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Conserved domains on  [gi|1972312038|ref|NP_001379385|]
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sulfite oxidase [Caenorhabditis elegans]

Protein Classification

Cyt-b5 and eukary_SO_Moco domain-containing protein( domain architecture ID 10445751)

Cyt-b5 and eukary_SO_Moco domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
eukary_SO_Moco cd02111
molybdopterin binding domain of sulfite oxidase (SO). SO catalyzes the terminal reaction in ...
 171-493 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: 520.03  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972312038 171 NIKTENHRLTVETIKGKTVDLSVEELKKKYKSYTIGSVIQCAGNRRADMNQYKKVQGLMWEGTAISNAEWTGVRLRDLLA 250
Cdd:cd02111    40 VVDPDTYSLEVEGPDGTTLSLSLEDLKSLFPKHEVTATLQCAGNRRSEMTKVKKVKGLQWGDGAISNAEWGGARLRDVLL 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972312038 251 DAGIDVFD-DKIKHVHFEGADVDPTGTPYGASIPIEKARG--DEVIVAYHMNGVDIPRDHGAPLRVIVPGNVGARQVKWL 327
Cdd:cd02111   120 DAGIPEDDsQGGLHVHFEGLDVDPTGTPYGASIPLSKALDpeADVLLAYEMNGTPLPRDHGFPLRVVVPGVVGARSVKWL 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972312038 328 RKIIVSEKESDSHWQQKDYRAFSPaVNIGDELKWNTVPSIQEYPVQCAICSPAPNTKV-DRGDETVDISGYAWSGGGRGI 406
Cdd:cd02111   200 DRIVVSDEESDSHWQQNDYKGFSP-SVDWDNVDFSKAPAIQEMPVQSAICSPSVGAPVvTVPPGKITVKGYAWSGGGRKI 278

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972312038 407 IRIEVSVDGGETWNSVEMEQEEKQD-QEHMYAWTLFKAEVKIPPGvKEFNIIAKAVDRAYNTQPETASGIWNVRGLIHNA 485
Cdd:cd02111   279 VRVDVSLDGGRTWKVAELEQEENVWpSGRKWAWTLWEATVPVPAG-KEAEIIAKAVDSAYNVQPETVEPIWNLRGVLNNA 357


                  ....*...
gi 1972312038 486 WHRVPIIV 493
Cdd:cd02111   358 WHRVKVVV 365
Cyt-b5 pfam00173
Cytochrome b5-like Heme/Steroid binding domain; This family includes heme binding domains from ...
 85-157 1.78e-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: 79.59  E-value: 1.78e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1972312038  85 EEVKKHGKDaDRIWVTYKDGVYDVTDFIAMHPGG-DKILLAAGA-AVDPFWALysQHKTKEVLEILEGYRIGKLD 157
Cdd:pfam00173   3 EELSKHNGD-GDCWVAINGKVYDVTKFLKEHPGGeDVILSAAGKdATDAFEAI--GHSEDAAEKLLKKYRIGELA 74
 
Name Accession Description Interval E-value
eukary_SO_Moco cd02111
molybdopterin binding domain of sulfite oxidase (SO). SO catalyzes the terminal reaction in ...
 171-493 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: 520.03  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972312038 171 NIKTENHRLTVETIKGKTVDLSVEELKKKYKSYTIGSVIQCAGNRRADMNQYKKVQGLMWEGTAISNAEWTGVRLRDLLA 250
Cdd:cd02111    40 VVDPDTYSLEVEGPDGTTLSLSLEDLKSLFPKHEVTATLQCAGNRRSEMTKVKKVKGLQWGDGAISNAEWGGARLRDVLL 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972312038 251 DAGIDVFD-DKIKHVHFEGADVDPTGTPYGASIPIEKARG--DEVIVAYHMNGVDIPRDHGAPLRVIVPGNVGARQVKWL 327
Cdd:cd02111   120 DAGIPEDDsQGGLHVHFEGLDVDPTGTPYGASIPLSKALDpeADVLLAYEMNGTPLPRDHGFPLRVVVPGVVGARSVKWL 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972312038 328 RKIIVSEKESDSHWQQKDYRAFSPaVNIGDELKWNTVPSIQEYPVQCAICSPAPNTKV-DRGDETVDISGYAWSGGGRGI 406
Cdd:cd02111   200 DRIVVSDEESDSHWQQNDYKGFSP-SVDWDNVDFSKAPAIQEMPVQSAICSPSVGAPVvTVPPGKITVKGYAWSGGGRKI 278

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972312038 407 IRIEVSVDGGETWNSVEMEQEEKQD-QEHMYAWTLFKAEVKIPPGvKEFNIIAKAVDRAYNTQPETASGIWNVRGLIHNA 485
Cdd:cd02111   279 VRVDVSLDGGRTWKVAELEQEENVWpSGRKWAWTLWEATVPVPAG-KEAEIIAKAVDSAYNVQPETVEPIWNLRGVLNNA 357


                  ....*...
gi 1972312038 486 WHRVPIIV 493
Cdd:cd02111   358 WHRVKVVV 365
PLN00177 PLN00177
sulfite oxidase; Provisional
 175-493 2.19e-92

sulfite oxidase; Provisional


Pssm-ID: 177772 [Multi-domain]  Cd Length: 393  Bit Score: 286.36  E-value: 2.19e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972312038 175 ENHRLTVETIKGKTVDLSVEELKKKYKsYTIGSVIQCAGNRRADMNQYKKVQGLMWEGTAISNAEWTGVRLRDLLADAGI 254
Cdd:PLN00177   63 ERYSVTITGLIENPRKLSMKDIRKLPK-YNVTATLQCAGNRRTAMSKVRKVRGVGWDVSAIGNAVWGGAKLADVLELVGI 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972312038 255 DVFDDKI----KHVHFEGADVDP--TGTPYGASIPIEKARGDE--VIVAYHMNGVDIPRDHGAPLRVIVPGNVGARQVKW 326
Cdd:PLN00177  142 PKLTSITssggKHVEFVSVDKCKeeNGGPYKASIPLSQATNPEadVLLAYEMNGEVLNRDHGYPLRVVVPGVIGARSVKW 221

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972312038 327 LRKIIVSEKESDSHWQQKDYRAFSPAVNiGDELKWNTVPSIQEYPVQCAICSPAPNTKVDRGDetVDISGYAWSGGGRGI 406
Cdd:PLN00177  222 LDSINIIAEECQGFFMQKDYKMFPPSVN-WDNINWSTRRPQMDFPVQSAICSLEDVNAIKPGK--VTVAGYALSGGGRGI 298

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972312038 407 IRIEVSVDGGETWnsVEMEQEEKQDQEHM--------YAWTLFKAEVKIPPGVKefnIIAKAVDRAYNTQPETASGIWNV 478
Cdd:PLN00177  299 ERVDISVDGGKTW--VEASRYQKPGVPYIsddissdkWAWVLFEATVDVPQSTE---IVAKAVDSAANVQPESVESIWNL 373

                         330
                  ....*....|....*
gi 1972312038 479 RGLIHNAWHRVPIIV 493
Cdd:PLN00177  374 RGILNTSWHRVQLRV 388
Oxidored_molyb pfam00174
Oxidoreductase molybdopterin binding domain; This domain is found in a variety of ...
 160-341 3.36e-75

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: 233.93  E-value: 3.36e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972312038 160 DVPKIDfedlsnikTENHRLTVETIKGKTVDLSVEELKKkYKSYTIGSVIQCAGNRRADMNQykkVQGLMWEGTAISNAE 239
Cdd:pfam00174   3 PVPEID--------PDTWRLRVDGLVEKPLTLTLDDLKA-FPQVTVTATLQCVGNRRKEMNR---VKGVQWGGGAIGNAE 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972312038 240 WTGVRLRDLLADAGIDvfdDKIKHVHFEGADVDPTGtPYGASIPIEKARGDEVIVAYHMNGVDIPRDHGAPLRVIVPGNV 319
Cdd:pfam00174  71 WTGVPLRDLLERAGVK---PGAKHVLFEGADTLGDG-GYTTSLPLEKALDDDVLLAYEMNGEPLPPDHGYPLRLVVPGWY 146

                         170       180
                  ....*....|....*....|..
gi 1972312038 320 GARQVKWLRKIIVSEKESDSHW 341
Cdd:pfam00174 147 GARSVKWLRRIEVTDEESPGFW 168
MsrP COG2041
Molybdopterin-dependent catalytic subunit of periplasmic DMSO/TMAO and ...
 150-351 1.67e-45

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: 157.24  E-value: 1.67e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972312038 150 GYRIGklDVKDVPKIDFEDlsniktenHRLTVETIKGKTVDLSVEELKKkYKSYTIGSVIQCAGNRRAdmnqykkvqglm 229
Cdd:COG2041    18 AFPVR--TAGGVPEIDPAD--------WRLRVDGLVEKPLTLTLDDLLA-LPLEERIYRLHCVENWSG------------ 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972312038 230 wegtaiSNAEWTGVRLRDLLADAGIDvfdDKIKHVHFEGADvdptgTPYGASIPIEKARGDEVIVAYHMNGVDIPRDHGA 309
Cdd:COG2041    75 ------GVAPWTGVPLRDLLERAGPK---PGAKYVLFESAD-----PGYTESLPLDEALDPDTLLAYGMNGEPLPPEHGA 140

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1972312038 310 PLRVIVPGNVGARQVKWLRKIIVSEKESDSHWQQKDYRAFSP 351
Cdd:COG2041   141 PLRLVVPGLYGFKSAKWLVRIEVTDEDPPGYWETRGYHFYAN 182
Cyt-b5 pfam00173
Cytochrome b5-like Heme/Steroid binding domain; This family includes heme binding domains from ...
 85-157 1.78e-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: 79.59  E-value: 1.78e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1972312038  85 EEVKKHGKDaDRIWVTYKDGVYDVTDFIAMHPGG-DKILLAAGA-AVDPFWALysQHKTKEVLEILEGYRIGKLD 157
Cdd:pfam00173   3 EELSKHNGD-GDCWVAINGKVYDVTKFLKEHPGGeDVILSAAGKdATDAFEAI--GHSEDAAEKLLKKYRIGELA 74
PLN02252 PLN02252
nitrate reductase [NADPH]
 77-174 9.07e-13

nitrate reductase [NADPH]


Pssm-ID: 215141 [Multi-domain]  Cd Length: 888  Bit Score: 70.86  E-value: 9.07e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972312038  77 ENLQIYKQEEVKKHGKdADRIWVTYKDGVYDVTDFIAMHPGG-DKILLAAGA-AVDPFWALYSQHKTKevleILEGYRIG 154
Cdd:PLN02252  515 TGSKQYTMSEVRKHNS-EDSCWIVVHGHVYDCTRFLKDHPGGaDSILINAGTdCTEEFDAIHSDKAKK----MLEDYRIG 589

                          90       100
                  ....*....|....*....|...
gi 1972312038 155 KLDVKDV---PKIDFEDLSNIKT 174
Cdd:PLN02252  590 ELVTTGAaasSSASSHPLSAIST 612
CYB5 COG5274
Cytochrome b involved in lipid metabolism [Energy production and conversion, Lipid transport ...
 82-156 5.47e-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: 5.47e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972312038  82 YKQEEVKKHgKDADRIWVTYKDGVYDVTDFIAMHPGGDKILLA-----AGAAVDpfwalySQHKTKE-VLEILEGYRIGK 155
Cdd:COG5274    18 YTLAEVATH-NTLSDCWMAIDGNVYDLTEYIPKHPGGEAVILRwcgkdATEAFN------TKHPHSPkAERLLESYRIGR 90


                  .
gi 1972312038 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 ...
 171-493 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: 520.03  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972312038 171 NIKTENHRLTVETIKGKTVDLSVEELKKKYKSYTIGSVIQCAGNRRADMNQYKKVQGLMWEGTAISNAEWTGVRLRDLLA 250
Cdd:cd02111    40 VVDPDTYSLEVEGPDGTTLSLSLEDLKSLFPKHEVTATLQCAGNRRSEMTKVKKVKGLQWGDGAISNAEWGGARLRDVLL 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972312038 251 DAGIDVFD-DKIKHVHFEGADVDPTGTPYGASIPIEKARG--DEVIVAYHMNGVDIPRDHGAPLRVIVPGNVGARQVKWL 327
Cdd:cd02111   120 DAGIPEDDsQGGLHVHFEGLDVDPTGTPYGASIPLSKALDpeADVLLAYEMNGTPLPRDHGFPLRVVVPGVVGARSVKWL 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972312038 328 RKIIVSEKESDSHWQQKDYRAFSPaVNIGDELKWNTVPSIQEYPVQCAICSPAPNTKV-DRGDETVDISGYAWSGGGRGI 406
Cdd:cd02111   200 DRIVVSDEESDSHWQQNDYKGFSP-SVDWDNVDFSKAPAIQEMPVQSAICSPSVGAPVvTVPPGKITVKGYAWSGGGRKI 278

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972312038 407 IRIEVSVDGGETWNSVEMEQEEKQD-QEHMYAWTLFKAEVKIPPGvKEFNIIAKAVDRAYNTQPETASGIWNVRGLIHNA 485
Cdd:cd02111   279 VRVDVSLDGGRTWKVAELEQEENVWpSGRKWAWTLWEATVPVPAG-KEAEIIAKAVDSAYNVQPETVEPIWNLRGVLNNA 357


                  ....*...
gi 1972312038 486 WHRVPIIV 493
Cdd:cd02111   358 WHRVKVVV 365
SO_family_Moco_dimer cd02110
Subgroup of sulfite oxidase (SO) family molybdopterin binding domains that contains conserved ...
 172-489 4.48e-101

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: 306.15  E-value: 4.48e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972312038 172 IKTENHRLTVETIKGKTVDLSVEELKKkYKSYTIGSVIQCAGNRRADMNqyKKVQGLMWEGTAISNAEWTGVRLRDLLAD 251
Cdd:cd02110    13 IDPDAWRLEIHGLVERPLTLTLDDLKR-LPSVEVVATLECSGNGRGGFI--PVRSGAQWGHGAVGNARWTGVPLKDLLEE 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972312038 252 AGIDvfdDKIKHVHFEGADVDPTGT--PYGASIPIEKARGDEVIVAYHMNGVDIPRDHGAPLRVIVPGNVGARQVKWLRK 329
Cdd:cd02110    90 AGVK---PGAKHVLFEGADVPPGEKaaDYTRSVPLSKALDDDALLAYEMNGEPLPPDHGYPLRLVVPGWYGARSVKWLRR 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972312038 330 IIVSEKESDSHWQQKDYRAFSPAVNigDELKWNTVPsIQEYPVQCAICSPAPNTKVDRGDETVdISGYAWSgGGRGIIRI 409
Cdd:cd02110   167 IEVTDQPSDGYWQTRDYTVPPPDVD--AVGGKARRP-IGEMPVKSVITSPSPGAELVSGGRVE-IGGVAWS-GGRGIRRV 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972312038 410 EVSVDGGETWNSVEMEQEEKqdqeHMYAWTLFKAEVKIPPGVKEfnIIAKAVDRAYNTQPETASGIWNVRGLIHNAWHRV 489
Cdd:cd02110   242 EVSLDGGRTWQEARLEGPLA----GPRAWRQWELDWDLPPGEYE--LVARATDSTGNVQPERAEWNWNPGGYGNNHWHRV 315
PLN00177 PLN00177
sulfite oxidase; Provisional
 175-493 2.19e-92

sulfite oxidase; Provisional


Pssm-ID: 177772 [Multi-domain]  Cd Length: 393  Bit Score: 286.36  E-value: 2.19e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972312038 175 ENHRLTVETIKGKTVDLSVEELKKKYKsYTIGSVIQCAGNRRADMNQYKKVQGLMWEGTAISNAEWTGVRLRDLLADAGI 254
Cdd:PLN00177   63 ERYSVTITGLIENPRKLSMKDIRKLPK-YNVTATLQCAGNRRTAMSKVRKVRGVGWDVSAIGNAVWGGAKLADVLELVGI 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972312038 255 DVFDDKI----KHVHFEGADVDP--TGTPYGASIPIEKARGDE--VIVAYHMNGVDIPRDHGAPLRVIVPGNVGARQVKW 326
Cdd:PLN00177  142 PKLTSITssggKHVEFVSVDKCKeeNGGPYKASIPLSQATNPEadVLLAYEMNGEVLNRDHGYPLRVVVPGVIGARSVKW 221

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972312038 327 LRKIIVSEKESDSHWQQKDYRAFSPAVNiGDELKWNTVPSIQEYPVQCAICSPAPNTKVDRGDetVDISGYAWSGGGRGI 406
Cdd:PLN00177  222 LDSINIIAEECQGFFMQKDYKMFPPSVN-WDNINWSTRRPQMDFPVQSAICSLEDVNAIKPGK--VTVAGYALSGGGRGI 298

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972312038 407 IRIEVSVDGGETWnsVEMEQEEKQDQEHM--------YAWTLFKAEVKIPPGVKefnIIAKAVDRAYNTQPETASGIWNV 478
Cdd:PLN00177  299 ERVDISVDGGKTW--VEASRYQKPGVPYIsddissdkWAWVLFEATVDVPQSTE---IVAKAVDSAANVQPESVESIWNL 373

                         330
                  ....*....|....*
gi 1972312038 479 RGLIHNAWHRVPIIV 493
Cdd:PLN00177  374 RGILNTSWHRVQLRV 388
eukary_NR_Moco cd02112
molybdopterin binding domain of eukaryotic nitrate reductase (NR). Assimilatory NRs catalyze ...
 172-491 9.83e-81

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: 256.16  E-value: 9.83e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972312038 172 IKTENHRLTVETIKGKTVDLSVEELKKKYKSYTIGSVIQCAGNRRADMNQYKKVQGLMWEGTAISNAEWTGVRLRDLLAD 251
Cdd:cd02112    56 EKWEDWTVEVTGLVEKPTTLTMDELVAMFPSVTFPVTLVCAGNRRKEQNMVKKTIGFNWGAAGTSTSLWTGVRLSDLLDR 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972312038 252 AGIDVFDDKIKHVHFEGADVDPTG--TPYGASIPIEKARGDE--VIVAYHMNGVDIPRDHGAPLRVIVPGNVGARQVKWL 327
Cdd:cd02112   136 CGPKSPKGGARHVCFEGADDLLPGpnGKYGTSITLSWAMDPSkdVMLAYKQNGELLHPDHGFPVRLIIPGQIGGRMVKWL 215

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972312038 328 RKIIVSEKESDSHWQQKDYRAFSPAVN--IGDELKWNTVPS--IQEYPVQCAICSPAPNTKVD----RGDETVDISGYAW 399
Cdd:cd02112   216 KRIVVSDRESQNHYHFHDNRVLPSHVDaeLANEEGWWYKPEyiINDLNVNSAITTPAHDEVLPlnglTTAETYTMKGYAY 295

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972312038 400 SGGGRGIIRIEVSVDGGETWNSVEMEQEEK-QDQEHMYAWTLFKAEVKIPP--GVKEfnIIAKAVDRAYNTQPETAsgIW 476
Cdd:cd02112   296 AGGGRRVTRVEVSLDDGKSWKLASIDYPEDpTKYGKCWCWCFWSLDVPLSEllAAKE--ICVRAWDESMNTQPRDM--TW 371

                         330
                  ....*....|....*
gi 1972312038 477 NVRGLIHNAWHRVPI 491
Cdd:cd02112   372 NVMGMMNNCWFRVKI 386
Oxidored_molyb pfam00174
Oxidoreductase molybdopterin binding domain; This domain is found in a variety of ...
 160-341 3.36e-75

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: 233.93  E-value: 3.36e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972312038 160 DVPKIDfedlsnikTENHRLTVETIKGKTVDLSVEELKKkYKSYTIGSVIQCAGNRRADMNQykkVQGLMWEGTAISNAE 239
Cdd:pfam00174   3 PVPEID--------PDTWRLRVDGLVEKPLTLTLDDLKA-FPQVTVTATLQCVGNRRKEMNR---VKGVQWGGGAIGNAE 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972312038 240 WTGVRLRDLLADAGIDvfdDKIKHVHFEGADVDPTGtPYGASIPIEKARGDEVIVAYHMNGVDIPRDHGAPLRVIVPGNV 319
Cdd:pfam00174  71 WTGVPLRDLLERAGVK---PGAKHVLFEGADTLGDG-GYTTSLPLEKALDDDVLLAYEMNGEPLPPDHGYPLRLVVPGWY 146

                         170       180
                  ....*....|....*....|..
gi 1972312038 320 GARQVKWLRKIIVSEKESDSHW 341
Cdd:pfam00174 147 GARSVKWLRRIEVTDEESPGFW 168
PLN02252 PLN02252
nitrate reductase [NADPH]
 161-491 1.89e-69

nitrate reductase [NADPH]


Pssm-ID: 215141 [Multi-domain]  Cd Length: 888  Bit Score: 238.04  E-value: 1.89e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972312038 161 VPKIDFEDlsniktenHRLTVETIKGKTVDLSVEELKKkYKSYTIGSVIQCAGNRRADMNQYKKVQGLMWEGTAISNAEW 240
Cdd:PLN02252  126 VPRADWDE--------WTVEVTGLVKRPARLTMDELVR-FPARELPVTLVCAGNRRKEQNMVKQTIGFNWGAAGVSTSVW 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972312038 241 TGVRLRDLLADAGIDVFDDKIKHVHFEGADVDPTG--TPYGASIPIEKAR--GDEVIVAYHMNGVDIPRDHGAPLRVIVP 316
Cdd:PLN02252  197 RGVRLRDVLRRCGVMSRKGGALNVCFEGAEDLPGGggSKYGTSITLERAMdpARDVILAYMQNGEPLTPDHGFPVRLIIP 276

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972312038 317 GNVGARQVKWLRKIIVSEKESDSHWQQKDYRAFSPAVN--IGDELKWNTVPS--IQEYPVQCAICSPAPNTKVD----RG 388
Cdd:PLN02252  277 GFIGGRMVKWLKRIIVTTAESDNYYHYRDNRVLPSHVDaeLANAEGWWYKPEyiINELNINSVITTPAHDEILPinasTT 356

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972312038 389 DETVDISGYAWSGGGRGIIRIEVSVDGGETWNSVEMEQEEKQDQEHMY-AWTLFKAEVKIPP--GVKEfnIIAKAVDRAY 465
Cdd:PLN02252  357 QRPYTMKGYAYSGGGRKVTRVEVSLDGGETWRLCDLDHPEKPTKYGKYwCWCFWSLDVEVLDllGAKE--IAVRAWDESM 434

                         330       340
                  ....*....|....*....|....*.
gi 1972312038 466 NTQPETAsgIWNVRGLIHNAWHRVPI 491
Cdd:PLN02252  435 NTQPEKL--IWNLMGMMNNCWFRVKV 458
Mo-co_dimer pfam03404
Mo-co oxidoreductase dimerization domain; This domain is found in molybdopterin cofactor ...
 365-494 5.60e-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: 188.34  E-value: 5.60e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972312038 365 PSIQEYPVQCAICSPAPNTKVDRG--DETVDISGYAWSGGGRGIIRIEVSVDGGETWNSVEMEQEEK-----QDQEHMYA 437
Cdd:pfam03404   2 YAIYDLNVNSAICSPEHDEVVKLGaaQGTYTIKGYAYSGGGRRITRVEVSLDGGKTWRLAEIDYEEDpyrygEWREKCWC 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1972312038 438 WTLFKAEVKIPPGVKEFNIIAKAVDRAYNTQPETAsgIWNVRGLIHNAWHRVPIIVK 494
Cdd:pfam03404  82 WCFWSLDIPVSDLLKAKEILVRAVDEAMNVQPEDM--YWNVRGMMNNPWHRVKIHVE 136
SO_family_Moco cd00321
Sulfite oxidase (SO) family, molybdopterin binding domain. This molybdopterin cofactor (Moco) ...
 170-335 6.07e-57

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: 186.24  E-value: 6.07e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972312038 170 SNIKTENHRLTVETIKGKTVDLSVEELKKkYKSYTIGSVIQCAGNRradmnqykkvqglmWEGTAISNAEWTGVRLRDLL 249
Cdd:cd00321    10 PEIDPDDWRLEVDGLVEKPLSLTLDDLKA-LPQVEVIATLHCVGNR--------------WGGGAVSNAEWTGVPLRDLL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972312038 250 ADAGIDvfdDKIKHVHFEGADvDPTGTPYGASIPIEKARGDEVIVAYHMNGVDIPRDHGAPLRVIVPGNVGARQVKWLRK 329
Cdd:cd00321    75 EEAGPK---PGARYVVFEGAD-DPGGDGYTTSLPLEKALDPDVLLAYEMNGEPLPPDHGFPLRLVVPGLYGWKSVKWLRR 150


                  ....*.
gi 1972312038 330 IIVSEK 335
Cdd:cd00321   151 IEVTDE 156
MsrP COG2041
Molybdopterin-dependent catalytic subunit of periplasmic DMSO/TMAO and ...
 150-351 1.67e-45

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: 157.24  E-value: 1.67e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972312038 150 GYRIGklDVKDVPKIDFEDlsniktenHRLTVETIKGKTVDLSVEELKKkYKSYTIGSVIQCAGNRRAdmnqykkvqglm 229
Cdd:COG2041    18 AFPVR--TAGGVPEIDPAD--------WRLRVDGLVEKPLTLTLDDLLA-LPLEERIYRLHCVENWSG------------ 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972312038 230 wegtaiSNAEWTGVRLRDLLADAGIDvfdDKIKHVHFEGADvdptgTPYGASIPIEKARGDEVIVAYHMNGVDIPRDHGA 309
Cdd:COG2041    75 ------GVAPWTGVPLRDLLERAGPK---PGAKYVLFESAD-----PGYTESLPLDEALDPDTLLAYGMNGEPLPPEHGA 140

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1972312038 310 PLRVIVPGNVGARQVKWLRKIIVSEKESDSHWQQKDYRAFSP 351
Cdd:COG2041   141 PLRLVVPGLYGFKSAKWLVRIEVTDEDPPGYWETRGYHFYAN 182
bact_SorA_Moco cd02114
sulfite:cytochrome c oxidoreductase subunit A (SorA), molybdopterin binding domain. SorA is ...
 172-491 1.05e-41

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: 152.67  E-value: 1.05e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972312038 172 IKTENHRLTVETIKGKTVDLSVEELKKKYKSYTIGSVIQCAGNRRADMNqyKKVQGLMWEGTAISNAEWTGVRLRDLLAD 251
Cdd:cd02114    60 IDPDAYTLTIDGKVRTPLTLSLAELKRIEPRFEVVAVNQCSGNSRGFFQ--PRVQGAQLANGAMGNARWAGVPLKAVLAK 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972312038 252 AGIDvfdDKIKHVHFEGAD--VDPTGTPYGASIPIEKARGDEVIVAYHMNGVDIPRDHGAPLRVIVPGNVGARQVKWLRK 329
Cdd:cd02114   138 AGVQ---DGARQVAFRGLDqpVLDVTPDFVKSLDIDHALDGEVMLAWEMNGEPLPVLNGYPLRLVVPGFYATYWVKHLSH 214

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972312038 330 IIVSEKESDSHWQQKDYRafspavnIGDELKWNTVPS--------IQEYPVQCAICSPAPNTKVDRGDETVdISGYAWSg 401
Cdd:cd02114   215 ITVLDKEFDGFWASQAYR-------IPDNADAGVEPGtapdrtapINRFKVRSFITSLENGAIVAPAGELA-LRGIAFD- 285

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972312038 402 GGRGIIRIEVSVDGGETWNSVEMEQEEKQdqehmYAWTLFKAEVKIP-PGvkEFNIIAKAVDRAYNTQPETASgiWNVRG 480
Cdd:cd02114   286 GGSGIRRVDVSADGGDSWTQATLGPDLGR-----FSFRGWKLTLDGVkKG--PLTLMVRATNNDGQTQPLRAP--WNPGG 356

                         330
                  ....*....|.
gi 1972312038 481 LIHNAWHRVPI 491
Cdd:cd02114   357 YMRNVVERTRI 367
bact_SoxC_Moco cd02113
bacterial SoxC is a member of the sulfite oxidase (SO) family of molybdopterin binding domains. ...
 161-491 5.69e-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: 141.38  E-value: 5.69e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972312038 161 VPKIDfedlsnikTENHRLTVETIKGKTVDLSVEELKKkYKSYTIGSVIQCAGNRRADMNqYKKVQGLMWEGTAISNAEW 240
Cdd:cd02113    23 VPDID--------PAQHRLMIHGMVKKPLVFTMDDLKR-FPSVSRIYFLECSGNGGTGWR-GAPLPTAQYTHGMLSCSEW 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972312038 241 TGVRLRDLLADAGIDvfdDKIKHVHFEGADvdptGTPYGASIPIEKARgDEVIVAYHMNGVDIPRDHGAPLRVIVPGNVG 320
Cdd:cd02113    93 TGVPLSTLLEEAGVK---PGAKWLLAEGAD----AAAMTRSIPLEKAL-DDALVAYAQNGEALRPENGYPLRLVVPGWEG 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972312038 321 ARQVKWLRKIIVsekeSDSHWQQKD-------------YRAFSpavnigdelkwntvpSIQEypVQCAICSPAPNTKVDR 387
Cdd:cd02113   165 NTNVKWLRRIEV----GDQPWMTREetskytdllpdgrARQFS---------------FVME--AKSVITSPSGGQRLRE 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972312038 388 GDETVdISGYAWSGGGRgIIRIEVSVDGGETWNSVEMEqeekqDQEHMYAWTLFKAEVKIPPgvKEFNIIAKAVDRAYNT 467
Cdd:cd02113   224 PGFHE-ISGLAWSGRGR-IRRVDVSFDGGRTWQDARLE-----GPVLPKALTRFRLPWKWDG--RPAVLQSRATDETGYV 294

                         330       340
                  ....*....|....*....|....
gi 1972312038 468 QPETASgIWNVRGlIHNAWHRVPI 491
Cdd:cd02113   295 QPTRAE-LRAVRG-TNSIYHNNAI 316
arch_bact_SO_family_Moco cd02109
bacterial and archael members of the sulfite oxidase (SO) family of molybdopterin binding ...
 154-346 1.01e-21

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: 92.31  E-value: 1.01e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972312038 154 GKLDVKDVPKIDFEDLSNIKTENHRLTVETIKGKTVDLSVEELKKKYKSytigsviqcagNRRADMNQYKKvqglmWegt 233
Cdd:cd02109     4 GQYLTEKFPVLDAGDVPEVDLEKWRLRVTGLVENPLSLTYEDLLALPQT-----------EYTADFHCVTG-----W--- 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972312038 234 AISNAEWTGVRLRDLLADAGIDvfdDKIKHVHFEGADvdptGtpYGASIPIEKARGDEVIVAYHMNGVDIPRDHGAPLRV 313
Cdd:cd02109    65 SKLDVVWEGVSLKDLLEAARPD---PEATFVMAHSYD----G--YTTNLPLEDLLREDSLLATKMDGEPLPPEHGGPARL 135

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1972312038 314 IVPGNVGARQVKWLRKIIVSEKESDSHWQQKDY 346
Cdd:cd02109   136 VVPHLYFWKSAKWLRGIEFLDEDEPGFWERRGY 168
Cyt-b5 pfam00173
Cytochrome b5-like Heme/Steroid binding domain; This family includes heme binding domains from ...
 85-157 1.78e-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: 79.59  E-value: 1.78e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1972312038  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 ...
 225-347 1.48e-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: 1.48e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972312038 225 VQGlmWegTAIsnAEWTGVRLRDLLADAGIDvfdDKIKHVHFEGADVDPTGTPYGASIPIEKARGDEVIVAYHMNGVDIP 304
Cdd:cd02108    63 VEG--W--SAI--GKWGGVPLRTILELVGPL---PEAKYVVFKCADDFAGGDRYYESIDMASALHPQTLLAYEMNGQPLP 133

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1972312038 305 RDHGAPLRVIVPGNVGARQVKWLRKIIVSEKESDSHWQQKDYR 347
Cdd:cd02108   134 IKNGAPLRLRVETQLGYKQAKWVTEIELVNDLPGIGGGKGGYW 176
PLN02252 PLN02252
nitrate reductase [NADPH]
 77-174 9.07e-13

nitrate reductase [NADPH]


Pssm-ID: 215141 [Multi-domain]  Cd Length: 888  Bit Score: 70.86  E-value: 9.07e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972312038  77 ENLQIYKQEEVKKHGKdADRIWVTYKDGVYDVTDFIAMHPGG-DKILLAAGA-AVDPFWALYSQHKTKevleILEGYRIG 154
Cdd:PLN02252  515 TGSKQYTMSEVRKHNS-EDSCWIVVHGHVYDCTRFLKDHPGGaDSILINAGTdCTEEFDAIHSDKAKK----MLEDYRIG 589

                          90       100
                  ....*....|....*....|...
gi 1972312038 155 KLDVKDV---PKIDFEDLSNIKT 174
Cdd:PLN02252  590 ELVTTGAaasSSASSHPLSAIST 612
CYB5 COG5274
Cytochrome b involved in lipid metabolism [Energy production and conversion, Lipid transport ...
 82-156 5.47e-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: 5.47e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972312038  82 YKQEEVKKHgKDADRIWVTYKDGVYDVTDFIAMHPGGDKILLA-----AGAAVDpfwalySQHKTKE-VLEILEGYRIGK 155
Cdd:COG5274    18 YTLAEVATH-NTLSDCWMAIDGNVYDLTEYIPKHPGGEAVILRwcgkdATEAFN------TKHPHSPkAERLLESYRIGR 90


                  .
gi 1972312038 156 L 156
Cdd:COG5274    91 L 91
COG3915 COG3915
Uncharacterized conserved protein [Function unknown];
239-316 1.32e-09

Uncharacterized conserved protein [Function unknown];


Pssm-ID: 443120  Cd Length: 167  Bit Score: 57.21  E-value: 1.32e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1972312038 239 EWTGVRLRDLLADAGIDVfddkiKHVHFEGADvDptgtpYGASIPIEKARGDEVIVAYHMNGVDIPRDHGAPLRVIVP 316
Cdd:COG3915    75 TFRGVLLRDLLAAVGAKG-----TTLRAVALN-D-----YAVEIPISDLEEYGVILAYRMDGKPMSVRDKGPLWLIYP 141
PLN03199 PLN03199
delta6-acyl-lipid desaturase-like protein; Provisional
 66-167 7.30e-06

delta6-acyl-lipid desaturase-like protein; Provisional


Pssm-ID: 178740 [Multi-domain]  Cd Length: 485  Bit Score: 48.50  E-value: 7.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972312038  66 AKDETMSEKKLENLQIYKQEEVKKHGKDADrIWVTYKDGVYDVTDFIAmHPGGDKILLAAG-AAVDPFWALYSQHKTKev 144
Cdd:PLN03199   10 AKGRSAALKLAEKPQKISWQEVKKHASPDD-AWIIHQNKVYDVSNWHD-HPGGAVIFTHAGdDMTDIFAAFHAPGSQA-- 85

                          90       100
                  ....*....|....*....|....*...
gi 1972312038 145 leILEGYRIGKL-----DVKDVPKIDFE 167
Cdd:PLN03199   86 --LMKKFYIGDLipestEHKDPQQIAFE 111
PLN03198 PLN03198
delta6-acyl-lipid desaturase; Provisional
 82-169 8.62e-06

delta6-acyl-lipid desaturase; Provisional


Pssm-ID: 178739 [Multi-domain]  Cd Length: 526  Bit Score: 48.15  E-value: 8.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972312038  82 YKQEEVKKHGKDADrIWVTYKDGVYDVTDFIAMHPGGDKILLAAGA-AVDPFWALYSQHKTKevleILEGYRIGKLD-VK 159
Cdd:PLN03198  106 HLLSEVAAHNKPND-CWIVIKNKVYDVSDFAAEHPGGSVISTYFGRdGTDAFSSFHAASTWK----ILQDFYIGDVDnVE 180

                          90
                  ....*....|..
gi 1972312038 160 DVPKI--DFEDL 169
Cdd:PLN03198  181 PTPELlkDFRDL 192
YedY_like_Moco cd02107
YedY_like molybdopterin cofactor (Moco) binding domain, a subgroup of the sulfite oxidase (SO) ...
 240-341 1.74e-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: 45.91  E-value: 1.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972312038 240 WTGVRLRDLLADAGIDvfdDKIKHVHFEgADVDPTGT------------PYGASIPIEKARGDEVIVAYHMNGVDIPRDH 307
Cdd:cd02107    72 WVGFPLAALLARAEPT---SEAKYVRFT-TLLDKEQMpgqsglfgvlpwPYVEGLRLDEAMHPLTLLAVGLYGEALPKQN 147

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1972312038 308 GAPLRVIVPGNVGARQVKWLRKIIVSEKESDSHW 341
Cdd:cd02107   148 GAPIRLVVPWKYGFKSIKSIVKIEFTKEQPPTTW 181
PRK05363 PRK05363
protein-methionine-sulfoxide reductase catalytic subunit MsrP;
240-343 7.34e-05

protein-methionine-sulfoxide reductase catalytic subunit MsrP;


Pssm-ID: 235431  Cd Length: 280  Bit Score: 44.43  E-value: 7.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972312038 240 WTGVRLRDLLADAGIDvfdDKIKHVHFEGAdVDPTGTPyGASIPI------EKARGDE-----VIVAYHMNGVDIPRDHG 308
Cdd:PRK05363  107 WIGFPLAKLLKRVEPT---SNAKYVAFETL-YDPEQMP-GQRSRFldwpyvEGLRLDEamhplTLLAVGLYGKTLPNQNG 181

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1972312038 309 APLRVIVPGNVGARQVKWLRKIIVSEKESDSHWQQ 343
Cdd:PRK05363  182 APIRLVVPWKYGFKSIKSIVRIRLTEEQPPTTWNL 216
COG4892 COG4892
Predicted heme/steroid binding protein [General function prediction only];
79-122 2.45e-04

Predicted heme/steroid binding protein [General function prediction only];


Pssm-ID: 443920 [Multi-domain]  Cd Length: 75  Bit Score: 39.42  E-value: 2.45e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1972312038  79 LQIYKQEEVKK-HGKDADRIWVTYKDGVYDV--------------------TDFIAMHPGGDKIL 122
Cdd:COG4892     1 MKEFTLEELAKyNGKDGNPAYVAVNGKVYDVtnsrlwkngthyghwagqdlTDELKDAPHGESVL 65
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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