|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05363 |
PRK05363 |
protein-methionine-sulfoxide reductase catalytic subunit MsrP; |
1-334 |
0e+00 |
|
protein-methionine-sulfoxide reductase catalytic subunit MsrP;
Pssm-ID: 235431 Cd Length: 280 Bit Score: 571.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831963 1 MKKNQFLKESDVTAESVFFmKRRQVLkalgisaaalslphaahadllswfkgndrppapagkalefskpaawqnnlPLTP 80
Cdd:PRK05363 3 IKKPWKLPESEVTPESVYL-NRRRFL--------------------------------------------------KLTP 31
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831963 81 ADKVSGYNNFYEFGLDKADPAANAGSLKTDPWTLKISGEVAKPLTLDHDDLTRRFPLEERIYRMRCVEAWSMVVPWIGFP 160
Cdd:PRK05363 32 EEDVTTYNNFYEFGTDKADPARNAGSLKTDPWTVKIDGEVEKPGTLDIDDLLKLFPLEERIYRLRCVEAWSMVIPWIGFP 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831963 161 LHKLLALAEPTSNAKYVAFETIYAPEQMPGQQDRFigggLKYPYVEGLRLDEAMHPLTLMTVGVYGKALPPQNGAPVRLI 240
Cdd:PRK05363 112 LAKLLKRVEPTSNAKYVAFETLYDPEQMPGQRSRF----LDWPYVEGLRLDEAMHPLTLLAVGLYGKTLPNQNGAPIRLV 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831963 241 VPWKYGFKGIKSIVSIKLTRERPPTTWNLAAPDEYGFYANVNPHVDHPRWSQATERFIGSGGILdVQRQPTLLFNGYADQ 320
Cdd:PRK05363 188 VPWKYGFKSIKSIVRIRLTEEQPPTTWNLLAPNEYGFYANVNPNVDHPRWSQATERRIGEGGLF-AERRPTLMFNGYGEQ 266
|
330
....*....|....
gi 15831963 321 VASLYRGLDLRENF 334
Cdd:PRK05363 267 VASLYAGMDLRKNF 280
|
|
| YedY_like_Moco |
cd02107 |
YedY_like molybdopterin cofactor (Moco) binding domain, a subgroup of the sulfite oxidase (SO) ... |
85-304 |
5.78e-160 |
|
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: 445.74 E-value: 5.78e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831963 85 SGYNNFYEFGLDKADPAANAGSLKTDPWTLKISGEVAKPLTLDHDDLTRRFPLEERIYRMRCVEAWSMVVPWIGFPLHKL 164
Cdd:cd02107 1 TTYNNFYEFGTGKDDPARNAGNLPTRPWTVSVSGLVKKPKTLDIDDLMKTFPLEERIYRFRCVEGWSMVVPWVGFPLAAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831963 165 LALAEPTSNAKYVAFETIYAPEQMPGQQDRFigGGLKYPYVEGLRLDEAMHPLTLMTVGVYGKALPPQNGAPVRLIVPWK 244
Cdd:cd02107 81 LARAEPTSEAKYVRFTTLLDKEQMPGQSGLF--GVLPWPYVEGLRLDEAMHPLTLLAVGLYGEALPKQNGAPIRLVVPWK 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831963 245 YGFKGIKSIVSIKLTRERPPTTWNLAAPDEYGFYANVNPHVDHPRWSQATERFIGSGGIL 304
Cdd:cd02107 159 YGFKSIKSIVKIEFTKEQPPTTWNLAAPDEYGFYANVNPSVDHPRWSQATERRIGEGGRR 218
|
|
| MsrP |
COG2041 |
Molybdopterin-dependent catalytic subunit of periplasmic DMSO/TMAO and ... |
91-281 |
9.46e-79 |
|
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: 238.13 E-value: 9.46e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831963 91 YEFGLDKADPAanagsLKTDPWTLKISGEVAKPLTLDHDDLtRRFPLEERIYRMRCVEAWS-MVVPWIGFPLHKLLALAE 169
Cdd:COG2041 19 FPVRTAGGVPE-----IDPADWRLRVDGLVEKPLTLTLDDL-LALPLEERIYRLHCVENWSgGVAPWTGVPLRDLLERAG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831963 170 PTSNAKYVAFETIYAPeqmpgqqdrfiggglkypYVEGLRLDEAMHPLTLMTVGVYGKALPPQNGAPVRLIVPWKYGFKG 249
Cdd:COG2041 93 PKPGAKYVLFESADPG------------------YTESLPLDEALDPDTLLAYGMNGEPLPPEHGAPLRLVVPGLYGFKS 154
|
170 180 190
....*....|....*....|....*....|..
gi 15831963 250 IKSIVSIKLTRERPPTTWNLAApdeYGFYANV 281
Cdd:COG2041 155 AKWLVRIEVTDEDPPGYWETRG---YHFYANI 183
|
|
| Oxidored_molyb |
pfam00174 |
Oxidoreductase molybdopterin binding domain; This domain is found in a variety of ... |
109-267 |
1.29e-41 |
|
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: 142.64 E-value: 1.29e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831963 109 TDPWTLKISGEVAKPLTLDHDDLtRRFPLEERIYRMRCVE------------AW----SMVVPWIGFPLHKLLALAEPTS 172
Cdd:pfam00174 9 PDTWRLRVDGLVEKPLTLTLDDL-KAFPQVTVTATLQCVGnrrkemnrvkgvQWgggaIGNAEWTGVPLRDLLERAGVKP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831963 173 NAKYVAFETIYAPEqmpgqqdrfiggglKYPYVEGLRLDEAMHPLTLMTVGVYGKALPPQNGAPVRLIVPWKYGFKGIKS 252
Cdd:pfam00174 88 GAKHVLFEGADTLG--------------DGGYTTSLPLEKALDDDVLLAYEMNGEPLPPDHGYPLRLVVPGWYGARSVKW 153
|
170
....*....|....*
gi 15831963 253 IVSIKLTRERPPTTW 267
Cdd:pfam00174 154 LRRIEVTDEESPGFW 168
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05363 |
PRK05363 |
protein-methionine-sulfoxide reductase catalytic subunit MsrP; |
1-334 |
0e+00 |
|
protein-methionine-sulfoxide reductase catalytic subunit MsrP;
Pssm-ID: 235431 Cd Length: 280 Bit Score: 571.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831963 1 MKKNQFLKESDVTAESVFFmKRRQVLkalgisaaalslphaahadllswfkgndrppapagkalefskpaawqnnlPLTP 80
Cdd:PRK05363 3 IKKPWKLPESEVTPESVYL-NRRRFL--------------------------------------------------KLTP 31
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831963 81 ADKVSGYNNFYEFGLDKADPAANAGSLKTDPWTLKISGEVAKPLTLDHDDLTRRFPLEERIYRMRCVEAWSMVVPWIGFP 160
Cdd:PRK05363 32 EEDVTTYNNFYEFGTDKADPARNAGSLKTDPWTVKIDGEVEKPGTLDIDDLLKLFPLEERIYRLRCVEAWSMVIPWIGFP 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831963 161 LHKLLALAEPTSNAKYVAFETIYAPEQMPGQQDRFigggLKYPYVEGLRLDEAMHPLTLMTVGVYGKALPPQNGAPVRLI 240
Cdd:PRK05363 112 LAKLLKRVEPTSNAKYVAFETLYDPEQMPGQRSRF----LDWPYVEGLRLDEAMHPLTLLAVGLYGKTLPNQNGAPIRLV 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831963 241 VPWKYGFKGIKSIVSIKLTRERPPTTWNLAAPDEYGFYANVNPHVDHPRWSQATERFIGSGGILdVQRQPTLLFNGYADQ 320
Cdd:PRK05363 188 VPWKYGFKSIKSIVRIRLTEEQPPTTWNLLAPNEYGFYANVNPNVDHPRWSQATERRIGEGGLF-AERRPTLMFNGYGEQ 266
|
330
....*....|....
gi 15831963 321 VASLYRGLDLRENF 334
Cdd:PRK05363 267 VASLYAGMDLRKNF 280
|
|
| YedY_like_Moco |
cd02107 |
YedY_like molybdopterin cofactor (Moco) binding domain, a subgroup of the sulfite oxidase (SO) ... |
85-304 |
5.78e-160 |
|
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: 445.74 E-value: 5.78e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831963 85 SGYNNFYEFGLDKADPAANAGSLKTDPWTLKISGEVAKPLTLDHDDLTRRFPLEERIYRMRCVEAWSMVVPWIGFPLHKL 164
Cdd:cd02107 1 TTYNNFYEFGTGKDDPARNAGNLPTRPWTVSVSGLVKKPKTLDIDDLMKTFPLEERIYRFRCVEGWSMVVPWVGFPLAAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831963 165 LALAEPTSNAKYVAFETIYAPEQMPGQQDRFigGGLKYPYVEGLRLDEAMHPLTLMTVGVYGKALPPQNGAPVRLIVPWK 244
Cdd:cd02107 81 LARAEPTSEAKYVRFTTLLDKEQMPGQSGLF--GVLPWPYVEGLRLDEAMHPLTLLAVGLYGEALPKQNGAPIRLVVPWK 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831963 245 YGFKGIKSIVSIKLTRERPPTTWNLAAPDEYGFYANVNPHVDHPRWSQATERFIGSGGIL 304
Cdd:cd02107 159 YGFKSIKSIVKIEFTKEQPPTTWNLAAPDEYGFYANVNPSVDHPRWSQATERRIGEGGRR 218
|
|
| MsrP |
COG2041 |
Molybdopterin-dependent catalytic subunit of periplasmic DMSO/TMAO and ... |
91-281 |
9.46e-79 |
|
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: 238.13 E-value: 9.46e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831963 91 YEFGLDKADPAanagsLKTDPWTLKISGEVAKPLTLDHDDLtRRFPLEERIYRMRCVEAWS-MVVPWIGFPLHKLLALAE 169
Cdd:COG2041 19 FPVRTAGGVPE-----IDPADWRLRVDGLVEKPLTLTLDDL-LALPLEERIYRLHCVENWSgGVAPWTGVPLRDLLERAG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831963 170 PTSNAKYVAFETIYAPeqmpgqqdrfiggglkypYVEGLRLDEAMHPLTLMTVGVYGKALPPQNGAPVRLIVPWKYGFKG 249
Cdd:COG2041 93 PKPGAKYVLFESADPG------------------YTESLPLDEALDPDTLLAYGMNGEPLPPEHGAPLRLVVPGLYGFKS 154
|
170 180 190
....*....|....*....|....*....|..
gi 15831963 250 IKSIVSIKLTRERPPTTWNLAApdeYGFYANV 281
Cdd:COG2041 155 AKWLVRIEVTDEDPPGYWETRG---YHFYANI 183
|
|
| SO_family_Moco |
cd00321 |
Sulfite oxidase (SO) family, molybdopterin binding domain. This molybdopterin cofactor (Moco) ... |
87-261 |
8.75e-55 |
|
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: 176.22 E-value: 8.75e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831963 87 YNNFYEFGLDKADPaanagslktDPWTLKISGEVAKPLTLDHDDLtRRFPLEERIYRMRCVE-----AWSMVVPWIGFPL 161
Cdd:cd00321 1 FVRNHGGVPPEIDP---------DDWRLEVDGLVEKPLSLTLDDL-KALPQVEVIATLHCVGnrwggGAVSNAEWTGVPL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831963 162 HKLLALAEPTSNAKYVAFETIYAPEqmpgqqdrfiggglKYPYVEGLRLDEAMHPLTLMTVGVYGKALPPQNGAPVRLIV 241
Cdd:cd00321 71 RDLLEEAGPKPGARYVVFEGADDPG--------------GDGYTTSLPLEKALDPDVLLAYEMNGEPLPPDHGFPLRLVV 136
|
170 180
....*....|....*....|
gi 15831963 242 PWKYGFKGIKSIVSIKLTRE 261
Cdd:cd00321 137 PGLYGWKSVKWLRRIEVTDE 156
|
|
| Oxidored_molyb |
pfam00174 |
Oxidoreductase molybdopterin binding domain; This domain is found in a variety of ... |
109-267 |
1.29e-41 |
|
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: 142.64 E-value: 1.29e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831963 109 TDPWTLKISGEVAKPLTLDHDDLtRRFPLEERIYRMRCVE------------AW----SMVVPWIGFPLHKLLALAEPTS 172
Cdd:pfam00174 9 PDTWRLRVDGLVEKPLTLTLDDL-KAFPQVTVTATLQCVGnrrkemnrvkgvQWgggaIGNAEWTGVPLRDLLERAGVKP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831963 173 NAKYVAFETIYAPEqmpgqqdrfiggglKYPYVEGLRLDEAMHPLTLMTVGVYGKALPPQNGAPVRLIVPWKYGFKGIKS 252
Cdd:pfam00174 88 GAKHVLFEGADTLG--------------DGGYTTSLPLEKALDDDVLLAYEMNGEPLPPDHGYPLRLVVPGWYGARSVKW 153
|
170
....*....|....*
gi 15831963 253 IVSIKLTRERPPTTW 267
Cdd:pfam00174 154 LRRIEVTDEESPGFW 168
|
|
| bact_SO_family_Moco |
cd02108 |
bacterial subgroup of the sulfite oxidase (SO) family of molybdopterin binding domains. This ... |
112-259 |
9.10e-32 |
|
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: 117.49 E-value: 9.10e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831963 112 WTLKISGEVAKPLTLDHDDLtRRFPLEERIYRMRCVEAWSMVVPWIGFPLHKLLALAEPTSNAKYVAFETIyapeqmpgq 191
Cdd:cd02108 29 YRLEVGGLVEHPLSLSLEEL-RALPQRTQITRHICVEGWSAIGKWGGVPLRTILELVGPLPEAKYVVFKCA--------- 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15831963 192 qDRFIGGGLkypYVEGLRLDEAMHPLTLMTVGVYGKALPPQNGAPVRLIVPWKYGFKGIKSIVSIKLT 259
Cdd:cd02108 99 -DDFAGGDR---YYESIDMASALHPQTLLAYEMNGQPLPIKNGAPLRLRVETQLGYKQAKWVTEIELV 162
|
|
| arch_bact_SO_family_Moco |
cd02109 |
bacterial and archael members of the sulfite oxidase (SO) family of molybdopterin binding ... |
107-283 |
1.89e-24 |
|
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: 97.70 E-value: 1.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831963 107 LKTDPWTLKISGEVAKPLTLDHDDLtRRFPLEERIYRMRCVEAWSMV-VPWIGFPLHKLLALAEPTSNAKYVAFETIYAp 185
Cdd:cd02109 22 VDLEKWRLRVTGLVENPLSLTYEDL-LALPQTEYTADFHCVTGWSKLdVVWEGVSLKDLLEAARPDPEATFVMAHSYDG- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831963 186 eqmpgqqdrfiggglkypYVEGLRLDEAMHPLTLMTVGVYGKALPPQNGAPVRLIVPWKYGFKGIKSIVSIKLTRERPPT 265
Cdd:cd02109 100 ------------------YTTNLPLEDLLREDSLLATKMDGEPLPPEHGGPARLVVPHLYFWKSAKWLRGIEFLDEDEPG 161
|
170
....*....|....*...
gi 15831963 266 TWnlaapDEYGFYANVNP 283
Cdd:cd02109 162 FW-----ERRGYHERGDP 174
|
|
| SO_family_Moco_dimer |
cd02110 |
Subgroup of sulfite oxidase (SO) family molybdopterin binding domains that contains conserved ... |
109-297 |
3.11e-21 |
|
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: 92.36 E-value: 3.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831963 109 TDPWTLKISGEVAKPLTLDHDDLtRRFPLEERIYRMRCV----EAWSMVVP-------------WIGFPLHKLLALAEPT 171
Cdd:cd02110 15 PDAWRLEIHGLVERPLTLTLDDL-KRLPSVEVVATLECSgngrGGFIPVRSgaqwghgavgnarWTGVPLKDLLEEAGVK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831963 172 SNAKYVAFETIYAPEQMPGQqdrfiggglkyPYVEGLRLDEAMHPLTLMTVGVYGKALPPQNGAPVRLIVPWKYGFKGIK 251
Cdd:cd02110 94 PGAKHVLFEGADVPPGEKAA-----------DYTRSVPLSKALDDDALLAYEMNGEPLPPDHGYPLRLVVPGWYGARSVK 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 15831963 252 SIVSIKLTRERppttwnLAAPDEYGFYANVNPHVDH--PRWSQATERF 297
Cdd:cd02110 163 WLRRIEVTDQP------SDGYWQTRDYTVPPPDVDAvgGKARRPIGEM 204
|
|
| PLN02252 |
PLN02252 |
nitrate reductase [NADPH] |
110-249 |
1.65e-10 |
|
nitrate reductase [NADPH]
Pssm-ID: 215141 [Multi-domain] Cd Length: 888 Bit Score: 62.00 E-value: 1.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831963 110 DPWTLKISGEVAKPLTLDHDDL----TRRFPL----------EERIYRMRCVEAW-----SMVVpWIGFPLHKLLALA-- 168
Cdd:PLN02252 132 DEWTVEVTGLVKRPARLTMDELvrfpARELPVtlvcagnrrkEQNMVKQTIGFNWgaagvSTSV-WRGVRLRDVLRRCgv 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831963 169 -EPTSNAKYVAFEtiyAPEQMPGqqdrfiGGGLKYPyvEGLRLDEAMHP-----LTLMTvgvYGKALPPQNGAPVRLIVP 242
Cdd:PLN02252 211 mSRKGGALNVCFE---GAEDLPG------GGGSKYG--TSITLERAMDPardviLAYMQ---NGEPLTPDHGFPVRLIIP 276
|
....*..
gi 15831963 243 wkyGFKG 249
Cdd:PLN02252 277 ---GFIG 280
|
|
| bact_SorA_Moco |
cd02114 |
sulfite:cytochrome c oxidoreductase subunit A (SorA), molybdopterin binding domain. SorA is ... |
106-258 |
4.79e-10 |
|
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: 60.22 E-value: 4.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831963 106 SLKTDPWTLKISGEVAKPLTLDHDDLTRRFPLEERIYRMRCV-EAWSMVVP----------------WIGFPLHKLLALA 168
Cdd:cd02114 59 DIDPDAYTLTIDGKVRTPLTLSLAELKRIEPRFEVVAVNQCSgNSRGFFQPrvqgaqlangamgnarWAGVPLKAVLAKA 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831963 169 EPTSNAKYVAFETIYAP--EQMPGqqdrfiggglkypYVEGLRLDEAMHPLTLMTVGVYGKALPPQNGAPVRLIVPWKYG 246
Cdd:cd02114 139 GVQDGARQVAFRGLDQPvlDVTPD-------------FVKSLDIDHALDGEVMLAWEMNGEPLPVLNGYPLRLVVPGFYA 205
|
170
....*....|..
gi 15831963 247 FKGIKSIVSIKL 258
Cdd:cd02114 206 TYWVKHLSHITV 217
|
|
| eukary_NR_Moco |
cd02112 |
molybdopterin binding domain of eukaryotic nitrate reductase (NR). Assimilatory NRs catalyze ... |
110-286 |
1.50e-08 |
|
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: 55.47 E-value: 1.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831963 110 DPWTLKISGEVAKPLTLDHDDLTRRFPLEERIYRMRCV----EAWSMVVPWIGF---------------PLHKLLALAEP 170
Cdd:cd02112 59 EDWTVEVTGLVEKPTTLTMDELVAMFPSVTFPVTLVCAgnrrKEQNMVKKTIGFnwgaagtstslwtgvRLSDLLDRCGP 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831963 171 TSN---AKYVAFEtiyAPEQMPGQqdrfiGGGlkyPYVEGLRLDEAMHPLTLMTV--GVYGKALPPQNGAPVRLIVPWKY 245
Cdd:cd02112 139 KSPkggARHVCFE---GADDLLPG-----PNG---KYGTSITLSWAMDPSKDVMLayKQNGELLHPDHGFPVRLIIPGQI 207
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 15831963 246 GFKGIKSIVSIKLTrERPPTTWnlaapdeYGFYAN-VNP-HVD 286
Cdd:cd02112 208 GGRMVKWLKRIVVS-DRESQNH-------YHFHDNrVLPsHVD 242
|
|
| eukary_SO_Moco |
cd02111 |
molybdopterin binding domain of sulfite oxidase (SO). SO catalyzes the terminal reaction in ... |
106-294 |
1.33e-06 |
|
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: 49.31 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831963 106 SLKTDPWTLKISGEVAKPLTLDHDDLTRRFPLEE----------RIYRMRCVEA-----WS----MVVPWIGFPLHKLLA 166
Cdd:cd02111 40 VVDPDTYSLEVEGPDGTTLSLSLEDLKSLFPKHEvtatlqcagnRRSEMTKVKKvkglqWGdgaiSNAEWGGARLRDVLL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15831963 167 LA---EPTSN-AKYVAFETIyapeqmpgqqDRFIGGGlkyPYVEGLRLDEAMHPL--TLMTVGVYGKALPPQNGAPVRLI 240
Cdd:cd02111 120 DAgipEDDSQgGLHVHFEGL----------DVDPTGT---PYGASIPLSKALDPEadVLLAYEMNGTPLPRDHGFPLRVV 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15831963 241 VPWKYGFKGIKSIVSIKLTRERPPTTWNlaAPDEYGFYANV---NPHVDHPRWSQAT 294
Cdd:cd02111 187 VPGVVGARSVKWLDRIVVSDEESDSHWQ--QNDYKGFSPSVdwdNVDFSKAPAIQEM 241
|
|
| |
