|
Name |
Accession |
Description |
Interval |
E-value |
| eukary_SO_Moco |
cd02111 |
molybdopterin binding domain of sulfite oxidase (SO). SO catalyzes the terminal reaction in ... |
128-486 |
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: 593.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508502 128 ALKVNSQRPFNAEPPPELLTENYITPNPIFFTRNHLPVPNLDPDTYRLHVVGaPGGQSLSLSLDDLH-NFPRYEITVTLQ 206
Cdd:cd02111 1 ALKVNSKKPFNAEPPSSLLASSFITPNELFYVRNHLPVPVVDPDTYSLEVEG-PDGTTLSLSLEDLKsLFPKHEVTATLQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508502 207 CAGNRRSEMTQVKEVKGLEWRTGAISTARWAGARLCDVLAQAGHQLC--ETEAHVCFEGLDSDPTGTAYGASIPLARAMD 284
Cdd:cd02111 80 CAGNRRSEMTKVKKVKGLQWGDGAISNAEWGGARLRDVLLDAGIPEDdsQGGLHVHFEGLDVDPTGTPYGASIPLSKALD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508502 285 PEAEVLLAYEMNGQPLPRDHGFPVRVVVPGVVGARHVKWLGRVSVQPEESYSHWQRRDYKGFSPSVDWETVDFDSAPSIQ 364
Cdd:cd02111 160 PEADVLLAYEMNGTPLPRDHGFPLRVVVPGVVGARSVKWLDRIVVSDEESDSHWQQNDYKGFSPSVDWDNVDFSKAPAIQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508502 365 ELPVQSAITEPRDGE---TVESGEVTIKGYAWSGGGRAVIRVDVSLDGGLTWQVAKLDGEEQR--PRKAWAWRLWQLKAP 439
Cdd:cd02111 240 EMPVQSAICSPSVGApvvTVPPGKITVKGYAWSGGGRKIVRVDVSLDGGRTWKVAELEQEENVwpSGRKWAWTLWEATVP 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 508502 440 VPAGqKELNIVCKAVDDGYNVQPDTVAPIWNLRGVLSNAWHRVHVYV 486
Cdd:cd02111 320 VPAG-KEAEIIAKAVDSAYNVQPETVEPIWNLRGVLNNAWHRVKVVV 365
|
|
| PLN00177 |
PLN00177 |
sulfite oxidase; Provisional |
111-486 |
1.82e-123 |
|
sulfite oxidase; Provisional
Pssm-ID: 177772 [Multi-domain] Cd Length: 393 Bit Score: 365.71 E-value: 1.82e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508502 111 PTVETSDPYADDPVRHPALKVNSQRPFNAEPPPELLTENYITPNPIFFTRNHLPVPNLDP-DTYRLHVVGAPGgQSLSLS 189
Cdd:PLN00177 2 PGLRGPSDYSQEPPRHPSLKINAKEPFNAEPPRSALVSSYITPVDLFYKRNHGPIPIVDDiERYSVTITGLIE-NPRKLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508502 190 LDDLHNFPRYEITVTLQCAGNRRSEMTQVKEVKGLEWRTGAISTARWAGARLCDVLAQAG-HQLCETEA----HVCFEGL 264
Cdd:PLN00177 81 MKDIRKLPKYNVTATLQCAGNRRTAMSKVRKVRGVGWDVSAIGNAVWGGAKLADVLELVGiPKLTSITSsggkHVEFVSV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508502 265 DSDP--TGTAYGASIPLARAMDPEAEVLLAYEMNGQPLPRDHGFPVRVVVPGVVGARHVKWLGRVSVQPEESYSHWQRRD 342
Cdd:PLN00177 161 DKCKeeNGGPYKASIPLSQATNPEADVLLAYEMNGEVLNRDHGYPLRVVVPGVIGARSVKWLDSINIIAEECQGFFMQKD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508502 343 YKGFSPSVDWETVDFDSAPSIQELPVQSAITEPRDGETVESGEVTIKGYAWSGGGRAVIRVDVSLDGGLTWQVAKLDGEE 422
Cdd:PLN00177 241 YKMFPPSVNWDNINWSTRRPQMDFPVQSAICSLEDVNAIKPGKVTVAGYALSGGGRGIERVDISVDGGKTWVEASRYQKP 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 508502 423 QRPRKA-------WAWRLWQLKAPVPAGQKelnIVCKAVDDGYNVQPDTVAPIWNLRGVLSNAWHRVHVYV 486
Cdd:PLN00177 321 GVPYISddissdkWAWVLFEATVDVPQSTE---IVAKAVDSAANVQPESVESIWNLRGILNTSWHRVQLRV 388
|
|
| Oxidored_molyb |
pfam00174 |
Oxidoreductase molybdopterin binding domain; This domain is found in a variety of ... |
162-338 |
2.08e-64 |
|
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: 205.81 E-value: 2.08e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508502 162 HLPVPNLDPDTYRLHVVGApGGQSLSLSLDDLHNFPRYEITVTLQCAGNRRSEMTQVKevkGLEWRTGAISTARWAGARL 241
Cdd:pfam00174 1 HGPVPEIDPDTWRLRVDGL-VEKPLTLTLDDLKAFPQVTVTATLQCVGNRRKEMNRVK---GVQWGGGAIGNAEWTGVPL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508502 242 CDVLAQAGhqLCETEAHVCFEGLDSDPTGtAYGASIPLARAMDPEaeVLLAYEMNGQPLPRDHGFPVRVVVPGVVGARHV 321
Cdd:pfam00174 77 RDLLERAG--VKPGAKHVLFEGADTLGDG-GYTTSLPLEKALDDD--VLLAYEMNGEPLPPDHGYPLRLVVPGWYGARSV 151
|
170
....*....|....*..
gi 508502 322 KWLGRVSVQPEESYSHW 338
Cdd:pfam00174 152 KWLRRIEVTDEESPGFW 168
|
|
| MsrP |
COG2041 |
Molybdopterin-dependent catalytic subunit of periplasmic DMSO/TMAO and ... |
157-348 |
5.32e-35 |
|
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: 129.12 E-value: 5.32e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508502 157 FFTRNHLPVPNLDPDTYRLHVVGApGGQSLSLSLDDLHNFPRYEITVTLQCAGNrrsemtqvkevkgleWRTGaisTARW 236
Cdd:COG2041 19 FPVRTAGGVPEIDPADWRLRVDGL-VEKPLTLTLDDLLALPLEERIYRLHCVEN---------------WSGG---VAPW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508502 237 AGARLCDVLAQAGHQlceTEA-HVCFEGLDSDptgtaYGASIPLARAMDPEAevLLAYEMNGQPLPRDHGFPVRvvvpgv 315
Cdd:COG2041 80 TGVPLRDLLERAGPK---PGAkYVLFESADPG-----YTESLPLDEALDPDT--LLAYGMNGEPLPPEHGAPLR------ 143
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 508502 316 vgAR--------HVKWLGRVSVQPEESYSHWQRRDYKGFSP 348
Cdd:COG2041 144 --LVvpglygfkSAKWLVRIEVTDEDPPGYWETRGYHFYAN 182
|
|
| Cyt-b5 |
pfam00173 |
Cytochrome b5-like Heme/Steroid binding domain; This family includes heme binding domains from ... |
29-103 |
3.74e-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: 78.82 E-value: 3.74e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 508502 29 TKEEVSSHTSPEtGIWVTLGSEVFDVTEFVDLHPGGPSKLMLAAGGPL-EPFWALyaVHNQSHVRELLAQYKIGEL 103
Cdd:pfam00173 1 TLEELSKHNGDG-DCWVAINGKVYDVTKFLKEHPGGEDVILSAAGKDAtDAFEAI--GHSEDAAEKLLKKYRIGEL 73
|
|
| PLN03199 |
PLN03199 |
delta6-acyl-lipid desaturase-like protein; Provisional |
23-118 |
2.93e-06 |
|
delta6-acyl-lipid desaturase-like protein; Provisional
Pssm-ID: 178740 [Multi-domain] Cd Length: 485 Bit Score: 49.65 E-value: 2.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508502 23 ESTHIYTKEEVSSHTSPETGiWVTLGSEVFDVTEFVDlHPGGPSKLMLAAGGPLEPFWALYAVHNQShvreLLAQYKIGE 102
Cdd:PLN03199 21 EKPQKISWQEVKKHASPDDA-WIIHQNKVYDVSNWHD-HPGGAVIFTHAGDDMTDIFAAFHAPGSQA----LMKKFYIGD 94
|
90
....*....|....*.
gi 508502 103 LNPEdkvapTVETSDP 118
Cdd:PLN03199 95 LIPE-----STEHKDP 105
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| eukary_SO_Moco |
cd02111 |
molybdopterin binding domain of sulfite oxidase (SO). SO catalyzes the terminal reaction in ... |
128-486 |
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: 593.60 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508502 128 ALKVNSQRPFNAEPPPELLTENYITPNPIFFTRNHLPVPNLDPDTYRLHVVGaPGGQSLSLSLDDLH-NFPRYEITVTLQ 206
Cdd:cd02111 1 ALKVNSKKPFNAEPPSSLLASSFITPNELFYVRNHLPVPVVDPDTYSLEVEG-PDGTTLSLSLEDLKsLFPKHEVTATLQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508502 207 CAGNRRSEMTQVKEVKGLEWRTGAISTARWAGARLCDVLAQAGHQLC--ETEAHVCFEGLDSDPTGTAYGASIPLARAMD 284
Cdd:cd02111 80 CAGNRRSEMTKVKKVKGLQWGDGAISNAEWGGARLRDVLLDAGIPEDdsQGGLHVHFEGLDVDPTGTPYGASIPLSKALD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508502 285 PEAEVLLAYEMNGQPLPRDHGFPVRVVVPGVVGARHVKWLGRVSVQPEESYSHWQRRDYKGFSPSVDWETVDFDSAPSIQ 364
Cdd:cd02111 160 PEADVLLAYEMNGTPLPRDHGFPLRVVVPGVVGARSVKWLDRIVVSDEESDSHWQQNDYKGFSPSVDWDNVDFSKAPAIQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508502 365 ELPVQSAITEPRDGE---TVESGEVTIKGYAWSGGGRAVIRVDVSLDGGLTWQVAKLDGEEQR--PRKAWAWRLWQLKAP 439
Cdd:cd02111 240 EMPVQSAICSPSVGApvvTVPPGKITVKGYAWSGGGRKIVRVDVSLDGGRTWKVAELEQEENVwpSGRKWAWTLWEATVP 319
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 508502 440 VPAGqKELNIVCKAVDDGYNVQPDTVAPIWNLRGVLSNAWHRVHVYV 486
Cdd:cd02111 320 VPAG-KEAEIIAKAVDSAYNVQPETVEPIWNLRGVLNNAWHRVKVVV 365
|
|
| PLN00177 |
PLN00177 |
sulfite oxidase; Provisional |
111-486 |
1.82e-123 |
|
sulfite oxidase; Provisional
Pssm-ID: 177772 [Multi-domain] Cd Length: 393 Bit Score: 365.71 E-value: 1.82e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508502 111 PTVETSDPYADDPVRHPALKVNSQRPFNAEPPPELLTENYITPNPIFFTRNHLPVPNLDP-DTYRLHVVGAPGgQSLSLS 189
Cdd:PLN00177 2 PGLRGPSDYSQEPPRHPSLKINAKEPFNAEPPRSALVSSYITPVDLFYKRNHGPIPIVDDiERYSVTITGLIE-NPRKLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508502 190 LDDLHNFPRYEITVTLQCAGNRRSEMTQVKEVKGLEWRTGAISTARWAGARLCDVLAQAG-HQLCETEA----HVCFEGL 264
Cdd:PLN00177 81 MKDIRKLPKYNVTATLQCAGNRRTAMSKVRKVRGVGWDVSAIGNAVWGGAKLADVLELVGiPKLTSITSsggkHVEFVSV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508502 265 DSDP--TGTAYGASIPLARAMDPEAEVLLAYEMNGQPLPRDHGFPVRVVVPGVVGARHVKWLGRVSVQPEESYSHWQRRD 342
Cdd:PLN00177 161 DKCKeeNGGPYKASIPLSQATNPEADVLLAYEMNGEVLNRDHGYPLRVVVPGVIGARSVKWLDSINIIAEECQGFFMQKD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508502 343 YKGFSPSVDWETVDFDSAPSIQELPVQSAITEPRDGETVESGEVTIKGYAWSGGGRAVIRVDVSLDGGLTWQVAKLDGEE 422
Cdd:PLN00177 241 YKMFPPSVNWDNINWSTRRPQMDFPVQSAICSLEDVNAIKPGKVTVAGYALSGGGRGIERVDISVDGGKTWVEASRYQKP 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 508502 423 QRPRKA-------WAWRLWQLKAPVPAGQKelnIVCKAVDDGYNVQPDTVAPIWNLRGVLSNAWHRVHVYV 486
Cdd:PLN00177 321 GVPYISddissdkWAWVLFEATVDVPQSTE---IVAKAVDSAANVQPESVESIWNLRGILNTSWHRVQLRV 388
|
|
| SO_family_Moco_dimer |
cd02110 |
Subgroup of sulfite oxidase (SO) family molybdopterin binding domains that contains conserved ... |
156-484 |
1.54e-111 |
|
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: 332.73 E-value: 1.54e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508502 156 IFFTRNHLPVPNLDPDTYRLHVVGApGGQSLSLSLDDLHNFPRYEITVTLQCAGNRRSEMTqvKEVKGLEWRTGAISTAR 235
Cdd:cd02110 1 LFFVRNHGGVPDIDPDAWRLEIHGL-VERPLTLTLDDLKRLPSVEVVATLECSGNGRGGFI--PVRSGAQWGHGAVGNAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508502 236 WAGARLCDVLAQAGHQlcETEAHVCFEGLDSDPTGTA--YGASIPLARAMDPEaeVLLAYEMNGQPLPRDHGFPVRVVVP 313
Cdd:cd02110 78 WTGVPLKDLLEEAGVK--PGAKHVLFEGADVPPGEKAadYTRSVPLSKALDDD--ALLAYEMNGEPLPPDHGYPLRLVVP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508502 314 GVVGARHVKWLGRVSVQPEESYSHWQRRDYKGFSPSVDWetVDFDSAPSIQELPVQSAITEPRDGETVESGEVTIKGYAW 393
Cdd:cd02110 154 GWYGARSVKWLRRIEVTDQPSDGYWQTRDYTVPPPDVDA--VGGKARRPIGEMPVKSVITSPSPGAELVSGGRVEIGGVA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508502 394 SGGGRAVIRVDVSLDGGLTWQVAKLDGEEQRPrkaWAWRLWQLKAPVPAGqkELNIVCKAVDDGYNVQPDTVAPIWNLRG 473
Cdd:cd02110 232 WSGGRGIRRVEVSLDGGRTWQEARLEGPLAGP---RAWRQWELDWDLPPG--EYELVARATDSTGNVQPERAEWNWNPGG 306
|
330
....*....|.
gi 508502 474 VLSNAWHRVHV 484
Cdd:cd02110 307 YGNNHWHRVQV 317
|
|
| PLN02252 |
PLN02252 |
nitrate reductase [NADPH] |
120-486 |
3.19e-97 |
|
nitrate reductase [NADPH]
Pssm-ID: 215141 [Multi-domain] Cd Length: 888 Bit Score: 312.38 E-value: 3.19e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508502 120 ADDPV-RHPAL-KVNSQRPFNAEPP-PELLTENYITPNPIFFTRNHLPVPNLDPDTYRLHVVGAPGgQSLSLSLDDLHNF 196
Cdd:PLN02252 78 PDEWIpRHPSLvRLTGKHPFNCEPPlARLMEHGFITPAPLHYVRNHGAVPRADWDEWTVEVTGLVK-RPARLTMDELVRF 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508502 197 PRYEITVTLQCAGNRRSEMTQVKEVKGLEWRTGAISTARWAGARLCDVLAQAGHQLCETEA-HVCFEGLDSDPTG--TAY 273
Cdd:PLN02252 157 PARELPVTLVCAGNRRKEQNMVKQTIGFNWGAAGVSTSVWRGVRLRDVLRRCGVMSRKGGAlNVCFEGAEDLPGGggSKY 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508502 274 GASIPLARAMDPEAEVLLAYEMNGQPLPRDHGFPVRVVVPGVVGARHVKWLGRVSVQPEESYSHWQRRDYKGFSPSVDWE 353
Cdd:PLN02252 237 GTSITLERAMDPARDVILAYMQNGEPLTPDHGFPVRLIIPGFIGGRMVKWLKRIIVTTAESDNYYHYRDNRVLPSHVDAE 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508502 354 TVDFDS---APS--IQELPVQSAITEPRDGETVESGEVTI------KGYAWSGGGRAVIRVDVSLDGGLTWQVAKLDGEE 422
Cdd:PLN02252 317 LANAEGwwyKPEyiINELNINSVITTPAHDEILPINASTTqrpytmKGYAYSGGGRKVTRVEVSLDGGETWRLCDLDHPE 396
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 508502 423 QRPR--KAWAWRLWQLKAPVP--AGQKElnIVCKAVDDGYNVQPDTvaPIWNLRGVLSNAWHRVHVYV 486
Cdd:PLN02252 397 KPTKygKYWCWCFWSLDVEVLdlLGAKE--IAVRAWDESMNTQPEK--LIWNLMGMMNNCWFRVKVNV 460
|
|
| eukary_NR_Moco |
cd02112 |
molybdopterin binding domain of eukaryotic nitrate reductase (NR). Assimilatory NRs catalyze ... |
125-484 |
5.39e-97 |
|
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: 297.76 E-value: 5.39e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508502 125 RHPAL-KVNSQRPFNAEPPP-ELLTENYITPNPIFFTRNHLPVPNLDPDTYRLHVVG---APggqsLSLSLDDLHN-FPR 198
Cdd:cd02112 11 RDPRLiRLTGKHPFNSEPPLtELMDHGFITPSNLHYVRNHGPVPREKWEDWTVEVTGlveKP----TTLTMDELVAmFPS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508502 199 YEITVTLQCAGNRRSEMTQVKEVKGLEWRTGAISTARWAGARLCDVLAQAGHQLCETEA-HVCFEGLDSDPTG--TAYGA 275
Cdd:cd02112 87 VTFPVTLVCAGNRRKEQNMVKKTIGFNWGAAGTSTSLWTGVRLSDLLDRCGPKSPKGGArHVCFEGADDLLPGpnGKYGT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508502 276 SIPLARAMDPEAEVLLAYEMNGQPLPRDHGFPVRVVVPGVVGARHVKWLGRVSVQPEESYSHWQRRDYKGFSPSVDWETV 355
Cdd:cd02112 167 SITLSWAMDPSKDVMLAYKQNGELLHPDHGFPVRLIIPGQIGGRMVKWLKRIVVSDRESQNHYHFHDNRVLPSHVDAELA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508502 356 D-----FDSAPSIQELPVQSAITEPRDGETVE------SGEVTIKGYAWSGGGRAVIRVDVSLDGGLTWQVAKLDGEEQR 424
Cdd:cd02112 247 NeegwwYKPEYIINDLNVNSAITTPAHDEVLPlnglttAETYTMKGYAYAGGGRRVTRVEVSLDDGKSWKLASIDYPEDP 326
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 508502 425 PR--KAWAWRLWQLKAPVPAGQKELNIVCKAVDDGYNVQPDTvaPIWNLRGVLSNAWHRVHV 484
Cdd:cd02112 327 TKygKCWCWCFWSLDVPLSELLAAKEICVRAWDESMNTQPRD--MTWNVMGMMNNCWFRVKI 386
|
|
| Oxidored_molyb |
pfam00174 |
Oxidoreductase molybdopterin binding domain; This domain is found in a variety of ... |
162-338 |
2.08e-64 |
|
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: 205.81 E-value: 2.08e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508502 162 HLPVPNLDPDTYRLHVVGApGGQSLSLSLDDLHNFPRYEITVTLQCAGNRRSEMTQVKevkGLEWRTGAISTARWAGARL 241
Cdd:pfam00174 1 HGPVPEIDPDTWRLRVDGL-VEKPLTLTLDDLKAFPQVTVTATLQCVGNRRKEMNRVK---GVQWGGGAIGNAEWTGVPL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508502 242 CDVLAQAGhqLCETEAHVCFEGLDSDPTGtAYGASIPLARAMDPEaeVLLAYEMNGQPLPRDHGFPVRVVVPGVVGARHV 321
Cdd:pfam00174 77 RDLLERAG--VKPGAKHVLFEGADTLGDG-GYTTSLPLEKALDDD--VLLAYEMNGEPLPPDHGYPLRLVVPGWYGARSV 151
|
170
....*....|....*..
gi 508502 322 KWLGRVSVQPEESYSHW 338
Cdd:pfam00174 152 KWLRRIEVTDEESPGFW 168
|
|
| Mo-co_dimer |
pfam03404 |
Mo-co oxidoreductase dimerization domain; This domain is found in molybdopterin cofactor ... |
361-487 |
2.22e-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: 189.11 E-value: 2.22e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508502 361 PSIQELPVQSAITEPRDGETVES----GEVTIKGYAWSGGGRAVIRVDVSLDGGLTWQVAKLDGEEQRPR------KAWA 430
Cdd:pfam03404 2 YAIYDLNVNSAICSPEHDEVVKLgaaqGTYTIKGYAYSGGGRRITRVEVSLDGGKTWRLAEIDYEEDPYRygewreKCWC 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 508502 431 WRLWQLKAPVPAGQKELNIVCKAVDDGYNVQPDTvaPIWNLRGVLSNAWHRVHVYVS 487
Cdd:pfam03404 82 WCFWSLDIPVSDLLKAKEILVRAVDEAMNVQPED--MYWNVRGMMNNPWHRVKIHVE 136
|
|
| SO_family_Moco |
cd00321 |
Sulfite oxidase (SO) family, molybdopterin binding domain. This molybdopterin cofactor (Moco) ... |
158-332 |
1.37e-48 |
|
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: 164.28 E-value: 1.37e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508502 158 FTRNHLPVP-NLDPDTYRLHVVGApGGQSLSLSLDDLHNFPRYEITVTLQCAGNRrsemtqvkevkgleWRTGAISTARW 236
Cdd:cd00321 1 FVRNHGGVPpEIDPDDWRLEVDGL-VEKPLSLTLDDLKALPQVEVIATLHCVGNR--------------WGGGAVSNAEW 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508502 237 AGARLCDVLAQAGHQlcETEAHVCFEGLDsDPTGTAYGASIPLARAMDPEaeVLLAYEMNGQPLPRDHGFPVRVVVPGVV 316
Cdd:cd00321 66 TGVPLRDLLEEAGPK--PGARYVVFEGAD-DPGGDGYTTSLPLEKALDPD--VLLAYEMNGEPLPPDHGFPLRLVVPGLY 140
|
170
....*....|....*.
gi 508502 317 GARHVKWLGRVSVQPE 332
Cdd:cd00321 141 GWKSVKWLRRIEVTDE 156
|
|
| bact_SorA_Moco |
cd02114 |
sulfite:cytochrome c oxidoreductase subunit A (SorA), molybdopterin binding domain. SorA is ... |
123-484 |
2.51e-48 |
|
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: 170.39 E-value: 2.51e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508502 123 PVRHPALKVNSqRPFNAEPPPELLTENYITPNPIFFTRNHLP-VP-NLDPDTYRLHVVGAPGgQSLSLSLDDLHNF-PRY 199
Cdd:cd02114 14 PQKRPLIRLTT-RPPHLETPFSVFNEGLITPNDAFFVRYHLAgIPlDIDPDAYTLTIDGKVR-TPLTLSLAELKRIePRF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508502 200 EITVTLQCAGNRRSEMTqvKEVKGLEWRTGAISTARWAGARLCDVLAQAGHQLCETEahVCFEGLDSDP--TGTAYGASI 277
Cdd:cd02114 92 EVVAVNQCSGNSRGFFQ--PRVQGAQLANGAMGNARWAGVPLKAVLAKAGVQDGARQ--VAFRGLDQPVldVTPDFVKSL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508502 278 PLARAMDPEaeVLLAYEMNGQPLPRDHGFPVRVVVPGVVGARHVKWLGRVSVQPEESYSHWQRRDYKgfSPSVDWETVDF 357
Cdd:cd02114 168 DIDHALDGE--VMLAWEMNGEPLPVLNGYPLRLVVPGFYATYWVKHLSHITVLDKEFDGFWASQAYR--IPDNADAGVEP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508502 358 DSAPS----IQELPVQSAITEPRDGETVES-GEVTIKGYAWSgGGRAVIRVDVSLDGGLTWQVAKLDGEEQRprkaWAWR 432
Cdd:cd02114 244 GTAPDrtapINRFKVRSFITSLENGAIVAPaGELALRGIAFD-GGSGIRRVDVSADGGDSWTQATLGPDLGR----FSFR 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 508502 433 LWQLKAPVPAgQKELNIVCKAVDDGYNVQPDTVApiWNLRGVLSNAWHRVHV 484
Cdd:cd02114 319 GWKLTLDGVK-KGPLTLMVRATNNDGQTQPLRAP--WNPGGYMRNVVERTRI 367
|
|
| bact_SoxC_Moco |
cd02113 |
bacterial SoxC is a member of the sulfite oxidase (SO) family of molybdopterin binding domains. ... |
151-476 |
1.06e-38 |
|
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: 143.31 E-value: 1.06e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508502 151 ITPNPIFFTRNHLPVPNLDPDTYRLHVVGAPGgQSLSLSLDDLHNFPRYEITVTLQCAGNRRSEMTQVKeVKGLEWRTGA 230
Cdd:cd02113 9 ITPNGLHFERHHGGVPDIDPAQHRLMIHGMVK-KPLVFTMDDLKRFPSVSRIYFLECSGNGGTGWRGAP-LPTAQYTHGM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508502 231 ISTARWAGARLCDVLAQAGhqLCETEAHVCFEGLDsdptGTAYGASIPLARAMDpeaEVLLAYEMNGQPLPRDHGFPVRV 310
Cdd:cd02113 87 LSCSEWTGVPLSTLLEEAG--VKPGAKWLLAEGAD----AAAMTRSIPLEKALD---DALVAYAQNGEALRPENGYPLRL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508502 311 VVPGVVGARHVKWLGRVSV--QPeesyshWQRRD----YKGFSPSVDWETVDFDSAPsiqelpvQSAITEPRDGETV-ES 383
Cdd:cd02113 158 VVPGWEGNTNVKWLRRIEVgdQP------WMTREetskYTDLLPDGRARQFSFVMEA-------KSVITSPSGGQRLrEP 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508502 384 GEVTIKGYAWSGGGRaVIRVDVSLDGGLTWQVAKLDGEEQ-----RPRKAWAWrlwqlkapvpaGQKELNIVCKAVDDGY 458
Cdd:cd02113 225 GFHEISGLAWSGRGR-IRRVDVSFDGGRTWQDARLEGPVLpkaltRFRLPWKW-----------DGRPAVLQSRATDETG 292
|
330
....*....|....*...
gi 508502 459 NVQPdTVAPIWNLRGVLS 476
Cdd:cd02113 293 YVQP-TRAELRAVRGTNS 309
|
|
| MsrP |
COG2041 |
Molybdopterin-dependent catalytic subunit of periplasmic DMSO/TMAO and ... |
157-348 |
5.32e-35 |
|
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: 129.12 E-value: 5.32e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508502 157 FFTRNHLPVPNLDPDTYRLHVVGApGGQSLSLSLDDLHNFPRYEITVTLQCAGNrrsemtqvkevkgleWRTGaisTARW 236
Cdd:COG2041 19 FPVRTAGGVPEIDPADWRLRVDGL-VEKPLTLTLDDLLALPLEERIYRLHCVEN---------------WSGG---VAPW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508502 237 AGARLCDVLAQAGHQlceTEA-HVCFEGLDSDptgtaYGASIPLARAMDPEAevLLAYEMNGQPLPRDHGFPVRvvvpgv 315
Cdd:COG2041 80 TGVPLRDLLERAGPK---PGAkYVLFESADPG-----YTESLPLDEALDPDT--LLAYGMNGEPLPPEHGAPLR------ 143
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 508502 316 vgAR--------HVKWLGRVSVQPEESYSHWQRRDYKGFSP 348
Cdd:COG2041 144 --LVvpglygfkSAKWLVRIEVTDEDPPGYWETRGYHFYAN 182
|
|
| Cyt-b5 |
pfam00173 |
Cytochrome b5-like Heme/Steroid binding domain; This family includes heme binding domains from ... |
29-103 |
3.74e-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: 78.82 E-value: 3.74e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 508502 29 TKEEVSSHTSPEtGIWVTLGSEVFDVTEFVDLHPGGPSKLMLAAGGPL-EPFWALyaVHNQSHVRELLAQYKIGEL 103
Cdd:pfam00173 1 TLEELSKHNGDG-DCWVAINGKVYDVTKFLKEHPGGEDVILSAAGKDAtDAFEAI--GHSEDAAEKLLKKYRIGEL 73
|
|
| arch_bact_SO_family_Moco |
cd02109 |
bacterial and archael members of the sulfite oxidase (SO) family of molybdopterin binding ... |
163-343 |
1.90e-16 |
|
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: 77.28 E-value: 1.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508502 163 LPVPNLDPDTYRLHVVGAPGGQsLSLSLDDLHNFPRYEITVTLQCagnrrsemtqvkeVKGleWrtgAISTARWAGARLC 242
Cdd:cd02109 17 GDVPEVDLEKWRLRVTGLVENP-LSLTYEDLLALPQTEYTADFHC-------------VTG--W---SKLDVVWEGVSLK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508502 243 DVLAQAGhqLCETEAHVCFEGLDsdptgtAYGASIPLARAMDPEAevLLAYEMNGQPLPRDHGFPVRVVVPGVVGARHVK 322
Cdd:cd02109 78 DLLEAAR--PDPEATFVMAHSYD------GYTTNLPLEDLLREDS--LLATKMDGEPLPPEHGGPARLVVPHLYFWKSAK 147
|
170 180
....*....|....*....|.
gi 508502 323 WLGRVSVQPEESYSHWQRRDY 343
Cdd:cd02109 148 WLRGIEFLDEDEPGFWERRGY 168
|
|
| bact_SO_family_Moco |
cd02108 |
bacterial subgroup of the sulfite oxidase (SO) family of molybdopterin binding domains. This ... |
158-306 |
4.80e-14 |
|
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: 70.49 E-value: 4.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508502 158 FTRNHLPVPNL---------DPDTYRLHVvgapGG---QSLSLSLDDLHNFPRyeitvtlqcagnrRSEMTQVKEVKGle 225
Cdd:cd02108 5 FRRNGIRKPEAlaykaleanDFADYRLEV----GGlveHPLSLSLEELRALPQ-------------RTQITRHICVEG-- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508502 226 WrtGAIstARWAGARLCDVLAQAGhqlCETEA-HVCFEGLDSDPTGTAYGASIPLARAMDPEAevLLAYEMNGQPLPRDH 304
Cdd:cd02108 66 W--SAI--GKWGGVPLRTILELVG---PLPEAkYVVFKCADDFAGGDRYYESIDMASALHPQT--LLAYEMNGQPLPIKN 136
|
..
gi 508502 305 GF 306
Cdd:cd02108 137 GA 138
|
|
| PLN02252 |
PLN02252 |
nitrate reductase [NADPH] |
20-189 |
1.72e-11 |
|
nitrate reductase [NADPH]
Pssm-ID: 215141 [Multi-domain] Cd Length: 888 Bit Score: 66.62 E-value: 1.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508502 20 AAQESTHIYTKEEVSSHTSPETgIWVTLGSEVFDVTEFVDLHPGGPSKLMLAAGGP-LEPFwalYAVHNqSHVRELLAQY 98
Cdd:PLN02252 512 NTNTGSKQYTMSEVRKHNSEDS-CWIVVHGHVYDCTRFLKDHPGGADSILINAGTDcTEEF---DAIHS-DKAKKMLEDY 586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508502 99 KIGELnpedkvaptVETSDPYADDPVRHPALKVNSQRPFNAEPPPellTENYITPNPifftRNHLPVP-----NLDPDTY 173
Cdd:PLN02252 587 RIGEL---------VTTGAAASSSASSHPLSAISTASALAAASPA---PGRPVALNP----REKIPCRlvekiSLSHDVR 650
|
170 180
....*....|....*....|....
gi 508502 174 RL--------HVVGAPGGQSLSLS 189
Cdd:PLN02252 651 LFrfalpsedHVLGLPVGKHVFLC 674
|
|
| PLN03199 |
PLN03199 |
delta6-acyl-lipid desaturase-like protein; Provisional |
23-118 |
2.93e-06 |
|
delta6-acyl-lipid desaturase-like protein; Provisional
Pssm-ID: 178740 [Multi-domain] Cd Length: 485 Bit Score: 49.65 E-value: 2.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508502 23 ESTHIYTKEEVSSHTSPETGiWVTLGSEVFDVTEFVDlHPGGPSKLMLAAGGPLEPFWALYAVHNQShvreLLAQYKIGE 102
Cdd:PLN03199 21 EKPQKISWQEVKKHASPDDA-WIIHQNKVYDVSNWHD-HPGGAVIFTHAGDDMTDIFAAFHAPGSQA----LMKKFYIGD 94
|
90
....*....|....*.
gi 508502 103 LNPEdkvapTVETSDP 118
Cdd:PLN03199 95 LIPE-----STEHKDP 105
|
|
| COG3915 |
COG3915 |
Uncharacterized conserved protein [Function unknown]; |
163-305 |
3.00e-05 |
|
Uncharacterized conserved protein [Function unknown];
Pssm-ID: 443120 Cd Length: 167 Bit Score: 44.49 E-value: 3.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508502 163 LPVPNLDPDtyrLHVVGAPG----GQSLSLSLDDLHNFPRYEITVTLqcagnrrsemtqvkevkglEWRTGAIstaRWAG 238
Cdd:COG3915 24 LPAPAGPVI---LTVSGKIGntnaGGAATFDLAMLEALPQTEITTTT-------------------PWTDGVQ---TFRG 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 508502 239 ARLCDVLAQAGhqlcETEAHVCFEGLDsdptgtAYGASIPLARAMdpEAEVLLAYEMNGQPLP-RDHG 305
Cdd:COG3915 79 VLLRDLLAAVG----AKGTTLRAVALN------DYAVEIPISDLE--EYGVILAYRMDGKPMSvRDKG 134
|
|
| PLN03198 |
PLN03198 |
delta6-acyl-lipid desaturase; Provisional |
17-121 |
7.20e-05 |
|
delta6-acyl-lipid desaturase; Provisional
Pssm-ID: 178739 [Multi-domain] Cd Length: 526 Bit Score: 45.45 E-value: 7.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 508502 17 RCRAAQE-STHIYTKEEVSSHTSPeTGIWVTLGSEVFDVTEFVDLHPGGPSKLMLAAGGPLEPFWALYAvhnqSHVRELL 95
Cdd:PLN03198 94 RRRSSKEkKSKSHLLSEVAAHNKP-NDCWIVIKNKVYDVSDFAAEHPGGSVISTYFGRDGTDAFSSFHA----ASTWKIL 168
|
90 100
....*....|....*....|....*.
gi 508502 96 AQYKIGELnpeDKVAPTVETSDPYAD 121
Cdd:PLN03198 169 QDFYIGDV---DNVEPTPELLKDFRD 191
|
|
| |
