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Conserved domains on  [gi|674227948|gb|KFK01312|]
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hypothetical protein BF23_01485 [Klebsiella variicola]

Protein Classification

protein-methionine-sulfoxide reductase catalytic subunit MsrP( domain architecture ID 10012348)

protein-methionine-sulfoxide reductase catalytic subunit MsrP is part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons

CATH:  3.90.420.10
EC:  1.8.5.-
Gene Ontology:  GO:0046872|GO:0016672|GO:0006979|GO:0043546|GO:0030091
PubMed:  25968643|9990727|12114025
SCOP:  4002574

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK05363 PRK05363
protein-methionine-sulfoxide reductase catalytic subunit MsrP;
1-211 9.72e-169

protein-methionine-sulfoxide reductase catalytic subunit MsrP;


:

Pssm-ID: 235431  Cd Length: 280  Bit Score: 464.69  E-value: 9.72e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674227948   1 MTLDHDDLTKRFPLEERIYRMRCVEAWSMVVPWVGFPLHKLLALVEPTSNARYVAFKTLYAPDQMPGQKDRFigggLAYP 80
Cdd:PRK05363  75 GTLDIDDLLKLFPLEERIYRLRCVEAWSMVIPWIGFPLAKLLKRVEPTSNAKYVAFETLYDPEQMPGQRSRF----LDWP 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674227948  81 YVEGLRLDEAMHPLTLLTVGVYGKALPPQNGAPIRLTVPWKYGFKGIKSIVSIELTREQPPTTWNLAAPDEYGFFANVNP 160
Cdd:PRK05363 151 YVEGLRLDEAMHPLTLLAVGLYGKTLPNQNGAPIRLVVPWKYGFKSIKSIVRIRLTEEQPPTTWNLLAPNEYGFYANVNP 230

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 674227948 161 HVDHPRWSQASERFIGSGGVLdVKRQPTLLFNGYADEVASLYRGMNLRENF 211
Cdd:PRK05363 231 NVDHPRWSQATERRIGEGGLF-AERRPTLMFNGYGEQVASLYAGMDLRKNF 280
 
Name Accession Description Interval E-value
PRK05363 PRK05363
protein-methionine-sulfoxide reductase catalytic subunit MsrP;
1-211 9.72e-169

protein-methionine-sulfoxide reductase catalytic subunit MsrP;


Pssm-ID: 235431  Cd Length: 280  Bit Score: 464.69  E-value: 9.72e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674227948   1 MTLDHDDLTKRFPLEERIYRMRCVEAWSMVVPWVGFPLHKLLALVEPTSNARYVAFKTLYAPDQMPGQKDRFigggLAYP 80
Cdd:PRK05363  75 GTLDIDDLLKLFPLEERIYRLRCVEAWSMVIPWIGFPLAKLLKRVEPTSNAKYVAFETLYDPEQMPGQRSRF----LDWP 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674227948  81 YVEGLRLDEAMHPLTLLTVGVYGKALPPQNGAPIRLTVPWKYGFKGIKSIVSIELTREQPPTTWNLAAPDEYGFFANVNP 160
Cdd:PRK05363 151 YVEGLRLDEAMHPLTLLAVGLYGKTLPNQNGAPIRLVVPWKYGFKSIKSIVRIRLTEEQPPTTWNLLAPNEYGFYANVNP 230

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 674227948 161 HVDHPRWSQASERFIGSGGVLdVKRQPTLLFNGYADEVASLYRGMNLRENF 211
Cdd:PRK05363 231 NVDHPRWSQATERRIGEGGLF-AERRPTLMFNGYGEQVASLYAGMDLRKNF 280
YedY_like_Moco cd02107
YedY_like molybdopterin cofactor (Moco) binding domain, a subgroup of the sulfite oxidase (SO) ...
 2-179 3.14e-131

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: 367.55  E-value: 3.14e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674227948   2 TLDHDDLTKRFPLEERIYRMRCVEAWSMVVPWVGFPLHKLLALVEPTSNARYVAFKTLYAPDQMPGQKDRFigGGLAYPY 81
Cdd:cd02107   41 TLDIDDLMKTFPLEERIYRFRCVEGWSMVVPWVGFPLAALLARAEPTSEAKYVRFTTLLDKEQMPGQSGLF--GVLPWPY 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674227948  82 VEGLRLDEAMHPLTLLTVGVYGKALPPQNGAPIRLTVPWKYGFKGIKSIVSIELTREQPPTTWNLAAPDEYGFFANVNPH 161
Cdd:cd02107  119 VEGLRLDEAMHPLTLLAVGLYGEALPKQNGAPIRLVVPWKYGFKSIKSIVKIEFTKEQPPTTWNLAAPDEYGFYANVNPS 198

                        170
                 ....*....|....*...
gi 674227948 162 VDHPRWSQASERFIGSGG 179
Cdd:cd02107  199 VDHPRWSQATERRIGEGG 216
MsrP COG2041
Molybdopterin-dependent catalytic subunit of periplasmic DMSO/TMAO and ...
 1-158 1.61e-64

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: 197.30  E-value: 1.61e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674227948   1 MTLDHDDLtKRFPLEERIYRMRCVEAWS-MVVPWVGFPLHKLLALVEPTSNARYVAFKTLYAPdqmpgqkdrfiggglay 79
Cdd:COG2041   47 LTLTLDDL-LALPLEERIYRLHCVENWSgGVAPWTGVPLRDLLERAGPKPGAKYVLFESADPG----------------- 108

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 674227948  80 pYVEGLRLDEAMHPLTLLTVGVYGKALPPQNGAPIRLTVPWKYGFKGIKSIVSIELTREQPPTTWNLAApdeYGFFANV 158
Cdd:COG2041  109 -YTESLPLDEALDPDTLLAYGMNGEPLPPEHGAPLRLVVPGLYGFKSAKWLVRIEVTDEDPPGYWETRG---YHFYANI 183
Oxidored_molyb pfam00174
Oxidoreductase molybdopterin binding domain; This domain is found in a variety of ...
 1-144 1.73e-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: 115.29  E-value: 1.73e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674227948    1 MTLDHDDLtKRFPLEERIYRMRCVE------------AW----SMVVPWVGFPLHKLLALVEPTSNARYVAFktlYAPDQ 64
Cdd:pfam00174  24 LTLTLDDL-KAFPQVTVTATLQCVGnrrkemnrvkgvQWgggaIGNAEWTGVPLRDLLERAGVKPGAKHVLF---EGADT 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674227948   65 MPGqkdrfiggglaYPYVEGLRLDEAMHPLTLLTVGVYGKALPPQNGAPIRLTVPWKYGFKGIKSIVSIELTREQPPTTW 144
Cdd:pfam00174 100 LGD-----------GGYTTSLPLEKALDDDVLLAYEMNGEPLPPDHGYPLRLVVPGWYGARSVKWLRRIEVTDEESPGFW 168
 
Name Accession Description Interval E-value
PRK05363 PRK05363
protein-methionine-sulfoxide reductase catalytic subunit MsrP;
1-211 9.72e-169

protein-methionine-sulfoxide reductase catalytic subunit MsrP;


Pssm-ID: 235431  Cd Length: 280  Bit Score: 464.69  E-value: 9.72e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674227948   1 MTLDHDDLTKRFPLEERIYRMRCVEAWSMVVPWVGFPLHKLLALVEPTSNARYVAFKTLYAPDQMPGQKDRFigggLAYP 80
Cdd:PRK05363  75 GTLDIDDLLKLFPLEERIYRLRCVEAWSMVIPWIGFPLAKLLKRVEPTSNAKYVAFETLYDPEQMPGQRSRF----LDWP 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674227948  81 YVEGLRLDEAMHPLTLLTVGVYGKALPPQNGAPIRLTVPWKYGFKGIKSIVSIELTREQPPTTWNLAAPDEYGFFANVNP 160
Cdd:PRK05363 151 YVEGLRLDEAMHPLTLLAVGLYGKTLPNQNGAPIRLVVPWKYGFKSIKSIVRIRLTEEQPPTTWNLLAPNEYGFYANVNP 230

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 674227948 161 HVDHPRWSQASERFIGSGGVLdVKRQPTLLFNGYADEVASLYRGMNLRENF 211
Cdd:PRK05363 231 NVDHPRWSQATERRIGEGGLF-AERRPTLMFNGYGEQVASLYAGMDLRKNF 280
YedY_like_Moco cd02107
YedY_like molybdopterin cofactor (Moco) binding domain, a subgroup of the sulfite oxidase (SO) ...
 2-179 3.14e-131

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: 367.55  E-value: 3.14e-131
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674227948   2 TLDHDDLTKRFPLEERIYRMRCVEAWSMVVPWVGFPLHKLLALVEPTSNARYVAFKTLYAPDQMPGQKDRFigGGLAYPY 81
Cdd:cd02107   41 TLDIDDLMKTFPLEERIYRFRCVEGWSMVVPWVGFPLAALLARAEPTSEAKYVRFTTLLDKEQMPGQSGLF--GVLPWPY 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674227948  82 VEGLRLDEAMHPLTLLTVGVYGKALPPQNGAPIRLTVPWKYGFKGIKSIVSIELTREQPPTTWNLAAPDEYGFFANVNPH 161
Cdd:cd02107  119 VEGLRLDEAMHPLTLLAVGLYGEALPKQNGAPIRLVVPWKYGFKSIKSIVKIEFTKEQPPTTWNLAAPDEYGFYANVNPS 198

                        170
                 ....*....|....*...
gi 674227948 162 VDHPRWSQASERFIGSGG 179
Cdd:cd02107  199 VDHPRWSQATERRIGEGG 216
MsrP COG2041
Molybdopterin-dependent catalytic subunit of periplasmic DMSO/TMAO and ...
 1-158 1.61e-64

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: 197.30  E-value: 1.61e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674227948   1 MTLDHDDLtKRFPLEERIYRMRCVEAWS-MVVPWVGFPLHKLLALVEPTSNARYVAFKTLYAPdqmpgqkdrfiggglay 79
Cdd:COG2041   47 LTLTLDDL-LALPLEERIYRLHCVENWSgGVAPWTGVPLRDLLERAGPKPGAKYVLFESADPG----------------- 108

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 674227948  80 pYVEGLRLDEAMHPLTLLTVGVYGKALPPQNGAPIRLTVPWKYGFKGIKSIVSIELTREQPPTTWNLAApdeYGFFANV 158
Cdd:COG2041  109 -YTESLPLDEALDPDTLLAYGMNGEPLPPEHGAPLRLVVPGLYGFKSAKWLVRIEVTDEDPPGYWETRG---YHFYANI 183
SO_family_Moco cd00321
Sulfite oxidase (SO) family, molybdopterin binding domain. This molybdopterin cofactor (Moco) ...
 1-138 1.33e-43

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: 143.09  E-value: 1.33e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674227948   1 MTLDHDDLtKRFPLEERIYRMRCVE-----AWSMVVPWVGFPLHKLLALVEPTSNARYVAFktlYAPDQMPGqkdrfigg 75
Cdd:cd00321   29 LSLTLDDL-KALPQVEVIATLHCVGnrwggGAVSNAEWTGVPLRDLLEEAGPKPGARYVVF---EGADDPGG-------- 96

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 674227948  76 glaYPYVEGLRLDEAMHPLTLLTVGVYGKALPPQNGAPIRLTVPWKYGFKGIKSIVSIELTRE 138
Cdd:cd00321   97 ---DGYTTSLPLEKALDPDVLLAYEMNGEPLPPDHGFPLRLVVPGLYGWKSVKWLRRIEVTDE 156
Oxidored_molyb pfam00174
Oxidoreductase molybdopterin binding domain; This domain is found in a variety of ...
 1-144 1.73e-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: 115.29  E-value: 1.73e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674227948    1 MTLDHDDLtKRFPLEERIYRMRCVE------------AW----SMVVPWVGFPLHKLLALVEPTSNARYVAFktlYAPDQ 64
Cdd:pfam00174  24 LTLTLDDL-KAFPQVTVTATLQCVGnrrkemnrvkgvQWgggaIGNAEWTGVPLRDLLERAGVKPGAKHVLF---EGADT 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674227948   65 MPGqkdrfiggglaYPYVEGLRLDEAMHPLTLLTVGVYGKALPPQNGAPIRLTVPWKYGFKGIKSIVSIELTREQPPTTW 144
Cdd:pfam00174 100 LGD-----------GGYTTSLPLEKALDDDVLLAYEMNGEPLPPDHGYPLRLVVPGWYGARSVKWLRRIEVTDEESPGFW 168
bact_SO_family_Moco cd02108
bacterial subgroup of the sulfite oxidase (SO) family of molybdopterin binding domains. This ...
 1-136 3.52e-29

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: 107.09  E-value: 3.52e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674227948   1 MTLDHDDLtKRFPLEERIYRMRCVEAWSMVVPWVGFPLHKLLALVEPTSNARYVAFKTLyapdqmpgqkDRFIGGGLayp 80
Cdd:cd02108   41 LSLSLEEL-RALPQRTQITRHICVEGWSAIGKWGGVPLRTILELVGPLPEAKYVVFKCA----------DDFAGGDR--- 106

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 674227948  81 YVEGLRLDEAMHPLTLLTVGVYGKALPPQNGAPIRLTVPWKYGFKGIKSIVSIELT 136
Cdd:cd02108  107 YYESIDMASALHPQTLLAYEMNGQPLPIKNGAPLRLRVETQLGYKQAKWVTEIELV 162
arch_bact_SO_family_Moco cd02109
bacterial and archael members of the sulfite oxidase (SO) family of molybdopterin binding ...
 1-160 2.03e-16

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: 73.82  E-value: 2.03e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674227948   1 MTLDHDDLTKrFPLEERIYRMRCVEAWSMV-VPWVGFPLHKLLALVEPTSNARYVAFKTLYApdqmpgqkdrfiggglay 79
Cdd:cd02109   39 LSLTYEDLLA-LPQTEYTADFHCVTGWSKLdVVWEGVSLKDLLEAARPDPEATFVMAHSYDG------------------ 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674227948  80 pYVEGLRLDEAMHPLTLLTVGVYGKALPPQNGAPIRLTVPWKYGFKGIKSIVSIELTREQPPTTWnlaapDEYGFFANVN 159
Cdd:cd02109  100 -YTTNLPLEDLLREDSLLATKMDGEPLPPEHGGPARLVVPHLYFWKSAKWLRGIEFLDEDEPGFW-----ERRGYHERGD 173


                 .
gi 674227948 160 P 160
Cdd:cd02109  174 P 174
SO_family_Moco_dimer cd02110
Subgroup of sulfite oxidase (SO) family molybdopterin binding domains that contains conserved ...
 1-140 2.04e-14

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: 70.41  E-value: 2.04e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674227948   1 MTLDHDDLtKRFPLEERIYRMRCV----EAWSMVVP-------------WVGFPLHKLLALVEPTSNARYVAFktlYAPD 63
Cdd:cd02110   30 LTLTLDDL-KRLPSVEVVATLECSgngrGGFIPVRSgaqwghgavgnarWTGVPLKDLLEEAGVKPGAKHVLF---EGAD 105

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 674227948  64 QMPGQKdrfiggglAYPYVEGLRLDEAMHPLTLLTVGVYGKALPPQNGAPIRLTVPWKYGFKGIKSIVSIELTrEQP 140
Cdd:cd02110  106 VPPGEK--------AADYTRSVPLSKALDDDALLAYEMNGEPLPPDHGYPLRLVVPGWYGARSVKWLRRIEVT-DQP 173
PLN02252 PLN02252
nitrate reductase [NADPH]
 33-136 6.24e-05

nitrate reductase [NADPH]


Pssm-ID: 215141 [Multi-domain]  Cd Length: 888  Bit Score: 43.13  E-value: 6.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674227948  33 WVGFPLHKLLA---LVEPTSNARYVAFKtlyAPDQMPGqkdrfiGGGLAYPyvEGLRLDEAMHPL--TLLTVGVYGKALP 107
Cdd:PLN02252 196 WRGVRLRDVLRrcgVMSRKGGALNVCFE---GAEDLPG------GGGSKYG--TSITLERAMDPArdVILAYMQNGEPLT 264

                         90       100       110
                 ....*....|....*....|....*....|..
gi 674227948 108 PQNGAPIRLTVPwkyGFKG---IKSIVSIELT 136
Cdd:PLN02252 265 PDHGFPVRLIIP---GFIGgrmVKWLKRIIVT 293
bact_SoxC_Moco cd02113
bacterial SoxC is a member of the sulfite oxidase (SO) family of molybdopterin binding domains. ...
 6-140 3.74e-04

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: 40.46  E-value: 3.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674227948   6 DDLtKRFPLEERIYRMRCVEAWSMvvPWVGFPLHKLLALVEPTSNARY--VAFKTLY-APDQMPGQKDRFIGGGLAYPYV 82
Cdd:cd02113   48 DDL-KRFPSVSRIYFLECSGNGGT--GWRGAPLPTAQYTHGMLSCSEWtgVPLSTLLeEAGVKPGAKWLLAEGADAAAMT 124

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 674227948  83 EGLRLDEAMHPlTLLTVGVYGKALPPQNGAPIRLTVPwkyGFKG---IKSIVSIELTrEQP 140
Cdd:cd02113  125 RSIPLEKALDD-ALVAYAQNGEALRPENGYPLRLVVP---GWEGntnVKWLRRIEVG-DQP 180
 
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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