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Conserved domains on  [gi|1002986206|ref|WP_061430733|]
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sulfite oxidase-like oxidoreductase [Microcystis aeruginosa]

Protein Classification

sulfite oxidase-like oxidoreductase( domain architecture ID 10114653)

sulfite oxidase-like oxidoreductase, similar to the uncharacterized oxidoreductase YuiH from Bacillus subtilis

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
arch_bact_SO_family_Moco cd02109
bacterial and archael members of the sulfite oxidase (SO) family of molybdopterin binding ...
 17-196 1.29e-101

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: 290.69  E-value: 1.29e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002986206  17 VPPGQYLASGFPVLTYGDTPQIKTEEWLFKVWGKVATTKTFNWSDFMALPQWEFTKDFHCVTRWSKLDVTWTGVKVSDLM 96
Cdd:cd02109     1 LPPGQYLTEKFPVLDAGDVPEVDLEKWRLRVTGLVENPLSLTYEDLLALPQTEYTADFHCVTGWSKLDVVWEGVSLKDLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002986206  97 TLIDLLPEATHVMQHCYGGYTTNLTLEEFLHEDNFFAFQLFGQPLPPDHGGPLRLVVPHLYAWKSSKWINGLEFLDREQS 176
Cdd:cd02109    81 EAARPDPEATFVMAHSYDGYTTNLPLEDLLREDSLLATKMDGEPLPPEHGGPARLVVPHLYFWKSAKWLRGIEFLDEDEP 160

                         170       180
                  ....*....|....*....|
gi 1002986206 177 GFWERNGYHRRGDPWLEERY 196
Cdd:cd02109   161 GFWERRGYHERGDPWREERF 180
 
Name Accession Description Interval E-value
arch_bact_SO_family_Moco cd02109
bacterial and archael members of the sulfite oxidase (SO) family of molybdopterin binding ...
 17-196 1.29e-101

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: 290.69  E-value: 1.29e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002986206  17 VPPGQYLASGFPVLTYGDTPQIKTEEWLFKVWGKVATTKTFNWSDFMALPQWEFTKDFHCVTRWSKLDVTWTGVKVSDLM 96
Cdd:cd02109     1 LPPGQYLTEKFPVLDAGDVPEVDLEKWRLRVTGLVENPLSLTYEDLLALPQTEYTADFHCVTGWSKLDVVWEGVSLKDLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002986206  97 TLIDLLPEATHVMQHCYGGYTTNLTLEEFLHEDNFFAFQLFGQPLPPDHGGPLRLVVPHLYAWKSSKWINGLEFLDREQS 176
Cdd:cd02109    81 EAARPDPEATFVMAHSYDGYTTNLPLEDLLREDSLLATKMDGEPLPPEHGGPARLVVPHLYFWKSAKWLRGIEFLDEDEP 160

                         170       180
                  ....*....|....*....|
gi 1002986206 177 GFWERNGYHRRGDPWLEERY 196
Cdd:cd02109   161 GFWERRGYHERGDPWREERF 180
MsrP COG2041
Molybdopterin-dependent catalytic subunit of periplasmic DMSO/TMAO and ...
 24-190 1.01e-79

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: 235.44  E-value: 1.01e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002986206  24 ASGFPVLTYGDTPQIKTEEWLFKVWGKVATTKTFNWSDFMALPQWEFTKDFHCVTRWSKLDVTWTGVKVSDLMTLIDLLP 103
Cdd:COG2041    16 ALAFPVRTAGGVPEIDPADWRLRVDGLVEKPLTLTLDDLLALPLEERIYRLHCVENWSGGVAPWTGVPLRDLLERAGPKP 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002986206 104 EATHVMQHCYG-GYTTNLTLEEFLHEDNFFAFQLFGQPLPPDHGGPLRLVVPHLYAWKSSKWINGLEFLDREQSGFWERN 182
Cdd:COG2041    96 GAKYVLFESADpGYTESLPLDEALDPDTLLAYGMNGEPLPPEHGAPLRLVVPGLYGFKSAKWLVRIEVTDEDPPGYWETR 175


                  ....*...
gi 1002986206 183 GYHRRGDP 190
Cdd:COG2041   176 GYHFYANI 183
Oxidored_molyb pfam00174
Oxidoreductase molybdopterin binding domain; This domain is found in a variety of ...
 32-179 1.05e-56

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: 176.54  E-value: 1.05e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002986206  32 YGDTPQIKTEEWLFKVWGKVATTKTFNWSDFMALPQWEFTKDFHCVT------------RW---SKLDVTWTGVKVSDLM 96
Cdd:pfam00174   1 HGPVPEIDPDTWRLRVDGLVEKPLTLTLDDLKAFPQVTVTATLQCVGnrrkemnrvkgvQWgggAIGNAEWTGVPLRDLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002986206  97 TLIDLLPEATHVMQHCY-----GGYTTNLTLEEFLHEDNFFAFQLFGQPLPPDHGGPLRLVVPHLYAWKSSKWINGLEFL 171
Cdd:pfam00174  81 ERAGVKPGAKHVLFEGAdtlgdGGYTTSLPLEKALDDDVLLAYEMNGEPLPPDHGYPLRLVVPGWYGARSVKWLRRIEVT 160


                  ....*...
gi 1002986206 172 DREQSGFW 179
Cdd:pfam00174 161 DEESPGFW 168
PRK05363 PRK05363
protein-methionine-sulfoxide reductase catalytic subunit MsrP;
39-181 5.05e-20

protein-methionine-sulfoxide reductase catalytic subunit MsrP;


Pssm-ID: 235431  Cd Length: 280  Bit Score: 84.88  E-value: 5.05e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002986206  39 KTEEWLFKVWGKVATTKTFNWSDFMAL-PQWEFTKDFHCVTRWSkLDVTWTGVKVSDLMTLIDLLPEATHV--------- 108
Cdd:PRK05363   59 KTDPWTVKIDGEVEKPGTLDIDDLLKLfPLEERIYRLRCVEAWS-MVIPWIGFPLAKLLKRVEPTSNAKYVafetlydpe 137

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002986206 109 -MQHCYGG-----YTTNLTLEEFLHEDNFFAFQLFGQPLPPDHGGPLRLVVPHLYAWKSSKWINGLEFLDREQSGFWER 181
Cdd:PRK05363  138 qMPGQRSRfldwpYVEGLRLDEAMHPLTLLAVGLYGKTLPNQNGAPIRLVVPWKYGFKSIKSIVRIRLTEEQPPTTWNL 216
 
Name Accession Description Interval E-value
arch_bact_SO_family_Moco cd02109
bacterial and archael members of the sulfite oxidase (SO) family of molybdopterin binding ...
 17-196 1.29e-101

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: 290.69  E-value: 1.29e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002986206  17 VPPGQYLASGFPVLTYGDTPQIKTEEWLFKVWGKVATTKTFNWSDFMALPQWEFTKDFHCVTRWSKLDVTWTGVKVSDLM 96
Cdd:cd02109     1 LPPGQYLTEKFPVLDAGDVPEVDLEKWRLRVTGLVENPLSLTYEDLLALPQTEYTADFHCVTGWSKLDVVWEGVSLKDLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002986206  97 TLIDLLPEATHVMQHCYGGYTTNLTLEEFLHEDNFFAFQLFGQPLPPDHGGPLRLVVPHLYAWKSSKWINGLEFLDREQS 176
Cdd:cd02109    81 EAARPDPEATFVMAHSYDGYTTNLPLEDLLREDSLLATKMDGEPLPPEHGGPARLVVPHLYFWKSAKWLRGIEFLDEDEP 160

                         170       180
                  ....*....|....*....|
gi 1002986206 177 GFWERNGYHRRGDPWLEERY 196
Cdd:cd02109   161 GFWERRGYHERGDPWREERF 180
MsrP COG2041
Molybdopterin-dependent catalytic subunit of periplasmic DMSO/TMAO and ...
 24-190 1.01e-79

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: 235.44  E-value: 1.01e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002986206  24 ASGFPVLTYGDTPQIKTEEWLFKVWGKVATTKTFNWSDFMALPQWEFTKDFHCVTRWSKLDVTWTGVKVSDLMTLIDLLP 103
Cdd:COG2041    16 ALAFPVRTAGGVPEIDPADWRLRVDGLVEKPLTLTLDDLLALPLEERIYRLHCVENWSGGVAPWTGVPLRDLLERAGPKP 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002986206 104 EATHVMQHCYG-GYTTNLTLEEFLHEDNFFAFQLFGQPLPPDHGGPLRLVVPHLYAWKSSKWINGLEFLDREQSGFWERN 182
Cdd:COG2041    96 GAKYVLFESADpGYTESLPLDEALDPDTLLAYGMNGEPLPPEHGAPLRLVVPGLYGFKSAKWLVRIEVTDEDPPGYWETR 175


                  ....*...
gi 1002986206 183 GYHRRGDP 190
Cdd:COG2041   176 GYHFYANI 183
SO_family_Moco cd00321
Sulfite oxidase (SO) family, molybdopterin binding domain. This molybdopterin cofactor (Moco) ...
 27-173 1.51e-59

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: 183.54  E-value: 1.51e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002986206  27 FPVLTYGDTPQIKTEEWLFKVWGKVATTKTFNWSDFMALPQWEFTKDFHCVT----RWSKLDVTWTGVKVSDLMTLIDLL 102
Cdd:cd00321     1 FVRNHGGVPPEIDPDDWRLEVDGLVEKPLSLTLDDLKALPQVEVIATLHCVGnrwgGGAVSNAEWTGVPLRDLLEEAGPK 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002986206 103 PEATHVMQHCY-----GGYTTNLTLEEFLHEDNFFAFQLFGQPLPPDHGGPLRLVVPHLYAWKSSKWINGLEFLDR 173
Cdd:cd00321    81 PGARYVVFEGAddpggDGYTTSLPLEKALDPDVLLAYEMNGEPLPPDHGFPLRLVVPGLYGWKSVKWLRRIEVTDE 156
Oxidored_molyb pfam00174
Oxidoreductase molybdopterin binding domain; This domain is found in a variety of ...
 32-179 1.05e-56

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: 176.54  E-value: 1.05e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002986206  32 YGDTPQIKTEEWLFKVWGKVATTKTFNWSDFMALPQWEFTKDFHCVT------------RW---SKLDVTWTGVKVSDLM 96
Cdd:pfam00174   1 HGPVPEIDPDTWRLRVDGLVEKPLTLTLDDLKAFPQVTVTATLQCVGnrrkemnrvkgvQWgggAIGNAEWTGVPLRDLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002986206  97 TLIDLLPEATHVMQHCY-----GGYTTNLTLEEFLHEDNFFAFQLFGQPLPPDHGGPLRLVVPHLYAWKSSKWINGLEFL 171
Cdd:pfam00174  81 ERAGVKPGAKHVLFEGAdtlgdGGYTTSLPLEKALDDDVLLAYEMNGEPLPPDHGYPLRLVVPGWYGARSVKWLRRIEVT 160


                  ....*...
gi 1002986206 172 DREQSGFW 179
Cdd:pfam00174 161 DEESPGFW 168
bact_SO_family_Moco cd02108
bacterial subgroup of the sulfite oxidase (SO) family of molybdopterin binding domains. This ...
 42-188 9.95e-25

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: 95.15  E-value: 9.95e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002986206  42 EWLFKVWGKVATTKTFNWSDFMALPQWEFTKDFHCVTRWSKLdVTWTGVKVSDLMTLIDLLPEATHVMQHC------YGG 115
Cdd:cd02108    28 DYRLEVGGLVEHPLSLSLEELRALPQRTQITRHICVEGWSAI-GKWGGVPLRTILELVGPLPEAKYVVFKCaddfagGDR 106

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002986206 116 YTTNLTLEEFLHEDNFFAFQLFGQPLPPDHGGPLRLVVPHLYAWKSSKWINGLEFLDR------EQSGFWERNGYHRRG 188
Cdd:cd02108   107 YYESIDMASALHPQTLLAYEMNGQPLPIKNGAPLRLRVETQLGYKQAKWVTEIELVNDlpgiggGKGGYWEDQGYNWFG 185
SO_family_Moco_dimer cd02110
Subgroup of sulfite oxidase (SO) family molybdopterin binding domains that contains conserved ...
 33-184 1.16e-24

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: 98.14  E-value: 1.16e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002986206  33 GDTPQIKTEEWLFKVWGKVATTKTFNWSDFMALPQWEFT----------KDFHCVTRWSKLD------VTWTGVKVSDLM 96
Cdd:cd02110     8 GGVPDIDPDAWRLEIHGLVERPLTLTLDDLKRLPSVEVVatlecsgngrGGFIPVRSGAQWGhgavgnARWTGVPLKDLL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002986206  97 TLIDLLPEATHVMqhCYG----------GYTTNLTLEEFLHEDNFFAFQLFGQPLPPDHGGPLRLVVPHLYAWKSSKWIN 166
Cdd:cd02110    88 EEAGVKPGAKHVL--FEGadvppgekaaDYTRSVPLSKALDDDALLAYEMNGEPLPPDHGYPLRLVVPGWYGARSVKWLR 165

                         170
                  ....*....|....*...
gi 1002986206 167 GLEFLDREQSGFWERNGY 184
Cdd:cd02110   166 RIEVTDQPSDGYWQTRDY 183
YedY_like_Moco cd02107
YedY_like molybdopterin cofactor (Moco) binding domain, a subgroup of the sulfite oxidase (SO) ...
 37-180 1.26e-22

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: 90.59  E-value: 1.26e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002986206  37 QIKTEEWLFKVWGKVATTKTFNWSDFM-ALPQWEFTKDFHCVTRWSKLdVTWTGVKVSDLMTLIDLLPEATHV------- 108
Cdd:cd02107    22 NLPTRPWTVSVSGLVKKPKTLDIDDLMkTFPLEERIYRFRCVEGWSMV-VPWVGFPLAALLARAEPTSEAKYVrfttlld 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002986206 109 ------MQHCYGG----YTTNLTLEEFLHEDNFFAFQLFGQPLPPDHGGPLRLVVPHLYAWKSSKWINGLEFLDREQSGF 178
Cdd:cd02107   101 keqmpgQSGLFGVlpwpYVEGLRLDEAMHPLTLLAVGLYGEALPKQNGAPIRLVVPWKYGFKSIKSIVKIEFTKEQPPTT 180


                  ..
gi 1002986206 179 WE 180
Cdd:cd02107   181 WN 182
PRK05363 PRK05363
protein-methionine-sulfoxide reductase catalytic subunit MsrP;
39-181 5.05e-20

protein-methionine-sulfoxide reductase catalytic subunit MsrP;


Pssm-ID: 235431  Cd Length: 280  Bit Score: 84.88  E-value: 5.05e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002986206  39 KTEEWLFKVWGKVATTKTFNWSDFMAL-PQWEFTKDFHCVTRWSkLDVTWTGVKVSDLMTLIDLLPEATHV--------- 108
Cdd:PRK05363   59 KTDPWTVKIDGEVEKPGTLDIDDLLKLfPLEERIYRLRCVEAWS-MVIPWIGFPLAKLLKRVEPTSNAKYVafetlydpe 137

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002986206 109 -MQHCYGG-----YTTNLTLEEFLHEDNFFAFQLFGQPLPPDHGGPLRLVVPHLYAWKSSKWINGLEFLDREQSGFWER 181
Cdd:PRK05363  138 qMPGQRSRfldwpYVEGLRLDEAMHPLTLLAVGLYGKTLPNQNGAPIRLVVPWKYGFKSIKSIVRIRLTEEQPPTTWNL 216
eukary_SO_Moco cd02111
molybdopterin binding domain of sulfite oxidase (SO). SO catalyzes the terminal reaction in ...
 18-184 1.61e-15

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: 73.58  E-value: 1.61e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002986206  18 PPGQYLASGF--PV-LTY----GDTPQIKTEEWLFKVWGKVATTKTFNWSDFMAL-PQWEFTKDFHC-------VTRWSK 82
Cdd:cd02111    14 PPSSLLASSFitPNeLFYvrnhLPVPVVDPDTYSLEVEGPDGTTLSLSLEDLKSLfPKHEVTATLQCagnrrseMTKVKK 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002986206  83 LD-----------VTWTGVKVSDLMTLI----DLLPEATHV----MQHCYGG--YTTNLTLEEFLHE--DNFFAFQLFGQ 139
Cdd:cd02111    94 VKglqwgdgaisnAEWGGARLRDVLLDAgipeDDSQGGLHVhfegLDVDPTGtpYGASIPLSKALDPeaDVLLAYEMNGT 173

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1002986206 140 PLPPDHGGPLRLVVPHLYAWKSSKWINGLEFLDREQSGFWERNGY 184
Cdd:cd02111   174 PLPRDHGFPLRVVVPGVVGARSVKWLDRIVVSDEESDSHWQQNDY 218
eukary_NR_Moco cd02112
molybdopterin binding domain of eukaryotic nitrate reductase (NR). Assimilatory NRs catalyze ...
 18-185 6.34e-13

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: 66.25  E-value: 6.34e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002986206  18 PPGQYLASGF--P-----VLTYGDTPQIKTEEWLFKVWGKVATTKTFNWSDFMAL-PQWEFTKDFHCVTR---------- 79
Cdd:cd02112    29 PLTELMDHGFitPsnlhyVRNHGPVPREKWEDWTVEVTGLVEKPTTLTMDELVAMfPSVTFPVTLVCAGNrrkeqnmvkk 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002986206  80 -----WSKLDV---TWTGVKVSDLMTLIDLLPE---ATHVmqhCY-----------GGYTTNLTLEEFL--HEDNFFAFQ 135
Cdd:cd02112   109 tigfnWGAAGTstsLWTGVRLSDLLDRCGPKSPkggARHV---CFegaddllpgpnGKYGTSITLSWAMdpSKDVMLAYK 185

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1002986206 136 LFGQPLPPDHGGPLRLVVPHLYAWKSSKWINGLEFLDREQSgfwerNGYH 185
Cdd:cd02112   186 QNGELLHPDHGFPVRLIIPGQIGGRMVKWLKRIVVSDRESQ-----NHYH 230
COG3915 COG3915
Uncharacterized conserved protein [Function unknown];
40-154 1.12e-12

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443120  Cd Length: 167  Bit Score: 62.98  E-value: 1.12e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002986206  40 TEEWLFKVWGKVATTK-----TFNWSDFMALPQWEFTKDfhcvTRWSKLDVTWTGVKVSDLMTLIDLlpEATHVMQHCYG 114
Cdd:COG3915    28 AGPVILTVSGKIGNTNaggaaTFDLAMLEALPQTEITTT----TPWTDGVQTFRGVLLRDLLAAVGA--KGTTLRAVALN 101

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1002986206 115 GYTTNLTLEEFLHEDNFFAFQLFGQPLPPDHGGPLRLVVP 154
Cdd:COG3915   102 DYAVEIPISDLEEYGVILAYRMDGKPMSVRDKGPLWLIYP 141
PLN00177 PLN00177
sulfite oxidase; Provisional
 49-184 3.86e-10

sulfite oxidase; Provisional


Pssm-ID: 177772 [Multi-domain]  Cd Length: 393  Bit Score: 57.94  E-value: 3.86e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002986206  49 GKVATTKTFNWSDFMALPQWEFTKDFHCV----TRWSKL--------DV------TWTGVKVSDLMTLIDL--LPEAT-- 106
Cdd:PLN00177   71 GLIENPRKLSMKDIRKLPKYNVTATLQCAgnrrTAMSKVrkvrgvgwDVsaignaVWGGAKLADVLELVGIpkLTSITss 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002986206 107 ---HV----MQHCY----GGYTTNLTLEEFLH--EDNFFAFQLFGQPLPPDHGGPLRLVVPHLYAWKSSKWINGLEFLDR 173
Cdd:PLN00177  151 ggkHVefvsVDKCKeengGPYKASIPLSQATNpeADVLLAYEMNGEVLNRDHGYPLRVVVPGVIGARSVKWLDSINIIAE 230

                         170
                  ....*....|.
gi 1002986206 174 EQSGFWERNGY 184
Cdd:PLN00177  231 ECQGFFMQKDY 241
bact_SorA_Moco cd02114
sulfite:cytochrome c oxidoreductase subunit A (SorA), molybdopterin binding domain. SorA is ...
 85-184 4.34e-07

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: 49.05  E-value: 4.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002986206  85 VTWTGVKVSDLMTLIDLLPEATHVMqhCYG----------GYTTNLTLEEFLHEDNFFAFQLFGQPLPPDHGGPLRLVVP 154
Cdd:cd02114   124 ARWAGVPLKAVLAKAGVQDGARQVA--FRGldqpvldvtpDFVKSLDIDHALDGEVMLAWEMNGEPLPVLNGYPLRLVVP 201

                          90       100       110
                  ....*....|....*....|....*....|
gi 1002986206 155 HLYAWKSSKWINGLEFLDREQSGFWERNGY 184
Cdd:cd02114   202 GFYATYWVKHLSHITVLDKEFDGFWASQAY 231
PLN02252 PLN02252
nitrate reductase [NADPH]
 29-187 6.56e-07

nitrate reductase [NADPH]


Pssm-ID: 215141 [Multi-domain]  Cd Length: 888  Bit Score: 48.91  E-value: 6.56e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002986206  29 VLTYGDTPQIKTEEWLFKVWGKVATTKTFNWSDFMALPQWEF-------------------TKDFHcvtrWSKLDVT--- 86
Cdd:PLN02252  120 VRNHGAVPRADWDEWTVEVTGLVKRPARLTMDELVRFPARELpvtlvcagnrrkeqnmvkqTIGFN----WGAAGVStsv 195

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002986206  87 WTGVKVSDLMTLIDLL---PEATHVmqhCY-----------GGYTTNLTLEEFLHE--DNFFAFQLFGQPLPPDHGGPLR 150
Cdd:PLN02252  196 WRGVRLRDVLRRCGVMsrkGGALNV---CFegaedlpggggSKYGTSITLERAMDParDVILAYMQNGEPLTPDHGFPVR 272

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1002986206 151 LVVPHLYAWKSSKWINGLEFLDREQSGFwerngYHRR 187
Cdd:PLN02252  273 LIIPGFIGGRMVKWLKRIIVTTAESDNY-----YHYR 304
bact_SoxC_Moco cd02113
bacterial SoxC is a member of the sulfite oxidase (SO) family of molybdopterin binding domains. ...
 32-172 9.26e-05

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: 42.00  E-value: 9.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002986206  32 YGDTPQIKTEEWLFKVWGKVATTKTFNWSDFMALPQ----------------WEFTKDFHC-VTRWSKLDVTWTGVKVSD 94
Cdd:cd02113    20 HGGVPDIDPAQHRLMIHGMVKKPLVFTMDDLKRFPSvsriyflecsgnggtgWRGAPLPTAqYTHGMLSCSEWTGVPLST 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002986206  95 LMTLIDLLPEATHVMQHCYGG--YTTNLTLEEFLhEDNFFAFQLFGQPLPPDHGGPLRLVVPHLYAWKSSKWINGLEFLD 172
Cdd:cd02113   100 LLEEAGVKPGAKWLLAEGADAaaMTRSIPLEKAL-DDALVAYAQNGEALRPENGYPLRLVVPGWEGNTNVKWLRRIEVGD 178
 
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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