|
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: 563.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489008121 1 MKRKKLTEADVTAESVFmLKRRQMLKmlgisatalslpaaaqadlldwfkghdrppapagkalefakpaewqanltLTPE 80
Cdd:PRK05363 4 KKPWKLPESEVTPESVY-LNRRRFLK--------------------------------------------------LTPE 32
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489008121 81 DKVAGYNNFYEFGLDKADPAANAGSLRTDPWTLTIGGEVAKPLTLDHDDLTKRFPLEERIYRMRCVEAWSMVVPWVGFPL 160
Cdd:PRK05363 33 EDVTTYNNFYEFGTDKADPARNAGSLKTDPWTVKIDGEVEKPGTLDIDDLLKLFPLEERIYRLRCVEAWSMVIPWIGFPL 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489008121 161 HKLLALVEPTSSARYVAFKTLYAPDQMPGQKDRFigggLAYPYVEGLRLDEAMHPLTLLTVGVYGKALPPQNGAPVRLTV 240
Cdd:PRK05363 113 AKLLKRVEPTSNAKYVAFETLYDPEQMPGQRSRF----LDWPYVEGLRLDEAMHPLTLLAVGLYGKTLPNQNGAPIRLVV 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489008121 241 PWKYGFKGIKSIVSIELTRERPPTTWNLAAPDEYGFFANVNPHVDHPRWSQASERFIGAGGVLdVKRQPTLLFNGYADEV 320
Cdd:PRK05363 189 PWKYGFKSIKSIVRIRLTEEQPPTTWNLLAPNEYGFYANVNPNVDHPRWSQATERRIGEGGLF-AERRPTLMFNGYGEQV 267
|
330
....*....|...
gi 489008121 321 ASLYRGMNLRENF 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 |
4.78e-155 |
|
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: 433.03 E-value: 4.78e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489008121 84 AGYNNFYEFGLDKADPAANAGSLRTDPWTLTIGGEVAKPLTLDHDDLTKRFPLEERIYRMRCVEAWSMVVPWVGFPLHKL 163
Cdd:cd02107 1 TTYNNFYEFGTGKDDPARNAGNLPTRPWTVSVSGLVKKPKTLDIDDLMKTFPLEERIYRFRCVEGWSMVVPWVGFPLAAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489008121 164 LALVEPTSSARYVAFKTLYAPDQMPGQKDRFigGGLAYPYVEGLRLDEAMHPLTLLTVGVYGKALPPQNGAPVRLTVPWK 243
Cdd:cd02107 81 LARAEPTSEAKYVRFTTLLDKEQMPGQSGLF--GVLPWPYVEGLRLDEAMHPLTLLAVGLYGEALPKQNGAPIRLVVPWK 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489008121 244 YGFKGIKSIVSIELTRERPPTTWNLAAPDEYGFFANVNPHVDHPRWSQASERFIGAGG 301
Cdd:cd02107 159 YGFKSIKSIVKIEFTKEQPPTTWNLAAPDEYGFYANVNPSVDHPRWSQATERRIGEGG 216
|
|
| MsrP |
COG2041 |
Molybdopterin-dependent catalytic subunit of periplasmic DMSO/TMAO and ... |
90-280 |
2.20e-76 |
|
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: 232.35 E-value: 2.20e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489008121 90 YEFGLDKADPAanagsLRTDPWTLTIGGEVAKPLTLDHDDLtKRFPLEERIYRMRCVEAWS-MVVPWVGFPLHKLLALVE 168
Cdd:COG2041 19 FPVRTAGGVPE-----IDPADWRLRVDGLVEKPLTLTLDDL-LALPLEERIYRLHCVENWSgGVAPWTGVPLRDLLERAG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489008121 169 PTSSARYVAFKTLYAPdqmpgqkdrfiggglaypYVEGLRLDEAMHPLTLLTVGVYGKALPPQNGAPVRLTVPWKYGFKG 248
Cdd:COG2041 93 PKPGAKYVLFESADPG------------------YTESLPLDEALDPDTLLAYGMNGEPLPPEHGAPLRLVVPGLYGFKS 154
|
170 180 190
....*....|....*....|....*....|..
gi 489008121 249 IKSIVSIELTRERPPTTWNLAApdeYGFFANV 280
Cdd:COG2041 155 AKWLVRIEVTDEDPPGYWETRG---YHFYANI 183
|
|
| Oxidored_molyb |
pfam00174 |
Oxidoreductase molybdopterin binding domain; This domain is found in a variety of ... |
106-266 |
1.14e-40 |
|
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: 139.94 E-value: 1.14e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489008121 106 LRTDPWTLTIGGEVAKPLTLDHDDLtKRFPLEERIYRMRCVE------------AW----SMVVPWVGFPLHKLLALVEP 169
Cdd:pfam00174 7 IDPDTWRLRVDGLVEKPLTLTLDDL-KAFPQVTVTATLQCVGnrrkemnrvkgvQWgggaIGNAEWTGVPLRDLLERAGV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489008121 170 TSSARYVAFktlYAPDQMPGqkdrfiggglaYPYVEGLRLDEAMHPLTLLTVGVYGKALPPQNGAPVRLTVPWKYGFKGI 249
Cdd:pfam00174 86 KPGAKHVLF---EGADTLGD-----------GGYTTSLPLEKALDDDVLLAYEMNGEPLPPDHGYPLRLVVPGWYGARSV 151
|
170
....*....|....*..
gi 489008121 250 KSIVSIELTRERPPTTW 266
Cdd:pfam00174 152 KWLRRIEVTDEESPGFW 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: 563.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489008121 1 MKRKKLTEADVTAESVFmLKRRQMLKmlgisatalslpaaaqadlldwfkghdrppapagkalefakpaewqanltLTPE 80
Cdd:PRK05363 4 KKPWKLPESEVTPESVY-LNRRRFLK--------------------------------------------------LTPE 32
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489008121 81 DKVAGYNNFYEFGLDKADPAANAGSLRTDPWTLTIGGEVAKPLTLDHDDLTKRFPLEERIYRMRCVEAWSMVVPWVGFPL 160
Cdd:PRK05363 33 EDVTTYNNFYEFGTDKADPARNAGSLKTDPWTVKIDGEVEKPGTLDIDDLLKLFPLEERIYRLRCVEAWSMVIPWIGFPL 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489008121 161 HKLLALVEPTSSARYVAFKTLYAPDQMPGQKDRFigggLAYPYVEGLRLDEAMHPLTLLTVGVYGKALPPQNGAPVRLTV 240
Cdd:PRK05363 113 AKLLKRVEPTSNAKYVAFETLYDPEQMPGQRSRF----LDWPYVEGLRLDEAMHPLTLLAVGLYGKTLPNQNGAPIRLVV 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489008121 241 PWKYGFKGIKSIVSIELTRERPPTTWNLAAPDEYGFFANVNPHVDHPRWSQASERFIGAGGVLdVKRQPTLLFNGYADEV 320
Cdd:PRK05363 189 PWKYGFKSIKSIVRIRLTEEQPPTTWNLLAPNEYGFYANVNPNVDHPRWSQATERRIGEGGLF-AERRPTLMFNGYGEQV 267
|
330
....*....|...
gi 489008121 321 ASLYRGMNLRENF 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 |
4.78e-155 |
|
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: 433.03 E-value: 4.78e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489008121 84 AGYNNFYEFGLDKADPAANAGSLRTDPWTLTIGGEVAKPLTLDHDDLTKRFPLEERIYRMRCVEAWSMVVPWVGFPLHKL 163
Cdd:cd02107 1 TTYNNFYEFGTGKDDPARNAGNLPTRPWTVSVSGLVKKPKTLDIDDLMKTFPLEERIYRFRCVEGWSMVVPWVGFPLAAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489008121 164 LALVEPTSSARYVAFKTLYAPDQMPGQKDRFigGGLAYPYVEGLRLDEAMHPLTLLTVGVYGKALPPQNGAPVRLTVPWK 243
Cdd:cd02107 81 LARAEPTSEAKYVRFTTLLDKEQMPGQSGLF--GVLPWPYVEGLRLDEAMHPLTLLAVGLYGEALPKQNGAPIRLVVPWK 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489008121 244 YGFKGIKSIVSIELTRERPPTTWNLAAPDEYGFFANVNPHVDHPRWSQASERFIGAGG 301
Cdd:cd02107 159 YGFKSIKSIVKIEFTKEQPPTTWNLAAPDEYGFYANVNPSVDHPRWSQATERRIGEGG 216
|
|
| MsrP |
COG2041 |
Molybdopterin-dependent catalytic subunit of periplasmic DMSO/TMAO and ... |
90-280 |
2.20e-76 |
|
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: 232.35 E-value: 2.20e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489008121 90 YEFGLDKADPAanagsLRTDPWTLTIGGEVAKPLTLDHDDLtKRFPLEERIYRMRCVEAWS-MVVPWVGFPLHKLLALVE 168
Cdd:COG2041 19 FPVRTAGGVPE-----IDPADWRLRVDGLVEKPLTLTLDDL-LALPLEERIYRLHCVENWSgGVAPWTGVPLRDLLERAG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489008121 169 PTSSARYVAFKTLYAPdqmpgqkdrfiggglaypYVEGLRLDEAMHPLTLLTVGVYGKALPPQNGAPVRLTVPWKYGFKG 248
Cdd:COG2041 93 PKPGAKYVLFESADPG------------------YTESLPLDEALDPDTLLAYGMNGEPLPPEHGAPLRLVVPGLYGFKS 154
|
170 180 190
....*....|....*....|....*....|..
gi 489008121 249 IKSIVSIELTRERPPTTWNLAApdeYGFFANV 280
Cdd:COG2041 155 AKWLVRIEVTDEDPPGYWETRG---YHFYANI 183
|
|
| SO_family_Moco |
cd00321 |
Sulfite oxidase (SO) family, molybdopterin binding domain. This molybdopterin cofactor (Moco) ... |
86-260 |
8.91e-53 |
|
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: 170.83 E-value: 8.91e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489008121 86 YNNFYEFGLDKADPaanagslrtDPWTLTIGGEVAKPLTLDHDDLtKRFPLEERIYRMRCVE-----AWSMVVPWVGFPL 160
Cdd:cd00321 1 FVRNHGGVPPEIDP---------DDWRLEVDGLVEKPLSLTLDDL-KALPQVEVIATLHCVGnrwggGAVSNAEWTGVPL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489008121 161 HKLLALVEPTSSARYVAFktlYAPDQMPGqkdrfiggglaYPYVEGLRLDEAMHPLTLLTVGVYGKALPPQNGAPVRLTV 240
Cdd:cd00321 71 RDLLEEAGPKPGARYVVF---EGADDPGG-----------DGYTTSLPLEKALDPDVLLAYEMNGEPLPPDHGFPLRLVV 136
|
170 180
....*....|....*....|
gi 489008121 241 PWKYGFKGIKSIVSIELTRE 260
Cdd:cd00321 137 PGLYGWKSVKWLRRIEVTDE 156
|
|
| Oxidored_molyb |
pfam00174 |
Oxidoreductase molybdopterin binding domain; This domain is found in a variety of ... |
106-266 |
1.14e-40 |
|
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: 139.94 E-value: 1.14e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489008121 106 LRTDPWTLTIGGEVAKPLTLDHDDLtKRFPLEERIYRMRCVE------------AW----SMVVPWVGFPLHKLLALVEP 169
Cdd:pfam00174 7 IDPDTWRLRVDGLVEKPLTLTLDDL-KAFPQVTVTATLQCVGnrrkemnrvkgvQWgggaIGNAEWTGVPLRDLLERAGV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489008121 170 TSSARYVAFktlYAPDQMPGqkdrfiggglaYPYVEGLRLDEAMHPLTLLTVGVYGKALPPQNGAPVRLTVPWKYGFKGI 249
Cdd:pfam00174 86 KPGAKHVLF---EGADTLGD-----------GGYTTSLPLEKALDDDVLLAYEMNGEPLPPDHGYPLRLVVPGWYGARSV 151
|
170
....*....|....*..
gi 489008121 250 KSIVSIELTRERPPTTW 266
Cdd:pfam00174 152 KWLRRIEVTDEESPGFW 168
|
|
| bact_SO_family_Moco |
cd02108 |
bacterial subgroup of the sulfite oxidase (SO) family of molybdopterin binding domains. This ... |
77-258 |
4.42e-34 |
|
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: 123.65 E-value: 4.42e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489008121 77 LTPEDKVAGYNNFyEFGLDKADPAANAGSlrtdpWTLTIGGEVAKPLTLDHDDLtKRFPLEERIYRMRCVEAWSMVVPWV 156
Cdd:cd02108 1 LAPEFRRNGIRKP-EALAYKALEANDFAD-----YRLEVGGLVEHPLSLSLEEL-RALPQRTQITRHICVEGWSAIGKWG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489008121 157 GFPLHKLLALVEPTSSARYVAFKTLyapdqmpgqkDRFIGGGLaypYVEGLRLDEAMHPLTLLTVGVYGKALPPQNGAPV 236
Cdd:cd02108 74 GVPLRTILELVGPLPEAKYVVFKCA----------DDFAGGDR---YYESIDMASALHPQTLLAYEMNGQPLPIKNGAPL 140
|
170 180
....*....|....*....|..
gi 489008121 237 RLTVPWKYGFKGIKSIVSIELT 258
Cdd:cd02108 141 RLRVETQLGYKQAKWVTEIELV 162
|
|
| arch_bact_SO_family_Moco |
cd02109 |
bacterial and archael members of the sulfite oxidase (SO) family of molybdopterin binding ... |
106-282 |
4.46e-23 |
|
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: 94.23 E-value: 4.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489008121 106 LRTDPWTLTIGGEVAKPLTLDHDDLTKrFPLEERIYRMRCVEAWSMV-VPWVGFPLHKLLALVEPTSSARYVAFKTLYAp 184
Cdd:cd02109 22 VDLEKWRLRVTGLVENPLSLTYEDLLA-LPQTEYTADFHCVTGWSKLdVVWEGVSLKDLLEAARPDPEATFVMAHSYDG- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489008121 185 dqmpgqkdrfiggglaypYVEGLRLDEAMHPLTLLTVGVYGKALPPQNGAPVRLTVPWKYGFKGIKSIVSIELTRERPPT 264
Cdd:cd02109 100 ------------------YTTNLPLEDLLREDSLLATKMDGEPLPPEHGGPARLVVPHLYFWKSAKWLRGIEFLDEDEPG 161
|
170
....*....|....*...
gi 489008121 265 TWnlaapDEYGFFANVNP 282
Cdd:cd02109 162 FW-----ERRGYHERGDP 174
|
|
| SO_family_Moco_dimer |
cd02110 |
Subgroup of sulfite oxidase (SO) family molybdopterin binding domains that contains conserved ... |
105-260 |
2.10e-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: 92.75 E-value: 2.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489008121 105 SLRTDPWTLTIGGEVAKPLTLDHDDLtKRFPLEERIYRMRCV----EAWSMVVP-------------WVGFPLHKLLALV 167
Cdd:cd02110 12 DIDPDAWRLEIHGLVERPLTLTLDDL-KRLPSVEVVATLECSgngrGGFIPVRSgaqwghgavgnarWTGVPLKDLLEEA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489008121 168 EPTSSARYVAFktlYAPDQMPGQKdrfiggglAYPYVEGLRLDEAMHPLTLLTVGVYGKALPPQNGAPVRLTVPWKYGFK 247
Cdd:cd02110 91 GVKPGAKHVLF---EGADVPPGEK--------AADYTRSVPLSKALDDDALLAYEMNGEPLPPDHGYPLRLVVPGWYGAR 159
|
170
....*....|...
gi 489008121 248 GIKSIVSIELTRE 260
Cdd:cd02110 160 SVKWLRRIEVTDQ 172
|
|
| bact_SorA_Moco |
cd02114 |
sulfite:cytochrome c oxidoreductase subunit A (SorA), molybdopterin binding domain. SorA is ... |
105-257 |
3.82e-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: 3.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489008121 105 SLRTDPWTLTIGGEVAKPLTLDHDDLTKRFPLEERIYRMRCV-EAWSMVVP----------------WVGFPLHKLLALV 167
Cdd:cd02114 59 DIDPDAYTLTIDGKVRTPLTLSLAELKRIEPRFEVVAVNQCSgNSRGFFQPrvqgaqlangamgnarWAGVPLKAVLAKA 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489008121 168 EPTSSARYVAFKTLYAP--DQMPGqkdrfiggglaypYVEGLRLDEAMHPLTLLTVGVYGKALPPQNGAPVRLTVPWKYG 245
Cdd:cd02114 139 GVQDGARQVAFRGLDQPvlDVTPD-------------FVKSLDIDHALDGEVMLAWEMNGEPLPVLNGYPLRLVVPGFYA 205
|
170
....*....|..
gi 489008121 246 FKGIKSIVSIEL 257
Cdd:cd02114 206 TYWVKHLSHITV 217
|
|
| PLN02252 |
PLN02252 |
nitrate reductase [NADPH] |
109-258 |
1.07e-07 |
|
nitrate reductase [NADPH]
Pssm-ID: 215141 [Multi-domain] Cd Length: 888 Bit Score: 53.53 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489008121 109 DPWTLTIGGEVAKPLTLDHDDLtKRFPL---------------EERIYRMRCVEAW-----SMVVpWVGFPLHKLLA--- 165
Cdd:PLN02252 132 DEWTVEVTGLVKRPARLTMDEL-VRFPArelpvtlvcagnrrkEQNMVKQTIGFNWgaagvSTSV-WRGVRLRDVLRrcg 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489008121 166 LVEPTSSARYVAFKtlyAPDQMPGqkdrfiGGGLAYPyvEGLRLDEAMHPL--TLLTVGVYGKALPPQNGAPVRLTVPwk 243
Cdd:PLN02252 210 VMSRKGGALNVCFE---GAEDLPG------GGGSKYG--TSITLERAMDPArdVILAYMQNGEPLTPDHGFPVRLIIP-- 276
|
170
....*....|....*...
gi 489008121 244 yGFKG---IKSIVSIELT 258
Cdd:PLN02252 277 -GFIGgrmVKWLKRIIVT 293
|
|
| eukary_NR_Moco |
cd02112 |
molybdopterin binding domain of eukaryotic nitrate reductase (NR). Assimilatory NRs catalyze ... |
109-285 |
1.18e-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: 52.77 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489008121 109 DPWTLTIGGEVAKPLTLDHDDLTKRFPLEERIYRMRCV----EAWSMVVP---------------WVGFPLHKLLALVEP 169
Cdd:cd02112 59 EDWTVEVTGLVEKPTTLTMDELVAMFPSVTFPVTLVCAgnrrKEQNMVKKtigfnwgaagtstslWTGVRLSDLLDRCGP 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489008121 170 TSS---ARYVAFKtlyAPDQMPGQKDRfiggglayPYVEGLRLDEAMHPLT--LLTVGVYGKALPPQNGAPVRLTVPWKY 244
Cdd:cd02112 139 KSPkggARHVCFE---GADDLLPGPNG--------KYGTSITLSWAMDPSKdvMLAYKQNGELLHPDHGFPVRLIIPGQI 207
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489008121 245 GFKGIKSIVSIELTrERPPTTWnlaapdeYGFFAN-VNP-HVD 285
Cdd:cd02112 208 GGRMVKWLKRIVVS-DRESQNH-------YHFHDNrVLPsHVD 242
|
|
| bact_SoxC_Moco |
cd02113 |
bacterial SoxC is a member of the sulfite oxidase (SO) family of molybdopterin binding domains. ... |
113-252 |
1.68e-06 |
|
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: 48.93 E-value: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489008121 113 LTIGGEVAKPLTLDHDDLtKRFPLEERIYRMRC-----VEAWSMVVPWVGFpLHKLLALVEPTSsaryVAFKTLY-APDQ 186
Cdd:cd02113 33 LMIHGMVKKPLVFTMDDL-KRFPSVSRIYFLECsgnggTGWRGAPLPTAQY-THGMLSCSEWTG----VPLSTLLeEAGV 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489008121 187 MPGQKDRFIGGGLAYPYVEGLRLDEAMHPlTLLTVGVYGKALPPQNGAPVRLTVPwkyGFKGIKSI 252
Cdd:cd02113 107 KPGAKWLLAEGADAAAMTRSIPLEKALDD-ALVAYAQNGEALRPENGYPLRLVVP---GWEGNTNV 168
|
|
| |
