NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1214740200|ref|NP_001340283|]
View 

NADH-cytochrome b5 reductase-like isoform 3 [Homo sapiens]

Protein Classification

cytochrome b5 reductase family protein( domain architecture ID 10153046)

cytochrome b5 reductase family protein such as NADH-cytochrome b5 reductase that catalyzes the reduction of 2 molecules of cytochrome b5 using NADH as an electron donor; the cytochrome b5/NADH cytochrome b5 reductase electron transfer system supports the catalytic activity of several sterol biosynthetic enzymes

CATH:  3.40.50.80
EC:  1.-.-.-
Gene Ontology:  GO:0016491
PubMed:  19997042

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
cyt_b5_reduct_like cd06183
Cytochrome b5 reductase catalyzes the reduction of 2 molecules of cytochrome b5 using NADH as ...
 2-167 1.23e-32

Cytochrome b5 reductase catalyzes the reduction of 2 molecules of cytochrome b5 using NADH as an electron donor. Like ferredoxin reductases, these proteins have an N-terminal FAD binding subdomain and a C-terminal NADH binding subdomain, separated by a cleft, which accepts FAD. The NADH-binding moiety interacts with part of the FAD and resembles a Rossmann fold. However, NAD is bound differently than in canonical Rossmann fold proteins. Nitrate reductases, flavoproteins similar to pyridine nucleotide cytochrome reductases, catalyze the reduction of nitrate to nitrite. The enzyme can be divided into three functional fragments that bind the cofactors molybdopterin, heme-iron, and FAD/NADH.


:

Pssm-ID: 99780 [Multi-domain]  Cd Length: 234  Bit Score: 115.74  E-value: 1.23e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214740200   2 GLMSRYVESWRVGDTAFWRGPFGDFFYKPNQY---------GellllaagTGLAPMVPILQSITDNENDETFVTLVGCFK 72
Cdd:cd06183    72 GKMSQYLHSLKPGDTVEIRGPFGKFEYKPNGKvkhigmiagG--------TGITPMLQLIRAILKDPEDKTKISLLYANR 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214740200  73 TFESIYLKTFLQE--QARFWNVRTFFVLSQESSseqlPWSYqektHFGHLGQDLIKELVS-CCRRKPFALVCGSAEFTK- 148
Cdd:cd06183   144 TEEDILLREELDElaKKHPDRFKVHYVLSRPPE----GWKG----GVGFITKEMIKEHLPpPPSEDTLVLVCGPPPMIEg 215

                         170
                  ....*....|....*....
gi 1214740200 149 DIARCLLCAGLTEDSYFLF 167
Cdd:cd06183   216 AVKGLLKELGYKKDNVFKF 234
 
Name Accession Description Interval E-value
cyt_b5_reduct_like cd06183
Cytochrome b5 reductase catalyzes the reduction of 2 molecules of cytochrome b5 using NADH as ...
 2-167 1.23e-32

Cytochrome b5 reductase catalyzes the reduction of 2 molecules of cytochrome b5 using NADH as an electron donor. Like ferredoxin reductases, these proteins have an N-terminal FAD binding subdomain and a C-terminal NADH binding subdomain, separated by a cleft, which accepts FAD. The NADH-binding moiety interacts with part of the FAD and resembles a Rossmann fold. However, NAD is bound differently than in canonical Rossmann fold proteins. Nitrate reductases, flavoproteins similar to pyridine nucleotide cytochrome reductases, catalyze the reduction of nitrate to nitrite. The enzyme can be divided into three functional fragments that bind the cofactors molybdopterin, heme-iron, and FAD/NADH.


Pssm-ID: 99780 [Multi-domain]  Cd Length: 234  Bit Score: 115.74  E-value: 1.23e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214740200   2 GLMSRYVESWRVGDTAFWRGPFGDFFYKPNQY---------GellllaagTGLAPMVPILQSITDNENDETFVTLVGCFK 72
Cdd:cd06183    72 GKMSQYLHSLKPGDTVEIRGPFGKFEYKPNGKvkhigmiagG--------TGITPMLQLIRAILKDPEDKTKISLLYANR 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214740200  73 TFESIYLKTFLQE--QARFWNVRTFFVLSQESSseqlPWSYqektHFGHLGQDLIKELVS-CCRRKPFALVCGSAEFTK- 148
Cdd:cd06183   144 TEEDILLREELDElaKKHPDRFKVHYVLSRPPE----GWKG----GVGFITKEMIKEHLPpPPSEDTLVLVCGPPPMIEg 215

                         170
                  ....*....|....*....
gi 1214740200 149 DIARCLLCAGLTEDSYFLF 167
Cdd:cd06183   216 AVKGLLKELGYKKDNVFKF 234
PLN02252 PLN02252
nitrate reductase [NADPH]
 2-167 2.41e-07

nitrate reductase [NADPH]


Pssm-ID: 215141 [Multi-domain]  Cd Length: 888  Bit Score: 49.29  E-value: 2.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214740200   2 GLMSRYVESWRVGDTAFWRGPFGDFFY----------KPNQYGELLLLAAGTGLAPMVPILQSITDNENDETFVTLVGCF 71
Cdd:PLN02252  717 GLMSQYLDSLPIGDTIDVKGPLGHIEYagrgsflvngKPKFAKKLAMLAGGTGITPMYQVIQAILRDPEDKTEMSLVYAN 796

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214740200  72 KTFESIYLKTFLQEQA-----RFwnvRTFFVLSQESSSEqlpWSYQekthFGHLGQDLIKELVSCCRRKPFALVCGSAEF 146
Cdd:PLN02252  797 RTEDDILLREELDRWAaehpdRL---KVWYVVSQVKREG---WKYS----VGRVTEAMLREHLPEGGDETLALMCGPPPM 866

                         170       180
                  ....*....|....*....|..
gi 1214740200 147 TKDIAR-CLLCAGLTEDSYFLF 167
Cdd:PLN02252  867 IEFACQpNLEKMGYDKDSILVF 888
Fpr COG1018
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
2-165 9.20e-07

Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];


Pssm-ID: 440641 [Multi-domain]  Cd Length: 231  Bit Score: 47.09  E-value: 9.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214740200   2 GLMSRYV-ESWRVGDTAFWRGPFGDFFYKPNQY--------GellllaagTGLAPMVPILQSITDNENDETfVTLVGCFK 72
Cdd:COG1018    76 GGGSNWLhDHLKVGDTLEVSGPRGDFVLDPEPArpllliagG--------IGITPFLSMLRTLLARGPFRP-VTLVYGAR 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214740200  73 TFESIYLKTFLQE-QARFWNVRTFFVLSQESSSEQlpwsyqekthfGHLGQDLIKELVsccrrKPFA----LVCGSAEFT 147
Cdd:COG1018   147 SPADLAFRDELEAlAARHPRLRLHPVLSREPAGLQ-----------GRLDAELLAALL-----PDPAdahvYLCGPPPMM 210

                         170
                  ....*....|....*...
gi 1214740200 148 KDIARCLLCAGLTEDSYF 165
Cdd:COG1018   211 EAVRAALAELGVPEERIH 228
NAD_binding_1 pfam00175
Oxidoreductase NAD-binding domain; Xanthine dehydrogenases, that also bind FAD/NAD, have ...
 44-152 1.33e-06

Oxidoreductase NAD-binding domain; Xanthine dehydrogenases, that also bind FAD/NAD, have essentially no similarity.


Pssm-ID: 425503 [Multi-domain]  Cd Length: 109  Bit Score: 44.56  E-value: 1.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214740200  44 GLAPMVPILQSITDNENDETFVTLVGCFKTFESIYLKTFLQE--QARFWNVRTFFVLSQESSSeqlpWSYQEkthfGHLG 121
Cdd:pfam00175   7 GIAPVRSMLRAILEDPKDPTQVVLVFGNRNEDDILYREELDElaEKHPGRLTVVYVVSRPEAG----WTGGK----GRVQ 78

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1214740200 122 QDLIKELVSCCRRKPFALVCGSAEFTKDIAR 152
Cdd:pfam00175  79 DALLEDHLSLPDEETHVYVCGPPGMIKAVRK 109
 
Name Accession Description Interval E-value
cyt_b5_reduct_like cd06183
Cytochrome b5 reductase catalyzes the reduction of 2 molecules of cytochrome b5 using NADH as ...
 2-167 1.23e-32

Cytochrome b5 reductase catalyzes the reduction of 2 molecules of cytochrome b5 using NADH as an electron donor. Like ferredoxin reductases, these proteins have an N-terminal FAD binding subdomain and a C-terminal NADH binding subdomain, separated by a cleft, which accepts FAD. The NADH-binding moiety interacts with part of the FAD and resembles a Rossmann fold. However, NAD is bound differently than in canonical Rossmann fold proteins. Nitrate reductases, flavoproteins similar to pyridine nucleotide cytochrome reductases, catalyze the reduction of nitrate to nitrite. The enzyme can be divided into three functional fragments that bind the cofactors molybdopterin, heme-iron, and FAD/NADH.


Pssm-ID: 99780 [Multi-domain]  Cd Length: 234  Bit Score: 115.74  E-value: 1.23e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214740200   2 GLMSRYVESWRVGDTAFWRGPFGDFFYKPNQY---------GellllaagTGLAPMVPILQSITDNENDETFVTLVGCFK 72
Cdd:cd06183    72 GKMSQYLHSLKPGDTVEIRGPFGKFEYKPNGKvkhigmiagG--------TGITPMLQLIRAILKDPEDKTKISLLYANR 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214740200  73 TFESIYLKTFLQE--QARFWNVRTFFVLSQESSseqlPWSYqektHFGHLGQDLIKELVS-CCRRKPFALVCGSAEFTK- 148
Cdd:cd06183   144 TEEDILLREELDElaKKHPDRFKVHYVLSRPPE----GWKG----GVGFITKEMIKEHLPpPPSEDTLVLVCGPPPMIEg 215

                         170
                  ....*....|....*....
gi 1214740200 149 DIARCLLCAGLTEDSYFLF 167
Cdd:cd06183   216 AVKGLLKELGYKKDNVFKF 234
FNR_like cd00322
Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a ...
 2-165 1.35e-07

Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a chloroplast reductase activity, catalyzing the electron transfer from reduced iron-sulfur protein ferredoxin to NADP+ as the final step in the electron transport mechanism of photosystem I. FNR transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) and then transfers a hydride ion to convert NADP+ to NADPH. FNR has since been shown to utilize a variety of electron acceptors and donors and has a variety of physiological functions including nitrogen assimilation, dinitrogen fixation, steroid hydroxylation, fatty acid metabolism, oxygenase activity, and methane assimilation in many organisms. FNR has an NAD(P)-binding sub-domain of the alpha/beta class and a discrete (usually N-terminal) flavin sub-domain which vary in orientation with respect to the NAD(P) binding domain. The N-terminal moeity may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Because flavins such as FAD can exist in oxidized, semiquinone (one- electron reduced), or fully reduced hydroquinone forms, FNR can interact with one and 2 electron carriers. FNR has a strong preference for NADP(H) vs NAD(H).


Pssm-ID: 99778 [Multi-domain]  Cd Length: 223  Bit Score: 49.37  E-value: 1.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214740200   2 GLMSRYVESWRVGDTAFWRGPFGDFFYKPNQYGELLLLAAGTGLAPMVPILQSITDNENDETFVTLVGCfKTFESI-YLK 80
Cdd:cd00322    66 GPFSAWLHDLKPGDEVEVSGPGGDFFLPLEESGPVVLIAGGIGITPFRSMLRHLAADKPGGEITLLYGA-RTPADLlFLD 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214740200  81 TFLQEQARFWNVRTFFVLSQESSSEQLPWsyqektHFGHLGQDLIKELVSccRRKPFALVCGSAEFTKDIARCLLCAGLT 160
Cdd:cd00322   145 ELEELAKEGPNFRLVLALSRESEAKLGPG------GRIDREAEILALLPD--DSGALVYICGPPAMAKAVREALVSLGVP 216


                  ....*
gi 1214740200 161 EDSYF 165
Cdd:cd00322   217 EERIH 221
PLN02252 PLN02252
nitrate reductase [NADPH]
 2-167 2.41e-07

nitrate reductase [NADPH]


Pssm-ID: 215141 [Multi-domain]  Cd Length: 888  Bit Score: 49.29  E-value: 2.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214740200   2 GLMSRYVESWRVGDTAFWRGPFGDFFY----------KPNQYGELLLLAAGTGLAPMVPILQSITDNENDETFVTLVGCF 71
Cdd:PLN02252  717 GLMSQYLDSLPIGDTIDVKGPLGHIEYagrgsflvngKPKFAKKLAMLAGGTGITPMYQVIQAILRDPEDKTEMSLVYAN 796

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214740200  72 KTFESIYLKTFLQEQA-----RFwnvRTFFVLSQESSSEqlpWSYQekthFGHLGQDLIKELVSCCRRKPFALVCGSAEF 146
Cdd:PLN02252  797 RTEDDILLREELDRWAaehpdRL---KVWYVVSQVKREG---WKYS----VGRVTEAMLREHLPEGGDETLALMCGPPPM 866

                         170       180
                  ....*....|....*....|..
gi 1214740200 147 TKDIAR-CLLCAGLTEDSYFLF 167
Cdd:PLN02252  867 IEFACQpNLEKMGYDKDSILVF 888
Fpr COG1018
Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];
2-165 9.20e-07

Flavodoxin/ferredoxin--NADP reductase [Energy production and conversion];


Pssm-ID: 440641 [Multi-domain]  Cd Length: 231  Bit Score: 47.09  E-value: 9.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214740200   2 GLMSRYV-ESWRVGDTAFWRGPFGDFFYKPNQY--------GellllaagTGLAPMVPILQSITDNENDETfVTLVGCFK 72
Cdd:COG1018    76 GGGSNWLhDHLKVGDTLEVSGPRGDFVLDPEPArpllliagG--------IGITPFLSMLRTLLARGPFRP-VTLVYGAR 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214740200  73 TFESIYLKTFLQE-QARFWNVRTFFVLSQESSSEQlpwsyqekthfGHLGQDLIKELVsccrrKPFA----LVCGSAEFT 147
Cdd:COG1018   147 SPADLAFRDELEAlAARHPRLRLHPVLSREPAGLQ-----------GRLDAELLAALL-----PDPAdahvYLCGPPPMM 210

                         170
                  ....*....|....*...
gi 1214740200 148 KDIARCLLCAGLTEDSYF 165
Cdd:COG1018   211 EAVRAALAELGVPEERIH 228
NAD_binding_1 pfam00175
Oxidoreductase NAD-binding domain; Xanthine dehydrogenases, that also bind FAD/NAD, have ...
 44-152 1.33e-06

Oxidoreductase NAD-binding domain; Xanthine dehydrogenases, that also bind FAD/NAD, have essentially no similarity.


Pssm-ID: 425503 [Multi-domain]  Cd Length: 109  Bit Score: 44.56  E-value: 1.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214740200  44 GLAPMVPILQSITDNENDETFVTLVGCFKTFESIYLKTFLQE--QARFWNVRTFFVLSQESSSeqlpWSYQEkthfGHLG 121
Cdd:pfam00175   7 GIAPVRSMLRAILEDPKDPTQVVLVFGNRNEDDILYREELDElaEKHPGRLTVVYVVSRPEAG----WTGGK----GRVQ 78

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1214740200 122 QDLIKELVSCCRRKPFALVCGSAEFTKDIAR 152
Cdd:pfam00175  79 DALLEDHLSLPDEETHVYVCGPPGMIKAVRK 109
FNR_iron_sulfur_binding cd06191
Iron-sulfur binding Ferredoxin Reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 2-158 5.71e-06

Iron-sulfur binding Ferredoxin Reductase (FNR) proteins combine the FAD and NAD(P) binding regions of FNR with a C-terminal iron-sulfur binding cluster domain. FNR was intially identified as a chloroplast reductase activity catalyzing the electron transfer from reduced iron-sulfur protein ferredoxin to NADP+ as the final step in the electron transport mechanism of photosystem I. FNR transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) and then transfers a hydride ion to convert NADP+ to NADPH. FNR has since been shown to utilize a variety of electron acceptors and donors and has a variety of physiological functions including nitrogen assimilation, dinitrogen fixation, steroid hydroxylation, fatty acid metabolism, oxygenase activity, and methnae assimilation in a variety of organisms. FNR has an NAD(P)-binding sub-domain of the alpha/beta class and a discrete (usually N-terminal) flavin sub-domain which vary in orientation with respect to the NAD(P) binding domain. The N-terminal moeity may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Because flavins such as FAD can exist in oxidized, semiquinone (one- electron reduced), or fully reduced hydroquinone forms, FNR can interact with one and 2 electron carriers. FNR has a strong preference for NADP(H) vs NAD(H).


Pssm-ID: 99788 [Multi-domain]  Cd Length: 231  Bit Score: 44.82  E-value: 5.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214740200   2 GLMSRY-VESWRVGDTAFWRGPFGDFFYKPNQYGELLLLAAGTGLAPMVPILQSITDNENDETFvTLVGCFKTFESIYLK 80
Cdd:cd06191    70 GRVSNYlREHIQPGMTVEVMGPQGHFVYQPQPPGRYLLVAAGSGITPLMAMIRATLQTAPESDF-TLIHSARTPADMIFA 148

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1214740200  81 TFLQEQARF-WNVRTFFVLSQESSseQLPWSYQEkthfGHLGQDLIKELVScCRRKPFALVCGSAEFTKDIARCLLCAG 158
Cdd:cd06191   149 QELRELADKpQRLRLLCIFTRETL--DSDLLHGR----IDGEQSLGAALIP-DRLEREAFICGPAGMMDAVETALKELG 220
FNR_iron_sulfur_binding_3 cd06217
Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding ...
 2-162 1.06e-05

Iron-sulfur binding ferredoxin reductase (FNR) proteins combine the FAD and NAD(P) binding regions of FNR with an iron-sulfur binding cluster domain. Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap between the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH.


Pssm-ID: 99813 [Multi-domain]  Cd Length: 235  Bit Score: 43.79  E-value: 1.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214740200   2 GLMSRY-VESWRVGDTAFWRGPFGDFFYKPNQYGELLLLAAGTGLAPMVPILQSITDNENDETFVTLVGCFKTFESIYLK 80
Cdd:cd06217    75 GEVSPYlHDEVKVGDLLEVRGPIGTFTWNPLHGDPVVLLAGGSGIVPLMSMIRYRRDLGWPVPFRLLYSARTAEDVIFRD 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214740200  81 TFLQEQARFWNVRTFFVLSQESSSEqlpWSyqekthfGHLGQ---DLIKELVSCCRRKPFaLVCGSAEFTKDIARCLLCA 157
Cdd:cd06217   155 ELEQLARRHPNLHVTEALTRAAPAD---WL-------GPAGRitaDLIAELVPPLAGRRV-YVCGPPAFVEAATRLLLEL 223


                  ....*
gi 1214740200 158 GLTED 162
Cdd:cd06217   224 GVPRD 228
PTZ00319 PTZ00319
NADH-cytochrome B5 reductase; Provisional
 2-167 2.64e-05

NADH-cytochrome B5 reductase; Provisional


Pssm-ID: 173521 [Multi-domain]  Cd Length: 300  Bit Score: 42.90  E-value: 2.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214740200   2 GLMSRYVESWRVGDTAFWRGPFGDFFYKPN-----QYGELLLLAAG----------TGLAPMVPILQSITDNENDETFVT 66
Cdd:PTZ00319  120 GRLSQHLYHMKLGDKIEMRGPVGKFEYLGNgtytvHKGKGGLKTMHvdafamiaggTGITPMLQIIHAIKKNKEDRTKVF 199

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214740200  67 LVGCFKTFESIYLKTFLQEQARFWNVRTFFVLSQESSSEqlpWSYQEkthfGHLGQDLIKELV------SCCRRKPFALV 140
Cdd:PTZ00319  200 LVYANQTEDDILLRKELDEAAKDPRFHVWYTLDREATPE---WKYGT----GYVDEEMLRAHLpvpdpqNSGIKKVMALM 272

                         170       180
                  ....*....|....*....|....*...
gi 1214740200 141 CGSAEFTKD-IARCLLCAGLTEDSYFLF 167
Cdd:PTZ00319  273 CGPPPMLQMaVKPNLEKIGYTADNMFTF 300
Mcr1 COG0543
NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion]; ...
 1-162 3.15e-04

NAD(P)H-flavin reductase [Coenzyme transport and metabolism, Energy production and conversion];


Pssm-ID: 440309 [Multi-domain]  Cd Length: 247  Bit Score: 39.85  E-value: 3.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214740200   1 MGLMSRYVESWRVGDTAFWRGPFGDFFYKPNQY----------GellllaagtgLAPMVPILQSITDNENDetfVTLV-G 69
Cdd:COG0543    64 VGKGTRALAELKPGDELDVRGPLGNGFPLEDSGrpvllvaggtG----------LAPLRSLAEALLARGRR---VTLYlG 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214740200  70 cFKTFESIYLKTFLQEqarfWNVRTFFVLSQESSseqlpwsyqekthFGHLG--QDLIKELVSccRRKPF-ALVCGSAEF 146
Cdd:COG0543   131 -ARTPEDLYLLDELEA----LADFRVVVTTDDGW-------------YGRKGfvTDALKELLA--EDSGDdVYACGPPPM 190

                         170
                  ....*....|....*.
gi 1214740200 147 TKDIARCLLCAGLTED 162
Cdd:COG0543   191 MKAVAELLLERGVPPE 206
PTZ00274 PTZ00274
cytochrome b5 reductase; Provisional
 2-151 1.34e-03

cytochrome b5 reductase; Provisional


Pssm-ID: 140300  Cd Length: 325  Bit Score: 37.98  E-value: 1.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1214740200   2 GLMSRYVESWRVGDTAFWRGPFGDFFYKPNQYGELLLLAAGTGLAPMVPIL-----QSITDNENDETFVTLVGCFKTFES 76
Cdd:PTZ00274  128 GLMTNHLFGMHVGDKLLFRSVTFKIQYRPNRWKHVGMIAGGTGFTPMLQIIrhsltEPWDSGEVDRTKLSFLFCNRTERH 207

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1214740200  77 IYLKTFLQEQA-RFWN-VRTFFVLSQESSSEQLPwsyqektHF-GHLGQDLIKELVSCC-RRKPFALVCGSAEFTKDIA 151
Cdd:PTZ00274  208 ILLKGLFDDLArRYSNrFKVYYTIDQAVEPDKWN-------HFlGYVTKEMVRRTMPAPeEKKKIIMLCGPDQLLNHVA 279
FAD_binding_6 pfam00970
Oxidoreductase FAD-binding domain;
2-28 4.44e-03

Oxidoreductase FAD-binding domain;


Pssm-ID: 425968 [Multi-domain]  Cd Length: 99  Bit Score: 34.86  E-value: 4.44e-03
                          10        20
                  ....*....|....*....|....*..
gi 1214740200   2 GLMSRYVESWRVGDTAFWRGPFGDFFY 28
Cdd:pfam00970  73 GKMSQYLDELKIGDTIDFKGPLGRFEY 99
NqrF COG2871
Na+-transporting NADH:ubiquinone oxidoreductase, subunit NqrF [Energy production and ...
 2-32 4.59e-03

Na+-transporting NADH:ubiquinone oxidoreductase, subunit NqrF [Energy production and conversion]; Na+-transporting NADH:ubiquinone oxidoreductase, subunit NqrF is part of the Pathway/BioSystem: Na+-translocating NADH dehydrogenase


Pssm-ID: 442118 [Multi-domain]  Cd Length: 396  Bit Score: 36.38  E-value: 4.59e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1214740200   2 GLMSRYVESWRVGDTAFWRGPFGDFFYKPNQ 32
Cdd:COG2871   231 GIGSSYIFSLKPGDKVTISGPYGEFFLRDSD 261
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH