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Conserved domains on  [gi|152031698|sp|Q07116|]
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RecName: Full=Sulfite oxidase, mitochondrial; Flags: Precursor

Protein Classification

Cyt-b5 and eukary_SO_Moco domain-containing protein( domain architecture ID 10445751)

Cyt-b5 and eukary_SO_Moco domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
eukary_SO_Moco cd02111
molybdopterin binding domain of sulfite oxidase (SO). SO catalyzes the terminal reaction in ...
 186-544 0e+00

molybdopterin binding domain of sulfite oxidase (SO). SO catalyzes the terminal reaction in the oxidative degradation of the sulfur-containing amino acids cysteine and methionine. Common features of all known members of the sulfite oxidase (SO) family of molybdopterin binding domains are that they contain one single pterin cofactor and part of the coordination of the metal (Mo) is a cysteine ligand of the protein and that they catalyze the transfer of an oxygen to or from a lone pair of electrons on the substrate.


:

Pssm-ID: 239029 [Multi-domain]  Cd Length: 365  Bit Score: 576.26  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152031698 186 ALRINSQRPFNAEPPPELLTESYITPNPIFFTRNHLPVPNLDPDTYRLHVVGaPGGQSLSLSLDDLHK-FPKHEVTVTLQ 264
Cdd:cd02111    1 ALKVNSKKPFNAEPPSSLLASSFITPNELFYVRNHLPVPVVDPDTYSLEVEG-PDGTTLSLSLEDLKSlFPKHEVTATLQ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152031698 265 CAGNRRSEMNKVKEVKGLEWRTGAISTARWAGARLCDVLAQAGHR--LRETEAHVCFEGLDSDPTGTAYGASIPLARAMD 342
Cdd:cd02111   80 CAGNRRSEMTKVKKVKGLQWGDGAISNAEWGGARLRDVLLDAGIPedDSQGGLHVHFEGLDVDPTGTPYGASIPLSKALD 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152031698 343 PQAEVLLAYEMNGQPLPRDHGFPVRVVVPGVVGARHVKWLGRVSVESEESYSHWQRRDYKGFSPSVDWDTVDFDLAPSIQ 422
Cdd:cd02111  160 PEADVLLAYEMNGTPLPRDHGFPLRVVVPGVVGARSVKWLDRIVVSDEESDSHWQQNDYKGFSPSVDWDNVDFSKAPAIQ 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152031698 423 ELPIQSAITQPQDGT---TVESGEVIIKGYAWSGGGRAVIRVDVSMDGGLTWQEAELEGEEQ--HPRKAWAWRIWQLKAH 497
Cdd:cd02111  240 EMPVQSAICSPSVGApvvTVPPGKITVKGYAWSGGGRKIVRVDVSLDGGRTWKVAELEQEENvwPSGRKWAWTLWEATVP 319

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 152031698 498 VPAEqKELNIICKAVDDSYNVQPDTVAPIWNLRGVLSNAWHRVHVQV 544
Cdd:cd02111  320 VPAG-KEAEIIAKAVDSAYNVQPETVEPIWNLRGVLNNAWHRVKVVV 365
Cyt-b5 pfam00173
Cytochrome b5-like Heme/Steroid binding domain; This family includes heme binding domains from ...
 87-161 1.11e-17

Cytochrome b5-like Heme/Steroid binding domain; This family includes heme binding domains from a diverse range of proteins. This family also includes proteins that bind to steroids. The family includes progesterone receptors. Many members of this subfamily are membrane anchored by an N-terminal transmembrane alpha helix. This family also includes a domain in some chitin synthases. There is no known ligand for this domain in the chitin synthases.


:

Pssm-ID: 459698 [Multi-domain]  Cd Length: 74  Bit Score: 77.66  E-value: 1.11e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 152031698   87 SKEDVRSHNNlKTGVWVTLGSEVFDVTKFVDLHPGGQSKLMLAAGGPL-EPFWALyaVHNQPHVRELLAEYKIGEL 161
Cdd:pfam00173   1 TLEELSKHNG-DGDCWVAINGKVYDVTKFLKEHPGGEDVILSAAGKDAtDAFEAI--GHSEDAAEKLLKKYRIGEL 73
 
Name Accession Description Interval E-value
eukary_SO_Moco cd02111
molybdopterin binding domain of sulfite oxidase (SO). SO catalyzes the terminal reaction in ...
 186-544 0e+00

molybdopterin binding domain of sulfite oxidase (SO). SO catalyzes the terminal reaction in the oxidative degradation of the sulfur-containing amino acids cysteine and methionine. Common features of all known members of the sulfite oxidase (SO) family of molybdopterin binding domains are that they contain one single pterin cofactor and part of the coordination of the metal (Mo) is a cysteine ligand of the protein and that they catalyze the transfer of an oxygen to or from a lone pair of electrons on the substrate.


Pssm-ID: 239029 [Multi-domain]  Cd Length: 365  Bit Score: 576.26  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152031698 186 ALRINSQRPFNAEPPPELLTESYITPNPIFFTRNHLPVPNLDPDTYRLHVVGaPGGQSLSLSLDDLHK-FPKHEVTVTLQ 264
Cdd:cd02111    1 ALKVNSKKPFNAEPPSSLLASSFITPNELFYVRNHLPVPVVDPDTYSLEVEG-PDGTTLSLSLEDLKSlFPKHEVTATLQ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152031698 265 CAGNRRSEMNKVKEVKGLEWRTGAISTARWAGARLCDVLAQAGHR--LRETEAHVCFEGLDSDPTGTAYGASIPLARAMD 342
Cdd:cd02111   80 CAGNRRSEMTKVKKVKGLQWGDGAISNAEWGGARLRDVLLDAGIPedDSQGGLHVHFEGLDVDPTGTPYGASIPLSKALD 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152031698 343 PQAEVLLAYEMNGQPLPRDHGFPVRVVVPGVVGARHVKWLGRVSVESEESYSHWQRRDYKGFSPSVDWDTVDFDLAPSIQ 422
Cdd:cd02111  160 PEADVLLAYEMNGTPLPRDHGFPLRVVVPGVVGARSVKWLDRIVVSDEESDSHWQQNDYKGFSPSVDWDNVDFSKAPAIQ 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152031698 423 ELPIQSAITQPQDGT---TVESGEVIIKGYAWSGGGRAVIRVDVSMDGGLTWQEAELEGEEQ--HPRKAWAWRIWQLKAH 497
Cdd:cd02111  240 EMPVQSAICSPSVGApvvTVPPGKITVKGYAWSGGGRKIVRVDVSLDGGRTWKVAELEQEENvwPSGRKWAWTLWEATVP 319

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 152031698 498 VPAEqKELNIICKAVDDSYNVQPDTVAPIWNLRGVLSNAWHRVHVQV 544
Cdd:cd02111  320 VPAG-KEAEIIAKAVDSAYNVQPETVEPIWNLRGVLNNAWHRVKVVV 365
PLN00177 PLN00177
sulfite oxidase; Provisional
 169-544 1.95e-127

sulfite oxidase; Provisional


Pssm-ID: 177772 [Multi-domain]  Cd Length: 393  Bit Score: 378.04  E-value: 1.95e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152031698 169 PPLEASDPYSNDPMRHPALRINSQRPFNAEPPPELLTESYITPNPIFFTRNHLPVPNLDP-DTYRLHVVGAPGgQSLSLS 247
Cdd:PLN00177   2 PGLRGPSDYSQEPPRHPSLKINAKEPFNAEPPRSALVSSYITPVDLFYKRNHGPIPIVDDiERYSVTITGLIE-NPRKLS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152031698 248 LDDLHKFPKHEVTVTLQCAGNRRSEMNKVKEVKGLEWRTGAISTARWAGARLCDVLAQAG-HRLRETEA----HVCFEGL 322
Cdd:PLN00177  81 MKDIRKLPKYNVTATLQCAGNRRTAMSKVRKVRGVGWDVSAIGNAVWGGAKLADVLELVGiPKLTSITSsggkHVEFVSV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152031698 323 DSDP--TGTAYGASIPLARAMDPQAEVLLAYEMNGQPLPRDHGFPVRVVVPGVVGARHVKWLGRVSVESEESYSHWQRRD 400
Cdd:PLN00177 161 DKCKeeNGGPYKASIPLSQATNPEADVLLAYEMNGEVLNRDHGYPLRVVVPGVIGARSVKWLDSINIIAEECQGFFMQKD 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152031698 401 YKGFSPSVDWDTVDFDLAPSIQELPIQSAITQPQDGTTVESGEVIIKGYAWSGGGRAVIRVDVSMDGGLTWQEAELEGEE 480
Cdd:PLN00177 241 YKMFPPSVNWDNINWSTRRPQMDFPVQSAICSLEDVNAIKPGKVTVAGYALSGGGRGIERVDISVDGGKTWVEASRYQKP 320

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 152031698 481 QHPRKA-------WAWRIWQLKAHVPAEQKelnIICKAVDDSYNVQPDTVAPIWNLRGVLSNAWHRVHVQV 544
Cdd:PLN00177 321 GVPYISddissdkWAWVLFEATVDVPQSTE---IVAKAVDSAANVQPESVESIWNLRGILNTSWHRVQLRV 388
Oxidored_molyb pfam00174
Oxidoreductase molybdopterin binding domain; This domain is found in a variety of ...
 220-396 1.21e-65

Oxidoreductase molybdopterin binding domain; This domain is found in a variety of oxidoreductases. This domain binds to a molybdopterin cofactor. Xanthine dehydrogenases, that also bind molybdopterin, have essentially no similarity.


Pssm-ID: 459699 [Multi-domain]  Cd Length: 168  Bit Score: 210.82  E-value: 1.21e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152031698  220 HLPVPNLDPDTYRLHVVGApGGQSLSLSLDDLHKFPKHEVTVTLQCAGNRRSEMNKVKevkGLEWRTGAISTARWAGARL 299
Cdd:pfam00174   1 HGPVPEIDPDTWRLRVDGL-VEKPLTLTLDDLKAFPQVTVTATLQCVGNRRKEMNRVK---GVQWGGGAIGNAEWTGVPL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152031698  300 CDVLAQAGhrLRETEAHVCFEGLDSDPTGtAYGASIPLARAMDPqaEVLLAYEMNGQPLPRDHGFPVRVVVPGVVGARHV 379
Cdd:pfam00174  77 RDLLERAG--VKPGAKHVLFEGADTLGDG-GYTTSLPLEKALDD--DVLLAYEMNGEPLPPDHGYPLRLVVPGWYGARSV 151

                         170
                  ....*....|....*..
gi 152031698  380 KWLGRVSVESEESYSHW 396
Cdd:pfam00174 152 KWLRRIEVTDEESPGFW 168
MsrP COG2041
Molybdopterin-dependent catalytic subunit of periplasmic DMSO/TMAO and ...
 215-406 3.12e-36

Molybdopterin-dependent catalytic subunit of periplasmic DMSO/TMAO and protein-methionine-sulfoxide reductases [Energy production and conversion];


Pssm-ID: 441644 [Multi-domain]  Cd Length: 183  Bit Score: 132.97  E-value: 3.12e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152031698 215 FFTRNHLPVPNLDPDTYRLHVVGApGGQSLSLSLDDLHKFPKHEVTVTLQCAGNrrsemnkvkevkgleWRTGaisTARW 294
Cdd:COG2041   19 FPVRTAGGVPEIDPADWRLRVDGL-VEKPLTLTLDDLLALPLEERIYRLHCVEN---------------WSGG---VAPW 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152031698 295 AGARLCDVLAQAGhrLRETEAHVCFEGLDSDptgtaYGASIPLARAMDPQAevLLAYEMNGQPLPRDHGFPVRvvvpgvv 374
Cdd:COG2041   80 TGVPLRDLLERAG--PKPGAKYVLFESADPG-----YTESLPLDEALDPDT--LLAYGMNGEPLPPEHGAPLR------- 143

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 152031698 375 gAR--------HVKWLGRVSVESEESYSHWQRRDYKGFSP 406
Cdd:COG2041  144 -LVvpglygfkSAKWLVRIEVTDEDPPGYWETRGYHFYAN 182
Cyt-b5 pfam00173
Cytochrome b5-like Heme/Steroid binding domain; This family includes heme binding domains from ...
 87-161 1.11e-17

Cytochrome b5-like Heme/Steroid binding domain; This family includes heme binding domains from a diverse range of proteins. This family also includes proteins that bind to steroids. The family includes progesterone receptors. Many members of this subfamily are membrane anchored by an N-terminal transmembrane alpha helix. This family also includes a domain in some chitin synthases. There is no known ligand for this domain in the chitin synthases.


Pssm-ID: 459698 [Multi-domain]  Cd Length: 74  Bit Score: 77.66  E-value: 1.11e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 152031698   87 SKEDVRSHNNlKTGVWVTLGSEVFDVTKFVDLHPGGQSKLMLAAGGPL-EPFWALyaVHNQPHVRELLAEYKIGEL 161
Cdd:pfam00173   1 TLEELSKHNG-DGDCWVAINGKVYDVTKFLKEHPGGEDVILSAAGKDAtDAFEAI--GHSEDAAEKLLKKYRIGEL 73
PLN03199 PLN03199
delta6-acyl-lipid desaturase-like protein; Provisional
 81-164 1.19e-03

delta6-acyl-lipid desaturase-like protein; Provisional


Pssm-ID: 178740 [Multi-domain]  Cd Length: 485  Bit Score: 41.56  E-value: 1.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152031698  81 ESPRIYSKEDVRSHNNlKTGVWVTLGSEVFDVTKFVDlHPGGQSKLMLAAGGPLEPFWALYAvhnqPHVRELLAEYKIGE 160
Cdd:PLN03199  21 EKPQKISWQEVKKHAS-PDDAWIIHQNKVYDVSNWHD-HPGGAVIFTHAGDDMTDIFAAFHA----PGSQALMKKFYIGD 94


                 ....
gi 152031698 161 LNPE 164
Cdd:PLN03199  95 LIPE 98
 
Name Accession Description Interval E-value
eukary_SO_Moco cd02111
molybdopterin binding domain of sulfite oxidase (SO). SO catalyzes the terminal reaction in ...
 186-544 0e+00

molybdopterin binding domain of sulfite oxidase (SO). SO catalyzes the terminal reaction in the oxidative degradation of the sulfur-containing amino acids cysteine and methionine. Common features of all known members of the sulfite oxidase (SO) family of molybdopterin binding domains are that they contain one single pterin cofactor and part of the coordination of the metal (Mo) is a cysteine ligand of the protein and that they catalyze the transfer of an oxygen to or from a lone pair of electrons on the substrate.


Pssm-ID: 239029 [Multi-domain]  Cd Length: 365  Bit Score: 576.26  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152031698 186 ALRINSQRPFNAEPPPELLTESYITPNPIFFTRNHLPVPNLDPDTYRLHVVGaPGGQSLSLSLDDLHK-FPKHEVTVTLQ 264
Cdd:cd02111    1 ALKVNSKKPFNAEPPSSLLASSFITPNELFYVRNHLPVPVVDPDTYSLEVEG-PDGTTLSLSLEDLKSlFPKHEVTATLQ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152031698 265 CAGNRRSEMNKVKEVKGLEWRTGAISTARWAGARLCDVLAQAGHR--LRETEAHVCFEGLDSDPTGTAYGASIPLARAMD 342
Cdd:cd02111   80 CAGNRRSEMTKVKKVKGLQWGDGAISNAEWGGARLRDVLLDAGIPedDSQGGLHVHFEGLDVDPTGTPYGASIPLSKALD 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152031698 343 PQAEVLLAYEMNGQPLPRDHGFPVRVVVPGVVGARHVKWLGRVSVESEESYSHWQRRDYKGFSPSVDWDTVDFDLAPSIQ 422
Cdd:cd02111  160 PEADVLLAYEMNGTPLPRDHGFPLRVVVPGVVGARSVKWLDRIVVSDEESDSHWQQNDYKGFSPSVDWDNVDFSKAPAIQ 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152031698 423 ELPIQSAITQPQDGT---TVESGEVIIKGYAWSGGGRAVIRVDVSMDGGLTWQEAELEGEEQ--HPRKAWAWRIWQLKAH 497
Cdd:cd02111  240 EMPVQSAICSPSVGApvvTVPPGKITVKGYAWSGGGRKIVRVDVSLDGGRTWKVAELEQEENvwPSGRKWAWTLWEATVP 319

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 152031698 498 VPAEqKELNIICKAVDDSYNVQPDTVAPIWNLRGVLSNAWHRVHVQV 544
Cdd:cd02111  320 VPAG-KEAEIIAKAVDSAYNVQPETVEPIWNLRGVLNNAWHRVKVVV 365
PLN00177 PLN00177
sulfite oxidase; Provisional
 169-544 1.95e-127

sulfite oxidase; Provisional


Pssm-ID: 177772 [Multi-domain]  Cd Length: 393  Bit Score: 378.04  E-value: 1.95e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152031698 169 PPLEASDPYSNDPMRHPALRINSQRPFNAEPPPELLTESYITPNPIFFTRNHLPVPNLDP-DTYRLHVVGAPGgQSLSLS 247
Cdd:PLN00177   2 PGLRGPSDYSQEPPRHPSLKINAKEPFNAEPPRSALVSSYITPVDLFYKRNHGPIPIVDDiERYSVTITGLIE-NPRKLS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152031698 248 LDDLHKFPKHEVTVTLQCAGNRRSEMNKVKEVKGLEWRTGAISTARWAGARLCDVLAQAG-HRLRETEA----HVCFEGL 322
Cdd:PLN00177  81 MKDIRKLPKYNVTATLQCAGNRRTAMSKVRKVRGVGWDVSAIGNAVWGGAKLADVLELVGiPKLTSITSsggkHVEFVSV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152031698 323 DSDP--TGTAYGASIPLARAMDPQAEVLLAYEMNGQPLPRDHGFPVRVVVPGVVGARHVKWLGRVSVESEESYSHWQRRD 400
Cdd:PLN00177 161 DKCKeeNGGPYKASIPLSQATNPEADVLLAYEMNGEVLNRDHGYPLRVVVPGVIGARSVKWLDSINIIAEECQGFFMQKD 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152031698 401 YKGFSPSVDWDTVDFDLAPSIQELPIQSAITQPQDGTTVESGEVIIKGYAWSGGGRAVIRVDVSMDGGLTWQEAELEGEE 480
Cdd:PLN00177 241 YKMFPPSVNWDNINWSTRRPQMDFPVQSAICSLEDVNAIKPGKVTVAGYALSGGGRGIERVDISVDGGKTWVEASRYQKP 320

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 152031698 481 QHPRKA-------WAWRIWQLKAHVPAEQKelnIICKAVDDSYNVQPDTVAPIWNLRGVLSNAWHRVHVQV 544
Cdd:PLN00177 321 GVPYISddissdkWAWVLFEATVDVPQSTE---IVAKAVDSAANVQPESVESIWNLRGILNTSWHRVQLRV 388
SO_family_Moco_dimer cd02110
Subgroup of sulfite oxidase (SO) family molybdopterin binding domains that contains conserved ...
 214-542 1.22e-112

Subgroup of sulfite oxidase (SO) family molybdopterin binding domains that contains conserved dimerization domain. This molybdopterin cofactor (Moco) binding domain is found in a variety of oxidoreductases, main members of this family are nitrate reductase (NR) and sulfite oxidase (SO).


Pssm-ID: 239028 [Multi-domain]  Cd Length: 317  Bit Score: 337.35  E-value: 1.22e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152031698 214 IFFTRNHLPVPNLDPDTYRLHVVGApGGQSLSLSLDDLHKFPKHEVTVTLQCAGNRRSEMNKVkeVKGLEWRTGAISTAR 293
Cdd:cd02110    1 LFFVRNHGGVPDIDPDAWRLEIHGL-VERPLTLTLDDLKRLPSVEVVATLECSGNGRGGFIPV--RSGAQWGHGAVGNAR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152031698 294 WAGARLCDVLAQAGhrLRETEAHVCFEGLDSDPTGTA--YGASIPLARAMDPqaEVLLAYEMNGQPLPRDHGFPVRVVVP 371
Cdd:cd02110   78 WTGVPLKDLLEEAG--VKPGAKHVLFEGADVPPGEKAadYTRSVPLSKALDD--DALLAYEMNGEPLPPDHGYPLRLVVP 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152031698 372 GVVGARHVKWLGRVSVESEESYSHWQRRDYKGFSPSVDWdtVDFDLAPSIQELPIQSAITQPQDGTTVESGEVIIKGYAW 451
Cdd:cd02110  154 GWYGARSVKWLRRIEVTDQPSDGYWQTRDYTVPPPDVDA--VGGKARRPIGEMPVKSVITSPSPGAELVSGGRVEIGGVA 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152031698 452 SGGGRAVIRVDVSMDGGLTWQEAELEGEEQHPrkaWAWRIWQLKahVPAEQKELNIICKAVDDSYNVQPDTVAPIWNLRG 531
Cdd:cd02110  232 WSGGRGIRRVEVSLDGGRTWQEARLEGPLAGP---RAWRQWELD--WDLPPGEYELVARATDSTGNVQPERAEWNWNPGG 306

                        330
                 ....*....|.
gi 152031698 532 VLSNAWHRVHV 542
Cdd:cd02110  307 YGNNHWHRVQV 317
PLN02252 PLN02252
nitrate reductase [NADPH]
 183-544 2.53e-94

nitrate reductase [NADPH]


Pssm-ID: 215141 [Multi-domain]  Cd Length: 888  Bit Score: 306.99  E-value: 2.53e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152031698 183 RHPAL-RINSQRPFNAEPP-PELLTESYITPNPIFFTRNHLPVPNLDPDTYRLHVVGAPGgQSLSLSLDDLHKFPKHEVT 260
Cdd:PLN02252  84 RHPSLvRLTGKHPFNCEPPlARLMEHGFITPAPLHYVRNHGAVPRADWDEWTVEVTGLVK-RPARLTMDELVRFPARELP 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152031698 261 VTLQCAGNRRSEMNKVKEVKGLEWRTGAISTARWAGARLCDVLAQAGHRLRETEA-HVCFEGLDSDPTG--TAYGASIPL 337
Cdd:PLN02252 163 VTLVCAGNRRKEQNMVKQTIGFNWGAAGVSTSVWRGVRLRDVLRRCGVMSRKGGAlNVCFEGAEDLPGGggSKYGTSITL 242

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152031698 338 ARAMDPQAEVLLAYEMNGQPLPRDHGFPVRVVVPGVVGARHVKWLGRVSVESEESYSHWQRRDYKgFSPSvdwdTVDFDL 417
Cdd:PLN02252 243 ERAMDPARDVILAYMQNGEPLTPDHGFPVRLIIPGFIGGRMVKWLKRIIVTTAESDNYYHYRDNR-VLPS----HVDAEL 317

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152031698 418 APS----------IQELPIQSAITQPQDGTTVESGEV------IIKGYAWSGGGRAVIRVDVSMDGGLTWQEAELEGEEQ 481
Cdd:PLN02252 318 ANAegwwykpeyiINELNINSVITTPAHDEILPINASttqrpyTMKGYAYSGGGRKVTRVEVSLDGGETWRLCDLDHPEK 397

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 152031698 482 HPR--KAWAWRIWQLKAHVP--AEQKElnIICKAVDDSYNVQPDTvaPIWNLRGVLSNAWHRVHVQV 544
Cdd:PLN02252 398 PTKygKYWCWCFWSLDVEVLdlLGAKE--IAVRAWDESMNTQPEK--LIWNLMGMMNNCWFRVKVNV 460
eukary_NR_Moco cd02112
molybdopterin binding domain of eukaryotic nitrate reductase (NR). Assimilatory NRs catalyze ...
 183-542 4.01e-94

molybdopterin binding domain of eukaryotic nitrate reductase (NR). Assimilatory NRs catalyze the reduction of nitrate to nitrite which is subsequently converted to NH4+ by nitrite reductase. Eukaryotic assimilatory nitrate reductases are cytosolic homodimeric enzymes with three prosthetic groups, flavin adenine dinucleotide (FAD), cytochrome b557, and Mo cofactor, which are located in three functional domains. Common features of all known members of the sulfite oxidase (SO) family of molybdopterin binding domains are that they contain one single pterin cofactor and part of the coordination of the metal (Mo) is a cysteine ligand of the protein and that they catalyze the transfer of an oxygen to or from a lone pair of electrons on the substrate.


Pssm-ID: 239030 [Multi-domain]  Cd Length: 386  Bit Score: 292.36  E-value: 4.01e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152031698 183 RHPAL-RINSQRPFNAEPPP-ELLTESYITPNPIFFTRNHLPVPNLDPDTYRLHVVG---APggqsLSLSLDDL-HKFPK 256
Cdd:cd02112   11 RDPRLiRLTGKHPFNSEPPLtELMDHGFITPSNLHYVRNHGPVPREKWEDWTVEVTGlveKP----TTLTMDELvAMFPS 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152031698 257 HEVTVTLQCAGNRRSEMNKVKEVKGLEWRTGAISTARWAGARLCDVLAQAGHRLRETEA-HVCFEGLDSDPTG--TAYGA 333
Cdd:cd02112   87 VTFPVTLVCAGNRRKEQNMVKKTIGFNWGAAGTSTSLWTGVRLSDLLDRCGPKSPKGGArHVCFEGADDLLPGpnGKYGT 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152031698 334 SIPLARAMDPQAEVLLAYEMNGQPLPRDHGFPVRVVVPGVVGARHVKWLGRVSVESEESYSHWQRRDYKGFSPSVDWDTV 413
Cdd:cd02112  167 SITLSWAMDPSKDVMLAYKQNGELLHPDHGFPVRLIIPGQIGGRMVKWLKRIVVSDRESQNHYHFHDNRVLPSHVDAELA 246

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152031698 414 D-----FDLAPSIQELPIQSAITQPQDGTTVESGEVI------IKGYAWSGGGRAVIRVDVSMDGGLTWQEAELEGEEQH 482
Cdd:cd02112  247 NeegwwYKPEYIINDLNVNSAITTPAHDEVLPLNGLTtaetytMKGYAYAGGGRRVTRVEVSLDDGKSWKLASIDYPEDP 326

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 152031698 483 PR--KAWAWRIWQLKAHVPAEQKELNIICKAVDDSYNVQPDTvaPIWNLRGVLSNAWHRVHV 542
Cdd:cd02112  327 TKygKCWCWCFWSLDVPLSELLAAKEICVRAWDESMNTQPRD--MTWNVMGMMNNCWFRVKI 386
Oxidored_molyb pfam00174
Oxidoreductase molybdopterin binding domain; This domain is found in a variety of ...
 220-396 1.21e-65

Oxidoreductase molybdopterin binding domain; This domain is found in a variety of oxidoreductases. This domain binds to a molybdopterin cofactor. Xanthine dehydrogenases, that also bind molybdopterin, have essentially no similarity.


Pssm-ID: 459699 [Multi-domain]  Cd Length: 168  Bit Score: 210.82  E-value: 1.21e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152031698  220 HLPVPNLDPDTYRLHVVGApGGQSLSLSLDDLHKFPKHEVTVTLQCAGNRRSEMNKVKevkGLEWRTGAISTARWAGARL 299
Cdd:pfam00174   1 HGPVPEIDPDTWRLRVDGL-VEKPLTLTLDDLKAFPQVTVTATLQCVGNRRKEMNRVK---GVQWGGGAIGNAEWTGVPL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152031698  300 CDVLAQAGhrLRETEAHVCFEGLDSDPTGtAYGASIPLARAMDPqaEVLLAYEMNGQPLPRDHGFPVRVVVPGVVGARHV 379
Cdd:pfam00174  77 RDLLERAG--VKPGAKHVLFEGADTLGDG-GYTTSLPLEKALDD--DVLLAYEMNGEPLPPDHGYPLRLVVPGWYGARSV 151

                         170
                  ....*....|....*..
gi 152031698  380 KWLGRVSVESEESYSHW 396
Cdd:pfam00174 152 KWLRRIEVTDEESPGFW 168
Mo-co_dimer pfam03404
Mo-co oxidoreductase dimerization domain; This domain is found in molybdopterin cofactor ...
 419-544 6.79e-52

Mo-co oxidoreductase dimerization domain; This domain is found in molybdopterin cofactor (Mo-co) oxidoreductases. It is involved in dimer formation, and has an Ig-fold structure.


Pssm-ID: 427280 [Multi-domain]  Cd Length: 136  Bit Score: 173.32  E-value: 6.79e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152031698  419 PSIQELPIQSAITQPQDGTTVES----GEVIIKGYAWSGGGRAVIRVDVSMDGGLTWQEAELEGEEQHPR------KAWA 488
Cdd:pfam03404   2 YAIYDLNVNSAICSPEHDEVVKLgaaqGTYTIKGYAYSGGGRRITRVEVSLDGGKTWRLAEIDYEEDPYRygewreKCWC 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 152031698  489 WRIWQLKAHVPAEQKELNIICKAVDDSYNVQPDTvaPIWNLRGVLSNAWHRVHVQV 544
Cdd:pfam03404  82 WCFWSLDIPVSDLLKAKEILVRAVDEAMNVQPED--MYWNVRGMMNNPWHRVKIHV 135
bact_SorA_Moco cd02114
sulfite:cytochrome c oxidoreductase subunit A (SorA), molybdopterin binding domain. SorA is ...
 176-542 7.61e-50

sulfite:cytochrome c oxidoreductase subunit A (SorA), molybdopterin binding domain. SorA is involved in oxidation of sulfur compounds during chemolithothrophic growth. Together with SorB, a small c-type heme containing subunit, it forms a hetrodimer. It is a member of the sulfite oxidase (SO) family of molybdopterin binding domains. This molybdopterin cofactor (Moco) binding domain is found in a variety of oxidoreductases, main members of this family are nitrate reductase (NR) and sulfite oxidase (SO). Common features of all known members of this family are that they contain one single pterin cofactor and part of the coordination of the metal (Mo) is a cysteine ligand of the protein and that they catalyze the transfer of an oxygen to or from a lone pair of electrons on the substrate.


Pssm-ID: 239032 [Multi-domain]  Cd Length: 367  Bit Score: 175.78  E-value: 7.61e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152031698 176 PYSNDPMRHPALRINSqRPFNAEPPPELLTESYITPNPIFFTRNHLP-VP-NLDPDTYRLHVVGAPGgQSLSLSLDDLHK 253
Cdd:cd02114    9 ELVPFPQKRPLIRLTT-RPPHLETPFSVFNEGLITPNDAFFVRYHLAgIPlDIDPDAYTLTIDGKVR-TPLTLSLAELKR 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152031698 254 F-PKHEVTVTLQCAGNRRSEMNKvkEVKGLEWRTGAISTARWAGARLCDVLAQAGhrLRETEAHVCFEGLDSDP--TGTA 330
Cdd:cd02114   87 IePRFEVVAVNQCSGNSRGFFQP--RVQGAQLANGAMGNARWAGVPLKAVLAKAG--VQDGARQVAFRGLDQPVldVTPD 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152031698 331 YGASIPLARAMDPqaEVLLAYEMNGQPLPRDHGFPVRVVVPGVVGARHVKWLGRVSVESEESYSHWQRRDYKgfSPSVDW 410
Cdd:cd02114  163 FVKSLDIDHALDG--EVMLAWEMNGEPLPVLNGYPLRLVVPGFYATYWVKHLSHITVLDKEFDGFWASQAYR--IPDNAD 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152031698 411 DTVDFDLAPS----IQELPIQSAITQPQDGTTVES-GEVIIKGYAWSgGGRAVIRVDVSMDGGLTWQEAELeGEEQhprK 485
Cdd:cd02114  239 AGVEPGTAPDrtapINRFKVRSFITSLENGAIVAPaGELALRGIAFD-GGSGIRRVDVSADGGDSWTQATL-GPDL---G 313

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 152031698 486 AWAWRIWQLkAHVPAEQKELNIICKAVDDSYNVQPDTVApiWNLRGVLSNAWHRVHV 542
Cdd:cd02114  314 RFSFRGWKL-TLDGVKKGPLTLMVRATNNDGQTQPLRAP--WNPGGYMRNVVERTRI 367
SO_family_Moco cd00321
Sulfite oxidase (SO) family, molybdopterin binding domain. This molybdopterin cofactor (Moco) ...
 216-387 4.73e-49

Sulfite oxidase (SO) family, molybdopterin binding domain. This molybdopterin cofactor (Moco) binding domain is found in a variety of oxidoreductases, main members of this family are nitrate reductase (NR) and sulfite oxidase (SO). SO catalyzes the terminal reaction in the oxidative degradation of the sulfur-containing amino acids cysteine and methionine. Assimilatory NRs catalyze the reduction of nitrate to nitrite which is subsequently converted to NH4+ by nitrite reductase. Common features of all known members of this family are that they contain one single pterin cofactor and part of the coordination of the metal (Mo) is a cysteine ligand of the protein and that they catalyze the transfer of an oxygen to or from a lone pair of electrons on the substrate.


Pssm-ID: 238198 [Multi-domain]  Cd Length: 156  Bit Score: 166.59  E-value: 4.73e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152031698 216 FTRNHLPVP-NLDPDTYRLHVVGApGGQSLSLSLDDLHKFPKHEVTVTLQCAGNRrsemnkvkevkgleWRTGAISTARW 294
Cdd:cd00321    1 FVRNHGGVPpEIDPDDWRLEVDGL-VEKPLSLTLDDLKALPQVEVIATLHCVGNR--------------WGGGAVSNAEW 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152031698 295 AGARLCDVLAQAGHRlrETEAHVCFEGLDsDPTGTAYGASIPLARAMDPqaEVLLAYEMNGQPLPRDHGFPVRVVVPGVV 374
Cdd:cd00321   66 TGVPLRDLLEEAGPK--PGARYVVFEGAD-DPGGDGYTTSLPLEKALDP--DVLLAYEMNGEPLPPDHGFPLRLVVPGLY 140

                        170
                 ....*....|...
gi 152031698 375 GARHVKWLGRVSV 387
Cdd:cd00321  141 GWKSVKWLRRIEV 153
bact_SoxC_Moco cd02113
bacterial SoxC is a member of the sulfite oxidase (SO) family of molybdopterin binding domains. ...
 209-534 4.78e-41

bacterial SoxC is a member of the sulfite oxidase (SO) family of molybdopterin binding domains. SoxC is involved in oxidation of sulfur compounds during chemolithothrophic growth. Together with SoxD, a small c-type heme containing subunit, it forms a hetrotetrameric sulfite dehydrogenase. This molybdopterin cofactor (Moco) binding domain is found in a variety of oxidoreductases, main members of this family are nitrate reductase (NR) and sulfite oxidase (SO). Common features of all known members of this family are that they contain one single pterin cofactor and part of the coordination of the metal (Mo) is a cysteine ligand of the protein and that they catalyze the transfer of an oxygen to or from a lone pair of electrons on the substrate.


Pssm-ID: 239031 [Multi-domain]  Cd Length: 326  Bit Score: 150.63  E-value: 4.78e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152031698 209 ITPNPIFFTRNHLPVPNLDPDTYRLHVVGAPGgQSLSLSLDDLHKFPKHEVTVTLQCAGNRRSEMNKVKeVKGLEWRTGA 288
Cdd:cd02113    9 ITPNGLHFERHHGGVPDIDPAQHRLMIHGMVK-KPLVFTMDDLKRFPSVSRIYFLECSGNGGTGWRGAP-LPTAQYTHGM 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152031698 289 ISTARWAGARLCDVLAQAGhrLRETEAHVCFEGLDsdptGTAYGASIPLARAMDpqaEVLLAYEMNGQPLPRDHGFPVRV 368
Cdd:cd02113   87 LSCSEWTGVPLSTLLEEAG--VKPGAKWLLAEGAD----AAAMTRSIPLEKALD---DALVAYAQNGEALRPENGYPLRL 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152031698 369 VVPGVVGARHVKWLGRVSVESEESYSHWQRRDYKGFSPSVDWDTVDFDLAPsiqelpiQSAITQPQDGTTV-ESGEVIIK 447
Cdd:cd02113  158 VVPGWEGNTNVKWLRRIEVGDQPWMTREETSKYTDLLPDGRARQFSFVMEA-------KSVITSPSGGQRLrEPGFHEIS 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152031698 448 GYAWSGGGRaVIRVDVSMDGGLTWQEAELEGEEQHP-----RKAWAWriwqlkahvpaEQKELNIICKAVDDSYNVQPdT 522
Cdd:cd02113  231 GLAWSGRGR-IRRVDVSFDGGRTWQDARLEGPVLPKaltrfRLPWKW-----------DGRPAVLQSRATDETGYVQP-T 297

                        330
                 ....*....|..
gi 152031698 523 VAPIWNLRGVLS 534
Cdd:cd02113  298 RAELRAVRGTNS 309
MsrP COG2041
Molybdopterin-dependent catalytic subunit of periplasmic DMSO/TMAO and ...
 215-406 3.12e-36

Molybdopterin-dependent catalytic subunit of periplasmic DMSO/TMAO and protein-methionine-sulfoxide reductases [Energy production and conversion];


Pssm-ID: 441644 [Multi-domain]  Cd Length: 183  Bit Score: 132.97  E-value: 3.12e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152031698 215 FFTRNHLPVPNLDPDTYRLHVVGApGGQSLSLSLDDLHKFPKHEVTVTLQCAGNrrsemnkvkevkgleWRTGaisTARW 294
Cdd:COG2041   19 FPVRTAGGVPEIDPADWRLRVDGL-VEKPLTLTLDDLLALPLEERIYRLHCVEN---------------WSGG---VAPW 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152031698 295 AGARLCDVLAQAGhrLRETEAHVCFEGLDSDptgtaYGASIPLARAMDPQAevLLAYEMNGQPLPRDHGFPVRvvvpgvv 374
Cdd:COG2041   80 TGVPLRDLLERAG--PKPGAKYVLFESADPG-----YTESLPLDEALDPDT--LLAYGMNGEPLPPEHGAPLR------- 143

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 152031698 375 gAR--------HVKWLGRVSVESEESYSHWQRRDYKGFSP 406
Cdd:COG2041  144 -LVvpglygfkSAKWLVRIEVTDEDPPGYWETRGYHFYAN 182
Cyt-b5 pfam00173
Cytochrome b5-like Heme/Steroid binding domain; This family includes heme binding domains from ...
 87-161 1.11e-17

Cytochrome b5-like Heme/Steroid binding domain; This family includes heme binding domains from a diverse range of proteins. This family also includes proteins that bind to steroids. The family includes progesterone receptors. Many members of this subfamily are membrane anchored by an N-terminal transmembrane alpha helix. This family also includes a domain in some chitin synthases. There is no known ligand for this domain in the chitin synthases.


Pssm-ID: 459698 [Multi-domain]  Cd Length: 74  Bit Score: 77.66  E-value: 1.11e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 152031698   87 SKEDVRSHNNlKTGVWVTLGSEVFDVTKFVDLHPGGQSKLMLAAGGPL-EPFWALyaVHNQPHVRELLAEYKIGEL 161
Cdd:pfam00173   1 TLEELSKHNG-DGDCWVAINGKVYDVTKFLKEHPGGEDVILSAAGKDAtDAFEAI--GHSEDAAEKLLKKYRIGEL 73
arch_bact_SO_family_Moco cd02109
bacterial and archael members of the sulfite oxidase (SO) family of molybdopterin binding ...
 221-401 2.51e-17

bacterial and archael members of the sulfite oxidase (SO) family of molybdopterin binding domains. This molybdopterin cofactor (Moco) binding domain is found in a variety of oxidoreductases, main members of this family are nitrate reductase (NR) and sulfite oxidase (SO). Common features of all known members of this family are that they contain one single pterin cofactor and part of the coordination of the metal (Mo) is a cysteine ligand of the protein and that they catalyze the transfer of an oxygen to or from a lone pair of electrons on the substrate. The specific function of this subgroup is unknown.


Pssm-ID: 239027 [Multi-domain]  Cd Length: 180  Bit Score: 79.98  E-value: 2.51e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152031698 221 LPVPNLDPDTYRLHVVGAPGGQsLSLSLDDLHKFPKHEVTVTLQCagnrrsemnkvkeVKGleWrtgAISTARWAGARLC 300
Cdd:cd02109   17 GDVPEVDLEKWRLRVTGLVENP-LSLTYEDLLALPQTEYTADFHC-------------VTG--W---SKLDVVWEGVSLK 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152031698 301 DVLAQAghRLRETEAHVCFEGLDsdptgtAYGASIPLARAMDPqaEVLLAYEMNGQPLPRDHGFPVRVVVPGVVGARHVK 380
Cdd:cd02109   78 DLLEAA--RPDPEATFVMAHSYD------GYTTNLPLEDLLRE--DSLLATKMDGEPLPPEHGGPARLVVPHLYFWKSAK 147

                        170       180
                 ....*....|....*....|.
gi 152031698 381 WLGRVSVESEESYSHWQRRDY 401
Cdd:cd02109  148 WLRGIEFLDEDEPGFWERRGY 168
bact_SO_family_Moco cd02108
bacterial subgroup of the sulfite oxidase (SO) family of molybdopterin binding domains. This ...
 216-364 2.21e-15

bacterial subgroup of the sulfite oxidase (SO) family of molybdopterin binding domains. This domain is found in a variety of oxidoreductases. Common features of all known members of this family, like sulfite oxidase and nitrite reductase, are that they contain one single pterin cofactor and part of the coordination of the metal (Mo) is a cysteine ligand of the protein and that they catalyze the transfer of an oxygen to or from a lone pair of electrons on the substrate. The specific function of this subgroup is unknown.


Pssm-ID: 239026 [Multi-domain]  Cd Length: 185  Bit Score: 74.35  E-value: 2.21e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152031698 216 FTRNHLPVPNL---------DPDTYRLHVvgapGG---QSLSLSLDDLHKFPKHEVTVTLQCagnrrsemnkvkeVKGle 283
Cdd:cd02108    5 FRRNGIRKPEAlaykaleanDFADYRLEV----GGlveHPLSLSLEELRALPQRTQITRHIC-------------VEG-- 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152031698 284 WrtGAIstARWAGARLCDVLAQAGhrlRETEA-HVCFEGLDSDPTGTAYGASIPLARAMDPQAevLLAYEMNGQPLPRDH 362
Cdd:cd02108   66 W--SAI--GKWGGVPLRTILELVG---PLPEAkYVVFKCADDFAGGDRYYESIDMASALHPQT--LLAYEMNGQPLPIKN 136


                 ..
gi 152031698 363 GF 364
Cdd:cd02108  137 GA 138
PLN02252 PLN02252
nitrate reductase [NADPH]
 81-247 7.43e-09

nitrate reductase [NADPH]


Pssm-ID: 215141 [Multi-domain]  Cd Length: 888  Bit Score: 58.54  E-value: 7.43e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152031698  81 ESPRIYSKEDVRSHNNlKTGVWVTLGSEVFDVTKFVDLHPGG-QSKLMLAAGGPLEPFwalYAVHNQpHVRELLAEYKIG 159
Cdd:PLN02252 515 TGSKQYTMSEVRKHNS-EDSCWIVVHGHVYDCTRFLKDHPGGaDSILINAGTDCTEEF---DAIHSD-KAKKMLEDYRIG 589

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152031698 160 ELnpeDRMSPPLEASDPYSNDPMRHPALRINSQRPfnAEPPPELLtesyitpNPifftRNHLPVP-----NLDPDTYRL- 233
Cdd:PLN02252 590 EL---VTTGAAASSSASSHPLSAISTASALAAASP--APGRPVAL-------NP----REKIPCRlvekiSLSHDVRLFr 653

                        170       180
                 ....*....|....*....|.
gi 152031698 234 -------HVVGAPGGQSLSLS 247
Cdd:PLN02252 654 falpsedHVLGLPVGKHVFLC 674
COG3915 COG3915
Uncharacterized conserved protein [Function unknown];
221-363 5.43e-06

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443120  Cd Length: 167  Bit Score: 46.81  E-value: 5.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152031698 221 LPVPNLDPDtyrLHVVGAPG----GQSLSLSLDDLHKFPKHEVTVTLqcagnrrsemnkvkevkglEWRTGAIstaRWAG 296
Cdd:COG3915   24 LPAPAGPVI---LTVSGKIGntnaGGAATFDLAMLEALPQTEITTTT-------------------PWTDGVQ---TFRG 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 152031698 297 ARLCDVLAQAGhrLRETEAHVcfegldsdptgTA---YGASIPLARAMDpqAEVLLAYEMNGQPLP-RDHG 363
Cdd:COG3915   79 VLLRDLLAAVG--AKGTTLRA-----------VAlndYAVEIPISDLEE--YGVILAYRMDGKPMSvRDKG 134
PLN03199 PLN03199
delta6-acyl-lipid desaturase-like protein; Provisional
 81-164 1.19e-03

delta6-acyl-lipid desaturase-like protein; Provisional


Pssm-ID: 178740 [Multi-domain]  Cd Length: 485  Bit Score: 41.56  E-value: 1.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152031698  81 ESPRIYSKEDVRSHNNlKTGVWVTLGSEVFDVTKFVDlHPGGQSKLMLAAGGPLEPFWALYAvhnqPHVRELLAEYKIGE 160
Cdd:PLN03199  21 EKPQKISWQEVKKHAS-PDDAWIIHQNKVYDVSNWHD-HPGGAVIFTHAGDDMTDIFAAFHA----PGSQALMKKFYIGD 94


                 ....
gi 152031698 161 LNPE 164
Cdd:PLN03199  95 LIPE 98
 
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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