|
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: 580.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727165403 1 MNKHPKLTEADVTPESVFHQRRKVLqalgitaaslalptgaqadllswfkgndrpkappgkalefskpaawqaqlAMTPE 80
Cdd:PRK05363 3 IKKPWKLPESEVTPESVYLNRRRFL--------------------------------------------------KLTPE 32
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727165403 81 DKVTGYNNFYEFGLDKADPAANAGGLKTEGWKVRIDGEVAKPITLDIDDLMKRFPLEQRIYRMRCVEAWSMVVPWIGFEL 160
Cdd:PRK05363 33 EDVTTYNNFYEFGTDKADPARNAGSLKTDPWTVKIDGEVEKPGTLDIDDLLKLFPLEERIYRLRCVEAWSMVIPWIGFPL 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727165403 161 GKLIKLAEPNGNARYVAFQTLYDPEQMPGQKDRFigggLKYPYVEGLRLDEAMHPLALLTVGVYGKTLPPQNGAPLRLIT 240
Cdd:PRK05363 113 AKLLKRVEPTSNAKYVAFETLYDPEQMPGQRSRF----LDWPYVEGLRLDEAMHPLTLLAVGLYGKTLPNQNGAPIRLVV 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727165403 241 PWKYGFKGIKSIVHIRLVRDRPPTTWNQSAPNEYGFYANVNPHVDHPRWSQATERFIGSGGILdVKRQPTLLFNGYADQV 320
Cdd:PRK05363 189 PWKYGFKSIKSIVRIRLTEEQPPTTWNLLAPNEYGFYANVNPNVDHPRWSQATERRIGEGGLF-AERRPTLMFNGYGEQV 267
|
330
....*....|...
gi 727165403 321 ASLYRGMDLRENF 333
Cdd:PRK05363 268 ASLYAGMDLRKNF 280
|
|
| YedY_like_Moco |
cd02107 |
YedY_like molybdopterin cofactor (Moco) binding domain, a subgroup of the sulfite oxidase (SO) ... |
84-303 |
1.89e-151 |
|
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: 424.17 E-value: 1.89e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727165403 84 TGYNNFYEFGLDKADPAANAGGLKTEGWKVRIDGEVAKPITLDIDDLMKRFPLEQRIYRMRCVEAWSMVVPWIGFELGKL 163
Cdd:cd02107 1 TTYNNFYEFGTGKDDPARNAGNLPTRPWTVSVSGLVKKPKTLDIDDLMKTFPLEERIYRFRCVEGWSMVVPWVGFPLAAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727165403 164 IKLAEPNGNARYVAFQTLYDPEQMPGQKDRFigGGLKYPYVEGLRLDEAMHPLALLTVGVYGKTLPPQNGAPLRLITPWK 243
Cdd:cd02107 81 LARAEPTSEAKYVRFTTLLDKEQMPGQSGLF--GVLPWPYVEGLRLDEAMHPLTLLAVGLYGEALPKQNGAPIRLVVPWK 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 727165403 244 YGFKGIKSIVHIRLVRDRPPTTWNQSAPNEYGFYANVNPHVDHPRWSQATERFIGSGGIL 303
Cdd:cd02107 159 YGFKSIKSIVKIEFTKEQPPTTWNLAAPDEYGFYANVNPSVDHPRWSQATERRIGEGGRR 218
|
|
| MsrP |
COG2041 |
Molybdopterin-dependent catalytic subunit of periplasmic DMSO/TMAO and ... |
90-280 |
2.16e-74 |
|
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: 226.96 E-value: 2.16e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727165403 90 YEFGLDKADPAanaggLKTEGWKVRIDGEVAKPITLDIDDLMkRFPLEQRIYRMRCVEAWS-MVVPWIGFELGKLIKLAE 168
Cdd:COG2041 19 FPVRTAGGVPE-----IDPADWRLRVDGLVEKPLTLTLDDLL-ALPLEERIYRLHCVENWSgGVAPWTGVPLRDLLERAG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727165403 169 PNGNARYVAFQTlYDPeqmpgqkdrfiggglkyPYVEGLRLDEAMHPLALLTVGVYGKTLPPQNGAPLRLITPWKYGFKG 248
Cdd:COG2041 93 PKPGAKYVLFES-ADP-----------------GYTESLPLDEALDPDTLLAYGMNGEPLPPEHGAPLRLVVPGLYGFKS 154
|
170 180 190
....*....|....*....|....*....|..
gi 727165403 249 IKSIVHIRLVRDRPPTTWNQSApneYGFYANV 280
Cdd:COG2041 155 AKWLVRIEVTDEDPPGYWETRG---YHFYANI 183
|
|
| Oxidored_molyb |
pfam00174 |
Oxidoreductase molybdopterin binding domain; This domain is found in a variety of ... |
108-266 |
3.75e-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: 131.08 E-value: 3.75e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727165403 108 TEGWKVRIDGEVAKPITLDIDDLmKRFPLEQRIYRMRCVE------------AW----SMVVPWIGFELGKLIKLAEPNG 171
Cdd:pfam00174 9 PDTWRLRVDGLVEKPLTLTLDDL-KAFPQVTVTATLQCVGnrrkemnrvkgvQWgggaIGNAEWTGVPLRDLLERAGVKP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727165403 172 NARYVAFQTLYDPEqmpgqkdrfiggglKYPYVEGLRLDEAMHPLALLTVGVYGKTLPPQNGAPLRLITPWKYGFKGIKS 251
Cdd:pfam00174 88 GAKHVLFEGADTLG--------------DGGYTTSLPLEKALDDDVLLAYEMNGEPLPPDHGYPLRLVVPGWYGARSVKW 153
|
170
....*....|....*
gi 727165403 252 IVHIRLVRDRPPTTW 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: 580.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727165403 1 MNKHPKLTEADVTPESVFHQRRKVLqalgitaaslalptgaqadllswfkgndrpkappgkalefskpaawqaqlAMTPE 80
Cdd:PRK05363 3 IKKPWKLPESEVTPESVYLNRRRFL--------------------------------------------------KLTPE 32
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727165403 81 DKVTGYNNFYEFGLDKADPAANAGGLKTEGWKVRIDGEVAKPITLDIDDLMKRFPLEQRIYRMRCVEAWSMVVPWIGFEL 160
Cdd:PRK05363 33 EDVTTYNNFYEFGTDKADPARNAGSLKTDPWTVKIDGEVEKPGTLDIDDLLKLFPLEERIYRLRCVEAWSMVIPWIGFPL 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727165403 161 GKLIKLAEPNGNARYVAFQTLYDPEQMPGQKDRFigggLKYPYVEGLRLDEAMHPLALLTVGVYGKTLPPQNGAPLRLIT 240
Cdd:PRK05363 113 AKLLKRVEPTSNAKYVAFETLYDPEQMPGQRSRF----LDWPYVEGLRLDEAMHPLTLLAVGLYGKTLPNQNGAPIRLVV 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727165403 241 PWKYGFKGIKSIVHIRLVRDRPPTTWNQSAPNEYGFYANVNPHVDHPRWSQATERFIGSGGILdVKRQPTLLFNGYADQV 320
Cdd:PRK05363 189 PWKYGFKSIKSIVRIRLTEEQPPTTWNLLAPNEYGFYANVNPNVDHPRWSQATERRIGEGGLF-AERRPTLMFNGYGEQV 267
|
330
....*....|...
gi 727165403 321 ASLYRGMDLRENF 333
Cdd:PRK05363 268 ASLYAGMDLRKNF 280
|
|
| YedY_like_Moco |
cd02107 |
YedY_like molybdopterin cofactor (Moco) binding domain, a subgroup of the sulfite oxidase (SO) ... |
84-303 |
1.89e-151 |
|
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: 424.17 E-value: 1.89e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727165403 84 TGYNNFYEFGLDKADPAANAGGLKTEGWKVRIDGEVAKPITLDIDDLMKRFPLEQRIYRMRCVEAWSMVVPWIGFELGKL 163
Cdd:cd02107 1 TTYNNFYEFGTGKDDPARNAGNLPTRPWTVSVSGLVKKPKTLDIDDLMKTFPLEERIYRFRCVEGWSMVVPWVGFPLAAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727165403 164 IKLAEPNGNARYVAFQTLYDPEQMPGQKDRFigGGLKYPYVEGLRLDEAMHPLALLTVGVYGKTLPPQNGAPLRLITPWK 243
Cdd:cd02107 81 LARAEPTSEAKYVRFTTLLDKEQMPGQSGLF--GVLPWPYVEGLRLDEAMHPLTLLAVGLYGEALPKQNGAPIRLVVPWK 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 727165403 244 YGFKGIKSIVHIRLVRDRPPTTWNQSAPNEYGFYANVNPHVDHPRWSQATERFIGSGGIL 303
Cdd:cd02107 159 YGFKSIKSIVKIEFTKEQPPTTWNLAAPDEYGFYANVNPSVDHPRWSQATERRIGEGGRR 218
|
|
| MsrP |
COG2041 |
Molybdopterin-dependent catalytic subunit of periplasmic DMSO/TMAO and ... |
90-280 |
2.16e-74 |
|
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: 226.96 E-value: 2.16e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727165403 90 YEFGLDKADPAanaggLKTEGWKVRIDGEVAKPITLDIDDLMkRFPLEQRIYRMRCVEAWS-MVVPWIGFELGKLIKLAE 168
Cdd:COG2041 19 FPVRTAGGVPE-----IDPADWRLRVDGLVEKPLTLTLDDLL-ALPLEERIYRLHCVENWSgGVAPWTGVPLRDLLERAG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727165403 169 PNGNARYVAFQTlYDPeqmpgqkdrfiggglkyPYVEGLRLDEAMHPLALLTVGVYGKTLPPQNGAPLRLITPWKYGFKG 248
Cdd:COG2041 93 PKPGAKYVLFES-ADP-----------------GYTESLPLDEALDPDTLLAYGMNGEPLPPEHGAPLRLVVPGLYGFKS 154
|
170 180 190
....*....|....*....|....*....|..
gi 727165403 249 IKSIVHIRLVRDRPPTTWNQSApneYGFYANV 280
Cdd:COG2041 155 AKWLVRIEVTDEDPPGYWETRG---YHFYANI 183
|
|
| SO_family_Moco |
cd00321 |
Sulfite oxidase (SO) family, molybdopterin binding domain. This molybdopterin cofactor (Moco) ... |
86-260 |
6.75e-49 |
|
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: 160.81 E-value: 6.75e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727165403 86 YNNFYEFGLDKADPaanagglktEGWKVRIDGEVAKPITLDIDDLMkRFPLEQRIYRMRCVE-----AWSMVVPWIGFEL 160
Cdd:cd00321 1 FVRNHGGVPPEIDP---------DDWRLEVDGLVEKPLSLTLDDLK-ALPQVEVIATLHCVGnrwggGAVSNAEWTGVPL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727165403 161 GKLIKLAEPNGNARYVAFQTLYDPEqmpgqkdrfiggglKYPYVEGLRLDEAMHPLALLTVGVYGKTLPPQNGAPLRLIT 240
Cdd:cd00321 71 RDLLEEAGPKPGARYVVFEGADDPG--------------GDGYTTSLPLEKALDPDVLLAYEMNGEPLPPDHGFPLRLVV 136
|
170 180
....*....|....*....|
gi 727165403 241 PWKYGFKGIKSIVHIRLVRD 260
Cdd:cd00321 137 PGLYGWKSVKWLRRIEVTDE 156
|
|
| Oxidored_molyb |
pfam00174 |
Oxidoreductase molybdopterin binding domain; This domain is found in a variety of ... |
108-266 |
3.75e-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: 131.08 E-value: 3.75e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727165403 108 TEGWKVRIDGEVAKPITLDIDDLmKRFPLEQRIYRMRCVE------------AW----SMVVPWIGFELGKLIKLAEPNG 171
Cdd:pfam00174 9 PDTWRLRVDGLVEKPLTLTLDDL-KAFPQVTVTATLQCVGnrrkemnrvkgvQWgggaIGNAEWTGVPLRDLLERAGVKP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727165403 172 NARYVAFQTLYDPEqmpgqkdrfiggglKYPYVEGLRLDEAMHPLALLTVGVYGKTLPPQNGAPLRLITPWKYGFKGIKS 251
Cdd:pfam00174 88 GAKHVLFEGADTLG--------------DGGYTTSLPLEKALDDDVLLAYEMNGEPLPPDHGYPLRLVVPGWYGARSVKW 153
|
170
....*....|....*
gi 727165403 252 IVHIRLVRDRPPTTW 266
Cdd:pfam00174 154 LRRIEVTDEESPGFW 168
|
|
| bact_SO_family_Moco |
cd02108 |
bacterial subgroup of the sulfite oxidase (SO) family of molybdopterin binding domains. This ... |
110-262 |
7.36e-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: 109.78 E-value: 7.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727165403 110 GWKVRIDGEVAKPITLDIDDLMKrFPLEQRIYRMRCVEAWSMVVPWIGFELGKLIKLAEPNGNARYVAFQTLYDpeqmpg 189
Cdd:cd02108 28 DYRLEVGGLVEHPLSLSLEELRA-LPQRTQITRHICVEGWSAIGKWGGVPLRTILELVGPLPEAKYVVFKCADD------ 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 727165403 190 qkdrfigGGLKYPYVEGLRLDEAMHPLALLTVGVYGKTLPPQNGAPLRLITPWKYGFKGIKSIVHIRLVRDRP 262
Cdd:cd02108 101 -------FAGGDRYYESIDMASALHPQTLLAYEMNGQPLPIKNGAPLRLRVETQLGYKQAKWVTEIELVNDLP 166
|
|
| arch_bact_SO_family_Moco |
cd02109 |
bacterial and archael members of the sulfite oxidase (SO) family of molybdopterin binding ... |
106-282 |
4.50e-22 |
|
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: 91.54 E-value: 4.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727165403 106 LKTEGWKVRIDGEVAKPITLDIDDLMKrFPLEQRIYRMRCVEAWSMV-VPWIGFELGKLIKLAEPNGNARYVAFQTLYDp 184
Cdd:cd02109 22 VDLEKWRLRVTGLVENPLSLTYEDLLA-LPQTEYTADFHCVTGWSKLdVVWEGVSLKDLLEAARPDPEATFVMAHSYDG- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727165403 185 eqmpgqkdrfiggglkypYVEGLRLDEAMHPLALLTVGVYGKTLPPQNGAPLRLITPWKYGFKGIKSIVHIRLVRDRPPT 264
Cdd:cd02109 100 ------------------YTTNLPLEDLLREDSLLATKMDGEPLPPEHGGPARLVVPHLYFWKSAKWLRGIEFLDEDEPG 161
|
170
....*....|....*...
gi 727165403 265 TWNQsapneYGFYANVNP 282
Cdd:cd02109 162 FWER-----RGYHERGDP 174
|
|
| SO_family_Moco_dimer |
cd02110 |
Subgroup of sulfite oxidase (SO) family molybdopterin binding domains that contains conserved ... |
108-268 |
5.60e-20 |
|
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: 88.51 E-value: 5.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727165403 108 TEGWKVRIDGEVAKPITLDIDDLmKRFPLEQRIYRMRCV----EAWSMVVP-------------WIGFELGKLIKLAEPN 170
Cdd:cd02110 15 PDAWRLEIHGLVERPLTLTLDDL-KRLPSVEVVATLECSgngrGGFIPVRSgaqwghgavgnarWTGVPLKDLLEEAGVK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727165403 171 GNARYVAFQTLYDPEQMPGQkdrfiggglkyPYVEGLRLDEAMHPLALLTVGVYGKTLPPQNGAPLRLITPWKYGFKGIK 250
Cdd:cd02110 94 PGAKHVLFEGADVPPGEKAA-----------DYTRSVPLSKALDDDALLAYEMNGEPLPPDHGYPLRLVVPGWYGARSVK 162
|
170
....*....|....*...
gi 727165403 251 SIVHIRlVRDRPPTTWNQ 268
Cdd:cd02110 163 WLRRIE-VTDQPSDGYWQ 179
|
|
| eukary_NR_Moco |
cd02112 |
molybdopterin binding domain of eukaryotic nitrate reductase (NR). Assimilatory NRs catalyze ... |
109-285 |
2.58e-07 |
|
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: 51.61 E-value: 2.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727165403 109 EGWKVRIDGEVAKPITLDIDDLMKRFPLEQRIYRMRCV----EAWSMVVPWIGFELG------------------KLIKL 166
Cdd:cd02112 59 EDWTVEVTGLVEKPTTLTMDELVAMFPSVTFPVTLVCAgnrrKEQNMVKKTIGFNWGaagtstslwtgvrlsdllDRCGP 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727165403 167 AEPNGNARYVAFQtlydpeqmpGQKDRFIGGGLKYPyvEGLRLDEAMHPLA--LLTVGVYGKTLPPQNGAPLRLITPWKY 244
Cdd:cd02112 139 KSPKGGARHVCFE---------GADDLLPGPNGKYG--TSITLSWAMDPSKdvMLAYKQNGELLHPDHGFPVRLIIPGQI 207
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 727165403 245 GFKGIKSIVHIrLVRDRPPTTWnqsapneYGFYAN-VNP-HVD 285
Cdd:cd02112 208 GGRMVKWLKRI-VVSDRESQNH-------YHFHDNrVLPsHVD 242
|
|
| PLN02252 |
PLN02252 |
nitrate reductase [NADPH] |
111-285 |
6.22e-07 |
|
nitrate reductase [NADPH]
Pssm-ID: 215141 [Multi-domain] Cd Length: 888 Bit Score: 51.22 E-value: 6.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727165403 111 WKVRIDGEVAKPITLDIDDLmKRFPL---------------EQRIYRMRCVEAW-----SMVVpWIGFELGKLIKLA--- 167
Cdd:PLN02252 134 WTVEVTGLVKRPARLTMDEL-VRFPArelpvtlvcagnrrkEQNMVKQTIGFNWgaagvSTSV-WRGVRLRDVLRRCgvm 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727165403 168 EPNGNARYVAFQtlyDPEQMPGqkdrfiGGGLKYPyvEGLRLDEAMHPL--ALLTVGVYGKTLPPQNGAPLRLITPwkyG 245
Cdd:PLN02252 212 SRKGGALNVCFE---GAEDLPG------GGGSKYG--TSITLERAMDPArdVILAYMQNGEPLTPDHGFPVRLIIP---G 277
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 727165403 246 FKG---IKSIVHIRlVRDRPPTtwnqsapNEYGFYAN--VNPHVD 285
Cdd:PLN02252 278 FIGgrmVKWLKRII-VTTAESD-------NYYHYRDNrvLPSHVD 314
|
|
| eukary_SO_Moco |
cd02111 |
molybdopterin binding domain of sulfite oxidase (SO). SO catalyzes the terminal reaction in ... |
106-293 |
7.19e-07 |
|
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: 50.47 E-value: 7.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727165403 106 LKTEGWKVRIDGEVAKPITLDIDDLMKRFP-------LE---QRIYRMRCVEA-----WS----MVVPWIGFELGKLIKL 166
Cdd:cd02111 41 VDPDTYSLEVEGPDGTTLSLSLEDLKSLFPkhevtatLQcagNRRSEMTKVKKvkglqWGdgaiSNAEWGGARLRDVLLD 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 727165403 167 A----EPNGNARYVAFQTLydpeqmpgqkDRFIGGGlkyPYVEGLRLDEAMHPLA--LLTVGVYGKTLPPQNGAPLRLIT 240
Cdd:cd02111 121 AgipeDDSQGGLHVHFEGL----------DVDPTGT---PYGASIPLSKALDPEAdvLLAYEMNGTPLPRDHGFPLRVVV 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 727165403 241 PWKYGFKGIKSIVHIRLVRDRPPTTWNQsapNEY-GFYANV---NPHVDHPRWSQAT 293
Cdd:cd02111 188 PGVVGARSVKWLDRIVVSDEESDSHWQQ---NDYkGFSPSVdwdNVDFSKAPAIQEM 241
|
|
| |
