NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|316892713|gb|ADU57608|]
View 

NADH dehydrogenase subunit 2, partial (mitochondrion) [Drosophila pychnochaetae]

Protein Classification

NADH dehydrogenase subunit 2( domain architecture ID 11475933)

NADH dehydrogenase subunit 2 is the core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), which functions in the transfer of electrons from NADH to the respiratory chain

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
ND2 MTH00160
NADH dehydrogenase subunit 2; Provisional
 1-163 6.88e-42

NADH dehydrogenase subunit 2; Provisional


:

Pssm-ID: 214442 [Multi-domain]  Cd Length: 335  Bit Score: 142.27  E-value: 6.88e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316892713   1 MFNNSSKILFMMMMITGTLITVTSNSWLGAWMGLEINLLSFIPLMSDNNNFKSTEASLKYFLTQALASTVLLFAVILLML 80
Cdd:MTH00160   1 MMMNSSKLLFLSTLIMGTLISISSNSWFGAWMGLEINLLSFIPLISNKKNLMSSESSLKYFLIQALASIILLFSIILNML 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316892713  81 KNNlnneINESFTSMIMLSTLLLKSGAAPFHFWFPNLMEGLTWMNALLLMTWQKIAPLMMISYLNLKNLLLISVILSVIV 160
Cdd:MTH00160  81 NLM----LFNNISSMLINSSLLLKLGAAPFHFWFPEVMEGLSWINCFILMTWQKIAPLILLSYLINNNFIIIIIILSAII 156


                 ...
gi 316892713 161 GAI 163
Cdd:MTH00160 157 GAI 159
 
Name Accession Description Interval E-value
ND2 MTH00160
NADH dehydrogenase subunit 2; Provisional
 1-163 6.88e-42

NADH dehydrogenase subunit 2; Provisional


Pssm-ID: 214442 [Multi-domain]  Cd Length: 335  Bit Score: 142.27  E-value: 6.88e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316892713   1 MFNNSSKILFMMMMITGTLITVTSNSWLGAWMGLEINLLSFIPLMSDNNNFKSTEASLKYFLTQALASTVLLFAVILLML 80
Cdd:MTH00160   1 MMMNSSKLLFLSTLIMGTLISISSNSWFGAWMGLEINLLSFIPLISNKKNLMSSESSLKYFLIQALASIILLFSIILNML 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316892713  81 KNNlnneINESFTSMIMLSTLLLKSGAAPFHFWFPNLMEGLTWMNALLLMTWQKIAPLMMISYLNLKNLLLISVILSVIV 160
Cdd:MTH00160  81 NLM----LFNNISSMLINSSLLLKLGAAPFHFWFPEVMEGLSWINCFILMTWQKIAPLILLSYLINNNFIIIIIILSAII 156


                 ...
gi 316892713 161 GAI 163
Cdd:MTH00160 157 GAI 159
Proton_antipo_M pfam00361
Proton-conducting membrane transporter; This is a family of membrane transporters that ...
 24-163 1.50e-12

Proton-conducting membrane transporter; This is a family of membrane transporters that inlcudes some 7 of potentially 14-16 TM regions. In many instances the family forms part of complex I that catalyzes the transfer of two electrons from NADH to ubiquinone in a reaction that is associated with proton translocation across the membrane, and in this context is a combination predominantly of subunits 2, 4, 5, 14, L, M and N. In many bacterial species these proteins are probable stand-alone transporters not coupled with oxidoreduction. The family in total represents homologs across the phyla.


Pssm-ID: 425636 [Multi-domain]  Cd Length: 291  Bit Score: 63.49  E-value: 1.50e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316892713   24 SNSWLGAWMGLEINLLSFIPLMSDN-NNFKSTEASLKYFLTQALASTVLLFAVIL-------------LMLKNNLNNEIN 89
Cdd:pfam00361   1 ANDLLLMYLGWEAVLLPSYLLIGYWgKSPRSSEAGMKYFLLTLLGSSILLFGISLmynytgtlsfdelSKALTGGLNSSG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316892713   90 ESFTSMIMLSTLLLKSGAAPFHFWFPNLMEGLTWMN-ALLLMTWQKIA--------PLMMISYLNLKNLLLISVILSVIV 160
Cdd:pfam00361  81 LLLLFLLILVGFLFKSAQVPFHTWLPDAYEGAPTPVsALLAATLVKAGgyglirrsLLYLPSSPFIQQILLILAIISMLL 160


                  ...
gi 316892713  161 GAI 163
Cdd:pfam00361 161 GSL 163
NuoN COG1007
NADH:ubiquinone oxidoreductase subunit 2 (chain N) [Energy production and conversion]; NADH: ...
 9-120 3.90e-07

NADH:ubiquinone oxidoreductase subunit 2 (chain N) [Energy production and conversion]; NADH:ubiquinone oxidoreductase subunit 2 (chain N) is part of the Pathway/BioSystem: NADH dehydrogenase


Pssm-ID: 440631 [Multi-domain]  Cd Length: 473  Bit Score: 48.57  E-value: 3.90e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316892713   9 LFMMMMITGTLITVTSNSWLGAWMGLEINLLSFIPLMS-DNNNFKSTEASLKYFLTQALASTVLLF--AVILLMLKNNLN 85
Cdd:COG1007  106 ALLLFATLGMMLMASANDLLTLFLGLELLSLSLYVLVAfRRDDRRSSEAALKYFLLGALSSGFLLYgiSLLYGATGSLNL 185

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 316892713  86 NEINESFTSMIMLSTLLL------------KSGAAPFHFWFPNLMEG 120
Cdd:COG1007  186 AGIAAALAAGGANSPLLLlglvlvlaglafKLSAVPFHMWTPDVYEG 232
NDH_I_N TIGR01770
proton-translocating NADH-quinone oxidoreductase, chain N; This model describes the 14th ...
 2-163 5.39e-07

proton-translocating NADH-quinone oxidoreductase, chain N; This model describes the 14th (based on E. coli) structural gene, N, of bacterial and chloroplast energy-transducing NADH (or NADPH) dehydrogenases. This model does not describe any subunit of the mitochondrial complex I (for which the subunit composition is very different), nor NADH dehydrogenases that are not coupled to ion transport. The Enzyme Commission designation 1.6.5.3, for NADH dehydrogenase (ubiquinone), is applied broadly, perhaps unfortunately, even if the quinone is menaquinone (Thermus, Mycobacterium) or plastoquinone (chloroplast). For chloroplast members, the name NADH-plastoquinone oxidoreductase is used for the complex and this protein is designated as subunit 2 or B. This model also includes a subunit of a related complex in the archaeal methanogen, Methanosarcina mazei, in which F420H2 replaces NADH and 2-hydroxyphenazine replaces the quinone. [Energy metabolism, Electron transport]


Pssm-ID: 273795 [Multi-domain]  Cd Length: 468  Bit Score: 48.02  E-value: 5.39e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316892713    2 FNNSSKILFMMMMITGTLITVTSNSWLGAWMGLEINLLSFIPLMS-DNNNFKSTEASLKYFLTQALASTVLLF------- 73
Cdd:TIGR01770  99 INKFEFYILLLFALLGIFLLVSSNDLLSIYLGLELQSLCFYVLAGlKRKSRFSTEAGLKYFILGAFSSGLLLFgisliyg 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316892713   74 -------AVILLMLKNNLNNEINESFTSMIMLSTLLLKSGAAPFHFWFPNLMEGLTWMNALLLMTWQKIA---PLMMIS- 142
Cdd:TIGR01770 179 ftgslnfEDLLLFLSNGMLNISLLLLGIVLILVGLLFKLSAVPFHMWVPDVYEGAPTPVTAFFSIVPKIAifaVFLRLFl 258

                         170       180
                  ....*....|....*....|....*..
gi 316892713  143 ------YLNLKNLLLISVILSVIVGAI 163
Cdd:TIGR01770 259 yilfgfSEAWQIFLAIIAFLSMLIGNF 285
 
Name Accession Description Interval E-value
ND2 MTH00160
NADH dehydrogenase subunit 2; Provisional
 1-163 6.88e-42

NADH dehydrogenase subunit 2; Provisional


Pssm-ID: 214442 [Multi-domain]  Cd Length: 335  Bit Score: 142.27  E-value: 6.88e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316892713   1 MFNNSSKILFMMMMITGTLITVTSNSWLGAWMGLEINLLSFIPLMSDNNNFKSTEASLKYFLTQALASTVLLFAVILLML 80
Cdd:MTH00160   1 MMMNSSKLLFLSTLIMGTLISISSNSWFGAWMGLEINLLSFIPLISNKKNLMSSESSLKYFLIQALASIILLFSIILNML 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316892713  81 KNNlnneINESFTSMIMLSTLLLKSGAAPFHFWFPNLMEGLTWMNALLLMTWQKIAPLMMISYLNLKNLLLISVILSVIV 160
Cdd:MTH00160  81 NLM----LFNNISSMLINSSLLLKLGAAPFHFWFPEVMEGLSWINCFILMTWQKIAPLILLSYLINNNFIIIIIILSAII 156


                 ...
gi 316892713 161 GAI 163
Cdd:MTH00160 157 GAI 159
ND2 MTH00105
NADH dehydrogenase subunit 2; Provisional
 8-162 2.14e-33

NADH dehydrogenase subunit 2; Provisional


Pssm-ID: 177167 [Multi-domain]  Cd Length: 347  Bit Score: 120.34  E-value: 2.14e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316892713   8 ILFMMMMITGTLITVTSNSWLGAWMGLEINLLSFIPLMSDNNNFKSTEASLKYFLTQALASTVLLFAVILLMLKNN--LN 85
Cdd:MTH00105   7 IIIYLTLFLGTMITMISSHWLLAWIGLEMNMLAIIPILMKKHNPRSTEAATKYFLTQATASMLLMMAIIINLMYSGqwTI 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316892713  86 NEINESFTSMIMLSTLLLKSGAAPFHFWFPNLMEGLTWMNALLLMTWQKIAPL----MMISYLNLkNLLLISVILSVIVG 161
Cdd:MTH00105  87 TKLTNPTASTLMTIALAMKLGLAPFHFWVPEVTQGIPLSSGMILLTWQKLAPLsilyQISPSINP-NLLLTLAILSILIG 165


                 .
gi 316892713 162 A 162
Cdd:MTH00105 166 G 166
ND2 MTH00112
NADH dehydrogenase subunit 2; Provisional
 6-161 1.57e-32

NADH dehydrogenase subunit 2; Provisional


Pssm-ID: 214423 [Multi-domain]  Cd Length: 346  Bit Score: 118.00  E-value: 1.57e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316892713   6 SKILFMMMMITGTLITVTSNSWLGAWMGLEINLLSFIPLMSDNNNFKSTEASLKYFLTQALASTVLLFAVILLMLKNNL- 84
Cdd:MTH00112   5 AKLIITTSLILGTIITISSNHWLMAWTGLEINTLAIIPLISKPHHPRATEAATKYFLTQAAASALILFSSTTNAWNTGQw 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316892713  85 -NNEINESFTSMIMLSTLLLKSGAAPFHFWFPNLMEGLTWMNALLLMTWQKIAP---LMMISYLNLKNLLLISVILSVIV 160
Cdd:MTH00112  85 dITQLTNPTSCTLLTLALAMKLGLAPFHFWLPEVLQGSTTTTALILSTWQKLAPltlLLMTSNSLNPTLLLTLAILSTLI 164


                 .
gi 316892713 161 G 161
Cdd:MTH00112 165 G 165
ND2 MTH00041
NADH dehydrogenase subunit 2; Validated
 3-163 9.78e-28

NADH dehydrogenase subunit 2; Validated


Pssm-ID: 177116 [Multi-domain]  Cd Length: 349  Bit Score: 105.40  E-value: 9.78e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316892713   3 NNSSKILFMMMMITGTLITVTSNSWLGAWMGLEINLLSFIPLMSDNNNFKSTEASLKYFLTQALASTVLLFAVILLMLKN 82
Cdd:MTH00041   2 NRNVLIFLITSIILGTIIVISSNHWFLIWLGLELNTLSIIPILSSNFSPRSVEATIKYFLVQAFSAAILLNGALIQAWLS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316892713  83 N--LNNEINESFTSMIMLSTLLLKSGAAPFHFWFPNLMEGLTWMNALLLMTWQKIAPLMMISYLN---LKNLLLISVILS 157
Cdd:MTH00041  82 GswSINGPLNTLSSIIITLALALKLGLAPCHFWFPDVLQGLPFLQGLIIATWQKIAPLILLISISnllNSNILILCGILS 161


                 ....*.
gi 316892713 158 VIVGAI 163
Cdd:MTH00041 162 VLVGGW 167
ND2 MTH00070
NADH dehydrogenase subunit 2; Provisional
 10-161 1.10e-27

NADH dehydrogenase subunit 2; Provisional


Pssm-ID: 177142 [Multi-domain]  Cd Length: 346  Bit Score: 105.39  E-value: 1.10e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316892713  10 FMMMMITGTLITVTSNSWLGAWMGLEINLLSFIPLMSDNNNFKSTEASLKYFLTQALASTVLLFAVILLMLKNNLNNEIN 89
Cdd:MTH00070   9 LLSSLALGTMITLSSNHWFLAWMGLEINTLAIIPLMTKTHHPRATEAATKYFLTQASASALILFSSTINAWFTGEWTIMN 88

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 316892713  90 -ESFTSMIMLST-LLLKSGAAPFHFWFPNLMEGLTWMNALLLMTWQKIAP---LMMISYLNLKNLLLISVILSVIVG 161
Cdd:MTH00070  89 mQTPLPTIMLTIaLMMKLGIAPFHFWLPEVLQGLDLTTGLILSTWQKLAPmalLIQISHLLNSNLLIIMGLLSTLIG 165
ND2 MTH00144
NADH dehydrogenase subunit 2; Provisional
 5-163 2.24e-27

NADH dehydrogenase subunit 2; Provisional


Pssm-ID: 214432 [Multi-domain]  Cd Length: 328  Bit Score: 104.20  E-value: 2.24e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316892713   5 SSKILFMMMMITGTLITVTSNSWLGAWMGLEINLLSFIPLMSDNNNFKSTEASLKYFLTQALASTVLLFAVILLMLKNnl 84
Cdd:MTH00144   4 PSNLLFLFLMVMGTLLSLSSSHWLGVWVGLEINLIGFLPLLVYKKKSSESESVVKYFIIQSLGSSLLIFGSLIMYNLS-- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316892713  85 nneiNESFTSMIMLSTLLLKSGAAPFHFWFPNLMEGLTWMNALLLMTWQKIAPLMMISYLN----LKNLLLISVILSVIV 160
Cdd:MTH00144  82 ----FSWFSMSLLLLGLCLKLGLFPFHFWVPSVMAGLSWLSCFLLLTWQKVAPLFLLSNFLdlywLAYLLCVISVLSALV 157


                 ...
gi 316892713 161 GAI 163
Cdd:MTH00144 158 GSI 160
ND2 MTH00135
NADH dehydrogenase subunit 2; Provisional
 17-161 2.74e-26

NADH dehydrogenase subunit 2; Provisional


Pssm-ID: 177193 [Multi-domain]  Cd Length: 347  Bit Score: 101.42  E-value: 2.74e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316892713  17 GTLITVTSNSWLGAWMGLEINLLSFIPLMSDNNNFKSTEASLKYFLTQALASTVLLFAVILLMLKN--NLNNEINESFTS 94
Cdd:MTH00135  16 GTTLTFASSHWLLAWMGLEINTLAIIPLMAQHHHPRAVEATTKYFLTQATAAAMILFASTTNAWLTgqWDIQQMSHPLPT 95

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 316892713  95 MIMLSTLLLKSGAAPFHFWFPNLMEGLTWMNALLLMTWQKIAPLMMISYLNLKN--LLLISVILSVIVG 161
Cdd:MTH00135  96 TMITLALALKIGLAPLHFWLPEVLQGLDLTTGLILSTWQKLAPFALILQIAPTNptLLITLGLTSTLVG 164
ND2 MTH00011
NADH dehydrogenase subunit 2; Validated
 9-163 7.97e-24

NADH dehydrogenase subunit 2; Validated


Pssm-ID: 164587 [Multi-domain]  Cd Length: 330  Bit Score: 94.85  E-value: 7.97e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316892713   9 LFMMMMITGTLITVTSNSWLGAWMGLEINLLSFIPLMSDNNNFKSTEASLKYFLTQALASTVLLFAVILLMLKNNLNNei 88
Cdd:MTH00011  10 LFSSTMTLGTLMALSSNNWLFLWMGMELNLLSFVPLMTSSKMNQESEAAVKYFLAQALGSGLLLLGMTMMWSFPSLLK-- 87

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 316892713  89 neSFTSMIMLSTLLLKSGAAPFHFWFPNLMEGLTWMNALLLMTWQKIAPLMMISYL---NLKNLLLISVILSVIVGAI 163
Cdd:MTH00011  88 --NITALMLLVSLMLKLGMAPCHFWFPSVMSSISWTLCLILSTWQKIAPLSILFFFtshNILPMMTSMAAMSALAGGL 163
ND2 MTH00200
NADH dehydrogenase subunit 2; Provisional
 9-163 4.35e-22

NADH dehydrogenase subunit 2; Provisional


Pssm-ID: 177246 [Multi-domain]  Cd Length: 347  Bit Score: 90.41  E-value: 4.35e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316892713   9 LFMMMMITGTLITVTSNSWLGAWMGLEINLLSFIPLMSDNNNFKSTEASLKYFLTQALASTVLLFAVILLMLKNNL--NN 86
Cdd:MTH00200   8 LFILSLGLGTLLTFSSSHWFLIWLGLEINTLAIIPLLIKQHHPRKVEATTKYFIIQATASALLLFGGLLNAWTSGQwgIS 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316892713  87 EINESFTSMIMLSTLLLKSGAAPFHFWFPNLMEGLTWMNALLLMTWQKIAPLMM---ISYLNLKNLLLISVILSVIVGAI 163
Cdd:MTH00200  88 EMLGPLSETLILLALALKLGLAPGHFWVPDVLQGLSLQTGLILSTWQKLAPFALliqLAPALNSNILLLLGLLSVLVGGW 167
ND2 MTH00197
NADH dehydrogenase subunit 2; Provisional
 9-163 1.85e-20

NADH dehydrogenase subunit 2; Provisional


Pssm-ID: 177244 [Multi-domain]  Cd Length: 323  Bit Score: 85.49  E-value: 1.85e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316892713   9 LFMMMMITGTLITVTSNSWLGAWMGLEINLLSFIPLMSDNNNFKSTEASLKYFLTQALASTVLLFAVILLMLKNNLnnei 88
Cdd:MTH00197   2 LFLFIIFGGVLFSLSSSNWFLVWIGMELNLIGFIPLLSQNKSITENEGAMKYFLFQEFGSALLLMGGSLSFSNLYL---- 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 316892713  89 nESFTSMIMLSTLLLKSGAAPFHFWFPNLMEGLTWMNALLLMTWQKIAPLMMISYL-NLKNLLLISVILSVIVGAI 163
Cdd:MTH00197  78 -SLLSVVLVILGLLLKLGAFPFHFWVPSVMESLSWFNCFLLATWQKLAPLLILAFNsSSFMGLLICSVLSSLIGGI 152
ND2 MTH00196
NADH dehydrogenase subunit 2; Provisional
 13-163 1.29e-12

NADH dehydrogenase subunit 2; Provisional


Pssm-ID: 214453 [Multi-domain]  Cd Length: 365  Bit Score: 64.28  E-value: 1.29e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316892713  13 MMITGTLITVTSNSWLGAWMGLEINLLS-FIPLMSDNNNFKSTEASLKYFLTQALASTVLLFAVI--------------- 76
Cdd:MTH00196   1 MVALGILCLISSSNWLSVYLAIELQTLSlFILIAQNRGSGYSAEAGLKYFVLGALSSGLFLFGCAllcgttgglhlsyin 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316892713  77 LLMLKNNLNNEINESFTSMIMLSTLLLKSGAAPFHFWFPNLMEGLTWMNALLLMTWQKIAPLMMISYLNLK-NLLLISVI 155
Cdd:MTH00196  81 LVLNSGQSFSSVSVPIGYLLIIVALLFKLSVAPFHMWAPDVYEGAPTKTTALLAIVPKLGIFSILVSIGLNvNILLIGGL 160


                 ....*...
gi 316892713 156 LSVIVGAI 163
Cdd:MTH00196 161 FSLFVGAI 168
Proton_antipo_M pfam00361
Proton-conducting membrane transporter; This is a family of membrane transporters that ...
 24-163 1.50e-12

Proton-conducting membrane transporter; This is a family of membrane transporters that inlcudes some 7 of potentially 14-16 TM regions. In many instances the family forms part of complex I that catalyzes the transfer of two electrons from NADH to ubiquinone in a reaction that is associated with proton translocation across the membrane, and in this context is a combination predominantly of subunits 2, 4, 5, 14, L, M and N. In many bacterial species these proteins are probable stand-alone transporters not coupled with oxidoreduction. The family in total represents homologs across the phyla.


Pssm-ID: 425636 [Multi-domain]  Cd Length: 291  Bit Score: 63.49  E-value: 1.50e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316892713   24 SNSWLGAWMGLEINLLSFIPLMSDN-NNFKSTEASLKYFLTQALASTVLLFAVIL-------------LMLKNNLNNEIN 89
Cdd:pfam00361   1 ANDLLLMYLGWEAVLLPSYLLIGYWgKSPRSSEAGMKYFLLTLLGSSILLFGISLmynytgtlsfdelSKALTGGLNSSG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316892713   90 ESFTSMIMLSTLLLKSGAAPFHFWFPNLMEGLTWMN-ALLLMTWQKIA--------PLMMISYLNLKNLLLISVILSVIV 160
Cdd:pfam00361  81 LLLLFLLILVGFLFKSAQVPFHTWLPDAYEGAPTPVsALLAATLVKAGgyglirrsLLYLPSSPFIQQILLILAIISMLL 160


                  ...
gi 316892713  161 GAI 163
Cdd:pfam00361 161 GSL 163
ND2 MTH00199
NADH dehydrogenase subunit 2; Provisional
 5-163 7.85e-12

NADH dehydrogenase subunit 2; Provisional


Pssm-ID: 177245 [Multi-domain]  Cd Length: 460  Bit Score: 61.96  E-value: 7.85e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316892713   5 SSKILFMMMMITGTLITVTSNSWLGAWMGLEINLLS-FIPLMSDNNNFKSTEASLKYFLTQALASTVLLF--AVILLMLK 81
Cdd:MTH00199  97 QSSPILILIVALGSLLLVSSINWLSIYLAIELQTLTlFILVALKRDSAYSTEAGLKYFVLGAVSSGLFLFgcALLYGLTG 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316892713  82 NNLNNEINESFTS-----MIMLStLLLKSGAAPFHFWFPNLMEGLTWMNALLLMTWQKI---APLMMISYLNlkNLLLIS 153
Cdd:MTH00199 177 ETSIQGINSILTGdvgkiLITIS-LLFKLSAAPFHMWAPDVYEGAPTITTALLATVPKIgvfSILVQIGPVT--NVVLIC 253

                        170
                 ....*....|
gi 316892713 154 VILSVIVGAI 163
Cdd:MTH00199 254 AVLSIIYGAI 263
PRK05777 PRK05777
NADH-quinone oxidoreductase subunit NuoN;
11-163 1.34e-08

NADH-quinone oxidoreductase subunit NuoN;


Pssm-ID: 235603 [Multi-domain]  Cd Length: 476  Bit Score: 52.52  E-value: 1.34e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316892713  11 MMMMITGTLITVTSNSWLGAWMGLEI-NLLSFIPLMSDNNNFKSTEASLKYFLTQALASTVLL--------------FAV 75
Cdd:PRK05777 109 VLFALLGMMVMVSANDLLTLFLGLELlSLPLYALAALRRDRRRSLEAAIKYFVLGALASGFLLygmsllygatgslsFAG 188

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316892713  76 ILLMLKNNLNNEINESFTSMIMLSTLLLKSGAAPFHFWFPNLMEGLTWMNALLLMTWQKIAPLMMI----------SYLN 145
Cdd:PRK05777 189 IAKALADGSGNSLLLLFGLVFLLVGLAFKLSAVPFHMWTPDVYEGAPTPVTAFLATAPKIAAFAVLlrllvvafggLSED 268

                        170
                 ....*....|....*...
gi 316892713 146 LKNLLLISVILSVIVGAI 163
Cdd:PRK05777 269 WQQVLAIIAIASMLVGNL 286
NuoN COG1007
NADH:ubiquinone oxidoreductase subunit 2 (chain N) [Energy production and conversion]; NADH: ...
 9-120 3.90e-07

NADH:ubiquinone oxidoreductase subunit 2 (chain N) [Energy production and conversion]; NADH:ubiquinone oxidoreductase subunit 2 (chain N) is part of the Pathway/BioSystem: NADH dehydrogenase


Pssm-ID: 440631 [Multi-domain]  Cd Length: 473  Bit Score: 48.57  E-value: 3.90e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316892713   9 LFMMMMITGTLITVTSNSWLGAWMGLEINLLSFIPLMS-DNNNFKSTEASLKYFLTQALASTVLLF--AVILLMLKNNLN 85
Cdd:COG1007  106 ALLLFATLGMMLMASANDLLTLFLGLELLSLSLYVLVAfRRDDRRSSEAALKYFLLGALSSGFLLYgiSLLYGATGSLNL 185

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 316892713  86 NEINESFTSMIMLSTLLL------------KSGAAPFHFWFPNLMEG 120
Cdd:COG1007  186 AGIAAALAAGGANSPLLLlglvlvlaglafKLSAVPFHMWTPDVYEG 232
NDH_I_N TIGR01770
proton-translocating NADH-quinone oxidoreductase, chain N; This model describes the 14th ...
 2-163 5.39e-07

proton-translocating NADH-quinone oxidoreductase, chain N; This model describes the 14th (based on E. coli) structural gene, N, of bacterial and chloroplast energy-transducing NADH (or NADPH) dehydrogenases. This model does not describe any subunit of the mitochondrial complex I (for which the subunit composition is very different), nor NADH dehydrogenases that are not coupled to ion transport. The Enzyme Commission designation 1.6.5.3, for NADH dehydrogenase (ubiquinone), is applied broadly, perhaps unfortunately, even if the quinone is menaquinone (Thermus, Mycobacterium) or plastoquinone (chloroplast). For chloroplast members, the name NADH-plastoquinone oxidoreductase is used for the complex and this protein is designated as subunit 2 or B. This model also includes a subunit of a related complex in the archaeal methanogen, Methanosarcina mazei, in which F420H2 replaces NADH and 2-hydroxyphenazine replaces the quinone. [Energy metabolism, Electron transport]


Pssm-ID: 273795 [Multi-domain]  Cd Length: 468  Bit Score: 48.02  E-value: 5.39e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316892713    2 FNNSSKILFMMMMITGTLITVTSNSWLGAWMGLEINLLSFIPLMS-DNNNFKSTEASLKYFLTQALASTVLLF------- 73
Cdd:TIGR01770  99 INKFEFYILLLFALLGIFLLVSSNDLLSIYLGLELQSLCFYVLAGlKRKSRFSTEAGLKYFILGAFSSGLLLFgisliyg 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316892713   74 -------AVILLMLKNNLNNEINESFTSMIMLSTLLLKSGAAPFHFWFPNLMEGLTWMNALLLMTWQKIA---PLMMIS- 142
Cdd:TIGR01770 179 ftgslnfEDLLLFLSNGMLNISLLLLGIVLILVGLLFKLSAVPFHMWVPDVYEGAPTPVTAFFSIVPKIAifaVFLRLFl 258

                         170       180
                  ....*....|....*....|....*..
gi 316892713  143 ------YLNLKNLLLISVILSVIVGAI 163
Cdd:TIGR01770 259 yilfgfSEAWQIFLAIIAFLSMLIGNF 285
ND2 MTH00198
NADH dehydrogenase subunit 2; Provisional
 17-162 8.69e-05

NADH dehydrogenase subunit 2; Provisional


Pssm-ID: 214454 [Multi-domain]  Cd Length: 607  Bit Score: 41.77  E-value: 8.69e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316892713  17 GTLITVTSNSWLGAWMGLEINLLSFIPLMSDNNNFKST---------EASLKYFLTQALASTVLLFA------------- 74
Cdd:MTH00198 200 GGLLLIESANWLTIYLALEFQTLALFILAGEGSQPGSHfpspgntppESGLKYWILGAMSSGFYLFGcalyfgftgnegm 279

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316892713  75 --VILLMLKNNLNNEINE-SFTSMIMLSTLLLKSGAAPFHFWFPNLMEGLTWMNALLLMTWQKIAPLMMISYLNLKNLLL 151
Cdd:MTH00198 280 lgTILSATLETTNIELRQgSLGYLFITVAILFKLAAAPFHMWTPDVYEGAPTPTTALIAIIPKFTVYILLTSLVITSKLL 359

                        170
                 ....*....|..
gi 316892713 152 ISV-ILSVIVGA 162
Cdd:MTH00198 360 LSVaIISLVVGA 371
HyfB COG0651
Formate hydrogenlyase subunit 3/Multisubunit Na+/H+ antiporter, MnhD subunit [Energy ...
 10-116 9.76e-03

Formate hydrogenlyase subunit 3/Multisubunit Na+/H+ antiporter, MnhD subunit [Energy production and conversion, Inorganic ion transport and metabolism];


Pssm-ID: 440416 [Multi-domain]  Cd Length: 430  Bit Score: 35.51  E-value: 9.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 316892713  10 FMMMMITGTLITVTSNSWLGAWMGLEINLLSFIPLMSDNNNFKSTEASLKYFLTQALASTVLLFAVILLMLKN------- 82
Cdd:COG0651  112 LFLLLLAGMNGAFLTGDLFNLFVFFEVMLLASYGLVALGGTKEALRAGLKYLILNLVGSALFLLGVGLLYGATgtlnmad 191

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 316892713  83 --NLNNEINESFTSMI---MLSTLLLKSGAAPFHFWFPN 116
Cdd:COG0651  192 laARLAELDPGLLLAAfalLLVGFGIKAALFPLHFWLPD 230
 
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