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Conserved domains on  [gi|81230446|ref|YP_398824|]
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cytochrome c oxidase subunit II (mitochondrion) [Leptotrombidium akamushi]

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 4.12e-100

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 289.42  E-value: 4.12e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81230446    1 MPIWQSIFLQNSSSPSMESLNFFHDHCMGILILILMISGGMAFFPLKTNNFSRFFEENEEMEIFWSTLPSIILIIIAIPS 80
Cdd:MTH00154   1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81230446   81 LKILYLLEETPNSNVTLKIIGSQWYWSYQMNESTK--FDSF------LEKGDFRLLSTSNFLSLPFKENIRVLISSTDVI 152
Cdd:MTH00154  81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNieFDSYmiptneLENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 81230446  153 HSWTLPSLGVKADAVPGRMNQLFFLSQNCGALFGQCSEICGAKHSFMPISTFFCPMTSFENQI 215
Cdd:MTH00154 161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWI 223
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-215 4.12e-100

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 289.42  E-value: 4.12e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81230446    1 MPIWQSIFLQNSSSPSMESLNFFHDHCMGILILILMISGGMAFFPLKTNNFSRFFEENEEMEIFWSTLPSIILIIIAIPS 80
Cdd:MTH00154   1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81230446   81 LKILYLLEETPNSNVTLKIIGSQWYWSYQMNESTK--FDSF------LEKGDFRLLSTSNFLSLPFKENIRVLISSTDVI 152
Cdd:MTH00154  81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNieFDSYmiptneLENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 81230446  153 HSWTLPSLGVKADAVPGRMNQLFFLSQNCGALFGQCSEICGAKHSFMPISTFFCPMTSFENQI 215
Cdd:MTH00154 161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWI 223
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 93-213 7.40e-59

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: 181.23  E-value: 7.40e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81230446  93 SNVTLKIIGSQWYWSYQM--NESTKFDSF------LEKGDFRLLSTSNFLSLPFKENIRVLISSTDVIHSWTLPSLGVKA 164
Cdd:cd13912   1 PSLTIKAIGHQWYWSYEYsdFNDLEFDSYmipeddLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 81230446 165 DAVPGRMNQLFFLSQNCGALFGQCSEICGAKHSFMPISTFFCPMTSFEN 213
Cdd:cd13912  81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLS 129
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
96-201 3.42e-50

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 159.11  E-value: 3.42e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81230446    96 TLKIIGSQWYWSYQMN--ESTKFDSF------LEKGDFRLLSTSNFLSLPFKENIRVLISSTDVIHSWTLPSLGVKADAV 167
Cdd:pfam00116   2 TIKAIGHQWYWSYEYTdfGDLEFDSYmiptedLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDAV 81

                          90       100       110
                  ....*....|....*....|....*....|....
gi 81230446   168 PGRMNQLFFLSQNCGALFGQCSEICGAKHSFMPI 201
Cdd:pfam00116  82 PGRLNQTSFSIDREGVFYGQCSEICGINHSFMPI 115
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
1-201 7.99e-31

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 113.00  E-value: 7.99e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81230446   1 MPIWQSIFLQNSSSPSMESLNFFHDHCMGI-LILILMISGGMAFFPLK-----TNNFSRFFEENEEMEIFWSTLPSIILI 74
Cdd:COG1622  13 LLLSGQLSLPDPAGPIAEEIDDLFWVSLIImLVIFVLVFGLLLYFAIRyrrrkGDADPAQFHHNTKLEIVWTVIPIIIVI 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81230446  75 IIAIPSLKILYLLEETPNSNVTLKIIGSQWYWSYqmnestkfdSFLEKGDFrllsTSNFLSLPFKENIRVLISSTDVIHS 154
Cdd:COG1622  93 VLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLF---------RYPDQGIA----TVNELVLPVGRPVRFLLTSADVIHS 159

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 81230446 155 WTLPSLGVKADAVPGRMNQLFFLSQNCGALFGQCSEICGAKHSFMPI 201
Cdd:COG1622 160 FWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRF 206
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 14-201 1.87e-30

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: 110.93  E-value: 1.87e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81230446    14 SPSMESLNFFHDHCM--GILILILMIsGGMAFFPLKTNNFSR-----FFEENEEMEIFWS-TLPSIILIIIAIPSLKILY 85
Cdd:TIGR02866   3 GEIAQQIAFLFLFVLavSTLISLLVA-ALLAYVVWKFRRKGDeekpsQIHGNRRLEYVWTvIPLIIVVGLFAATAKGLLY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81230446    86 LLEETPNSNVTLKIIGSQWYWSYQMNESTkfdsflekgdfrlLSTSNFLSLPFKENIRVLISSTDVIHSWTLPSLGVKAD 165
Cdd:TIGR02866  82 LERPIPKDALKVKVTGYQWWWDFEYPESG-------------FTTVNELVLPAGTPVELQVTSKDVIHSFWVPELGGKID 148

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 81230446   166 AVPGRMNQLFFLSQNCGALFGQCSEICGAKHSFMPI 201
Cdd:TIGR02866 149 AIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLF 184
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-215 4.12e-100

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 289.42  E-value: 4.12e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81230446    1 MPIWQSIFLQNSSSPSMESLNFFHDHCMGILILILMISGGMAFFPLKTNNFSRFFEENEEMEIFWSTLPSIILIIIAIPS 80
Cdd:MTH00154   1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81230446   81 LKILYLLEETPNSNVTLKIIGSQWYWSYQMNESTK--FDSF------LEKGDFRLLSTSNFLSLPFKENIRVLISSTDVI 152
Cdd:MTH00154  81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNieFDSYmiptneLENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 81230446  153 HSWTLPSLGVKADAVPGRMNQLFFLSQNCGALFGQCSEICGAKHSFMPISTFFCPMTSFENQI 215
Cdd:MTH00154 161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWI 223
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-213 1.05e-75

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 227.56  E-value: 1.05e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81230446    1 MPIWQSIFLQNSSSPSMESLNFFHDHCMGILILILMISGGMAFFPLKTNNFSRFFEENEEMEIFWSTLPSIILIIIAIPS 80
Cdd:MTH00168   1 MATYSQLGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81230446   81 LKILYLLEETPNSNVTLKIIGSQWYWSYQMNE--STKFDSF------LEKGDFRLLSTSNFLSLPFKENIRVLISSTDVI 152
Cdd:MTH00168  81 LRLLYLMDEIDKPDLTIKAVGHQWYWSYEYTDynDLEFDSYmvptqdLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 81230446  153 HSWTLPSLGVKADAVPGRMNQLFFLSQNCGALFGQCSEICGAKHSFMPISTFFCPMTSFEN 213
Cdd:MTH00168 161 HSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFEN 221
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-216 1.97e-75

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 226.91  E-value: 1.97e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81230446    1 MPIWQSIFLQNSSSPSMESLNFFHDHCMGILILILMISGGMAFFPLKTNNFSRFFEENEEMEIFWSTLPSIILIIIAIPS 80
Cdd:MTH00139   1 MAYWGQLGFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81230446   81 LKILYLLEETPNSNVTLKIIGSQWYWSYQMN--ESTKFDSF------LEKGDFRLLSTSNFLSLPFKENIRVLISSTDVI 152
Cdd:MTH00139  81 LRLLYLMDEVSDPYLTFKAVGHQWYWSYEYSdfKNLSFDSYmiptedLSSGEFRLLEVDNRLVLPYKSNIRALITAADVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 81230446  153 HSWTLPSLGVKADAVPGRMNQLFFLSQNCGALFGQCSEICGAKHSFMPISTFFCPMTSFENQIL 216
Cdd:MTH00139 161 HSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEWIL 224
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-213 5.06e-75

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 225.97  E-value: 5.06e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81230446    1 MPIWQSIFLQNSSSPSMESLNFFHDHCMGILILILMISGGMAFFPLKTNNFSRFFEENEEMEIFWSTLPSIILIIIAIPS 80
Cdd:MTH00140   1 MSYWGQLGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81230446   81 LKILYLLEETPNSNVTLKIIGSQWYWSYQMNEST--KFDSF------LEKGDFRLLSTSNFLSLPFKENIRVLISSTDVI 152
Cdd:MTH00140  81 LRLLYLLDETNNPLLTVKAIGHQWYWSYEYSDFSviEFDSYmvpeneLELGDFRLLEVDNRLVLPYSVDTRVLVTSADVI 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 81230446  153 HSWTLPSLGVKADAVPGRMNQLFFLSQNCGALFGQCSEICGAKHSFMPISTFFCPMTSFEN 213
Cdd:MTH00140 161 HSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVK 221
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-215 9.73e-69

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 209.94  E-value: 9.73e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81230446    1 MPIWQSIFLQNSSSPSMESLNFFHDHCMGILILI-LMISGGMAFFPLKTNNFsRFFEENEEMEIFWSTLPSIILIIIAIP 79
Cdd:MTH00038   1 MATWLQLGLQDASSPLMEELIYFHDYALIILTLItILVFYGLASLLFSSPTN-RFFLEGQELETIWTIVPAFILIFIALP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81230446   80 SLKILYLLEETPNSNVTLKIIGSQWYWSYQM--NESTKFDSF------LEKGDFRLLSTSNFLSLPFKENIRVLISSTDV 151
Cdd:MTH00038  80 SLQLLYLMDEVNNPFLTIKAIGHQWYWSYEYtdYNDLEFDSYmvptsdLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADV 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 81230446  152 IHSWTLPSLGVKADAVPGRMNQLFFLSQNCGALFGQCSEICGAKHSFMPISTFFCPMTSFENQI 215
Cdd:MTH00038 160 LHSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWV 223
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 9-213 2.63e-68

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 208.61  E-value: 2.63e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81230446    9 LQNSSSPSMESLNFFHDHCMGILILI----LMISGGMAFFPLKTNNFsrffEENEEMEIFWSTLPSIILIIIAIPSLKIL 84
Cdd:MTH00117   9 FQDASSPIMEELLFFHDHALMVALLIsslvLYLLTLMLTTKLTHTNT----VDAQEVELIWTILPAIVLILLALPSLRIL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81230446   85 YLLEETPNSNVTLKIIGSQWYWSYQM--NESTKFDSF------LEKGDFRLLSTSNFLSLPFKENIRVLISSTDVIHSWT 156
Cdd:MTH00117  85 YLMDEINNPHLTIKAIGHQWYWSYEYtdYKDLSFDSYmiptqdLPNGHFRLLEVDHRMVIPMESPIRILITAEDVLHSWA 164

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 81230446  157 LPSLGVKADAVPGRMNQLFFLSQNCGALFGQCSEICGAKHSFMPISTFFCPMTSFEN 213
Cdd:MTH00117 165 VPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFEN 221
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-216 2.59e-64

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 198.93  E-value: 2.59e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81230446    1 MPIWQSIFLQNSSSPSMESLNFFHDHCMGILILILMISGgMAFFPLKTNNFS-RFFEENEEMEIFWSTLPSIILIIIAIP 79
Cdd:MTH00008   1 MPHWGQLMFQDAASPVMLQLISFHDHALLILTLVLTVVG-YAMTSLMFNKLSnRYILEAQQIETIWTILPALILLFLAFP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81230446   80 SLKILYLLEETPNSNVTLKIIGSQWYWSYQMNE--STKFDSF------LEKGDFRLLSTSNFLSLPFKENIRVLISSTDV 151
Cdd:MTH00008  80 SLRLLYLMDEVSNPSITLKTIGHQWYWSYEYSDfsNLEFDSYmlptsdLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADV 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 81230446  152 IHSWTLPSLGVKADAVPGRMNQLFFLSQNCGALFGQCSEICGAKHSFMPISTFFCPMTSFENQIL 216
Cdd:MTH00008 160 IHSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKWVS 224
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 4-216 1.96e-60

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 189.19  E-value: 1.96e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81230446    4 WQSIFlQNSSSPSMESLNFFHDHCMGILILILMISGGMAFFPLKTNNFSRFFEENEEMEIFWSTLPSIILIIIAIPSLKI 83
Cdd:MTH00023  14 WQLGF-QDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKL 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81230446   84 LYLLEETPNSNVTLKIIGSQWYWSYQMN----ESTKFDSF------LEKGDFRLLSTSNFLSLPFKENIRVLISSTDVIH 153
Cdd:MTH00023  93 LYLMDEVVSPALTIKAIGHQWYWSYEYSdyegETLEFDSYmvptsdLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLH 172

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 81230446  154 SWTLPSLGVKADAVPGRMNQLFFLSQNCGALFGQCSEICGAKHSFMPISTFFCPMTSFENQIL 216
Cdd:MTH00023 173 SFAVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWLL 235
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 9-213 4.35e-60

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 188.17  E-value: 4.35e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81230446    9 LQNSSSPSMESLNFFHDHCMGILILILMISGGMAFFPLKTNNFSRFFEENEEMEIFWSTLPSIILIIIAIPSLKILYLLE 88
Cdd:MTH00185   9 LQDAASPVMEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPSLRILYLMD 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81230446   89 ETPNSNVTLKIIGSQWYWSYQMN--ESTKFDSF------LEKGDFRLLSTSNFLSLPFKENIRVLISSTDVIHSWTLPSL 160
Cdd:MTH00185  89 EINDPHLTIKAMGHQWYWSYEYTdyEQLEFDSYmtptqdLTPGQFRLLETDHRMVVPMESPIRVLITAEDVLHSWTVPAL 168

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 81230446  161 GVKADAVPGRMNQLFFLSQNCGALFGQCSEICGAKHSFMPISTFFCPMTSFEN 213
Cdd:MTH00185 169 GVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFEN 221
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 93-213 7.40e-59

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: 181.23  E-value: 7.40e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81230446  93 SNVTLKIIGSQWYWSYQM--NESTKFDSF------LEKGDFRLLSTSNFLSLPFKENIRVLISSTDVIHSWTLPSLGVKA 164
Cdd:cd13912   1 PSLTIKAIGHQWYWSYEYsdFNDLEFDSYmipeddLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 81230446 165 DAVPGRMNQLFFLSQNCGALFGQCSEICGAKHSFMPISTFFCPMTSFEN 213
Cdd:cd13912  81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLS 129
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 9-213 1.42e-58

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 184.15  E-value: 1.42e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81230446    9 LQNSSSPSMESLNFFHDHCMGILILI--LMISGGMAFFPLKTNNfsRFFEENEEMEIFWSTLPSIILIIIAIPSLKILYL 86
Cdd:MTH00129   9 FQDAASPVMEELLHFHDHALMIVFLIstLVLYIIVAMVSTKLTN--KYILDSQEIEIIWTVLPAVILILIALPSLRILYL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81230446   87 LEETPNSNVTLKIIGSQWYWSYQMN--ESTKFDSF------LEKGDFRLLSTSNFLSLPFKENIRVLISSTDVIHSWTLP 158
Cdd:MTH00129  87 MDEINDPHLTIKAMGHQWYWSYEYTdyEDLGFDSYmiptqdLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVLHSWAVP 166

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 81230446  159 SLGVKADAVPGRMNQLFFLSQNCGALFGQCSEICGAKHSFMPISTFFCPMTSFEN 213
Cdd:MTH00129 167 ALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFEN 221
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 9-213 3.72e-58

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 183.00  E-value: 3.72e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81230446    9 LQNSSSPSMESLNFFHDHCMGILILI----LMISGGMaffpLKTNNFSRFFEENEEMEIFWSTLPSIILIIIAIPSLKIL 84
Cdd:MTH00098   9 FQDATSPIMEELLHFHDHTLMIVFLIsslvLYIISLM----LTTKLTHTSTMDAQEVETIWTILPAIILILIALPSLRIL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81230446   85 YLLEETPNSNVTLKIIGSQWYWSYQMN--ESTKFDS------FLEKGDFRLLSTSNFLSLPFKENIRVLISSTDVIHSWT 156
Cdd:MTH00098  85 YMMDEINNPSLTVKTMGHQWYWSYEYTdyEDLSFDSymiptsDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVLHSWA 164

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 81230446  157 LPSLGVKADAVPGRMNQLFFLSQNCGALFGQCSEICGAKHSFMPISTFFCPMTSFEN 213
Cdd:MTH00098 165 VPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEK 221
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 4-201 1.04e-57

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 182.29  E-value: 1.04e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81230446    4 WQSIFlQNSSSPSMESLNFFHDHCMGILILILMISGGMAFFPLKTNNFSRFFEENEEMEIFWSTLPSIILIIIAIPSLKI 83
Cdd:MTH00051   7 WQLGF-QDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSLKL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81230446   84 LYLLEETPNSNVTLKIIGSQWYWSYQMN----ESTKFDSF------LEKGDFRLLSTSNFLSLPFKENIRVLISSTDVIH 153
Cdd:MTH00051  86 LYLMDEVIDPALTIKAIGHQWYWSYEYSdygtDTIEFDSYmiptsdLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLH 165

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 81230446  154 SWTLPSLGVKADAVPGRMNQLFFLSQNCGALFGQCSEICGAKHSFMPI 201
Cdd:MTH00051 166 SFAVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPI 213
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 9-213 3.45e-53

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 170.34  E-value: 3.45e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81230446    9 LQNSSSPSMESLNFFHDHCMGILILILM-----ISGGMAFFPLKTNNFsrffeENEEMEIFWSTLPSIILIIIAIPSLKI 83
Cdd:MTH00076   9 FQDAASPIMEELLHFHDHALMAVFLISTlvlyiITIMMTTKLTNTNTM-----DAQEIEMVWTIMPAIILIVIALPSLRI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81230446   84 LYLLEETPNSNVTLKIIGSQWYWSYQMN--ESTKFDSF------LEKGDFRLLSTSNFLSLPFKENIRVLISSTDVIHSW 155
Cdd:MTH00076  84 LYLMDEINDPHLTVKAIGHQWYWSYEYTdyEDLSFDSYmiptqdLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVLHSW 163

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 81230446  156 TLPSLGVKADAVPGRMNQLFFLSQNCGALFGQCSEICGAKHSFMPISTFFCPMTSFEN 213
Cdd:MTH00076 164 AVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLN 221
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
96-201 3.42e-50

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 159.11  E-value: 3.42e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81230446    96 TLKIIGSQWYWSYQMN--ESTKFDSF------LEKGDFRLLSTSNFLSLPFKENIRVLISSTDVIHSWTLPSLGVKADAV 167
Cdd:pfam00116   2 TIKAIGHQWYWSYEYTdfGDLEFDSYmiptedLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDAV 81

                          90       100       110
                  ....*....|....*....|....*....|....
gi 81230446   168 PGRMNQLFFLSQNCGALFGQCSEICGAKHSFMPI 201
Cdd:pfam00116  82 PGRLNQTSFSIDREGVFYGQCSEICGINHSFMPI 115
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 4-201 7.47e-46

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 152.87  E-value: 7.47e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81230446    4 WQSIFlQNSSSPSMESLNFFHDHCMGILILILMISGGMAFFPLKTNNFSRFFEENEE---MEIFWSTLPSIILIIIAIPS 80
Cdd:MTH00027  33 WQLGF-QDAGSPVMEEIIMLHDQILFILTIIVGVVLWLIIRILLGNNYYSYYWNKLDgslIEVIWTLIPAFILILIAFPS 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81230446   81 LKILYLLEETP-NSNVTLKIIGSQWYWSYQMNE----STKFDSF------LEKGDFRLLSTSNFLSLPFKENIRVLISST 149
Cdd:MTH00027 112 LRLLYIMDECGfSANITIKVTGHQWYWSYSYEDygekNIEFDSYmiptadLEFGDLRLLEVDNRLILPVDTNVRVLITAA 191

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 81230446  150 DVIHSWTLPSLGVKADAVPGRMNQLFFLSQNCGALFGQCSEICGAKHSFMPI 201
Cdd:MTH00027 192 DVLHSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPI 243
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 8-213 1.03e-41

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 140.92  E-value: 1.03e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81230446    8 FLQNSSSPSMESLNFFHDHCM-GILILILMISGGMAFFpLKTNNFSRFFEENEEMEIFWSTLPSIILIIIAIPSLKILYL 86
Cdd:MTH00080  10 FSNSLFSSYMDWFHNFNCSLLfGEFVLAFVVFLFLYLI-SNNFYFKSKKIEYQFGELLCSVFPVLILLMQMVPSLSLLYY 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81230446   87 LEETP-NSNVTLKIIGSQWYWSYQMNESTK--FDSF------LEKGDFRLLSTSNFLSLPFKENIRVLISSTDVIHSWTL 157
Cdd:MTH00080  89 YGLMNlDSNLTVKVTGHQWYWSYEFSDIPGleFDSYmksldqLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWAL 168

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 81230446  158 PSLGVKADAVPGRMNQLFFLSQNCGALFGQCSEICGAKHSFMPISTFFCPMTSFEN 213
Cdd:MTH00080 169 PSLSIKMDAMSGILSTLCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKE 224
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 93-201 4.67e-33

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 117.75  E-value: 4.67e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81230446   93 SNVTLKIIGSQWYWSYQMNESTKFDSFLEKGDFrllSTSNFLSLPFKENIRVLISSTDVIHSWTLPSLGVKADAVPGRMN 172
Cdd:MTH00047  80 SSETIKVIGHQWYWSYEYSFGGSYDSFMTDDIF---GVDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRIN 156

                         90       100
                 ....*....|....*....|....*....
gi 81230446  173 QLFFLSQNCGALFGQCSEICGAKHSFMPI 201
Cdd:MTH00047 157 HLFFCPDRHGVFVGYCSELCGVGHSYMPI 185
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 105-201 7.46e-31

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 111.07  E-value: 7.46e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81230446  105 YWSYQMNESTKFDsfLEKGDFRLLSTSNFLSLPFKENIRVLISSTDVIHSWTLPSLGVKADAVPGRMNQLFFLSQNCGAL 184
Cdd:PTZ00047  48 YYSFQSNLVTDED--LKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVF 125

                         90
                 ....*....|....*..
gi 81230446  185 FGQCSEICGAKHSFMPI 201
Cdd:PTZ00047 126 YGQCSEMCGTLHGFMPI 142
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
1-201 7.99e-31

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 113.00  E-value: 7.99e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81230446   1 MPIWQSIFLQNSSSPSMESLNFFHDHCMGI-LILILMISGGMAFFPLK-----TNNFSRFFEENEEMEIFWSTLPSIILI 74
Cdd:COG1622  13 LLLSGQLSLPDPAGPIAEEIDDLFWVSLIImLVIFVLVFGLLLYFAIRyrrrkGDADPAQFHHNTKLEIVWTVIPIIIVI 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81230446  75 IIAIPSLKILYLLEETPNSNVTLKIIGSQWYWSYqmnestkfdSFLEKGDFrllsTSNFLSLPFKENIRVLISSTDVIHS 154
Cdd:COG1622  93 VLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLF---------RYPDQGIA----TVNELVLPVGRPVRFLLTSADVIHS 159

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 81230446 155 WTLPSLGVKADAVPGRMNQLFFLSQNCGALFGQCSEICGAKHSFMPI 201
Cdd:COG1622 160 FWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRF 206
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 14-201 1.87e-30

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: 110.93  E-value: 1.87e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81230446    14 SPSMESLNFFHDHCM--GILILILMIsGGMAFFPLKTNNFSR-----FFEENEEMEIFWS-TLPSIILIIIAIPSLKILY 85
Cdd:TIGR02866   3 GEIAQQIAFLFLFVLavSTLISLLVA-ALLAYVVWKFRRKGDeekpsQIHGNRRLEYVWTvIPLIIVVGLFAATAKGLLY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81230446    86 LLEETPNSNVTLKIIGSQWYWSYQMNESTkfdsflekgdfrlLSTSNFLSLPFKENIRVLISSTDVIHSWTLPSLGVKAD 165
Cdd:TIGR02866  82 LERPIPKDALKVKVTGYQWWWDFEYPESG-------------FTTVNELVLPAGTPVELQVTSKDVIHSFWVPELGGKID 148

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 81230446   166 AVPGRMNQLFFLSQNCGALFGQCSEICGAKHSFMPI 201
Cdd:TIGR02866 149 AIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLF 184
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 95-199 2.49e-22

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: 87.29  E-value: 2.49e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81230446  95 VTLKIIGSQWYWSYQMnestkfdsflEKGDFRLLSTSNFLSLPFKENIRVLISSTDVIHSWTLPSLGVKADAVPGRMNQL 174
Cdd:cd04213   2 LTIEVTGHQWWWEFRY----------PDEPGRGIVTANELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMDMIPGRTNRL 71

                        90       100
                ....*....|....*....|....*
gi 81230446 175 FFLSQNCGALFGQCSEICGAKHSFM 199
Cdd:cd04213  72 WLQADEPGVYRGQCAEFCGASHALM 96
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 95-200 3.17e-22

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: 86.58  E-value: 3.17e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81230446  95 VTLKIIGSQWYWSYQMNESTkfdsflekgdfrllsTSNFLSLPFKENIRVLISSTDVIHSWTLPSLGVKADAVPGRMNQL 174
Cdd:cd13842   1 LTVYVTGVQWSWTFIYPNVR---------------TPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDAVPGYTSEL 65

                        90       100
                ....*....|....*....|....*.
gi 81230446 175 FFLSQNCGALFGQCSEICGAKHSFMP 200
Cdd:cd13842  66 WFVADKPGTYTIICAEYCGLGHSYML 91
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-199 4.42e-19

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: 78.84  E-value: 4.42e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81230446  95 VTLKIIGSQWYWSYQMNESTkfdsflEKGDFRLLSTSNFLSLPFKENIRVLISSTDVIHSWTLPSLGVKADAVPGRMNQL 174
Cdd:cd13919   2 LVVEVTAQQWAWTFRYPGGD------GKLGTDDDVTSPELHLPVGRPVLFNLRSKDVIHSFWVPEFRVKQDAVPGRTTRL 75

                        90       100
                ....*....|....*....|....*
gi 81230446 175 FFLSQNCGALFGQCSEICGAKHSFM 199
Cdd:cd13919  76 WFTPTREGEYEVRCAELCGLGHYRM 100
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 96-199 3.78e-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: 259982 [Multi-domain]  Cd Length: 98  Bit Score: 76.13  E-value: 3.78e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81230446  96 TLKIIGSQWYWSyqmnestkfdsFLEKGDFRllsTSNFLSLPFKENIRVLISSTDVIHSWTLPSLGVKADAVPGRMNQLF 175
Cdd:cd13915   3 EIQVTGRQWMWE-----------FTYPNGKR---EINELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQDVVPGRYTYLW 68

                        90       100
                ....*....|....*....|....
gi 81230446 176 FLSQNCGALFGQCSEICGAKHSFM 199
Cdd:cd13915  69 FEATKPGEYDLFCTEYCGTGHSGM 92
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-199 5.66e-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: 259981 [Multi-domain]  Cd Length: 108  Bit Score: 70.90  E-value: 5.66e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81230446  95 VTLKIIGSQWYWSYQMNESTkfdsflekgdfrlLSTSNFLSLPFKENIRVLISSTDVIHSWTLPSLGVKADAVPGRMNQL 174
Cdd:cd13914   1 VEIEVEAYQWGWEFSYPEAN-------------VTTSEQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDAFPGQYNTI 67

                        90       100
                ....*....|....*....|....*
gi 81230446 175 FFLSQNCGALFGQCSEICGAKHSFM 199
Cdd:cd13914  68 KTEATEEGEYQLYCAEYCGAGHSQM 92
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 83-199 6.82e-14

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: 65.94  E-value: 6.82e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81230446  83 ILYLlEETPNSN----VTLKIIGSQWYWSYQM-NESTkfdsflekgdfrllsTSNFLSLPFKENIRVLISSTDVIHSWTL 157
Cdd:cd13918  18 LLYV-EDPPDEAdedaLEVEVEGFQFGWQFEYpNGVT---------------TGNTLRVPADTPIALRVTSTDVFHTFGI 81

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 81230446 158 PSLGVKADAVPGRMNQLFFLSQNCGALFGQCSEICGAKHSFM 199
Cdd:cd13918  82 PELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLM 123
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-76 3.15e-06

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: 43.86  E-value: 3.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81230446     1 MPIWQSIFLQNSSSPSMESLNFFHDHCMGILILILMISGGMAFFPLKTNNFS------RFFEENEEMEIFWSTLPSIILI 74
Cdd:pfam02790   1 MPTPWGLGFQDAASPLMEGLLELHDYIMFILTLILILVLYILVTCLIRFNRRknpitaRYTTHGQTIEIIWTIIPAVILI 80


                  ..
gi 81230446    75 II 76
Cdd:pfam02790  81 LI 82
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 130-199 6.44e-03

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: 34.85  E-value: 6.44e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81230446 130 TSNFLSLPFKENIRVLISSTDVIHSWTLPSLGVKADAVPGRMNQLFFLSQNCGALFGQCSEICGAKHSFM 199
Cdd:cd13913  23 NPNEIEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNM 92
 
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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