NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|145331724|ref|NP_001078089|]
View 

sulfite oxidase [Arabidopsis thaliana]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PLN00177 super family cl30134
sulfite oxidase; Provisional
 14-241 2.41e-178

sulfite oxidase; Provisional


The actual alignment was detected with superfamily member PLN00177:

Pssm-ID: 177772 [Multi-domain]  Cd Length: 393  Bit Score: 495.14  E-value: 2.41e-178
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145331724  14 ENGGPYKASITLSQATNPEADVLLAYEMNGETLNRDHGFPLRVVVPGVIGARSVKWLDSINVIAEESQGFFMQKDYKMFP 93
Cdd:PLN00177 166 ENGGPYKASIPLSQATNPEADVLLAYEMNGEVLNRDHGYPLRVVVPGVIGARSVKWLDSINIIAEECQGFFMQKDYKMFP 245

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145331724  94 PSVNWDNINWSSRRPQMDFPVQSAICSVEDVQMVKPGKVSIKGYAVSGGGRGIERVDISLDGGKNWVEASRTQEPGKQYI 173
Cdd:PLN00177 246 PSVNWDNINWSTRRPQMDFPVQSAICSLEDVNAIKPGKVTVAGYALSGGGRGIERVDISVDGGKTWVEASRYQKPGVPYI 325

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145331724 174 SEHSSSDKWAWVLFEATIDVSQTTEVIAKAVDSAANVQPENVESVWNLRGVLNTSWHRVLLRLGHSNL 241
Cdd:PLN00177 326 SDDISSDKWAWVLFEATVDVPQSTEIVAKAVDSAANVQPESVESIWNLRGILNTSWHRVQLRVGHSNM 393
 
Name Accession Description Interval E-value
PLN00177 PLN00177
sulfite oxidase; Provisional
 14-241 2.41e-178

sulfite oxidase; Provisional


Pssm-ID: 177772 [Multi-domain]  Cd Length: 393  Bit Score: 495.14  E-value: 2.41e-178
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145331724  14 ENGGPYKASITLSQATNPEADVLLAYEMNGETLNRDHGFPLRVVVPGVIGARSVKWLDSINVIAEESQGFFMQKDYKMFP 93
Cdd:PLN00177 166 ENGGPYKASIPLSQATNPEADVLLAYEMNGEVLNRDHGYPLRVVVPGVIGARSVKWLDSINIIAEECQGFFMQKDYKMFP 245

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145331724  94 PSVNWDNINWSSRRPQMDFPVQSAICSVEDVQMVKPGKVSIKGYAVSGGGRGIERVDISLDGGKNWVEASRTQEPGKQYI 173
Cdd:PLN00177 246 PSVNWDNINWSTRRPQMDFPVQSAICSLEDVNAIKPGKVTVAGYALSGGGRGIERVDISVDGGKTWVEASRYQKPGVPYI 325

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145331724 174 SEHSSSDKWAWVLFEATIDVSQTTEVIAKAVDSAANVQPENVESVWNLRGVLNTSWHRVLLRLGHSNL 241
Cdd:PLN00177 326 SDDISSDKWAWVLFEATVDVPQSTEIVAKAVDSAANVQPESVESIWNLRGILNTSWHRVQLRVGHSNM 393
eukary_SO_Moco cd02111
molybdopterin binding domain of sulfite oxidase (SO). SO catalyzes the terminal reaction in ...
 7-235 1.42e-129

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: 370.57  E-value: 1.42e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145331724   7 FSTSEIMENGGPYKASITLSQATNPEADVLLAYEMNGETLNRDHGFPLRVVVPGVIGARSVKWLDSINVIAEESQGFFMQ 86
Cdd:cd02111  136 FEGLDVDPTGTPYGASIPLSKALDPEADVLLAYEMNGTPLPRDHGFPLRVVVPGVVGARSVKWLDRIVVSDEESDSHWQQ 215

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145331724  87 KDYKMFPPSVNWDNINWSSRRPQMDFPVQSAICSVEDVQ---MVKPGKVSIKGYAVSGGGRGIERVDISLDGGKNWVEAS 163
Cdd:cd02111  216 NDYKGFSPSVDWDNVDFSKAPAIQEMPVQSAICSPSVGApvvTVPPGKITVKGYAWSGGGRKIVRVDVSLDGGRTWKVAE 295

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 145331724 164 RTQEPGKQyisehSSSDKWAWVLFEATIDVSQ--TTEVIAKAVDSAANVQPENVESVWNLRGVLNTSWHRVLLR 235
Cdd:cd02111  296 LEQEENVW-----PSGRKWAWTLWEATVPVPAgkEAEIIAKAVDSAYNVQPETVEPIWNLRGVLNNAWHRVKVV 364
Mo-co_dimer pfam03404
Mo-co oxidoreductase dimerization domain; This domain is found in molybdopterin cofactor ...
 106-237 5.34e-54

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: 170.24  E-value: 5.34e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145331724  106 RRPQMDFPVQSAICSVEDVQMVK----PGKVSIKGYAVSGGGRGIERVDISLDGGKNWVEASRTQEPGKQYISEhSSSDK 181
Cdd:pfam03404   1 RYAIYDLNVNSAICSPEHDEVVKlgaaQGTYTIKGYAYSGGGRRITRVEVSLDGGKTWRLAEIDYEEDPYRYGE-WREKC 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 145331724  182 WAWVLFEATIDVSQ---TTEVIAKAVDSAANVQPEnvESVWNLRGVLNTSWHRVLLRLG 237
Cdd:pfam03404  80 WCWCFWSLDIPVSDllkAKEILVRAVDEAMNVQPE--DMYWNVRGMMNNPWHRVKIHVE 136
MsrP COG2041
Molybdopterin-dependent catalytic subunit of periplasmic DMSO/TMAO and ...
 16-94 7.09e-24

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: 94.07  E-value: 7.09e-24
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 145331724  16 GGPYKASITLSQATNPeaDVLLAYEMNGETLNRDHGFPLRVVVPGVIGARSVKWLDSINVIAEESQGFFMQKDYKMFPP 94
Cdd:COG2041  106 DPGYTESLPLDEALDP--DTLLAYGMNGEPLPPEHGAPLRLVVPGLYGFKSAKWLVRIEVTDEDPPGYWETRGYHFYAN 182
 
Name Accession Description Interval E-value
PLN00177 PLN00177
sulfite oxidase; Provisional
 14-241 2.41e-178

sulfite oxidase; Provisional


Pssm-ID: 177772 [Multi-domain]  Cd Length: 393  Bit Score: 495.14  E-value: 2.41e-178
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145331724  14 ENGGPYKASITLSQATNPEADVLLAYEMNGETLNRDHGFPLRVVVPGVIGARSVKWLDSINVIAEESQGFFMQKDYKMFP 93
Cdd:PLN00177 166 ENGGPYKASIPLSQATNPEADVLLAYEMNGEVLNRDHGYPLRVVVPGVIGARSVKWLDSINIIAEECQGFFMQKDYKMFP 245

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145331724  94 PSVNWDNINWSSRRPQMDFPVQSAICSVEDVQMVKPGKVSIKGYAVSGGGRGIERVDISLDGGKNWVEASRTQEPGKQYI 173
Cdd:PLN00177 246 PSVNWDNINWSTRRPQMDFPVQSAICSLEDVNAIKPGKVTVAGYALSGGGRGIERVDISVDGGKTWVEASRYQKPGVPYI 325

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145331724 174 SEHSSSDKWAWVLFEATIDVSQTTEVIAKAVDSAANVQPENVESVWNLRGVLNTSWHRVLLRLGHSNL 241
Cdd:PLN00177 326 SDDISSDKWAWVLFEATVDVPQSTEIVAKAVDSAANVQPESVESIWNLRGILNTSWHRVQLRVGHSNM 393
eukary_SO_Moco cd02111
molybdopterin binding domain of sulfite oxidase (SO). SO catalyzes the terminal reaction in ...
 7-235 1.42e-129

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: 370.57  E-value: 1.42e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145331724   7 FSTSEIMENGGPYKASITLSQATNPEADVLLAYEMNGETLNRDHGFPLRVVVPGVIGARSVKWLDSINVIAEESQGFFMQ 86
Cdd:cd02111  136 FEGLDVDPTGTPYGASIPLSKALDPEADVLLAYEMNGTPLPRDHGFPLRVVVPGVVGARSVKWLDRIVVSDEESDSHWQQ 215

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145331724  87 KDYKMFPPSVNWDNINWSSRRPQMDFPVQSAICSVEDVQ---MVKPGKVSIKGYAVSGGGRGIERVDISLDGGKNWVEAS 163
Cdd:cd02111  216 NDYKGFSPSVDWDNVDFSKAPAIQEMPVQSAICSPSVGApvvTVPPGKITVKGYAWSGGGRKIVRVDVSLDGGRTWKVAE 295

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 145331724 164 RTQEPGKQyisehSSSDKWAWVLFEATIDVSQ--TTEVIAKAVDSAANVQPENVESVWNLRGVLNTSWHRVLLR 235
Cdd:cd02111  296 LEQEENVW-----PSGRKWAWTLWEATVPVPAgkEAEIIAKAVDSAYNVQPETVEPIWNLRGVLNNAWHRVKVV 364
SO_family_Moco_dimer cd02110
Subgroup of sulfite oxidase (SO) family molybdopterin binding domains that contains conserved ...
 14-232 1.95e-84

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: 254.15  E-value: 1.95e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145331724  14 ENGGPYKASITLSQATNPeaDVLLAYEMNGETLNRDHGFPLRVVVPGVIGARSVKWLDSINVIAEESQGFFMQKDYKMFP 93
Cdd:cd02110  110 EKAADYTRSVPLSKALDD--DALLAYEMNGEPLPPDHGYPLRLVVPGWYGARSVKWLRRIEVTDQPSDGYWQTRDYTVPP 187

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145331724  94 PSVNWdnINWSSRRPQMDFPVQSAICSVEDVQMVKPGKVSIKGYAVSGGGRGIERVDISLDGGKNWVEAsRTQEPgkqyi 173
Cdd:cd02110  188 PDVDA--VGGKARRPIGEMPVKSVITSPSPGAELVSGGRVEIGGVAWSGGRGIRRVEVSLDGGRTWQEA-RLEGP----- 259

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 145331724 174 sehsSSDKWAWVLFEATIDVSQ-TTEVIAKAVDSAANVQPENVESVWNLRGVLNTSWHRV 232
Cdd:cd02110  260 ----LAGPRAWRQWELDWDLPPgEYELVARATDSTGNVQPERAEWNWNPGGYGNNHWHRV 315
Mo-co_dimer pfam03404
Mo-co oxidoreductase dimerization domain; This domain is found in molybdopterin cofactor ...
 106-237 5.34e-54

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: 170.24  E-value: 5.34e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145331724  106 RRPQMDFPVQSAICSVEDVQMVK----PGKVSIKGYAVSGGGRGIERVDISLDGGKNWVEASRTQEPGKQYISEhSSSDK 181
Cdd:pfam03404   1 RYAIYDLNVNSAICSPEHDEVVKlgaaQGTYTIKGYAYSGGGRRITRVEVSLDGGKTWRLAEIDYEEDPYRYGE-WREKC 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 145331724  182 WAWVLFEATIDVSQ---TTEVIAKAVDSAANVQPEnvESVWNLRGVLNTSWHRVLLRLG 237
Cdd:pfam03404  80 WCWCFWSLDIPVSDllkAKEILVRAVDEAMNVQPE--DMYWNVRGMMNNPWHRVKIHVE 136
eukary_NR_Moco cd02112
molybdopterin binding domain of eukaryotic nitrate reductase (NR). Assimilatory NRs catalyze ...
 16-232 6.13e-54

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: 177.96  E-value: 6.13e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145331724  16 GGPYKASITLSQATNPEADVLLAYEMNGETLNRDHGFPLRVVVPGVIGARSVKWLDSINVIAEESQGFFMQKDYKMFPPS 95
Cdd:cd02112  161 NGKYGTSITLSWAMDPSKDVMLAYKQNGELLHPDHGFPVRLIIPGQIGGRMVKWLKRIVVSDRESQNHYHFHDNRVLPSH 240

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145331724  96 VNWDNIN----WS-SRRPQMDFPVQSAICSVEDVQMVKPGKV------SIKGYAVSGGGRGIERVDISLDGGKNWVEASr 164
Cdd:cd02112  241 VDAELANeegwWYkPEYIINDLNVNSAITTPAHDEVLPLNGLttaetyTMKGYAYAGGGRRVTRVEVSLDDGKSWKLAS- 319

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 145331724 165 tqepgKQYISEHSSSDK-WAWVLFEATIDVS---QTTEVIAKAVDSAANVQPENVesVWNLRGVLNTSWHRV 232
Cdd:cd02112  320 -----IDYPEDPTKYGKcWCWCFWSLDVPLSellAAKEICVRAWDESMNTQPRDM--TWNVMGMMNNCWFRV 384
PLN02252 PLN02252
nitrate reductase [NADPH]
 7-232 4.76e-47

nitrate reductase [NADPH]


Pssm-ID: 215141 [Multi-domain]  Cd Length: 888  Bit Score: 166.39  E-value: 4.76e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145331724   7 FSTSEIMENGG--PYKASITLSQATNPEADVLLAYEMNGETLNRDHGFPLRVVVPGVIGARSVKWLDSINVIAEESQGFF 84
Cdd:PLN02252 222 FEGAEDLPGGGgsKYGTSITLERAMDPARDVILAYMQNGEPLTPDHGFPVRLIIPGFIGGRMVKWLKRIIVTTAESDNYY 301

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145331724  85 MQKDYKMFPPSVNWDNIN----WssRRPQM---DFPVQSAICS--------VEDVQMVKPgkVSIKGYAVSGGGRGIERV 149
Cdd:PLN02252 302 HYRDNRVLPSHVDAELANaegwW--YKPEYiinELNINSVITTpahdeilpINASTTQRP--YTMKGYAYSGGGRKVTRV 377

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145331724 150 DISLDGGKNWVEAS--RTQEP---GKQyisehsssdkWAWVLFE---ATIDVSQTTEVIAKAVDSAANVQPENVesVWNL 221
Cdd:PLN02252 378 EVSLDGGETWRLCDldHPEKPtkyGKY----------WCWCFWSldvEVLDLLGAKEIAVRAWDESMNTQPEKL--IWNL 445

                        250
                 ....*....|.
gi 145331724 222 RGVLNTSWHRV 232
Cdd:PLN02252 446 MGMMNNCWFRV 456
Oxidored_molyb pfam00174
Oxidoreductase molybdopterin binding domain; This domain is found in a variety of ...
 16-84 1.23e-32

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: 116.45  E-value: 1.23e-32
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 145331724   16 GGPYKASITLSQATNPeaDVLLAYEMNGETLNRDHGFPLRVVVPGVIGARSVKWLDSINVIAEESQGFF 84
Cdd:pfam00174 102 DGGYTTSLPLEKALDD--DVLLAYEMNGEPLPPDHGYPLRLVVPGWYGARSVKWLRRIEVTDEESPGFW 168
SO_family_Moco cd00321
Sulfite oxidase (SO) family, molybdopterin binding domain. This molybdopterin cofactor (Moco) ...
 15-78 2.21e-27

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: 102.65  E-value: 2.21e-27
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 145331724  15 NGGPYKASITLSQATNPeaDVLLAYEMNGETLNRDHGFPLRVVVPGVIGARSVKWLDSINVIAE 78
Cdd:cd00321   95 GGDGYTTSLPLEKALDP--DVLLAYEMNGEPLPPDHGFPLRLVVPGLYGWKSVKWLRRIEVTDE 156
bact_SorA_Moco cd02114
sulfite:cytochrome c oxidoreductase subunit A (SorA), molybdopterin binding domain. SorA is ...
 12-170 1.04e-24

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: 100.28  E-value: 1.04e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145331724  12 IMENGGPYKASITLSQATNPEadVLLAYEMNGETLNRDHGFPLRVVVPGVIGARSVKWLDSINVIAEESQGFFMQKDYKM 91
Cdd:cd02114  156 VLDVTPDFVKSLDIDHALDGE--VMLAWEMNGEPLPVLNGYPLRLVVPGFYATYWVKHLSHITVLDKEFDGFWASQAYRI 233

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145331724  92 fpPSVNWDNINWSSR----RPQMDFPVQSAICSVEDVQMVKP-GKVSIKGYAVSgGGRGIERVDISLDGGKNWVEASRTQ 166
Cdd:cd02114  234 --PDNADAGVEPGTApdrtAPINRFKVRSFITSLENGAIVAPaGELALRGIAFD-GGSGIRRVDVSADGGDSWTQATLGP 310


                 ....
gi 145331724 167 EPGK 170
Cdd:cd02114  311 DLGR 314
MsrP COG2041
Molybdopterin-dependent catalytic subunit of periplasmic DMSO/TMAO and ...
 16-94 7.09e-24

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: 94.07  E-value: 7.09e-24
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 145331724  16 GGPYKASITLSQATNPeaDVLLAYEMNGETLNRDHGFPLRVVVPGVIGARSVKWLDSINVIAEESQGFFMQKDYKMFPP 94
Cdd:COG2041  106 DPGYTESLPLDEALDP--DTLLAYGMNGEPLPPEHGAPLRLVVPGLYGFKSAKWLVRIEVTDEDPPGYWETRGYHFYAN 182
bact_SoxC_Moco cd02113
bacterial SoxC is a member of the sulfite oxidase (SO) family of molybdopterin binding domains. ...
 34-216 1.34e-21

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: 91.31  E-value: 1.34e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145331724  34 DVLLAYEMNGETLNRDHGFPLRVVVPGVIGARSVKWLDSINVIAEEsqgfFMQKD----YKMFPPSVNWDNINWSsrrpq 109
Cdd:cd02113  135 DALVAYAQNGEALRPENGYPLRLVVPGWEGNTNVKWLRRIEVGDQP----WMTREetskYTDLLPDGRARQFSFV----- 205

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145331724 110 MDfpVQSAICSVEDVQMVK-PGKVSIKGYAVSGGGRgIERVDISLDGGKNWVEAsRTQEPGKQYisehsssdkwAWVLFE 188
Cdd:cd02113  206 ME--AKSVITSPSGGQRLRePGFHEISGLAWSGRGR-IRRVDVSFDGGRTWQDA-RLEGPVLPK----------ALTRFR 271

                        170       180
                 ....*....|....*....|....*....
gi 145331724 189 ATIDVS-QTTEVIAKAVDSAANVQPENVE 216
Cdd:cd02113  272 LPWKWDgRPAVLQSRATDETGYVQPTRAE 300
arch_bact_SO_family_Moco cd02109
bacterial and archael members of the sulfite oxidase (SO) family of molybdopterin binding ...
 19-91 1.97e-13

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: 66.11  E-value: 1.97e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 145331724  19 YKASITLSQATNPeaDVLLAYEMNGETLNRDHGFPLRVVVPGVIGARSVKWLDSINVIAEESQGFFMQKDYKM 91
Cdd:cd02109  100 YTTNLPLEDLLRE--DSLLATKMDGEPLPPEHGGPARLVVPHLYFWKSAKWLRGIEFLDEDEPGFWERRGYHE 170
bact_SO_family_Moco cd02108
bacterial subgroup of the sulfite oxidase (SO) family of molybdopterin binding domains. This ...
 7-77 3.61e-11

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: 60.09  E-value: 3.61e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 145331724   7 FSTSEIMENGGPYKASITLSQATNPEAdvLLAYEMNGETLNRDHGFPLRVVVPGVIGARSVKWLDSINVIA 77
Cdd:cd02108   95 FKCADDFAGGDRYYESIDMASALHPQT--LLAYEMNGQPLPIKNGAPLRLRVETQLGYKQAKWVTEIELVN 163
YedY_like_Moco cd02107
YedY_like molybdopterin cofactor (Moco) binding domain, a subgroup of the sulfite oxidase (SO) ...
 18-113 6.95e-07

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: 48.60  E-value: 6.95e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145331724  18 PYKASITLSQATNPEAdvLLAYEMNGETLNRDHGFPLRVVVPGVIGARSVKWLDSINVIAEEsqgffmqkdykmfpPSVN 97
Cdd:cd02107  117 PYVEGLRLDEAMHPLT--LLAVGLYGEALPKQNGAPIRLVVPWKYGFKSIKSIVKIEFTKEQ--------------PPTT 180

                         90       100
                 ....*....|....*....|..
gi 145331724  98 WDNIN------WSSRRPQMDFP 113
Cdd:cd02107  181 WNLAApdeygfYANVNPSVDHP 202
COG3915 COG3915
Uncharacterized conserved protein [Function unknown];
19-75 3.34e-06

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443120  Cd Length: 167  Bit Score: 45.65  E-value: 3.34e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145331724  19 YKASITLSQATnpEADVLLAYEMNGETLN-RDHGfPLRVVVP---------GVIGARSVkW-LDSINV 75
Cdd:COG3915  103 YAVEIPISDLE--EYGVILAYRMDGKPMSvRDKG-PLWLIYPyddypelqtEVYYSRSV-WqLKRIEV 166
PRK05363 PRK05363
protein-methionine-sulfoxide reductase catalytic subunit MsrP;
18-86 4.15e-04

protein-methionine-sulfoxide reductase catalytic subunit MsrP;


Pssm-ID: 235431  Cd Length: 280  Bit Score: 40.58  E-value: 4.15e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 145331724  18 PYKASITLSQATNPEAdvLLAYEMNGETLNRDHGFPLRVVVPGVIGARSVKWLDSINVIAEESQGFFMQ 86
Cdd:PRK05363 150 PYVEGLRLDEAMHPLT--LLAVGLYGKTLPNQNGAPIRLVVPWKYGFKSIKSIVRIRLTEEQPPTTWNL 216
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH