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Conserved domains on  [gi|493452040|ref|WP_006407317|]
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cytochrome c biogenesis protein DipZ [Burkholderia multivorans]

Protein Classification

cytochrome c biogenesis protein DipZ( domain architecture ID 14298428)

integral membrane cytochrome c biogenesis protein DipZ, or DsbD, is involved in disulfide bond formation of target proteins by transporting electrons from cytoplasmic thioredoxin to DsbC and DsbG

CATH:  3.40.30.10
Gene Ontology:  GO:0015036|GO:0017004
PubMed:  12074972|9099998|10049365|15558583
SCOP:  3000031

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TlpA_like_DipZ_like cd03012
TlpA-like family, DipZ-like subfamily; composed uncharacterized proteins containing a ...
 309-433 3.82e-76

TlpA-like family, DipZ-like subfamily; composed uncharacterized proteins containing a TlpA-like TRX domain. Some members show domain architectures similar to that of E. coli DipZ protein (also known as DsbD). The only eukaryotic members of the TlpA family belong to this subfamily. TlpA is a disulfide reductase known to have a crucial role in the biogenesis of cytochrome aa3.


:

Pssm-ID: 239310 [Multi-domain]  Cd Length: 126  Bit Score: 238.36  E-value: 3.82e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493452040 309 PPLDGAVQWLNS-PPLTAAALRGKVVLVDFWTYSCINCLRTLPYTNAWARKYARYGLVVIGVHAPEFAFERDIGNVKKAV 387
Cdd:cd03012    1 PEFEGILQWLNTdKPLSLAQLRGKVVLLDFWTYCCINCLHTLPYLTDLEQKYKDDGLVVIGVHSPEFAFERDLANVKSAV 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 493452040 388 HDLGIDYPVAIDNRYAIWRAFNNEYWPAHYFVDAQGRIRRHHFGEG 433
Cdd:cd03012   81 LRYGITYPVANDNDYATWRAYGNQYWPALYLIDPTGNVRHVHFGEG 126
Thioredoxin_10 pfam17991
Thioredoxin like C-terminal domain; This is the C-terminal thioredoxin like domain found in ...
 480-626 1.06e-73

Thioredoxin like C-terminal domain; This is the C-terminal thioredoxin like domain found in Rv2874 in the pathogenic bacterium Mycobacterium tuberculosis. Structure analysis of Rv2874-C shows the presence of a C-terminal domain formed by the 128 residues Thr568-Gly695. These residues form a jelly-roll structure in which two antiparallel beta-sheets sandwich a hydrophobic core. This domain is combined with a second domain with a carbohydrate-binding module (CBM) fold.


:

Pssm-ID: 465607  Cd Length: 142  Bit Score: 232.47  E-value: 1.06e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493452040  480 SPETYVGYARAEDFASPGGVVRDAAHRYDAPAHPALNDWGLAGTWQVGAEHATLAAPAGRIVYRFHARDLHLVLGpgaNG 559
Cdd:pfam17991   1 TPETYLGYERAENFAGPGGLRPGTPATYTAPADLPLNTWALSGTWTVGAESITAASAGARIRLRFHARDVHLVLG---GG 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493452040  560 KPVRFRVTVDGaAPGDAHGSDVDAQGYGTVTGQRLYQLVRQpGAIADRTFSIEFLDAGVDAYAFTFG 626
Cdd:pfam17991  78 GPGTVRVTLDG-KAGADHGADVDADGTITVSGPRLYQLVRQ-GAVRDGTLEIEFLDPGVEAYSFTFG 142
CcdA COG0785
Cytochrome c biogenesis protein CcdA [Energy production and conversion, Posttranslational ...
 1-195 2.14e-35

Cytochrome c biogenesis protein CcdA [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


:

Pssm-ID: 440548 [Multi-domain]  Cd Length: 193  Bit Score: 131.89  E-value: 2.14e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493452040   1 MLLIVLAYLGGVLTILSPCILPVLPFVFARADQP-------FVRTGLPLLVGMALTFAVVATLAAVGGGWVAQANQAGRW 73
Cdd:COG0785    2 LLSLLLAFLAGLLSFLSPCVLPLLPGYLSYLTGLsrasrrrALLRALLFVLGFSLVFVLLGALASALGSLLGQYQDLLRI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493452040  74 AAIVLLAIFGLSLLmprvaEHLTRPLVAAGNRLtglaqRDGRPAGPVSSLLLGVATGLLWAPCAGPILGLVLTGAALHGA 153
Cdd:COG0785   82 VAGVLLILFGLVLL-----GLLKIPFLQREARI-----NLRRKAGLLGAFLLGLAFGLGWTPCIGPILGAILALAATSGS 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 493452040 154 NVGTTLLLIAYAAGAATSLGVALVIGGKVFAAMKRSLGAGEW 195
Cdd:COG0785  152 VLRGALLLLAYALGLGLPFLLLALFAGRLLGRLRRLRRHLRW 193
 
Name Accession Description Interval E-value
TlpA_like_DipZ_like cd03012
TlpA-like family, DipZ-like subfamily; composed uncharacterized proteins containing a ...
 309-433 3.82e-76

TlpA-like family, DipZ-like subfamily; composed uncharacterized proteins containing a TlpA-like TRX domain. Some members show domain architectures similar to that of E. coli DipZ protein (also known as DsbD). The only eukaryotic members of the TlpA family belong to this subfamily. TlpA is a disulfide reductase known to have a crucial role in the biogenesis of cytochrome aa3.


Pssm-ID: 239310 [Multi-domain]  Cd Length: 126  Bit Score: 238.36  E-value: 3.82e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493452040 309 PPLDGAVQWLNS-PPLTAAALRGKVVLVDFWTYSCINCLRTLPYTNAWARKYARYGLVVIGVHAPEFAFERDIGNVKKAV 387
Cdd:cd03012    1 PEFEGILQWLNTdKPLSLAQLRGKVVLLDFWTYCCINCLHTLPYLTDLEQKYKDDGLVVIGVHSPEFAFERDLANVKSAV 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 493452040 388 HDLGIDYPVAIDNRYAIWRAFNNEYWPAHYFVDAQGRIRRHHFGEG 433
Cdd:cd03012   81 LRYGITYPVANDNDYATWRAYGNQYWPALYLIDPTGNVRHVHFGEG 126
Thioredoxin_10 pfam17991
Thioredoxin like C-terminal domain; This is the C-terminal thioredoxin like domain found in ...
 480-626 1.06e-73

Thioredoxin like C-terminal domain; This is the C-terminal thioredoxin like domain found in Rv2874 in the pathogenic bacterium Mycobacterium tuberculosis. Structure analysis of Rv2874-C shows the presence of a C-terminal domain formed by the 128 residues Thr568-Gly695. These residues form a jelly-roll structure in which two antiparallel beta-sheets sandwich a hydrophobic core. This domain is combined with a second domain with a carbohydrate-binding module (CBM) fold.


Pssm-ID: 465607  Cd Length: 142  Bit Score: 232.47  E-value: 1.06e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493452040  480 SPETYVGYARAEDFASPGGVVRDAAHRYDAPAHPALNDWGLAGTWQVGAEHATLAAPAGRIVYRFHARDLHLVLGpgaNG 559
Cdd:pfam17991   1 TPETYLGYERAENFAGPGGLRPGTPATYTAPADLPLNTWALSGTWTVGAESITAASAGARIRLRFHARDVHLVLG---GG 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493452040  560 KPVRFRVTVDGaAPGDAHGSDVDAQGYGTVTGQRLYQLVRQpGAIADRTFSIEFLDAGVDAYAFTFG 626
Cdd:pfam17991  78 GPGTVRVTLDG-KAGADHGADVDADGTITVSGPRLYQLVRQ-GAVRDGTLEIEFLDPGVEAYSFTFG 142
CcdA COG0785
Cytochrome c biogenesis protein CcdA [Energy production and conversion, Posttranslational ...
 1-195 2.14e-35

Cytochrome c biogenesis protein CcdA [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440548 [Multi-domain]  Cd Length: 193  Bit Score: 131.89  E-value: 2.14e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493452040   1 MLLIVLAYLGGVLTILSPCILPVLPFVFARADQP-------FVRTGLPLLVGMALTFAVVATLAAVGGGWVAQANQAGRW 73
Cdd:COG0785    2 LLSLLLAFLAGLLSFLSPCVLPLLPGYLSYLTGLsrasrrrALLRALLFVLGFSLVFVLLGALASALGSLLGQYQDLLRI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493452040  74 AAIVLLAIFGLSLLmprvaEHLTRPLVAAGNRLtglaqRDGRPAGPVSSLLLGVATGLLWAPCAGPILGLVLTGAALHGA 153
Cdd:COG0785   82 VAGVLLILFGLVLL-----GLLKIPFLQREARI-----NLRRKAGLLGAFLLGLAFGLGWTPCIGPILGAILALAATSGS 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 493452040 154 NVGTTLLLIAYAAGAATSLGVALVIGGKVFAAMKRSLGAGEW 195
Cdd:COG0785  152 VLRGALLLLAYALGLGLPFLLLALFAGRLLGRLRRLRRHLRW 193
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 307-448 6.09e-34

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 125.96  E-value: 6.09e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493452040 307 TLPPLDGAvqwlnspPLTAAALRGKVVLVDFWTYSCINCLRTLPYTNAWARKYAryGLVVIGVHapefaFERDIGNVKKA 386
Cdd:COG0526   12 TLTDLDGK-------PLSLADLKGKPVLVNFWATWCPPCRAEMPVLKELAEEYG--GVVFVGVD-----VDENPEAVKAF 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493452040 387 VHDLGIDYPVAIDNRYAIWRAFNNEYWPAHYFVDAQGRIRRHHFGEGEYAESERAIQSLLAE 448
Cdd:COG0526   78 LKELGLPYPVLLDPDGELAKAYGVRGIPTTVLIDKDGKIVARHVGPLSPEELEEALEKLLAK 139
PLN02919 PLN02919
haloacid dehalogenase-like hydrolase family protein
 307-456 1.11e-22

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215497 [Multi-domain]  Cd Length: 1057  Bit Score: 103.39  E-value: 1.11e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493452040  307 TLPPLDGAVQWLNSPPLT-AAALRGKVVLVDFWTYSCINCLRTLPYTNAWARKYARYGLVVIGVHAPEFAFERDIGNVKK 385
Cdd:PLN02919  396 KVPEFPPKLDWLNTAPLQfRRDLKGKVVILDFWTYCCINCMHVLPDLEFLEKKYKDQPFTVVGVHSAKFDNEKDLEAIRN 475

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493452040  386 AVHDLGIDYPVAIDNRYAIWRAFNNEYWPAHYFVDAQGRIRRHHFGEGEYAESERAIQSLLAEAGHPDALN 456
Cdd:PLN02919  476 AVLRYNISHPVVNDGDMYLWRELGVSSWPTFAVVSPNGKLIAQLSGEGHRKDLDDLVEAALQYYGEKKLLD 546
DsbD pfam02683
Cytochrome C biogenesis protein transmembrane region; This family consists of the ...
 7-207 1.57e-11

Cytochrome C biogenesis protein transmembrane region; This family consists of the transmembrane (i.e. non-catalytic) region of Cytochrome C biogenesis proteins also known as disulphide interchange proteins. These proteins posses a protein disulphide isomerase like domain that is not found within the aligned region of this family.


Pssm-ID: 280792 [Multi-domain]  Cd Length: 213  Bit Score: 63.96  E-value: 1.57e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493452040    7 AYLGGVLTILSPCILPVLPFVFA-------------RADQPFVRTGLPLLVGMALTFAVVATLAAVGGGWVAQANQAGRW 73
Cdd:pfam02683   1 AFLAGLLSFLSPCILPLIPAYLSyisgvsvgdrkqgKKRVRVLLKSLLFVLGLSLVFVLLGLSAAFLGQLFGDFKGWVRI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493452040   74 AAIVLLAIFGLSLLMPRVAEHLTRPlvaagnRLTGLAQRdgRPAGPV-SSLLLGVATGLLWAPCAGPILGLVLTGAALHG 152
Cdd:pfam02683  81 IAGLIVILFGLHFLGVFRIPFLYKL------RLVHKTKK--KISLPVlGAFLLGMTFALGWTPCIGPILASVLALAASTG 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 493452040  153 ANVGTTLLLIAYAAGaatsLGVALVIGGKVFAAMKRSLgagEWIRRGIGAALLAG 207
Cdd:pfam02683 153 SLLLGAGLMVVYVLG----LAAPFLLASLFFGSLLLRL---KWLRKNSHWVKIAG 200
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 307-426 3.59e-09

AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) and thiol specific antioxidant (TSA).


Pssm-ID: 425763 [Multi-domain]  Cd Length: 124  Bit Score: 54.92  E-value: 3.59e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493452040  307 TLPPLDGAvqwlnspPLTAAALRGKVVLVDFW-TYSCINCLRTLPYTNAWARKYARYGLVVIGVhAPEFAFerdigNVKK 385
Cdd:pfam00578   9 ELPDGDGG-------TVSLSDYRGKWVVLFFYpADWTPVCTTELPALADLYEEFKKLGVEVLGV-SVDSPE-----SHKA 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 493452040  386 AVHDLGIDYPVAID------NRYAIWRAFNNEYWPAHYFVDAQGRIR 426
Cdd:pfam00578  76 FAEKYGLPFPLLSDpdgevaRAYGVLNEEEGGALRATFVIDPDGKVR 122
dipZ PRK00293
thiol:disulfide interchange protein precursor; Provisional
 4-206 1.96e-03

thiol:disulfide interchange protein precursor; Provisional


Pssm-ID: 234717 [Multi-domain]  Cd Length: 571  Bit Score: 41.35  E-value: 1.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493452040   4 IVLAYLGGVLTILSPCILPVLPF----VFARADQPFVRTGLPLLV----GMALTFAVVATLAAVGGGWVAQANQAGrWAA 75
Cdd:PRK00293 169 LLWFFLIGIGLAFTPCVLPMYPIlsgiVLGGKQRLSTARALLLSFvyvqGMALTYTLLGLVVAAAGLQFQAALQHP-YVL 247

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493452040  76 IVL--------LAIFGL-SLLMPRvaehltrplvAAGNRLTGLA--QRDGRPAGpvsSLLLGVATGLLWAPC-AGPILGL 143
Cdd:PRK00293 248 IGLsilfvllaLSMFGLfTLQLPS----------SLQTRLTLLSnrQQGGSLGG---VFVMGAISGLICSPCtTAPLSGA 314

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493452040 144 VL----TGAALHGAnvgttLLLIAYAAGaatsLGVALVI----GGKVFAAmkrslgAGEW---IRRGIGAALLA 206
Cdd:PRK00293 315 LLyiaqSGDLLLGG-----LTLYLLALG----MGLPLILittfGNKLLPK------SGPWmnqVKTAFGFVLLA 373
 
Name Accession Description Interval E-value
TlpA_like_DipZ_like cd03012
TlpA-like family, DipZ-like subfamily; composed uncharacterized proteins containing a ...
 309-433 3.82e-76

TlpA-like family, DipZ-like subfamily; composed uncharacterized proteins containing a TlpA-like TRX domain. Some members show domain architectures similar to that of E. coli DipZ protein (also known as DsbD). The only eukaryotic members of the TlpA family belong to this subfamily. TlpA is a disulfide reductase known to have a crucial role in the biogenesis of cytochrome aa3.


Pssm-ID: 239310 [Multi-domain]  Cd Length: 126  Bit Score: 238.36  E-value: 3.82e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493452040 309 PPLDGAVQWLNS-PPLTAAALRGKVVLVDFWTYSCINCLRTLPYTNAWARKYARYGLVVIGVHAPEFAFERDIGNVKKAV 387
Cdd:cd03012    1 PEFEGILQWLNTdKPLSLAQLRGKVVLLDFWTYCCINCLHTLPYLTDLEQKYKDDGLVVIGVHSPEFAFERDLANVKSAV 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 493452040 388 HDLGIDYPVAIDNRYAIWRAFNNEYWPAHYFVDAQGRIRRHHFGEG 433
Cdd:cd03012   81 LRYGITYPVANDNDYATWRAYGNQYWPALYLIDPTGNVRHVHFGEG 126
Thioredoxin_10 pfam17991
Thioredoxin like C-terminal domain; This is the C-terminal thioredoxin like domain found in ...
 480-626 1.06e-73

Thioredoxin like C-terminal domain; This is the C-terminal thioredoxin like domain found in Rv2874 in the pathogenic bacterium Mycobacterium tuberculosis. Structure analysis of Rv2874-C shows the presence of a C-terminal domain formed by the 128 residues Thr568-Gly695. These residues form a jelly-roll structure in which two antiparallel beta-sheets sandwich a hydrophobic core. This domain is combined with a second domain with a carbohydrate-binding module (CBM) fold.


Pssm-ID: 465607  Cd Length: 142  Bit Score: 232.47  E-value: 1.06e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493452040  480 SPETYVGYARAEDFASPGGVVRDAAHRYDAPAHPALNDWGLAGTWQVGAEHATLAAPAGRIVYRFHARDLHLVLGpgaNG 559
Cdd:pfam17991   1 TPETYLGYERAENFAGPGGLRPGTPATYTAPADLPLNTWALSGTWTVGAESITAASAGARIRLRFHARDVHLVLG---GG 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 493452040  560 KPVRFRVTVDGaAPGDAHGSDVDAQGYGTVTGQRLYQLVRQpGAIADRTFSIEFLDAGVDAYAFTFG 626
Cdd:pfam17991  78 GPGTVRVTLDG-KAGADHGADVDADGTITVSGPRLYQLVRQ-GAVRDGTLEIEFLDPGVEAYSFTFG 142
CcdA COG0785
Cytochrome c biogenesis protein CcdA [Energy production and conversion, Posttranslational ...
 1-195 2.14e-35

Cytochrome c biogenesis protein CcdA [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440548 [Multi-domain]  Cd Length: 193  Bit Score: 131.89  E-value: 2.14e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493452040   1 MLLIVLAYLGGVLTILSPCILPVLPFVFARADQP-------FVRTGLPLLVGMALTFAVVATLAAVGGGWVAQANQAGRW 73
Cdd:COG0785    2 LLSLLLAFLAGLLSFLSPCVLPLLPGYLSYLTGLsrasrrrALLRALLFVLGFSLVFVLLGALASALGSLLGQYQDLLRI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493452040  74 AAIVLLAIFGLSLLmprvaEHLTRPLVAAGNRLtglaqRDGRPAGPVSSLLLGVATGLLWAPCAGPILGLVLTGAALHGA 153
Cdd:COG0785   82 VAGVLLILFGLVLL-----GLLKIPFLQREARI-----NLRRKAGLLGAFLLGLAFGLGWTPCIGPILGAILALAATSGS 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 493452040 154 NVGTTLLLIAYAAGAATSLGVALVIGGKVFAAMKRSLGAGEW 195
Cdd:COG0785  152 VLRGALLLLAYALGLGLPFLLLALFAGRLLGRLRRLRRHLRW 193
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 307-431 3.18e-34

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: 125.81  E-value: 3.18e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493452040 307 TLPPLDGAvqwlnspPLTAAALRGKVVLVDFWTYSCINCLRTLPYTNAWARKYARYGLVVIGVHAPEFaferDIGNVKKA 386
Cdd:cd02966    3 SLPDLDGK-------PVSLSDLKGKVVLVNFWASWCPPCRAEMPELEALAKEYKDDGVEVVGVNVDDD----DPAAVKAF 71

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 493452040 387 VHDLGIDYPVAIDNRYAIWRAFNNEYWPAHYFVDAQGRIRRHHFG 431
Cdd:cd02966   72 LKKYGITFPVLLDPDGELAKAYGVRGLPTTFLIDRDGRIRARHVG 116
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 307-448 6.09e-34

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 125.96  E-value: 6.09e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493452040 307 TLPPLDGAvqwlnspPLTAAALRGKVVLVDFWTYSCINCLRTLPYTNAWARKYAryGLVVIGVHapefaFERDIGNVKKA 386
Cdd:COG0526   12 TLTDLDGK-------PLSLADLKGKPVLVNFWATWCPPCRAEMPVLKELAEEYG--GVVFVGVD-----VDENPEAVKAF 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493452040 387 VHDLGIDYPVAIDNRYAIWRAFNNEYWPAHYFVDAQGRIRRHHFGEGEYAESERAIQSLLAE 448
Cdd:COG0526   78 LKELGLPYPVLLDPDGELAKAYGVRGIPTTVLIDKDGKIVARHVGPLSPEELEEALEKLLAK 139
PLN02919 PLN02919
haloacid dehalogenase-like hydrolase family protein
 307-456 1.11e-22

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215497 [Multi-domain]  Cd Length: 1057  Bit Score: 103.39  E-value: 1.11e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493452040  307 TLPPLDGAVQWLNSPPLT-AAALRGKVVLVDFWTYSCINCLRTLPYTNAWARKYARYGLVVIGVHAPEFAFERDIGNVKK 385
Cdd:PLN02919  396 KVPEFPPKLDWLNTAPLQfRRDLKGKVVILDFWTYCCINCMHVLPDLEFLEKKYKDQPFTVVGVHSAKFDNEKDLEAIRN 475

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493452040  386 AVHDLGIDYPVAIDNRYAIWRAFNNEYWPAHYFVDAQGRIRRHHFGEGEYAESERAIQSLLAEAGHPDALN 456
Cdd:PLN02919  476 AVLRYNISHPVVNDGDMYLWRELGVSSWPTFAVVSPNGKLIAQLSGEGHRKDLDDLVEAALQYYGEKKLLD 546
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
307-449 7.08e-22

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 91.85  E-value: 7.08e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493452040 307 TLPPLDGAvqwlnspPLTAAALRGKVVLVDFWTYSCINCLRTLPYTNAWARKYARYGLVVIGVHApefafeRDIGNVKKA 386
Cdd:COG1225    5 TLPDLDGK-------TVSLSDLRGKPVVLYFYATWCPGCTAELPELRDLYEEFKDKGVEVLGVSS------DSDEAHKKF 71

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493452040 387 VHDLGIDYPVAIDNRYAIWRAFNNEYWPAHYFVDAQGRIRRHHFGEGEYAES-ERAIQSLLAEA 449
Cdd:COG1225   72 AEKYGLPFPLLSDPDGEVAKAYGVRGTPTTFLIDPDGKIRYVWVGPVDPRPHlEEVLEALLAEL 135
DsbD COG4232
Thiol:disulfide interchange protein DsbD [Posttranslational modification, protein turnover, ...
 2-345 9.73e-13

Thiol:disulfide interchange protein DsbD [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443376 [Multi-domain]  Cd Length: 416  Bit Score: 70.22  E-value: 9.73e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493452040   2 LLIVLAYLGGVLTILSPCILPVLP----FVFARADQPFVRTGLPLLV---GMALTFAVVATLAAVGGGWVAQANQAGRWA 74
Cdd:COG4232    4 LILLLAFLGGLLLNLTPCVLPMLPikssIIVGQGGKSRRRAFLLSLAyvlGMALTYTLLGLLAALLGGAVGWGFQLQSPW 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493452040  75 AIVLLA----IFGLSLL------MPRvaehltrplvAAGNRLTGLAQRDGrpagPVSSLLLGVATGLLWAPCAGPILGLV 144
Cdd:COG4232   84 VLGALAllfvLLALSMFglfelqLPS----------SLQNRLAALSNGGG----LLGAFFMGVLAALVATPCTAPFLGGA 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493452040 145 LtGAALHGANVgttllLIAYAAGAATSLGVA---LVIGgkVFAAMKRSL-GAGEW---IRRGIGAALLA----------- 206
Cdd:COG4232  150 L-GYALQTGDA-----LLGLLALFALGLGMAlplLLLG--LFPGLLKLLpKPGAWmetVKQVFGFLLLAtaiwllsvllp 221

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493452040 207 --GVGAIALGLdTGALAQLSTIATGGLeTRLVDRLGGRPAGMPIAMAAVDGASGRMQRDAGPGPAMMAAADTAAAERSAP 284
Cdd:COG4232  222 qaGLDAVALLL-WALLLLALALWLLGA-LRLPHDSSGRRLSVRKGLGLLLLLAGLALLLGALSGADPLQPLAAGAAAAAA 299

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 493452040 285 PAGTMMRaaapmaapaalpvegtlPPLDGAVQwlnsppltAAALRGKVVLVDFWTYSCINC 345
Cdd:COG4232  300 AAGLAWQ-----------------ADLEAALA--------EARAEGKPVFVDFTADWCVTC 335
DsbD pfam02683
Cytochrome C biogenesis protein transmembrane region; This family consists of the ...
 7-207 1.57e-11

Cytochrome C biogenesis protein transmembrane region; This family consists of the transmembrane (i.e. non-catalytic) region of Cytochrome C biogenesis proteins also known as disulphide interchange proteins. These proteins posses a protein disulphide isomerase like domain that is not found within the aligned region of this family.


Pssm-ID: 280792 [Multi-domain]  Cd Length: 213  Bit Score: 63.96  E-value: 1.57e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493452040    7 AYLGGVLTILSPCILPVLPFVFA-------------RADQPFVRTGLPLLVGMALTFAVVATLAAVGGGWVAQANQAGRW 73
Cdd:pfam02683   1 AFLAGLLSFLSPCILPLIPAYLSyisgvsvgdrkqgKKRVRVLLKSLLFVLGLSLVFVLLGLSAAFLGQLFGDFKGWVRI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493452040   74 AAIVLLAIFGLSLLMPRVAEHLTRPlvaagnRLTGLAQRdgRPAGPV-SSLLLGVATGLLWAPCAGPILGLVLTGAALHG 152
Cdd:pfam02683  81 IAGLIVILFGLHFLGVFRIPFLYKL------RLVHKTKK--KISLPVlGAFLLGMTFALGWTPCIGPILASVLALAASTG 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 493452040  153 ANVGTTLLLIAYAAGaatsLGVALVIGGKVFAAMKRSLgagEWIRRGIGAALLAG 207
Cdd:pfam02683 153 SLLLGAGLMVVYVLG----LAAPFLLASLFFGSLLLRL---KWLRKNSHWVKIAG 200
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 307-426 3.59e-09

AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) and thiol specific antioxidant (TSA).


Pssm-ID: 425763 [Multi-domain]  Cd Length: 124  Bit Score: 54.92  E-value: 3.59e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493452040  307 TLPPLDGAvqwlnspPLTAAALRGKVVLVDFW-TYSCINCLRTLPYTNAWARKYARYGLVVIGVhAPEFAFerdigNVKK 385
Cdd:pfam00578   9 ELPDGDGG-------TVSLSDYRGKWVVLFFYpADWTPVCTTELPALADLYEEFKKLGVEVLGV-SVDSPE-----SHKA 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 493452040  386 AVHDLGIDYPVAID------NRYAIWRAFNNEYWPAHYFVDAQGRIR 426
Cdd:pfam00578  76 FAEKYGLPFPLLSDpdgevaRAYGVLNEEEGGALRATFVIDPDGKVR 122
PRK03147 PRK03147
thiol-disulfide oxidoreductase ResA;
328-432 5.75e-09

thiol-disulfide oxidoreductase ResA;


Pssm-ID: 179545 [Multi-domain]  Cd Length: 173  Bit Score: 55.78  E-value: 5.75e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493452040 328 LRGKVVLVDFWTYSCINCLRTLPYTNAWARKYARYGLVVIGVHA--PEFAferdignVKKAVHDLGIDYPVAIDNRYAIW 405
Cdd:PRK03147  59 LKGKGVFLNFWGTWCKPCEKEMPYMNELYPKYKEKGVEIIAVNVdeTELA-------VKNFVNRYGLTFPVAIDKGRQVI 131

                         90       100
                 ....*....|....*....|....*..
gi 493452040 406 RAFNNEYWPAHYFVDAQGRIRRHHFGE 432
Cdd:PRK03147 132 DAYGVGPLPTTFLIDKDGKVVKVITGE 158
Thioredoxin_8 pfam13905
Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 330-425 9.30e-08

Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the reversible oxidation of an active centre disulfide bond.


Pssm-ID: 464033 [Multi-domain]  Cd Length: 95  Bit Score: 50.00  E-value: 9.30e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493452040  330 GKVVLVDFWTYSCINCLRTLPYTNAWARKYARY-GLVVIGVHapefaFERDIGNVKKAVHDLG---IDYPVAIDNRYAIW 405
Cdd:pfam13905   1 GKVVLLYFGASWCKPCRRFTPLLKELYEKLKKKkNVEIVFVS-----LDRDLEEFKDYLKKMPkdwLSVPFDDDERNELK 75

                          90       100
                  ....*....|....*....|
gi 493452040  406 RAFNNEYWPAHYFVDAQGRI 425
Cdd:pfam13905  76 RKYGVNAIPTLVLLDPNGEV 95
Redoxin pfam08534
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
 322-426 3.58e-06

Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.


Pssm-ID: 400717 [Multi-domain]  Cd Length: 148  Bit Score: 46.98  E-value: 3.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493452040  322 PLTAAALRGKVVLVDFW-TYSCINCLRTLPYTNAWARKYARYGLVVIGVHAPEFAFerdigNVKKAVHDLGIDYPVAIDN 400
Cdd:pfam08534  20 TVSLSDFKGKKVVLNFWpGAFCPTCSAEHPYLEKLNELYKEKGVDVVAVNSDNDAF-----FVKRFWGKEGLPFPFLSDG 94

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 493452040  401 RYAIWRAFNNE--------YWPAHYFV-DAQGRIR 426
Cdd:pfam08534  95 NAAFTKALGLPieedasagLRSPRYAViDEDGKVV 129
TlpA_like_DsbE cd03010
TlpA-like family, DsbE (also known as CcmG and CycY) subfamily; DsbE is a membrane-anchored, ...
 307-431 8.64e-05

TlpA-like family, DsbE (also known as CcmG and CycY) subfamily; DsbE is a membrane-anchored, periplasmic TRX-like reductase containing a CXXC motif that specifically donates reducing equivalents to apocytochrome c via CcmH, another cytochrome c maturation (Ccm) factor with a redox active CXXC motif. Assembly of cytochrome c requires the ligation of heme to reduced thiols of the apocytochrome. In bacteria, this assembly occurs in the periplasm. The reductase activity of DsbE in the oxidizing environment of the periplasm is crucial in the maturation of cytochrome c.


Pssm-ID: 239308 [Multi-domain]  Cd Length: 127  Bit Score: 42.56  E-value: 8.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493452040 307 TLPPLDGAvqwlnSPPLTAAALRGKVVLVDFWTYSCINCLRTLPYTNAWARKyaryGLV-VIGVH---APEFA--FERDI 380
Cdd:cd03010    7 SLPALPGP-----DKTLTSADLKGKPYLLNVWASWCAPCREEHPVLMALARQ----GRVpIYGINykdNPENAlaWLARH 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 493452040 381 GNVKKAVhdlGIDYP--VAIDnrYAIWRAfnneywPAHYFVDAQGRIRRHHFG 431
Cdd:cd03010   78 GNPYAAV---GFDPDgrVGID--LGVYGV------PETFLIDGDGIIRYKHVG 119
TlpA_like_ScsD_MtbDsbE cd03011
TlpA-like family, suppressor for copper sensitivity D protein (ScsD) and actinobacterial DsbE ...
 314-423 1.77e-04

TlpA-like family, suppressor for copper sensitivity D protein (ScsD) and actinobacterial DsbE homolog subfamily; composed of ScsD, the DsbE homolog of Mycobacterium tuberculosis (MtbDsbE) and similar proteins, all containing a redox-active CXXC motif. The Salmonella typhimurium ScsD is a thioredoxin-like protein which confers copper tolerance to copper-sensitive mutants of E. coli. MtbDsbE has been characterized as an oxidase in vitro, catalyzing the disulfide bond formation of substrates like hirudin. The reduced form of MtbDsbE is more stable than its oxidized form, consistent with an oxidase function. This is in contrast to the function of DsbE from gram-negative bacteria which is a specific reductase of apocytochrome c.


Pssm-ID: 239309 [Multi-domain]  Cd Length: 123  Bit Score: 41.51  E-value: 1.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493452040 314 AVQWLNSPPLTAAALRGKVVLVDFWTYSCINCLRTLPYTNAWARKYAryglvVIGVHAPEfafeRDIGNVKKAVHDLGID 393
Cdd:cd03011    4 TATTLDGEQFDLESLSGKPVLVYFWATWCPVCRFTSPTVNQLAADYP-----VVSVALRS----GDDGAVARFMQKKGYG 74

                         90       100       110
                 ....*....|....*....|....*....|
gi 493452040 394 YPVAIDNRYAIWRAFNNEYWPAHYFVDAQG 423
Cdd:cd03011   75 FPVINDPDGVISARWGVSVTPAIVIVDPGG 104
dipZ PRK00293
thiol:disulfide interchange protein precursor; Provisional
 4-206 1.96e-03

thiol:disulfide interchange protein precursor; Provisional


Pssm-ID: 234717 [Multi-domain]  Cd Length: 571  Bit Score: 41.35  E-value: 1.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493452040   4 IVLAYLGGVLTILSPCILPVLPF----VFARADQPFVRTGLPLLV----GMALTFAVVATLAAVGGGWVAQANQAGrWAA 75
Cdd:PRK00293 169 LLWFFLIGIGLAFTPCVLPMYPIlsgiVLGGKQRLSTARALLLSFvyvqGMALTYTLLGLVVAAAGLQFQAALQHP-YVL 247

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493452040  76 IVL--------LAIFGL-SLLMPRvaehltrplvAAGNRLTGLA--QRDGRPAGpvsSLLLGVATGLLWAPC-AGPILGL 143
Cdd:PRK00293 248 IGLsilfvllaLSMFGLfTLQLPS----------SLQTRLTLLSnrQQGGSLGG---VFVMGAISGLICSPCtTAPLSGA 314

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 493452040 144 VL----TGAALHGAnvgttLLLIAYAAGaatsLGVALVI----GGKVFAAmkrslgAGEW---IRRGIGAALLA 206
Cdd:PRK00293 315 LLyiaqSGDLLLGG-----LTLYLLALG----MGLPLILittfGNKLLPK------SGPWmnqVKTAFGFVLLA 373
DsbD_2 pfam13386
Cytochrome C biogenesis protein transmembrane region;
2-208 6.39e-03

Cytochrome C biogenesis protein transmembrane region;


Pssm-ID: 463866  Cd Length: 199  Bit Score: 38.36  E-value: 6.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493452040    2 LLIVLAYLGGVltilsPCILPVLPFVFARADQPFVRTGLPLL--VGMALTFAVVATLAAVGGGWVAQANQ------AGRW 73
Cdd:pfam13386   1 AAFLLGLLGSF-----HCLGMCGGIVLALSLALPSRRFALLLynLGRILSYTLLGALAGLLGSVLSLAGQlaglrgVLGV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493452040   74 AAIVLLAIFGLSLLMPRVAEHLTRPLVAAGNRLTGLAQRDGRPAGPvssLLLGVATGLLwaPCagPILGLVLTGAALHGA 153
Cdd:pfam13386  76 LLGLLLLLLGLYLLGLPGLLKLERLGKGLWRLLSPLAKRLKSPGGA---FLLGLLWGLL--PC--GLVYSALLYAAATGS 148

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 493452040  154 NVGTTLLLIAYAAGaaTSLgvALVIGGKVFAAMKRSLGaGEWIRRGIGAALLAGV 208
Cdd:pfam13386 149 ALEGALVMLAFGLG--TLP--ALLLFGLLAGFLSKKLR-KRLQRLAGVLLILLGI 198
 
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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