|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10877 |
PRK10877 |
protein disulfide isomerase II DsbC; Provisional |
1-232 |
4.43e-173 |
|
protein disulfide isomerase II DsbC; Provisional
Pssm-ID: 182802 [Multi-domain] Cd Length: 232 Bit Score: 475.35 E-value: 4.43e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138724 1 MKKSLLLLPMLMAALSGVANADDSAIQQTLKKLDIQQADIQPSPIPGISTVMTESGVLYISADGKHLLQGPLYDVSGDQP 80
Cdd:PRK10877 1 MKKGFLLFTLLAAAFSGFAHADDAAIQQTLAKLGIQSADIQPSPVAGMKTVLTESGVLYITDDGKHIIQGPMYDVSGTAP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138724 81 INVTNQALLKKLEALSSEMIVYKAPEEKHVITVFTDITCGYCRKLHEQMKDYNALGITVRYLAFPRQGLSSQAEKDMRSI 160
Cdd:PRK10877 81 VNVTNQLLLKKLNALEKEMIVYKAPQEKHVITVFTDITCGYCHKLHEQMKDYNALGITVRYLAFPRQGLDSQAEKDMKSI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488138724 161 WCMADRNKAFDDAMKNNDISPATCKTDISKHYQLGVQFGIQGTPAIVLQNGTIVPGYQGPKEMLQMLNAHQA 232
Cdd:PRK10877 161 WCAADRNKAFDDAMKGKDVSPASCDVDIADHYALGVQFGVQGTPAIVLSNGTLVPGYQGPKEMKAFLDEHQK 232
|
|
| DsbA_DsbC_DsbG |
cd03020 |
DsbA family, DsbC and DsbG subfamily; V-shaped homodimeric proteins containing a redox active ... |
39-227 |
6.34e-78 |
|
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: 232.98 E-value: 6.34e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138724 39 DIQPSPIPGISTVMTESGVLYISADGKHLLQGPLYDVSG---DQPINVTNQALLKKLEAL-SSEMIVYKAPEEKHVITVF 114
Cdd:cd03020 5 SVFKTPVAGLYEVVTGGGVLYTDDDGRYLIQGNLYDAKGrkdDLTEARLAQLNAIDLSALpLDDAIVYGKGNGKRVVYVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138724 115 TDITCGYCRKLHEQMKDyNALGITVRYLAFPRQGLSsQAEKDMRSIWCMADRNKAFDDAMKNNDISP--ATCKTDISKHY 192
Cdd:cd03020 85 TDPDCPYCRKLEKELKP-NADGVTVRIFPVPILGLP-DSTAKAAAIWCAKDRAKAWTDAMSGGKVPPpaASCDNPVAANL 162
|
170 180 190
....*....|....*....|....*....|....*
gi 488138724 193 QLGVQFGIQGTPAIVLQNGTIVPGYQGPKEMLQML 227
Cdd:cd03020 163 ALGRQLGVNGTPTIVLADGRVVPGAPPAAQLEALL 197
|
|
| DsbG |
COG1651 |
Protein thiol-disulfide isomerase DsbC [Posttranslational modification, protein turnover, ... |
108-229 |
2.11e-27 |
|
Protein thiol-disulfide isomerase DsbC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 441257 [Multi-domain] Cd Length: 152 Bit Score: 102.38 E-value: 2.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138724 108 KHVITVFTDITCGYCRKLHEQMKDYNAL----GITVRYLAFPRqgLSSQAEKDMRSIWCMADRNK--AFDDAM------- 174
Cdd:COG1651 1 KVTVVEFFDYQCPYCARFHPELPELLKKyvdgKVRVVYRPFPL--LHPDSLRAARAALCAADQGKfwAFHDALfanqpal 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488138724 175 ---------KNNDISPATCKTD---------ISKHYQLGVQFGIQGTPAIVLqNGTIVPGYQGPKEMLQMLNA 229
Cdd:COG1651 79 tdddlreiaKEAGLDAAKFDAClnsgavaakVEADTALAQALGVTGTPTFVV-NGKLVSGAVPYEELEAALDA 150
|
|
| Thioredoxin_2 |
pfam13098 |
Thioredoxin-like domain; |
104-227 |
5.31e-27 |
|
Thioredoxin-like domain;
Pssm-ID: 379034 [Multi-domain] Cd Length: 103 Bit Score: 99.81 E-value: 5.31e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138724 104 APEEKHVITVFTDITCGYCRKLHEQMKDYNalGITVRYlafprqglSSQAEKDMRSIWCMADRNKAFddamknndispat 183
Cdd:pfam13098 1 KGNGKPVLVVFTDPDCPYCKKLKKELLEDP--DVTVYL--------GPNFVFIAVNIWCAKEVAKAF------------- 57
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 488138724 184 ckTDISKHYQLGVQFGIQGTPAIVLQNGT----IVPGYQGPKEMLQML 227
Cdd:pfam13098 58 --TDILENKELGRKYGVRGTPTIVFFDGKgellRLPGYVPAEEFLALL 103
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10877 |
PRK10877 |
protein disulfide isomerase II DsbC; Provisional |
1-232 |
4.43e-173 |
|
protein disulfide isomerase II DsbC; Provisional
Pssm-ID: 182802 [Multi-domain] Cd Length: 232 Bit Score: 475.35 E-value: 4.43e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138724 1 MKKSLLLLPMLMAALSGVANADDSAIQQTLKKLDIQQADIQPSPIPGISTVMTESGVLYISADGKHLLQGPLYDVSGDQP 80
Cdd:PRK10877 1 MKKGFLLFTLLAAAFSGFAHADDAAIQQTLAKLGIQSADIQPSPVAGMKTVLTESGVLYITDDGKHIIQGPMYDVSGTAP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138724 81 INVTNQALLKKLEALSSEMIVYKAPEEKHVITVFTDITCGYCRKLHEQMKDYNALGITVRYLAFPRQGLSSQAEKDMRSI 160
Cdd:PRK10877 81 VNVTNQLLLKKLNALEKEMIVYKAPQEKHVITVFTDITCGYCHKLHEQMKDYNALGITVRYLAFPRQGLDSQAEKDMKSI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488138724 161 WCMADRNKAFDDAMKNNDISPATCKTDISKHYQLGVQFGIQGTPAIVLQNGTIVPGYQGPKEMLQMLNAHQA 232
Cdd:PRK10877 161 WCAADRNKAFDDAMKGKDVSPASCDVDIADHYALGVQFGVQGTPAIVLSNGTLVPGYQGPKEMKAFLDEHQK 232
|
|
| DsbA_DsbC_DsbG |
cd03020 |
DsbA family, DsbC and DsbG subfamily; V-shaped homodimeric proteins containing a redox active ... |
39-227 |
6.34e-78 |
|
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: 232.98 E-value: 6.34e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138724 39 DIQPSPIPGISTVMTESGVLYISADGKHLLQGPLYDVSG---DQPINVTNQALLKKLEAL-SSEMIVYKAPEEKHVITVF 114
Cdd:cd03020 5 SVFKTPVAGLYEVVTGGGVLYTDDDGRYLIQGNLYDAKGrkdDLTEARLAQLNAIDLSALpLDDAIVYGKGNGKRVVYVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138724 115 TDITCGYCRKLHEQMKDyNALGITVRYLAFPRQGLSsQAEKDMRSIWCMADRNKAFDDAMKNNDISP--ATCKTDISKHY 192
Cdd:cd03020 85 TDPDCPYCRKLEKELKP-NADGVTVRIFPVPILGLP-DSTAKAAAIWCAKDRAKAWTDAMSGGKVPPpaASCDNPVAANL 162
|
170 180 190
....*....|....*....|....*....|....*
gi 488138724 193 QLGVQFGIQGTPAIVLQNGTIVPGYQGPKEMLQML 227
Cdd:cd03020 163 ALGRQLGVNGTPTIVLADGRVVPGAPPAAQLEALL 197
|
|
| DsbG |
COG1651 |
Protein thiol-disulfide isomerase DsbC [Posttranslational modification, protein turnover, ... |
108-229 |
2.11e-27 |
|
Protein thiol-disulfide isomerase DsbC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 441257 [Multi-domain] Cd Length: 152 Bit Score: 102.38 E-value: 2.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138724 108 KHVITVFTDITCGYCRKLHEQMKDYNAL----GITVRYLAFPRqgLSSQAEKDMRSIWCMADRNK--AFDDAM------- 174
Cdd:COG1651 1 KVTVVEFFDYQCPYCARFHPELPELLKKyvdgKVRVVYRPFPL--LHPDSLRAARAALCAADQGKfwAFHDALfanqpal 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488138724 175 ---------KNNDISPATCKTD---------ISKHYQLGVQFGIQGTPAIVLqNGTIVPGYQGPKEMLQMLNA 229
Cdd:COG1651 79 tdddlreiaKEAGLDAAKFDAClnsgavaakVEADTALAQALGVTGTPTFVV-NGKLVSGAVPYEELEAALDA 150
|
|
| Thioredoxin_2 |
pfam13098 |
Thioredoxin-like domain; |
104-227 |
5.31e-27 |
|
Thioredoxin-like domain;
Pssm-ID: 379034 [Multi-domain] Cd Length: 103 Bit Score: 99.81 E-value: 5.31e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138724 104 APEEKHVITVFTDITCGYCRKLHEQMKDYNalGITVRYlafprqglSSQAEKDMRSIWCMADRNKAFddamknndispat 183
Cdd:pfam13098 1 KGNGKPVLVVFTDPDCPYCKKLKKELLEDP--DVTVYL--------GPNFVFIAVNIWCAKEVAKAF------------- 57
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 488138724 184 ckTDISKHYQLGVQFGIQGTPAIVLQNGT----IVPGYQGPKEMLQML 227
Cdd:pfam13098 58 --TDILENKELGRKYGVRGTPTIVFFDGKgellRLPGYVPAEEFLALL 103
|
|
| DsbA_family |
cd02972 |
DsbA family; consists of DsbA and DsbA-like proteins, including DsbC, DsbG, glutathione (GSH) ... |
111-218 |
1.06e-15 |
|
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: 1.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138724 111 ITVFTDITCGYCRKLHEQMKDY---NALGITVRYLAFPRQG-LSSQAEKDMRSIWCMADRNK--AFDDAMKNndispatc 184
Cdd:cd02972 1 IVEFFDPLCPYCYLFEPELEKLlyaDDGGVRVVYRPFPLLGgMPPNSLAAARAALAAAAQGKfeALHEALAD-------- 72
|
90 100 110
....*....|....*....|....*....|....
gi 488138724 185 ktdiskhYQLGVQFGIQGTPAIVLqNGTIVPGYQ 218
Cdd:cd02972 73 -------TALARALGVTGTPTFVV-NGEKYSGAG 98
|
|
| DsbC_N |
pfam10411 |
Disulfide bond isomerase protein N-terminus; This is the N-terminal domain of the disulfide ... |
27-77 |
1.29e-14 |
|
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: 65.96 E-value: 1.29e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 488138724 27 QQTLKKL--DIQQADIQPSPIPGISTVMTESGVLYISADGKHLLQGPLYDVSG 77
Cdd:pfam10411 1 KAALEKRfpNLKVDSVSPSPVPGLYEVVTGGQVLYTDEDGRYLIQGRLYDLKT 53
|
|
| DsbA_Com1_like |
cd03023 |
DsbA family, Com1-like subfamily; composed of proteins similar to Com1, a 27-kDa outer ... |
104-228 |
1.76e-11 |
|
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: 60.30 E-value: 1.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138724 104 APEEKHVITVFTDITCGYCRKLHEQM--------------KDYNALG----------ITVR------YLAFPRQGLSSQA 153
Cdd:cd03023 2 NPNGDVTIVEFFDYNCGYCKKLAPELekllkedpdvrvvfKEFPILGessvlaarvaLAVWkngpgkYLEFHNALMATRG 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488138724 154 EKDMRSIWCMADRN----KAFDDAMKNNDISPAtcktdISKHYQLGVQFGIQGTPAIVLqNGTIVPGYQGPKEMLQMLN 228
Cdd:cd03023 82 RLNEESLLRIAKKAgldeAKLKKDMDDPEIEAT-----IDKNRQLARALGITGTPAFII-GDTVIPGAVPADTLKEAID 154
|
|
| dsbG |
PRK11657 |
disulfide isomerase/thiol-disulfide oxidase; Provisional |
42-227 |
1.56e-09 |
|
disulfide isomerase/thiol-disulfide oxidase; Provisional
Pssm-ID: 183262 [Multi-domain] Cd Length: 251 Bit Score: 56.51 E-value: 1.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138724 42 PSPIPGISTVMTESGV-LYISADGKHLLQGPLYDVSGDqpiNVTNQALLKKLEA-LSSEM---------IVYKAPEEKHV 110
Cdd:PRK11657 44 PGGLKGYAAKYQDMGVtIYLTPDGKHAISGYMYDEKGE---NLSEALLEKEVYApMGREMwqrleqshwILDGKADAPRI 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138724 111 ITVFTDITCGYCRKLHEQMKDYNALG-ITVRYL--AFPRQGLSSQAEkdmrSIWCMADRNKAFDDAMKNND--------- 178
Cdd:PRK11657 121 VYVFADPNCPYCKQFWQQARPWVDSGkVQLRHIlvGIIKPDSPGKAA----AILAAKDPAKALQEYEASGGklglkppas 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 488138724 179 ISPATCKTdISKHYQLGVQFGIQGTPAIVLQNGT-IVPGYQG---PKEMLQML 227
Cdd:PRK11657 197 IPAAVRKQ-LADNQKLMDDLGANATPAIYYMDKDgTLQQVVGlpdPAQLAEIM 248
|
|
| Thioredoxin_4 |
pfam13462 |
Thioredoxin; |
100-229 |
1.78e-08 |
|
Thioredoxin;
Pssm-ID: 433227 [Multi-domain] Cd Length: 164 Bit Score: 52.34 E-value: 1.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138724 100 IVYKAPEEKHVITVFTDITCGYCRKLHEQM----KDYNALGItVRY----LAFPRQGLSSQA-------EKDMRSIWCMA 164
Cdd:pfam13462 5 PVIGNPDAPVTVVEYADLRCPHCAKFHEEVlkllEEYIDTGK-VRFiirdFPLDGEGESLLAamaarcaGDQSPEYFLVI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138724 165 DR-----------------NKAFDDAMKNNDISPATCKTDISKHYQLGVQFGIQGTPAIVLqNGTIVPGYQGPKEMLQML 227
Cdd:pfam13462 84 DKllysqqeewaqdlelaaLAGLKDEEFEACLEEEDFLALVMADVKEARAAGINFTPTFII-NGKKVDGPLTYEELKKLI 162
|
..
gi 488138724 228 NA 229
Cdd:pfam13462 163 DD 164
|
|
| CnoX |
COG3118 |
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ... |
184-230 |
6.33e-04 |
|
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: 38.26 E-value: 6.33e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 488138724 184 CKTDISKHYQLGVQFGIQGTPAIVL-QNGTIVPGYQG--PKEML-QMLNAH 230
Cdd:COG3118 54 VKVDVDENPELAAQFGVRSIPTLLLfKDGQPVDRFVGalPKEQLrEFLDKV 104
|
|
| PTZ00056 |
PTZ00056 |
glutathione peroxidase; Provisional |
79-213 |
2.64e-03 |
|
glutathione peroxidase; Provisional
Pssm-ID: 240248 [Multi-domain] Cd Length: 199 Bit Score: 37.91 E-value: 2.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138724 79 QPINVTNQAL--------LKKLEALSSEMIVYKApeeKHVITVFTDITCGYCRKLHEQMKD----YNALGITVryLAFPR 146
Cdd:PTZ00056 6 KKITVSKDELrksiydytVKTLEGTTVPMSSLKN---KVLMITNSASKCGLTKKHVDQMNRlhsvFNPLGLEI--LAFPT 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488138724 147 QGLSSQAEKDMRSIWCMADRNKafddaMKNNDISPatCKTDISKHYQLgVQFGIQGTPAIVLQNGTI 213
Cdd:PTZ00056 81 SQFLNQEFPNTKDIRKFNDKNK-----IKYNFFEP--IEVNGENTHEL-FKFLKANCDSMHDENGTL 139
|
|
| |
