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Conserved domains on  [gi|5835740|ref|NP_008552|]
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cytochrome c oxidase subunit II (mitochondrion) [Chrysemys picta]

Protein Classification

cytochrome c oxidase subunit II( domain architecture ID 11475905)

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 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-226 6.69e-173

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 474.02  E-value: 6.69e-173
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835740     1 MAHPLLLGFQDAMSPIMEELLHFHDHTLMIVFLISTMVLYIITLMMTTKLTYTNTMNAQEVEMIWTILPAIVLITIALPS 80
Cdd:MTH00117   1 MANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835740    81 LRVLYLMDEINNPHLTIKAMGHQWYWTYEYTDYENLEFDSYMTPTQTLPNGHFRLLEVDHRMVMPMESPIRMLISAEDVL 160
Cdd:MTH00117  81 LRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5835740   161 HSWAVPSLGVKTDAVPGRLNQATFIVTRPGVFYGQCSEICGANHSFMPIVIESVPLWHFENWSSLM 226
Cdd:MTH00117 161 HSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSLL 226
 
Name Accession Description Interval E-value
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-226 6.69e-173

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 474.02  E-value: 6.69e-173
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835740     1 MAHPLLLGFQDAMSPIMEELLHFHDHTLMIVFLISTMVLYIITLMMTTKLTYTNTMNAQEVEMIWTILPAIVLITIALPS 80
Cdd:MTH00117   1 MANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835740    81 LRVLYLMDEINNPHLTIKAMGHQWYWTYEYTDYENLEFDSYMTPTQTLPNGHFRLLEVDHRMVMPMESPIRMLISAEDVL 160
Cdd:MTH00117  81 LRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5835740   161 HSWAVPSLGVKTDAVPGRLNQATFIVTRPGVFYGQCSEICGANHSFMPIVIESVPLWHFENWSSLM 226
Cdd:MTH00117 161 HSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSLL 226
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 93-222 4.72e-92

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: 265.97  E-value: 4.72e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835740   93 PHLTIKAMGHQWYWTYEYTDYENLEFDSYMTPTQTLPNGHFRLLEVDHRMVMPMESPIRMLISAEDVLHSWAVPSLGVKT 172
Cdd:cd13912   1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 5835740  173 DAVPGRLNQATFIVTRPGVFYGQCSEICGANHSFMPIVIESVPLWHFENW 222
Cdd:cd13912  81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-214 3.78e-85

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 248.09  E-value: 3.78e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835740     95 LTIKAMGHQWYWTYEYTDYENLEFDSYMTPTQTLPNGHFRLLEVDHRMVMPMESPIRMLISAEDVLHSWAVPSLGVKTDA 174
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 5835740    175 VPGRLNQATFIVTRPGVFYGQCSEICGANHSFMPIVIESV 214
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
7-222 2.74e-52

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 168.47  E-value: 2.74e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835740    7 LGFQDAMSPIMEELLHFHDHTL--MIVFLISTMVLYIITL---------MMTTKLTYTNTmnaqeVEMIWTILPAIVLIT 75
Cdd:COG1622  19 LSLPDPAGPIAEEIDDLFWVSLiiMLVIFVLVFGLLLYFAiryrrrkgdADPAQFHHNTK-----LEIVWTVIPIIIVIV 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835740   76 IALPSLRVLYLMDEINNPHLTIKAMGHQWYWTYEYTDYENLefdsymtptqtlpnghfrlleVDHRMVMPMESPIRMLIS 155
Cdd:COG1622  94 LAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIA---------------------TVNELVLPVGRPVRFLLT 152

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 5835740  156 AEDVLHSWAVPSLGVKTDAVPGRLNQATFIVTRPGVFYGQCSEICGANHSFMPIVIESVPLWHFENW 222
Cdd:COG1622 153 SADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAW 219
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 14-222 1.93e-39

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: 134.82  E-value: 1.93e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835740     14 SPIMEELlhFHDHTLMIVFLISTMVLyIITLMMTTKLTYTNTMNAQE---------VEMIWTILPA-IVLITIALPSLRV 83
Cdd:TIGR02866   3 GEIAQQI--AFLFLFVLAVSTLISLL-VAALLAYVVWKFRRKGDEEKpsqihgnrrLEYVWTVIPLiIVVGLFAATAKGL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835740     84 LYLMDEINNPHLTIKAMGHQWYWTYEYtdyenlefdsymtptqtlPNGHFRlleVDHRMVMPMESPIRMLISAEDVLHSW 163
Cdd:TIGR02866  80 LYLERPIPKDALKVKVTGYQWWWDFEY------------------PESGFT---TVNELVLPAGTPVELQVTSKDVIHSF 138

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 5835740    164 AVPSLGVKTDAVPGRLNQATFIVTRPGVFYGQCSEICGANHSFMPIVIESVPLWHFENW 222
Cdd:TIGR02866 139 WVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAY 197
 
Name Accession Description Interval E-value
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-226 6.69e-173

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 474.02  E-value: 6.69e-173
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835740     1 MAHPLLLGFQDAMSPIMEELLHFHDHTLMIVFLISTMVLYIITLMMTTKLTYTNTMNAQEVEMIWTILPAIVLITIALPS 80
Cdd:MTH00117   1 MANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835740    81 LRVLYLMDEINNPHLTIKAMGHQWYWTYEYTDYENLEFDSYMTPTQTLPNGHFRLLEVDHRMVMPMESPIRMLISAEDVL 160
Cdd:MTH00117  81 LRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5835740   161 HSWAVPSLGVKTDAVPGRLNQATFIVTRPGVFYGQCSEICGANHSFMPIVIESVPLWHFENWSSLM 226
Cdd:MTH00117 161 HSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSLL 226
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 1-226 2.17e-155

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 429.90  E-value: 2.17e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835740     1 MAHPLLLGFQDAMSPIMEELLHFHDHTLMIVFLISTMVLYIITLMMTTKLTYTNTMNAQEVEMIWTILPAIVLITIALPS 80
Cdd:MTH00129   1 MAHPSQLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835740    81 LRVLYLMDEINNPHLTIKAMGHQWYWTYEYTDYENLEFDSYMTPTQTLPNGHFRLLEVDHRMVMPMESPIRMLISAEDVL 160
Cdd:MTH00129  81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5835740   161 HSWAVPSLGVKTDAVPGRLNQATFIVTRPGVFYGQCSEICGANHSFMPIVIESVPLWHFENWSSLM 226
Cdd:MTH00129 161 HSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLM 226
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-226 3.44e-154

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 426.83  E-value: 3.44e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835740     1 MAHPLLLGFQDAMSPIMEELLHFHDHTLMIVFLISTMVLYIITLMMTTKLTYTNTMNAQEVEMIWTILPAIVLITIALPS 80
Cdd:MTH00098   1 MAYPFQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835740    81 LRVLYLMDEINNPHLTIKAMGHQWYWTYEYTDYENLEFDSYMTPTQTLPNGHFRLLEVDHRMVMPMESPIRMLISAEDVL 160
Cdd:MTH00098  81 LRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5835740   161 HSWAVPSLGVKTDAVPGRLNQATFIVTRPGVFYGQCSEICGANHSFMPIVIESVPLWHFENWSSLM 226
Cdd:MTH00098 161 HSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKWSASM 226
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 1-226 1.86e-149

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 414.95  E-value: 1.86e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835740     1 MAHPLLLGFQDAMSPIMEELLHFHDHTLMIVFLISTMVLYIITLMMTTKLTYTNTMNAQEVEMIWTILPAIVLITIALPS 80
Cdd:MTH00076   1 MAHPSQLGFQDAASPIMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835740    81 LRVLYLMDEINNPHLTIKAMGHQWYWTYEYTDYENLEFDSYMTPTQTLPNGHFRLLEVDHRMVMPMESPIRMLISAEDVL 160
Cdd:MTH00076  81 LRILYLMDEINDPHLTVKAIGHQWYWSYEYTDYEDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5835740   161 HSWAVPSLGVKTDAVPGRLNQATFIVTRPGVFYGQCSEICGANHSFMPIVIESVPLWHFENWSSLM 226
Cdd:MTH00076 161 HSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLNWSSSM 226
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 1-227 1.78e-144

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 402.34  E-value: 1.78e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835740     1 MAHPLLLGFQDAMSPIMEELLHFHDHTLMIVFLISTMVLYIITLMMTTKLTYTNTMNAQEVEMIWTILPAIVLITIALPS 80
Cdd:MTH00185   1 MAHPSQLGLQDAASPVMEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835740    81 LRVLYLMDEINNPHLTIKAMGHQWYWTYEYTDYENLEFDSYMTPTQTLPNGHFRLLEVDHRMVMPMESPIRMLISAEDVL 160
Cdd:MTH00185  81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 5835740   161 HSWAVPSLGVKTDAVPGRLNQATFIVTRPGVFYGQCSEICGANHSFMPIVIESVPLWHFENWSSLMF 227
Cdd:MTH00185 161 HSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLML 227
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-227 2.34e-132

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 371.47  E-value: 2.34e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835740     1 MAHPLLLGFQDAMSPIMEELLHFHDHTLMIVFLISTMVLYIITLMMTTKLTYTNTMNAQEVEMIWTILPAIVLITIALPS 80
Cdd:MTH00154   1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835740    81 LRVLYLMDEINNPHLTIKAMGHQWYWTYEYTDYENLEFDSYMTPTQTLPNGHFRLLEVDHRMVMPMESPIRMLISAEDVL 160
Cdd:MTH00154  81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 5835740   161 HSWAVPSLGVKTDAVPGRLNQATFIVTRPGVFYGQCSEICGANHSFMPIVIESVPLWHFENWSSLMF 227
Cdd:MTH00154 161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNMS 227
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-224 4.92e-129

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 363.15  E-value: 4.92e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835740     1 MAHPLLLGFQDAMSPIMEELLHFHDHTLMIVFLISTMVLYIITLMMTTKLTYTNTMNAQEVEMIWTILPAIVLITIALPS 80
Cdd:MTH00168   1 MATYSQLGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835740    81 LRVLYLMDEINNPHLTIKAMGHQWYWTYEYTDYENLEFDSYMTPTQTLPNGHFRLLEVDHRMVMPMESPIRMLISAEDVL 160
Cdd:MTH00168  81 LRLLYLMDEIDKPDLTIKAVGHQWYWSYEYTDYNDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 5835740   161 HSWAVPSLGVKTDAVPGRLNQATFIVTRPGVFYGQCSEICGANHSFMPIVIESVPLWHFENWSS 224
Cdd:MTH00168 161 HSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENWVD 224
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-224 1.18e-124

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 352.08  E-value: 1.18e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835740     1 MAHPLLLGFQDAMSPIMEELLHFHDHTLMIVFLISTMVLYIITLMMTTKLTYTNTMNAQEVEMIWTILPAIVLITIALPS 80
Cdd:MTH00038   1 MATWLQLGLQDASSPLMEELIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835740    81 LRVLYLMDEINNPHLTIKAMGHQWYWTYEYTDYENLEFDSYMTPTQTLPNGHFRLLEVDHRMVMPMESPIRMLISAEDVL 160
Cdd:MTH00038  81 LQLLYLMDEVNNPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 5835740   161 HSWAVPSLGVKTDAVPGRLNQATFIVTRPGVFYGQCSEICGANHSFMPIVIESVPLWHFENWSS 224
Cdd:MTH00038 161 HSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVS 224
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 7-226 2.54e-118

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 336.14  E-value: 2.54e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835740     7 LGFQDAMSPIMEELLHFHDHTLMIVFLISTMVLYIITLMMTTKLTYTNTMNAQEVEMIWTILPAIVLITIALPSLRVLYL 86
Cdd:MTH00140   7 LGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPSLRLLYL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835740    87 MDEINNPHLTIKAMGHQWYWTYEYTDYENLEFDSYMTPTQTLPNGHFRLLEVDHRMVMPMESPIRMLISAEDVLHSWAVP 166
Cdd:MTH00140  87 LDETNNPLLTVKAIGHQWYWSYEYSDFSVIEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVIHSWTVP 166

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835740   167 SLGVKTDAVPGRLNQATFIVTRPGVFYGQCSEICGANHSFMPIVIESVPLWHFENWSSLM 226
Cdd:MTH00140 167 SLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWLELM 226
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-222 1.25e-116

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 331.68  E-value: 1.25e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835740     1 MAHPLLLGFQDAMSPIMEELLHFHDHTLMIVFLISTMVLYIITLMMTTKLTYTNTMNAQEVEMIWTILPAIVLITIALPS 80
Cdd:MTH00139   1 MAYWGQLGFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835740    81 LRVLYLMDEINNPHLTIKAMGHQWYWTYEYTDYENLEFDSYMTPTQTLPNGHFRLLEVDHRMVMPMESPIRMLISAEDVL 160
Cdd:MTH00139  81 LRLLYLMDEVSDPYLTFKAVGHQWYWSYEYSDFKNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5835740   161 HSWAVPSLGVKTDAVPGRLNQATFIVTRPGVFYGQCSEICGANHSFMPIVIESVPLWHFENW 222
Cdd:MTH00139 161 HSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEW 222
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-224 1.53e-109

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 314.10  E-value: 1.53e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835740     1 MAHPLLLGFQDAMSPIMEELLHFHDHTLMIVFLISTMVLYIITLMMTTKLTYTNTMNAQEVEMIWTILPAIVLITIALPS 80
Cdd:MTH00008   1 MPHWGQLMFQDAASPVMLQLISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835740    81 LRVLYLMDEINNPHLTIKAMGHQWYWTYEYTDYENLEFDSYMTPTQTLPNGHFRLLEVDHRMVMPMESPIRMLISAEDVL 160
Cdd:MTH00008  81 LRLLYLMDEVSNPSITLKTIGHQWYWSYEYSDFSNLEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVI 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 5835740   161 HSWAVPSLGVKTDAVPGRLNQATFIVTRPGVFYGQCSEICGANHSFMPIVIESVPLWHFENWSS 224
Cdd:MTH00008 161 HSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKWVS 224
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 2-224 7.04e-106

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 305.14  E-value: 7.04e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835740     2 AHPLLLGFQDAMSPIMEELLHFHDHTLMIVFLISTMVLYIITLMMTTKLTYTNTMNAQEVEMIWTILPAIVLITIALPSL 81
Cdd:MTH00023  11 PEPWQLGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSL 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835740    82 RVLYLMDEINNPHLTIKAMGHQWYWTYEYTDY--ENLEFDSYMTPTQTLPNGHFRLLEVDHRMVMPMESPIRMLISAEDV 159
Cdd:MTH00023  91 KLLYLMDEVVSPALTIKAIGHQWYWSYEYSDYegETLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADV 170

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 5835740   160 LHSWAVPSLGVKTDAVPGRLNQATFIVTRPGVFYGQCSEICGANHSFMPIVIESVPLWHFENWSS 224
Cdd:MTH00023 171 LHSFAVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWLL 235
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 2-222 3.20e-105

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 303.24  E-value: 3.20e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835740     2 AHPLLLGFQDAMSPIMEELLHFHDHTLMIVFLISTMVLYIITLMMTTKLTYTNTMNAQEVEMIWTILPAIVLITIALPSL 81
Cdd:MTH00051   4 PEPWQLGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835740    82 RVLYLMDEINNPHLTIKAMGHQWYWTYEYTDY--ENLEFDSYMTPTQTLPNGHFRLLEVDHRMVMPMESPIRMLISAEDV 159
Cdd:MTH00051  84 KLLYLMDEVIDPALTIKAIGHQWYWSYEYSDYgtDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADV 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5835740   160 LHSWAVPSLGVKTDAVPGRLNQATFIVTRPGVFYGQCSEICGANHSFMPIVIESVPLWHFENW 222
Cdd:MTH00051 164 LHSFAVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINW 226
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 93-222 4.72e-92

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: 265.97  E-value: 4.72e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835740   93 PHLTIKAMGHQWYWTYEYTDYENLEFDSYMTPTQTLPNGHFRLLEVDHRMVMPMESPIRMLISAEDVLHSWAVPSLGVKT 172
Cdd:cd13912   1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 5835740  173 DAVPGRLNQATFIVTRPGVFYGQCSEICGANHSFMPIVIESVPLWHFENW 222
Cdd:cd13912  81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-214 3.78e-85

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 248.09  E-value: 3.78e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835740     95 LTIKAMGHQWYWTYEYTDYENLEFDSYMTPTQTLPNGHFRLLEVDHRMVMPMESPIRMLISAEDVLHSWAVPSLGVKTDA 174
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 5835740    175 VPGRLNQATFIVTRPGVFYGQCSEICGANHSFMPIVIESV 214
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 4-222 2.57e-84

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 251.48  E-value: 2.57e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835740     4 PLLLGFQDAMSPIMEELLHFHDHTLMIVFLISTMVLYIITLMMTTKLTYT---NTMNAQEVEMIWTILPAIVLITIALPS 80
Cdd:MTH00027  32 PWQLGFQDAGSPVMEEIIMLHDQILFILTIIVGVVLWLIIRILLGNNYYSyywNKLDGSLIEVIWTLIPAFILILIAFPS 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835740    81 LRVLYLMDE-INNPHLTIKAMGHQWYWTYEYTDY--ENLEFDSYMTPTQTLPNGHFRLLEVDHRMVMPMESPIRMLISAE 157
Cdd:MTH00027 112 LRLLYIMDEcGFSANITIKVTGHQWYWSYSYEDYgeKNIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAA 191

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 5835740   158 DVLHSWAVPSLGVKTDAVPGRLNQATFIVTRPGVFYGQCSEICGANHSFMPIVIESVPLWHFENW 222
Cdd:MTH00027 192 DVLHSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYIDW 256
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 7-227 4.17e-71

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 216.41  E-value: 4.17e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835740     7 LGFQDAMSPIMEELLH-FHDHTLMIVFLISTMVLYIITLMMTTKLTYTNTMNAQEVEMIWTILPAIVLITIALPSLRVLY 85
Cdd:MTH00080   8 LNFSNSLFSSYMDWFHnFNCSLLFGEFVLAFVVFLFLYLISNNFYFKSKKIEYQFGELLCSVFPVLILLMQMVPSLSLLY 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835740    86 LMDEIN-NPHLTIKAMGHQWYWTYEYTDYENLEFDSYMTPTQTLPNGHFRLLEVDHRMVMPMESPIRMLISAEDVLHSWA 164
Cdd:MTH00080  88 YYGLMNlDSNLTVKVTGHQWYWSYEFSDIPGLEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWA 167

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5835740   165 VPSLGVKTDAVPGRLNQATFIVTRPGVFYGQCSEICGANHSFMPIVIESVPLWHFENWSSLMF 227
Cdd:MTH00080 168 LPSLSIKMDAMSGILSTLCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKEWCKLLL 230
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
7-222 2.74e-52

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 168.47  E-value: 2.74e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835740    7 LGFQDAMSPIMEELLHFHDHTL--MIVFLISTMVLYIITL---------MMTTKLTYTNTmnaqeVEMIWTILPAIVLIT 75
Cdd:COG1622  19 LSLPDPAGPIAEEIDDLFWVSLiiMLVIFVLVFGLLLYFAiryrrrkgdADPAQFHHNTK-----LEIVWTVIPIIIVIV 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835740   76 IALPSLRVLYLMDEINNPHLTIKAMGHQWYWTYEYTDYENLefdsymtptqtlpnghfrlleVDHRMVMPMESPIRMLIS 155
Cdd:COG1622  94 LAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIA---------------------TVNELVLPVGRPVRFLLT 152

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 5835740  156 AEDVLHSWAVPSLGVKTDAVPGRLNQATFIVTRPGVFYGQCSEICGANHSFMPIVIESVPLWHFENW 222
Cdd:COG1622 153 SADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAW 219
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 17-214 5.32e-44

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 146.25  E-value: 5.32e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835740    17 MEELLHFHDHTLMIVFL---ISTMVLYIITLMMTTKLTYTNTMN-AQEVEMIWTILPAivLITIALPSLRVLYLMDEIN- 91
Cdd:MTH00047   1 MNLSLLYYDIVCYILALcvfIPCWVYIMLCWQVVSGNGSVNFGSeNQVLELLWTVVPT--LLVLVLCFLNLNFITSDLDc 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835740    92 NPHLTIKAMGHQWYWTYEYTDyeNLEFDSYMTptqTLPNGhfrlleVDHRMVMPMESPIRMLISAEDVLHSWAVPSLGVK 171
Cdd:MTH00047  79 FSSETIKVIGHQWYWSYEYSF--GGSYDSFMT---DDIFG------VDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLK 147

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 5835740   172 TDAVPGRLNQATFIVTRPGVFYGQCSEICGANHSFMPIVIESV 214
Cdd:MTH00047 148 MDAIPGRINHLFFCPDRHGVFVGYCSELCGVGHSYMPIVIEVV 190
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 14-222 1.93e-39

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: 134.82  E-value: 1.93e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835740     14 SPIMEELlhFHDHTLMIVFLISTMVLyIITLMMTTKLTYTNTMNAQE---------VEMIWTILPA-IVLITIALPSLRV 83
Cdd:TIGR02866   3 GEIAQQI--AFLFLFVLAVSTLISLL-VAALLAYVVWKFRRKGDEEKpsqihgnrrLEYVWTVIPLiIVVGLFAATAKGL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835740     84 LYLMDEINNPHLTIKAMGHQWYWTYEYtdyenlefdsymtptqtlPNGHFRlleVDHRMVMPMESPIRMLISAEDVLHSW 163
Cdd:TIGR02866  80 LYLERPIPKDALKVKVTGYQWWWDFEY------------------PESGFT---TVNELVLPAGTPVELQVTSKDVIHSF 138

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 5835740    164 AVPSLGVKTDAVPGRLNQATFIVTRPGVFYGQCSEICGANHSFMPIVIESVPLWHFENW 222
Cdd:TIGR02866 139 WVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAY 197
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 118-214 4.87e-39

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 132.64  E-value: 4.87e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835740   118 FDSYMTPTQTLPNGHFRLLEVDHRMVMPMESPIRMLISAEDVLHSWAVPSLGVKTDAVPGRLNQATFIVTRPGVFYGQCS 197
Cdd:PTZ00047  51 FQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCS 130

                         90
                 ....*....|....*..
gi 5835740   198 EICGANHSFMPIVIESV 214
Cdd:PTZ00047 131 EMCGTLHGFMPIVVEAV 147
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 95-212 1.51e-29

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: 105.84  E-value: 1.51e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835740   95 LTIKAMGHQWYWTYEYTDyenlefdsymtptqtlpnghfrlLEVDHRMVMPMESPIRMLISAEDVLHSWAVPSLGVKTDA 174
Cdd:cd13842   1 LTVYVTGVQWSWTFIYPN-----------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDA 57

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 5835740  175 VPGRLNQATFIVTRPGVFYGQCSEICGANHSFMPIVIE 212
Cdd:cd13842  58 VPGYTSELWFVADKPGTYTIICAEYCGLGHSYMLGKVE 95
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 94-207 4.12e-28

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: 102.31  E-value: 4.12e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835740   94 HLTIKAMGHQWYWTYEYtdyenlefdsymtptqtlPNGHFRLLEVDHRMVMPMESPIRMLISAEDVLHSWAVPSLGVKTD 173
Cdd:cd04213   1 ALTIEVTGHQWWWEFRY------------------PDEPGRGIVTANELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMD 62

                        90       100       110
                ....*....|....*....|....*....|....
gi 5835740  174 AVPGRLNQATFIVTRPGVFYGQCSEICGANHSFM 207
Cdd:cd04213  63 MIPGRTNRLWLQADEPGVYRGQCAEFCGASHALM 96
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-83 1.71e-24

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: 92.78  E-value: 1.71e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835740      1 MAHPLLLGFQDAMSPIMEELLHFHDHTLMIVFLISTMVLYIITLMMTT------KLTYTNTMNAQEVEMIWTILPAIVLI 74
Cdd:pfam02790   1 MPTPWGLGFQDAASPLMEGLLELHDYIMFILTLILILVLYILVTCLIRfnrrknPITARYTTHGQTIEIIWTIIPAVILI 80


                  ....*....
gi 5835740     75 TIALPSLRV 83
Cdd:pfam02790  81 LIALPSFKL 89
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-207 6.48e-23

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: 88.84  E-value: 6.48e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835740   95 LTIKAMGHQWYWTYEYtdyenlefdsymtptqtlPNGhfrlLEVDHRMVMPMESPIRMLISAEDVLHSWAVPSLGVKTDA 174
Cdd:cd13915   2 LEIQVTGRQWMWEFTY------------------PNG----KREINELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQDV 59

                        90       100       110
                ....*....|....*....|....*....|...
gi 5835740  175 VPGRLNQATFIVTRPGVFYGQCSEICGANHSFM 207
Cdd:cd13915  60 VPGRYTYLWFEATKPGEYDLFCTEYCGTGHSGM 92
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-207 7.98e-23

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: 88.85  E-value: 7.98e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835740   95 LTIKAMGHQWYWTYEYTDYENLEFDSYMTPTQTLpnghfrllevdhrmVMPMESPIRMLISAEDVLHSWAVPSLGVKTDA 174
Cdd:cd13919   2 LVVEVTAQQWAWTFRYPGGDGKLGTDDDVTSPEL--------------HLPVGRPVLFNLRSKDVIHSFWVPEFRVKQDA 67

                        90       100       110
                ....*....|....*....|....*....|...
gi 5835740  175 VPGRLNQATFIVTRPGVFYGQCSEICGANHSFM 207
Cdd:cd13919  68 VPGRTTRLWFTPTREGEYEVRCAELCGLGHYRM 100
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 67-222 1.68e-20

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


Pssm-ID: 259985 [Multi-domain]  Cd Length: 139  Bit Score: 83.66  E-value: 1.68e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835740   67 ILPAIVLIT-IALPSLRVLYLMD---EINNPHLTIKAMGHQWYWTYEYtdyenlefdsymtptqtlPNGHFRLLEvdhrM 142
Cdd:cd13918   1 GLSAIIVISlIVWTYGMLLYVEDppdEADEDALEVEVEGFQFGWQFEY------------------PNGVTTGNT----L 58

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835740  143 VMPMESPIRMLISAEDVLHSWAVPSLGVKTDAVPGRLNQATFIVTRPGVFYGQCSEICGANHSFMPIVIESVPLWHFENW 222
Cdd:cd13918  59 RVPADTPIALRVTSTDVFHTFGIPELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEFEAW 138
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 96-222 5.12e-20

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


Pssm-ID: 259981 [Multi-domain]  Cd Length: 108  Bit Score: 81.69  E-value: 5.12e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835740   96 TIKAMGHQWYWTYEYTDYENLEFDsymtptqtlpnghfrllevdhRMVMPMESPIRMLISAEDVLHSWAVPSLGVKTDAV 175
Cdd:cd13914   2 EIEVEAYQWGWEFSYPEANVTTSE---------------------QLVIPADRPVYFRITSRDVIHAFHVPELGLKQDAF 60

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 5835740  176 PGRLNQATFIVTRPGVFYGQCSEICGANHSFMPIVIESVPLWHFENW 222
Cdd:cd13914  61 PGQYNTIKTEATEEGEYQLYCAEYCGAGHSQMLSTVTVVSQDEYQQW 107
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 142-207 4.67e-07

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: 46.79  E-value: 4.67e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5835740  142 MVMPMESPIRMLISAEDVLHSWAVPSLGVKTDAVPGRLNQATFIVTRPGVFYGQCSEICGANHSFM 207
Cdd:cd13913  27 IEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNM 92
N2OR_C cd04223
The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase ...
 156-207 8.54e-06

The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase participates in nitrogen metabolism and catalyzes the last step in dissimilatory nitrate reduction, the two-electron reduction of N2O to N2. It contains copper ions as cofactors in the form of a binuclear CuA center at the site of electron entry and a tetranuclear CuZ centre at the active site. The C-terminus of Nitrous-oxide reductase is a cupredoxin domain.


Pssm-ID: 259885 [Multi-domain]  Cd Length: 95  Bit Score: 42.99  E-value: 8.54e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 5835740  156 AEDVLHSWAVPSLGVKTDAVPGRLNQATFIVTRPGVFYGQCSEICGANHSFM 207
Cdd:cd04223  36 DEDITHGFAIPGYNVNLSLEPGETATVTFVADKPGVYPYYCTEFCSALHLEM 87
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 96-207 6.50e-05

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: 259983 [Multi-domain]  Cd Length: 93  Bit Score: 40.44  E-value: 6.50e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5835740   96 TIKAMGHQWYWTyeytdyenlefdsyMTPTqTLPNGhfrllevdhrmvmpmeSPIRMLISAEDVLHSWAVPS----LGVK 171
Cdd:cd13916   2 VVAVTGHQWYWE--------------LSRT-EIPAG----------------KPVEFRVTSADVNHGFGIYDpdmrLLAQ 50

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 5835740  172 TDAVPGRLNQATFIVTRPGVFYGQCSEICGANHSFM 207
Cdd:cd13916  51 TQAMPGYTNVLRYTFDKPGTYTILCLEYCGLAHHVM 86
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 142-207 9.63e-04

The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase in the respiratory chains of aerobic bacteria, is a multi-chain transmembrane protein located in the cell membrane. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits in ubiquinol oxidase varies from two to five. Although subunit II of ubiquinol oxidase lacks the binuclear CuA site found in cytochrome c oxidases, the structure is conserved.


Pssm-ID: 259874 [Multi-domain]  Cd Length: 99  Bit Score: 37.53  E-value: 9.63e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5835740  142 MVMPMESPIRMLISAEDVLHSWAVPSLGVKTDAVPGRLNQATFIVTRPGVFYGQCSEICGANHSFM 207
Cdd:cd04212  27 LVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGTYQGLSANYSGEGFSDM 92
PRK02888 PRK02888
nitrous-oxide reductase; Validated
 157-207 9.85e-04

nitrous-oxide reductase; Validated


Pssm-ID: 235082 [Multi-domain]  Cd Length: 635  Bit Score: 39.57  E-value: 9.85e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 5835740   157 EDVLHSWAVPSLGVKTDAVPGRLNQATFIVTRPGVFYGQCSEICGANHSFM 207
Cdd:PRK02888 576 EDLTHGFAIPNYGVNMEVAPQATASVTFTADKPGVYWYYCTWFCHALHMEM 626
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 153-212 1.89e-03

Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in inter-molecular electron transfer reactions. Cupredoxins are blue copper proteins, having an intense blue color due to the presence of a mononuclear type 1 (T1) copper site. Structurally, the cupredoxin-like fold consists of a beta-sandwich with 7 strands in 2 beta-sheets, which is arranged in a Greek-key beta-barrel. Some of these proteins have lost the ability to bind copper. The majority of family members contain multiple cupredoxin domain repeats: ceruloplasmin and the coagulation factors V/VIII have six repeats; laccase, ascorbate oxidase, spore coat protein A, and multicopper oxidase CueO contain three repeats; and nitrite reductase has two repeats. Others are mono-domain cupredoxins, such as plastocyanin, pseudoazurin, plantacyanin, azurin, rusticyanin, stellacyanin, quinol oxidase, and the periplasmic domain of cytochrome c oxidase subunit II.


Pssm-ID: 259860 [Multi-domain]  Cd Length: 110  Bit Score: 36.83  E-value: 1.89e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 5835740  153 LISAEDVLHSWAVPSLGVKTDA---------------VPGRLNQATFIVTRPGVFYGQCSEICGaNHSFMPIVIE 212
Cdd:cd00920  37 FVNKLGENHSVTIAGFGVPVVAmagganpglvntlviGPGESAEVTFTTDQAGVYWFYCTIPGH-NHAGMVGTIN 110
 
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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