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Conserved domains on  [gi|74099702|ref|NP_001027558|]
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sulfite oxidase, mitochondrial [Homo sapiens]

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 ...
 185-543 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: 598.22  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099702 185 ALKVNSQRPFNAEPPPELLTENYITPNPIFFTRNHLPVPNLDPDTYRLHVVGaPGGQSLSLSLDDLH-NFPRYEITVTLQ 263
Cdd:cd02111   1 ALKVNSKKPFNAEPPSSLLASSFITPNELFYVRNHLPVPVVDPDTYSLEVEG-PDGTTLSLSLEDLKsLFPKHEVTATLQ 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099702 264 CAGNRRSEMTQVKEVKGLEWRTGAISTARWAGARLCDVLAQAGHQLC--ETEAHVCFEGLDSDPTGTAYGASIPLARAMD 341
Cdd:cd02111  80 CAGNRRSEMTKVKKVKGLQWGDGAISNAEWGGARLRDVLLDAGIPEDdsQGGLHVHFEGLDVDPTGTPYGASIPLSKALD 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099702 342 PEAEVLLAYEMNGQPLPRDHGFPVRVVVPGVVGARHVKWLGRVSVQPEESYSHWQRRDYKGFSPSVDWETVDFDSAPSIQ 421
Cdd:cd02111 160 PEADVLLAYEMNGTPLPRDHGFPLRVVVPGVVGARSVKWLDRIVVSDEESDSHWQQNDYKGFSPSVDWDNVDFSKAPAIQ 239

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099702 422 ELPVQSAITEPRDGE---TVESGEVTIKGYAWSGGGRAVIRVDVSLDGGLTWQVAKLDGEEQR--PRKAWAWRLWQLKAP 496
Cdd:cd02111 240 EMPVQSAICSPSVGApvvTVPPGKITVKGYAWSGGGRKIVRVDVSLDGGRTWKVAELEQEENVwpSGRKWAWTLWEATVP 319

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*..
gi 74099702 497 VPAGqKELNIVCKAVDDGYNVQPDTVAPIWNLRGVLSNAWHRVHVYV 543
Cdd:cd02111 320 VPAG-KEAEIIAKAVDSAYNVQPETVEPIWNLRGVLNNAWHRVKVVV 365
Cyt-b5 pfam00173
Cytochrome b5-like Heme/Steroid binding domain; This family includes heme binding domains from ...
 86-160 1.95e-18

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: 79.59  E-value: 1.95e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 74099702    86 TKEEVSSHTSPEtGIWVTLGSEVFDVTEFVDLHPGGPSKLMLAAGGPL-EPFWALyaVHNQSHVRELLAQYKIGEL 160
Cdd:pfam00173   1 TLEELSKHNGDG-DCWVAINGKVYDVTKFLKEHPGGEDVILSAAGKDAtDAFEAI--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 ...
 185-543 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: 598.22  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099702 185 ALKVNSQRPFNAEPPPELLTENYITPNPIFFTRNHLPVPNLDPDTYRLHVVGaPGGQSLSLSLDDLH-NFPRYEITVTLQ 263
Cdd:cd02111   1 ALKVNSKKPFNAEPPSSLLASSFITPNELFYVRNHLPVPVVDPDTYSLEVEG-PDGTTLSLSLEDLKsLFPKHEVTATLQ 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099702 264 CAGNRRSEMTQVKEVKGLEWRTGAISTARWAGARLCDVLAQAGHQLC--ETEAHVCFEGLDSDPTGTAYGASIPLARAMD 341
Cdd:cd02111  80 CAGNRRSEMTKVKKVKGLQWGDGAISNAEWGGARLRDVLLDAGIPEDdsQGGLHVHFEGLDVDPTGTPYGASIPLSKALD 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099702 342 PEAEVLLAYEMNGQPLPRDHGFPVRVVVPGVVGARHVKWLGRVSVQPEESYSHWQRRDYKGFSPSVDWETVDFDSAPSIQ 421
Cdd:cd02111 160 PEADVLLAYEMNGTPLPRDHGFPLRVVVPGVVGARSVKWLDRIVVSDEESDSHWQQNDYKGFSPSVDWDNVDFSKAPAIQ 239

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099702 422 ELPVQSAITEPRDGE---TVESGEVTIKGYAWSGGGRAVIRVDVSLDGGLTWQVAKLDGEEQR--PRKAWAWRLWQLKAP 496
Cdd:cd02111 240 EMPVQSAICSPSVGApvvTVPPGKITVKGYAWSGGGRKIVRVDVSLDGGRTWKVAELEQEENVwpSGRKWAWTLWEATVP 319

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*..
gi 74099702 497 VPAGqKELNIVCKAVDDGYNVQPDTVAPIWNLRGVLSNAWHRVHVYV 543
Cdd:cd02111 320 VPAG-KEAEIIAKAVDSAYNVQPETVEPIWNLRGVLNNAWHRVKVVV 365
PLN00177 PLN00177
sulfite oxidase; Provisional
 168-543 2.70e-123

sulfite oxidase; Provisional


Pssm-ID: 177772 [Multi-domain]  Cd Length: 393  Bit Score: 367.64  E-value: 2.70e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099702  168 PTVETSDPYADDPVRHPALKVNSQRPFNAEPPPELLTENYITPNPIFFTRNHLPVPNLDP-DTYRLHVVGAPGgQSLSLS 246
Cdd:PLN00177   2 PGLRGPSDYSQEPPRHPSLKINAKEPFNAEPPRSALVSSYITPVDLFYKRNHGPIPIVDDiERYSVTITGLIE-NPRKLS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099702  247 LDDLHNFPRYEITVTLQCAGNRRSEMTQVKEVKGLEWRTGAISTARWAGARLCDVLAQAG-HQLCETEA----HVCFEGL 321
Cdd:PLN00177  81 MKDIRKLPKYNVTATLQCAGNRRTAMSKVRKVRGVGWDVSAIGNAVWGGAKLADVLELVGiPKLTSITSsggkHVEFVSV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099702  322 DSDP--TGTAYGASIPLARAMDPEAEVLLAYEMNGQPLPRDHGFPVRVVVPGVVGARHVKWLGRVSVQPEESYSHWQRRD 399
Cdd:PLN00177 161 DKCKeeNGGPYKASIPLSQATNPEADVLLAYEMNGEVLNRDHGYPLRVVVPGVIGARSVKWLDSINIIAEECQGFFMQKD 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099702  400 YKGFSPSVDWETVDFDSAPSIQELPVQSAITEPRDGETVESGEVTIKGYAWSGGGRAVIRVDVSLDGGLTWQVAKLDGEE 479
Cdd:PLN00177 241 YKMFPPSVNWDNINWSTRRPQMDFPVQSAICSLEDVNAIKPGKVTVAGYALSGGGRGIERVDISVDGGKTWVEASRYQKP 320

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 74099702  480 QRPRKA-------WAWRLWQLKAPVPAGQKelnIVCKAVDDGYNVQPDTVAPIWNLRGVLSNAWHRVHVYV 543
Cdd:PLN00177 321 GVPYISddissdkWAWVLFEATVDVPQSTE---IVAKAVDSAANVQPESVESIWNLRGILNTSWHRVQLRV 388
Oxidored_molyb pfam00174
Oxidoreductase molybdopterin binding domain; This domain is found in a variety of ...
 219-395 1.38e-64

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: 207.74  E-value: 1.38e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099702   219 HLPVPNLDPDTYRLHVVGApGGQSLSLSLDDLHNFPRYEITVTLQCAGNRRSEMTQVKevkGLEWRTGAISTARWAGARL 298
Cdd:pfam00174   1 HGPVPEIDPDTWRLRVDGL-VEKPLTLTLDDLKAFPQVTVTATLQCVGNRRKEMNRVK---GVQWGGGAIGNAEWTGVPL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099702   299 CDVLAQAGhqLCETEAHVCFEGLDSDPTGtAYGASIPLARAMDPEaeVLLAYEMNGQPLPRDHGFPVRVVVPGVVGARHV 378
Cdd:pfam00174  77 RDLLERAG--VKPGAKHVLFEGADTLGDG-GYTTSLPLEKALDDD--VLLAYEMNGEPLPPDHGYPLRLVVPGWYGARSV 151

                         170
                  ....*....|....*..
gi 74099702   379 KWLGRVSVQPEESYSHW 395
Cdd:pfam00174 152 KWLRRIEVTDEESPGFW 168
MsrP COG2041
Molybdopterin-dependent catalytic subunit of periplasmic DMSO/TMAO and ...
 214-405 2.44e-35

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: 130.66  E-value: 2.44e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099702 214 FFTRNHLPVPNLDPDTYRLHVVGApGGQSLSLSLDDLHNFPRYEITVTLQCAGNrrsemtqvkevkgleWRTGaisTARW 293
Cdd:COG2041  19 FPVRTAGGVPEIDPADWRLRVDGL-VEKPLTLTLDDLLALPLEERIYRLHCVEN---------------WSGG---VAPW 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099702 294 AGARLCDVLAQAGHQlceTEA-HVCFEGLDSDptgtaYGASIPLARAMDPEAevLLAYEMNGQPLPRDHGFPVRvvvpgv 372
Cdd:COG2041  80 TGVPLRDLLERAGPK---PGAkYVLFESADPG-----YTESLPLDEALDPDT--LLAYGMNGEPLPPEHGAPLR------ 143

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 74099702 373 vgAR--------HVKWLGRVSVQPEESYSHWQRRDYKGFSP 405
Cdd:COG2041 144 --LVvpglygfkSAKWLVRIEVTDEDPPGYWETRGYHFYAN 182
Cyt-b5 pfam00173
Cytochrome b5-like Heme/Steroid binding domain; This family includes heme binding domains from ...
 86-160 1.95e-18

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: 79.59  E-value: 1.95e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 74099702    86 TKEEVSSHTSPEtGIWVTLGSEVFDVTEFVDLHPGGPSKLMLAAGGPL-EPFWALyaVHNQSHVRELLAQYKIGEL 160
Cdd:pfam00173   1 TLEELSKHNGDG-DCWVAINGKVYDVTKFLKEHPGGEDVILSAAGKDAtDAFEAI--GHSEDAAEKLLKKYRIGEL 73
PLN03199 PLN03199
delta6-acyl-lipid desaturase-like protein; Provisional
 80-175 3.48e-06

delta6-acyl-lipid desaturase-like protein; Provisional


Pssm-ID: 178740 [Multi-domain]  Cd Length: 485  Bit Score: 49.65  E-value: 3.48e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099702   80 ESTHIYTKEEVSSHTSPETGiWVTLGSEVFDVTEFVDlHPGGPSKLMLAAGGPLEPFWALYAVHNQShvreLLAQYKIGE 159
Cdd:PLN03199  21 EKPQKISWQEVKKHASPDDA-WIIHQNKVYDVSNWHD-HPGGAVIFTHAGDDMTDIFAAFHAPGSQA----LMKKFYIGD 94

                         90
                 ....*....|....*.
gi 74099702  160 LNPEdkvapTVETSDP 175
Cdd:PLN03199  95 LIPE-----STEHKDP 105
 
Name Accession Description Interval E-value
eukary_SO_Moco cd02111
molybdopterin binding domain of sulfite oxidase (SO). SO catalyzes the terminal reaction in ...
 185-543 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: 598.22  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099702 185 ALKVNSQRPFNAEPPPELLTENYITPNPIFFTRNHLPVPNLDPDTYRLHVVGaPGGQSLSLSLDDLH-NFPRYEITVTLQ 263
Cdd:cd02111   1 ALKVNSKKPFNAEPPSSLLASSFITPNELFYVRNHLPVPVVDPDTYSLEVEG-PDGTTLSLSLEDLKsLFPKHEVTATLQ 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099702 264 CAGNRRSEMTQVKEVKGLEWRTGAISTARWAGARLCDVLAQAGHQLC--ETEAHVCFEGLDSDPTGTAYGASIPLARAMD 341
Cdd:cd02111  80 CAGNRRSEMTKVKKVKGLQWGDGAISNAEWGGARLRDVLLDAGIPEDdsQGGLHVHFEGLDVDPTGTPYGASIPLSKALD 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099702 342 PEAEVLLAYEMNGQPLPRDHGFPVRVVVPGVVGARHVKWLGRVSVQPEESYSHWQRRDYKGFSPSVDWETVDFDSAPSIQ 421
Cdd:cd02111 160 PEADVLLAYEMNGTPLPRDHGFPLRVVVPGVVGARSVKWLDRIVVSDEESDSHWQQNDYKGFSPSVDWDNVDFSKAPAIQ 239

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099702 422 ELPVQSAITEPRDGE---TVESGEVTIKGYAWSGGGRAVIRVDVSLDGGLTWQVAKLDGEEQR--PRKAWAWRLWQLKAP 496
Cdd:cd02111 240 EMPVQSAICSPSVGApvvTVPPGKITVKGYAWSGGGRKIVRVDVSLDGGRTWKVAELEQEENVwpSGRKWAWTLWEATVP 319

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*..
gi 74099702 497 VPAGqKELNIVCKAVDDGYNVQPDTVAPIWNLRGVLSNAWHRVHVYV 543
Cdd:cd02111 320 VPAG-KEAEIIAKAVDSAYNVQPETVEPIWNLRGVLNNAWHRVKVVV 365
PLN00177 PLN00177
sulfite oxidase; Provisional
 168-543 2.70e-123

sulfite oxidase; Provisional


Pssm-ID: 177772 [Multi-domain]  Cd Length: 393  Bit Score: 367.64  E-value: 2.70e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099702  168 PTVETSDPYADDPVRHPALKVNSQRPFNAEPPPELLTENYITPNPIFFTRNHLPVPNLDP-DTYRLHVVGAPGgQSLSLS 246
Cdd:PLN00177   2 PGLRGPSDYSQEPPRHPSLKINAKEPFNAEPPRSALVSSYITPVDLFYKRNHGPIPIVDDiERYSVTITGLIE-NPRKLS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099702  247 LDDLHNFPRYEITVTLQCAGNRRSEMTQVKEVKGLEWRTGAISTARWAGARLCDVLAQAG-HQLCETEA----HVCFEGL 321
Cdd:PLN00177  81 MKDIRKLPKYNVTATLQCAGNRRTAMSKVRKVRGVGWDVSAIGNAVWGGAKLADVLELVGiPKLTSITSsggkHVEFVSV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099702  322 DSDP--TGTAYGASIPLARAMDPEAEVLLAYEMNGQPLPRDHGFPVRVVVPGVVGARHVKWLGRVSVQPEESYSHWQRRD 399
Cdd:PLN00177 161 DKCKeeNGGPYKASIPLSQATNPEADVLLAYEMNGEVLNRDHGYPLRVVVPGVIGARSVKWLDSINIIAEECQGFFMQKD 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099702  400 YKGFSPSVDWETVDFDSAPSIQELPVQSAITEPRDGETVESGEVTIKGYAWSGGGRAVIRVDVSLDGGLTWQVAKLDGEE 479
Cdd:PLN00177 241 YKMFPPSVNWDNINWSTRRPQMDFPVQSAICSLEDVNAIKPGKVTVAGYALSGGGRGIERVDISVDGGKTWVEASRYQKP 320

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 74099702  480 QRPRKA-------WAWRLWQLKAPVPAGQKelnIVCKAVDDGYNVQPDTVAPIWNLRGVLSNAWHRVHVYV 543
Cdd:PLN00177 321 GVPYISddissdkWAWVLFEATVDVPQSTE---IVAKAVDSAANVQPESVESIWNLRGILNTSWHRVQLRV 388
SO_family_Moco_dimer cd02110
Subgroup of sulfite oxidase (SO) family molybdopterin binding domains that contains conserved ...
 213-541 4.57e-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: 335.81  E-value: 4.57e-112
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099702 213 IFFTRNHLPVPNLDPDTYRLHVVGApGGQSLSLSLDDLHNFPRYEITVTLQCAGNRRSEMTqvKEVKGLEWRTGAISTAR 292
Cdd:cd02110   1 LFFVRNHGGVPDIDPDAWRLEIHGL-VERPLTLTLDDLKRLPSVEVVATLECSGNGRGGFI--PVRSGAQWGHGAVGNAR 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099702 293 WAGARLCDVLAQAGHQlcETEAHVCFEGLDSDPTGTA--YGASIPLARAMDPEaeVLLAYEMNGQPLPRDHGFPVRVVVP 370
Cdd:cd02110  78 WTGVPLKDLLEEAGVK--PGAKHVLFEGADVPPGEKAadYTRSVPLSKALDDD--ALLAYEMNGEPLPPDHGYPLRLVVP 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099702 371 GVVGARHVKWLGRVSVQPEESYSHWQRRDYKGFSPSVDWetVDFDSAPSIQELPVQSAITEPRDGETVESGEVTIKGYAW 450
Cdd:cd02110 154 GWYGARSVKWLRRIEVTDQPSDGYWQTRDYTVPPPDVDA--VGGKARRPIGEMPVKSVITSPSPGAELVSGGRVEIGGVA 231

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099702 451 SGGGRAVIRVDVSLDGGLTWQVAKLDGEEQRPrkaWAWRLWQLKAPVPAGqkELNIVCKAVDDGYNVQPDTVAPIWNLRG 530
Cdd:cd02110 232 WSGGRGIRRVEVSLDGGRTWQEARLEGPLAGP---RAWRQWELDWDLPPG--EYELVARATDSTGNVQPERAEWNWNPGG 306

                       330
                ....*....|.
gi 74099702 531 VLSNAWHRVHV 541
Cdd:cd02110 307 YGNNHWHRVQV 317
PLN02252 PLN02252
nitrate reductase [NADPH]
 177-543 2.49e-97

nitrate reductase [NADPH]


Pssm-ID: 215141 [Multi-domain]  Cd Length: 888  Bit Score: 314.69  E-value: 2.49e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099702  177 ADDPV-RHPAL-KVNSQRPFNAEPP-PELLTENYITPNPIFFTRNHLPVPNLDPDTYRLHVVGAPGgQSLSLSLDDLHNF 253
Cdd:PLN02252  78 PDEWIpRHPSLvRLTGKHPFNCEPPlARLMEHGFITPAPLHYVRNHGAVPRADWDEWTVEVTGLVK-RPARLTMDELVRF 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099702  254 PRYEITVTLQCAGNRRSEMTQVKEVKGLEWRTGAISTARWAGARLCDVLAQAGHQLCETEA-HVCFEGLDSDPTG--TAY 330
Cdd:PLN02252 157 PARELPVTLVCAGNRRKEQNMVKQTIGFNWGAAGVSTSVWRGVRLRDVLRRCGVMSRKGGAlNVCFEGAEDLPGGggSKY 236

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099702  331 GASIPLARAMDPEAEVLLAYEMNGQPLPRDHGFPVRVVVPGVVGARHVKWLGRVSVQPEESYSHWQRRDYKGFSPSVDWE 410
Cdd:PLN02252 237 GTSITLERAMDPARDVILAYMQNGEPLTPDHGFPVRLIIPGFIGGRMVKWLKRIIVTTAESDNYYHYRDNRVLPSHVDAE 316

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099702  411 TVDFDS---APS--IQELPVQSAITEPRDGETVESGEVTI------KGYAWSGGGRAVIRVDVSLDGGLTWQVAKLDGEE 479
Cdd:PLN02252 317 LANAEGwwyKPEyiINELNINSVITTPAHDEILPINASTTqrpytmKGYAYSGGGRKVTRVEVSLDGGETWRLCDLDHPE 396

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 74099702  480 QRPR--KAWAWRLWQLKAPVP--AGQKElnIVCKAVDDGYNVQPDTvaPIWNLRGVLSNAWHRVHVYV 543
Cdd:PLN02252 397 KPTKygKYWCWCFWSLDVEVLdlLGAKE--IAVRAWDESMNTQPEK--LIWNLMGMMNNCWFRVKVNV 460
eukary_NR_Moco cd02112
molybdopterin binding domain of eukaryotic nitrate reductase (NR). Assimilatory NRs catalyze ...
 182-541 5.09e-97

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: 299.68  E-value: 5.09e-97
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099702 182 RHPAL-KVNSQRPFNAEPPP-ELLTENYITPNPIFFTRNHLPVPNLDPDTYRLHVVG---APggqsLSLSLDDLHN-FPR 255
Cdd:cd02112  11 RDPRLiRLTGKHPFNSEPPLtELMDHGFITPSNLHYVRNHGPVPREKWEDWTVEVTGlveKP----TTLTMDELVAmFPS 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099702 256 YEITVTLQCAGNRRSEMTQVKEVKGLEWRTGAISTARWAGARLCDVLAQAGHQLCETEA-HVCFEGLDSDPTG--TAYGA 332
Cdd:cd02112  87 VTFPVTLVCAGNRRKEQNMVKKTIGFNWGAAGTSTSLWTGVRLSDLLDRCGPKSPKGGArHVCFEGADDLLPGpnGKYGT 166

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099702 333 SIPLARAMDPEAEVLLAYEMNGQPLPRDHGFPVRVVVPGVVGARHVKWLGRVSVQPEESYSHWQRRDYKGFSPSVDWETV 412
Cdd:cd02112 167 SITLSWAMDPSKDVMLAYKQNGELLHPDHGFPVRLIIPGQIGGRMVKWLKRIVVSDRESQNHYHFHDNRVLPSHVDAELA 246

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099702 413 D-----FDSAPSIQELPVQSAITEPRDGETVE------SGEVTIKGYAWSGGGRAVIRVDVSLDGGLTWQVAKLDGEEQR 481
Cdd:cd02112 247 NeegwwYKPEYIINDLNVNSAITTPAHDEVLPlnglttAETYTMKGYAYAGGGRRVTRVEVSLDDGKSWKLASIDYPEDP 326

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 74099702 482 PR--KAWAWRLWQLKAPVPAGQKELNIVCKAVDDGYNVQPDTvaPIWNLRGVLSNAWHRVHV 541
Cdd:cd02112 327 TKygKCWCWCFWSLDVPLSELLAAKEICVRAWDESMNTQPRD--MTWNVMGMMNNCWFRVKI 386
Oxidored_molyb pfam00174
Oxidoreductase molybdopterin binding domain; This domain is found in a variety of ...
 219-395 1.38e-64

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: 207.74  E-value: 1.38e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099702   219 HLPVPNLDPDTYRLHVVGApGGQSLSLSLDDLHNFPRYEITVTLQCAGNRRSEMTQVKevkGLEWRTGAISTARWAGARL 298
Cdd:pfam00174   1 HGPVPEIDPDTWRLRVDGL-VEKPLTLTLDDLKAFPQVTVTATLQCVGNRRKEMNRVK---GVQWGGGAIGNAEWTGVPL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099702   299 CDVLAQAGhqLCETEAHVCFEGLDSDPTGtAYGASIPLARAMDPEaeVLLAYEMNGQPLPRDHGFPVRVVVPGVVGARHV 378
Cdd:pfam00174  77 RDLLERAG--VKPGAKHVLFEGADTLGDG-GYTTSLPLEKALDDD--VLLAYEMNGEPLPPDHGYPLRLVVPGWYGARSV 151

                         170
                  ....*....|....*..
gi 74099702   379 KWLGRVSVQPEESYSHW 395
Cdd:pfam00174 152 KWLRRIEVTDEESPGFW 168
Mo-co_dimer pfam03404
Mo-co oxidoreductase dimerization domain; This domain is found in molybdopterin cofactor ...
 418-544 2.26e-58

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: 190.65  E-value: 2.26e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099702   418 PSIQELPVQSAITEPRDGETVES----GEVTIKGYAWSGGGRAVIRVDVSLDGGLTWQVAKLDGEEQRPR------KAWA 487
Cdd:pfam03404   2 YAIYDLNVNSAICSPEHDEVVKLgaaqGTYTIKGYAYSGGGRRITRVEVSLDGGKTWRLAEIDYEEDPYRygewreKCWC 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 74099702   488 WRLWQLKAPVPAGQKELNIVCKAVDDGYNVQPDTvaPIWNLRGVLSNAWHRVHVYVS 544
Cdd:pfam03404  82 WCFWSLDIPVSDLLKAKEILVRAVDEAMNVQPED--MYWNVRGMMNNPWHRVKIHVE 136
SO_family_Moco cd00321
Sulfite oxidase (SO) family, molybdopterin binding domain. This molybdopterin cofactor (Moco) ...
 215-389 7.13e-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: 166.21  E-value: 7.13e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099702 215 FTRNHLPVP-NLDPDTYRLHVVGApGGQSLSLSLDDLHNFPRYEITVTLQCAGNRrsemtqvkevkgleWRTGAISTARW 293
Cdd:cd00321   1 FVRNHGGVPpEIDPDDWRLEVDGL-VEKPLSLTLDDLKALPQVEVIATLHCVGNR--------------WGGGAVSNAEW 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099702 294 AGARLCDVLAQAGHQlcETEAHVCFEGLDsDPTGTAYGASIPLARAMDPEaeVLLAYEMNGQPLPRDHGFPVRVVVPGVV 373
Cdd:cd00321  66 TGVPLRDLLEEAGPK--PGARYVVFEGAD-DPGGDGYTTSLPLEKALDPD--VLLAYEMNGEPLPPDHGFPLRLVVPGLY 140

                       170
                ....*....|....*.
gi 74099702 374 GARHVKWLGRVSVQPE 389
Cdd:cd00321 141 GWKSVKWLRRIEVTDE 156
bact_SorA_Moco cd02114
sulfite:cytochrome c oxidoreductase subunit A (SorA), molybdopterin binding domain. SorA is ...
 180-541 2.07e-48

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: 171.93  E-value: 2.07e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099702 180 PVRHPALKVNSqRPFNAEPPPELLTENYITPNPIFFTRNHLP-VP-NLDPDTYRLHVVGAPGgQSLSLSLDDLHNF-PRY 256
Cdd:cd02114  14 PQKRPLIRLTT-RPPHLETPFSVFNEGLITPNDAFFVRYHLAgIPlDIDPDAYTLTIDGKVR-TPLTLSLAELKRIePRF 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099702 257 EITVTLQCAGNRRSEMTqvKEVKGLEWRTGAISTARWAGARLCDVLAQAGHQLCETEahVCFEGLDSDP--TGTAYGASI 334
Cdd:cd02114  92 EVVAVNQCSGNSRGFFQ--PRVQGAQLANGAMGNARWAGVPLKAVLAKAGVQDGARQ--VAFRGLDQPVldVTPDFVKSL 167

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099702 335 PLARAMDPEaeVLLAYEMNGQPLPRDHGFPVRVVVPGVVGARHVKWLGRVSVQPEESYSHWQRRDYKgfSPSVDWETVDF 414
Cdd:cd02114 168 DIDHALDGE--VMLAWEMNGEPLPVLNGYPLRLVVPGFYATYWVKHLSHITVLDKEFDGFWASQAYR--IPDNADAGVEP 243

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099702 415 DSAPS----IQELPVQSAITEPRDGETVES-GEVTIKGYAWSgGGRAVIRVDVSLDGGLTWQVAKLDGEEQRprkaWAWR 489
Cdd:cd02114 244 GTAPDrtapINRFKVRSFITSLENGAIVAPaGELALRGIAFD-GGSGIRRVDVSADGGDSWTQATLGPDLGR----FSFR 318

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|..
gi 74099702 490 LWQLKAPVPAgQKELNIVCKAVDDGYNVQPDTVApiWNLRGVLSNAWHRVHV 541
Cdd:cd02114 319 GWKLTLDGVK-KGPLTLMVRATNNDGQTQPLRAP--WNPGGYMRNVVERTRI 367
bact_SoxC_Moco cd02113
bacterial SoxC is a member of the sulfite oxidase (SO) family of molybdopterin binding domains. ...
 208-533 8.97e-39

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: 144.46  E-value: 8.97e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099702 208 ITPNPIFFTRNHLPVPNLDPDTYRLHVVGAPGgQSLSLSLDDLHNFPRYEITVTLQCAGNRRSEMTQVKeVKGLEWRTGA 287
Cdd:cd02113   9 ITPNGLHFERHHGGVPDIDPAQHRLMIHGMVK-KPLVFTMDDLKRFPSVSRIYFLECSGNGGTGWRGAP-LPTAQYTHGM 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099702 288 ISTARWAGARLCDVLAQAGhqLCETEAHVCFEGLDsdptGTAYGASIPLARAMDpeaEVLLAYEMNGQPLPRDHGFPVRV 367
Cdd:cd02113  87 LSCSEWTGVPLSTLLEEAG--VKPGAKWLLAEGAD----AAAMTRSIPLEKALD---DALVAYAQNGEALRPENGYPLRL 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099702 368 VVPGVVGARHVKWLGRVSV--QPeesyshWQRRD----YKGFSPSVDWETVDFDSAPsiqelpvQSAITEPRDGETV-ES 440
Cdd:cd02113 158 VVPGWEGNTNVKWLRRIEVgdQP------WMTREetskYTDLLPDGRARQFSFVMEA-------KSVITSPSGGQRLrEP 224

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099702 441 GEVTIKGYAWSGGGRaVIRVDVSLDGGLTWQVAKLDGEEQ-----RPRKAWAWrlwqlkapvpaGQKELNIVCKAVDDGY 515
Cdd:cd02113 225 GFHEISGLAWSGRGR-IRRVDVSFDGGRTWQDARLEGPVLpkaltRFRLPWKW-----------DGRPAVLQSRATDETG 292

                       330
                ....*....|....*...
gi 74099702 516 NVQPdTVAPIWNLRGVLS 533
Cdd:cd02113 293 YVQP-TRAELRAVRGTNS 309
MsrP COG2041
Molybdopterin-dependent catalytic subunit of periplasmic DMSO/TMAO and ...
 214-405 2.44e-35

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: 130.66  E-value: 2.44e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099702 214 FFTRNHLPVPNLDPDTYRLHVVGApGGQSLSLSLDDLHNFPRYEITVTLQCAGNrrsemtqvkevkgleWRTGaisTARW 293
Cdd:COG2041  19 FPVRTAGGVPEIDPADWRLRVDGL-VEKPLTLTLDDLLALPLEERIYRLHCVEN---------------WSGG---VAPW 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099702 294 AGARLCDVLAQAGHQlceTEA-HVCFEGLDSDptgtaYGASIPLARAMDPEAevLLAYEMNGQPLPRDHGFPVRvvvpgv 372
Cdd:COG2041  80 TGVPLRDLLERAGPK---PGAkYVLFESADPG-----YTESLPLDEALDPDT--LLAYGMNGEPLPPEHGAPLR------ 143

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 74099702 373 vgAR--------HVKWLGRVSVQPEESYSHWQRRDYKGFSP 405
Cdd:COG2041 144 --LVvpglygfkSAKWLVRIEVTDEDPPGYWETRGYHFYAN 182
Cyt-b5 pfam00173
Cytochrome b5-like Heme/Steroid binding domain; This family includes heme binding domains from ...
 86-160 1.95e-18

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: 79.59  E-value: 1.95e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 74099702    86 TKEEVSSHTSPEtGIWVTLGSEVFDVTEFVDLHPGGPSKLMLAAGGPL-EPFWALyaVHNQSHVRELLAQYKIGEL 160
Cdd:pfam00173   1 TLEELSKHNGDG-DCWVAINGKVYDVTKFLKEHPGGEDVILSAAGKDAtDAFEAI--GHSEDAAEKLLKKYRIGEL 73
arch_bact_SO_family_Moco cd02109
bacterial and archael members of the sulfite oxidase (SO) family of molybdopterin binding ...
 198-400 6.00e-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: 78.83  E-value: 6.00e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099702 198 PPPELLTENYitpnPIFFTrnhLPVPNLDPDTYRLHVVGAPGGQsLSLSLDDLHNFPRYEITVTLQCagnrrsemtqvke 277
Cdd:cd02109   2 PPGQYLTEKF----PVLDA---GDVPEVDLEKWRLRVTGLVENP-LSLTYEDLLALPQTEYTADFHC------------- 60

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099702 278 VKGleWrtgAISTARWAGARLCDVLAQAGhqLCETEAHVCFEGLDsdptgtAYGASIPLARAMDPEAevLLAYEMNGQPL 357
Cdd:cd02109  61 VTG--W---SKLDVVWEGVSLKDLLEAAR--PDPEATFVMAHSYD------GYTTNLPLEDLLREDS--LLATKMDGEPL 125

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 74099702 358 PRDHGFPVRVVVPGVVGARHVKWLGRVSVQPEESYSHWQRRDY 400
Cdd:cd02109 126 PPEHGGPARLVVPHLYFWKSAKWLRGIEFLDEDEPGFWERRGY 168
bact_SO_family_Moco cd02108
bacterial subgroup of the sulfite oxidase (SO) family of molybdopterin binding domains. This ...
 215-363 2.77e-14

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: 71.26  E-value: 2.77e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099702 215 FTRNHLPVPNL---------DPDTYRLHVvgapGG---QSLSLSLDDLHNFPRyeitvtlqcagnrRSEMTQVKEVKGle 282
Cdd:cd02108   5 FRRNGIRKPEAlaykaleanDFADYRLEV----GGlveHPLSLSLEELRALPQ-------------RTQITRHICVEG-- 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099702 283 WrtGAIstARWAGARLCDVLAQAGhqlCETEA-HVCFEGLDSDPTGTAYGASIPLARAMDPEAevLLAYEMNGQPLPRDH 361
Cdd:cd02108  66 W--SAI--GKWGGVPLRTILELVG---PLPEAkYVVFKCADDFAGGDRYYESIDMASALHPQT--LLAYEMNGQPLPIKN 136


                ..
gi 74099702 362 GF 363
Cdd:cd02108 137 GA 138
PLN02252 PLN02252
nitrate reductase [NADPH]
 77-246 1.20e-11

nitrate reductase [NADPH]


Pssm-ID: 215141 [Multi-domain]  Cd Length: 888  Bit Score: 67.39  E-value: 1.20e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099702   77 AAQESTHIYTKEEVSSHTSPETgIWVTLGSEVFDVTEFVDLHPGGPSKLMLAAGGP-LEPFwalYAVHNqSHVRELLAQY 155
Cdd:PLN02252 512 NTNTGSKQYTMSEVRKHNSEDS-CWIVVHGHVYDCTRFLKDHPGGADSILINAGTDcTEEF---DAIHS-DKAKKMLEDY 586

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099702  156 KIGELnpedkvaptVETSDPYADDPVRHPALKVNSQRPFNAEPPPellTENYITPNPifftRNHLPVP-----NLDPDTY 230
Cdd:PLN02252 587 RIGEL---------VTTGAAASSSASSHPLSAISTASALAAASPA---PGRPVALNP----REKIPCRlvekiSLSHDVR 650

                        170       180
                 ....*....|....*....|....
gi 74099702  231 RL--------HVVGAPGGQSLSLS 246
Cdd:PLN02252 651 LFrfalpsedHVLGLPVGKHVFLC 674
PLN03199 PLN03199
delta6-acyl-lipid desaturase-like protein; Provisional
 80-175 3.48e-06

delta6-acyl-lipid desaturase-like protein; Provisional


Pssm-ID: 178740 [Multi-domain]  Cd Length: 485  Bit Score: 49.65  E-value: 3.48e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099702   80 ESTHIYTKEEVSSHTSPETGiWVTLGSEVFDVTEFVDlHPGGPSKLMLAAGGPLEPFWALYAVHNQShvreLLAQYKIGE 159
Cdd:PLN03199  21 EKPQKISWQEVKKHASPDDA-WIIHQNKVYDVSNWHD-HPGGAVIFTHAGDDMTDIFAAFHAPGSQA----LMKKFYIGD 94

                         90
                 ....*....|....*.
gi 74099702  160 LNPEdkvapTVETSDP 175
Cdd:PLN03199  95 LIPE-----STEHKDP 105
COG3915 COG3915
Uncharacterized conserved protein [Function unknown];
220-362 2.54e-05

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443120  Cd Length: 167  Bit Score: 44.88  E-value: 2.54e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099702 220 LPVPNLDPDtyrLHVVGAPG----GQSLSLSLDDLHNFPRYEITVTLqcagnrrsemtqvkevkglEWRTGAIstaRWAG 295
Cdd:COG3915  24 LPAPAGPVI---LTVSGKIGntnaGGAATFDLAMLEALPQTEITTTT-------------------PWTDGVQ---TFRG 78

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 74099702 296 ARLCDVLAQAGhqlcETEAHVCFEGLDsdptgtAYGASIPLARAMdpEAEVLLAYEMNGQPLP-RDHG 362
Cdd:COG3915  79 VLLRDLLAAVG----AKGTTLRAVALN------DYAVEIPISDLE--EYGVILAYRMDGKPMSvRDKG 134
PLN03198 PLN03198
delta6-acyl-lipid desaturase; Provisional
 49-178 3.16e-05

delta6-acyl-lipid desaturase; Provisional


Pssm-ID: 178739 [Multi-domain]  Cd Length: 526  Bit Score: 46.61  E-value: 3.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74099702   49 NSSTQGwrvmgTLLGLGAVLAYQDHRCRAAQESTHIYTKEEVSSHTSPeTGIWVTLGSEVFDVTEFVDLHPGGPSKLMLA 128
Cdd:PLN03198  75 NSNSQE-----AAEALAESVVKPTRRRSSKEKKSKSHLLSEVAAHNKP-NDCWIVIKNKVYDVSDFAAEHPGGSVISTYF 148

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 74099702  129 AGGPLEPFWALYAvhnqSHVRELLAQYKIGELnpeDKVAPTVETSDPYAD 178
Cdd:PLN03198 149 GRDGTDAFSSFHA----ASTWKILQDFYIGDV---DNVEPTPELLKDFRD 191
Big_7 pfam17957
Bacterial Ig domain; This entry represents a bacterial ig-like domain that is found in ...
 428-469 9.89e-03

Bacterial Ig domain; This entry represents a bacterial ig-like domain that is found in glycosyl hydrolase enzymes.


Pssm-ID: 436171 [Multi-domain]  Cd Length: 67  Bit Score: 34.89  E-value: 9.89e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 74099702   428 AITEPRDGETVESGEVTIKGYAwSGGGrAVIRVDVSLDGGLT 469
Cdd:pfam17957   2 SITSPANGATVSGGTVTISATA-SDDG-GVSKVEFYVDGTLV 41
 
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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