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Conserved domains on  [gi|302632631|ref|YP_003848727|]
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cytochrome c oxidase subunit II (mitochondrion) [Tetranychus cinnabarinus]

Protein Classification

cytochrome c oxidase subunit II( domain architecture ID 999987)

cytochrome c oxidase subunit II, part of the functional core of the enzyme, transfers the electrons from cytochrome c via its binuclear copper A center to the bimetallic center of the catalytic subunit I

CATH:  1.10.287.90
EC:  7.1.1.9
Gene Ontology:  GO:0004129|GO:0005507
PubMed:  6307356|8083153
TCDB:  3.D.4.6.2

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
COX2 super family cl33359
cytochrome c oxidase subunit II; Provisional
 1-211 2.55e-70

cytochrome c oxidase subunit II; Provisional


The actual alignment was detected with superfamily member MTH00154:

Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 213.92  E-value: 2.55e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302632631   1 MTNMNSLWMQNFNNMMMKNMDIFNSSITNLIVFLSIFLSILIFFSMMNKNSMSFSNESNELELFWTIIPSFIILIISLPS 80
Cdd:MTH00154   1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302632631  81 MFLLYCYEENKFSFLDIKIMGNQWYWTYEYPSMNLSE--SYIKGSLFL-----RCINTSNSLIIPSNKFIRLLLSSNDVL 153
Cdd:MTH00154  81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEfdSYMIPTNELenngfRLLDVDNRLVLPMNTQIRILITAADVI 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 302632631 154 HSWTIPSLMSKMDAVPGRLNMMFFNCNKSILLKGQCSDICGINHSFMPISVLSLNFNK 211
Cdd:MTH00154 161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNN 218
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-211 2.55e-70

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 213.92  E-value: 2.55e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302632631   1 MTNMNSLWMQNFNNMMMKNMDIFNSSITNLIVFLSIFLSILIFFSMMNKNSMSFSNESNELELFWTIIPSFIILIISLPS 80
Cdd:MTH00154   1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302632631  81 MFLLYCYEENKFSFLDIKIMGNQWYWTYEYPSMNLSE--SYIKGSLFL-----RCINTSNSLIIPSNKFIRLLLSSNDVL 153
Cdd:MTH00154  81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEfdSYMIPTNELenngfRLLDVDNRLVLPMNTQIRILITAADVI 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 302632631 154 HSWTIPSLMSKMDAVPGRLNMMFFNCNKSILLKGQCSDICGINHSFMPISVLSLNFNK 211
Cdd:MTH00154 161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNN 218
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 93-204 3.47e-47

C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal oxidase in the respiratory chains of eukaryotes and most bacteria, is a multi-chain transmembrane protein located in the inner membrane of mitochondria and the cell membrane of prokaryotes. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. Only subunits I and II are essential for function. Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunit II contains a copper-copper binuclear site called CuA, which is believed to be involved in electron transfer from cytochrome c to the binuclear center (active site) in subunit I.


Pssm-ID: 259979 [Multi-domain]  Cd Length: 130  Bit Score: 151.57  E-value: 3.47e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302632631  93 SFLDIKIMGNQWYWTYEYPSMNLSE--SYI--KGSLF---LRCINTSNSLIIPSNKFIRLLLSSNDVLHSWTIPSLMSKM 165
Cdd:cd13912    1 PSLTIKAIGHQWYWSYEYSDFNDLEfdSYMipEDDLEkgqLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 302632631 166 DAVPGRLNMMFFNCNKSILLKGQCSDICGINHSFMPISV 204
Cdd:cd13912   81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVV 119
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-204 1.34e-42

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 139.47  E-value: 1.34e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302632631   95 LDIKIMGNQWYWTYEYPS-MNLS-ESYIKGSLFL-----RCINTSNSLIIPSNKFIRLLLSSNDVLHSWTIPSLMSKMDA 167
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDfGDLEfDSYMIPTEDLeegqlRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 302632631  168 VPGRLNMMFFNCNKSILLKGQCSDICGINHSFMPISV 204
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVI 117
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
30-204 6.22e-32

Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 115.70  E-value: 6.22e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302632631  30 LIVFLSIFlsILIFFSMM------NKNSMSFSNESNELELFWTIIPSFIILIISLPSMFLLYCYEENKFSFLDIKIMGNQ 103
Cdd:COG1622   44 LVIFVLVF--GLLLYFAIryrrrkGDADPAQFHHNTKLEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQ 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302632631 104 WYWTYEYPSMNlsesyikgslflrcINTSNSLIIPSNKFIRLLLSSNDVLHSWTIPSLMSKMDAVPGRLNMMFFNCNKSI 183
Cdd:COG1622  122 WKWLFRYPDQG--------------IATVNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPG 187

                        170       180
                 ....*....|....*....|.
gi 302632631 184 LLKGQCSDICGINHSFMPISV 204
Cdd:COG1622  188 TYRGQCAELCGTGHAGMRFKV 208
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 30-212 1.92e-29

cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of mitochondria (and one of several possible acceptors in prokaryotes) in the electron transport chain of aerobic respiration. The enzyme couples the oxidation of reduced cytochrome c with the reduction of molecular oxygen to water. This process results in the pumping of four protons across the membrane which are used in the proton gradient powered synthesis of ATP. The oxidase contains two heme a cofactors and three copper atoms as well as other bound ions. [Energy metabolism, Electron transport]


Pssm-ID: 274329 [Multi-domain]  Cd Length: 199  Bit Score: 108.24  E-value: 1.92e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302632631   30 LIVFLSIFLSILIFFSMMNKNSMSFSNESNELELFWTIIPSFIILIISLPS-MFLLYCYEENKFSFLDIKIMGNQWYWTY 108
Cdd:TIGR02866  25 LLVAALLAYVVWKFRRKGDEEKPSQIHGNRRLEYVWTVIPLIIVVGLFAATaKGLLYLERPIPKDALKVKVTGYQWWWDF 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302632631  109 EYPsmnlsesyikGSLFLrcinTSNSLIIPSNKFIRLLLSSNDVLHSWTIPSLMSKMDAVPGRLNMMFFNCNKSILLKGQ 188
Cdd:TIGR02866 105 EYP----------ESGFT----TVNELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGF 170

                         170       180
                  ....*....|....*....|....*..
gi 302632631  189 CSDICGINHSFMPISVLSL---NFNKI 212
Cdd:TIGR02866 171 CAELCGAGHSLMLFKVVVVpkeEFDAY 197
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-211 2.55e-70

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 213.92  E-value: 2.55e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302632631   1 MTNMNSLWMQNFNNMMMKNMDIFNSSITNLIVFLSIFLSILIFFSMMNKNSMSFSNESNELELFWTIIPSFIILIISLPS 80
Cdd:MTH00154   1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302632631  81 MFLLYCYEENKFSFLDIKIMGNQWYWTYEYPSMNLSE--SYIKGSLFL-----RCINTSNSLIIPSNKFIRLLLSSNDVL 153
Cdd:MTH00154  81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEfdSYMIPTNELenngfRLLDVDNRLVLPMNTQIRILITAADVI 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 302632631 154 HSWTIPSLMSKMDAVPGRLNMMFFNCNKSILLKGQCSDICGINHSFMPISVLSLNFNK 211
Cdd:MTH00154 161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNN 218
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 30-210 8.59e-51

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 163.96  E-value: 8.59e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302632631  30 LIVFLSIFLSILIFFSMMNKNSMSFSNESNELELFWTIIPSFIILIISLPSMFLLYCYEENKFSFLDIKIMGNQWYWTYE 109
Cdd:MTH00140  30 VLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPSLRLLYLLDETNNPLLTVKAIGHQWYWSYE 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302632631 110 YPSMNLSE--SYI-----KGSLFLRCINTSNSLIIPSNKFIRLLLSSNDVLHSWTIPSLMSKMDAVPGRLNMMFFNCNKS 182
Cdd:MTH00140 110 YSDFSVIEfdSYMvpeneLELGDFRLLEVDNRLVLPYSVDTRVLVTSADVIHSWTVPSLGVKVDAIPGRLNQLSFEPKRP 189

                        170       180
                 ....*....|....*....|....*...
gi 302632631 183 ILLKGQCSDICGINHSFMPISVLSLNFN 210
Cdd:MTH00140 190 GVFYGQCSEICGANHSFMPIVVEAVPLE 217
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 36-210 1.60e-50

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 163.33  E-value: 1.60e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302632631  36 IFLSILIFFSMMNKNSMSFSN----ESNELELFWTIIPSFIILIISLPSMFLLYCYEENKFSFLDIKIMGNQWYWTYEYP 111
Cdd:MTH00038  32 TLITILVFYGLASLLFSSPTNrfflEGQELETIWTIVPAFILIFIALPSLQLLYLMDEVNNPFLTIKAIGHQWYWSYEYT 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302632631 112 SMNLSE--SYIK-----GSLFLRCINTSNSLIIPSNKFIRLLLSSNDVLHSWTIPSLMSKMDAVPGRLNMMFFNCNKSIL 184
Cdd:MTH00038 112 DYNDLEfdSYMVptsdlSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVLHSWAVPSLGVKMDAVPGRLNQTTFFISRTGL 191

                        170       180
                 ....*....|....*....|....*.
gi 302632631 185 LKGQCSDICGINHSFMPISVLSLNFN 210
Cdd:MTH00038 192 FYGQCSEICGANHSFMPIVIESVPFN 217
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 30-204 2.48e-49

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 160.15  E-value: 2.48e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302632631  30 LIVFLSIFLSILIFFSMMNKNSM-SFSNESNELELFWTIIPSFIILIISLPSMFLLYCYEENKFSFLDIKIMGNQWYWTY 108
Cdd:MTH00168  29 LILVLILTLVLYSLLVLVTSKYTnRFLLDSQMIEFVWTIIPAFILISLALPSLRLLYLMDEIDKPDLTIKAVGHQWYWSY 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302632631 109 EYPSMNLSE--SYIKGSLFL-----RCINTSNSLIIPSNKFIRLLLSSNDVLHSWTIPSLMSKMDAVPGRLNMMFFNCNK 181
Cdd:MTH00168 109 EYTDYNDLEfdSYMVPTQDLspgqfRLLEVDNRLVLPMDSKIRVLVTSADVLHSWTLPSLGLKMDAVPGRLNQLAFLSSR 188

                        170       180
                 ....*....|....*....|...
gi 302632631 182 SILLKGQCSDICGINHSFMPISV 204
Cdd:MTH00168 189 PGSFYGQCSEICGANHSFMPIVV 211
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 30-206 1.08e-47

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 156.23  E-value: 1.08e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302632631  30 LIVFLSIFLSILIFFSMMNKNSMSFSN--ESNELELFWTIIPSFIILIISLPSMFLLYCYEENKFSFLDIKIMGNQWYWT 107
Cdd:MTH00117  28 LMVALLISSLVLYLLTLMLTTKLTHTNtvDAQEVELIWTILPAIVLILLALPSLRILYLMDEINNPHLTIKAIGHQWYWS 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302632631 108 YEYPSM-NLS-ESYI-------KGSlfLRCINTSNSLIIPSNKFIRLLLSSNDVLHSWTIPSLMSKMDAVPGRLNMMFFN 178
Cdd:MTH00117 108 YEYTDYkDLSfDSYMiptqdlpNGH--FRLLEVDHRMVIPMESPIRILITAEDVLHSWAVPSLGVKTDAVPGRLNQTSFI 185

                        170       180
                 ....*....|....*....|....*...
gi 302632631 179 CNKSILLKGQCSDICGINHSFMPISVLS 206
Cdd:MTH00117 186 TTRPGVFYGQCSEICGANHSFMPIVVES 213
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 93-204 3.47e-47

C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal oxidase in the respiratory chains of eukaryotes and most bacteria, is a multi-chain transmembrane protein located in the inner membrane of mitochondria and the cell membrane of prokaryotes. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. Only subunits I and II are essential for function. Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunit II contains a copper-copper binuclear site called CuA, which is believed to be involved in electron transfer from cytochrome c to the binuclear center (active site) in subunit I.


Pssm-ID: 259979 [Multi-domain]  Cd Length: 130  Bit Score: 151.57  E-value: 3.47e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302632631  93 SFLDIKIMGNQWYWTYEYPSMNLSE--SYI--KGSLF---LRCINTSNSLIIPSNKFIRLLLSSNDVLHSWTIPSLMSKM 165
Cdd:cd13912    1 PSLTIKAIGHQWYWSYEYSDFNDLEfdSYMipEDDLEkgqLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 302632631 166 DAVPGRLNMMFFNCNKSILLKGQCSDICGINHSFMPISV 204
Cdd:cd13912   81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVV 119
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 30-211 1.46e-43

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 145.63  E-value: 1.46e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302632631  30 LIVFLSIFLSILIFFSMMNKNSMSFSNESNELELFWTIIPSFIILIISLPSMFLLYCYEENKFSFLDIKIMGNQWYWTYE 109
Cdd:MTH00139  30 ILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPSLRLLYLMDEVSDPYLTFKAVGHQWYWSYE 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302632631 110 YPS-MNLS-ESYIKGSLFL-----RCINTSNSLIIPSNKFIRLLLSSNDVLHSWTIPSLMSKMDAVPGRLNMMFFNCNKS 182
Cdd:MTH00139 110 YSDfKNLSfDSYMIPTEDLssgefRLLEVDNRLVLPYKSNIRALITAADVLHSWTVPSLGVKIDAVPGRLNQVGFFINRP 189

                        170       180
                 ....*....|....*....|....*....
gi 302632631 183 ILLKGQCSDICGINHSFMPISVLSLNFNK 211
Cdd:MTH00139 190 GVFYGQCSEICGANHSFMPIVVEAISPKF 218
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 28-204 5.32e-43

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 144.26  E-value: 5.32e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302632631  28 TNLIVFLsifLSILIFFSMMNKNSMSFSN----ESNELELFWTIIPSFIILIISLPSMFLLYCYEENKFSFLDIKIMGNQ 103
Cdd:MTH00185  27 TLMIVFL---ISTLVLYIIVAMVTTKLTNkyilDSQEIEIVWTILPAIILIMIALPSLRILYLMDEINDPHLTIKAMGHQ 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302632631 104 WYWTYEYPSMNLSE--SYIKGSLFL-----RCINTSNSLIIPSNKFIRLLLSSNDVLHSWTIPSLMSKMDAVPGRLNMMF 176
Cdd:MTH00185 104 WYWSYEYTDYEQLEfdSYMTPTQDLtpgqfRLLETDHRMVVPMESPIRVLITAEDVLHSWTVPALGVKMDAVPGRLNQAT 183

                        170       180
                 ....*....|....*....|....*...
gi 302632631 177 FNCNKSILLKGQCSDICGINHSFMPISV 204
Cdd:MTH00185 184 FIISRPGLYYGQCSEICGANHSFMPIVV 211
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-204 1.34e-42

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 139.47  E-value: 1.34e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302632631   95 LDIKIMGNQWYWTYEYPS-MNLS-ESYIKGSLFL-----RCINTSNSLIIPSNKFIRLLLSSNDVLHSWTIPSLMSKMDA 167
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDfGDLEfDSYMIPTEDLeegqlRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 302632631  168 VPGRLNMMFFNCNKSILLKGQCSDICGINHSFMPISV 204
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVI 117
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 30-204 3.50e-41

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 139.46  E-value: 3.50e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302632631  30 LIVFL-SIFLSILIFFSMMNKNSMSFSNESNELELFWTIIPSFIILIISLPSMFLLYCYEENKFSFLDIKIMGNQWYWTY 108
Cdd:MTH00129  29 MIVFLiSTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPSLRILYLMDEINDPHLTIKAMGHQWYWSY 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302632631 109 EYPSM-NLS-ESYIKGSLFL-----RCINTSNSLIIPSNKFIRLLLSSNDVLHSWTIPSLMSKMDAVPGRLNMMFFNCNK 181
Cdd:MTH00129 109 EYTDYeDLGfDSYMIPTQDLtpgqfRLLEADHRMVVPVESPIRVLVSAEDVLHSWAVPALGVKMDAVPGRLNQTAFIASR 188

                        170       180
                 ....*....|....*....|...
gi 302632631 182 SILLKGQCSDICGINHSFMPISV 204
Cdd:MTH00129 189 PGVFYGQCSEICGANHSFMPIVV 211
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 23-211 5.91e-41

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 139.11  E-value: 5.91e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302632631  23 FNSSITNLIVFLSIFLSILIFFSMMNKNSMSFSNESNELELFWTIIPSFIILIISLPSMFLLYCYEENKFSFLDIKIMGN 102
Cdd:MTH00023  32 FHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKLLYLMDEVVSPALTIKAIGH 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302632631 103 QWYWTYEYPSMNLS----ESYIKGSLFL-----RCINTSNSLIIPSNKFIRLLLSSNDVLHSWTIPSLMSKMDAVPGRLN 173
Cdd:MTH00023 112 QWYWSYEYSDYEGEtlefDSYMVPTSDLnsgdfRLLEVDNRLVVPINTHVRILVTGADVLHSFAVPSLGLKIDAVPGRLN 191

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 302632631 174 MMFFNCNKSILLKGQCSDICGINHSFMPISVLSLNFNK 211
Cdd:MTH00023 192 QTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDK 229
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 28-202 1.07e-40

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 138.31  E-value: 1.07e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302632631  28 TNLIVFLSIFLSILIFFSMMNKNSMSFSN-ESNELELFWTIIPSFIILIISLPSMFLLYCYEENKFSFLDIKIMGNQWYW 106
Cdd:MTH00098  27 TLMIVFLISSLVLYIISLMLTTKLTHTSTmDAQEVETIWTILPAIILILIALPSLRILYMMDEINNPSLTVKTMGHQWYW 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302632631 107 TYEYPSM-NLS-ESYIKGSLFL-----RCINTSNSLIIPSNKFIRLLLSSNDVLHSWTIPSLMSKMDAVPGRLNMMFFNC 179
Cdd:MTH00098 107 SYEYTDYeDLSfDSYMIPTSDLkpgelRLLEVDNRVVLPMEMPIRMLISSEDVLHSWAVPSLGLKTDAIPGRLNQTTLMS 186

                        170       180
                 ....*....|....*....|...
gi 302632631 180 NKSILLKGQCSDICGINHSFMPI 202
Cdd:MTH00098 187 TRPGLYYGQCSEICGSNHSFMPI 209
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 23-211 3.90e-38

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 131.83  E-value: 3.90e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302632631  23 FNSSITNLIVFLSIFLSILIFFSMMNKNSMSFSNESNELELFWTIIPSFIILIISLPSMFLLYCYEENKFSFLDIKIMGN 102
Cdd:MTH00051  25 FHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSLKLLYLMDEVIDPALTIKAIGH 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302632631 103 QWYWTYEYPSMNLS----ESYI-----KGSLFLRCINTSNSLIIPSNKFIRLLLSSNDVLHSWTIPSLMSKMDAVPGRLN 173
Cdd:MTH00051 105 QWYWSYEYSDYGTDtiefDSYMiptsdLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSFAVPSLSVKIDAVPGRLN 184

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 302632631 174 MMFFNCNKSILLKGQCSDICGINHSFMPISVLSLNFNK 211
Cdd:MTH00051 185 QTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDK 222
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 31-204 2.36e-37

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 129.59  E-value: 2.36e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302632631  31 IVFLSIFLSIL---IFFSMMNKNSMSFSNESNELELFWTIIPSFIILIISLPSMFLLYCYEENKFSFLDIKIMGNQWYWT 107
Cdd:MTH00008  28 LLILTLVLTVVgyaMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPSLRLLYLMDEVSNPSITLKTIGHQWYWS 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302632631 108 YEYP--------SMNLSESYIKGSLFlRCINTSNSLIIPSNKFIRLLLSSNDVLHSWTIPSLMSKMDAVPGRLNMMFFNC 179
Cdd:MTH00008 108 YEYSdfsnlefdSYMLPTSDLSPGQF-RLLEVDNRAVLPMQTEIRVLVTAADVIHSWTVPSLGVKVDAVPGRLNQIGFTI 186

                        170       180
                 ....*....|....*....|....*
gi 302632631 180 NKSILLKGQCSDICGINHSFMPISV 204
Cdd:MTH00008 187 TRPGVFYGQCSEICGANHSFMPIVL 211
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 30-207 1.35e-36

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 127.59  E-value: 1.35e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302632631  30 LIVFLSIFLSILIFFSMM-----NKNSMsfsnESNELELFWTIIPSFIILIISLPSMFLLYCYEENKFSFLDIKIMGNQW 104
Cdd:MTH00076  29 MAVFLISTLVLYIITIMMttkltNTNTM----DAQEIEMVWTIMPAIILIVIALPSLRILYLMDEINDPHLTVKAIGHQW 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302632631 105 YWTYEYPSM-NLS-ESYIKGSLFL-----RCINTSNSLIIPSNKFIRLLLSSNDVLHSWTIPSLMSKMDAVPGRLNMMFF 177
Cdd:MTH00076 105 YWSYEYTDYeDLSfDSYMIPTQDLtpgqfRLLEVDNRMVVPMESPIRMLITAEDVLHSWAVPSLGIKTDAIPGRLNQTSF 184

                        170       180       190
                 ....*....|....*....|....*....|
gi 302632631 178 NCNKSILLKGQCSDICGINHSFMPISVLSL 207
Cdd:MTH00076 185 IASRPGVYYGQCSEICGANHSFMPIVVEAT 214
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 30-204 2.22e-33

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 118.13  E-value: 2.22e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302632631  30 LIVFLSIFLSILIFFSMMNKN-SMSFSNESNELELFWTIipsfiiliisLPSMFLLY-C--------YEENKFSFLDIKI 99
Cdd:MTH00047  17 LCVFIPCWVYIMLCWQVVSGNgSVNFGSENQVLELLWTV----------VPTLLVLVlCflnlnfitSDLDCFSSETIKV 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302632631 100 MGNQWYWTYEYPSMNLSESYIKGSLFlrciNTSNSLIIPSNKFIRLLLSSNDVLHSWTIPSLMSKMDAVPGRLNMMFFNC 179
Cdd:MTH00047  87 IGHQWYWSYEYSFGGSYDSFMTDDIF----GVDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCP 162

                        170       180
                 ....*....|....*....|....*
gi 302632631 180 NKSILLKGQCSDICGINHSFMPISV 204
Cdd:MTH00047 163 DRHGVFVGYCSELCGVGHSYMPIVI 187
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 21-204 1.47e-32

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 117.42  E-value: 1.47e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302632631  21 DIFNSSITNLIVFLSIFLSILIFFSMMNKNSMSFSNESNELELFWTIIPSFIILIISLPSMFLLYCYE-ENKFSFLDIKI 99
Cdd:MTH00080  23 HNFNCSLLFGEFVLAFVVFLFLYLISNNFYFKSKKIEYQFGELLCSVFPVLILLMQMVPSLSLLYYYGlMNLDSNLTVKV 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302632631 100 MGNQWYWTYEYP-SMNLS-ESYIKGSLFL-----RCINTSNSLIIPSNKFIRLLLSSNDVLHSWTIPSLMSKMDAVPGRL 172
Cdd:MTH00080 103 TGHQWYWSYEFSdIPGLEfDSYMKSLDQLrlgepRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDAMSGIL 182

                        170       180       190
                 ....*....|....*....|....*....|..
gi 302632631 173 NMMFFNCNKSILLKGQCSDICGINHSFMPISV 204
Cdd:MTH00080 183 STLCYSFPMPGVFYGQCSEICGANHSFMPIAV 214
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 61-211 2.38e-32

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 117.82  E-value: 2.38e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302632631  61 LELFWTIIPSFIILIISLPSMFLLYCYEENKFSF-LDIKIMGNQWYWTY---EYPSMNLS-ESYIKGSLFL-----RCIN 130
Cdd:MTH00027  92 IEVIWTLIPAFILILIAFPSLRLLYIMDECGFSAnITIKVTGHQWYWSYsyeDYGEKNIEfDSYMIPTADLefgdlRLLE 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302632631 131 TSNSLIIPSNKFIRLLLSSNDVLHSWTIPSLMSKMDAVPGRLNMMFFNCNKSILLKGQCSDICGINHSFMPISVLSLNFN 210
Cdd:MTH00027 172 VDNRLILPVDTNVRVLITAADVLHSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLS 251


                 .
gi 302632631 211 K 211
Cdd:MTH00027 252 K 252
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
30-204 6.22e-32

Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 115.70  E-value: 6.22e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302632631  30 LIVFLSIFlsILIFFSMM------NKNSMSFSNESNELELFWTIIPSFIILIISLPSMFLLYCYEENKFSFLDIKIMGNQ 103
Cdd:COG1622   44 LVIFVLVF--GLLLYFAIryrrrkGDADPAQFHHNTKLEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQ 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302632631 104 WYWTYEYPSMNlsesyikgslflrcINTSNSLIIPSNKFIRLLLSSNDVLHSWTIPSLMSKMDAVPGRLNMMFFNCNKSI 183
Cdd:COG1622  122 WKWLFRYPDQG--------------IATVNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPG 187

                        170       180
                 ....*....|....*....|.
gi 302632631 184 LLKGQCSDICGINHSFMPISV 204
Cdd:COG1622  188 TYRGQCAELCGTGHAGMRFKV 208
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 30-212 1.92e-29

cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of mitochondria (and one of several possible acceptors in prokaryotes) in the electron transport chain of aerobic respiration. The enzyme couples the oxidation of reduced cytochrome c with the reduction of molecular oxygen to water. This process results in the pumping of four protons across the membrane which are used in the proton gradient powered synthesis of ATP. The oxidase contains two heme a cofactors and three copper atoms as well as other bound ions. [Energy metabolism, Electron transport]


Pssm-ID: 274329 [Multi-domain]  Cd Length: 199  Bit Score: 108.24  E-value: 1.92e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302632631   30 LIVFLSIFLSILIFFSMMNKNSMSFSNESNELELFWTIIPSFIILIISLPS-MFLLYCYEENKFSFLDIKIMGNQWYWTY 108
Cdd:TIGR02866  25 LLVAALLAYVVWKFRRKGDEEKPSQIHGNRRLEYVWTVIPLIIVVGLFAATaKGLLYLERPIPKDALKVKVTGYQWWWDF 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302632631  109 EYPsmnlsesyikGSLFLrcinTSNSLIIPSNKFIRLLLSSNDVLHSWTIPSLMSKMDAVPGRLNMMFFNCNKSILLKGQ 188
Cdd:TIGR02866 105 EYP----------ESGFT----TVNELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGF 170

                         170       180
                  ....*....|....*....|....*..
gi 302632631  189 CSDICGINHSFMPISVLSL---NFNKI 212
Cdd:TIGR02866 171 CAELCGAGHSLMLFKVVVVpkeEFDAY 197
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 95-207 2.45e-27

The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), the terminal oxidase in the respiratory chains of most bacteria, is a multi-chain transmembrane protein located in the inner membrane the cell membrane of prokaryotes. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. Caa3 type of CcO Subunit II contains a copper-copper binuclear site called CuA, which is believed to be involved in electron transfer from cytochrome c to the cytochromes a, a3 and CuB active site in subunit I.


Pssm-ID: 259875 [Multi-domain]  Cd Length: 103  Bit Score: 100.00  E-value: 2.45e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302632631  95 LDIKIMGNQWYWTYEYPsmnlsESYIKGslflrcINTSNSLIIPSNKFIRLLLSSNDVLHSWTIPSLMSKMDAVPGRLNM 174
Cdd:cd04213    2 LTIEVTGHQWWWEFRYP-----DEPGRG------IVTANELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMDMIPGRTNR 70

                         90       100       110
                 ....*....|....*....|....*....|...
gi 302632631 175 MFFNCNKSILLKGQCSDICGINHSFMPISVLSL 207
Cdd:cd04213   71 LWLQADEPGVYRGQCAEFCGASHALMRFKVIAL 103
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 95-204 3.50e-25

Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I.


Pssm-ID: 259911 [Multi-domain]  Cd Length: 95  Bit Score: 94.29  E-value: 3.50e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302632631  95 LDIKIMGNQWYWTYEYPSmnlsesyikgslflrcINTSNSLIIPSNKFIRLLLSSNDVLHSWTIPSLMSKMDAVPGRLNM 174
Cdd:cd13842    1 LTVYVTGVQWSWTFIYPN----------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDAVPGYTSE 64

                         90       100       110
                 ....*....|....*....|....*....|
gi 302632631 175 MFFNCNKSILLKGQCSDICGINHSFMPISV 204
Cdd:cd13842   65 LWFVADKPGTYTIICAEYCGLGHSYMLGKV 94
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-200 4.70e-24

Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I.


Pssm-ID: 259986 [Multi-domain]  Cd Length: 107  Bit Score: 91.55  E-value: 4.70e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302632631  95 LDIKIMGNQWYWTYEYPSMNlsesyikGSLFLRCINTSNSLIIPSNKFIRLLLSSNDVLHSWTIPSLMSKMDAVPGRLNM 174
Cdd:cd13919    2 LVVEVTAQQWAWTFRYPGGD-------GKLGTDDDVTSPELHLPVGRPVLFNLRSKDVIHSFWVPEFRVKQDAVPGRTTR 74

                         90       100
                 ....*....|....*....|....*.
gi 302632631 175 MFFNCNKSILLKGQCSDICGINHSFM 200
Cdd:cd13919   75 LWFTPTREGEYEVRCAELCGLGHYRM 100
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-200 1.17e-20

Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I.


Pssm-ID: 259982 [Multi-domain]  Cd Length: 98  Bit Score: 82.68  E-value: 1.17e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302632631  95 LDIKIMGNQWYWTYEYPSMNlsesyikgslflrciNTSNSLIIPSNKFIRLLLSSNDVLHSWTIPSLMSKMDAVPGRLNM 174
Cdd:cd13915    2 LEIQVTGRQWMWEFTYPNGK---------------REINELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQDVVPGRYTY 66

                         90       100
                 ....*....|....*....|....*.
gi 302632631 175 MFFNCNKSILLKGQCSDICGINHSFM 200
Cdd:cd13915   67 LWFEATKPGEYDLFCTEYCGTGHSGM 92
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 126-204 5.21e-19

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 80.25  E-value: 5.21e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302632631 126 LRCINTSNSLIIPSNKFIRLLLSSNDVLHSWTIPSLMSKMDAVPGRLNMMffncNKSILLK----GQCSDICGINHSFMP 201
Cdd:PTZ00047  66 LRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKI----NTFILREgvfyGQCSEMCGTLHGFMP 141


                 ...
gi 302632631 202 ISV 204
Cdd:PTZ00047 142 IVV 144
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 97-200 4.97e-18

Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I.


Pssm-ID: 259981 [Multi-domain]  Cd Length: 108  Bit Score: 75.91  E-value: 4.97e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302632631  97 IKIMGNQWYWTYEYPSMNlsesyikgslflrcINTSNSLIIPSNKFIRLLLSSNDVLHSWTIPSLMSKMDAVPGRLNMMF 176
Cdd:cd13914    3 IEVEAYQWGWEFSYPEAN--------------VTTSEQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDAFPGQYNTIK 68

                         90       100
                 ....*....|....*....|....
gi 302632631 177 FNCNKSILLKGQCSDICGINHSFM 200
Cdd:cd13914   69 TEATEEGEYQLYCAEYCGAGHSQM 92
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-208 3.15e-17

Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from two to five in bacteria and up to 13 in mammalian mitochondria. Subunits I, II, and III of mammalian cytochrome c oxidase (CcO) are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. Subunit II is found in CcO, ubiquinol oxidase, and the ba3-like oxidases, while the cbb3 oxidases contain alternative additional subunits. Additionally, nitrous oxide reductase contains the globular portion of subunit II as a domain within its structure. In some families, subunit II contains a copper-copper binuclear center that is involved in the transfer of electrons from the substrate to the binuclear center (active site) in subunit I.


Pssm-ID: 259985 [Multi-domain]  Cd Length: 139  Bit Score: 74.80  E-value: 3.15e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 302632631  95 LDIKIMGNQWYWTYEYPSMnlsesyikgslflrcINTSNSLIIPSNKFIRLLLSSNDVLHSWTIPSLMSKMDAVPGRLNM 174
Cdd:cd13918   33 LEVEVEGFQFGWQFEYPNG---------------VTTGNTLRVPADTPIALRVTSTDVFHTFGIPELRVKADAIPGEYTS 97

                         90       100       110
                 ....*....|....*....|....*....|....
gi 302632631 175 MFFNCNKSILLKGQCSDICGINHSFMPISVLSLN 208
Cdd:cd13918   98 TWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMD 131
 
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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