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Conserved domains on  [gi|494648283|ref|WP_007406227|]
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MULTISPECIES: molybdopterin-dependent oxidoreductase [Alphaproteobacteria]

Protein Classification

molybdopterin-binding protein( domain architecture ID 1861)

molybdopterin-binding protein similar to sulfite oxidase and nitrite reductase that catalyze the transfer of an oxygen to or from a lone pair of electrons on the substrate

Gene Ontology:  GO:0043546
PubMed:  9242907

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SO_family_Moco super family cl00199
Sulfite oxidase (SO) family, molybdopterin binding domain. This molybdopterin cofactor (Moco) ...
 7-354 2.62e-113

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.


The actual alignment was detected with superfamily member cd02111:

Pssm-ID: 469652 [Multi-domain]  Cd Length: 365  Bit Score: 333.97  E-value: 2.62e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494648283   7 RSSDPYNAEPTPGALIERFLTPQALFYVRSHGPVPDL-PANHRIEVSGRGMASRFFSVQELKSTFATRTVTAVLQCAGNR 85
Cdd:cd02111    5 NSKKPFNAEPPSSLLASSFITPNELFYVRNHLPVPVVdPDTYSLEVEGPDGTTLSLSLEDLKSLFPKHEVTATLQCAGNR 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494648283  86 RTDLQQVANTSGDPWDVGAIGNAEWTGVRLADVLDAVGAPDAS---ELFVAFTGADeVDVEGEEalFGVSIAMSKAREP- 161
Cdd:cd02111   85 RSEMTKVKKVKGLQWGDGAISNAEWGGARLRDVLLDAGIPEDDsqgGLHVHFEGLD-VDPTGTP--YGASIPLSKALDPe 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494648283 162 -DVLLAWAMNGEPLTPEHGAPLRMVVPGYAGVRSAKWLTRIEVRETPSEAPIQAHDYKLFPAAVTSDTVDWSQGLTINAM 240
Cdd:cd02111  162 aDVLLAYEMNGTPLPRDHGFPLRVVVPGVVGARSVKWLDRIVVSDEESDSHWQQNDYKGFSPSVDWDNVDFSKAPAIQEM 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494648283 241 PLNAAICSPGAGESLAA---GEVRIEGYAIAYD-RRISRIEVSVNGGRDWQQATF-----ADDPETRWGWRRWILDATLA 311
Cdd:cd02111  242 PVQSAICSPSVGAPVVTvppGKITVKGYAWSGGgRKIVRVDVSLDGGRTWKVAELeqeenVWPSGRKWAWTLWEATVPVP 321

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 494648283 312 KGRQ-HLVARAFDETGQGQPERPDTMWNFAGYLCTAWHHVHVLV 354
Cdd:cd02111  322 AGKEaEIIAKAVDSAYNVQPETVEPIWNLRGVLNNAWHRVKVVV 365
 
Name Accession Description Interval E-value
eukary_SO_Moco cd02111
molybdopterin binding domain of sulfite oxidase (SO). SO catalyzes the terminal reaction in ...
 7-354 2.62e-113

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: 333.97  E-value: 2.62e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494648283   7 RSSDPYNAEPTPGALIERFLTPQALFYVRSHGPVPDL-PANHRIEVSGRGMASRFFSVQELKSTFATRTVTAVLQCAGNR 85
Cdd:cd02111    5 NSKKPFNAEPPSSLLASSFITPNELFYVRNHLPVPVVdPDTYSLEVEGPDGTTLSLSLEDLKSLFPKHEVTATLQCAGNR 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494648283  86 RTDLQQVANTSGDPWDVGAIGNAEWTGVRLADVLDAVGAPDAS---ELFVAFTGADeVDVEGEEalFGVSIAMSKAREP- 161
Cdd:cd02111   85 RSEMTKVKKVKGLQWGDGAISNAEWGGARLRDVLLDAGIPEDDsqgGLHVHFEGLD-VDPTGTP--YGASIPLSKALDPe 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494648283 162 -DVLLAWAMNGEPLTPEHGAPLRMVVPGYAGVRSAKWLTRIEVRETPSEAPIQAHDYKLFPAAVTSDTVDWSQGLTINAM 240
Cdd:cd02111  162 aDVLLAYEMNGTPLPRDHGFPLRVVVPGVVGARSVKWLDRIVVSDEESDSHWQQNDYKGFSPSVDWDNVDFSKAPAIQEM 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494648283 241 PLNAAICSPGAGESLAA---GEVRIEGYAIAYD-RRISRIEVSVNGGRDWQQATF-----ADDPETRWGWRRWILDATLA 311
Cdd:cd02111  242 PVQSAICSPSVGAPVVTvppGKITVKGYAWSGGgRKIVRVDVSLDGGRTWKVAELeqeenVWPSGRKWAWTLWEATVPVP 321

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 494648283 312 KGRQ-HLVARAFDETGQGQPERPDTMWNFAGYLCTAWHHVHVLV 354
Cdd:cd02111  322 AGKEaEIIAKAVDSAYNVQPETVEPIWNLRGVLNNAWHRVKVVV 365
PLN00177 PLN00177
sulfite oxidase; Provisional
 8-354 1.12e-90

sulfite oxidase; Provisional


Pssm-ID: 177772 [Multi-domain]  Cd Length: 393  Bit Score: 277.12  E-value: 1.12e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494648283   8 SSDPYNAEPTPGALIERFLTPQALFYVRSHGPVPDLPANHRIEVSGRGMA--SRFFSVQELKStFATRTVTAVLQCAGNR 85
Cdd:PLN00177  24 AKEPFNAEPPRSALVSSYITPVDLFYKRNHGPIPIVDDIERYSVTITGLIenPRKLSMKDIRK-LPKYNVTATLQCAGNR 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494648283  86 RTDLQQVANTSGDPWDVGAIGNAEWTGVRLADVLDAVGAPDASEL------FVAFTGADEVDvEGEEALFGVSIAMSKAR 159
Cdd:PLN00177 103 RTAMSKVRKVRGVGWDVSAIGNAVWGGAKLADVLELVGIPKLTSItssggkHVEFVSVDKCK-EENGGPYKASIPLSQAT 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494648283 160 EP--DVLLAWAMNGEPLTPEHGAPLRMVVPGYAGVRSAKWLTRIEVRETPSEAPIQAHDYKLFPAAVTSDTVDWSQGLTI 237
Cdd:PLN00177 182 NPeaDVLLAYEMNGEVLNRDHGYPLRVVVPGVIGARSVKWLDSINIIAEECQGFFMQKDYKMFPPSVNWDNINWSTRRPQ 261

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494648283 238 NAMPLNAAICSPGAGESLAAGEVRIEGYAIA-YDRRISRIEVSVNGGRDWQQAT---------FADDPET-RWGWRrwIL 306
Cdd:PLN00177 262 MDFPVQSAICSLEDVNAIKPGKVTVAGYALSgGGRGIERVDISVDGGKTWVEASryqkpgvpyISDDISSdKWAWV--LF 339

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 494648283 307 DATL-AKGRQHLVARAFDETGQGQPERPDTMWNFAGYLCTAWHHVHVLV 354
Cdd:PLN00177 340 EATVdVPQSTEIVAKAVDSAANVQPESVESIWNLRGILNTSWHRVQLRV 388
Oxidored_molyb pfam00174
Oxidoreductase molybdopterin binding domain; This domain is found in a variety of ...
 37-211 8.94e-73

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: 223.15  E-value: 8.94e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494648283   37 HGPVPDL-PANHRIEVSGRGMASRFFSVQELKStFATRTVTAVLQCAGNRRTDLQQVantSGDPWDVGAIGNAEWTGVRL 115
Cdd:pfam00174   1 HGPVPEIdPDTWRLRVDGLVEKPLTLTLDDLKA-FPQVTVTATLQCVGNRRKEMNRV---KGVQWGGGAIGNAEWTGVPL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494648283  116 ADVLDAVGaPDASELFVAFTGADEVDVEGeealFGVSIAMSKAREPDVLLAWAMNGEPLTPEHGAPLRMVVPGYAGVRSA 195
Cdd:pfam00174  77 RDLLERAG-VKPGAKHVLFEGADTLGDGG----YTTSLPLEKALDDDVLLAYEMNGEPLPPDHGYPLRLVVPGWYGARSV 151

                         170
                  ....*....|....*.
gi 494648283  196 KWLTRIEVRETPSEAP 211
Cdd:pfam00174 152 KWLRRIEVTDEESPGF 167
MsrP COG2041
Molybdopterin-dependent catalytic subunit of periplasmic DMSO/TMAO and ...
 24-217 5.29e-50

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: 165.33  E-value: 5.29e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494648283  24 RFLTPQALFY-VRSHGPVPDL-PANHRIEVSGRGMASRFFSVQELKStFATRTVTAVLQCAGNRRtdlqqvantsgdpwd 101
Cdd:COG2041   10 RFLKGGALAFpVRTAGGVPEIdPADWRLRVDGLVEKPLTLTLDDLLA-LPLEERIYRLHCVENWS--------------- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494648283 102 vgaIGNAEWTGVRLADVLDAVGaPDASELFVAFTGADEVdvegeealFGVSIAMSKAREPDVLLAWAMNGEPLTPEHGAP 181
Cdd:COG2041   74 ---GGVAPWTGVPLRDLLERAG-PKPGAKYVLFESADPG--------YTESLPLDEALDPDTLLAYGMNGEPLPPEHGAP 141

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 494648283 182 LRMVVPGYAGVRSAKWLTRIEVRETPSEAPIQAHDY 217
Cdd:COG2041  142 LRLVVPGLYGFKSAKWLVRIEVTDEDPPGYWETRGY 177
 
Name Accession Description Interval E-value
eukary_SO_Moco cd02111
molybdopterin binding domain of sulfite oxidase (SO). SO catalyzes the terminal reaction in ...
 7-354 2.62e-113

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: 333.97  E-value: 2.62e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494648283   7 RSSDPYNAEPTPGALIERFLTPQALFYVRSHGPVPDL-PANHRIEVSGRGMASRFFSVQELKSTFATRTVTAVLQCAGNR 85
Cdd:cd02111    5 NSKKPFNAEPPSSLLASSFITPNELFYVRNHLPVPVVdPDTYSLEVEGPDGTTLSLSLEDLKSLFPKHEVTATLQCAGNR 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494648283  86 RTDLQQVANTSGDPWDVGAIGNAEWTGVRLADVLDAVGAPDAS---ELFVAFTGADeVDVEGEEalFGVSIAMSKAREP- 161
Cdd:cd02111   85 RSEMTKVKKVKGLQWGDGAISNAEWGGARLRDVLLDAGIPEDDsqgGLHVHFEGLD-VDPTGTP--YGASIPLSKALDPe 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494648283 162 -DVLLAWAMNGEPLTPEHGAPLRMVVPGYAGVRSAKWLTRIEVRETPSEAPIQAHDYKLFPAAVTSDTVDWSQGLTINAM 240
Cdd:cd02111  162 aDVLLAYEMNGTPLPRDHGFPLRVVVPGVVGARSVKWLDRIVVSDEESDSHWQQNDYKGFSPSVDWDNVDFSKAPAIQEM 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494648283 241 PLNAAICSPGAGESLAA---GEVRIEGYAIAYD-RRISRIEVSVNGGRDWQQATF-----ADDPETRWGWRRWILDATLA 311
Cdd:cd02111  242 PVQSAICSPSVGAPVVTvppGKITVKGYAWSGGgRKIVRVDVSLDGGRTWKVAELeqeenVWPSGRKWAWTLWEATVPVP 321

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 494648283 312 KGRQ-HLVARAFDETGQGQPERPDTMWNFAGYLCTAWHHVHVLV 354
Cdd:cd02111  322 AGKEaEIIAKAVDSAYNVQPETVEPIWNLRGVLNNAWHRVKVVV 365
SO_family_Moco_dimer cd02110
Subgroup of sulfite oxidase (SO) family molybdopterin binding domains that contains conserved ...
 31-352 2.80e-111

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: 326.95  E-value: 2.80e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494648283  31 LFYVRSHGPVPDL-PANHRIEVSGRGMASRFFSVQELKStFATRTVTAVLQCAGNRRTDLQQVanTSGDPWDVGAIGNAE 109
Cdd:cd02110    1 LFFVRNHGGVPDIdPDAWRLEIHGLVERPLTLTLDDLKR-LPSVEVVATLECSGNGRGGFIPV--RSGAQWGHGAVGNAR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494648283 110 WTGVRLADVLDAVGAPDASeLFVAFTGADeVDVEGEEALFGVSIAMSKAREPDVLLAWAMNGEPLTPEHGAPLRMVVPGY 189
Cdd:cd02110   78 WTGVPLKDLLEEAGVKPGA-KHVLFEGAD-VPPGEKAADYTRSVPLSKALDDDALLAYEMNGEPLPPDHGYPLRLVVPGW 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494648283 190 AGVRSAKWLTRIEVRETPSEAPIQAHDYKLFPAAVtsDTVDWSQGLTINAMPLNAAICSPGAG-ESLAAGEVRIEGYAIA 268
Cdd:cd02110  156 YGARSVKWLRRIEVTDQPSDGYWQTRDYTVPPPDV--DAVGGKARRPIGEMPVKSVITSPSPGaELVSGGRVEIGGVAWS 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494648283 269 YDRRISRIEVSVNGGRDWQQATFADDPETRWGWRRWILDATLAKGRQHLVARAFDETGQGQPERPDTMWNFAGYLCTAWH 348
Cdd:cd02110  234 GGRGIRRVEVSLDGGRTWQEARLEGPLAGPRAWRQWELDWDLPPGEYELVARATDSTGNVQPERAEWNWNPGGYGNNHWH 313


                 ....
gi 494648283 349 HVHV 352
Cdd:cd02110  314 RVQV 317
PLN00177 PLN00177
sulfite oxidase; Provisional
 8-354 1.12e-90

sulfite oxidase; Provisional


Pssm-ID: 177772 [Multi-domain]  Cd Length: 393  Bit Score: 277.12  E-value: 1.12e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494648283   8 SSDPYNAEPTPGALIERFLTPQALFYVRSHGPVPDLPANHRIEVSGRGMA--SRFFSVQELKStFATRTVTAVLQCAGNR 85
Cdd:PLN00177  24 AKEPFNAEPPRSALVSSYITPVDLFYKRNHGPIPIVDDIERYSVTITGLIenPRKLSMKDIRK-LPKYNVTATLQCAGNR 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494648283  86 RTDLQQVANTSGDPWDVGAIGNAEWTGVRLADVLDAVGAPDASEL------FVAFTGADEVDvEGEEALFGVSIAMSKAR 159
Cdd:PLN00177 103 RTAMSKVRKVRGVGWDVSAIGNAVWGGAKLADVLELVGIPKLTSItssggkHVEFVSVDKCK-EENGGPYKASIPLSQAT 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494648283 160 EP--DVLLAWAMNGEPLTPEHGAPLRMVVPGYAGVRSAKWLTRIEVRETPSEAPIQAHDYKLFPAAVTSDTVDWSQGLTI 237
Cdd:PLN00177 182 NPeaDVLLAYEMNGEVLNRDHGYPLRVVVPGVIGARSVKWLDSINIIAEECQGFFMQKDYKMFPPSVNWDNINWSTRRPQ 261

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494648283 238 NAMPLNAAICSPGAGESLAAGEVRIEGYAIA-YDRRISRIEVSVNGGRDWQQAT---------FADDPET-RWGWRrwIL 306
Cdd:PLN00177 262 MDFPVQSAICSLEDVNAIKPGKVTVAGYALSgGGRGIERVDISVDGGKTWVEASryqkpgvpyISDDISSdKWAWV--LF 339

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 494648283 307 DATL-AKGRQHLVARAFDETGQGQPERPDTMWNFAGYLCTAWHHVHVLV 354
Cdd:PLN00177 340 EATVdVPQSTEIVAKAVDSAANVQPESVESIWNLRGILNTSWHRVQLRV 388
eukary_NR_Moco cd02112
molybdopterin binding domain of eukaryotic nitrate reductase (NR). Assimilatory NRs catalyze ...
 11-352 3.45e-90

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: 275.42  E-value: 3.45e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494648283  11 PYNAEPTPGALIER-FLTPQALFYVRSHGPVPDLP-ANHRIEVSGRGMASRFFSVQELKSTFATRTVTAVLQCAGNRRTD 88
Cdd:cd02112   23 PFNSEPPLTELMDHgFITPSNLHYVRNHGPVPREKwEDWTVEVTGLVEKPTTLTMDELVAMFPSVTFPVTLVCAGNRRKE 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494648283  89 LQQVANTSGDPWDVGAIGNAEWTGVRLADVLDAVG--APDASELFVAFTGADEVDVEGEEAlFGVSIAMSKAREP--DVL 164
Cdd:cd02112  103 QNMVKKTIGFNWGAAGTSTSLWTGVRLSDLLDRCGpkSPKGGARHVCFEGADDLLPGPNGK-YGTSITLSWAMDPskDVM 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494648283 165 LAWAMNGEPLTPEHGAPLRMVVPGYAGVRSAKWLTRIEVRETPSEAPIQAHDYKLFPAAVTSDTVD----WSQG-LTINA 239
Cdd:cd02112  182 LAYKQNGELLHPDHGFPVRLIIPGQIGGRMVKWLKRIVVSDRESQNHYHFHDNRVLPSHVDAELANeegwWYKPeYIIND 261

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494648283 240 MPLNAAICSPGAGESL------AAGEVRIEGYAIA-YDRRISRIEVSVNGGRDWQQA--TFADDPETR---WGWRRWILD 307
Cdd:cd02112  262 LNVNSAITTPAHDEVLplngltTAETYTMKGYAYAgGGRRVTRVEVSLDDGKSWKLAsiDYPEDPTKYgkcWCWCFWSLD 341

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 494648283 308 ATLA--KGRQHLVARAFDETGQGQPErpDTMWNFAGYLCTAWHHVHV 352
Cdd:cd02112  342 VPLSelLAAKEICVRAWDESMNTQPR--DMTWNVMGMMNNCWFRVKI 386
Oxidored_molyb pfam00174
Oxidoreductase molybdopterin binding domain; This domain is found in a variety of ...
 37-211 8.94e-73

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: 223.15  E-value: 8.94e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494648283   37 HGPVPDL-PANHRIEVSGRGMASRFFSVQELKStFATRTVTAVLQCAGNRRTDLQQVantSGDPWDVGAIGNAEWTGVRL 115
Cdd:pfam00174   1 HGPVPEIdPDTWRLRVDGLVEKPLTLTLDDLKA-FPQVTVTATLQCVGNRRKEMNRV---KGVQWGGGAIGNAEWTGVPL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494648283  116 ADVLDAVGaPDASELFVAFTGADEVDVEGeealFGVSIAMSKAREPDVLLAWAMNGEPLTPEHGAPLRMVVPGYAGVRSA 195
Cdd:pfam00174  77 RDLLERAG-VKPGAKHVLFEGADTLGDGG----YTTSLPLEKALDDDVLLAYEMNGEPLPPDHGYPLRLVVPGWYGARSV 151

                         170
                  ....*....|....*.
gi 494648283  196 KWLTRIEVRETPSEAP 211
Cdd:pfam00174 152 KWLRRIEVTDEESPGF 167
PLN02252 PLN02252
nitrate reductase [NADPH]
 3-352 2.84e-71

nitrate reductase [NADPH]


Pssm-ID: 215141 [Multi-domain]  Cd Length: 888  Bit Score: 238.04  E-value: 2.84e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494648283   3 DMIERSSD--------PYNAEPTPGALIE-RFLTPQALFYVRSHGPVPDLP-ANHRIEVSGRGMASRFFSVQELKStFAT 72
Cdd:PLN02252  80 EWIPRHPSlvrltgkhPFNCEPPLARLMEhGFITPAPLHYVRNHGAVPRADwDEWTVEVTGLVKRPARLTMDELVR-FPA 158

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494648283  73 RTVTAVLQCAGNRRTDLQQVANTSGDPWDVGAIGNAEWTGVRLADVLDAVG--APDASELFVAFTGADEVDvEGEEALFG 150
Cdd:PLN02252 159 RELPVTLVCAGNRRKEQNMVKQTIGFNWGAAGVSTSVWRGVRLRDVLRRCGvmSRKGGALNVCFEGAEDLP-GGGGSKYG 237

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494648283 151 VSIAMSKAREP--DVLLAWAMNGEPLTPEHGAPLRMVVPGYAGVRSAKWLTRIEVRETPSEAPIQAHDYKLFPAAVTSDT 228
Cdd:PLN02252 238 TSITLERAMDParDVILAYMQNGEPLTPDHGFPVRLIIPGFIGGRMVKWLKRIIVTTAESDNYYHYRDNRVLPSHVDAEL 317

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494648283 229 VDwSQG------LTINAMPLNAAICSPGAGESLAAGEVRIE------GYaiAYD---RRISRIEVSVNGGRDWQQATFaD 293
Cdd:PLN02252 318 AN-AEGwwykpeYIINELNINSVITTPAHDEILPINASTTQrpytmkGY--AYSgggRKVTRVEVSLDGGETWRLCDL-D 393

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 494648283 294 DPE--TR----WGWRRWILDATLAK--GRQHLVARAFDETGQGQPERPdtMWNFAGYLCTAWHHVHV 352
Cdd:PLN02252 394 HPEkpTKygkyWCWCFWSLDVEVLDllGAKEIAVRAWDESMNTQPEKL--IWNLMGMMNNCWFRVKV 458
SO_family_Moco cd00321
Sulfite oxidase (SO) family, molybdopterin binding domain. This molybdopterin cofactor (Moco) ...
 33-205 6.39e-60

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: 190.09  E-value: 6.39e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494648283  33 YVRSHGPVPDL--PANHRIEVSGRGMASRFFSVQELKsTFATRTVTAVLQCAGNRrtdlqqvantsgdpWDVGAIGNAEW 110
Cdd:cd00321    1 FVRNHGGVPPEidPDDWRLEVDGLVEKPLSLTLDDLK-ALPQVEVIATLHCVGNR--------------WGGGAVSNAEW 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494648283 111 TGVRLADVLDAVGaPDASELFVAFTGADEVDVEGeealFGVSIAMSKAREPDVLLAWAMNGEPLTPEHGAPLRMVVPGYA 190
Cdd:cd00321   66 TGVPLRDLLEEAG-PKPGARYVVFEGADDPGGDG----YTTSLPLEKALDPDVLLAYEMNGEPLPPDHGFPLRLVVPGLY 140

                        170
                 ....*....|....*
gi 494648283 191 GVRSAKWLTRIEVRE 205
Cdd:cd00321  141 GWKSVKWLRRIEVTD 155
MsrP COG2041
Molybdopterin-dependent catalytic subunit of periplasmic DMSO/TMAO and ...
 24-217 5.29e-50

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: 165.33  E-value: 5.29e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494648283  24 RFLTPQALFY-VRSHGPVPDL-PANHRIEVSGRGMASRFFSVQELKStFATRTVTAVLQCAGNRRtdlqqvantsgdpwd 101
Cdd:COG2041   10 RFLKGGALAFpVRTAGGVPEIdPADWRLRVDGLVEKPLTLTLDDLLA-LPLEERIYRLHCVENWS--------------- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494648283 102 vgaIGNAEWTGVRLADVLDAVGaPDASELFVAFTGADEVdvegeealFGVSIAMSKAREPDVLLAWAMNGEPLTPEHGAP 181
Cdd:COG2041   74 ---GGVAPWTGVPLRDLLERAG-PKPGAKYVLFESADPG--------YTESLPLDEALDPDTLLAYGMNGEPLPPEHGAP 141

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 494648283 182 LRMVVPGYAGVRSAKWLTRIEVRETPSEAPIQAHDY 217
Cdd:COG2041  142 LRLVVPGLYGFKSAKWLVRIEVTDEDPPGYWETRGY 177
bact_SorA_Moco cd02114
sulfite:cytochrome c oxidoreductase subunit A (SorA), molybdopterin binding domain. SorA is ...
 23-342 2.37e-49

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: 169.61  E-value: 2.37e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494648283  23 ERFLTPQALFYVRSH---GPVPDLPANHRIEVSGRGMASRFFSVQELKSTFATRTVTAVLQCAGNRRTDLQ------QVA 93
Cdd:cd02114   38 EGLITPNDAFFVRYHlagIPLDIDPDAYTLTIDGKVRTPLTLSLAELKRIEPRFEVVAVNQCSGNSRGFFQprvqgaQLA 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494648283  94 NtsgdpwdvGAIGNAEWTGVRLADVLDAVGAPDASELfVAFTGADEVDVEGEEAlFGVSIAMSKAREPDVLLAWAMNGEP 173
Cdd:cd02114  118 N--------GAMGNARWAGVPLKAVLAKAGVQDGARQ-VAFRGLDQPVLDVTPD-FVKSLDIDHALDGEVMLAWEMNGEP 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494648283 174 LTPEHGAPLRMVVPGYAGVRSAKWLTRIEVRETPSEAPIQAHDYKL--FPAAVTSDTVDWSQGLTINAMPLNAAICSPGA 251
Cdd:cd02114  188 LPVLNGYPLRLVVPGFYATYWVKHLSHITVLDKEFDGFWASQAYRIpdNADAGVEPGTAPDRTAPINRFKVRSFITSLEN 267

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494648283 252 G-ESLAAGEVRIEGYAIAYDRRISRIEVSVNGGRDWQQATFADDPeTRWGWRRWILDATL-AKGRQHLVARAFDETGQGQ 329
Cdd:cd02114  268 GaIVAPAGELALRGIAFDGGSGIRRVDVSADGGDSWTQATLGPDL-GRFSFRGWKLTLDGvKKGPLTLMVRATNNDGQTQ 346

                        330
                 ....*....|...
gi 494648283 330 PERpdTMWNFAGY 342
Cdd:cd02114  347 PLR--APWNPGGY 357
bact_SoxC_Moco cd02113
bacterial SoxC is a member of the sulfite oxidase (SO) family of molybdopterin binding domains. ...
 26-332 5.07e-47

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: 162.18  E-value: 5.07e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494648283  26 LTPQALFYVRSHGPVPDL-PANHRIEVSGRGMASRFFSVQELKStFATRTVTAVLQCAGNRRTDLQQVA-NTSGDPwdVG 103
Cdd:cd02113    9 ITPNGLHFERHHGGVPDIdPAQHRLMIHGMVKKPLVFTMDDLKR-FPSVSRIYFLECSGNGGTGWRGAPlPTAQYT--HG 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494648283 104 AIGNAEWTGVRLADVLDAVGAPDASELFVAfTGADEvdvegeeALFGVSIAMSKAREpDVLLAWAMNGEPLTPEHGAPLR 183
Cdd:cd02113   86 MLSCSEWTGVPLSTLLEEAGVKPGAKWLLA-EGADA-------AAMTRSIPLEKALD-DALVAYAQNGEALRPENGYPLR 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494648283 184 MVVPGYAGVRSAKWLTRIEVRETPSEAPIQAHDYklfpaavTSDTVDWSQGLTINAMPLNAAICSPGAGESLAA-GEVRI 262
Cdd:cd02113  157 LVVPGWEGNTNVKWLRRIEVGDQPWMTREETSKY-------TDLLPDGRARQFSFVMEAKSVITSPSGGQRLREpGFHEI 229

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 494648283 263 EGYAIAYDRRISRIEVSVNGGRDWQQATFADDPETRWGWR---RWILDATLAKgrqhLVARAFDETGQGQPER 332
Cdd:cd02113  230 SGLAWSGRGRIRRVDVSFDGGRTWQDARLEGPVLPKALTRfrlPWKWDGRPAV----LQSRATDETGYVQPTR 298
Mo-co_dimer pfam03404
Mo-co oxidoreductase dimerization domain; This domain is found in molybdopterin cofactor ...
 237-355 2.72e-23

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: 93.58  E-value: 2.72e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494648283  237 INAMPLNAAICSPGAGESL----AAGEVRIEGYAIAYD-RRISRIEVSVNGGRDWQQA--TFADDP-------ETRWGWR 302
Cdd:pfam03404   4 IYDLNVNSAICSPEHDEVVklgaAQGTYTIKGYAYSGGgRRITRVEVSLDGGKTWRLAeiDYEEDPyrygewrEKCWCWC 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 494648283  303 RWILDATLAKGRQ--HLVARAFDETGQGQPErpDTMWNFAGYLCTAWHHVHVLVE 355
Cdd:pfam03404  84 FWSLDIPVSDLLKakEILVRAVDEAMNVQPE--DMYWNVRGMMNNPWHRVKIHVE 136
arch_bact_SO_family_Moco cd02109
bacterial and archael members of the sulfite oxidase (SO) family of molybdopterin binding ...
 32-205 1.79e-20

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: 87.30  E-value: 1.79e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494648283  32 FYVRSHGPVPDL-PANHRIEVSGRGMASRFFSVQELKStFATRTVTAVLQCAgnrrtdlqqvanTSGDPWDVgaignaEW 110
Cdd:cd02109   11 FPVLDAGDVPEVdLEKWRLRVTGLVENPLSLTYEDLLA-LPQTEYTADFHCV------------TGWSKLDV------VW 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494648283 111 TGVRLADVLDAVGaPDASELFVAFTGADEvdvegeealFGVSIAMSKAREPDVLLAWAMNGEPLTPEHGAPLRMVVPGYA 190
Cdd:cd02109   72 EGVSLKDLLEAAR-PDPEATFVMAHSYDG---------YTTNLPLEDLLREDSLLATKMDGEPLPPEHGGPARLVVPHLY 141

                        170
                 ....*....|....*
gi 494648283 191 GVRSAKWLTRIEVRE 205
Cdd:cd02109  142 FWKSAKWLRGIEFLD 156
bact_SO_family_Moco cd02108
bacterial subgroup of the sulfite oxidase (SO) family of molybdopterin binding domains. This ...
 104-203 6.38e-18

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: 80.51  E-value: 6.38e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494648283 104 AIGnaEWTGVRLADVLDAVGaPDASELFVAFTGADevDVEGEEALFGvSIAMSKAREPDVLLAWAMNGEPLTPEHGAPLR 183
Cdd:cd02108   68 AIG--KWGGVPLRTILELVG-PLPEAKYVVFKCAD--DFAGGDRYYE-SIDMASALHPQTLLAYEMNGQPLPIKNGAPLR 141

                         90       100
                 ....*....|....*....|
gi 494648283 184 MVVPGYAGVRSAKWLTRIEV 203
Cdd:cd02108  142 LRVETQLGYKQAKWVTEIEL 161
YedY_like_Moco cd02107
YedY_like molybdopterin cofactor (Moco) binding domain, a subgroup of the sulfite oxidase (SO) ...
 110-233 9.38e-12

YedY_like molybdopterin cofactor (Moco) binding domain, a subgroup of the sulfite oxidase (SO) family of molybdopterin binding domains. Escherichia coli YedY has been proposed to form a heterodimer, consisting of a soluble catalytic subunit termed YedY, which is likely membrane-anchored by a heme-containing trans-membrane subunit YedZ. Preliminary results indicate that YedY may represent a new type of membrane-associated bacterial 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: 239025 [Multi-domain]  Cd Length: 218  Bit Score: 63.62  E-value: 9.38e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494648283 110 WTGVRLADVLDAVgAPDASELFVAFTG-ADEVDVEGEEALFGV-------SIAMSKAREPDVLLAWAMNGEPLTPEHGAP 181
Cdd:cd02107   72 WVGFPLAALLARA-EPTSEAKYVRFTTlLDKEQMPGQSGLFGVlpwpyveGLRLDEAMHPLTLLAVGLYGEALPKQNGAP 150

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 494648283 182 LRMVVPGYAGVRSAKWLTRIE-VRETPSE--APIQAHDYKlFPAAVTSDtVD---WSQ 233
Cdd:cd02107  151 IRLVVPWKYGFKSIKSIVKIEfTKEQPPTtwNLAAPDEYG-FYANVNPS-VDhprWSQ 206
COG3915 COG3915
Uncharacterized conserved protein [Function unknown];
89-204 4.18e-11

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443120  Cd Length: 167  Bit Score: 60.67  E-value: 4.18e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494648283  89 LQQVANTSGDPWDVGAIgnaEWTGVRLADVLDAVGAPDASELFVAFTGadevdvegeealFGVSIAMSKAREPDVLLAWA 168
Cdd:COG3915   58 LPQTEITTTTPWTDGVQ---TFRGVLLRDLLAAVGAKGTTLRAVALND------------YAVEIPISDLEEYGVILAYR 122

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 494648283 169 MNGEPLTPEHGAPLRMVVP------GYAGVRSAKW---LTRIEVR 204
Cdd:COG3915  123 MDGKPMSVRDKGPLWLIYPyddypeLQTEVYYSRSvwqLKRIEVE 167
PRK05363 PRK05363
protein-methionine-sulfoxide reductase catalytic subunit MsrP;
110-233 6.01e-11

protein-methionine-sulfoxide reductase catalytic subunit MsrP;


Pssm-ID: 235431  Cd Length: 280  Bit Score: 62.15  E-value: 6.01e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 494648283 110 WTGVRLADVLDAVGaPDASELFVAFTGADEVD--------------VEGeealfgvsIAMSKAREPDVLLAWAMNGEPLT 175
Cdd:PRK05363 107 WIGFPLAKLLKRVE-PTSNAKYVAFETLYDPEqmpgqrsrfldwpyVEG--------LRLDEAMHPLTLLAVGLYGKTLP 177

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 494648283 176 PEHGAPLRMVVPGYAGVRSAKWLTRIE-VRETPSEA--PIQAHDYKlFPAAVTSDtVD---WSQ 233
Cdd:PRK05363 178 NQNGAPIRLVVPWKYGFKSIKSIVRIRlTEEQPPTTwnLLAPNEYG-FYANVNPN-VDhprWSQ 239
 
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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