|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05363 |
PRK05363 |
protein-methionine-sulfoxide reductase catalytic subunit MsrP; |
1-333 |
0e+00 |
|
protein-methionine-sulfoxide reductase catalytic subunit MsrP;
Pssm-ID: 235431 Cd Length: 280 Bit Score: 564.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384914 1 MKTRKLTEADVTSESVFmLQRRQILKmlgisataltltpaahadlldwfkgndrpkapsgaplnftkpaqwqnklaLTPE 80
Cdd:PRK05363 4 KKPWKLPESEVTPESVY-LNRRRFLK--------------------------------------------------LTPE 32
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384914 81 DKVTGYNNFYEFGLDKADPAANAGSMKTDPWTLKIDGEVAKPLTLDHHDLTTRFPLEERIYRMRCVEAWSMVVPWVGFPL 160
Cdd:PRK05363 33 EDVTTYNNFYEFGTDKADPARNAGSLKTDPWTVKIDGEVEKPGTLDIDDLLKLFPLEERIYRLRCVEAWSMVIPWIGFPL 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384914 161 HKLLALVEPTSNAKYVSFQTRYAPDEMPGQKDRFigggLEYPYVEGLRLDEAMHPLTLLTVGVYGKALPPQNGAPIRLTV 240
Cdd:PRK05363 113 AKLLKRVEPTSNAKYVAFETLYDPEQMPGQRSRF----LDWPYVEGLRLDEAMHPLTLLAVGLYGKTLPNQNGAPIRLVV 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384914 241 PWKYGFKGIKSIVSIKLTRERPPTTWNLAAPDEYGFFANVNPHVDHPRWSQATERFIGSGGaLDVKRQPTLLFNGYADEV 320
Cdd:PRK05363 189 PWKYGFKSIKSIVRIRLTEEQPPTTWNLLAPNEYGFYANVNPNVDHPRWSQATERRIGEGG-LFAERRPTLMFNGYGEQV 267
|
330
....*....|...
gi 505384914 321 ASLYRGLNLRENF 333
Cdd:PRK05363 268 ASLYAGMDLRKNF 280
|
|
| YedY_like_Moco |
cd02107 |
YedY_like molybdopterin cofactor (Moco) binding domain, a subgroup of the sulfite oxidase (SO) ... |
84-301 |
4.82e-154 |
|
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: 430.72 E-value: 4.82e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384914 84 TGYNNFYEFGLDKADPAANAGSMKTDPWTLKIDGEVAKPLTLDHHDLTTRFPLEERIYRMRCVEAWSMVVPWVGFPLHKL 163
Cdd:cd02107 1 TTYNNFYEFGTGKDDPARNAGNLPTRPWTVSVSGLVKKPKTLDIDDLMKTFPLEERIYRFRCVEGWSMVVPWVGFPLAAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384914 164 LALVEPTSNAKYVSFQTRYAPDEMPGQKDRFigGGLEYPYVEGLRLDEAMHPLTLLTVGVYGKALPPQNGAPIRLTVPWK 243
Cdd:cd02107 81 LARAEPTSEAKYVRFTTLLDKEQMPGQSGLF--GVLPWPYVEGLRLDEAMHPLTLLAVGLYGEALPKQNGAPIRLVVPWK 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 505384914 244 YGFKGIKSIVSIKLTRERPPTTWNLAAPDEYGFFANVNPHVDHPRWSQATERFIGSGG 301
Cdd:cd02107 159 YGFKSIKSIVKIEFTKEQPPTTWNLAAPDEYGFYANVNPSVDHPRWSQATERRIGEGG 216
|
|
| MsrP |
COG2041 |
Molybdopterin-dependent catalytic subunit of periplasmic DMSO/TMAO and ... |
90-280 |
1.29e-73 |
|
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: 225.04 E-value: 1.29e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384914 90 YEFGLDKADPAanagsMKTDPWTLKIDGEVAKPLTLDHHDLTtRFPLEERIYRMRCVEAWS-MVVPWVGFPLHKLLALVE 168
Cdd:COG2041 19 FPVRTAGGVPE-----IDPADWRLRVDGLVEKPLTLTLDDLL-ALPLEERIYRLHCVENWSgGVAPWTGVPLRDLLERAG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384914 169 PTSNAKYVSFQtryapdempgqkdrfiggGLEYPYVEGLRLDEAMHPLTLLTVGVYGKALPPQNGAPIRLTVPWKYGFKG 248
Cdd:COG2041 93 PKPGAKYVLFE------------------SADPGYTESLPLDEALDPDTLLAYGMNGEPLPPEHGAPLRLVVPGLYGFKS 154
|
170 180 190
....*....|....*....|....*....|..
gi 505384914 249 IKSIVSIKLTRERPPTTWNLAApdeYGFFANV 280
Cdd:COG2041 155 AKWLVRIEVTDEDPPGYWETRG---YHFYANI 183
|
|
| Oxidored_molyb |
pfam00174 |
Oxidoreductase molybdopterin binding domain; This domain is found in a variety of ... |
108-266 |
1.59e-37 |
|
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: 131.85 E-value: 1.59e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384914 108 TDPWTLKIDGEVAKPLTLDHHDLTtRFPLEERIYRMRCVE------------AW----SMVVPWVGFPLHKLLALVEPTS 171
Cdd:pfam00174 9 PDTWRLRVDGLVEKPLTLTLDDLK-AFPQVTVTATLQCVGnrrkemnrvkgvQWgggaIGNAEWTGVPLRDLLERAGVKP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384914 172 NAKYVSFqtrYAPDEMPGqkdrfigggleYPYVEGLRLDEAMHPLTLLTVGVYGKALPPQNGAPIRLTVPWKYGFKGIKS 251
Cdd:pfam00174 88 GAKHVLF---EGADTLGD-----------GGYTTSLPLEKALDDDVLLAYEMNGEPLPPDHGYPLRLVVPGWYGARSVKW 153
|
170
....*....|....*
gi 505384914 252 IVSIKLTRERPPTTW 266
Cdd:pfam00174 154 LRRIEVTDEESPGFW 168
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05363 |
PRK05363 |
protein-methionine-sulfoxide reductase catalytic subunit MsrP; |
1-333 |
0e+00 |
|
protein-methionine-sulfoxide reductase catalytic subunit MsrP;
Pssm-ID: 235431 Cd Length: 280 Bit Score: 564.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384914 1 MKTRKLTEADVTSESVFmLQRRQILKmlgisataltltpaahadlldwfkgndrpkapsgaplnftkpaqwqnklaLTPE 80
Cdd:PRK05363 4 KKPWKLPESEVTPESVY-LNRRRFLK--------------------------------------------------LTPE 32
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384914 81 DKVTGYNNFYEFGLDKADPAANAGSMKTDPWTLKIDGEVAKPLTLDHHDLTTRFPLEERIYRMRCVEAWSMVVPWVGFPL 160
Cdd:PRK05363 33 EDVTTYNNFYEFGTDKADPARNAGSLKTDPWTVKIDGEVEKPGTLDIDDLLKLFPLEERIYRLRCVEAWSMVIPWIGFPL 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384914 161 HKLLALVEPTSNAKYVSFQTRYAPDEMPGQKDRFigggLEYPYVEGLRLDEAMHPLTLLTVGVYGKALPPQNGAPIRLTV 240
Cdd:PRK05363 113 AKLLKRVEPTSNAKYVAFETLYDPEQMPGQRSRF----LDWPYVEGLRLDEAMHPLTLLAVGLYGKTLPNQNGAPIRLVV 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384914 241 PWKYGFKGIKSIVSIKLTRERPPTTWNLAAPDEYGFFANVNPHVDHPRWSQATERFIGSGGaLDVKRQPTLLFNGYADEV 320
Cdd:PRK05363 189 PWKYGFKSIKSIVRIRLTEEQPPTTWNLLAPNEYGFYANVNPNVDHPRWSQATERRIGEGG-LFAERRPTLMFNGYGEQV 267
|
330
....*....|...
gi 505384914 321 ASLYRGLNLRENF 333
Cdd:PRK05363 268 ASLYAGMDLRKNF 280
|
|
| YedY_like_Moco |
cd02107 |
YedY_like molybdopterin cofactor (Moco) binding domain, a subgroup of the sulfite oxidase (SO) ... |
84-301 |
4.82e-154 |
|
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: 430.72 E-value: 4.82e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384914 84 TGYNNFYEFGLDKADPAANAGSMKTDPWTLKIDGEVAKPLTLDHHDLTTRFPLEERIYRMRCVEAWSMVVPWVGFPLHKL 163
Cdd:cd02107 1 TTYNNFYEFGTGKDDPARNAGNLPTRPWTVSVSGLVKKPKTLDIDDLMKTFPLEERIYRFRCVEGWSMVVPWVGFPLAAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384914 164 LALVEPTSNAKYVSFQTRYAPDEMPGQKDRFigGGLEYPYVEGLRLDEAMHPLTLLTVGVYGKALPPQNGAPIRLTVPWK 243
Cdd:cd02107 81 LARAEPTSEAKYVRFTTLLDKEQMPGQSGLF--GVLPWPYVEGLRLDEAMHPLTLLAVGLYGEALPKQNGAPIRLVVPWK 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 505384914 244 YGFKGIKSIVSIKLTRERPPTTWNLAAPDEYGFFANVNPHVDHPRWSQATERFIGSGG 301
Cdd:cd02107 159 YGFKSIKSIVKIEFTKEQPPTTWNLAAPDEYGFYANVNPSVDHPRWSQATERRIGEGG 216
|
|
| MsrP |
COG2041 |
Molybdopterin-dependent catalytic subunit of periplasmic DMSO/TMAO and ... |
90-280 |
1.29e-73 |
|
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: 225.04 E-value: 1.29e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384914 90 YEFGLDKADPAanagsMKTDPWTLKIDGEVAKPLTLDHHDLTtRFPLEERIYRMRCVEAWS-MVVPWVGFPLHKLLALVE 168
Cdd:COG2041 19 FPVRTAGGVPE-----IDPADWRLRVDGLVEKPLTLTLDDLL-ALPLEERIYRLHCVENWSgGVAPWTGVPLRDLLERAG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384914 169 PTSNAKYVSFQtryapdempgqkdrfiggGLEYPYVEGLRLDEAMHPLTLLTVGVYGKALPPQNGAPIRLTVPWKYGFKG 248
Cdd:COG2041 93 PKPGAKYVLFE------------------SADPGYTESLPLDEALDPDTLLAYGMNGEPLPPEHGAPLRLVVPGLYGFKS 154
|
170 180 190
....*....|....*....|....*....|..
gi 505384914 249 IKSIVSIKLTRERPPTTWNLAApdeYGFFANV 280
Cdd:COG2041 155 AKWLVRIEVTDEDPPGYWETRG---YHFYANI 183
|
|
| SO_family_Moco |
cd00321 |
Sulfite oxidase (SO) family, molybdopterin binding domain. This molybdopterin cofactor (Moco) ... |
86-260 |
3.16e-51 |
|
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: 166.98 E-value: 3.16e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384914 86 YNNFYEFGLDKADPaanagsmktDPWTLKIDGEVAKPLTLDHHDLTtRFPLEERIYRMRCVE-----AWSMVVPWVGFPL 160
Cdd:cd00321 1 FVRNHGGVPPEIDP---------DDWRLEVDGLVEKPLSLTLDDLK-ALPQVEVIATLHCVGnrwggGAVSNAEWTGVPL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384914 161 HKLLALVEPTSNAKYVSFqtrYAPDEMPGqkdrfigggleYPYVEGLRLDEAMHPLTLLTVGVYGKALPPQNGAPIRLTV 240
Cdd:cd00321 71 RDLLEEAGPKPGARYVVF---EGADDPGG-----------DGYTTSLPLEKALDPDVLLAYEMNGEPLPPDHGFPLRLVV 136
|
170 180
....*....|....*....|
gi 505384914 241 PWKYGFKGIKSIVSIKLTRE 260
Cdd:cd00321 137 PGLYGWKSVKWLRRIEVTDE 156
|
|
| Oxidored_molyb |
pfam00174 |
Oxidoreductase molybdopterin binding domain; This domain is found in a variety of ... |
108-266 |
1.59e-37 |
|
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: 131.85 E-value: 1.59e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384914 108 TDPWTLKIDGEVAKPLTLDHHDLTtRFPLEERIYRMRCVE------------AW----SMVVPWVGFPLHKLLALVEPTS 171
Cdd:pfam00174 9 PDTWRLRVDGLVEKPLTLTLDDLK-AFPQVTVTATLQCVGnrrkemnrvkgvQWgggaIGNAEWTGVPLRDLLERAGVKP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384914 172 NAKYVSFqtrYAPDEMPGqkdrfigggleYPYVEGLRLDEAMHPLTLLTVGVYGKALPPQNGAPIRLTVPWKYGFKGIKS 251
Cdd:pfam00174 88 GAKHVLF---EGADTLGD-----------GGYTTSLPLEKALDDDVLLAYEMNGEPLPPDHGYPLRLVVPGWYGARSVKW 153
|
170
....*....|....*
gi 505384914 252 IVSIKLTRERPPTTW 266
Cdd:pfam00174 154 LRRIEVTDEESPGFW 168
|
|
| bact_SO_family_Moco |
cd02108 |
bacterial subgroup of the sulfite oxidase (SO) family of molybdopterin binding domains. This ... |
95-258 |
2.53e-31 |
|
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: 116.33 E-value: 2.53e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384914 95 DKADPAANA--GSMKTDP--WTLKIDGEVAKPLTLDHHDLTtRFPLEERIYRMRCVEAWSMVVPWVGFPLHKLLALVEPT 170
Cdd:cd02108 9 GIRKPEALAykALEANDFadYRLEVGGLVEHPLSLSLEELR-ALPQRTQITRHICVEGWSAIGKWGGVPLRTILELVGPL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384914 171 SNAKYVSFQTryapdempgqKDRFIGGGLeypYVEGLRLDEAMHPLTLLTVGVYGKALPPQNGAPIRLTVPWKYGFKGIK 250
Cdd:cd02108 88 PEAKYVVFKC----------ADDFAGGDR---YYESIDMASALHPQTLLAYEMNGQPLPIKNGAPLRLRVETQLGYKQAK 154
|
....*...
gi 505384914 251 SIVSIKLT 258
Cdd:cd02108 155 WVTEIELV 162
|
|
| arch_bact_SO_family_Moco |
cd02109 |
bacterial and archael members of the sulfite oxidase (SO) family of molybdopterin binding ... |
107-282 |
2.36e-21 |
|
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: 89.61 E-value: 2.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384914 107 KTDPWTLKIDGEVAKPLTLDHHDLTtRFPLEERIYRMRCVEAWSMV-VPWVGFPLHKLLALVEPTSNAKYVSFqtryapd 185
Cdd:cd02109 23 DLEKWRLRVTGLVENPLSLTYEDLL-ALPQTEYTADFHCVTGWSKLdVVWEGVSLKDLLEAARPDPEATFVMA------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384914 186 empgqkdRFIGGgleypYVEGLRLDEAMHPLTLLTVGVYGKALPPQNGAPIRLTVPWKYGFKGIKSIVSIKLTRERPPTT 265
Cdd:cd02109 95 -------HSYDG-----YTTNLPLEDLLREDSLLATKMDGEPLPPEHGGPARLVVPHLYFWKSAKWLRGIEFLDEDEPGF 162
|
170
....*....|....*..
gi 505384914 266 WnlaapDEYGFFANVNP 282
Cdd:cd02109 163 W-----ERRGYHERGDP 174
|
|
| SO_family_Moco_dimer |
cd02110 |
Subgroup of sulfite oxidase (SO) family molybdopterin binding domains that contains conserved ... |
108-259 |
9.97e-18 |
|
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: 82.35 E-value: 9.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384914 108 TDPWTLKIDGEVAKPLTLDHHDLTtRFPLEERIYRMRCV----EAWSMVVP-------------WVGFPLHKLLALVEPT 170
Cdd:cd02110 15 PDAWRLEIHGLVERPLTLTLDDLK-RLPSVEVVATLECSgngrGGFIPVRSgaqwghgavgnarWTGVPLKDLLEEAGVK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384914 171 SNAKYVSFqtrYAPDEMPGQKDRfigggleyPYVEGLRLDEAMHPLTLLTVGVYGKALPPQNGAPIRLTVPwkyGFKGik 250
Cdd:cd02110 94 PGAKHVLF---EGADVPPGEKAA--------DYTRSVPLSKALDDDALLAYEMNGEPLPPDHGYPLRLVVP---GWYG-- 157
|
170
....*....|
gi 505384914 251 sIVSIK-LTR 259
Cdd:cd02110 158 -ARSVKwLRR 166
|
|
| bact_SorA_Moco |
cd02114 |
sulfite:cytochrome c oxidoreductase subunit A (SorA), molybdopterin binding domain. SorA is ... |
105-257 |
3.53e-09 |
|
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: 57.52 E-value: 3.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384914 105 SMKTDPWTLKIDGEVAKPLTLDHHDLTTRFPLEERIYRMRCV-EAWSMVVP----------------WVGFPLHKLLALV 167
Cdd:cd02114 59 DIDPDAYTLTIDGKVRTPLTLSLAELKRIEPRFEVVAVNQCSgNSRGFFQPrvqgaqlangamgnarWAGVPLKAVLAKA 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384914 168 EPTSNAKYVSFQTRYAP--DEMPGqkdrfigggleypYVEGLRLDEAMHPLTLLTVGVYGKALPPQNGAPIRLTVPWKYG 245
Cdd:cd02114 139 GVQDGARQVAFRGLDQPvlDVTPD-------------FVKSLDIDHALDGEVMLAWEMNGEPLPVLNGYPLRLVVPGFYA 205
|
170
....*....|..
gi 505384914 246 FKGIKSIVSIKL 257
Cdd:cd02114 206 TYWVKHLSHITV 217
|
|
| eukary_NR_Moco |
cd02112 |
molybdopterin binding domain of eukaryotic nitrate reductase (NR). Assimilatory NRs catalyze ... |
106-285 |
2.24e-06 |
|
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: 48.92 E-value: 2.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384914 106 MKTDPWTLKIDGEVAKPLTLDHHDLTTRFPLEERIYRMRCV----EAWSMVVP---------------WVGFPLHKLLAL 166
Cdd:cd02112 56 EKWEDWTVEVTGLVEKPTTLTMDELVAMFPSVTFPVTLVCAgnrrKEQNMVKKtigfnwgaagtstslWTGVRLSDLLDR 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384914 167 VEPTSN---AKYVSFqtRYAPDEMPGqkdrfiGGGleyPYVEGLRLDEAMHPLT--LLTVGVYGKALPPQNGAPIRLTVP 241
Cdd:cd02112 136 CGPKSPkggARHVCF--EGADDLLPG------PNG---KYGTSITLSWAMDPSKdvMLAYKQNGELLHPDHGFPVRLIIP 204
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 505384914 242 WKYGFKGIKSIVSIKLTrERPPTTWnlaapdeYGFFAN-VNP-HVD 285
Cdd:cd02112 205 GQIGGRMVKWLKRIVVS-DRESQNH-------YHFHDNrVLPsHVD 242
|
|
| PLN02252 |
PLN02252 |
nitrate reductase [NADPH] |
109-248 |
1.45e-05 |
|
nitrate reductase [NADPH]
Pssm-ID: 215141 [Multi-domain] Cd Length: 888 Bit Score: 46.59 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384914 109 DPWTLKIDGEVAKPLTLDHHDLtTRFPL---------------EERIYRMRCVEAW-----SMVVpWVGFPLHKLLA--- 165
Cdd:PLN02252 132 DEWTVEVTGLVKRPARLTMDEL-VRFPArelpvtlvcagnrrkEQNMVKQTIGFNWgaagvSTSV-WRGVRLRDVLRrcg 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384914 166 LVEPTSNAKYVSFQtryAPDEMPGqkdrfiGGGLEYPyvEGLRLDEAMHPL--TLLTVGVYGKALPPQNGAPIRLTVPwk 243
Cdd:PLN02252 210 VMSRKGGALNVCFE---GAEDLPG------GGGSKYG--TSITLERAMDPArdVILAYMQNGEPLTPDHGFPVRLIIP-- 276
|
....*
gi 505384914 244 yGFKG 248
Cdd:PLN02252 277 -GFIG 280
|
|
| bact_SoxC_Moco |
cd02113 |
bacterial SoxC is a member of the sulfite oxidase (SO) family of molybdopterin binding domains. ... |
113-252 |
3.00e-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: 42.00 E-value: 3.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384914 113 LKIDGEVAKPLTLDHHDLTtRFPLEERIYRMRCV----------------EAWSMV--VPWVGFPLHKLLALVEPTSNAK 174
Cdd:cd02113 33 LMIHGMVKKPLVFTMDDLK-RFPSVSRIYFLECSgnggtgwrgaplptaqYTHGMLscSEWTGVPLSTLLEEAGVKPGAK 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505384914 175 YV-------SFQTRYAPDEMPgqkdrfigggleypyveglrLDEAMhpltlLTVGVYGKALPPQNGAPIRLTVPwkyGFK 247
Cdd:cd02113 112 WLlaegadaAAMTRSIPLEKA--------------------LDDAL-----VAYAQNGEALRPENGYPLRLVVP---GWE 163
|
....*
gi 505384914 248 GIKSI 252
Cdd:cd02113 164 GNTNV 168
|
|
| |
