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Conserved domains on  [gi|2265312620|gb|UTD49231|]
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cytochrome c oxidase subunit II (mitochondrion) [Acropora aspera]

Protein Classification

cytochrome c oxidase subunit II( domain architecture ID 11475873)

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 MTH00023
cytochrome c oxidase subunit II; Validated
 1-247 1.15e-161

cytochrome c oxidase subunit II; Validated


:

Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 446.89  E-value: 1.15e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265312620   1 MLNNFFYivnvcgkKDIPESWHLGFQEAAAPVMEEIVFFHDQIMFLLVIIVIVVLWLLVEALNGKYYDRDLIDGTLLEIV 80
Cdd:MTH00023    1 MFNNFFY-------RDIPEPWQLGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIV 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265312620  81 WTLIPAVILVFIASPSLKLLYLMDEVVSPALTIKAIGHQWYWSYEYSDYQEETLEFDSYMVPTSDLNSGDFRLLEVDNRL 160
Cdd:MTH00023   74 WTIIPAVILVFIALPSLKLLYLMDEVVSPALTIKAIGHQWYWSYEYSDYEGETLEFDSYMVPTSDLNSGDFRLLEVDNRL 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265312620 161 VVPINTHVRILVTGADVLHSFAVPALGIKTDAVPGRLNQAGIFIKRPGTFYGQCSEICGANHSFMPIVIEAVSLDRYINW 240
Cdd:MTH00023  154 VVPINTHVRILVTGADVLHSFAVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINW 233


                  ....*..
gi 2265312620 241 MLSLSNE 247
Cdd:MTH00023  234 LLSLSND 240
 
Name Accession Description Interval E-value
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 1-247 1.15e-161

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 446.89  E-value: 1.15e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265312620   1 MLNNFFYivnvcgkKDIPESWHLGFQEAAAPVMEEIVFFHDQIMFLLVIIVIVVLWLLVEALNGKYYDRDLIDGTLLEIV 80
Cdd:MTH00023    1 MFNNFFY-------RDIPEPWQLGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIV 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265312620  81 WTLIPAVILVFIASPSLKLLYLMDEVVSPALTIKAIGHQWYWSYEYSDYQEETLEFDSYMVPTSDLNSGDFRLLEVDNRL 160
Cdd:MTH00023   74 WTIIPAVILVFIALPSLKLLYLMDEVVSPALTIKAIGHQWYWSYEYSDYEGETLEFDSYMVPTSDLNSGDFRLLEVDNRL 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265312620 161 VVPINTHVRILVTGADVLHSFAVPALGIKTDAVPGRLNQAGIFIKRPGTFYGQCSEICGANHSFMPIVIEAVSLDRYINW 240
Cdd:MTH00023  154 VVPINTHVRILVTGADVLHSFAVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINW 233


                  ....*..
gi 2265312620 241 MLSLSNE 247
Cdd:MTH00023  234 LLSLSND 240
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 109-240 4.12e-97

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: 279.46  E-value: 4.12e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265312620 109 PALTIKAIGHQWYWSYEYSDYqeETLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSFAVPALGI 188
Cdd:cd13912     1 PSLTIKAIGHQWYWSYEYSDF--NDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGI 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2265312620 189 KTDAVPGRLNQAGIFIKRPGTFYGQCSEICGANHSFMPIVIEAVSLDRYINW 240
Cdd:cd13912    79 KVDAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
111-232 1.78e-82

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 242.32  E-value: 1.78e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265312620 111 LTIKAIGHQWYWSYEYSDYqeETLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSFAVPALGIKT 190
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDF--GDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKT 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2265312620 191 DAVPGRLNQAGIFIKRPGTFYGQCSEICGANHSFMPIVIEAV 232
Cdd:pfam00116  79 DAVPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
75-241 3.90e-60

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 189.27  E-value: 3.90e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265312620  75 TLLEIVWTLIPAVILVFIASPSLKLLYLMDEVVSPALTIKAIGHQWYWSYEYSDYQEETlefdsymvptsdlnsgdfrll 154
Cdd:COG1622    77 TKLEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIAT--------------------- 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265312620 155 evDNRLVVPINTHVRILVTGADVLHSFAVPALGIKTDAVPGRLNQAGIFIKRPGTFYGQCSEICGANHSFMPIVIEAVSL 234
Cdd:COG1622   136 --VNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSP 213


                  ....*..
gi 2265312620 235 DRYINWM 241
Cdd:COG1622   214 EEFDAWL 220
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 74-241 2.50e-49

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: 160.62  E-value: 2.50e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265312620  74 GTLLEIVWTLIPAVILV-FIASPSLKLLYLMDEVVSPALTIKAIGHQWYWSYEYSDYqeetlefdsymvptsdlnsgdfr 152
Cdd:TIGR02866  53 NRRLEYVWTVIPLIIVVgLFAATAKGLLYLERPIPKDALKVKVTGYQWWWDFEYPES----------------------- 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265312620 153 LLEVDNRLVVPINTHVRILVTGADVLHSFAVPALGIKTDAVPGRLNQAGIFIKRPGTFYGQCSEICGANHSFMPIVIEAV 232
Cdd:TIGR02866 110 GFTTVNELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVV 189


                  ....*....
gi 2265312620 233 SLDRYINWM 241
Cdd:TIGR02866 190 PKEEFDAYV 198
 
Name Accession Description Interval E-value
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 1-247 1.15e-161

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 446.89  E-value: 1.15e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265312620   1 MLNNFFYivnvcgkKDIPESWHLGFQEAAAPVMEEIVFFHDQIMFLLVIIVIVVLWLLVEALNGKYYDRDLIDGTLLEIV 80
Cdd:MTH00023    1 MFNNFFY-------RDIPEPWQLGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIV 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265312620  81 WTLIPAVILVFIASPSLKLLYLMDEVVSPALTIKAIGHQWYWSYEYSDYQEETLEFDSYMVPTSDLNSGDFRLLEVDNRL 160
Cdd:MTH00023   74 WTIIPAVILVFIALPSLKLLYLMDEVVSPALTIKAIGHQWYWSYEYSDYEGETLEFDSYMVPTSDLNSGDFRLLEVDNRL 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265312620 161 VVPINTHVRILVTGADVLHSFAVPALGIKTDAVPGRLNQAGIFIKRPGTFYGQCSEICGANHSFMPIVIEAVSLDRYINW 240
Cdd:MTH00023  154 VVPINTHVRILVTGADVLHSFAVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINW 233


                  ....*..
gi 2265312620 241 MLSLSNE 247
Cdd:MTH00023  234 LLSLSND 240
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 15-247 8.07e-142

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 396.84  E-value: 8.07e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265312620  15 KDIPESWHLGFQEAAAPVMEEIVFFHDQIMFLLVIIVIVVLWLLVEALNGKYYDRDLIDGTLLEIVWTLIPAVILVFIAS 94
Cdd:MTH00051    1 KDAPEPWQLGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265312620  95 PSLKLLYLMDEVVSPALTIKAIGHQWYWSYEYSDYQEETLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTG 174
Cdd:MTH00051   81 PSLKLLYLMDEVIDPALTIKAIGHQWYWSYEYSDYGTDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTA 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2265312620 175 ADVLHSFAVPALGIKTDAVPGRLNQAGIFIKRPGTFYGQCSEICGANHSFMPIVIEAVSLDRYINWMLSLSNE 247
Cdd:MTH00051  161 ADVLHSFAVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINWVATQSEE 233
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 20-245 2.26e-125

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 354.91  E-value: 2.26e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265312620  20 SW-HLGFQEAAAPVMEEIVFFHDQIMFLLVIIVIVVLWLLVEALNGKYYDRDLIDGTLLEIVWTLIPAVILVFIASPSLK 98
Cdd:MTH00154    3 TWsNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265312620  99 LLYLMDEVVSPALTIKAIGHQWYWSYEYSDYQEetLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVL 178
Cdd:MTH00154   83 LLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKN--IEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2265312620 179 HSFAVPALGIKTDAVPGRLNQAGIFIKRPGTFYGQCSEICGANHSFMPIVIEAVSLDRYINWMLSLS 245
Cdd:MTH00154  161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNMS 227
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 18-245 1.24e-122

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 347.67  E-value: 1.24e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265312620  18 PESWHLGFQEAAAPVMEEIVFFHDQIMFLLVIIVIVVLWLLVEALNGKYYDRDLIDGTLLEIVWTLIPAVILVFIASPSL 97
Cdd:MTH00117    2 ANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPSL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265312620  98 KLLYLMDEVVSPALTIKAIGHQWYWSYEYSDYqeETLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADV 177
Cdd:MTH00117   82 RILYLMDEINNPHLTIKAIGHQWYWSYEYTDY--KDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDV 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2265312620 178 LHSFAVPALGIKTDAVPGRLNQAGIFIKRPGTFYGQCSEICGANHSFMPIVIEAVSLDRYINWMLSLS 245
Cdd:MTH00117  160 LHSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSLLS 227
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 23-246 8.14e-116

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 330.75  E-value: 8.14e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265312620  23 LGFQEAAAPVMEEIVFFHDQIMFLLVIIVIVVLWLLVEALNGKYYDRDLIDGTLLEIVWTLIPAVILVFIASPSLKLLYL 102
Cdd:MTH00140    7 LGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPSLRLLYL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265312620 103 MDEVVSPALTIKAIGHQWYWSYEYSDYQEetLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSFA 182
Cdd:MTH00140   87 LDETNNPLLTVKAIGHQWYWSYEYSDFSV--IEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVIHSWT 164

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2265312620 183 VPALGIKTDAVPGRLNQAGIFIKRPGTFYGQCSEICGANHSFMPIVIEAVSLDRYINWMLSLSN 246
Cdd:MTH00140  165 VPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWLELMSE 228
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 23-243 2.22e-115

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 329.25  E-value: 2.22e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265312620  23 LGFQEAAAPVMEEIVFFHDQIMFLLVIIVIVVLWLLVEALNGKYYDRDLIDGTLLEIVWTLIPAVILVFIASPSLKLLYL 102
Cdd:MTH00168    7 LGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPSLRLLYL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265312620 103 MDEVVSPALTIKAIGHQWYWSYEYSDYQEetLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSFA 182
Cdd:MTH00168   87 MDEIDKPDLTIKAVGHQWYWSYEYTDYND--LEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVLHSWT 164

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2265312620 183 VPALGIKTDAVPGRLNQAGIFIKRPGTFYGQCSEICGANHSFMPIVIEAVSLDRYINWMLS 243
Cdd:MTH00168  165 LPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENWVDS 225
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 23-243 9.25e-114

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 325.52  E-value: 9.25e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265312620  23 LGFQEAAAPVMEEIVFFHDQIMFLLVIIVIVVLWLLVEALNGKYYDRDLIDGTLLEIVWTLIPAVILVFIASPSLKLLYL 102
Cdd:MTH00139    7 LGFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPSLRLLYL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265312620 103 MDEVVSPALTIKAIGHQWYWSYEYSDYqeETLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSFA 182
Cdd:MTH00139   87 MDEVSDPYLTFKAVGHQWYWSYEYSDF--KNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVLHSWT 164

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2265312620 183 VPALGIKTDAVPGRLNQAGIFIKRPGTFYGQCSEICGANHSFMPIVIEAVSLDRYINWMLS 243
Cdd:MTH00139  165 VPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEWILE 225
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 23-247 1.52e-112

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 322.42  E-value: 1.52e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265312620  23 LGFQEAAAPVMEEIVFFHDQIMFLLVIIVIVVLWLLVEALNGKYYDRDLIDGTLLEIVWTLIPAVILVFIASPSLKLLYL 102
Cdd:MTH00038    7 LGLQDASSPLMEELIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPSLQLLYL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265312620 103 MDEVVSPALTIKAIGHQWYWSYEYSDYQEetLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSFA 182
Cdd:MTH00038   87 MDEVNNPFLTIKAIGHQWYWSYEYTDYND--LEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVLHSWA 164

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2265312620 183 VPALGIKTDAVPGRLNQAGIFIKRPGTFYGQCSEICGANHSFMPIVIEAVSLDRYINWMLSLSNE 247
Cdd:MTH00038  165 VPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVSNFLEE 229
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 23-244 8.32e-107

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 307.80  E-value: 8.32e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265312620  23 LGFQEAAAPVMEEIVFFHDQIMFLLVIIVIVVLWLLVEALNGKYYDRDLIDGTLLEIVWTLIPAVILVFIASPSLKLLYL 102
Cdd:MTH00129    7 LGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPSLRILYL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265312620 103 MDEVVSPALTIKAIGHQWYWSYEYSDYqeETLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSFA 182
Cdd:MTH00129   87 MDEINDPHLTIKAMGHQWYWSYEYTDY--EDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVLHSWA 164

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2265312620 183 VPALGIKTDAVPGRLNQAGIFIKRPGTFYGQCSEICGANHSFMPIVIEAVSLDRYINWMLSL 244
Cdd:MTH00129  165 VPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLM 226
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 23-244 2.36e-106

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 306.64  E-value: 2.36e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265312620  23 LGFQEAAAPVMEEIVFFHDQIMFLLVIIVIVVLWLLVEALNGKYYDRDLIDGTLLEIVWTLIPAVILVFIASPSLKLLYL 102
Cdd:MTH00098    7 LGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPSLRILYM 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265312620 103 MDEVVSPALTIKAIGHQWYWSYEYSDYqeETLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSFA 182
Cdd:MTH00098   87 MDEINNPSLTVKTMGHQWYWSYEYTDY--EDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVLHSWA 164

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2265312620 183 VPALGIKTDAVPGRLNQAGIFIKRPGTFYGQCSEICGANHSFMPIVIEAVSLDRYINWMLSL 244
Cdd:MTH00098  165 VPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKWSASM 226
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 23-243 1.40e-104

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 302.08  E-value: 1.40e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265312620  23 LGFQEAAAPVMEEIVFFHDQIMFLLVIIVIVVLWLLVEALNGKYYDRDLIDGTLLEIVWTLIPAVILVFIASPSLKLLYL 102
Cdd:MTH00076    7 LGFQDAASPIMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPSLRILYL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265312620 103 MDEVVSPALTIKAIGHQWYWSYEYSDYqeETLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSFA 182
Cdd:MTH00076   87 MDEINDPHLTVKAIGHQWYWSYEYTDY--EDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVLHSWA 164

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2265312620 183 VPALGIKTDAVPGRLNQAGIFIKRPGTFYGQCSEICGANHSFMPIVIEAVSLDRYINWMLS 243
Cdd:MTH00076  165 VPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLNWSSS 225
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 23-245 1.80e-104

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 301.78  E-value: 1.80e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265312620  23 LGFQEAAAPVMEEIVFFHDQIMFLLVIIVIVVLWLLVEALNGKYYDRDLIDGTLLEIVWTLIPAVILVFIASPSLKLLYL 102
Cdd:MTH00008    7 LMFQDAASPVMLQLISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPSLRLLYL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265312620 103 MDEVVSPALTIKAIGHQWYWSYEYSDYQEetLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSFA 182
Cdd:MTH00008   87 MDEVSNPSITLKTIGHQWYWSYEYSDFSN--LEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVIHSWT 164

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2265312620 183 VPALGIKTDAVPGRLNQAGIFIKRPGTFYGQCSEICGANHSFMPIVIEAVSLDRYINWMLSLS 245
Cdd:MTH00008  165 VPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKWVSSFA 227
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 22-240 2.33e-102

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 296.80  E-value: 2.33e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265312620  22 HLGFQEAAAPVMEEIVFFHDQIMFLLVIIVIVVLWLLVEALNGKYYDRDLIDGTLLEIVWTLIPAVILVFIASPSLKLLY 101
Cdd:MTH00185    6 QLGLQDAASPVMEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPSLRILY 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265312620 102 LMDEVVSPALTIKAIGHQWYWSYEYSDYqeETLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSF 181
Cdd:MTH00185   86 LMDEINDPHLTIKAMGHQWYWSYEYTDY--EQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVLHSW 163

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2265312620 182 AVPALGIKTDAVPGRLNQAGIFIKRPGTFYGQCSEICGANHSFMPIVIEAVSLDRYINW 240
Cdd:MTH00185  164 TVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENW 222
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 15-241 2.95e-99

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 290.00  E-value: 2.95e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265312620  15 KDIPESWHLGFQEAAAPVMEEIVFFHDQIMFLLVIIVIVVLWLLVEALNGKYYDR---DLIDGTLLEIVWTLIPAVILVF 91
Cdd:MTH00027   27 KDANEPWQLGFQDAGSPVMEEIIMLHDQILFILTIIVGVVLWLIIRILLGNNYYSyywNKLDGSLIEVIWTLIPAFILIL 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265312620  92 IASPSLKLLYLMDE-VVSPALTIKAIGHQWYWSYEYSDYQEETLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRI 170
Cdd:MTH00027  107 IAFPSLRLLYIMDEcGFSANITIKVTGHQWYWSYSYEDYGEKNIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRV 186

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2265312620 171 LVTGADVLHSFAVPALGIKTDAVPGRLNQAGIFIKRPGTFYGQCSEICGANHSFMPIVIEAVSLDRYINWM 241
Cdd:MTH00027  187 LITAADVLHSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYIDWI 257
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 109-240 4.12e-97

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: 279.46  E-value: 4.12e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265312620 109 PALTIKAIGHQWYWSYEYSDYqeETLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSFAVPALGI 188
Cdd:cd13912     1 PSLTIKAIGHQWYWSYEYSDF--NDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGI 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2265312620 189 KTDAVPGRLNQAGIFIKRPGTFYGQCSEICGANHSFMPIVIEAVSLDRYINW 240
Cdd:cd13912    79 KVDAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
111-232 1.78e-82

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 242.32  E-value: 1.78e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265312620 111 LTIKAIGHQWYWSYEYSDYqeETLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSFAVPALGIKT 190
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDF--GDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKT 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2265312620 191 DAVPGRLNQAGIFIKRPGTFYGQCSEICGANHSFMPIVIEAV 232
Cdd:pfam00116  79 DAVPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 62-244 4.99e-73

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 222.19  E-value: 4.99e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265312620  62 LNGKYYDRDLIDGTLLEIVWTLIPAVILVFIASPSLKLLYLMDEV-VSPALTIKAIGHQWYWSYEYSDYQEetLEFDSYM 140
Cdd:MTH00080   48 SNNFYFKSKKIEYQFGELLCSVFPVLILLMQMVPSLSLLYYYGLMnLDSNLTVKVTGHQWYWSYEFSDIPG--LEFDSYM 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265312620 141 VPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSFAVPALGIKTDAVPGRLNQAGIFIKRPGTFYGQCSEICGA 220
Cdd:MTH00080  126 KSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDAMSGILSTLCYSFPMPGVFYGQCSEICGA 205

                         170       180
                  ....*....|....*....|....
gi 2265312620 221 NHSFMPIVIEAVSLDRYINWMLSL 244
Cdd:MTH00080  206 NHSFMPIAVEVTLLDNFKEWCKLL 229
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
75-241 3.90e-60

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 189.27  E-value: 3.90e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265312620  75 TLLEIVWTLIPAVILVFIASPSLKLLYLMDEVVSPALTIKAIGHQWYWSYEYSDYQEETlefdsymvptsdlnsgdfrll 154
Cdd:COG1622    77 TKLEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIAT--------------------- 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265312620 155 evDNRLVVPINTHVRILVTGADVLHSFAVPALGIKTDAVPGRLNQAGIFIKRPGTFYGQCSEICGANHSFMPIVIEAVSL 234
Cdd:COG1622   136 --VNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSP 213


                  ....*..
gi 2265312620 235 DRYINWM 241
Cdd:COG1622   214 EEFDAWL 220
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 74-241 2.50e-49

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: 160.62  E-value: 2.50e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265312620  74 GTLLEIVWTLIPAVILV-FIASPSLKLLYLMDEVVSPALTIKAIGHQWYWSYEYSDYqeetlefdsymvptsdlnsgdfr 152
Cdd:TIGR02866  53 NRRLEYVWTVIPLIIVVgLFAATAKGLLYLERPIPKDALKVKVTGYQWWWDFEYPES----------------------- 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265312620 153 LLEVDNRLVVPINTHVRILVTGADVLHSFAVPALGIKTDAVPGRLNQAGIFIKRPGTFYGQCSEICGANHSFMPIVIEAV 232
Cdd:TIGR02866 110 GFTTVNELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVV 189


                  ....*....
gi 2265312620 233 SLDRYINWM 241
Cdd:TIGR02866 190 PKEEFDAYV 198
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 76-232 1.83e-47

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 155.88  E-value: 1.83e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265312620  76 LLEIVWTLIPAVILVFIASpsLKLLYLM-DEVVSPALTIKAIGHQWYWSYEYSDyqeeTLEFDSYMvpTSDLNSgdfrll 154
Cdd:MTH00047   48 VLELLWTVVPTLLVLVLCF--LNLNFITsDLDCFSSETIKVIGHQWYWSYEYSF----GGSYDSFM--TDDIFG------ 113

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2265312620 155 eVDNRLVVPINTHVRILVTGADVLHSFAVPALGIKTDAVPGRLNQAGIFIKRPGTFYGQCSEICGANHSFMPIVIEAV 232
Cdd:MTH00047  114 -VDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCPDRHGVFVGYCSELCGVGHSYMPIVIEVV 190
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 136-237 1.93e-46

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 151.90  E-value: 1.93e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265312620 136 FDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSFAVPALGIKTDAVPGRLNQAGIFIKRPGTFYGQCS 215
Cdd:PTZ00047   51 FQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCS 130

                          90       100
                  ....*....|....*....|..
gi 2265312620 216 EICGANHSFMPIVIEAVSLDRY 237
Cdd:PTZ00047  131 EMCGTLHGFMPIVVEAVSPEAY 152
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 111-230 8.03e-31

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: 109.69  E-value: 8.03e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265312620 111 LTIKAIGHQWYWSYEYSDyqeetlefdsymvptsdlnsgdfrlLEVDNRLVVPINTHVRILVTGADVLHSFAVPALGIKT 190
Cdd:cd13842     1 LTVYVTGVQWSWTFIYPN-------------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKV 55

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2265312620 191 DAVPGRLNQAGIFIKRPGTFYGQCSEICGANHSFMPIVIE 230
Cdd:cd13842    56 DAVPGYTSELWFVADKPGTYTIICAEYCGLGHSYMLGKVE 95
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 110-225 1.14e-30

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: 109.63  E-value: 1.14e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265312620 110 ALTIKAIGHQWYWSYEYSDYQEETLEfdsymvpTSdlnsgdfrllevdNRLVVPINTHVRILVTGADVLHSFAVPALGIK 189
Cdd:cd04213     1 ALTIEVTGHQWWWEFRYPDEPGRGIV-------TA-------------NELHIPVGRPVRLRLTSADVIHSFWVPSLAGK 60

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2265312620 190 TDAVPGRLNQAGIFIKRPGTFYGQCSEICGANHSFM 225
Cdd:cd04213    61 MDMIPGRTNRLWLQADEPGVYRGQCAEFCGASHALM 96
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 110-225 3.51e-27

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: 100.40  E-value: 3.51e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265312620 110 ALTIKAIGHQWYWSYEYSDYQEEtlefdsymvptsdlnsgdfrllevDNRLVVPINTHVRILVTGADVLHSFAVPALGIK 189
Cdd:cd13915     1 ALEIQVTGRQWMWEFTYPNGKRE------------------------INELHVPVGKPVRLILTSKDVIHSFYVPAFRIK 56

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2265312620 190 TDAVPGRLNQAGIFIKRPGTFYGQCSEICGANHSFM 225
Cdd:cd13915    57 QDVVPGRYTYLWFEATKPGEYDLFCTEYCGTGHSGM 92
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 110-225 3.87e-25

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: 95.40  E-value: 3.87e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265312620 110 ALTIKAIGHQWYWSYEYSDYqeetlefDSYMVPTSDLNSGDfrllevdnrLVVPINTHVRILVTGADVLHSFAVPALGIK 189
Cdd:cd13919     1 ALVVEVTAQQWAWTFRYPGG-------DGKLGTDDDVTSPE---------LHLPVGRPVLFNLRSKDVIHSFWVPEFRVK 64

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2265312620 190 TDAVPGRLNQAGIFIKRPGTFYGQCSEICGANHSFM 225
Cdd:cd13919    65 QDAVPGRTTRLWFTPTREGEYEVRCAELCGLGHYRM 100
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 112-241 2.44e-24

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


Pssm-ID: 259981 [Multi-domain]  Cd Length: 108  Bit Score: 93.24  E-value: 2.44e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265312620 112 TIKAIGHQWYWSYEYSDYQEETlefdsymvptsdlnsgdfrllevDNRLVVPINTHVRILVTGADVLHSFAVPALGIKTD 191
Cdd:cd13914     2 EIEVEAYQWGWEFSYPEANVTT-----------------------SEQLVIPADRPVYFRITSRDVIHAFHVPELGLKQD 58

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2265312620 192 AVPGRLNQAGIFIKRPGTFYGQCSEICGANHSFMPIVIEAVSLDRYINWM 241
Cdd:cd13914    59 AFPGQYNTIKTEATEEGEYQLYCAEYCGAGHSQMLSTVTVVSQDEYQQWL 108
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 84-241 7.05e-24

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


Pssm-ID: 259985 [Multi-domain]  Cd Length: 139  Bit Score: 93.29  E-value: 7.05e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265312620  84 IPAVILV-FIASPSLKLLYLMD---EVVSPALTIKAIGHQWYWSYEYSDYQEETlefdsymvptsdlnsgdfrllevdNR 159
Cdd:cd13918     2 LSAIIVIsLIVWTYGMLLYVEDppdEADEDALEVEVEGFQFGWQFEYPNGVTTG------------------------NT 57

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265312620 160 LVVPINTHVRILVTGADVLHSFAVPALGIKTDAVPGRLNQAGIFIKRPGTFYGQCSEICGANHSFMPIVIEAVSLDRYIN 239
Cdd:cd13918    58 LRVPADTPIALRVTSTDVFHTFGIPELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEFEA 137


                  ..
gi 2265312620 240 WM 241
Cdd:cd13918   138 WY 139
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 17-99 8.30e-17

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: 73.13  E-value: 8.30e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265312620  17 IPESWHLGFQEAAAPVMEEIVFFHDQIMFLLVIIVIVVLWLLVEAL------NGKYYDRDLIDGTLLEIVWTLIPAVILV 90
Cdd:pfam02790   1 MPTPWGLGFQDAASPLMEGLLELHDYIMFILTLILILVLYILVTCLirfnrrKNPITARYTTHGQTIEIIWTIIPAVILI 80


                  ....*....
gi 2265312620  91 FIASPSLKL 99
Cdd:pfam02790  81 LIALPSFKL 89
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 158-225 2.92e-12

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: 61.05  E-value: 2.92e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2265312620 158 NRLVVPINTHVRILVTGADVLHSFAVPALGIKTDAVPGRLNQAGIFIKRPGTFYGQCSEICGANHSFM 225
Cdd:cd13913    25 NEIEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNM 92
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 111-232 4.24e-08

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: 49.85  E-value: 4.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265312620 111 LTIKAIGHQWYWSYEYSDYQEETLefdsymvptsdlnsgdfrllevdNRLVVPINTHVRILVTGADVLHSFAVPALGIKT 190
Cdd:cd04212     1 LEIQVVSLDWKWLFIYPEQGIATV-----------------------NELVIPVGRPVNFRLTSDSVMNSFFIPQLGGQI 57

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2265312620 191 DAVPGRLNQAGIFIKRPGTFYGQCSEICGANHSFMPIVIEAV 232
Cdd:cd04212    58 YAMAGMQTQLHLIADKPGTYQGLSANYSGEGFSDMKFKVLAV 99
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 112-225 3.04e-07

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: 47.38  E-value: 3.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265312620 112 TIKAIGHQWYWSyeysdyqeetlefdsyMVPTsdlnsgdfrllevdnrlVVPINTHVRILVTGADVLHSFAV--PALGI- 188
Cdd:cd13916     2 VVAVTGHQWYWE----------------LSRT-----------------EIPAGKPVEFRVTSADVNHGFGIydPDMRLl 48

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2265312620 189 -KTDAVPGRLNQAGIFIKRPGTFYGQCSEICGANHSFM 225
Cdd:cd13916    49 aQTQAMPGYTNVLRYTFDKPGTYTILCLEYCGLAHHVM 86
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 147-230 4.08e-04

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: 38.75  E-value: 4.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2265312620 147 NSGDFRLLEVDNRLVVPINTHVR-ILVTGADVLHSFAVPALGIKTDA---------------VPGRLNQAGIFIKRPGTF 210
Cdd:cd00920    12 FTYNGVLLFGPPVLVVPVGDTVRvQFVNKLGENHSVTIAGFGVPVVAmagganpglvntlviGPGESAEVTFTTDQAGVY 91

                          90       100
                  ....*....|....*....|
gi 2265312620 211 YGQCSEICGaNHSFMPIVIE 230
Cdd:cd00920    92 WFYCTIPGH-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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