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Conserved domains on  [gi|15610011|ref|NP_217390|]
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integral membrane C-type cytochrome biogenesis protein DipZ [Mycobacterium tuberculosis H37Rv]

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 ...
 401-528 5.45e-74

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: 234.51  E-value: 5.45e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610011 401 PDLKGITGWLNTpgNKPIDLKSLRGKVVLIDFWAYSCINCQRAIPHVVGWYQAYKDSGLAVIGVHTPEYAFEKVPGNVAK 480
Cdd:cd03012   1 PEFEGILQWLNT--DKPLSLAQLRGKVVLLDFWTYCCINCLHTLPYLTDLEQKYKDDGLVVIGVHSPEFAFERDLANVKS 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 15610011 481 GAANLGISYPIALDNNYATWTNYRNRYWPAEYLIDATGTVRHIKFGEG 528
Cdd:cd03012  79 AVLRYGITYPVANDNDYATWRAYGNQYWPALYLIDPTGNVRHVHFGEG 126
Thioredoxin_10 pfam17991
Thioredoxin like C-terminal domain; This is the C-terminal thioredoxin like domain found in ...
 568-695 5.99e-41

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: 146.19  E-value: 5.99e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610011   568 TPETYFGVGKVVNYGGGGAYDEGSAV-FDYPPSLAANSFALRGRWALDYQGATSDGNDAAIKLNYHAKDVYIVVG--GTG 644
Cdd:pfam17991   1 TPETYLGYERAENFAGPGGLRPGTPAtYTAPADLPLNTWALSGTWTVGAESITAASAGARIRLRFHARDVHLVLGggGPG 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15610011   645 TLTVVRDGKPA-----------TLPISGpPTTHQVVAGYRLASETLEVR-PSKGLQVFSFTYG 695
Cdd:pfam17991  81 TVRVTLDGKAGadhgadvdadgTITVSG-PRLYQLVRQGAVRDGTLEIEfLDPGVEAYSFTFG 142
CcdA COG0785
Cytochrome c biogenesis protein CcdA [Energy production and conversion, Posttranslational ...
 115-321 5.56e-38

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


:

Pssm-ID: 440548 [Multi-domain]  Cd Length: 193  Bit Score: 139.59  E-value: 5.56e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610011 115 LTLALVGFLGGLITGISPCILPVLPVIFFSGAqsvdaaqvakpeGAVAVRRKRALSATLRpyrVIGGLVLSFGMVTLLGS 194
Cdd:COG0785   2 LLSLLLAFLAGLLSFLSPCVLPLLPGYLSYLT------------GLSRASRRRALLRALL---FVLGFSLVFVLLGALAS 66

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610011 195 ALLSVLHLPQDAIRWAALVALVAIGAGLIFPRFEQLLEKPFsRIPQKQIVTRSNGFGLGLALGVLYVPCAGPILAAIVVA 274
Cdd:COG0785  67 ALGSLLGQYQDLLRIVAGVLLILFGLVLLGLLKIPFLQREA-RINLRRKAGLLGAFLLGLAFGLGWTPCIGPILGAILAL 145

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 15610011 275 GATATIGLGTVVLTATFALGAALPLLFFALAGQRIAERVGAFRRRQR 321
Cdd:COG0785 146 AATSGSVLRGALLLLAYALGLGLPFLLLALFAGRLLGRLRRLRRHLR 192
 
Name Accession Description Interval E-value
TlpA_like_DipZ_like cd03012
TlpA-like family, DipZ-like subfamily; composed uncharacterized proteins containing a ...
 401-528 5.45e-74

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: 234.51  E-value: 5.45e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610011 401 PDLKGITGWLNTpgNKPIDLKSLRGKVVLIDFWAYSCINCQRAIPHVVGWYQAYKDSGLAVIGVHTPEYAFEKVPGNVAK 480
Cdd:cd03012   1 PEFEGILQWLNT--DKPLSLAQLRGKVVLLDFWTYCCINCLHTLPYLTDLEQKYKDDGLVVIGVHSPEFAFERDLANVKS 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 15610011 481 GAANLGISYPIALDNNYATWTNYRNRYWPAEYLIDATGTVRHIKFGEG 528
Cdd:cd03012  79 AVLRYGITYPVANDNDYATWRAYGNQYWPALYLIDPTGNVRHVHFGEG 126
Thioredoxin_10 pfam17991
Thioredoxin like C-terminal domain; This is the C-terminal thioredoxin like domain found in ...
 568-695 5.99e-41

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: 146.19  E-value: 5.99e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610011   568 TPETYFGVGKVVNYGGGGAYDEGSAV-FDYPPSLAANSFALRGRWALDYQGATSDGNDAAIKLNYHAKDVYIVVG--GTG 644
Cdd:pfam17991   1 TPETYLGYERAENFAGPGGLRPGTPAtYTAPADLPLNTWALSGTWTVGAESITAASAGARIRLRFHARDVHLVLGggGPG 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15610011   645 TLTVVRDGKPA-----------TLPISGpPTTHQVVAGYRLASETLEVR-PSKGLQVFSFTYG 695
Cdd:pfam17991  81 TVRVTLDGKAGadhgadvdadgTITVSG-PRLYQLVRQGAVRDGTLEIEfLDPGVEAYSFTFG 142
CcdA COG0785
Cytochrome c biogenesis protein CcdA [Energy production and conversion, Posttranslational ...
 115-321 5.56e-38

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


Pssm-ID: 440548 [Multi-domain]  Cd Length: 193  Bit Score: 139.59  E-value: 5.56e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610011 115 LTLALVGFLGGLITGISPCILPVLPVIFFSGAqsvdaaqvakpeGAVAVRRKRALSATLRpyrVIGGLVLSFGMVTLLGS 194
Cdd:COG0785   2 LLSLLLAFLAGLLSFLSPCVLPLLPGYLSYLT------------GLSRASRRRALLRALL---FVLGFSLVFVLLGALAS 66

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610011 195 ALLSVLHLPQDAIRWAALVALVAIGAGLIFPRFEQLLEKPFsRIPQKQIVTRSNGFGLGLALGVLYVPCAGPILAAIVVA 274
Cdd:COG0785  67 ALGSLLGQYQDLLRIVAGVLLILFGLVLLGLLKIPFLQREA-RINLRRKAGLLGAFLLGLAFGLGWTPCIGPILGAILAL 145

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 15610011 275 GATATIGLGTVVLTATFALGAALPLLFFALAGQRIAERVGAFRRRQR 321
Cdd:COG0785 146 AATSGSVLRGALLLLAYALGLGLPFLLLALFAGRLLGRLRRLRRHLR 192
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 399-542 3.28e-31

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 118.64  E-value: 3.28e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610011 399 TAPDLKgitgwLNTPGNKPIDLKSLRGKVVLIDFWAYSCINCQRAIPHVVGWYQAYKdsGLAVIGVHtpeyaFEKVPGNV 478
Cdd:COG0526   7 PAPDFT-----LTDLDGKPLSLADLKGKPVLVNFWATWCPPCRAEMPVLKELAEEYG--GVVFVGVD-----VDENPEAV 74

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15610011 479 AKGAANLGISYPIALDNNYATWTNYRNRYWPAEYLIDATGTVRHIKFGEGDYNVTETLVRQLLN 542
Cdd:COG0526  75 KAFLKELGLPYPVLLDPDGELAKAYGVRGIPTTVLIDKDGKIVARHVGPLSPEELEEALEKLLA 138
DsbD pfam02683
Cytochrome C biogenesis protein transmembrane region; This family consists of the ...
 122-340 4.36e-18

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: 83.61  E-value: 4.36e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610011   122 FLGGLITGISPCILPVLPVI--FFSGAQSVDAAQVAKpegavavrrkrALSATLRPYRVIGGLVLSFGMVTLLGSALLSV 199
Cdd:pfam02683   2 FLAGLLSFLSPCILPLIPAYlsYISGVSVGDRKQGKK-----------RVRVLLKSLLFVLGLSLVFVLLGLSAAFLGQL 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610011   200 LHLPQDAIRWAAlvALVAIGAGLIF---PRFEQLLEKPFSRIPQKQI-VTRSNGFGLGLALGVLYVPCAGPILAAIVVAG 275
Cdd:pfam02683  71 FGDFKGWVRIIA--GLIVILFGLHFlgvFRIPFLYKLRLVHKTKKKIsLPVLGAFLLGMTFALGWTPCIGPILASVLALA 148

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15610011   276 ATATIGLGTVVLTATFALGAALPLLFFALAGQRIAERVGAFRRRQREIRIATGSVTILLAVALVF 340
Cdd:pfam02683 149 ASTGSLLLGAGLMVVYVLGLAAPFLLASLFFGSLLLRLKWLRKNSHWVKIAGGVLLILFGVLLLL 213
PLN02919 PLN02919
haloacid dehalogenase-like hydrolase family protein
 392-528 3.49e-16

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215497 [Multi-domain]  Cd Length: 1057  Bit Score: 82.98  E-value: 3.49e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610011   392 AQLESCGTA---PDLKGITGWLNTpgnKPIDLK-SLRGKVVLIDFWAYSCINCQRAIPHVVGWYQAYKDSGLAVIGVHTP 467
Cdd:PLN02919  386 SDLESKKTAtkvPEFPPKLDWLNT---APLQFRrDLKGKVVILDFWTYCCINCMHVLPDLEFLEKKYKDQPFTVVGVHSA 462

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15610011   468 EYAFEKVPGNVAKGAANLGISYPIALDNNYATWTNYRNRYWPAEYLIDATGTVRHIKFGEG 528
Cdd:PLN02919  463 KFDNEKDLEAIRNAVLRYNISHPVVNDGDMYLWRELGVSSWPTFAVVSPNGKLIAQLSGEG 523
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 400-523 6.47e-12

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: 63.01  E-value: 6.47e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610011   400 APDLKgitgwLNTPGNKPIDLKSLRGKVVLIDFWA-YSCINCQRAIPHVVGWYQAYKDSGLAVIGVhTPEyafekVPGNV 478
Cdd:pfam00578   5 APDFE-----LPDGDGGTVSLSDYRGKWVVLFFYPaDWTPVCTTELPALADLYEEFKKLGVEVLGV-SVD-----SPESH 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 15610011   479 AKGAANLGISYPIALDNN------YATWTNYRNRYWPAEYLIDATGTVRHI 523
Cdd:pfam00578  74 KAFAEKYGLPFPLLSDPDgevaraYGVLNEEEGGALRATFVIDPDGKVRYI 124
 
Name Accession Description Interval E-value
TlpA_like_DipZ_like cd03012
TlpA-like family, DipZ-like subfamily; composed uncharacterized proteins containing a ...
 401-528 5.45e-74

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: 234.51  E-value: 5.45e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610011 401 PDLKGITGWLNTpgNKPIDLKSLRGKVVLIDFWAYSCINCQRAIPHVVGWYQAYKDSGLAVIGVHTPEYAFEKVPGNVAK 480
Cdd:cd03012   1 PEFEGILQWLNT--DKPLSLAQLRGKVVLLDFWTYCCINCLHTLPYLTDLEQKYKDDGLVVIGVHSPEFAFERDLANVKS 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 15610011 481 GAANLGISYPIALDNNYATWTNYRNRYWPAEYLIDATGTVRHIKFGEG 528
Cdd:cd03012  79 AVLRYGITYPVANDNDYATWRAYGNQYWPALYLIDPTGNVRHVHFGEG 126
Thioredoxin_10 pfam17991
Thioredoxin like C-terminal domain; This is the C-terminal thioredoxin like domain found in ...
 568-695 5.99e-41

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: 146.19  E-value: 5.99e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610011   568 TPETYFGVGKVVNYGGGGAYDEGSAV-FDYPPSLAANSFALRGRWALDYQGATSDGNDAAIKLNYHAKDVYIVVG--GTG 644
Cdd:pfam17991   1 TPETYLGYERAENFAGPGGLRPGTPAtYTAPADLPLNTWALSGTWTVGAESITAASAGARIRLRFHARDVHLVLGggGPG 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15610011   645 TLTVVRDGKPA-----------TLPISGpPTTHQVVAGYRLASETLEVR-PSKGLQVFSFTYG 695
Cdd:pfam17991  81 TVRVTLDGKAGadhgadvdadgTITVSG-PRLYQLVRQGAVRDGTLEIEfLDPGVEAYSFTFG 142
CcdA COG0785
Cytochrome c biogenesis protein CcdA [Energy production and conversion, Posttranslational ...
 115-321 5.56e-38

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


Pssm-ID: 440548 [Multi-domain]  Cd Length: 193  Bit Score: 139.59  E-value: 5.56e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610011 115 LTLALVGFLGGLITGISPCILPVLPVIFFSGAqsvdaaqvakpeGAVAVRRKRALSATLRpyrVIGGLVLSFGMVTLLGS 194
Cdd:COG0785   2 LLSLLLAFLAGLLSFLSPCVLPLLPGYLSYLT------------GLSRASRRRALLRALL---FVLGFSLVFVLLGALAS 66

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610011 195 ALLSVLHLPQDAIRWAALVALVAIGAGLIFPRFEQLLEKPFsRIPQKQIVTRSNGFGLGLALGVLYVPCAGPILAAIVVA 274
Cdd:COG0785  67 ALGSLLGQYQDLLRIVAGVLLILFGLVLLGLLKIPFLQREA-RINLRRKAGLLGAFLLGLAFGLGWTPCIGPILGAILAL 145

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 15610011 275 GATATIGLGTVVLTATFALGAALPLLFFALAGQRIAERVGAFRRRQR 321
Cdd:COG0785 146 AATSGSVLRGALLLLAYALGLGLPFLLLALFAGRLLGRLRRLRRHLR 192
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 410-526 3.57e-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: 126.20  E-value: 3.57e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610011 410 LNTPGNKPIDLKSLRGKVVLIDFWAYSCINCQRAIPHVVGWYQAYKDSGLAVIGVHTPEYafekVPGNVAKGAANLGISY 489
Cdd:cd02966   4 LPDLDGKPVSLSDLKGKVVLVNFWASWCPPCRAEMPELEALAKEYKDDGVEVVGVNVDDD----DPAAVKAFLKKYGITF 79

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 15610011 490 PIALDNNYATWTNYRNRYWPAEYLIDATGTVRHIKFG 526
Cdd:cd02966  80 PVLLDPDGELAKAYGVRGLPTTFLIDRDGRIRARHVG 116
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 399-542 3.28e-31

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 118.64  E-value: 3.28e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610011 399 TAPDLKgitgwLNTPGNKPIDLKSLRGKVVLIDFWAYSCINCQRAIPHVVGWYQAYKdsGLAVIGVHtpeyaFEKVPGNV 478
Cdd:COG0526   7 PAPDFT-----LTDLDGKPLSLADLKGKPVLVNFWATWCPPCRAEMPVLKELAEEYG--GVVFVGVD-----VDENPEAV 74

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15610011 479 AKGAANLGISYPIALDNNYATWTNYRNRYWPAEYLIDATGTVRHIKFGEGDYNVTETLVRQLLN 542
Cdd:COG0526  75 KAFLKELGLPYPVLLDPDGELAKAYGVRGIPTTVLIDKDGKIVARHVGPLSPEELEEALEKLLA 138
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
400-545 6.19e-25

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 100.71  E-value: 6.19e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610011 400 APDLKgitgwLNTPGNKPIDLKSLRGKVVLIDFWAYSCINCQRAIPHVVGWYQAYKDSGLAVIGVHTPEyafekvPGNVA 479
Cdd:COG1225   1 APDFT-----LPDLDGKTVSLSDLRGKPVVLYFYATWCPGCTAELPELRDLYEEFKDKGVEVLGVSSDS------DEAHK 69

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15610011 480 KGAANLGISYPIALDNNYATWTNYRNRYWPAEYLIDATGTVRHIKFGEGDYNVT-ETLVRQLLNDAK 545
Cdd:COG1225  70 KFAEKYGLPFPLLSDPDGEVAKAYGVRGTPTTFLIDPDGKIRYVWVGPVDPRPHlEEVLEALLAELK 136
DsbD pfam02683
Cytochrome C biogenesis protein transmembrane region; This family consists of the ...
 122-340 4.36e-18

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: 83.61  E-value: 4.36e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610011   122 FLGGLITGISPCILPVLPVI--FFSGAQSVDAAQVAKpegavavrrkrALSATLRPYRVIGGLVLSFGMVTLLGSALLSV 199
Cdd:pfam02683   2 FLAGLLSFLSPCILPLIPAYlsYISGVSVGDRKQGKK-----------RVRVLLKSLLFVLGLSLVFVLLGLSAAFLGQL 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610011   200 LHLPQDAIRWAAlvALVAIGAGLIF---PRFEQLLEKPFSRIPQKQI-VTRSNGFGLGLALGVLYVPCAGPILAAIVVAG 275
Cdd:pfam02683  71 FGDFKGWVRIIA--GLIVILFGLHFlgvFRIPFLYKLRLVHKTKKKIsLPVLGAFLLGMTFALGWTPCIGPILASVLALA 148

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15610011   276 ATATIGLGTVVLTATFALGAALPLLFFALAGQRIAERVGAFRRRQREIRIATGSVTILLAVALVF 340
Cdd:pfam02683 149 ASTGSLLLGAGLMVVYVLGLAAPFLLASLFFGSLLLRLKWLRKNSHWVKIAGGVLLILFGVLLLL 213
PLN02919 PLN02919
haloacid dehalogenase-like hydrolase family protein
 392-528 3.49e-16

haloacid dehalogenase-like hydrolase family protein


Pssm-ID: 215497 [Multi-domain]  Cd Length: 1057  Bit Score: 82.98  E-value: 3.49e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610011   392 AQLESCGTA---PDLKGITGWLNTpgnKPIDLK-SLRGKVVLIDFWAYSCINCQRAIPHVVGWYQAYKDSGLAVIGVHTP 467
Cdd:PLN02919  386 SDLESKKTAtkvPEFPPKLDWLNT---APLQFRrDLKGKVVILDFWTYCCINCMHVLPDLEFLEKKYKDQPFTVVGVHSA 462

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15610011   468 EYAFEKVPGNVAKGAANLGISYPIALDNNYATWTNYRNRYWPAEYLIDATGTVRHIKFGEG 528
Cdd:PLN02919  463 KFDNEKDLEAIRNAVLRYNISHPVVNDGDMYLWRELGVSSWPTFAVVSPNGKLIAQLSGEG 523
PRK03147 PRK03147
thiol-disulfide oxidoreductase ResA;
414-546 1.58e-13

thiol-disulfide oxidoreductase ResA;


Pssm-ID: 179545 [Multi-domain]  Cd Length: 173  Bit Score: 69.26  E-value: 1.58e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610011  414 GNKpIDLKSLRGKVVLIDFWAYSCINCQRAIPHVVGWYQAYKDSGLAVIGVHTPEyafekVPGNVAKGAANLGISYPIAL 493
Cdd:PRK03147  51 GKK-IELKDLKGKGVFLNFWGTWCKPCEKEMPYMNELYPKYKEKGVEIIAVNVDE-----TELAVKNFVNRYGLTFPVAI 124

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 15610011  494 DNNYATWTNYRNRYWPAEYLIDATGTVRHIKFGEgdynVTETLVRQLLNDAKP 546
Cdd:PRK03147 125 DKGRQVIDAYGVGPLPTTFLIDKDGKVVKVITGE----MTEEQLEEYLEKIKP 173
DsbD COG4232
Thiol:disulfide interchange protein DsbD [Posttranslational modification, protein turnover, ...
 119-441 5.84e-12

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


Pssm-ID: 443376 [Multi-domain]  Cd Length: 416  Bit Score: 68.29  E-value: 5.84e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610011 119 LVGFLGGLITGISPCILPVLP--VIFFSGAQSVDAAQVakpegavavrRKRALSATLrpyrvigGLVLSFgmvTLLGSAL 196
Cdd:COG4232   7 LLAFLGGLLLNLTPCVLPMLPikSSIIVGQGGKSRRRA----------FLLSLAYVL-------GMALTY---TLLGLLA 66

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610011 197 LSVLhlpqDAIRW----------AALVAL-VAIGAGLiFPRFE-QLlekpFSRIPQKqIVTRSNG------FGLGLALGV 258
Cdd:COG4232  67 ALLG----GAVGWgfqlqspwvlGALALLfVLLALSM-FGLFElQL----PSSLQNR-LAALSNGggllgaFFMGVLAAL 136

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610011 259 LYVPCAGPILA-AIVVAGATATIGLGTVVLTAtFALGAALPLLFFALAGQRIA------------ERVGAF--------- 316
Cdd:COG4232 137 VATPCTAPFLGgALGYALQTGDALLGLLALFA-LGLGMALPLLLLGLFPGLLKllpkpgawmetvKQVFGFlllataiwl 215

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610011 317 -RR--RQREIRIATGSVTILLAVALVFDLPAALQRAIPDYTASLQQQISTGTEIReqlnLGGIVNAqnAQLSNCSDGAAQ 393
Cdd:COG4232 216 lSVllPQAGLDAVALLLWALLLLALALWLLGALRLPHDSSGRRLSVRKGLGLLLL----LAGLALL--LGALSGADPLQP 289

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*...
gi 15610011 394 LESCGTAPDLKGITGWLNTPGNKPIDLKSlRGKVVLIDFWAYSCINCQ 441
Cdd:COG4232 290 LAAGAAAAAAAAGLAWQADLEAALAEARA-EGKPVFVDFTADWCVTCK 336
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 400-523 6.47e-12

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: 63.01  E-value: 6.47e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610011   400 APDLKgitgwLNTPGNKPIDLKSLRGKVVLIDFWA-YSCINCQRAIPHVVGWYQAYKDSGLAVIGVhTPEyafekVPGNV 478
Cdd:pfam00578   5 APDFE-----LPDGDGGTVSLSDYRGKWVVLFFYPaDWTPVCTTELPALADLYEEFKKLGVEVLGV-SVD-----SPESH 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 15610011   479 AKGAANLGISYPIALDNN------YATWTNYRNRYWPAEYLIDATGTVRHI 523
Cdd:pfam00578  74 KAFAEKYGLPFPLLSDPDgevaraYGVLNEEEGGALRATFVIDPDGKVRYI 124
TauE COG0730
Sulfite exporter TauE/SafE/YfcA and related permeases, UPF0721 family [Inorganic ion transport ...
 111-342 2.79e-07

Sulfite exporter TauE/SafE/YfcA and related permeases, UPF0721 family [Inorganic ion transport and metabolism];


Pssm-ID: 440494  Cd Length: 250  Bit Score: 52.12  E-value: 2.79e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610011 111 ITDVLTLALVGFLGGLI---TGISPCILpVLPVIFFSGAQSVDAAQVAKPEGAVAvrrkrALSATLRPYR---VIGGLVL 184
Cdd:COG0730   1 LMLLLLLLLAGFLAGFLdglLGVGGGLI-TVPALLLFGLPPAVAVGTSLLAVVFT-----SLSGALAHRRrgnVDWRLLL 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610011 185 SFGMVTLLGSAL--LSVLHLPQDAIRWAALVALVAIGAGLIFPRfeQLLEKPFSRIPQKQIVTrsnGFGLGLALGV---- 258
Cdd:COG0730  75 PLALGALIGALLgaLLLLLLPADVLKLLFGVLLLLVALLMLLRP--KPGAEPERRLPRRSPLL---LLLLGFVIGFlsgl 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610011 259 -------LYVP-----CAGPILAAI----VVAGATATIGLGTVVLTATFALGAALPLLFFALAGQRIAERVGAfRRRQRE 322
Cdd:COG0730 150 fgigggfLLVPalvllLGLPLKRAVatslALIFVTALAGLIGFALLGYVDWPLALLLALGSLLGAYLGARLAR-RLPPKL 228

                       250       260
                ....*....|....*....|
gi 15610011 323 IRIATGSVTILLAVALVFDL 342
Cdd:COG0730 229 LRRLFAVVLLLVGLKLLLKA 248
Redoxin pfam08534
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
 399-527 1.59e-06

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


Pssm-ID: 400717 [Multi-domain]  Cd Length: 148  Bit Score: 48.13  E-value: 1.59e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610011   399 TAPDLKGITgwLNTPGNkPIDLKSLRGKVVLIDFWA-YSCINCQRAIPHVVGWYQAYKDSGLAVIGVHTPEYAFekvpgN 477
Cdd:pfam08534   5 KAPDFTLPD--AATDGN-TVSLSDFKGKKVVLNFWPgAFCPTCSAEHPYLEKLNELYKEKGVDVVAVNSDNDAF-----F 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 15610011   478 VAKGAANLGISYPIALDNNYATWTNY--------RNRYWPAEY-LIDATGTVRHIKFGE 527
Cdd:pfam08534  77 VKRFWGKEGLPFPFLSDGNAAFTKALglpieedaSAGLRSPRYaVIDEDGKVVYLFVGP 135
Gdt1 COG2119
Putative Ca2+/H+ antiporter, TMEM165/GDT1 family [General function prediction only];
168-342 2.86e-05

Putative Ca2+/H+ antiporter, TMEM165/GDT1 family [General function prediction only];


Pssm-ID: 441722 [Multi-domain]  Cd Length: 192  Bit Score: 45.58  E-value: 2.86e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610011 168 ALSATLRPYRVIGGLVLSFGMVTLLGSALLSVL--HLPQDAIRWAALVALVAIGAGLIFPRFEQLLEKPfsripqKQIVT 245
Cdd:COG2119  27 ALATRYRPWPVLAGILAATLLNHALAVALGSWLasLLPPDYLRWVAALLFLAFGLWLLRPDKLDEEEAK------AAEKS 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610011 246 RSNGFglglalgvlyvpcaGPILAAIVVA--G-AT--ATIGLGT-------VVLTATFALGAA--LPLLFFALAGQRIAE 311
Cdd:COG2119 101 RFGPF--------------LTTFVAFFLAemGdKTqlATIALAArygaplaVWLGTTLGMMLAsaLAVLLGRKLAKRIPL 166

                       170       180       190
                ....*....|....*....|....*....|.
gi 15610011 312 RVgafrrrqreIRIATGSVTILLAVALVFDL 342
Cdd:COG2119 167 RL---------IHRIAAALFLLFGLVTLLEA 188
TauE pfam01925
Sulfite exporter TauE/SafE; This is a family of integral membrane proteins where the alignment ...
 118-336 6.45e-05

Sulfite exporter TauE/SafE; This is a family of integral membrane proteins where the alignment appears to contain two duplicated modules of three transmembrane helices. The proteins are involved in the transport of anions across the cytoplasmic membrane during taurine metabolism as an exporter of sulfoacetate. This family used to be known as DUF81.


Pssm-ID: 460386  Cd Length: 235  Bit Score: 44.88  E-value: 6.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610011   118 ALVGFLGGLITGISPC-----ILPVLpVIFFSGAQSVDAAQVAkpegAVAVrrkrALSATLRPYR---VIGGLVLSFGMV 189
Cdd:pfam01925   1 LLAGLLAGFVGGLLGFgggliAVPLL-LLLLPPAVAVGTSLLA----AVAT----SLSGALAHRRrgaVDWRLLLRLLLG 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610011   190 TLLGSAL--LSVLHLPQDAIRWAALVALVAIGAGLIFPRFEQLLEKPFSRIPQKQIVTRSNGFG------LGLALGVLYV 261
Cdd:pfam01925  72 GLIGALLgaLLLLLLPEALLKLLFGVLLLLAALLMLLRRRLGAAPRARRRRPGPLALALLGGLIgflsglFGIGGGFLLV 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610011   262 P-----CAGPILAAI----VVAGATATIGLGTVVLTATFALGAALPLLFFALAGQRIAERVGAfRRRQREIRIATGSVTI 332
Cdd:pfam01925 152 PallylLGLPLKKAVgtslLLFLVSNLAALLGYALLGAVDWPLLLLLLLGALLGAYLGARLAR-RLPPRLLRRLFAVLLL 230


                  ....
gi 15610011   333 LLAV 336
Cdd:pfam01925 231 LVGL 234
Thioredoxin_8 pfam13905
Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the ...
 425-520 7.03e-05

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: 42.29  E-value: 7.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610011   425 GKVVLIDFWAYSCINCQRAIPHVVGWYQAYKDS-GLAVIGVH--TPEYAFEkvpgNVAKGAANLGISYPIALDNNYATWT 501
Cdd:pfam13905   1 GKVVLLYFGASWCKPCRRFTPLLKELYEKLKKKkNVEIVFVSldRDLEEFK----DYLKKMPKDWLSVPFDDDERNELKR 76

                          90
                  ....*....|....*....
gi 15610011   502 NYRNRYWPAEYLIDATGTV 520
Cdd:pfam13905  77 KYGVNAIPTLVLLDPNGEV 95
RhtB COG1280
Threonine/homoserine/homoserine lactone efflux protein [Amino acid transport and metabolism];
165-341 2.25e-04

Threonine/homoserine/homoserine lactone efflux protein [Amino acid transport and metabolism];


Pssm-ID: 440891  Cd Length: 205  Bit Score: 42.90  E-value: 2.25e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610011 165 RKRALSATLrpyrvigGLVLSFGMVTLLG----SALLSVLHLPQDAIRWAALVALVAIGAGLIFPRFEQLlekpfsRIPQ 240
Cdd:COG1280  36 RRAGLAAAL-------GIALGDLVHILLAalglAALLAASPLLFTVLKLAGAAYLLYLGWKLLRSAGRPL------AAEA 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610011 241 KQIVTRSNGFGLGLALGVLYvPCAGPILAAIV--VAGATATIGLGTVVLTATFALGAALPLLFFALAGQRIAERVgAFRR 318
Cdd:COG1280 103 AAAASARRLFRQGFLLNLLN-PKAILFFLAFLpqFVDPGAPLLLQLLLLGATFLLVSLLWLLLYALLASRLRRRL-RSPR 180

                       170       180
                ....*....|....*....|...
gi 15610011 319 RQREIRIATGSVTILLAVALVFD 341
Cdd:COG1280 181 ALRWLNRVAGLLLIGFGLRLALS 203
PRX_like1 cd02969
Peroxiredoxin (PRX)-like 1 family; hypothetical proteins that show sequence similarity to PRXs. ...
 400-521 5.98e-04

Peroxiredoxin (PRX)-like 1 family; hypothetical proteins that show sequence similarity to PRXs. Members of this group contain a conserved cysteine that aligns to the first cysteine in the CXXC motif of TRX. This does not correspond to the peroxidatic cysteine found in PRXs, which aligns to the second cysteine in the CXXC motif of TRX. In addition, these proteins do not contain the other two conserved residues of the catalytic triad of PRX. PRXs confer a protective antioxidant role in cells through their peroxidase activity in which hydrogen peroxide, peroxynitrate, and organic hydroperoxides are reduced and detoxified using reducing equivalents derived from either thioredoxin, glutathione, trypanothione and AhpF.


Pssm-ID: 239267 [Multi-domain]  Cd Length: 171  Bit Score: 41.07  E-value: 5.98e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610011 400 APD--LKGITGwlntpgnKPIDLKSLR-GKVVLIDFWAYSCINCQRAIPHVVGWYQAYKDSGLAVIGVH------TPEYA 470
Cdd:cd02969   4 APDfsLPDTDG-------KTYSLADFAdGKALVVMFICNHCPYVKAIEDRLNRLAKEYGAKGVAVVAINsndieaYPEDS 76

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 15610011 471 FEkvpgNVAKGAANLGISYPIALDNNYATWTNYRNRYWPAEYLIDATGTVR 521
Cdd:cd02969  77 PE----NMKAKAKEHGYPFPYLLDETQEVAKAYGAACTPDFFLFDPDGKLV 123
TgpA_N pfam11992
TgpA N-terminal domain; This domain can be found at the N terminus of TgpA from Pseudomonas ...
 189-376 6.99e-03

TgpA N-terminal domain; This domain can be found at the N terminus of TgpA from Pseudomonas aeruginosa. TgpA is a transglutaminase that plays a critical role in the viability of Pseudomonas aeruginosa. This domain is composed of 5 transmembrane helices.


Pssm-ID: 463423  Cd Length: 336  Bit Score: 39.34  E-value: 6.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610011   189 VTLLGSALLSVLHLPQDAIRWAALVALVAIGAGLIFPRfeqLLEKPFSRIPQKQIVTrsNGFGLGLALGVLYVPCA---G 265
Cdd:pfam11992   1 LLLLAAALALLPLLSGLPWWVPALLLVALVLAVGALLR---RLRLPRWRLPPALLLA--GLLVLALLLTLFLAGTAllgL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15610011   266 PILAAIVVAGATATIGLGTVVLTATFALGAALPLLFF-------------------------ALAGQRIAERVGAFRRRQ 320
Cdd:pfam11992  76 SLGLLAAVALLLLALLLKLLEVRLRRDALAGLLLLLFllvpaallsqslglllflllalaflLLLLVDLRDRSRTPPGRR 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 15610011   321 REIRIATGSVTILLAVALVFDLPAALQRAIPDYTASLQQQISTGTEIREQLNLGGI 376
Cdd:pfam11992 156 LRGLLRTAARLGLVALPLALVLFLLLPRLPPPLWGLGPGGGGATTGLSPTLSLGDI 211
 
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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