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Conserved domains on  [gi|428257268|gb|AFZ23218|]
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hypothetical protein Cylst_0892 [Cylindrospermum stagnale PCC 7417]

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
COG3915 COG3915
Uncharacterized conserved protein [Function unknown];
59-200 1.15e-33

Uncharacterized conserved protein [Function unknown];


:

Pssm-ID: 443120  Cd Length: 167  Bit Score: 121.92  E-value: 1.15e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428257268  59 PSEWNLVIQGE---TATGKPVKLDWQQLFALANTHVKTTDANQvvqrERIFDFRGIPVSGLLKNFGYQSnvTEVTFVCYD 135
Cdd:COG3915   28 AGPVILTVSGKignTNAGGAATFDLAMLEALPQTEITTTTPWT----DGVQTFRGVLLRDLLAAVGAKG--TTLRAVALN 101

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 428257268 136 AYQVTLPLTDLLAYPIILALTSNGKPIERDQGGPTYLVFPDTDFPQLLQKYDSSSWAFYVNHVVV 200
Cdd:COG3915  102 DYAVEIPISDLEEYGVILAYRMDGKPMSVRDKGPLWLIYPYDDYPELQTEVYYSRSVWQLKRIEV 166
SO_family_Moco super family cl00199
Sulfite oxidase (SO) family, molybdopterin binding domain. This molybdopterin cofactor (Moco) ...
 193-315 5.56e-07

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 cd00321:

Pssm-ID: 469652 [Multi-domain]  Cd Length: 156  Bit Score: 48.72  E-value: 5.56e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428257268 193 FYVNH----VVVGTERVKLQVG---KRELNLT--DLDKLPQVTLT---EPVGYRvgWPNGKI---QLHGVRMRDVLALAG 257
Cdd:cd00321    1 FVRNHggvpPEIDPDDWRLEVDglvEKPLSLTldDLKALPQVEVIatlHCVGNR--WGGGAVsnaEWTGVPLRDLLEEAG 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 428257268 258 VQlPSLGFVVVRG-----KPPIYNNpanpvtLPAANVRDCDIVLAtrWGEDKQLIPARKGGPI 315
Cdd:cd00321   79 PK-PGARYVVFEGaddpgGDGYTTS------LPLEKALDPDVLLA--YEMNGEPLPPDHGFPL 132
 
Name Accession Description Interval E-value
COG3915 COG3915
Uncharacterized conserved protein [Function unknown];
59-200 1.15e-33

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443120  Cd Length: 167  Bit Score: 121.92  E-value: 1.15e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428257268  59 PSEWNLVIQGE---TATGKPVKLDWQQLFALANTHVKTTDANQvvqrERIFDFRGIPVSGLLKNFGYQSnvTEVTFVCYD 135
Cdd:COG3915   28 AGPVILTVSGKignTNAGGAATFDLAMLEALPQTEITTTTPWT----DGVQTFRGVLLRDLLAAVGAKG--TTLRAVALN 101

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 428257268 136 AYQVTLPLTDLLAYPIILALTSNGKPIERDQGGPTYLVFPDTDFPQLLQKYDSSSWAFYVNHVVV 200
Cdd:COG3915  102 DYAVEIPISDLEEYGVILAYRMDGKPMSVRDKGPLWLIYPYDDYPELQTEVYYSRSVWQLKRIEV 166
arch_bact_SO_family_Moco cd02109
bacterial and archael members of the sulfite oxidase (SO) family of molybdopterin binding ...
 58-179 1.23e-14

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: 71.12  E-value: 1.23e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428257268  58 RPSEWNLVIQGETAtgKPVKLDWQQLFALANTHVkTTDANqVVQRERIFD--FRGIPVSGLLKNFGYQSNVTEVTFVCYD 135
Cdd:cd02109   23 DLEKWRLRVTGLVE--NPLSLTYEDLLALPQTEY-TADFH-CVTGWSKLDvvWEGVSLKDLLEAARPDPEATFVMAHSYD 98

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 428257268 136 AYQVTLPLTDLLAYPIILALTSNGKPIERDQGGPTYLVFPDTDF 179
Cdd:cd02109   99 GYTTNLPLEDLLREDSLLATKMDGEPLPPEHGGPARLVVPHLYF 142
Oxidored_molyb pfam00174
Oxidoreductase molybdopterin binding domain; This domain is found in a variety of ...
 58-175 4.14e-11

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: 60.59  E-value: 4.14e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428257268   58 RPSEWNLVIQGETatGKPVKLDWQQLFALANTHVKTT---------DANQV----VQRERIFD--FRGIPVSGLLKNFGY 122
Cdd:pfam00174   8 DPDTWRLRVDGLV--EKPLTLTLDDLKAFPQVTVTATlqcvgnrrkEMNRVkgvqWGGGAIGNaeWTGVPLRDLLERAGV 85

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 428257268  123 QSNVTEVTFVCYD-----AYQVTLPLTDLLAYPIILALTSNGKPIERDQGGPTYLVFP 175
Cdd:pfam00174  86 KPGAKHVLFEGADtlgdgGYTTSLPLEKALDDDVLLAYEMNGEPLPPDHGYPLRLVVP 143
SO_family_Moco cd00321
Sulfite oxidase (SO) family, molybdopterin binding domain. This molybdopterin cofactor (Moco) ...
 193-315 5.56e-07

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: 48.72  E-value: 5.56e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428257268 193 FYVNH----VVVGTERVKLQVG---KRELNLT--DLDKLPQVTLT---EPVGYRvgWPNGKI---QLHGVRMRDVLALAG 257
Cdd:cd00321    1 FVRNHggvpPEIDPDDWRLEVDglvEKPLSLTldDLKALPQVEVIatlHCVGNR--WGGGAVsnaEWTGVPLRDLLEEAG 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 428257268 258 VQlPSLGFVVVRG-----KPPIYNNpanpvtLPAANVRDCDIVLAtrWGEDKQLIPARKGGPI 315
Cdd:cd00321   79 PK-PGARYVVFEGaddpgGDGYTTS------LPLEKALDPDVLLA--YEMNGEPLPPDHGFPL 132
MsrP COG2041
Molybdopterin-dependent catalytic subunit of periplasmic DMSO/TMAO and ...
 188-315 1.59e-06

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: 47.84  E-value: 1.59e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428257268 188 SSSWAFYVNHV----VVGTERVKLQVG-----KRELNLTDLDKLPQVTLTepvgYRV----GWPNGKIQLHGVRMRDVLA 254
Cdd:COG2041   14 GGALAFPVRTAggvpEIDPADWRLRVDglvekPLTLTLDDLLALPLEERI----YRLhcveNWSGGVAPWTGVPLRDLLE 89

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 428257268 255 LAGVQlPSLGFVVVRGK-PPIYNNpanpvtLPAANVRDCDIVLATRW-GEDkqlIPARKGGPI 315
Cdd:COG2041   90 RAGPK-PGAKYVLFESAdPGYTES------LPLDEALDPDTLLAYGMnGEP---LPPEHGAPL 142
Oxidored_molyb pfam00174
Oxidoreductase molybdopterin binding domain; This domain is found in a variety of ...
 204-315 7.81e-05

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: 42.49  E-value: 7.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428257268  204 RVKLQVGK-RELNLTDLDKLPQVTLT---EPVGYR---------VGWPNGKI---QLHGVRMRDVLALAGVQlPSLGFVV 267
Cdd:pfam00174  15 RVDGLVEKpLTLTLDDLKAFPQVTVTatlQCVGNRrkemnrvkgVQWGGGAIgnaEWTGVPLRDLLERAGVK-PGAKHVL 93

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 428257268  268 VRGkppiYNNPANP---VTLPAANVRDCDIVLATRW-GEDkqlIPARKGGPI 315
Cdd:pfam00174  94 FEG----ADTLGDGgytTSLPLEKALDDDVLLAYEMnGEP---LPPDHGYPL 138
PRK05363 PRK05363
protein-methionine-sulfoxide reductase catalytic subunit MsrP;
40-132 2.41e-04

protein-methionine-sulfoxide reductase catalytic subunit MsrP;


Pssm-ID: 235431  Cd Length: 280  Bit Score: 42.12  E-value: 2.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428257268  40 KEAIARNAQivadnAKKTRPseWNLVIQGETAtgKPVKLDWQQLFALANthvkttdanqvvQRERIFDFR---------- 109
Cdd:PRK05363  48 KADPARNAG-----SLKTDP--WTVKIDGEVE--KPGTLDIDDLLKLFP------------LEERIYRLRcveawsmvip 106

                         90       100
                 ....*....|....*....|....*
gi 428257268 110 --GIPVSGLLKNFGYQSNVTEVTFV 132
Cdd:PRK05363 107 wiGFPLAKLLKRVEPTSNAKYVAFE 131
 
Name Accession Description Interval E-value
COG3915 COG3915
Uncharacterized conserved protein [Function unknown];
59-200 1.15e-33

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443120  Cd Length: 167  Bit Score: 121.92  E-value: 1.15e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428257268  59 PSEWNLVIQGE---TATGKPVKLDWQQLFALANTHVKTTDANQvvqrERIFDFRGIPVSGLLKNFGYQSnvTEVTFVCYD 135
Cdd:COG3915   28 AGPVILTVSGKignTNAGGAATFDLAMLEALPQTEITTTTPWT----DGVQTFRGVLLRDLLAAVGAKG--TTLRAVALN 101

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 428257268 136 AYQVTLPLTDLLAYPIILALTSNGKPIERDQGGPTYLVFPDTDFPQLLQKYDSSSWAFYVNHVVV 200
Cdd:COG3915  102 DYAVEIPISDLEEYGVILAYRMDGKPMSVRDKGPLWLIYPYDDYPELQTEVYYSRSVWQLKRIEV 166
MsrP COG2041
Molybdopterin-dependent catalytic subunit of periplasmic DMSO/TMAO and ...
 58-175 1.12e-14

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: 71.34  E-value: 1.12e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428257268  58 RPSEWNLVIQGETAtgKPVKLDWQQLFALANTHVKTTdaNQVVQRERIFD--FRGIPVSGLLKNFGYQSNVTEVTFVCYD 135
Cdd:COG2041   31 DPADWRLRVDGLVE--KPLTLTLDDLLALPLEERIYR--LHCVENWSGGVapWTGVPLRDLLERAGPKPGAKYVLFESAD 106

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 428257268 136 A-YQVTLPLTDLLAYPIILALTSNGKPIERDQGGPTYLVFP 175
Cdd:COG2041  107 PgYTESLPLDEALDPDTLLAYGMNGEPLPPEHGAPLRLVVP 147
arch_bact_SO_family_Moco cd02109
bacterial and archael members of the sulfite oxidase (SO) family of molybdopterin binding ...
 58-179 1.23e-14

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: 71.12  E-value: 1.23e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428257268  58 RPSEWNLVIQGETAtgKPVKLDWQQLFALANTHVkTTDANqVVQRERIFD--FRGIPVSGLLKNFGYQSNVTEVTFVCYD 135
Cdd:cd02109   23 DLEKWRLRVTGLVE--NPLSLTYEDLLALPQTEY-TADFH-CVTGWSKLDvvWEGVSLKDLLEAARPDPEATFVMAHSYD 98

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 428257268 136 AYQVTLPLTDLLAYPIILALTSNGKPIERDQGGPTYLVFPDTDF 179
Cdd:cd02109   99 GYTTNLPLEDLLREDSLLATKMDGEPLPPEHGGPARLVVPHLYF 142
Oxidored_molyb pfam00174
Oxidoreductase molybdopterin binding domain; This domain is found in a variety of ...
 58-175 4.14e-11

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: 60.59  E-value: 4.14e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428257268   58 RPSEWNLVIQGETatGKPVKLDWQQLFALANTHVKTT---------DANQV----VQRERIFD--FRGIPVSGLLKNFGY 122
Cdd:pfam00174   8 DPDTWRLRVDGLV--EKPLTLTLDDLKAFPQVTVTATlqcvgnrrkEMNRVkgvqWGGGAIGNaeWTGVPLRDLLERAGV 85

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 428257268  123 QSNVTEVTFVCYD-----AYQVTLPLTDLLAYPIILALTSNGKPIERDQGGPTYLVFP 175
Cdd:pfam00174  86 KPGAKHVLFEGADtlgdgGYTTSLPLEKALDDDVLLAYEMNGEPLPPDHGYPLRLVVP 143
SO_family_Moco cd00321
Sulfite oxidase (SO) family, molybdopterin binding domain. This molybdopterin cofactor (Moco) ...
 45-175 5.33e-10

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: 57.19  E-value: 5.33e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428257268  45 RNAQIVADNAKktrPSEWNLVIQGETAtgKPVKLDWQQLFALAnthvkttdanqvvQRERIFDFR--------------- 109
Cdd:cd00321    3 RNHGGVPPEID---PDDWRLEVDGLVE--KPLSLTLDDLKALP-------------QVEVIATLHcvgnrwgggavsnae 64

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 428257268 110 --GIPVSGLLKNFGYQSNVTEVTFVCYD-----AYQVTLPLTDLLAYPIILALTSNGKPIERDQGGPTYLVFP 175
Cdd:cd00321   65 wtGVPLRDLLEEAGPKPGARYVVFEGADdpggdGYTTSLPLEKALDPDVLLAYEMNGEPLPPDHGFPLRLVVP 137
SO_family_Moco cd00321
Sulfite oxidase (SO) family, molybdopterin binding domain. This molybdopterin cofactor (Moco) ...
 193-315 5.56e-07

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: 48.72  E-value: 5.56e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428257268 193 FYVNH----VVVGTERVKLQVG---KRELNLT--DLDKLPQVTLT---EPVGYRvgWPNGKI---QLHGVRMRDVLALAG 257
Cdd:cd00321    1 FVRNHggvpPEIDPDDWRLEVDglvEKPLSLTldDLKALPQVEVIatlHCVGNR--WGGGAVsnaEWTGVPLRDLLEEAG 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 428257268 258 VQlPSLGFVVVRG-----KPPIYNNpanpvtLPAANVRDCDIVLAtrWGEDKQLIPARKGGPI 315
Cdd:cd00321   79 PK-PGARYVVFEGaddpgGDGYTTS------LPLEKALDPDVLLA--YEMNGEPLPPDHGFPL 132
MsrP COG2041
Molybdopterin-dependent catalytic subunit of periplasmic DMSO/TMAO and ...
 188-315 1.59e-06

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: 47.84  E-value: 1.59e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428257268 188 SSSWAFYVNHV----VVGTERVKLQVG-----KRELNLTDLDKLPQVTLTepvgYRV----GWPNGKIQLHGVRMRDVLA 254
Cdd:COG2041   14 GGALAFPVRTAggvpEIDPADWRLRVDglvekPLTLTLDDLLALPLEERI----YRLhcveNWSGGVAPWTGVPLRDLLE 89

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 428257268 255 LAGVQlPSLGFVVVRGK-PPIYNNpanpvtLPAANVRDCDIVLATRW-GEDkqlIPARKGGPI 315
Cdd:COG2041   90 RAGPK-PGAKYVLFESAdPGYTES------LPLDEALDPDTLLAYGMnGEP---LPPEHGAPL 142
COG3915 COG3915
Uncharacterized conserved protein [Function unknown];
210-315 2.66e-06

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443120  Cd Length: 167  Bit Score: 46.81  E-value: 2.66e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428257268 210 GKRELNLTDLDKLPQV---TLTEpvgyrvgWPNGKIQLHGVRMRDVLALAGVQLPSLGFVVVRGkppiYNnpanpVTLPA 286
Cdd:COG3915   46 GAATFDLAMLEALPQTeitTTTP-------WTDGVQTFRGVLLRDLLAAVGAKGTTLRAVALND----YA-----VEIPI 109

                         90       100
                 ....*....|....*....|....*....
gi 428257268 287 ANVRDCDIVLATRwgEDKQLIPARKGGPI 315
Cdd:COG3915  110 SDLEEYGVILAYR--MDGKPMSVRDKGPL 136
SO_family_Moco_dimer cd02110
Subgroup of sulfite oxidase (SO) family molybdopterin binding domains that contains conserved ...
 108-175 2.27e-05

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: 45.37  E-value: 2.27e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 428257268 108 FRGIPVSGLLKNFGYQSNVTEVTFVCYD--------AYQVTLPLTDLLAYPIILALTSNGKPIERDQGGPTYLVFP 175
Cdd:cd02110   78 WTGVPLKDLLEEAGVKPGAKHVLFEGADvppgekaaDYTRSVPLSKALDDDALLAYEMNGEPLPPDHGYPLRLVVP 153
SO_family_Moco_dimer cd02110
Subgroup of sulfite oxidase (SO) family molybdopterin binding domains that contains conserved ...
 192-317 4.10e-05

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: 44.60  E-value: 4.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428257268 192 AFYV-NH---VVVGTERVKLQVG---KRELNLT--DLDKLPQVTLT-------------EPVGYRVGWPNGKI---QLHG 246
Cdd:cd02110    1 LFFVrNHggvPDIDPDAWRLEIHglvERPLTLTldDLKRLPSVEVVatlecsgngrggfIPVRSGAQWGHGAVgnaRWTG 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 428257268 247 VRMRDVLALAGVQlPSLGFVVVRG--KPPIYNNPANPVTLPAANVRDCDIVLAtrWGEDKQLIPARKGGPITL 317
Cdd:cd02110   81 VPLKDLLEEAGVK-PGAKHVLFEGadVPPGEKAADYTRSVPLSKALDDDALLA--YEMNGEPLPPDHGYPLRL 150
Oxidored_molyb pfam00174
Oxidoreductase molybdopterin binding domain; This domain is found in a variety of ...
 204-315 7.81e-05

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: 42.49  E-value: 7.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428257268  204 RVKLQVGK-RELNLTDLDKLPQVTLT---EPVGYR---------VGWPNGKI---QLHGVRMRDVLALAGVQlPSLGFVV 267
Cdd:pfam00174  15 RVDGLVEKpLTLTLDDLKAFPQVTVTatlQCVGNRrkemnrvkgVQWGGGAIgnaEWTGVPLRDLLERAGVK-PGAKHVL 93

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 428257268  268 VRGkppiYNNPANP---VTLPAANVRDCDIVLATRW-GEDkqlIPARKGGPI 315
Cdd:pfam00174  94 FEG----ADTLGDGgytTSLPLEKALDDDVLLAYEMnGEP---LPPDHGYPL 138
PRK05363 PRK05363
protein-methionine-sulfoxide reductase catalytic subunit MsrP;
40-132 2.41e-04

protein-methionine-sulfoxide reductase catalytic subunit MsrP;


Pssm-ID: 235431  Cd Length: 280  Bit Score: 42.12  E-value: 2.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428257268  40 KEAIARNAQivadnAKKTRPseWNLVIQGETAtgKPVKLDWQQLFALANthvkttdanqvvQRERIFDFR---------- 109
Cdd:PRK05363  48 KADPARNAG-----SLKTDP--WTVKIDGEVE--KPGTLDIDDLLKLFP------------LEERIYRLRcveawsmvip 106

                         90       100
                 ....*....|....*....|....*
gi 428257268 110 --GIPVSGLLKNFGYQSNVTEVTFV 132
Cdd:PRK05363 107 wiGFPLAKLLKRVEPTSNAKYVAFE 131
bact_SorA_Moco cd02114
sulfite:cytochrome c oxidoreductase subunit A (SorA), molybdopterin binding domain. SorA is ...
 240-317 4.29e-03

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: 38.65  E-value: 4.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 428257268 240 GKIQLHGVRMRDVLALAGVQlPSLGFVVVRG--KPPIYNNPANPVTLPAANVRDCDIVLAtrWGEDKQLIPARKGGPITL 317
Cdd:cd02114  122 GNARWAGVPLKAVLAKAGVQ-DGARQVAFRGldQPVLDVTPDFVKSLDIDHALDGEVMLA--WEMNGEPLPVLNGYPLRL 198
 
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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