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Conserved domains on  [gi|75074252|sp|Q9GCE7|]
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RecName: Full=Cytochrome c oxidase subunit 2; AltName: Full=Cytochrome c oxidase polypeptide II

Protein Classification

cytochrome c oxidase subunit II( domain architecture ID 11475897)

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 MTH00098
cytochrome c oxidase subunit II; Validated
 1-227 8.11e-154

cytochrome c oxidase subunit II; Validated


:

Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 426.06  E-value: 8.11e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75074252    1 MAHPVHVGLKEATSPFMEELIAFHDHTLMIIFLISSLVLYIISMMLTTKLTHTSTMNAQEIEIIWTILPAIILIMIALPS 80
Cdd:MTH00098   1 MAYPFQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75074252   81 LRILYMTDEFNKPYLTLKAIGHQWYWSYEYSDYVDLAFDSYIMPTYFLEPGEFRLLEVDNRTTLPMEADIRMLISSQDVL 160
Cdd:MTH00098  81 LRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 75074252  161 HSWAVPS*GVKADAIPGRLNQAMLASMRPGLFYGQCSEICGSNHCFMPIVLEFSYF*DFETWASYLY 227
Cdd:MTH00098 161 HSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKWSASML 227
 
Name Accession Description Interval E-value
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-227 8.11e-154

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 426.06  E-value: 8.11e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75074252    1 MAHPVHVGLKEATSPFMEELIAFHDHTLMIIFLISSLVLYIISMMLTTKLTHTSTMNAQEIEIIWTILPAIILIMIALPS 80
Cdd:MTH00098   1 MAYPFQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75074252   81 LRILYMTDEFNKPYLTLKAIGHQWYWSYEYSDYVDLAFDSYIMPTYFLEPGEFRLLEVDNRTTLPMEADIRMLISSQDVL 160
Cdd:MTH00098  81 LRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 75074252  161 HSWAVPS*GVKADAIPGRLNQAMLASMRPGLFYGQCSEICGSNHCFMPIVLEFSYF*DFETWASYLY 227
Cdd:MTH00098 161 HSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKWSASML 227
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 93-222 1.02e-79

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: 234.77  E-value: 1.02e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75074252  93 PYLTLKAIGHQWYWSYEYSDYVDLAFDSYIMPTYFLEPGEFRLLEVDNRTTLPMEADIRMLISSQDVLHSWAVPS*GVKA 172
Cdd:cd13912   1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 75074252 173 DAIPGRLNQAMLASMRPGLFYGQCSEICGSNHCFMPIVLEFSYF*DFETW 222
Cdd:cd13912  81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-212 1.88e-74

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 221.13  E-value: 1.88e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75074252    95 LTLKAIGHQWYWSYEYSDYVDLAFDSYIMPTYFLEPGEFRLLEVDNRTTLPMEADIRMLISSQDVLHSWAVPS*GVKADA 174
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 75074252   175 IPGRLNQAMLASMRPGLFYGQCSEICGSNHCFMPIVLE 212
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIE 118
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
61-212 1.11e-40

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 138.81  E-value: 1.11e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75074252  61 IEIIWTILPAIILIMIALPSLRILYMTDEFNKPYLTLKAIGHQWYWSYEYSDYVDLafdsyimptyflepgefrlleVDN 140
Cdd:COG1622  79 LEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIA---------------------TVN 137

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 75074252 141 RTTLPMEADIRMLISSQDVLHSWAVPS*GVKADAIPGRLNQAMLASMRPGLFYGQCSEICGSNHCFMPIVLE 212
Cdd:COG1622 138 ELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVV 209
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 12-222 6.22e-36

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: 125.57  E-value: 6.22e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75074252    12 ATSPFMEELIAFHDHTLMIIFLISSLVLYII-----------SMMLTTKLTHTSTMnaqeiEIIWTILPAIILI-MIALP 79
Cdd:TIGR02866   1 PGGEIAQQIAFLFLFVLAVSTLISLLVAALLayvvwkfrrkgDEEKPSQIHGNRRL-----EYVWTVIPLIIVVgLFAAT 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75074252    80 SLRILYMTDEFNKPYLTLKAIGHQWYWSYEYSDYvdlafdsyimptyflepgefrLLEVDNRTTLPMEADIRMLISSQDV 159
Cdd:TIGR02866  76 AKGLLYLERPIPKDALKVKVTGYQWWWDFEYPES---------------------GFTTVNELVLPAGTPVELQVTSKDV 134

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 75074252   160 LHSWAVPS*GVKADAIPGRLNQAMLASMRPGLFYGQCSEICGSNHCFMPIVLEFSYF*DFETW 222
Cdd:TIGR02866 135 IHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAY 197
 
Name Accession Description Interval E-value
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-227 8.11e-154

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 426.06  E-value: 8.11e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75074252    1 MAHPVHVGLKEATSPFMEELIAFHDHTLMIIFLISSLVLYIISMMLTTKLTHTSTMNAQEIEIIWTILPAIILIMIALPS 80
Cdd:MTH00098   1 MAYPFQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75074252   81 LRILYMTDEFNKPYLTLKAIGHQWYWSYEYSDYVDLAFDSYIMPTYFLEPGEFRLLEVDNRTTLPMEADIRMLISSQDVL 160
Cdd:MTH00098  81 LRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 75074252  161 HSWAVPS*GVKADAIPGRLNQAMLASMRPGLFYGQCSEICGSNHCFMPIVLEFSYF*DFETWASYLY 227
Cdd:MTH00098 161 HSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKWSASML 227
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-226 1.47e-143

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 400.06  E-value: 1.47e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75074252    1 MAHPVHVGLKEATSPFMEELIAFHDHTLMIIFLISSLVLYIISMMLTTKLTHTSTMNAQEIEIIWTILPAIILIMIALPS 80
Cdd:MTH00117   1 MANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75074252   81 LRILYMTDEFNKPYLTLKAIGHQWYWSYEYSDYVDLAFDSYIMPTYFLEPGEFRLLEVDNRTTLPMEADIRMLISSQDVL 160
Cdd:MTH00117  81 LRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 75074252  161 HSWAVPS*GVKADAIPGRLNQAMLASMRPGLFYGQCSEICGSNHCFMPIVLEFSYF*DFETWASYL 226
Cdd:MTH00117 161 HSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSLL 226
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 1-224 1.97e-126

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 356.78  E-value: 1.97e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75074252    1 MAHPVHVGLKEATSPFMEELIAFHDHTLMIIFLISSLVLYIISMMLTTKLTHTSTMNAQEIEIIWTILPAIILIMIALPS 80
Cdd:MTH00076   1 MAHPSQLGFQDAASPIMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75074252   81 LRILYMTDEFNKPYLTLKAIGHQWYWSYEYSDYVDLAFDSYIMPTYFLEPGEFRLLEVDNRTTLPMEADIRMLISSQDVL 160
Cdd:MTH00076  81 LRILYLMDEINDPHLTVKAIGHQWYWSYEYTDYEDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 75074252  161 HSWAVPS*GVKADAIPGRLNQAMLASMRPGLFYGQCSEICGSNHCFMPIVLEFSYF*DFETWAS 224
Cdd:MTH00076 161 HSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLNWSS 224
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 1-224 1.26e-125

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 354.79  E-value: 1.26e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75074252    1 MAHPVHVGLKEATSPFMEELIAFHDHTLMIIFLISSLVLYIISMMLTTKLTHTSTMNAQEIEIIWTILPAIILIMIALPS 80
Cdd:MTH00129   1 MAHPSQLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75074252   81 LRILYMTDEFNKPYLTLKAIGHQWYWSYEYSDYVDLAFDSYIMPTYFLEPGEFRLLEVDNRTTLPMEADIRMLISSQDVL 160
Cdd:MTH00129  81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 75074252  161 HSWAVPS*GVKADAIPGRLNQAMLASMRPGLFYGQCSEICGSNHCFMPIVLEFSYF*DFETWAS 224
Cdd:MTH00129 161 HSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFENWSS 224
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-222 1.35e-122

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 347.20  E-value: 1.35e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75074252    1 MAHPVHVGLKEATSPFMEELIAFHDHTLMIIFLISSLVLYIISMMLTTKLTHTSTMNAQEIEIIWTILPAIILIMIALPS 80
Cdd:MTH00154   1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75074252   81 LRILYMTDEFNKPYLTLKAIGHQWYWSYEYSDYVDLAFDSYIMPTYFLEPGEFRLLEVDNRTTLPMEADIRMLISSQDVL 160
Cdd:MTH00154  81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 75074252  161 HSWAVPS*GVKADAIPGRLNQAMLASMRPGLFYGQCSEICGSNHCFMPIVLEFSYF*DFETW 222
Cdd:MTH00154 161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINW 222
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 1-224 8.63e-120

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 340.32  E-value: 8.63e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75074252    1 MAHPVHVGLKEATSPFMEELIAFHDHTLMIIFLISSLVLYIISMMLTTKLTHTSTMNAQEIEIIWTILPAIILIMIALPS 80
Cdd:MTH00185   1 MAHPSQLGLQDAASPVMEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75074252   81 LRILYMTDEFNKPYLTLKAIGHQWYWSYEYSDYVDLAFDSYIMPTYFLEPGEFRLLEVDNRTTLPMEADIRMLISSQDVL 160
Cdd:MTH00185  81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 75074252  161 HSWAVPS*GVKADAIPGRLNQAMLASMRPGLFYGQCSEICGSNHCFMPIVLEFSYF*DFETWAS 224
Cdd:MTH00185 161 HSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENWSS 224
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-222 4.41e-117

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 333.10  E-value: 4.41e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75074252    1 MAHPVHVGLKEATSPFMEELIAFHDHTLMIIFLISSLVLYIISMMLTTKLTHTSTMNAQEIEIIWTILPAIILIMIALPS 80
Cdd:MTH00168   1 MATYSQLGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75074252   81 LRILYMTDEFNKPYLTLKAIGHQWYWSYEYSDYVDLAFDSYIMPTYFLEPGEFRLLEVDNRTTLPMEADIRMLISSQDVL 160
Cdd:MTH00168  81 LRLLYLMDEIDKPDLTIKAVGHQWYWSYEYTDYNDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 75074252  161 HSWAVPS*GVKADAIPGRLNQAMLASMRPGLFYGQCSEICGSNHCFMPIVLEFSYF*DFETW 222
Cdd:MTH00168 161 HSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENW 222
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 7-226 1.00e-111

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 319.58  E-value: 1.00e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75074252    7 VGLKEATSPFMEELIAFHDHTLMIIFLISSLVLYIISMMLTTKLTHTSTMNAQEIEIIWTILPAIILIMIALPSLRILYM 86
Cdd:MTH00140   7 LGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPSLRLLYL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75074252   87 TDEFNKPYLTLKAIGHQWYWSYEYSDYVDLAFDSYIMPTYFLEPGEFRLLEVDNRTTLPMEADIRMLISSQDVLHSWAVP 166
Cdd:MTH00140  87 LDETNNPLLTVKAIGHQWYWSYEYSDFSVIEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVIHSWTVP 166

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 75074252  167 S*GVKADAIPGRLNQAMLASMRPGLFYGQCSEICGSNHCFMPIVLEFSYF*DFETWASYL 226
Cdd:MTH00140 167 SLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWLELM 226
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-224 1.83e-108

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 311.25  E-value: 1.83e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75074252    1 MAHPVHVGLKEATSPFMEELIAFHDHTLMIIFLISSLVLYIISMMLTTKLTHTSTMNAQEIEIIWTILPAIILIMIALPS 80
Cdd:MTH00038   1 MATWLQLGLQDASSPLMEELIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75074252   81 LRILYMTDEFNKPYLTLKAIGHQWYWSYEYSDYVDLAFDSYIMPTYFLEPGEFRLLEVDNRTTLPMEADIRMLISSQDVL 160
Cdd:MTH00038  81 LQLLYLMDEVNNPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 75074252  161 HSWAVPS*GVKADAIPGRLNQAMLASMRPGLFYGQCSEICGSNHCFMPIVLEFSYF*DFETWAS 224
Cdd:MTH00038 161 HSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVS 224
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-224 2.02e-106

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 306.26  E-value: 2.02e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75074252    1 MAHPVHVGLKEATSPFMEELIAFHDHTLMIIFLISSLVLYIISMMLTTKLTHTSTMNAQEIEIIWTILPAIILIMIALPS 80
Cdd:MTH00139   1 MAYWGQLGFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75074252   81 LRILYMTDEFNKPYLTLKAIGHQWYWSYEYSDYVDLAFDSYIMPTYFLEPGEFRLLEVDNRTTLPMEADIRMLISSQDVL 160
Cdd:MTH00139  81 LRLLYLMDEVSDPYLTFKAVGHQWYWSYEYSDFKNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 75074252  161 HSWAVPS*GVKADAIPGRLNQAMLASMRPGLFYGQCSEICGSNHCFMPIVLEFSYF*DFETWAS 224
Cdd:MTH00139 161 HSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEWIL 224
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-224 2.71e-100

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 290.60  E-value: 2.71e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75074252    1 MAHPVHVGLKEATSPFMEELIAFHDHTLMIIFLISSLVLYIISMMLTTKLTHTSTMNAQEIEIIWTILPAIILIMIALPS 80
Cdd:MTH00008   1 MPHWGQLMFQDAASPVMLQLISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75074252   81 LRILYMTDEFNKPYLTLKAIGHQWYWSYEYSDYVDLAFDSYIMPTYFLEPGEFRLLEVDNRTTLPMEADIRMLISSQDVL 160
Cdd:MTH00008  81 LRLLYLMDEVSNPSITLKTIGHQWYWSYEYSDFSNLEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVI 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 75074252  161 HSWAVPS*GVKADAIPGRLNQAMLASMRPGLFYGQCSEICGSNHCFMPIVLEFSYF*DFETWAS 224
Cdd:MTH00008 161 HSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKWVS 224
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 2-212 1.49e-92

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 271.62  E-value: 1.49e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75074252    2 AHPVHVGLKEATSPFMEELIAFHDHTLMIIFLISSLVLYIISMMLTTKLTHTSTMNAQEIEIIWTILPAIILIMIALPSL 81
Cdd:MTH00023  11 PEPWQLGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSL 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75074252   82 RILYMTDEFNKPYLTLKAIGHQWYWSYEYSDYVD--LAFDSYIMPTYFLEPGEFRLLEVDNRTTLPMEADIRMLISSQDV 159
Cdd:MTH00023  91 KLLYLMDEVVSPALTIKAIGHQWYWSYEYSDYEGetLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADV 170

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 75074252  160 LHSWAVPS*GVKADAIPGRLNQAMLASMRPGLFYGQCSEICGSNHCFMPIVLE 212
Cdd:MTH00023 171 LHSFAVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIE 223
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 2-222 1.91e-89

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 263.56  E-value: 1.91e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75074252    2 AHPVHVGLKEATSPFMEELIAFHDHTLMIIFLISSLVLYIISMMLTTKLTHTSTMNAQEIEIIWTILPAIILIMIALPSL 81
Cdd:MTH00051   4 PEPWQLGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75074252   82 RILYMTDEFNKPYLTLKAIGHQWYWSYEYSDY--VDLAFDSYIMPTYFLEPGEFRLLEVDNRTTLPMEADIRMLISSQDV 159
Cdd:MTH00051  84 KLLYLMDEVIDPALTIKAIGHQWYWSYEYSDYgtDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADV 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 75074252  160 LHSWAVPS*GVKADAIPGRLNQAMLASMRPGLFYGQCSEICGSNHCFMPIVLEFSYF*DFETW 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 1.02e-79

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: 234.77  E-value: 1.02e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75074252  93 PYLTLKAIGHQWYWSYEYSDYVDLAFDSYIMPTYFLEPGEFRLLEVDNRTTLPMEADIRMLISSQDVLHSWAVPS*GVKA 172
Cdd:cd13912   1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 75074252 173 DAIPGRLNQAMLASMRPGLFYGQCSEICGSNHCFMPIVLEFSYF*DFETW 222
Cdd:cd13912  81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-212 1.88e-74

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 221.13  E-value: 1.88e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75074252    95 LTLKAIGHQWYWSYEYSDYVDLAFDSYIMPTYFLEPGEFRLLEVDNRTTLPMEADIRMLISSQDVLHSWAVPS*GVKADA 174
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 75074252   175 IPGRLNQAMLASMRPGLFYGQCSEICGSNHCFMPIVLE 212
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIE 118
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 4-222 3.88e-71

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 217.97  E-value: 3.88e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75074252    4 PVHVGLKEATSPFMEELIAFHDHTLMIIFLISSLVLYIISMMLTTKLTHT---STMNAQEIEIIWTILPAIILIMIALPS 80
Cdd:MTH00027  32 PWQLGFQDAGSPVMEEIIMLHDQILFILTIIVGVVLWLIIRILLGNNYYSyywNKLDGSLIEVIWTLIPAFILILIAFPS 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75074252   81 LRILYMTDEFN-KPYLTLKAIGHQWYWSYEYSDY--VDLAFDSYIMPTYFLEPGEFRLLEVDNRTTLPMEADIRMLISSQ 157
Cdd:MTH00027 112 LRLLYIMDECGfSANITIKVTGHQWYWSYSYEDYgeKNIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAA 191

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 75074252  158 DVLHSWAVPS*GVKADAIPGRLNQAMLASMRPGLFYGQCSEICGSNHCFMPIVLEFSYF*DFETW 222
Cdd:MTH00027 192 DVLHSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYIDW 256
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 14-222 2.31e-70

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 214.87  E-value: 2.31e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75074252   14 SPFMEELIAFHDHTLMIIFLISSLVLYIISMMLTTKLTHTSTMNAQEIEIIWTILPAIILIMIALPSLRILYMTDEFN-K 92
Cdd:MTH00080  16 SSYMDWFHNFNCSLLFGEFVLAFVVFLFLYLISNNFYFKSKKIEYQFGELLCSVFPVLILLMQMVPSLSLLYYYGLMNlD 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75074252   93 PYLTLKAIGHQWYWSYEYSDYVDLAFDSYIMPTYFLEPGEFRLLEVDNRTTLPMEADIRMLISSQDVLHSWAVPS*GVKA 172
Cdd:MTH00080  96 SNLTVKVTGHQWYWSYEFSDIPGLEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKM 175

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 75074252  173 DAIPGRLNQAMLASMRPGLFYGQCSEICGSNHCFMPIVLEFSYF*DFETW 222
Cdd:MTH00080 176 DAMSGILSTLCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKEW 225
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
61-212 1.11e-40

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 138.81  E-value: 1.11e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75074252  61 IEIIWTILPAIILIMIALPSLRILYMTDEFNKPYLTLKAIGHQWYWSYEYSDYVDLafdsyimptyflepgefrlleVDN 140
Cdd:COG1622  79 LEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIA---------------------TVN 137

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 75074252 141 RTTLPMEADIRMLISSQDVLHSWAVPS*GVKADAIPGRLNQAMLASMRPGLFYGQCSEICGSNHCFMPIVLE 212
Cdd:COG1622 138 ELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVV 209
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 17-212 4.13e-36

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 125.84  E-value: 4.13e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75074252   17 MEELIAFHDHTLMIIFLISSLVLYIISMMLTTKLTHTSTMN----AQEIEIIWTILPAIILIMiaLPSLRILYMTDEFN- 91
Cdd:MTH00047   1 MNLSLLYYDIVCYILALCVFIPCWVYIMLCWQVVSGNGSVNfgseNQVLELLWTVVPTLLVLV--LCFLNLNFITSDLDc 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75074252   92 KPYLTLKAIGHQWYWSYEYSDyvDLAFDSYIMPTYFLepgefrlleVDNRTTLPMEADIRMLISSQDVLHSWAVPS*GVK 171
Cdd:MTH00047  79 FSSETIKVIGHQWYWSYEYSF--GGSYDSFMTDDIFG---------VDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLK 147

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 75074252  172 ADAIPGRLNQAMLASMRPGLFYGQCSEICGSNHCFMPIVLE 212
Cdd:MTH00047 148 MDAIPGRINHLFFCPDRHGVFVGYCSELCGVGHSYMPIVIE 188
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 12-222 6.22e-36

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: 125.57  E-value: 6.22e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75074252    12 ATSPFMEELIAFHDHTLMIIFLISSLVLYII-----------SMMLTTKLTHTSTMnaqeiEIIWTILPAIILI-MIALP 79
Cdd:TIGR02866   1 PGGEIAQQIAFLFLFVLAVSTLISLLVAALLayvvwkfrrkgDEEKPSQIHGNRRL-----EYVWTVIPLIIVVgLFAAT 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75074252    80 SLRILYMTDEFNKPYLTLKAIGHQWYWSYEYSDYvdlafdsyimptyflepgefrLLEVDNRTTLPMEADIRMLISSQDV 159
Cdd:TIGR02866  76 AKGLLYLERPIPKDALKVKVTGYQWWWDFEYPES---------------------GFTTVNELVLPAGTPVELQVTSKDV 134

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 75074252   160 LHSWAVPS*GVKADAIPGRLNQAMLASMRPGLFYGQCSEICGSNHCFMPIVLEFSYF*DFETW 222
Cdd:TIGR02866 135 IHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAY 197
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 128-212 6.49e-36

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 124.55  E-value: 6.49e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75074252  128 LEPGEFRLLEVDNRTTLPMEADIRMLISSQDVLHSWAVPS*GVKADAIPGRLNQAMLASMRPGLFYGQCSEICGSNHCFM 207
Cdd:PTZ00047  61 LKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCSEMCGTLHGFM 140


                 ....*
gi 75074252  208 PIVLE 212
Cdd:PTZ00047 141 PIVVE 145
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-83 6.63e-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: 91.24  E-value: 6.63e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75074252     1 MAHPVHVGLKEATSPFMEELIAFHDHTLMIIFLISSLVLYIISMMLTT------KLTHTSTMNAQEIEIIWTILPAIILI 74
Cdd:pfam02790   1 MPTPWGLGFQDAASPLMEGLLELHDYIMFILTLILILVLYILVTCLIRfnrrknPITARYTTHGQTIEIIWTIIPAVILI 80


                  ....*....
gi 75074252    75 MIALPSLRI 83
Cdd:pfam02790  81 LIALPSFKL 89
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 95-212 1.70e-23

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


Pssm-ID: 259911 [Multi-domain]  Cd Length: 95  Bit Score: 90.43  E-value: 1.70e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75074252  95 LTLKAIGHQWYWSYEYSDyvdlafdsyimptyflepgefrlLEVDNRTTLPMEADIRMLISSQDVLHSWAVPS*GVKADA 174
Cdd:cd13842   1 LTVYVTGVQWSWTFIYPN-----------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDA 57

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 75074252 175 IPGRLNQAMLASMRPGLFYGQCSEICGSNHCFMPIVLE 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), ...
 95-207 3.11e-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: 3.11e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75074252  95 LTLKAIGHQWYWSYEYSDYvdlafdsyimptyflepgEFRLLEVDNRTTLPMEADIRMLISSQDVLHSWAVPS*GVKADA 174
Cdd:cd04213   2 LTIEVTGHQWWWEFRYPDE------------------PGRGIVTANELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMDM 63

                        90       100       110
                ....*....|....*....|....*....|...
gi 75074252 175 IPGRLNQAMLASMRPGLFYGQCSEICGSNHCFM 207
Cdd:cd04213  64 IPGRTNRLWLQADEPGVYRGQCAEFCGASHALM 96
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-207 2.71e-17

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


Pssm-ID: 259986 [Multi-domain]  Cd Length: 107  Bit Score: 74.60  E-value: 2.71e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75074252  95 LTLKAIGHQWYWSYEYSDYvdlafDSYIMPTYFLEPGEFRLlevdnrttlPMEADIRMLISSQDVLHSWAVPS*GVKADA 174
Cdd:cd13919   2 LVVEVTAQQWAWTFRYPGG-----DGKLGTDDDVTSPELHL---------PVGRPVLFNLRSKDVIHSFWVPEFRVKQDA 67

                        90       100       110
                ....*....|....*....|....*....|...
gi 75074252 175 IPGRLNQAMLASMRPGLFYGQCSEICGSNHCFM 207
Cdd:cd13919  68 VPGRTTRLWFTPTREGEYEVRCAELCGLGHYRM 100
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 67-207 3.09e-17

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


Pssm-ID: 259985 [Multi-domain]  Cd Length: 139  Bit Score: 75.18  E-value: 3.09e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75074252  67 ILPAIILI-MIALPSLRILYMTD---EFNKPYLTLKAIGHQWYWSYEYSDyvdlafdsyimptyflepgefrllEVDNRT 142
Cdd:cd13918   1 GLSAIIVIsLIVWTYGMLLYVEDppdEADEDALEVEVEGFQFGWQFEYPN------------------------GVTTGN 56

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 75074252 143 TLPMEAD--IRMLISSQDVLHSWAVPS*GVKADAIPGRLNQAMLASMRPGLFYGQCSEICGSNHCFM 207
Cdd:cd13918  57 TLRVPADtpIALRVTSTDVFHTFGIPELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLM 123
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-207 5.57e-17

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


Pssm-ID: 259982 [Multi-domain]  Cd Length: 98  Bit Score: 73.43  E-value: 5.57e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75074252  95 LTLKAIGHQWYWSYEYsdyvdlafdsyimptyflePGEFRlleVDNRTTLPMEADIRMLISSQDVLHSWAVPS*GVKADA 174
Cdd:cd13915   2 LEIQVTGRQWMWEFTY-------------------PNGKR---EINELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQDV 59

                        90       100       110
                ....*....|....*....|....*....|...
gi 75074252 175 IPGRLNQAMLASMRPGLFYGQCSEICGSNHCFM 207
Cdd:cd13915  60 VPGRYTYLWFEATKPGEYDLFCTEYCGTGHSGM 92
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 96-207 9.90e-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: 259981 [Multi-domain]  Cd Length: 108  Bit Score: 65.12  E-value: 9.90e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75074252  96 TLKAIGHQWYWSYEYsdyvdlafdsyimptyflePGEfrllEVDNRTTL--PMEADIRMLISSQDVLHSWAVPS*GVKAD 173
Cdd:cd13914   2 EIEVEAYQWGWEFSY-------------------PEA----NVTTSEQLviPADRPVYFRITSRDVIHAFHVPELGLKQD 58

                        90       100       110
                ....*....|....*....|....*....|....
gi 75074252 174 AIPGRLNQAMLASMRPGLFYGQCSEICGSNHCFM 207
Cdd:cd13914  59 AFPGQYNTIKTEATEEGEYQLYCAEYCGAGHSQM 92
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 140-207 1.77e-05

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: 42.17  E-value: 1.77e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 75074252 140 NRTTLPMEADIRMLISSQDVLHSWAVPS*GVKADAIPGRLNQAMLASMRPGLFYGQCSEICGSNHCFM 207
Cdd:cd13913  25 NEIEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNM 92
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 125-212 6.51e-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: 35.28  E-value: 6.51e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75074252 125 TYFLEPGEFRLLEVDNRTTLPMEADIRM-LISSQDVLHSWAVPS*GV---------------KADAIPGRLNQAMLASMR 188
Cdd:cd00920   8 WGWSFTYNGVLLFGPPVLVVPVGDTVRVqFVNKLGENHSVTIAGFGVpvvamagganpglvnTLVIGPGESAEVTFTTDQ 87

                        90       100
                ....*....|....*....|....
gi 75074252 189 PGLFYGQCSEIcGSNHCFMPIVLE 212
Cdd:cd00920  88 AGVYWFYCTIP-GHNHAGMVGTIN 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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