALAQALGVTGTPTFVV-NGKLVSGAVPYEELEAALDA 150
DsbA_family cd02972
DsbA family; consists of DsbA and DsbA-like proteins, including DsbC, DsbG, glutathione (GSH) ...
 111-218 9.08e-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: 70.51  E-value: 9.08e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446668268 111 ITVFTDITCGYCHKLHEEMKDY---NALGITVRYLAFPRQGLESQAEQD-MKSIWCAKDKNK--AFDDAMAgkgvkpasc 184
Cdd:cd02972    1 IVEFFDPLCPYCYLFEPELEKLlyaDDGGVRVVYRPFPLLGGMPPNSLAaARAALAAAAQGKfeALHEALA--------- 71

                         90       100       110
                 ....*....|....*....|....*....|....
gi 446668268 185 dvniadHYALGVQLGVSGTPAIVLsNGYVVPGYQ 218
Cdd:cd02972   72 ------DTALARALGVTGTPTFVV-NGEKYSGAG 98
dsbG PRK11657
disulfide isomerase/thiol-disulfide oxidase; Provisional
 2-207 6.71e-15

disulfide isomerase/thiol-disulfide oxidase; Provisional


Pssm-ID: 183262 [Multi-domain]  Cd Length: 251  Bit Score: 71.54  E-value: 6.71e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446668268   2 KKRFMMFTLLAAAFSGVAHADD--AAIrQSLAKLGVQSTEIQASPvAGMKTVLTHSG----VLYVTDDGKHIIQGPMYDV 75
Cdd:PRK11657   1 MKRMLKLILLLALLPLSAAAEElpAPV-KALEKQGITIIKTFDAP-GGLKGYAAKYQdmgvTIYLTPDGKHAISGYMYDE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446668268  76 SGAhpvNVTNKLLMSQLNA-LEKEM---------IVYKAPDEKHVITVFTDITCGYCHKLHEEMKDYNALG-ITVRYL-- 142
Cdd:PRK11657  79 KGE---NLSEALLEKEVYApMGREMwqrleqshwILDGKADAPRIVYVFADPNCPYCKQFWQQARPWVDSGkVQLRHIlv 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446668268 143 AFPRQGLESQAEqdmkSIWCAKDKNKAFDD-AMAGK--GVKPA---SCDVN--IADHYALGVQLGVSGTPAIV 207
Cdd:PRK11657 156 GIIKPDSPGKAA----AILAAKDPAKALQEyEASGGklGLKPPasiPAAVRkqLADNQKLMDDLGANATPAIY 224
DsbC_N pfam10411
Disulfide bond isomerase protein N-terminus; This is the N-terminal domain of the disulfide ...
 27-77 3.66e-13

Disulfide bond isomerase protein N-terminus; This is the N-terminal domain of the disulfide bond isomerase DsbC. The whole molecule is V-shaped, where each arm is a DsbC monomer of two domains linked by a hinge; and the N-termini of each monomer join to form the dimer interface at the base of the V, so are vital for dimerization. DsbC is required for disulfide bond formation and functions as a disulfide bond isomerase during oxidative protein-folding in bacterial periplasm. It also has chaperone activity.


Pssm-ID: 431267 [Multi-domain]  Cd Length: 54  Bit Score: 62.10  E-value: 3.66e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 446668268   27 RQSLAKL--GVQSTEIQASPVAGMKTVLTHSGVLYVTDDGKHIIQGPMYDVSG 77
Cdd:pfam10411   1 KAALEKRfpNLKVDSVSPSPVPGLYEVVTGGQVLYTDEDGRYLIQGRLYDLKT 53
Thioredoxin_4 pfam13462
Thioredoxin;
100-229 3.58e-08

Thioredoxin;


Pssm-ID: 433227 [Multi-domain]  Cd Length: 164  Bit Score: 51.19  E-value: 3.58e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446668268  100 IVYKAPDEKHVITVFTDITCGYCHKLHEEM----KDYNALGItVRY----LAFPRQGLESQA--------EQDMKSIWCA 163
Cdd:pfam13462   5 PVIGNPDAPVTVVEYADLRCPHCAKFHEEVlkllEEYIDTGK-VRFiirdFPLDGEGESLLAamaarcagDQSPEYFLVI 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446668268  164 K----------------DKNKAFDDAMAGKGVKPASCDVNIADHYALGVQLGVSGTPAIVLsNGYVVPGYQGPKEMKAFL 227
Cdd:pfam13462  84 DkllysqqeewaqdlelAALAGLKDEEFEACLEEEDFLALVMADVKEARAAGINFTPTFII-NGKKVDGPLTYEELKKLI 162


                  ..
gi 446668268  228 DE 229
Cdd:pfam13462 163 DD 164
DsbA_Com1_like cd03023
DsbA family, Com1-like subfamily; composed of proteins similar to Com1, a 27-kDa outer ...
 104-225 5.44e-08

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: 50.67  E-value: 5.44e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446668268 104 APDEKHVITVFTDITCGYCHKLHEEM--------------KDYNALG----------ITVR------YLAFPRQGLESQA 153
Cdd:cd03023    2 NPNGDVTIVEFFDYNCGYCKKLAPELekllkedpdvrvvfKEFPILGessvlaarvaLAVWkngpgkYLEFHNALMATRG 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446668268 154 EQDMKSIWCAKDKN----KAFDDAMAGKGVKPAscdvnIADHYALGVQLGVSGTPAIVLsNGYVVPGYQGPKEMKA 225
Cdd:cd03023   82 RLNEESLLRIAKKAgldeAKLKKDMDDPEIEAT-----IDKNRQLARALGITGTPAFII-GDTVIPGAVPADTLKE 151
DUF4093 pfam13331
Domain of unknown function (DUF4093); This domain lies at the C-terminus of primase proteins ...
 17-45 2.59e-03

Domain of unknown function (DUF4093); This domain lies at the C-terminus of primase proteins carrying the TOPRIM, pfam01751, domain. The exact function of the domain is not known.


Pssm-ID: 433122  Cd Length: 85  Bit Score: 35.91  E-value: 2.59e-03
                          10        20
                  ....*....|....*....|....*....
gi 446668268   17 GVAHADDAAIRQSLAKLGVQSTEIQASPV 45
Cdd:pfam13331   2 GVEHASPEAIREALAKAGTETEEKNNESI 30
FrnE COG2761
Predicted dithiol-disulfide isomerase, DsbA/YjbH family (virulence, stress resistance) ...
 192-229 4.38e-03

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: 37.17  E-value: 4.38e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 446668268 192 YALGVQLGVSGTPAIVLSNGYVVPGYQGPKEMKAFLDE 229
Cdd:COG2761  165 EAEARELGVTGVPTFVFDGKYAVSGAQPYEVFEQALRQ 202
 
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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