|
Name |
Accession |
Description |
Interval |
E-value |
| eukary_SO_Moco |
cd02111 |
molybdopterin binding domain of sulfite oxidase (SO). SO catalyzes the terminal reaction in ... |
178-539 |
0e+00 |
|
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: 598.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992535 178 ALLVRNSKPFNAETPPSLLTDHFYTPNELFFVRNHLPVPDIKTENHRLTVETIKGKTVDLSVEELKKKYKSYTIGSVIQC 257
Cdd:cd02111 1 ALKVNSKKPFNAEPPSSLLASSFITPNELFYVRNHLPVPVVDPDTYSLEVEGPDGTTLSLSLEDLKSLFPKHEVTATLQC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992535 258 AGNRRADMNQYKKVQGLMWEGTAISNAEWTGVRLRDLLADAGIDVFD-DKIKHVHFEGADVDPTGTPYGASIPIEKARG- 335
Cdd:cd02111 81 AGNRRSEMTKVKKVKGLQWGDGAISNAEWGGARLRDVLLDAGIPEDDsQGGLHVHFEGLDVDPTGTPYGASIPLSKALDp 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992535 336 -DEVIVAYHMNGVDIPRDHGAPLRVIVPGNVGARQVKWLRKIIVSEKESDSHWQQKDYRAFSPaVNIGDELKWNTVPSIQ 414
Cdd:cd02111 161 eADVLLAYEMNGTPLPRDHGFPLRVVVPGVVGARSVKWLDRIVVSDEESDSHWQQNDYKGFSP-SVDWDNVDFSKAPAIQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992535 415 EYPVQCAICSPAPNTKV-DRGDETVDISGYAWSGGGRGIIRIEVSVDGGETWNSVEMEQEEKQD-QEHMYAWTLFKAEVK 492
Cdd:cd02111 240 EMPVQSAICSPSVGAPVvTVPPGKITVKGYAWSGGGRKIVRVDVSLDGGRTWKVAELEQEENVWpSGRKWAWTLWEATVP 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 71992535 493 IPPGvKEFNIIAKAVDRAYNTQPETASGIWNVRGLIHNAWHRVPIIV 539
Cdd:cd02111 320 VPAG-KEAEIIAKAVDSAYNVQPETVEPIWNLRGVLNNAWHRVKVVV 365
|
|
| PLN00177 |
PLN00177 |
sulfite oxidase; Provisional |
169-539 |
1.44e-111 |
|
sulfite oxidase; Provisional
Pssm-ID: 177772 [Multi-domain] Cd Length: 393 Bit Score: 337.21 E-value: 1.44e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992535 169 FSNDPERHPALLVRNSKPFNAETPPSLLTDHFYTPNELFFVRNHLPVP---DIktENHRLTVETIKGKTVDLSVEELKKK 245
Cdd:PLN00177 10 YSQEPPRHPSLKINAKEPFNAEPPRSALVSSYITPVDLFYKRNHGPIPivdDI--ERYSVTITGLIENPRKLSMKDIRKL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992535 246 YKsYTIGSVIQCAGNRRADMNQYKKVQGLMWEGTAISNAEWTGVRLRDLLADAGIDVFDDKI----KHVHFEGADVDP-- 319
Cdd:PLN00177 88 PK-YNVTATLQCAGNRRTAMSKVRKVRGVGWDVSAIGNAVWGGAKLADVLELVGIPKLTSITssggKHVEFVSVDKCKee 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992535 320 TGTPYGASIPIEKARGDE--VIVAYHMNGVDIPRDHGAPLRVIVPGNVGARQVKWLRKIIVSEKESDSHWQQKDYRAFSP 397
Cdd:PLN00177 167 NGGPYKASIPLSQATNPEadVLLAYEMNGEVLNRDHGYPLRVVVPGVIGARSVKWLDSINIIAEECQGFFMQKDYKMFPP 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992535 398 AVNiGDELKWNTVPSIQEYPVQCAICSPAPNTKVDRGDetVDISGYAWSGGGRGIIRIEVSVDGGETWnsVEMEQEEKQD 477
Cdd:PLN00177 247 SVN-WDNINWSTRRPQMDFPVQSAICSLEDVNAIKPGK--VTVAGYALSGGGRGIERVDISVDGGKTW--VEASRYQKPG 321
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992535 478 QEHM--------YAWTLFKAEVKIPPGVKefnIIAKAVDRAYNTQPETASGIWNVRGLIHNAWHRVPIIV 539
Cdd:PLN00177 322 VPYIsddissdkWAWVLFEATVDVPQSTE---IVAKAVDSAANVQPESVESIWNLRGILNTSWHRVQLRV 388
|
|
| Oxidored_molyb |
pfam00174 |
Oxidoreductase molybdopterin binding domain; This domain is found in a variety of ... |
212-387 |
1.34e-78 |
|
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: 243.95 E-value: 1.34e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992535 212 HLPVPDIKTENHRLTVETIKGKTVDLSVEELKKkYKSYTIGSVIQCAGNRRADMNQykkVQGLMWEGTAISNAEWTGVRL 291
Cdd:pfam00174 1 HGPVPEIDPDTWRLRVDGLVEKPLTLTLDDLKA-FPQVTVTATLQCVGNRRKEMNR---VKGVQWGGGAIGNAEWTGVPL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992535 292 RDLLADAGIDvfdDKIKHVHFEGADVDPTGtPYGASIPIEKARGDEVIVAYHMNGVDIPRDHGAPLRVIVPGNVGARQVK 371
Cdd:pfam00174 77 RDLLERAGVK---PGAKHVLFEGADTLGDG-GYTTSLPLEKALDDDVLLAYEMNGEPLPPDHGYPLRLVVPGWYGARSVK 152
|
170
....*....|....*.
gi 71992535 372 WLRKIIVSEKESDSHW 387
Cdd:pfam00174 153 WLRRIEVTDEESPGFW 168
|
|
| MsrP |
COG2041 |
Molybdopterin-dependent catalytic subunit of periplasmic DMSO/TMAO and ... |
207-397 |
1.57e-49 |
|
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: 168.80 E-value: 1.57e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992535 207 FFVRNHLPVPDIKTENHRLTVETIKGKTVDLSVEELKKkYKSYTIGSVIQCAGNRRAdmnqykkvqglmwegtaiSNAEW 286
Cdd:COG2041 19 FPVRTAGGVPEIDPADWRLRVDGLVEKPLTLTLDDLLA-LPLEERIYRLHCVENWSG------------------GVAPW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992535 287 TGVRLRDLLADAGIDvfdDKIKHVHFEGADvdptgTPYGASIPIEKARGDEVIVAYHMNGVDIPRDHGAPLRVIVPGNVG 366
Cdd:COG2041 80 TGVPLRDLLERAGPK---PGAKYVLFESAD-----PGYTESLPLDEALDPDTLLAYGMNGEPLPPEHGAPLRLVVPGLYG 151
|
170 180 190
....*....|....*....|....*....|.
gi 71992535 367 ARQVKWLRKIIVSEKESDSHWQQKDYRAFSP 397
Cdd:COG2041 152 FKSAKWLVRIEVTDEDPPGYWETRGYHFYAN 182
|
|
| Cyt-b5 |
pfam00173 |
Cytochrome b5-like Heme/Steroid binding domain; This family includes heme binding domains from ... |
85-157 |
1.20e-18 |
|
Cytochrome b5-like Heme/Steroid binding domain; This family includes heme binding domains from a diverse range of proteins. This family also includes proteins that bind to steroids. The family includes progesterone receptors. Many members of this subfamily are membrane anchored by an N-terminal transmembrane alpha helix. This family also includes a domain in some chitin synthases. There is no known ligand for this domain in the chitin synthases.
Pssm-ID: 459698 [Multi-domain] Cd Length: 74 Bit Score: 80.36 E-value: 1.20e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71992535 85 EEVKKHGKDaDRIWVTYKDGVYDVTDFIAMHPGG-DKILLAAGA-AVDPFWALysQHKTKEVLEILEGYRIGKLD 157
Cdd:pfam00173 3 EELSKHNGD-GDCWVAINGKVYDVTKFLKEHPGGeDVILSAAGKdATDAFEAI--GHSEDAAEKLLKKYRIGELA 74
|
|
| PLN02252 |
PLN02252 |
nitrate reductase [NADPH] |
77-197 |
1.83e-13 |
|
nitrate reductase [NADPH]
Pssm-ID: 215141 [Multi-domain] Cd Length: 888 Bit Score: 73.17 E-value: 1.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992535 77 ENLQIYKQEEVKKHGKdADRIWVTYKDGVYDVTDFIAMHPGG-DKILLAAGA-AVDPFWALYSQHKTKevleILEGYRIG 154
Cdd:PLN02252 515 TGSKQYTMSEVRKHNS-EDSCWIVVHGHVYDCTRFLKDHPGGaDSILINAGTdCTEEFDAIHSDKAKK----MLEDYRIG 589
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 71992535 155 KLDVKDVpkPVADAFSNDPERHPALLVRNSKPFNAETPPSLLT 197
Cdd:PLN02252 590 ELVTTGA--AASSSASSHPLSAISTASALAAASPAPGRPVALN 630
|
|
| CYB5 |
COG5274 |
Cytochrome b involved in lipid metabolism [Energy production and conversion, Lipid transport ... |
82-156 |
5.74e-11 |
|
Cytochrome b involved in lipid metabolism [Energy production and conversion, Lipid transport and metabolism];
Pssm-ID: 444085 [Multi-domain] Cd Length: 93 Bit Score: 58.90 E-value: 5.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992535 82 YKQEEVKKHgKDADRIWVTYKDGVYDVTDFIAMHPGGDKILLA-----AGAAVDpfwalySQHKTKE-VLEILEGYRIGK 155
Cdd:COG5274 18 YTLAEVATH-NTLSDCWMAIDGNVYDLTEYIPKHPGGEAVILRwcgkdATEAFN------TKHPHSPkAERLLESYRIGR 90
|
.
gi 71992535 156 L 156
Cdd:COG5274 91 L 91
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| eukary_SO_Moco |
cd02111 |
molybdopterin binding domain of sulfite oxidase (SO). SO catalyzes the terminal reaction in ... |
178-539 |
0e+00 |
|
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: 598.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992535 178 ALLVRNSKPFNAETPPSLLTDHFYTPNELFFVRNHLPVPDIKTENHRLTVETIKGKTVDLSVEELKKKYKSYTIGSVIQC 257
Cdd:cd02111 1 ALKVNSKKPFNAEPPSSLLASSFITPNELFYVRNHLPVPVVDPDTYSLEVEGPDGTTLSLSLEDLKSLFPKHEVTATLQC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992535 258 AGNRRADMNQYKKVQGLMWEGTAISNAEWTGVRLRDLLADAGIDVFD-DKIKHVHFEGADVDPTGTPYGASIPIEKARG- 335
Cdd:cd02111 81 AGNRRSEMTKVKKVKGLQWGDGAISNAEWGGARLRDVLLDAGIPEDDsQGGLHVHFEGLDVDPTGTPYGASIPLSKALDp 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992535 336 -DEVIVAYHMNGVDIPRDHGAPLRVIVPGNVGARQVKWLRKIIVSEKESDSHWQQKDYRAFSPaVNIGDELKWNTVPSIQ 414
Cdd:cd02111 161 eADVLLAYEMNGTPLPRDHGFPLRVVVPGVVGARSVKWLDRIVVSDEESDSHWQQNDYKGFSP-SVDWDNVDFSKAPAIQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992535 415 EYPVQCAICSPAPNTKV-DRGDETVDISGYAWSGGGRGIIRIEVSVDGGETWNSVEMEQEEKQD-QEHMYAWTLFKAEVK 492
Cdd:cd02111 240 EMPVQSAICSPSVGAPVvTVPPGKITVKGYAWSGGGRKIVRVDVSLDGGRTWKVAELEQEENVWpSGRKWAWTLWEATVP 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 71992535 493 IPPGvKEFNIIAKAVDRAYNTQPETASGIWNVRGLIHNAWHRVPIIV 539
Cdd:cd02111 320 VPAG-KEAEIIAKAVDSAYNVQPETVEPIWNLRGVLNNAWHRVKVVV 365
|
|
| PLN00177 |
PLN00177 |
sulfite oxidase; Provisional |
169-539 |
1.44e-111 |
|
sulfite oxidase; Provisional
Pssm-ID: 177772 [Multi-domain] Cd Length: 393 Bit Score: 337.21 E-value: 1.44e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992535 169 FSNDPERHPALLVRNSKPFNAETPPSLLTDHFYTPNELFFVRNHLPVP---DIktENHRLTVETIKGKTVDLSVEELKKK 245
Cdd:PLN00177 10 YSQEPPRHPSLKINAKEPFNAEPPRSALVSSYITPVDLFYKRNHGPIPivdDI--ERYSVTITGLIENPRKLSMKDIRKL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992535 246 YKsYTIGSVIQCAGNRRADMNQYKKVQGLMWEGTAISNAEWTGVRLRDLLADAGIDVFDDKI----KHVHFEGADVDP-- 319
Cdd:PLN00177 88 PK-YNVTATLQCAGNRRTAMSKVRKVRGVGWDVSAIGNAVWGGAKLADVLELVGIPKLTSITssggKHVEFVSVDKCKee 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992535 320 TGTPYGASIPIEKARGDE--VIVAYHMNGVDIPRDHGAPLRVIVPGNVGARQVKWLRKIIVSEKESDSHWQQKDYRAFSP 397
Cdd:PLN00177 167 NGGPYKASIPLSQATNPEadVLLAYEMNGEVLNRDHGYPLRVVVPGVIGARSVKWLDSINIIAEECQGFFMQKDYKMFPP 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992535 398 AVNiGDELKWNTVPSIQEYPVQCAICSPAPNTKVDRGDetVDISGYAWSGGGRGIIRIEVSVDGGETWnsVEMEQEEKQD 477
Cdd:PLN00177 247 SVN-WDNINWSTRRPQMDFPVQSAICSLEDVNAIKPGK--VTVAGYALSGGGRGIERVDISVDGGKTW--VEASRYQKPG 321
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992535 478 QEHM--------YAWTLFKAEVKIPPGVKefnIIAKAVDRAYNTQPETASGIWNVRGLIHNAWHRVPIIV 539
Cdd:PLN00177 322 VPYIsddissdkWAWVLFEATVDVPQSTE---IVAKAVDSAANVQPESVESIWNLRGILNTSWHRVQLRV 388
|
|
| SO_family_Moco_dimer |
cd02110 |
Subgroup of sulfite oxidase (SO) family molybdopterin binding domains that contains conserved ... |
206-535 |
1.90e-110 |
|
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: 331.57 E-value: 1.90e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992535 206 LFFVRNHLPVPDIKTENHRLTVETIKGKTVDLSVEELKKkYKSYTIGSVIQCAGNRRADMNqyKKVQGLMWEGTAISNAE 285
Cdd:cd02110 1 LFFVRNHGGVPDIDPDAWRLEIHGLVERPLTLTLDDLKR-LPSVEVVATLECSGNGRGGFI--PVRSGAQWGHGAVGNAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992535 286 WTGVRLRDLLADAGIDvfdDKIKHVHFEGADVDPTGT--PYGASIPIEKARGDEVIVAYHMNGVDIPRDHGAPLRVIVPG 363
Cdd:cd02110 78 WTGVPLKDLLEEAGVK---PGAKHVLFEGADVPPGEKaaDYTRSVPLSKALDDDALLAYEMNGEPLPPDHGYPLRLVVPG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992535 364 NVGARQVKWLRKIIVSEKESDSHWQQKDYRAFSPAVNigDELKWNTVPsIQEYPVQCAICSPAPNTKVDRGDETVdISGY 443
Cdd:cd02110 155 WYGARSVKWLRRIEVTDQPSDGYWQTRDYTVPPPDVD--AVGGKARRP-IGEMPVKSVITSPSPGAELVSGGRVE-IGGV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992535 444 AWSgGGRGIIRIEVSVDGGETWNSVEMEQEEKqdqeHMYAWTLFKAEVKIPPGVKEfnIIAKAVDRAYNTQPETASGIWN 523
Cdd:cd02110 231 AWS-GGRGIRRVEVSLDGGRTWQEARLEGPLA----GPRAWRQWELDWDLPPGEYE--LVARATDSTGNVQPERAEWNWN 303
|
330
....*....|..
gi 71992535 524 VRGLIHNAWHRV 535
Cdd:cd02110 304 PGGYGNNHWHRV 315
|
|
| eukary_NR_Moco |
cd02112 |
molybdopterin binding domain of eukaryotic nitrate reductase (NR). Assimilatory NRs catalyze ... |
174-537 |
1.84e-99 |
|
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: 305.85 E-value: 1.84e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992535 174 ERHPALL-VRNSKPFNAETPPSLLTDH-FYTPNELFFVRNHLPVPDIKTENHRLTVETIKGKTVDLSVEELKKKYKSYTI 251
Cdd:cd02112 10 PRDPRLIrLTGKHPFNSEPPLTELMDHgFITPSNLHYVRNHGPVPREKWEDWTVEVTGLVEKPTTLTMDELVAMFPSVTF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992535 252 GSVIQCAGNRRADMNQYKKVQGLMWEGTAISNAEWTGVRLRDLLADAGIDVFDDKIKHVHFEGADVDPTG--TPYGASIP 329
Cdd:cd02112 90 PVTLVCAGNRRKEQNMVKKTIGFNWGAAGTSTSLWTGVRLSDLLDRCGPKSPKGGARHVCFEGADDLLPGpnGKYGTSIT 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992535 330 IEKARGDE--VIVAYHMNGVDIPRDHGAPLRVIVPGNVGARQVKWLRKIIVSEKESDSHWQQKDYRAFSPAVN--IGDEL 405
Cdd:cd02112 170 LSWAMDPSkdVMLAYKQNGELLHPDHGFPVRLIIPGQIGGRMVKWLKRIVVSDRESQNHYHFHDNRVLPSHVDaeLANEE 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992535 406 KWNTVPS--IQEYPVQCAICSPAPNTKVD----RGDETVDISGYAWSGGGRGIIRIEVSVDGGETWNSVEMEQEEK-QDQ 478
Cdd:cd02112 250 GWWYKPEyiINDLNVNSAITTPAHDEVLPlnglTTAETYTMKGYAYAGGGRRVTRVEVSLDDGKSWKLASIDYPEDpTKY 329
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71992535 479 EHMYAWTLFKAEVKIPP--GVKEfnIIAKAVDRAYNTQPETAsgIWNVRGLIHNAWHRVPI 537
Cdd:cd02112 330 GKCWCWCFWSLDVPLSEllAAKE--ICVRAWDESMNTQPRDM--TWNVMGMMNNCWFRVKI 386
|
|
| PLN02252 |
PLN02252 |
nitrate reductase [NADPH] |
174-537 |
9.29e-84 |
|
nitrate reductase [NADPH]
Pssm-ID: 215141 [Multi-domain] Cd Length: 888 Bit Score: 278.48 E-value: 9.29e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992535 174 ERHPALLVRNSK-PFNAETPPSLLTDH-FYTPNELFFVRNHLPVPDIKTENHRLTVETIKGKTVDLSVEELKKkYKSYTI 251
Cdd:PLN02252 83 PRHPSLVRLTGKhPFNCEPPLARLMEHgFITPAPLHYVRNHGAVPRADWDEWTVEVTGLVKRPARLTMDELVR-FPAREL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992535 252 GSVIQCAGNRRADMNQYKKVQGLMWEGTAISNAEWTGVRLRDLLADAGIDVFDDKIKHVHFEGADVDPTG--TPYGASIP 329
Cdd:PLN02252 162 PVTLVCAGNRRKEQNMVKQTIGFNWGAAGVSTSVWRGVRLRDVLRRCGVMSRKGGALNVCFEGAEDLPGGggSKYGTSIT 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992535 330 IEKAR--GDEVIVAYHMNGVDIPRDHGAPLRVIVPGNVGARQVKWLRKIIVSEKESDSHWQQKDYRAFSPAVN--IGDEL 405
Cdd:PLN02252 242 LERAMdpARDVILAYMQNGEPLTPDHGFPVRLIIPGFIGGRMVKWLKRIIVTTAESDNYYHYRDNRVLPSHVDaeLANAE 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992535 406 KWNTVPS--IQEYPVQCAICSPAPNTKVD----RGDETVDISGYAWSGGGRGIIRIEVSVDGGETWNSVEMEQEEKQDQE 479
Cdd:PLN02252 322 GWWYKPEyiINELNINSVITTPAHDEILPinasTTQRPYTMKGYAYSGGGRKVTRVEVSLDGGETWRLCDLDHPEKPTKY 401
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71992535 480 HMY-AWTLFKAEVKIPP--GVKEfnIIAKAVDRAYNTQPETAsgIWNVRGLIHNAWHRVPI 537
Cdd:PLN02252 402 GKYwCWCFWSLDVEVLDllGAKE--IAVRAWDESMNTQPEKL--IWNLMGMMNNCWFRVKV 458
|
|
| Oxidored_molyb |
pfam00174 |
Oxidoreductase molybdopterin binding domain; This domain is found in a variety of ... |
212-387 |
1.34e-78 |
|
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: 243.95 E-value: 1.34e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992535 212 HLPVPDIKTENHRLTVETIKGKTVDLSVEELKKkYKSYTIGSVIQCAGNRRADMNQykkVQGLMWEGTAISNAEWTGVRL 291
Cdd:pfam00174 1 HGPVPEIDPDTWRLRVDGLVEKPLTLTLDDLKA-FPQVTVTATLQCVGNRRKEMNR---VKGVQWGGGAIGNAEWTGVPL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992535 292 RDLLADAGIDvfdDKIKHVHFEGADVDPTGtPYGASIPIEKARGDEVIVAYHMNGVDIPRDHGAPLRVIVPGNVGARQVK 371
Cdd:pfam00174 77 RDLLERAGVK---PGAKHVLFEGADTLGDG-GYTTSLPLEKALDDDVLLAYEMNGEPLPPDHGYPLRLVVPGWYGARSVK 152
|
170
....*....|....*.
gi 71992535 372 WLRKIIVSEKESDSHW 387
Cdd:pfam00174 153 WLRRIEVTDEESPGFW 168
|
|
| SO_family_Moco |
cd00321 |
Sulfite oxidase (SO) family, molybdopterin binding domain. This molybdopterin cofactor (Moco) ... |
208-381 |
6.98e-62 |
|
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: 200.10 E-value: 6.98e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992535 208 FVRNHLPVPD-IKTENHRLTVETIKGKTVDLSVEELKKkYKSYTIGSVIQCAGNRradmnqykkvqglmWEGTAISNAEW 286
Cdd:cd00321 1 FVRNHGGVPPeIDPDDWRLEVDGLVEKPLSLTLDDLKA-LPQVEVIATLHCVGNR--------------WGGGAVSNAEW 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992535 287 TGVRLRDLLADAGIDvfdDKIKHVHFEGADvDPTGTPYGASIPIEKARGDEVIVAYHMNGVDIPRDHGAPLRVIVPGNVG 366
Cdd:cd00321 66 TGVPLRDLLEEAGPK---PGARYVVFEGAD-DPGGDGYTTSLPLEKALDPDVLLAYEMNGEPLPPDHGFPLRLVVPGLYG 141
|
170
....*....|....*
gi 71992535 367 ARQVKWLRKIIVSEK 381
Cdd:cd00321 142 WKSVKWLRRIEVTDE 156
|
|
| Mo-co_dimer |
pfam03404 |
Mo-co oxidoreductase dimerization domain; This domain is found in molybdopterin cofactor ... |
411-540 |
2.52e-58 |
|
Mo-co oxidoreductase dimerization domain; This domain is found in molybdopterin cofactor (Mo-co) oxidoreductases. It is involved in dimer formation, and has an Ig-fold structure.
Pssm-ID: 427280 [Multi-domain] Cd Length: 136 Bit Score: 190.27 E-value: 2.52e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992535 411 PSIQEYPVQCAICSPAPNTKVDRG--DETVDISGYAWSGGGRGIIRIEVSVDGGETWNSVEMEQEEK-----QDQEHMYA 483
Cdd:pfam03404 2 YAIYDLNVNSAICSPEHDEVVKLGaaQGTYTIKGYAYSGGGRRITRVEVSLDGGKTWRLAEIDYEEDpyrygEWREKCWC 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 71992535 484 WTLFKAEVKIPPGVKEFNIIAKAVDRAYNTQPETAsgIWNVRGLIHNAWHRVPIIVK 540
Cdd:pfam03404 82 WCFWSLDIPVSDLLKAKEILVRAVDEAMNVQPEDM--YWNVRGMMNNPWHRVKIHVE 136
|
|
| bact_SorA_Moco |
cd02114 |
sulfite:cytochrome c oxidoreductase subunit A (SorA), molybdopterin binding domain. SorA is ... |
170-537 |
2.88e-52 |
|
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: 181.94 E-value: 2.88e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992535 170 SNDPERHPALLVrNSKPFNAETPPSLLTDHFYTPNELFFVRNHLP-VP-DIKTENHRLTVETIKGKTVDLSVEELKKKYK 247
Cdd:cd02114 11 VPFPQKRPLIRL-TTRPPHLETPFSVFNEGLITPNDAFFVRYHLAgIPlDIDPDAYTLTIDGKVRTPLTLSLAELKRIEP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992535 248 SYTIGSVIQCAGNRRADMNqyKKVQGLMWEGTAISNAEWTGVRLRDLLADAGIDvfdDKIKHVHFEGAD--VDPTGTPYG 325
Cdd:cd02114 90 RFEVVAVNQCSGNSRGFFQ--PRVQGAQLANGAMGNARWAGVPLKAVLAKAGVQ---DGARQVAFRGLDqpVLDVTPDFV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992535 326 ASIPIEKARGDEVIVAYHMNGVDIPRDHGAPLRVIVPGNVGARQVKWLRKIIVSEKESDSHWQQKDYRafspavnIGDEL 405
Cdd:cd02114 165 KSLDIDHALDGEVMLAWEMNGEPLPVLNGYPLRLVVPGFYATYWVKHLSHITVLDKEFDGFWASQAYR-------IPDNA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992535 406 KWNTVPS--------IQEYPVQCAICSPAPNTKVDRGDETVdISGYAWSgGGRGIIRIEVSVDGGETWNSVEMEQEEKQd 477
Cdd:cd02114 238 DAGVEPGtapdrtapINRFKVRSFITSLENGAIVAPAGELA-LRGIAFD-GGSGIRRVDVSADGGDSWTQATLGPDLGR- 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71992535 478 qehmYAWTLFKAEVKIP-PGvkEFNIIAKAVDRAYNTQPETASgiWNVRGLIHNAWHRVPI 537
Cdd:cd02114 315 ----FSFRGWKLTLDGVkKG--PLTLMVRATNNDGQTQPLRAP--WNPGGYMRNVVERTRI 367
|
|
| MsrP |
COG2041 |
Molybdopterin-dependent catalytic subunit of periplasmic DMSO/TMAO and ... |
207-397 |
1.57e-49 |
|
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: 168.80 E-value: 1.57e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992535 207 FFVRNHLPVPDIKTENHRLTVETIKGKTVDLSVEELKKkYKSYTIGSVIQCAGNRRAdmnqykkvqglmwegtaiSNAEW 286
Cdd:COG2041 19 FPVRTAGGVPEIDPADWRLRVDGLVEKPLTLTLDDLLA-LPLEERIYRLHCVENWSG------------------GVAPW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992535 287 TGVRLRDLLADAGIDvfdDKIKHVHFEGADvdptgTPYGASIPIEKARGDEVIVAYHMNGVDIPRDHGAPLRVIVPGNVG 366
Cdd:COG2041 80 TGVPLRDLLERAGPK---PGAKYVLFESAD-----PGYTESLPLDEALDPDTLLAYGMNGEPLPPEHGAPLRLVVPGLYG 151
|
170 180 190
....*....|....*....|....*....|.
gi 71992535 367 ARQVKWLRKIIVSEKESDSHWQQKDYRAFSP 397
Cdd:COG2041 152 FKSAKWLVRIEVTDEDPPGYWETRGYHFYAN 182
|
|
| bact_SoxC_Moco |
cd02113 |
bacterial SoxC is a member of the sulfite oxidase (SO) family of molybdopterin binding domains. ... |
202-537 |
9.64e-46 |
|
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: 163.34 E-value: 9.64e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992535 202 TPNELFFVRNHLPVPDIKTENHRLTVETIKGKTVDLSVEELKKkYKSYTIGSVIQCAGNRRADMNqYKKVQGLMWEGTAI 281
Cdd:cd02113 10 TPNGLHFERHHGGVPDIDPAQHRLMIHGMVKKPLVFTMDDLKR-FPSVSRIYFLECSGNGGTGWR-GAPLPTAQYTHGML 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992535 282 SNAEWTGVRLRDLLADAGIDvfdDKIKHVHFEGADvdptGTPYGASIPIEKARgDEVIVAYHMNGVDIPRDHGAPLRVIV 361
Cdd:cd02113 88 SCSEWTGVPLSTLLEEAGVK---PGAKWLLAEGAD----AAAMTRSIPLEKAL-DDALVAYAQNGEALRPENGYPLRLVV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992535 362 PGNVGARQVKWLRKIIVsekeSDSHWQQKD-------------YRAFSpavnigdelkwntvpSIQEypVQCAICSPAPN 428
Cdd:cd02113 160 PGWEGNTNVKWLRRIEV----GDQPWMTREetskytdllpdgrARQFS---------------FVME--AKSVITSPSGG 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992535 429 TKVDRGDETVdISGYAWSGGGRgIIRIEVSVDGGETWNSVEMEqeekqDQEHMYAWTLFKAEVKIPPgvKEFNIIAKAVD 508
Cdd:cd02113 219 QRLREPGFHE-ISGLAWSGRGR-IRRVDVSFDGGRTWQDARLE-----GPVLPKALTRFRLPWKWDG--RPAVLQSRATD 289
|
330 340
....*....|....*....|....*....
gi 71992535 509 RAYNTQPETASgIWNVRGlIHNAWHRVPI 537
Cdd:cd02113 290 ETGYVQPTRAE-LRAVRG-TNSIYHNNAI 316
|
|
| arch_bact_SO_family_Moco |
cd02109 |
bacterial and archael members of the sulfite oxidase (SO) family of molybdopterin binding ... |
200-392 |
4.72e-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: 93.46 E-value: 4.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992535 200 FYTPNelFFVRNHLPVPDIKTENHRLTVETIKGKTVDLSVEELKKKYKSytigsviqcagNRRADMNQYKKvqglmWegt 279
Cdd:cd02109 6 YLTEK--FPVLDAGDVPEVDLEKWRLRVTGLVENPLSLTYEDLLALPQT-----------EYTADFHCVTG-----W--- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992535 280 AISNAEWTGVRLRDLLADAGIDvfdDKIKHVHFEGADvdptgtPYGASIPIEKARGDEVIVAYHMNGVDIPRDHGAPLRV 359
Cdd:cd02109 65 SKLDVVWEGVSLKDLLEAARPD---PEATFVMAHSYD------GYTTNLPLEDLLREDSLLATKMDGEPLPPEHGGPARL 135
|
170 180 190
....*....|....*....|....*....|...
gi 71992535 360 IVPGNVGARQVKWLRKIIVSEKESDSHWQQKDY 392
Cdd:cd02109 136 VVPHLYFWKSAKWLRGIEFLDEDEPGFWERRGY 168
|
|
| Cyt-b5 |
pfam00173 |
Cytochrome b5-like Heme/Steroid binding domain; This family includes heme binding domains from ... |
85-157 |
1.20e-18 |
|
Cytochrome b5-like Heme/Steroid binding domain; This family includes heme binding domains from a diverse range of proteins. This family also includes proteins that bind to steroids. The family includes progesterone receptors. Many members of this subfamily are membrane anchored by an N-terminal transmembrane alpha helix. This family also includes a domain in some chitin synthases. There is no known ligand for this domain in the chitin synthases.
Pssm-ID: 459698 [Multi-domain] Cd Length: 74 Bit Score: 80.36 E-value: 1.20e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71992535 85 EEVKKHGKDaDRIWVTYKDGVYDVTDFIAMHPGG-DKILLAAGA-AVDPFWALysQHKTKEVLEILEGYRIGKLD 157
Cdd:pfam00173 3 EELSKHNGD-GDCWVAINGKVYDVTKFLKEHPGGeDVILSAAGKdATDAFEAI--GHSEDAAEKLLKKYRIGELA 74
|
|
| bact_SO_family_Moco |
cd02108 |
bacterial subgroup of the sulfite oxidase (SO) family of molybdopterin binding domains. This ... |
271-393 |
1.99e-17 |
|
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: 80.51 E-value: 1.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992535 271 VQGlmWegTAIsnAEWTGVRLRDLLADAGIDvfdDKIKHVHFEGADVDPTGTPYGASIPIEKARGDEVIVAYHMNGVDIP 350
Cdd:cd02108 63 VEG--W--SAI--GKWGGVPLRTILELVGPL---PEAKYVVFKCADDFAGGDRYYESIDMASALHPQTLLAYEMNGQPLP 133
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 71992535 351 RDHGAPLRVIVPGNVGARQVKWLRKIIVSEKESDSHWQQKDYR 393
Cdd:cd02108 134 IKNGAPLRLRVETQLGYKQAKWVTEIELVNDLPGIGGGKGGYW 176
|
|
| PLN02252 |
PLN02252 |
nitrate reductase [NADPH] |
77-197 |
1.83e-13 |
|
nitrate reductase [NADPH]
Pssm-ID: 215141 [Multi-domain] Cd Length: 888 Bit Score: 73.17 E-value: 1.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992535 77 ENLQIYKQEEVKKHGKdADRIWVTYKDGVYDVTDFIAMHPGG-DKILLAAGA-AVDPFWALYSQHKTKevleILEGYRIG 154
Cdd:PLN02252 515 TGSKQYTMSEVRKHNS-EDSCWIVVHGHVYDCTRFLKDHPGGaDSILINAGTdCTEEFDAIHSDKAKK----MLEDYRIG 589
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 71992535 155 KLDVKDVpkPVADAFSNDPERHPALLVRNSKPFNAETPPSLLT 197
Cdd:PLN02252 590 ELVTTGA--AASSSASSHPLSAISTASALAAASPAPGRPVALN 630
|
|
| CYB5 |
COG5274 |
Cytochrome b involved in lipid metabolism [Energy production and conversion, Lipid transport ... |
82-156 |
5.74e-11 |
|
Cytochrome b involved in lipid metabolism [Energy production and conversion, Lipid transport and metabolism];
Pssm-ID: 444085 [Multi-domain] Cd Length: 93 Bit Score: 58.90 E-value: 5.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992535 82 YKQEEVKKHgKDADRIWVTYKDGVYDVTDFIAMHPGGDKILLA-----AGAAVDpfwalySQHKTKE-VLEILEGYRIGK 155
Cdd:COG5274 18 YTLAEVATH-NTLSDCWMAIDGNVYDLTEYIPKHPGGEAVILRwcgkdATEAFN------TKHPHSPkAERLLESYRIGR 90
|
.
gi 71992535 156 L 156
Cdd:COG5274 91 L 91
|
|
| COG3915 |
COG3915 |
Uncharacterized conserved protein [Function unknown]; |
285-362 |
1.47e-09 |
|
Uncharacterized conserved protein [Function unknown];
Pssm-ID: 443120 Cd Length: 167 Bit Score: 57.21 E-value: 1.47e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71992535 285 EWTGVRLRDLLADAGIDVfddkiKHVHFEGADvDptgtpYGASIPIEKARGDEVIVAYHMNGVDIPRDHGAPLRVIVP 362
Cdd:COG3915 75 TFRGVLLRDLLAAVGAKG-----TTLRAVALN-D-----YAVEIPISDLEEYGVILAYRMDGKPMSVRDKGPLWLIYP 141
|
|
| YedY_like_Moco |
cd02107 |
YedY_like molybdopterin cofactor (Moco) binding domain, a subgroup of the sulfite oxidase (SO) ... |
286-387 |
3.08e-05 |
|
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: 45.14 E-value: 3.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992535 286 WTGVRLRDLLADAGIDvfdDKIKHVHFEgADVDPTGT------------PYGASIPIEKARGDEVIVAYHMNGVDIPRDH 353
Cdd:cd02107 72 WVGFPLAALLARAEPT---SEAKYVRFT-TLLDKEQMpgqsglfgvlpwPYVEGLRLDEAMHPLTLLAVGLYGEALPKQN 147
|
90 100 110
....*....|....*....|....*....|....
gi 71992535 354 GAPLRVIVPGNVGARQVKWLRKIIVSEKESDSHW 387
Cdd:cd02107 148 GAPIRLVVPWKYGFKSIKSIVKIEFTKEQPPTTW 181
|
|
| PLN03198 |
PLN03198 |
delta6-acyl-lipid desaturase; Provisional |
82-167 |
5.21e-05 |
|
delta6-acyl-lipid desaturase; Provisional
Pssm-ID: 178739 [Multi-domain] Cd Length: 526 Bit Score: 45.84 E-value: 5.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992535 82 YKQEEVKKHGKDADrIWVTYKDGVYDVTDFIAMHPGGDKILLAAGA-AVDPFWALYSQHKTKevleILEGYRIGKLD-VK 159
Cdd:PLN03198 106 HLLSEVAAHNKPND-CWIVIKNKVYDVSDFAAEHPGGSVISTYFGRdGTDAFSSFHAASTWK----ILQDFYIGDVDnVE 180
|
....*...
gi 71992535 160 DVPKPVAD 167
Cdd:PLN03198 181 PTPELLKD 188
|
|
| PRK05363 |
PRK05363 |
protein-methionine-sulfoxide reductase catalytic subunit MsrP; |
286-389 |
1.17e-04 |
|
protein-methionine-sulfoxide reductase catalytic subunit MsrP;
Pssm-ID: 235431 Cd Length: 280 Bit Score: 44.05 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992535 286 WTGVRLRDLLADAGIDvfdDKIKHVHFEGAdVDPTGTPyGASIPI------EKARGDE-----VIVAYHMNGVDIPRDHG 354
Cdd:PRK05363 107 WIGFPLAKLLKRVEPT---SNAKYVAFETL-YDPEQMP-GQRSRFldwpyvEGLRLDEamhplTLLAVGLYGKTLPNQNG 181
|
90 100 110
....*....|....*....|....*....|....*
gi 71992535 355 APLRVIVPGNVGARQVKWLRKIIVSEKESDSHWQQ 389
Cdd:PRK05363 182 APIRLVVPWKYGFKSIKSIVRIRLTEEQPPTTWNL 216
|
|
| PLN03199 |
PLN03199 |
delta6-acyl-lipid desaturase-like protein; Provisional |
66-152 |
1.77e-04 |
|
delta6-acyl-lipid desaturase-like protein; Provisional
Pssm-ID: 178740 [Multi-domain] Cd Length: 485 Bit Score: 44.26 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71992535 66 AKDETMSEKKLENLQIYKQEEVKKHGKDADrIWVTYKDGVYDVTDFIAmHPGGDKILLAAG-AAVDPFWALYSQ------ 138
Cdd:PLN03199 10 AKGRSAALKLAEKPQKISWQEVKKHASPDD-AWIIHQNKVYDVSNWHD-HPGGAVIFTHAGdDMTDIFAAFHAPgsqalm 87
|
90 100
....*....|....*....|....*...
gi 71992535 139 --------------HKTKEVLEILEGYR 152
Cdd:PLN03199 88 kkfyigdlipesteHKDPQQIAFEKGYR 115
|
|
| COG4892 |
COG4892 |
Predicted heme/steroid binding protein [General function prediction only]; |
79-122 |
2.07e-04 |
|
Predicted heme/steroid binding protein [General function prediction only];
Pssm-ID: 443920 [Multi-domain] Cd Length: 75 Bit Score: 39.81 E-value: 2.07e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71992535 79 LQIYKQEEVKK-HGKDADRIWVTYKDGVYDV--------------------TDFIAMHPGGDKIL 122
Cdd:COG4892 1 MKEFTLEELAKyNGKDGNPAYVAVNGKVYDVtnsrlwkngthyghwagqdlTDELKDAPHGESVL 65
|
|
| |
