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Conserved domains on  [gi|749502631|gb|AJF22970|]
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cytochrome oxidase subunit 2, partial (mitochondrion) [Haaniella dehaanii]

Protein Classification

cytochrome c oxidase subunit II( domain architecture ID 11475927)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-215 7.87e-134

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 374.55  E-value: 7.87e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749502631   1 WPNMILQDSTSPLMEQLTFFHDHIMMILMMIVTTVSYTIIMLVTNKSTDRN**EGQMIELIWTVTPAMTLFFIATPSLRL 80
Cdd:MTH00154   4 WSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749502631  81 LYLMDEINNPMMTMKAVGHQWYWTYEYSDFNEMEFDSYM--NNQLEENSMRLLDVDNRTVLPSNTFIRMIITSTDVIHSW 158
Cdd:MTH00154  84 LYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMipTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSW 163

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 749502631 159 TLPSTGIKIDGTPGRLNQASMMLNRNGLIYGQCSEICGTNHSFMPIVVESVPINTFI 215
Cdd:MTH00154 164 TVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFI 220
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-215 7.87e-134

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 374.55  E-value: 7.87e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749502631   1 WPNMILQDSTSPLMEQLTFFHDHIMMILMMIVTTVSYTIIMLVTNKSTDRN**EGQMIELIWTVTPAMTLFFIATPSLRL 80
Cdd:MTH00154   4 WSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749502631  81 LYLMDEINNPMMTMKAVGHQWYWTYEYSDFNEMEFDSYM--NNQLEENSMRLLDVDNRTVLPSNTFIRMIITSTDVIHSW 158
Cdd:MTH00154  84 LYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMipTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSW 163

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 749502631 159 TLPSTGIKIDGTPGRLNQASMMLNRNGLIYGQCSEICGTNHSFMPIVVESVPINTFI 215
Cdd:MTH00154 164 TVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFI 220
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 90-215 1.09e-78

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: 231.69  E-value: 1.09e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749502631  90 PMMTMKAVGHQWYWTYEYSDFNEMEFDSYM--NNQLEENSMRLLDVDNRTVLPSNTFIRMIITSTDVIHSWTLPSTGIKI 167
Cdd:cd13912    1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMipEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 749502631 168 DGTPGRLNQASMMLNRNGLIYGQCSEICGTNHSFMPIVVESVPINTFI 215
Cdd:cd13912   81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFL 128
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
92-209 8.93e-70

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 208.80  E-value: 8.93e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749502631   92 MTMKAVGHQWYWTYEYSDFNEMEFDSYM--NNQLEENSMRLLDVDNRTVLPSNTFIRMIITSTDVIHSWTLPSTGIKIDG 169
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMipTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 749502631  170 TPGRLNQASMMLNRNGLIYGQCSEICGTNHSFMPIVVESV 209
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
3-210 6.70e-46

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 151.52  E-value: 6.70e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749502631   3 NMILQDSTSPLMEQLTFFHDhIMMILMMIVTTVsyTIIMLV---------TNKSTDRN**EGQMIELIWTVTPAMTLFFI 73
Cdd:COG1622   18 QLSLPDPAGPIAEEIDDLFW-VSLIIMLVIFVL--VFGLLLyfairyrrrKGDADPAQFHHNTKLEIVWTVIPIIIVIVL 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749502631  74 ATPSLRLLYLMDEINNPMMTMKAVGHQWYWTYEYSDFNEmefdsymnnqleensmrllDVDNRTVLPSNTFIRMIITSTD 153
Cdd:COG1622   95 AVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGI-------------------ATVNELVLPVGRPVRFLLTSAD 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 749502631 154 VIHSWTLPSTGIKIDGTPGRLNQASMMLNRNGLIYGQCSEICGTNHSFMPIVVESVP 210
Cdd:COG1622  156 VIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVS 212
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 10-214 3.53e-40

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: 135.97  E-value: 3.53e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749502631   10 TSPLMEQLTFFHDhIMMILMMIVTTVSYTIIMLVT----NKSTDRN---**EGQMIELIWTVTPAMTLF-FIATPSLRLL 81
Cdd:TIGR02866   2 GGEIAQQIAFLFL-FVLAVSTLISLLVAALLAYVVwkfrRKGDEEKpsqIHGNRRLEYVWTVIPLIIVVgLFAATAKGLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749502631   82 YLMDEINNPMMTMKAVGHQWYWTYEYSDFnemefdsymnnqleensmrLLDVDNRTVLPSNTFIRMIITSTDVIHSWTLP 161
Cdd:TIGR02866  81 YLERPIPKDALKVKVTGYQWWWDFEYPES-------------------GFTTVNELVLPAGTPVELQVTSKDVIHSFWVP 141

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 749502631  162 STGIKIDGTPGRLNQASMMLNRNGLIYGQCSEICGTNHSFMPIVVESVPINTF 214
Cdd:TIGR02866 142 ELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEF 194
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-215 7.87e-134

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 374.55  E-value: 7.87e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749502631   1 WPNMILQDSTSPLMEQLTFFHDHIMMILMMIVTTVSYTIIMLVTNKSTDRN**EGQMIELIWTVTPAMTLFFIATPSLRL 80
Cdd:MTH00154   4 WSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749502631  81 LYLMDEINNPMMTMKAVGHQWYWTYEYSDFNEMEFDSYM--NNQLEENSMRLLDVDNRTVLPSNTFIRMIITSTDVIHSW 158
Cdd:MTH00154  84 LYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMipTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSW 163

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 749502631 159 TLPSTGIKIDGTPGRLNQASMMLNRNGLIYGQCSEICGTNHSFMPIVVESVPINTFI 215
Cdd:MTH00154 164 TVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFI 220
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 6-214 4.93e-112

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 319.55  E-value: 4.93e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749502631   6 LQDSTSPLMEQLTFFHDHIMMILMMIVTTVSYTIIMLVTNKSTDRN**EGQMIELIWTVTPAMTLFFIATPSLRLLYLMD 85
Cdd:MTH00117   9 FQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPSLRILYLMD 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749502631  86 EINNPMMTMKAVGHQWYWTYEYSDFNEMEFDSYM--NNQLEENSMRLLDVDNRTVLPSNTFIRMIITSTDVIHSWTLPST 163
Cdd:MTH00117  89 EINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMipTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVLHSWAVPSL 168

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 749502631 164 GIKIDGTPGRLNQASMMLNRNGLIYGQCSEICGTNHSFMPIVVESVPINTF 214
Cdd:MTH00117 169 GVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHF 219
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-215 1.62e-110

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 315.72  E-value: 1.62e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749502631   1 WPNMILQDSTSPLMEQLTFFHDHIMMILMMIVTTVSYTIIMLVTNKSTDRN**EGQMIELIWTVTPAMTLFFIATPSLRL 80
Cdd:MTH00140   4 WGQLGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPSLRL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749502631  81 LYLMDEINNPMMTMKAVGHQWYWTYEYSDFNEMEFDSYM--NNQLEENSMRLLDVDNRTVLPSNTFIRMIITSTDVIHSW 158
Cdd:MTH00140  84 LYLLDETNNPLLTVKAIGHQWYWSYEYSDFSVIEFDSYMvpENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVIHSW 163

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 749502631 159 TLPSTGIKIDGTPGRLNQASMMLNRNGLIYGQCSEICGTNHSFMPIVVESVPINTFI 215
Cdd:MTH00140 164 TVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFV 220
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-214 5.65e-108

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 309.32  E-value: 5.65e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749502631   1 WPNMILQDSTSPLMEQLTFFHDHIMMILMMIVTTVSYTIIMLVTNKSTDRN**EGQMIELIWTVTPAMTLFFIATPSLRL 80
Cdd:MTH00038   4 WLQLGLQDASSPLMEELIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPSLQL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749502631  81 LYLMDEINNPMMTMKAVGHQWYWTYEYSDFNEMEFDSYM--NNQLEENSMRLLDVDNRTVLPSNTFIRMIITSTDVIHSW 158
Cdd:MTH00038  84 LYLMDEVNNPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMvpTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVLHSW 163

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 749502631 159 TLPSTGIKIDGTPGRLNQASMMLNRNGLIYGQCSEICGTNHSFMPIVVESVPINTF 214
Cdd:MTH00038 164 AVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTF 219
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-215 2.69e-107

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 307.80  E-value: 2.69e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749502631   1 WPNMILQDSTSPLMEQLTFFHDHIMMILMMIVTTVSYTIIMLVTNKSTDRN**EGQMIELIWTVTPAMTLFFIATPSLRL 80
Cdd:MTH00139   4 WGQLGFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPSLRL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749502631  81 LYLMDEINNPMMTMKAVGHQWYWTYEYSDFNEMEFDSYM--NNQLEENSMRLLDVDNRTVLPSNTFIRMIITSTDVIHSW 158
Cdd:MTH00139  84 LYLMDEVSDPYLTFKAVGHQWYWSYEYSDFKNLSFDSYMipTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVLHSW 163

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 749502631 159 TLPSTGIKIDGTPGRLNQASMMLNRNGLIYGQCSEICGTNHSFMPIVVESVPINTFI 215
Cdd:MTH00139 164 TVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFL 220
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-215 9.28e-105

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 301.13  E-value: 9.28e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749502631   1 WPNMILQDSTSPLMEQLTFFHDHIMMILMMIVTTVSYTIIMLVTNKSTDRN**EGQMIELIWTVTPAMTLFFIATPSLRL 80
Cdd:MTH00168   4 YSQLGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPSLRL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749502631  81 LYLMDEINNPMMTMKAVGHQWYWTYEYSDFNEMEFDSYMNNQ--LEENSMRLLDVDNRTVLPSNTFIRMIITSTDVIHSW 158
Cdd:MTH00168  84 LYLMDEIDKPDLTIKAVGHQWYWSYEYTDYNDLEFDSYMVPTqdLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVLHSW 163

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 749502631 159 TLPSTGIKIDGTPGRLNQASMMLNRNGLIYGQCSEICGTNHSFMPIVVESVPINTFI 215
Cdd:MTH00168 164 TLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFE 220
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 6-214 2.29e-98

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 285.07  E-value: 2.29e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749502631   6 LQDSTSPLMEQLTFFHDHIMMILMMIVTTVSYTIIMLVTNKSTDRN**EGQMIELIWTVTPAMTLFFIATPSLRLLYLMD 85
Cdd:MTH00098   9 FQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPSLRILYMMD 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749502631  86 EINNPMMTMKAVGHQWYWTYEYSDFNEMEFDSYM--NNQLEENSMRLLDVDNRTVLPSNTFIRMIITSTDVIHSWTLPST 163
Cdd:MTH00098  89 EINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMipTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVLHSWAVPSL 168

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 749502631 164 GIKIDGTPGRLNQASMMLNRNGLIYGQCSEICGTNHSFMPIVVESVPINTF 214
Cdd:MTH00098 169 GLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYF 219
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 6-214 1.92e-97

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 282.76  E-value: 1.92e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749502631   6 LQDSTSPLMEQLTFFHDHIMMILMMIVTTVSYTIIMLVTNKSTDRN**EGQMIELIWTVTPAMTLFFIATPSLRLLYLMD 85
Cdd:MTH00129   9 FQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPSLRILYLMD 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749502631  86 EINNPMMTMKAVGHQWYWTYEYSDFNEMEFDSYM--NNQLEENSMRLLDVDNRTVLPSNTFIRMIITSTDVIHSWTLPST 163
Cdd:MTH00129  89 EINDPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMipTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVLHSWAVPAL 168

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 749502631 164 GIKIDGTPGRLNQASMMLNRNGLIYGQCSEICGTNHSFMPIVVESVPINTF 214
Cdd:MTH00129 169 GVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHF 219
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-215 5.92e-97

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 281.74  E-value: 5.92e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749502631   1 WPNMILQDSTSPLMEQLTFFHDHIMMILMMIVTTVSYTIIMLVTNKSTDRN**EGQMIELIWTVTPAMTLFFIATPSLRL 80
Cdd:MTH00008   4 WGQLMFQDAASPVMLQLISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPSLRL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749502631  81 LYLMDEINNPMMTMKAVGHQWYWTYEYSDFNEMEFDSYM--NNQLEENSMRLLDVDNRTVLPSNTFIRMIITSTDVIHSW 158
Cdd:MTH00008  84 LYLMDEVSNPSITLKTIGHQWYWSYEYSDFSNLEFDSYMlpTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVIHSW 163

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 749502631 159 TLPSTGIKIDGTPGRLNQASMMLNRNGLIYGQCSEICGTNHSFMPIVVESVPINTFI 215
Cdd:MTH00008 164 TVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFM 220
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 6-215 1.40e-96

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 280.87  E-value: 1.40e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749502631   6 LQDSTSPLMEQLTFFHDHIMMILMMIVTTVSYTIIMLVTNKSTDRN**EGQMIELIWTVTPAMTLFFIATPSLRLLYLMD 85
Cdd:MTH00023  18 FQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKLLYLMD 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749502631  86 EINNPMMTMKAVGHQWYWTYEYSDFNE--MEFDSYM--NNQLEENSMRLLDVDNRTVLPSNTFIRMIITSTDVIHSWTLP 161
Cdd:MTH00023  98 EVVSPALTIKAIGHQWYWSYEYSDYEGetLEFDSYMvpTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSFAVP 177

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 749502631 162 STGIKIDGTPGRLNQASMMLNRNGLIYGQCSEICGTNHSFMPIVVESVPINTFI 215
Cdd:MTH00023 178 SLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYI 231
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 6-214 1.42e-95

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 278.31  E-value: 1.42e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749502631   6 LQDSTSPLMEQLTFFHDHIMMILMMIVTTVSYTIIMLVTNKSTDRN**EGQMIELIWTVTPAMTLFFIATPSLRLLYLMD 85
Cdd:MTH00185   9 LQDAASPVMEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPSLRILYLMD 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749502631  86 EINNPMMTMKAVGHQWYWTYEYSDFNEMEFDSYM--NNQLEENSMRLLDVDNRTVLPSNTFIRMIITSTDVIHSWTLPST 163
Cdd:MTH00185  89 EINDPHLTIKAMGHQWYWSYEYTDYEQLEFDSYMtpTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVLHSWTVPAL 168

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 749502631 164 GIKIDGTPGRLNQASMMLNRNGLIYGQCSEICGTNHSFMPIVVESVPINTF 214
Cdd:MTH00185 169 GVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHF 219
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 6-215 4.83e-94

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 274.35  E-value: 4.83e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749502631   6 LQDSTSPLMEQLTFFHDHIMMILMMIVTTVSYTIIMLVTNKSTDRN**EGQMIELIWTVTPAMTLFFIATPSLRLLYLMD 85
Cdd:MTH00076   9 FQDAASPIMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPSLRILYLMD 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749502631  86 EINNPMMTMKAVGHQWYWTYEYSDFNEMEFDSYM--NNQLEENSMRLLDVDNRTVLPSNTFIRMIITSTDVIHSWTLPST 163
Cdd:MTH00076  89 EINDPHLTVKAIGHQWYWSYEYTDYEDLSFDSYMipTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVLHSWAVPSL 168

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 749502631 164 GIKIDGTPGRLNQASMMLNRNGLIYGQCSEICGTNHSFMPIVVESVPINTFI 215
Cdd:MTH00076 169 GIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFL 220
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 7-215 1.29e-92

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 270.88  E-value: 1.29e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749502631   7 QDSTSPLMEQLTFFHDHIMMILMMIVTTVSYTIIMLVTNKSTDRN**EGQMIELIWTVTPAMTLFFIATPSLRLLYLMDE 86
Cdd:MTH00051  12 QDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSLKLLYLMDE 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749502631  87 INNPMMTMKAVGHQWYWTYEYSDF--NEMEFDSYM--NNQLEENSMRLLDVDNRTVLPSNTFIRMIITSTDVIHSWTLPS 162
Cdd:MTH00051  92 VIDPALTIKAIGHQWYWSYEYSDYgtDTIEFDSYMipTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSFAVPS 171

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 749502631 163 TGIKIDGTPGRLNQASMMLNRNGLIYGQCSEICGTNHSFMPIVVESVPINTFI 215
Cdd:MTH00051 172 LSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYI 224
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 90-215 1.09e-78

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: 231.69  E-value: 1.09e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749502631  90 PMMTMKAVGHQWYWTYEYSDFNEMEFDSYM--NNQLEENSMRLLDVDNRTVLPSNTFIRMIITSTDVIHSWTLPSTGIKI 167
Cdd:cd13912    1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMipEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 749502631 168 DGTPGRLNQASMMLNRNGLIYGQCSEICGTNHSFMPIVVESVPINTFI 215
Cdd:cd13912   81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFL 128
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 6-215 5.19e-70

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 214.50  E-value: 5.19e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749502631   6 LQDSTSPLMEQLTFFHDHIMMILMMIVTTVSYTIIMLVTNK---STDRN**EGQMIELIWTVTPAMTLFFIATPSLRLLY 82
Cdd:MTH00027  37 FQDAGSPVMEEIIMLHDQILFILTIIVGVVLWLIIRILLGNnyySYYWNKLDGSLIEVIWTLIPAFILILIAFPSLRLLY 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749502631  83 LMDE-INNPMMTMKAVGHQWYWTYEYSDFNE--MEFDSYM--NNQLEENSMRLLDVDNRTVLPSNTFIRMIITSTDVIHS 157
Cdd:MTH00027 117 IMDEcGFSANITIKVTGHQWYWSYSYEDYGEknIEFDSYMipTADLEFGDLRLLEVDNRLILPVDTNVRVLITAADVLHS 196

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 749502631 158 WTLPSTGIKIDGTPGRLNQASMMLNRNGLIYGQCSEICGTNHSFMPIVVESVPINTFI 215
Cdd:MTH00027 197 WTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYI 254
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
92-209 8.93e-70

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 208.80  E-value: 8.93e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749502631   92 MTMKAVGHQWYWTYEYSDFNEMEFDSYM--NNQLEENSMRLLDVDNRTVLPSNTFIRMIITSTDVIHSWTLPSTGIKIDG 169
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMipTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 749502631  170 TPGRLNQASMMLNRNGLIYGQCSEICGTNHSFMPIVVESV 209
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 4-215 9.84e-68

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 207.55  E-value: 9.84e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749502631   4 MILQDSTSPLMEQLTFFHDHIMMILMMIVTTVSYTIIMLVTNKSTDRN**EGQMIELIWTVTPAMTLFFIATPSLRLLYL 83
Cdd:MTH00080   9 NFSNSLFSSYMDWFHNFNCSLLFGEFVLAFVVFLFLYLISNNFYFKSKKIEYQFGELLCSVFPVLILLMQMVPSLSLLYY 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749502631  84 MDEIN-NPMMTMKAVGHQWYWTYEYSDFNEMEFDSYMN--NQLEENSMRLLDVDNRTVLPSNTFIRMIITSTDVIHSWTL 160
Cdd:MTH00080  89 YGLMNlDSNLTVKVTGHQWYWSYEFSDIPGLEFDSYMKslDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWAL 168

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 749502631 161 PSTGIKIDGTPGRLNQASMMLNRNGLIYGQCSEICGTNHSFMPIVVESVPINTFI 215
Cdd:MTH00080 169 PSLSIKMDAMSGILSTLCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFK 223
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
3-210 6.70e-46

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 151.52  E-value: 6.70e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749502631   3 NMILQDSTSPLMEQLTFFHDhIMMILMMIVTTVsyTIIMLV---------TNKSTDRN**EGQMIELIWTVTPAMTLFFI 73
Cdd:COG1622   18 QLSLPDPAGPIAEEIDDLFW-VSLIIMLVIFVL--VFGLLLyfairyrrrKGDADPAQFHHNTKLEIVWTVIPIIIVIVL 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749502631  74 ATPSLRLLYLMDEINNPMMTMKAVGHQWYWTYEYSDFNEmefdsymnnqleensmrllDVDNRTVLPSNTFIRMIITSTD 153
Cdd:COG1622   95 AVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGI-------------------ATVNELVLPVGRPVRFLLTSAD 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 749502631 154 VIHSWTLPSTGIKIDGTPGRLNQASMMLNRNGLIYGQCSEICGTNHSFMPIVVESVP 210
Cdd:COG1622  156 VIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVS 212
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 54-209 4.12e-42

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 140.86  E-value: 4.12e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749502631  54 EGQMIELIWTVTPAMTLFFIAtpSLRLLYLMDEINNPMM-TMKAVGHQWYWTYEYSdfNEMEFDSYMNNQLeensmrlLD 132
Cdd:MTH00047  45 ENQVLELLWTVVPTLLVLVLC--FLNLNFITSDLDCFSSeTIKVIGHQWYWSYEYS--FGGSYDSFMTDDI-------FG 113

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 749502631 133 VDNRTVLPSNTFIRMIITSTDVIHSWTLPSTGIKIDGTPGRLNQASMMLNRNGLIYGQCSEICGTNHSFMPIVVESV 209
Cdd:MTH00047 114 VDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCPDRHGVFVGYCSELCGVGHSYMPIVIEVV 190
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 10-214 3.53e-40

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: 135.97  E-value: 3.53e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749502631   10 TSPLMEQLTFFHDhIMMILMMIVTTVSYTIIMLVT----NKSTDRN---**EGQMIELIWTVTPAMTLF-FIATPSLRLL 81
Cdd:TIGR02866   2 GGEIAQQIAFLFL-FVLAVSTLISLLVAALLAYVVwkfrRKGDEEKpsqIHGNRRLEYVWTVIPLIIVVgLFAATAKGLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749502631   82 YLMDEINNPMMTMKAVGHQWYWTYEYSDFnemefdsymnnqleensmrLLDVDNRTVLPSNTFIRMIITSTDVIHSWTLP 161
Cdd:TIGR02866  81 YLERPIPKDALKVKVTGYQWWWDFEYPES-------------------GFTTVNELVLPAGTPVELQVTSKDVIHSFWVP 141

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 749502631  162 STGIKIDGTPGRLNQASMMLNRNGLIYGQCSEICGTNHSFMPIVVESVPINTF 214
Cdd:TIGR02866 142 ELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEF 194
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 115-214 1.37e-36

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 125.70  E-value: 1.37e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749502631 115 FDSYM--NNQLEENSMRLLDVDNRTVLPSNTFIRMIITSTDVIHSWTLPSTGIKIDGTPGRLNQASMMLNRNGLIYGQCS 192
Cdd:PTZ00047  51 FQSNLvtDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCS 130

                         90       100
                 ....*....|....*....|..
gi 749502631 193 EICGTNHSFMPIVVESVPINTF 214
Cdd:PTZ00047 131 EMCGTLHGFMPIVVEAVSPEAY 152
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 92-207 1.41e-23

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: 90.05  E-value: 1.41e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749502631  92 MTMKAVGHQWYWTYEYSDFNemefdsymnnqleensmrlldVDNRTVLPSNTFIRMIITSTDVIHSWTLPSTGIKIDGTP 171
Cdd:cd13842    1 LTVYVTGVQWSWTFIYPNVR---------------------TPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDAVP 59

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 749502631 172 GRLNQASMMLNRNGLIYGQCSEICGTNHSFMPIVVE 207
Cdd:cd13842   60 GYTSELWFVADKPGTYTIICAEYCGLGHSYMLGKVE 95
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-80 1.42e-21

Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C oxidase contains two transmembrane alpha-helices.


Pssm-ID: 397083 [Multi-domain]  Cd Length: 89  Bit Score: 84.69  E-value: 1.42e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749502631    1 WPNMILQDSTSPLMEQLTFFHDHIMMILMMIVTTVSYTIIMLVT------NKSTDRN**EGQMIELIWTVTPAMTLFFIA 74
Cdd:pfam02790   4 PWGLGFQDAASPLMEGLLELHDYIMFILTLILILVLYILVTCLIrfnrrkNPITARYTTHGQTIEIIWTIIPAVILILIA 83


                  ....*.
gi 749502631   75 TPSLRL 80
Cdd:pfam02790  84 LPSFKL 89
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 92-202 1.76e-19

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: 79.59  E-value: 1.76e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749502631  92 MTMKAVGHQWYWTYEYSDFNEMEFdsymnnqleENSmrlldvdNRTVLPSNTFIRMIITSTDVIHSWTLPSTGIKIDGTP 171
Cdd:cd04213    2 LTIEVTGHQWWWEFRYPDEPGRGI---------VTA-------NELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMDMIP 65

                         90       100       110
                 ....*....|....*....|....*....|.
gi 749502631 172 GRLNQASMMLNRNGLIYGQCSEICGTNHSFM 202
Cdd:cd04213   66 GRTNRLWLQADEPGVYRGQCAEFCGASHALM 96
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 92-207 8.16e-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: 259986 [Multi-domain]  Cd Length: 107  Bit Score: 75.37  E-value: 8.16e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749502631  92 MTMKAVGHQWYWTYEYSDFNEMEfdsymNNQLEENSMRLldvdnrtVLPSNTFIRMIITSTDVIHSWTLPSTGIKIDGTP 171
Cdd:cd13919    2 LVVEVTAQQWAWTFRYPGGDGKL-----GTDDDVTSPEL-------HLPVGRPVLFNLRSKDVIHSFWVPEFRVKQDAVP 69

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 749502631 172 GRLNQASMMLNRNGLIYGQCSEICGTNHSFM--PIVVE 207
Cdd:cd13919   70 GRTTRLWFTPTREGEYEVRCAELCGLGHYRMraTVKVV 107
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 92-206 2.00e-16

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: 71.51  E-value: 2.00e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749502631  92 MTMKAVGHQWYWTYEYSdfnemefdsymNNQLEENSMrlldvdnrtVLPSNTFIRMIITSTDVIHSWTLPSTGIKIDGTP 171
Cdd:cd13915    2 LEIQVTGRQWMWEFTYP-----------NGKREINEL---------HVPVGKPVRLILTSKDVIHSFYVPAFRIKQDVVP 61

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 749502631 172 GRLNQASMMLNRNGLIYGQCSEICGTNHSFMPIVV 206
Cdd:cd13915   62 GRYTYLWFEATKPGEYDLFCTEYCGTGHSGMIGKV 96
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 80-214 9.58e-16

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: 70.95  E-value: 9.58e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749502631  80 LLYLMD---EINNPMMTMKAVGHQWYWTYEYSdfNEMEFDSYMnnqleensmrlldvdnrtVLPSNTFIRMIITSTDVIH 156
Cdd:cd13918   18 LLYVEDppdEADEDALEVEVEGFQFGWQFEYP--NGVTTGNTL------------------RVPADTPIALRVTSTDVFH 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 749502631 157 SWTLPSTGIKIDGTPGRLNQASMMLNRNGLIYGQCSEICGTNHSFMPIVVESVPINTF 214
Cdd:cd13918   78 TFGIPELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEF 135
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 93-214 2.11e-15

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: 69.36  E-value: 2.11e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 749502631  93 TMKAVGHQWYWTYEYSDFNemefdsymnnqleensmrlLDVDNRTVLPSNTFIRMIITSTDVIHSWTLPSTGIKIDGTPG 172
Cdd:cd13914    2 EIEVEAYQWGWEFSYPEAN-------------------VTTSEQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDAFPG 62

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 749502631 173 RLNQASMMLNRNGLIYGQCSEICGTNHSFMPIVVESVPINTF 214
Cdd:cd13914   63 QYNTIKTEATEEGEYQLYCAEYCGAGHSQMLSTVTVVSQDEY 104
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 135-207 4.62e-06

C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and some archaea, which catalyze the reduction of O2 and simultaneously pump protons across the membrane. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. The ba3 family contains oxidases that lack the conserved residues that form the D- and K-pathways in CcO and ubiquinol oxidase. Instead, they contain a potential alternative K-pathway. Additional proton channels have been proposed for this family of oxidases but none have been identified definitively.


Pssm-ID: 259980 [Multi-domain]  Cd Length: 99  Bit Score: 43.71  E-value: 4.62e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 749502631 135 NRTVLPSNTFIRMIITSTDVIHSWTLPSTGIKIDGTPGRLNQASMMLNRNGLIYGQCSEICGTNHSFM--PIVVE 207
Cdd:cd13913   25 NEIEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNMygKIIVE 99
 
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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