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Conserved domains on  [gi|685654399|gb|AIO41529|]
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Tat (twin-arginine translocation) pathway signal sequence domain protein [Burkholderia cenocepacia]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK11433 super family cl36021
aldehyde oxidoreductase 2Fe-2S subunit; Provisional
 1-209 5.14e-85

aldehyde oxidoreductase 2Fe-2S subunit; Provisional


The actual alignment was detected with superfamily member PRK11433:

Pssm-ID: 236910 [Multi-domain]  Cd Length: 217  Bit Score: 251.23  E-value: 5.14e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685654399   1 MSHDTPSSAARRRFLQSAAAAATVGAAAPHVHPQPAHAAAApavahrDAAPAQPVHLDINGRAYTLQLEPRVTLLDALRE 80
Cdd:PRK11433   4 MHEPHDLSLTRRDLLKVSAATAATAAAYPHSTLAASVPAAT------PAPEISPVTLKVNGKTEQLEVDTRTTLLDALRE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685654399  81 YAGLTGTKKGCDRGQCGACTVLVDGRRINACLTLAVMHEGQRITTVEGLASDGELSPVQRAFVEYDAFQCGYCTPGQLCS 160
Cdd:PRK11433  78 HLHLTGTKKGCDHGQCGACTVLVNGRRLNACLTLAVMHQGAEITTIEGLGSPDNLHPMQAAFVKHDGFQCGYCTPGQICS 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 685654399 161 ATALLDEFSSGAASAVTADVRQRPaQLSDDEIRERMSGNLCRCGAYSNI 209
Cdd:PRK11433 158 SVAVLKEIKDGIPSHVTVDLTAAP-ELTADEIRERMSGNICRCGAYSNI 205
 
Name Accession Description Interval E-value
PRK11433 PRK11433
aldehyde oxidoreductase 2Fe-2S subunit; Provisional
 1-209 5.14e-85

aldehyde oxidoreductase 2Fe-2S subunit; Provisional


Pssm-ID: 236910 [Multi-domain]  Cd Length: 217  Bit Score: 251.23  E-value: 5.14e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685654399   1 MSHDTPSSAARRRFLQSAAAAATVGAAAPHVHPQPAHAAAApavahrDAAPAQPVHLDINGRAYTLQLEPRVTLLDALRE 80
Cdd:PRK11433   4 MHEPHDLSLTRRDLLKVSAATAATAAAYPHSTLAASVPAAT------PAPEISPVTLKVNGKTEQLEVDTRTTLLDALRE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685654399  81 YAGLTGTKKGCDRGQCGACTVLVDGRRINACLTLAVMHEGQRITTVEGLASDGELSPVQRAFVEYDAFQCGYCTPGQLCS 160
Cdd:PRK11433  78 HLHLTGTKKGCDHGQCGACTVLVNGRRLNACLTLAVMHQGAEITTIEGLGSPDNLHPMQAAFVKHDGFQCGYCTPGQICS 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 685654399 161 ATALLDEFSSGAASAVTADVRQRPaQLSDDEIRERMSGNLCRCGAYSNI 209
Cdd:PRK11433 158 SVAVLKEIKDGIPSHVTVDLTAAP-ELTADEIRERMSGNICRCGAYSNI 205
CutS COG2080
Aldehyde, CO, or xanthine dehydrogenase, Fe-S subunit, CoxS/CutS family [Energy production and ...
 54-209 1.15e-83

Aldehyde, CO, or xanthine dehydrogenase, Fe-S subunit, CoxS/CutS family [Energy production and conversion]; Aldehyde, CO, or xanthine dehydrogenase, Fe-S subunit, CoxS/CutS family is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway


Pssm-ID: 441683 [Multi-domain]  Cd Length: 155  Bit Score: 245.39  E-value: 1.15e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685654399  54 PVHLDINGRAYTLQLEPRVTLLDALREYAGLTGTKKGCDRGQCGACTVLVDGRRINACLTLAVMHEGQRITTVEGLASDG 133
Cdd:COG2080    3 MITLTVNGKPVEVDVDPDTPLLDVLRDDLGLTGTKFGCGHGQCGACTVLVDGKAVRSCLTLAVQADGKEITTIEGLAEDG 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 685654399 134 ELSPVQRAFVEYDAFQCGYCTPGQLCSATALLDEFSSGaasavtadvrqrpaqlSDDEIRERMSGNLCRCGAYSNI 209
Cdd:COG2080   83 ELHPLQQAFIEHGALQCGYCTPGMIMAAVALLDENPNP----------------TEEEIREALSGNLCRCTGYVRI 142
glyceraldDH_gamma NF041020
glyceraldehyde dehydrogenase subunit gamma;
55-209 2.71e-53

glyceraldehyde dehydrogenase subunit gamma;


Pssm-ID: 468949 [Multi-domain]  Cd Length: 162  Bit Score: 168.44  E-value: 2.71e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685654399  55 VHLDINGRAYTLQLEPRVTLLDALREYAGLTGTKKGCDRGQCGACTVLVDGRRINACLTLAVMHEGQRITTVEGLASDGE 134
Cdd:NF041020  11 IRVKVNGVWYEAEVEPRKLLVHFLRDDLGFTGTHVGCDTSTCGACTVIMNGKSVKSCTVLAVQADGAEITTIEGLSKDGK 90

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 685654399 135 LSPVQRAFVEYDAFQCGYCTPGQLCSATALLDEfssgaasavtadvRQRPaqlSDDEIRERMSGNLCRCGAYSNI 209
Cdd:NF041020  91 LHPIQEAFWENHALQCGYCTPGMIMQAYFLLKE-------------NPNP---TEEEIRDGIHGNLCRCTGYQNI 149
pucE TIGR03198
xanthine dehydrogenase E subunit; This gene has been characterized in B. subtilis as the ...
 54-209 1.40e-41

xanthine dehydrogenase E subunit; This gene has been characterized in B. subtilis as the Iron-sulfur cluster binding-subunit of xanthine dehydrogenase (pucE), acting in conjunction with pucC, the FAD-binding subunit and pucD, the molybdopterin binding subunit. The more common XDH complex (GenProp0640) includes the xdhA gene as the Fe-S cluster binding component.


Pssm-ID: 132242 [Multi-domain]  Cd Length: 151  Bit Score: 138.45  E-value: 1.40e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685654399   54 PVHLDINGRAYTLQLEPRVTLLDALREYAGLTGTKKGCDRGQCGACTVLVDGRRINACLTLAVMHEGQRITTVEGLASDg 133
Cdd:TIGR03198   3 QFRFTVNGQAWEVAAVPTTRLSDLLRKELQLTGTKVSCGIGRCGACSVLIDGKLANACLTMAYQADGHEITTIEGIAEN- 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 685654399  134 ELSPVQRAFVEYDAFQCGYCTPGQLCSATALLDEfssgaasavtadvRQRPaqlSDDEIRERMSGNLCRCGAYSNI 209
Cdd:TIGR03198  82 ELDPCQTAFLEEGGFQCGYCTPGMVVALKALFRE-------------TPQP---SDEDMEEGLSGNLCRCTGYGGI 141
Fer2_2 pfam01799
[2Fe-2S] binding domain;
125-209 5.74e-32

[2Fe-2S] binding domain;


Pssm-ID: 460336 [Multi-domain]  Cd Length: 73  Bit Score: 110.98  E-value: 5.74e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685654399  125 TVEGLASDGELsPVQRAFVEYDAFQCGYCTPGQLCSATALLDEfssgaasavtadvrqRPAQLSDDEIRERMSGNLCRCG 204
Cdd:pfam01799   1 TIEGLAESGGE-PVQQAFAEAGAVQCGYCTPGMIMSAYALLER---------------NPPPPTEAEIREALSGNLCRCT 64


                  ....*
gi 685654399  205 AYSNI 209
Cdd:pfam01799  65 GYRRI 69
fer2 cd00207
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ...
 55-115 3.03e-06

2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in electron transfer processes and in various enzymatic reactions. The family includes plant and algal ferredoxins, which act as electron carriers in photosynthesis and ferredoxins, which participate in redox chains (from bacteria to mammals). Fold is ismilar to thioredoxin.


Pssm-ID: 238126 [Multi-domain]  Cd Length: 84  Bit Score: 43.92  E-value: 3.03e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 685654399  55 VHLDINGRAYTLQLEPRVTLLDALREyAGLTgTKKGCDRGQCGACTVLVD------------------GRRINACLTLA 115
Cdd:cd00207    1 VTINVPGSGVEVEVPEGETLLDAARE-AGID-IPYSCRAGACGTCKVEVVegevdqsdpslldeeeaeGGYVLACQTRV 77
 
Name Accession Description Interval E-value
PRK11433 PRK11433
aldehyde oxidoreductase 2Fe-2S subunit; Provisional
 1-209 5.14e-85

aldehyde oxidoreductase 2Fe-2S subunit; Provisional


Pssm-ID: 236910 [Multi-domain]  Cd Length: 217  Bit Score: 251.23  E-value: 5.14e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685654399   1 MSHDTPSSAARRRFLQSAAAAATVGAAAPHVHPQPAHAAAApavahrDAAPAQPVHLDINGRAYTLQLEPRVTLLDALRE 80
Cdd:PRK11433   4 MHEPHDLSLTRRDLLKVSAATAATAAAYPHSTLAASVPAAT------PAPEISPVTLKVNGKTEQLEVDTRTTLLDALRE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685654399  81 YAGLTGTKKGCDRGQCGACTVLVDGRRINACLTLAVMHEGQRITTVEGLASDGELSPVQRAFVEYDAFQCGYCTPGQLCS 160
Cdd:PRK11433  78 HLHLTGTKKGCDHGQCGACTVLVNGRRLNACLTLAVMHQGAEITTIEGLGSPDNLHPMQAAFVKHDGFQCGYCTPGQICS 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 685654399 161 ATALLDEFSSGAASAVTADVRQRPaQLSDDEIRERMSGNLCRCGAYSNI 209
Cdd:PRK11433 158 SVAVLKEIKDGIPSHVTVDLTAAP-ELTADEIRERMSGNICRCGAYSNI 205
CutS COG2080
Aldehyde, CO, or xanthine dehydrogenase, Fe-S subunit, CoxS/CutS family [Energy production and ...
 54-209 1.15e-83

Aldehyde, CO, or xanthine dehydrogenase, Fe-S subunit, CoxS/CutS family [Energy production and conversion]; Aldehyde, CO, or xanthine dehydrogenase, Fe-S subunit, CoxS/CutS family is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway


Pssm-ID: 441683 [Multi-domain]  Cd Length: 155  Bit Score: 245.39  E-value: 1.15e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685654399  54 PVHLDINGRAYTLQLEPRVTLLDALREYAGLTGTKKGCDRGQCGACTVLVDGRRINACLTLAVMHEGQRITTVEGLASDG 133
Cdd:COG2080    3 MITLTVNGKPVEVDVDPDTPLLDVLRDDLGLTGTKFGCGHGQCGACTVLVDGKAVRSCLTLAVQADGKEITTIEGLAEDG 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 685654399 134 ELSPVQRAFVEYDAFQCGYCTPGQLCSATALLDEFSSGaasavtadvrqrpaqlSDDEIRERMSGNLCRCGAYSNI 209
Cdd:COG2080   83 ELHPLQQAFIEHGALQCGYCTPGMIMAAVALLDENPNP----------------TEEEIREALSGNLCRCTGYVRI 142
glyceraldDH_gamma NF041020
glyceraldehyde dehydrogenase subunit gamma;
55-209 2.71e-53

glyceraldehyde dehydrogenase subunit gamma;


Pssm-ID: 468949 [Multi-domain]  Cd Length: 162  Bit Score: 168.44  E-value: 2.71e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685654399  55 VHLDINGRAYTLQLEPRVTLLDALREYAGLTGTKKGCDRGQCGACTVLVDGRRINACLTLAVMHEGQRITTVEGLASDGE 134
Cdd:NF041020  11 IRVKVNGVWYEAEVEPRKLLVHFLRDDLGFTGTHVGCDTSTCGACTVIMNGKSVKSCTVLAVQADGAEITTIEGLSKDGK 90

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 685654399 135 LSPVQRAFVEYDAFQCGYCTPGQLCSATALLDEfssgaasavtadvRQRPaqlSDDEIRERMSGNLCRCGAYSNI 209
Cdd:NF041020  91 LHPIQEAFWENHALQCGYCTPGMIMQAYFLLKE-------------NPNP---TEEEIRDGIHGNLCRCTGYQNI 149
PRK09908 PRK09908
xanthine dehydrogenase iron sulfur-binding subunit XdhC;
59-209 5.58e-43

xanthine dehydrogenase iron sulfur-binding subunit XdhC;


Pssm-ID: 182139 [Multi-domain]  Cd Length: 159  Bit Score: 142.36  E-value: 5.58e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685654399  59 INGRAYTLQLEPRVTLLDALREYaGLTGTKKGCDRGQCGACTVLVDGRRINACLTLAVMHEGQRITTVEGLASDGELSPV 138
Cdd:PRK09908  13 INGMPFQLHAAPGTPLSELLREQ-GLLSVKQGCCVGECGACTVLVDGTAIDSCLYLAAWAEGKEIRTLEGEAKGGKLSHV 91

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 685654399 139 QRAFVEYDAFQCGYCTPGQLCSATALLDEfssgaasavtadVRQRPaqLSDDEIRERMSGNLCRCGAYSNI 209
Cdd:PRK09908  92 QQAYAKSGAVQCGFCTPGLIMATTAMLAK------------PREKP--LTITEIRRGLAGNLCRCTGYQMI 148
XdhA COG4630
Xanthine dehydrogenase, Fe-S cluster and FAD-binding subunit XdhA [Nucleotide transport and ...
 59-206 9.85e-42

Xanthine dehydrogenase, Fe-S cluster and FAD-binding subunit XdhA [Nucleotide transport and metabolism];


Pssm-ID: 443668 [Multi-domain]  Cd Length: 476  Bit Score: 147.21  E-value: 9.85e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685654399  59 INGRAYTLQ-LEPRVTLLDALREYAGLTGTKKGCDRGQCGACTVLV----DGRR----INACLTLAVMHEGQRITTVEGL 129
Cdd:COG4630    5 LNGELVELSdVPPTTTLLDWLREDRGLTGTKEGCAEGDCGACTVVVgeldDGGLryraVNACILFLPQLDGKALVTVEGL 84

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 685654399 130 AS-DGELSPVQRAFVEYDAFQCGYCTPGQLCSATALldefssgaasavtadvRQRPAQLSDDEIRERMSGNLCRCGAY 206
Cdd:COG4630   85 AGpDGALHPVQQAMVDHHGSQCGFCTPGFVMSLFAL----------------YERGPAPDRADIEDALSGNLCRCTGY 146
pucE TIGR03198
xanthine dehydrogenase E subunit; This gene has been characterized in B. subtilis as the ...
 54-209 1.40e-41

xanthine dehydrogenase E subunit; This gene has been characterized in B. subtilis as the Iron-sulfur cluster binding-subunit of xanthine dehydrogenase (pucE), acting in conjunction with pucC, the FAD-binding subunit and pucD, the molybdopterin binding subunit. The more common XDH complex (GenProp0640) includes the xdhA gene as the Fe-S cluster binding component.


Pssm-ID: 132242 [Multi-domain]  Cd Length: 151  Bit Score: 138.45  E-value: 1.40e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685654399   54 PVHLDINGRAYTLQLEPRVTLLDALREYAGLTGTKKGCDRGQCGACTVLVDGRRINACLTLAVMHEGQRITTVEGLASDg 133
Cdd:TIGR03198   3 QFRFTVNGQAWEVAAVPTTRLSDLLRKELQLTGTKVSCGIGRCGACSVLIDGKLANACLTMAYQADGHEITTIEGIAEN- 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 685654399  134 ELSPVQRAFVEYDAFQCGYCTPGQLCSATALLDEfssgaasavtadvRQRPaqlSDDEIRERMSGNLCRCGAYSNI 209
Cdd:TIGR03198  82 ELDPCQTAFLEEGGFQCGYCTPGMVVALKALFRE-------------TPQP---SDEDMEEGLSGNLCRCTGYGGI 141
xanthine_xdhA TIGR02963
xanthine dehydrogenase, small subunit; Members of this protein family are the small subunit ...
 60-209 1.30e-33

xanthine dehydrogenase, small subunit; Members of this protein family are the small subunit (or, in eukaryotes, the N-terminal domain) of xanthine dehydrogenase, an enzyme of purine catabolism via urate. The small subunit contains both an FAD and a 2Fe-2S cofactor. Aldehyde oxidase (retinal oxidase) appears to have arisen as a neofunctionalization among xanthine dehydrogenases in eukaryotes and [Purines, pyrimidines, nucleosides, and nucleotides, Other]


Pssm-ID: 274365 [Multi-domain]  Cd Length: 467  Bit Score: 125.08  E-value: 1.30e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685654399   60 NGRAYTLQ-LEPRVTLLDALREYAGLTGTKKGCDRGQCGACTVLV----DGRRI-----NACLT-LAVMHeGQRITTVEG 128
Cdd:TIGR02963   6 NGETVTLSdVDPTRTLLDYLREDAGLTGTKEGCAEGDCGACTVVVgelvDGGKLryrsvNACIQfLPSLD-GKAVVTVED 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685654399  129 LAS-DGELSPVQRAFVEYDAFQCGYCTPGQLCSATALLdefssgaasavtadvrQRPAQLSDDEIRERMSGNLCRCGAYS 207
Cdd:TIGR02963  85 LRQpDGRLHPVQQAMVECHGSQCGFCTPGFVMSLYALY----------------KNSPAPSRADIEDALQGNLCRCTGYR 148


                  ..
gi 685654399  208 NI 209
Cdd:TIGR02963 149 PI 150
Fer2_2 pfam01799
[2Fe-2S] binding domain;
125-209 5.74e-32

[2Fe-2S] binding domain;


Pssm-ID: 460336 [Multi-domain]  Cd Length: 73  Bit Score: 110.98  E-value: 5.74e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685654399  125 TVEGLASDGELsPVQRAFVEYDAFQCGYCTPGQLCSATALLDEfssgaasavtadvrqRPAQLSDDEIRERMSGNLCRCG 204
Cdd:pfam01799   1 TIEGLAESGGE-PVQQAFAEAGAVQCGYCTPGMIMSAYALLER---------------NPPPPTEAEIREALSGNLCRCT 64


                  ....*
gi 685654399  205 AYSNI 209
Cdd:pfam01799  65 GYRRI 69
PLN02906 PLN02906
xanthine dehydrogenase
 73-209 7.59e-28

xanthine dehydrogenase


Pssm-ID: 215491 [Multi-domain]  Cd Length: 1319  Bit Score: 110.56  E-value: 7.59e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685654399   73 TLLDALREYaGLTGTKKGCDRGQCGACTVLVDG----------RRINACLTLAVMHEGQRITTVEGLAS--DGeLSPVQR 140
Cdd:PLN02906    3 TLLEYLRDL-GLTGTKLGCGEGGCGACTVMVSHydrktgkcvhYAVNACLAPLYSVEGMHVITVEGIGNrrDG-LHPVQE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 685654399  141 AFVEYDAFQCGYCTPGQLCSATALLdefssgaasavtadvRQRPAQLSDDEIRERMSGNLCRCGAYSNI 209
Cdd:PLN02906   81 ALASMHGSQCGFCTPGFIMSMYALL---------------RSSKTPPTEEQIEECLAGNLCRCTGYRPI 134
mam_aldehyde_ox TIGR02969
aldehyde oxidase; Members of this family are mammalian aldehyde oxidase (EC 1.2.3.1) isozymes, ...
 59-209 3.31e-25

aldehyde oxidase; Members of this family are mammalian aldehyde oxidase (EC 1.2.3.1) isozymes, closely related to xanthine dehydrogenase/oxidase.


Pssm-ID: 132014 [Multi-domain]  Cd Length: 1330  Bit Score: 103.17  E-value: 3.31e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685654399    59 INGRAYT-LQLEPRVTLLDALREYAGLTGTKKGCDRGQCGACTVLVD-----GRRI-----NACLTLAVMHEGQRITTVE 127
Cdd:TIGR02969    7 VNGRKVVeKNVDPETMLLPYLRKKLRLTGTKYGCGGGGCGACTVMISrynpsTKSIrhhpvNACLTPICSLYGAAVTTVE 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685654399   128 GLASD-GELSPVQRAFVEYDAFQCGYCTPGQLCSATALLdefssgaasavtadvRQRPaQLSDDEIRERMSGNLCRCGAY 206
Cdd:TIGR02969   87 GIGSTrTRLHPVQERIAKCHGTQCGFCTPGMVMSMYALL---------------RNHP-EPTLDQLTDALGGNLCRCTGY 150


                   ...
gi 685654399   207 SNI 209
Cdd:TIGR02969  151 RPI 153
PLN00192 PLN00192
aldehyde oxidase
 59-209 1.53e-23

aldehyde oxidase


Pssm-ID: 215096 [Multi-domain]  Cd Length: 1344  Bit Score: 98.25  E-value: 1.53e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685654399   59 INGRAYTL-QLEPRVTLLDALREYAGLTGTKKGCDRGQCGACTVL----------VDGRRINACLTLAVMHEGQRITTVE 127
Cdd:PLN00192   10 VNGERFELsSVDPSTTLLEFLRTQTPFKSVKLGCGEGGCGACVVLlskydpvldqVEDFTVSSCLTLLCSVNGCSITTSE 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685654399  128 GLAS--DGeLSPVQRAFVEYDAFQCGYCTPGQLCSATALLdefssgaasaVTADVRQRP------AQLSDDEIRERMSGN 199
Cdd:PLN00192   90 GLGNskDG-FHPIHKRFAGFHASQCGFCTPGMCISLFSAL----------VNADKTDRPeppsgfSKLTVVEAEKAVSGN 158

                         170
                  ....*....|
gi 685654399  200 LCRCGAYSNI 209
Cdd:PLN00192  159 LCRCTGYRPI 168
PRK09800 PRK09800
putative hypoxanthine oxidase; Provisional
 55-206 1.75e-10

putative hypoxanthine oxidase; Provisional


Pssm-ID: 182084 [Multi-domain]  Cd Length: 956  Bit Score: 59.85  E-value: 1.75e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685654399  55 VHLDINGRAYTLQLEP---RVTLLDALReYAGLTGTKKGcdRGQCGACTVLVDGRRINACLTLAVMHEGQRITTVEGLAS 131
Cdd:PRK09800   3 IHFTLNGAPQELTVNPgenVQKLLFNMG-MHSVRNSDDG--FGFAGSDAIIFNGNIVNASLLIAAQLEKADIRTAESLGK 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 685654399 132 DGELSPVQRAFVEYDAFQCGYCTPgqlcsatalldefssgAASAVTADVRQRPAQLSDDEIRERMSGNLCRCGAY 206
Cdd:PRK09800  80 WNELSLVQQAMVDVGVVQSGYNDP----------------AAALIITDLLDRIAAPTREEIDDALSGLFSRDAGW 138
fer2 cd00207
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ...
 55-115 3.03e-06

2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in electron transfer processes and in various enzymatic reactions. The family includes plant and algal ferredoxins, which act as electron carriers in photosynthesis and ferredoxins, which participate in redox chains (from bacteria to mammals). Fold is ismilar to thioredoxin.


Pssm-ID: 238126 [Multi-domain]  Cd Length: 84  Bit Score: 43.92  E-value: 3.03e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 685654399  55 VHLDINGRAYTLQLEPRVTLLDALREyAGLTgTKKGCDRGQCGACTVLVD------------------GRRINACLTLA 115
Cdd:cd00207    1 VTINVPGSGVEVEVPEGETLLDAARE-AGID-IPYSCRAGACGTCKVEVVegevdqsdpslldeeeaeGGYVLACQTRV 77
Fer2_3 pfam13085
2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core ...
 64-143 4.75e-04

2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core structure consisting of beta(2)-alpha-beta(2) which abeta-grasp type fold. The domain is around one hundred amino acids with four conserved cysteine residues to which the 2Fe-2S cluster is ligated.


Pssm-ID: 432963 [Multi-domain]  Cd Length: 107  Bit Score: 38.37  E-value: 4.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685654399   64 YTLQLEPRVTLLDALRE-YAGLTGT---KKGCDRGQCGACTVLVDGRRINACLTLaVMHEGQRITTVEGLASdgelSPVQ 139
Cdd:pfam13085  21 YEVPYEEGMTVLDALNKiKEEQDPTlafRRSCREGICGSCAMNINGKPRLACKTL-IDDLLGQDITLEPLPG----FPVI 95


                  ....
gi 685654399  140 RAFV 143
Cdd:pfam13085  96 RDLV 99
Fer2_4 pfam13510
2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core ...
 52-128 5.68e-03

2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core structure consisting of beta(2)-alpha-beta(2) which a beta-grasp type fold. The domain is around one hundred amino acids with four conserved cysteine residues to which the 2Fe-2S cluster is ligated. This cluster appears within sarcosine oxidase proteins.


Pssm-ID: 433268 [Multi-domain]  Cd Length: 82  Bit Score: 34.82  E-value: 5.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 685654399   52 AQPVHLDINGRAYTLqlEPRVTLLDALREyAG---LTGTKKG------CDRGQCGACTVLVDGRR-INACLTLAvmHEGQ 121
Cdd:pfam13510   1 SRPVTFTFDGRPVTA--PEGDTIAAALLA-NGvrvPRSCKYGrprgifCAMGECRNCLVEVDGVPnVRACTTPV--REGM 75


                  ....*..
gi 685654399  122 RITTVEG 128
Cdd:pfam13510  76 VVRTQNG 82
PRK06259 PRK06259
succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Provisional
 64-115 7.18e-03

succinate dehydrogenase/fumarate reductase iron-sulfur subunit; Provisional


Pssm-ID: 235756 [Multi-domain]  Cd Length: 486  Bit Score: 36.91  E-value: 7.18e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 685654399  64 YTLQLEPRVTLLDAL----REYAGLTGTKKGCDRGQCGACTVLVDGRRINACLTLA 115
Cdd:PRK06259  23 YEVPVKEGMTVLDALeyinKTYDANIAFRSSCRAGQCGSCAVTINGEPVLACKTEV 78
Fer2 pfam00111
2Fe-2S iron-sulfur cluster binding domain;
57-104 8.83e-03

2Fe-2S iron-sulfur cluster binding domain;


Pssm-ID: 395061 [Multi-domain]  Cd Length: 77  Bit Score: 34.04  E-value: 8.83e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 685654399   57 LDINGRAYTLQLEPRVT-LLDALREyaGLTGTKKGCDRGQCGACTVLVD 104
Cdd:pfam00111   1 VTINGKGVTIEVPDGETtLLDAAEE--AGIDIPYSCRGGGCGTCAVKVL 47
 
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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