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Conserved domains on  [gi|1958789846|ref|XP_038935239|]
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thymidine phosphorylase isoform X5 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SCO cd02968
SCO (an acronym for Synthesis of Cytochrome c Oxidase) family; composed of proteins similar to ...
 341-482 8.89e-64

SCO (an acronym for Synthesis of Cytochrome c Oxidase) family; composed of proteins similar to Sco1, a membrane-anchored protein possessing a soluble domain with a TRX fold. Members of this family are required for the proper assembly of cytochrome c oxidase (COX). They contain a metal binding motif, typically CXXXC, which is located in a flexible loop. COX, the terminal enzyme in the respiratory chain, is imbedded in the inner mitochondrial membrane of all eukaryotes and in the plasma membrane of some prokaryotes. It is composed of two subunits, COX I and COX II. It has been proposed that Sco1 specifically delivers copper to the CuA site, a dinuclear copper center, of the COX II subunit. Mutations in human Sco1 and Sco2 cause fatal infantile hepatoencephalomyopathy and cardioencephalomyopathy, respectively. Both disorders are associated with severe COX deficiency in affected tissues. More recently, it has been argued that the redox sensitivity of the copper binding properties of Sco1 implies that it participates in signaling events rather than functioning as a chaperone that transfers copper to COX II.


:

Pssm-ID: 239266  Cd Length: 142  Bit Score: 203.99  E-value: 8.89e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789846 341 QGDFSLLDHKGQPRCKADFRGQWVLMYFGFTHCPDICPDELEKLVQVVQKLEAEPeLPLVQPVFVTVDPERDDVAAMARY 420
Cdd:cd02968     2 GPDFTLTDQDGRPVTLSDLKGKPVLVYFGYTHCPDVCPTTLANLAQALKQLGADG-GDDVQVVFISVDPERDTPEVLKAY 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958789846 421 VQEFHPRLLGLTGSTEQVAHASRNYRVYYSAGPKDeDQDYIVDHSIAIYLLNPDGLFTDYYG 482
Cdd:cd02968    81 AKAFGPGWIGLTGTPEEIEALAKAFGVYYEKVPED-DGDYLVDHSAAIYLVDPDGKLVRYYG 141
DeoA super family cl43065
Thymidine phosphorylase [Nucleotide transport and metabolism]; Thymidine phosphorylase is part ...
 2-129 5.97e-32

Thymidine phosphorylase [Nucleotide transport and metabolism]; Thymidine phosphorylase is part of the Pathway/BioSystem: Pyrimidine salvage


The actual alignment was detected with superfamily member COG0213:

Pssm-ID: 439983 [Multi-domain]  Cd Length: 431  Bit Score: 127.08  E-value: 5.97e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789846   2 GLGLQVAAALTAMDNPLGRNVGHTLEVEEALLCLDGAGPPDLRDLVIRLaGGAILWLSGQAETQDQGAARVAAALDDGSA 81
Cdd:COG0213   225 GAGRKTVALITDMNQPLGRAVGNALEVKEAIETLKGEGPEDLTELTLAL-GAEMLVLAGLAKDLEEARAKLEEALASGKA 303

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1958789846  82 LHRFQLMLSAQGVDPGLAralcsgsptQRRQLLPHARKQEELLSPADG 129
Cdd:COG0213   304 LEKFKEMVAAQGGDPDVV---------DDPELLPQAPVVREVKAPRSG 342
 
Name Accession Description Interval E-value
SCO cd02968
SCO (an acronym for Synthesis of Cytochrome c Oxidase) family; composed of proteins similar to ...
 341-482 8.89e-64

SCO (an acronym for Synthesis of Cytochrome c Oxidase) family; composed of proteins similar to Sco1, a membrane-anchored protein possessing a soluble domain with a TRX fold. Members of this family are required for the proper assembly of cytochrome c oxidase (COX). They contain a metal binding motif, typically CXXXC, which is located in a flexible loop. COX, the terminal enzyme in the respiratory chain, is imbedded in the inner mitochondrial membrane of all eukaryotes and in the plasma membrane of some prokaryotes. It is composed of two subunits, COX I and COX II. It has been proposed that Sco1 specifically delivers copper to the CuA site, a dinuclear copper center, of the COX II subunit. Mutations in human Sco1 and Sco2 cause fatal infantile hepatoencephalomyopathy and cardioencephalomyopathy, respectively. Both disorders are associated with severe COX deficiency in affected tissues. More recently, it has been argued that the redox sensitivity of the copper binding properties of Sco1 implies that it participates in signaling events rather than functioning as a chaperone that transfers copper to COX II.


Pssm-ID: 239266  Cd Length: 142  Bit Score: 203.99  E-value: 8.89e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789846 341 QGDFSLLDHKGQPRCKADFRGQWVLMYFGFTHCPDICPDELEKLVQVVQKLEAEPeLPLVQPVFVTVDPERDDVAAMARY 420
Cdd:cd02968     2 GPDFTLTDQDGRPVTLSDLKGKPVLVYFGYTHCPDVCPTTLANLAQALKQLGADG-GDDVQVVFISVDPERDTPEVLKAY 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958789846 421 VQEFHPRLLGLTGSTEQVAHASRNYRVYYSAGPKDeDQDYIVDHSIAIYLLNPDGLFTDYYG 482
Cdd:cd02968    81 AKAFGPGWIGLTGTPEEIEALAKAFGVYYEKVPED-DGDYLVDHSAAIYLVDPDGKLVRYYG 141
SCO1-SenC pfam02630
SCO1/SenC; This family is involved in biogenesis of respiratory and photosynthetic systems. ...
 342-477 4.60e-60

SCO1/SenC; This family is involved in biogenesis of respiratory and photosynthetic systems. SCO1 is required for a post-translational step in the accumulation of subunits COXI and COXII of cytochrome c oxidase. SenC is required for optimal cytochrome c oxidase activity and maximal induction of genes encoding the light-harvesting and reaction centre complexes of R. capsulatus.


Pssm-ID: 460630  Cd Length: 134  Bit Score: 193.94  E-value: 4.60e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789846 342 GDFSLLDHKGQPRCKADFRGQWVLMYFGFTHCPDICPDELEKLVQVVQKLEAEPELplVQPVFVTVDPERDDVAAMARYV 421
Cdd:pfam02630   2 GPFELVDQDGKAVTEADFEGRPSLVFFGFTHCPDVCPTTLPNMAQVLDALGEEGID--VQPVFITVDPERDTPEVLAEYL 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958789846 422 QEFHPRLLGLTGSTEQVAHASRNYRVYYSAGPkDEDQDYIVDHSIAIYLLNPDGLF 477
Cdd:pfam02630  80 EAFGPRIIGLTGSPEQIAAAARAFRVYYEKVP-DDGGDYTVDHTASVYLVDPDGRF 134
Sco1 COG1999
Cytochrome oxidase Cu insertion factor, SCO1/SenC/PrrC family [Posttranslational modification, ...
 345-500 9.42e-55

Cytochrome oxidase Cu insertion factor, SCO1/SenC/PrrC family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441602  Cd Length: 156  Bit Score: 180.87  E-value: 9.42e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789846 345 SLLDHKGQPRCKADFRGQWVLMYFGFTHCPDICPDELEKLVQVVQKLEAEPELPlVQPVFVTVDPERDDVAAMARYVQEF 424
Cdd:COG1999     4 TLTDQDGKPVTLADLRGKPVLVFFGYTSCPDVCPTTLANLAQVQEALGEDGGDD-VQVLFISVDPERDTPEVLKAYAEAF 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958789846 425 H-PRLLGLTGSTEQVAHASRNYRVYYSagpKDEDQDYIVDHSIAIYLLNPDGLFTDYYGRSRSAEQIVESVRRHIAA 500
Cdd:COG1999    83 GaPRWIGLTGDPEEIAALAKAFGVYYE---KVPDGDYTFDHSAAVYLVDPDGRLRGYYPAGEDPEELAADLKALLEE 156
DeoA COG0213
Thymidine phosphorylase [Nucleotide transport and metabolism]; Thymidine phosphorylase is part ...
 2-129 5.97e-32

Thymidine phosphorylase [Nucleotide transport and metabolism]; Thymidine phosphorylase is part of the Pathway/BioSystem: Pyrimidine salvage


Pssm-ID: 439983 [Multi-domain]  Cd Length: 431  Bit Score: 127.08  E-value: 5.97e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789846   2 GLGLQVAAALTAMDNPLGRNVGHTLEVEEALLCLDGAGPPDLRDLVIRLaGGAILWLSGQAETQDQGAARVAAALDDGSA 81
Cdd:COG0213   225 GAGRKTVALITDMNQPLGRAVGNALEVKEAIETLKGEGPEDLTELTLAL-GAEMLVLAGLAKDLEEARAKLEEALASGKA 303

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1958789846  82 LHRFQLMLSAQGVDPGLAralcsgsptQRRQLLPHARKQEELLSPADG 129
Cdd:COG0213   304 LEKFKEMVAAQGGDPDVV---------DDPELLPQAPVVREVKAPRSG 342
deoA PRK05820
thymidine phosphorylase; Reviewed
 2-129 2.31e-20

thymidine phosphorylase; Reviewed


Pssm-ID: 180276 [Multi-domain]  Cd Length: 440  Bit Score: 93.35  E-value: 2.31e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789846   2 GLGLQVAAALTAMDNPLGRNVGHTLEVEEALLCLDGA-GPPDLRDLVIRLAGgAILWLSGQAETQDQGAARVAAALDDGS 80
Cdd:PRK05820  230 GAGVRTTALLTDMNQPLASSAGNALEVREAVEFLTGGyRPPRLVEVTMALAA-EMLVLAGLAKDEAEARADLAAVLDSGK 308

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1958789846  81 ALHRFQLMLSAQGVDPGLaralcsgsPTQRRQLLPHARKQEELLSPADG 129
Cdd:PRK05820  309 AAERFGRMVAAQGGPPDF--------VENYDKYLPTAPHTKPVYADRSG 349
Glycos_transf_3 pfam00591
Glycosyl transferase family, a/b domain; This family includes anthranilate ...
 4-82 5.21e-13

Glycosyl transferase family, a/b domain; This family includes anthranilate phosphoribosyltransferase (TrpD), thymidine phosphorylase. All these proteins can transfer a phosphorylated ribose substrate.


Pssm-ID: 459860 [Multi-domain]  Cd Length: 253  Bit Score: 68.85  E-value: 5.21e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789846   4 GLQVAAALTAMDNPLGRNVGHTLEV---EEALLCLDGA--GPPDL--RDLVIRLAGGAiLWLSGQAETQDQGAARVAAAL 76
Cdd:pfam00591 169 GEITEYTLTPEDFGLGRATLEALEGgspKENADILKGVlgGKGSAahRDLVALNAGAA-LYLAGKADSLKEGVAKALEVI 247


                  ....*.
gi 1958789846  77 DDGSAL 82
Cdd:pfam00591 248 DSGKAL 253
 
Name Accession Description Interval E-value
SCO cd02968
SCO (an acronym for Synthesis of Cytochrome c Oxidase) family; composed of proteins similar to ...
 341-482 8.89e-64

SCO (an acronym for Synthesis of Cytochrome c Oxidase) family; composed of proteins similar to Sco1, a membrane-anchored protein possessing a soluble domain with a TRX fold. Members of this family are required for the proper assembly of cytochrome c oxidase (COX). They contain a metal binding motif, typically CXXXC, which is located in a flexible loop. COX, the terminal enzyme in the respiratory chain, is imbedded in the inner mitochondrial membrane of all eukaryotes and in the plasma membrane of some prokaryotes. It is composed of two subunits, COX I and COX II. It has been proposed that Sco1 specifically delivers copper to the CuA site, a dinuclear copper center, of the COX II subunit. Mutations in human Sco1 and Sco2 cause fatal infantile hepatoencephalomyopathy and cardioencephalomyopathy, respectively. Both disorders are associated with severe COX deficiency in affected tissues. More recently, it has been argued that the redox sensitivity of the copper binding properties of Sco1 implies that it participates in signaling events rather than functioning as a chaperone that transfers copper to COX II.


Pssm-ID: 239266  Cd Length: 142  Bit Score: 203.99  E-value: 8.89e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789846 341 QGDFSLLDHKGQPRCKADFRGQWVLMYFGFTHCPDICPDELEKLVQVVQKLEAEPeLPLVQPVFVTVDPERDDVAAMARY 420
Cdd:cd02968     2 GPDFTLTDQDGRPVTLSDLKGKPVLVYFGYTHCPDVCPTTLANLAQALKQLGADG-GDDVQVVFISVDPERDTPEVLKAY 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958789846 421 VQEFHPRLLGLTGSTEQVAHASRNYRVYYSAGPKDeDQDYIVDHSIAIYLLNPDGLFTDYYG 482
Cdd:cd02968    81 AKAFGPGWIGLTGTPEEIEALAKAFGVYYEKVPED-DGDYLVDHSAAIYLVDPDGKLVRYYG 141
SCO1-SenC pfam02630
SCO1/SenC; This family is involved in biogenesis of respiratory and photosynthetic systems. ...
 342-477 4.60e-60

SCO1/SenC; This family is involved in biogenesis of respiratory and photosynthetic systems. SCO1 is required for a post-translational step in the accumulation of subunits COXI and COXII of cytochrome c oxidase. SenC is required for optimal cytochrome c oxidase activity and maximal induction of genes encoding the light-harvesting and reaction centre complexes of R. capsulatus.


Pssm-ID: 460630  Cd Length: 134  Bit Score: 193.94  E-value: 4.60e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789846 342 GDFSLLDHKGQPRCKADFRGQWVLMYFGFTHCPDICPDELEKLVQVVQKLEAEPELplVQPVFVTVDPERDDVAAMARYV 421
Cdd:pfam02630   2 GPFELVDQDGKAVTEADFEGRPSLVFFGFTHCPDVCPTTLPNMAQVLDALGEEGID--VQPVFITVDPERDTPEVLAEYL 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958789846 422 QEFHPRLLGLTGSTEQVAHASRNYRVYYSAGPkDEDQDYIVDHSIAIYLLNPDGLF 477
Cdd:pfam02630  80 EAFGPRIIGLTGSPEQIAAAARAFRVYYEKVP-DDGGDYTVDHTASVYLVDPDGRF 134
Sco1 COG1999
Cytochrome oxidase Cu insertion factor, SCO1/SenC/PrrC family [Posttranslational modification, ...
 345-500 9.42e-55

Cytochrome oxidase Cu insertion factor, SCO1/SenC/PrrC family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441602  Cd Length: 156  Bit Score: 180.87  E-value: 9.42e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789846 345 SLLDHKGQPRCKADFRGQWVLMYFGFTHCPDICPDELEKLVQVVQKLEAEPELPlVQPVFVTVDPERDDVAAMARYVQEF 424
Cdd:COG1999     4 TLTDQDGKPVTLADLRGKPVLVFFGYTSCPDVCPTTLANLAQVQEALGEDGGDD-VQVLFISVDPERDTPEVLKAYAEAF 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958789846 425 H-PRLLGLTGSTEQVAHASRNYRVYYSagpKDEDQDYIVDHSIAIYLLNPDGLFTDYYGRSRSAEQIVESVRRHIAA 500
Cdd:COG1999    83 GaPRWIGLTGDPEEIAALAKAFGVYYE---KVPDGDYTFDHSAAVYLVDPDGRLRGYYPAGEDPEELAADLKALLEE 156
DeoA COG0213
Thymidine phosphorylase [Nucleotide transport and metabolism]; Thymidine phosphorylase is part ...
 2-129 5.97e-32

Thymidine phosphorylase [Nucleotide transport and metabolism]; Thymidine phosphorylase is part of the Pathway/BioSystem: Pyrimidine salvage


Pssm-ID: 439983 [Multi-domain]  Cd Length: 431  Bit Score: 127.08  E-value: 5.97e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789846   2 GLGLQVAAALTAMDNPLGRNVGHTLEVEEALLCLDGAGPPDLRDLVIRLaGGAILWLSGQAETQDQGAARVAAALDDGSA 81
Cdd:COG0213   225 GAGRKTVALITDMNQPLGRAVGNALEVKEAIETLKGEGPEDLTELTLAL-GAEMLVLAGLAKDLEEARAKLEEALASGKA 303

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1958789846  82 LHRFQLMLSAQGVDPGLAralcsgsptQRRQLLPHARKQEELLSPADG 129
Cdd:COG0213   304 LEKFKEMVAAQGGDPDVV---------DDPELLPQAPVVREVKAPRSG 342
deoA PRK05820
thymidine phosphorylase; Reviewed
 2-129 2.31e-20

thymidine phosphorylase; Reviewed


Pssm-ID: 180276 [Multi-domain]  Cd Length: 440  Bit Score: 93.35  E-value: 2.31e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789846   2 GLGLQVAAALTAMDNPLGRNVGHTLEVEEALLCLDGA-GPPDLRDLVIRLAGgAILWLSGQAETQDQGAARVAAALDDGS 80
Cdd:PRK05820  230 GAGVRTTALLTDMNQPLASSAGNALEVREAVEFLTGGyRPPRLVEVTMALAA-EMLVLAGLAKDEAEARADLAAVLDSGK 308

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1958789846  81 ALHRFQLMLSAQGVDPGLaralcsgsPTQRRQLLPHARKQEELLSPADG 129
Cdd:PRK05820  309 AAERFGRMVAAQGGPPDF--------VENYDKYLPTAPHTKPVYADRSG 349
PRK06078 PRK06078
pyrimidine-nucleoside phosphorylase; Reviewed
 4-129 2.53e-17

pyrimidine-nucleoside phosphorylase; Reviewed


Pssm-ID: 180387 [Multi-domain]  Cd Length: 434  Bit Score: 83.98  E-value: 2.53e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789846   4 GLQVAAALTAMDNPLGRNVGHTLEVEEALLCLDGAGPPDLRDLVIRLaGGAILWLSGQAETQDQGAARVAAALDDGSALH 83
Cdd:PRK06078  229 GRNTMAVISDMSQPLGRAIGNALEVLEAIDTLQGKGPKDLTELVLTL-GSQMVVLAGKAKTLEEAREHLIEVMNNGKALE 307

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1958789846  84 RFQLMLSAQGVDPGLARALcsgsptqrrQLLPHARKQEELLSPADG 129
Cdd:PRK06078  308 KFKEFLSAQGGDASVVDDP---------EKLPQAKYQIEVPAKESG 344
PRK04350 PRK04350
thymidine phosphorylase; Provisional
 2-129 1.21e-14

thymidine phosphorylase; Provisional


Pssm-ID: 235289 [Multi-domain]  Cd Length: 490  Bit Score: 76.00  E-value: 1.21e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789846   2 GLGLQVAAALTAMDNPLGRNVGHTLEVEEALLCL--DGAGPPDLRDLVIRLAgGAILWLSGQAETqDQGAARVAAALDDG 79
Cdd:PRK04350  302 RLGLRVECAITDGSQPIGRGIGPALEARDVLAVLenDPDAPNDLREKSLRLA-GILLEMGGVAPG-GEGYALAREILESG 379

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958789846  80 SALHRFQLMLSAQGVDPglaralcsgsptqRRqlLPHARKQEELLSPADG 129
Cdd:PRK04350  380 KALEKFQEIIEAQGGDS-------------ED--IPLGDHTHDVTAPRDG 414
Glycos_transf_3 pfam00591
Glycosyl transferase family, a/b domain; This family includes anthranilate ...
 4-82 5.21e-13

Glycosyl transferase family, a/b domain; This family includes anthranilate phosphoribosyltransferase (TrpD), thymidine phosphorylase. All these proteins can transfer a phosphorylated ribose substrate.


Pssm-ID: 459860 [Multi-domain]  Cd Length: 253  Bit Score: 68.85  E-value: 5.21e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789846   4 GLQVAAALTAMDNPLGRNVGHTLEV---EEALLCLDGA--GPPDL--RDLVIRLAGGAiLWLSGQAETQDQGAARVAAAL 76
Cdd:pfam00591 169 GEITEYTLTPEDFGLGRATLEALEGgspKENADILKGVlgGKGSAahRDLVALNAGAA-LYLAGKADSLKEGVAKALEVI 247


                  ....*.
gi 1958789846  77 DDGSAL 82
Cdd:pfam00591 248 DSGKAL 253
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
343-494 7.84e-10

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 56.80  E-value: 7.84e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789846 343 DFSLLDHKGQPRCKADFRGQWVLMYFGFTHCPdICPDELEKLVQVVQKLEAEPelplVQPVFVTVdperDDVAAMARYVQ 422
Cdd:COG1225     3 DFTLPDLDGKTVSLSDLRGKPVVLYFYATWCP-GCTAELPELRDLYEEFKDKG----VEVLGVSS----DSDEAHKKFAE 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958789846 423 EFH---PRLLGLTGSTeqvahaSRNYRVYysAGPkdedqdyivdhsiAIYLLNPDG----LFTDYYGRSRSAEQIVESV 494
Cdd:COG1225    74 KYGlpfPLLSDPDGEV------AKAYGVR--GTP-------------TTFLIDPDGkiryVWVGPVDPRPHLEEVLEAL 131
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 343-500 8.72e-09

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


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 53.93  E-value: 8.72e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789846 343 DFSLLDHKGQPRCKADFRGQWVLMYFGFTHCPDiCPDELEKLVQVVQkleaepELPLVQPVFVTVDPERDDVAAMARYVQ 422
Cdd:COG0526    10 DFTLTDLDGKPLSLADLKGKPVLVNFWATWCPP-CRAEMPVLKELAE------EYGGVVFVGVDVDENPEAVKAFLKELG 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958789846 423 EFHPRLLGLTGSteqvahASRNYRVYysagpkdedqdyivdhSI-AIYLLNPDGLFTDYYGRSRSAEQIVESVRRHIAA 500
Cdd:COG0526    83 LPYPVLLDPDGE------LAKAYGVR----------------GIpTTVLIDKDGKIVARHVGPLSPEELEEALEKLLAK 139
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 343-463 4.85e-06

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: 45.68  E-value: 4.85e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789846 343 DFSLLDHKGQPRCKADFRGQW-VLMYFGFTHCPdICPDELEKLVQVVQKLEAEPelplVQPVFVTVDPERDDVAAMARYV 421
Cdd:pfam00578   7 DFELPDGDGGTVSLSDYRGKWvVLFFYPADWTP-VCTTELPALADLYEEFKKLG----VEVLGVSVDSPESHKAFAEKYG 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1958789846 422 QEFhPRLLGLTGsteqvaHASRNYRVYYSAGPKDEDQDYIVD 463
Cdd:pfam00578  82 LPF-PLLSDPDG------EVARAYGVLNEEEGGALRATFVID 116
TrpD COG0547
Anthranilate phosphoribosyltransferase, glycosyltransferase domain [Amino acid transport and ...
 35-82 4.03e-05

Anthranilate phosphoribosyltransferase, glycosyltransferase domain [Amino acid transport and metabolism]; Anthranilate phosphoribosyltransferase, glycosyltransferase domain is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis


Pssm-ID: 440313 [Multi-domain]  Cd Length: 327  Bit Score: 45.45  E-value: 4.03e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1958789846  35 LDGAGPPdLRDLVIrLAGGAILWLSGQAETQDQGAARVAAALDDGSAL 82
Cdd:COG0547   279 LAGEGGP-ARDAVL-LNAAAALYVAGKADSLAEGVELAREAIDSGAAL 324
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 343-449 1.88e-04

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: 41.07  E-value: 1.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958789846 343 DFSLLDHKGQPRCKADFRGQWVLMYFGFTHCPdICPDELEKLVQVVQKLEAEpelplvQPVFVTVDPERDDVAAMARYVQ 422
Cdd:cd02966     1 DFSLPDLDGKPVSLSDLKGKVVLVNFWASWCP-PCRAEMPELEALAKEYKDD------GVEVVGVNVDDDDPAAVKAFLK 73

                          90       100
                  ....*....|....*....|....*..
gi 1958789846 423 EFHPRLLGLTGSTEQVAhasRNYRVYY 449
Cdd:cd02966    74 KYGITFPVLLDPDGELA---KAYGVRG 97
PRK14607 PRK14607
bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;
35-82 7.52e-04

bifunctional anthranilate synthase component II/anthranilate phosphoribosyltransferase;


Pssm-ID: 237764 [Multi-domain]  Cd Length: 534  Bit Score: 42.01  E-value: 7.52e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1958789846  35 LDGAGPPDLRDLVIrLAGGAILWLSGQAETQDQGAARVAAALDDGSAL 82
Cdd:PRK14607  472 LKGEPRRPQRDAVA-LNAGAALYLVGEADSIKEGVGKALDLIDDGRAY 518
PRX_BCP cd03017
Peroxiredoxin (PRX) family, Bacterioferritin comigratory protein (BCP) subfamily; composed of ...
 343-368 6.05e-03

Peroxiredoxin (PRX) family, Bacterioferritin comigratory protein (BCP) subfamily; composed of thioredoxin-dependent thiol peroxidases, widely expressed in pathogenic bacteria, that protect cells against toxicity from reactive oxygen species by reducing and detoxifying hydroperoxides. The protein was named BCP based on its electrophoretic mobility before its function was known. BCP shows substrate selectivity toward fatty acid hydroperoxides rather than hydrogen peroxide or alkyl hydroperoxides. BCP contains the peroxidatic cysteine but appears not to possess a resolving cysteine (some sequences, not all, contain a second cysteine but its role is still unknown). Unlike other PRXs, BCP exists as a monomer. The plant homolog of BCP is PRX Q, which is expressed only in leaves and is cellularly localized in the chloroplasts and the guard cells of stomata. Also included in this subfamily is the fungal nuclear protein, Dot5p (for disrupter of telomere silencing protein 5), which functions as an alkyl-hydroperoxide reductase during post-diauxic growth.


Pssm-ID: 239315  Cd Length: 140  Bit Score: 37.14  E-value: 6.05e-03
                          10        20
                  ....*....|....*....|....*.
gi 1958789846 343 DFSLLDHKGQPRCKADFRGQWVLMYF 368
Cdd:cd03017     5 DFTLPDQDGETVSLSDLRGKPVVLYF 30
 
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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