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Conserved domains on  [gi|2509724777|gb|WHU32463|]
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cytochrome c oxidase subunit II, partial (mitochondrion) [Anopheles marshallii]

Protein Classification

cytochrome c oxidase subunit II( domain architecture ID 11475927)

cytochrome c oxidase subunit II, part of the functional core of the enzyme, transfers the electrons from cytochrome c via its binuclear copper A center to the bimetallic center of the catalytic subunit I

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-188 4.34e-140

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 389.19  E-value: 4.34e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509724777   1 SSPLMEQLNFFHDHTLLILTMITILVGYIMGMLMFNKFTNRYLLHGQTIEIIWTVLPAIILMFIAFPSLRLLYLMDEINT 80
Cdd:MTH00154   13 ASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLYLLDEVNN 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509724777  81 PSITLKSIGHQWYWSYEYSDFLNLEFDSYMIPTNELDMNGFRLLDVDNRIILPMNNQIRILVTATDVLHSWTVPSLGVKV 160
Cdd:MTH00154   93 PSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKV 172

                         170       180
                  ....*....|....*....|....*...
gi 2509724777 161 DATPGRLNQINFLINRPGLFFGQCSEIC 188
Cdd:MTH00154  173 DAVPGRLNQLNFLINRPGLFFGQCSEIC 200
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-188 4.34e-140

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 389.19  E-value: 4.34e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509724777   1 SSPLMEQLNFFHDHTLLILTMITILVGYIMGMLMFNKFTNRYLLHGQTIEIIWTVLPAIILMFIAFPSLRLLYLMDEINT 80
Cdd:MTH00154   13 ASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLYLLDEVNN 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509724777  81 PSITLKSIGHQWYWSYEYSDFLNLEFDSYMIPTNELDMNGFRLLDVDNRIILPMNNQIRILVTATDVLHSWTVPSLGVKV 160
Cdd:MTH00154   93 PSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKV 172

                         170       180
                  ....*....|....*....|....*...
gi 2509724777 161 DATPGRLNQINFLINRPGLFFGQCSEIC 188
Cdd:MTH00154  173 DAVPGRLNQLNFLINRPGLFFGQCSEIC 200
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 81-188 4.18e-76

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: 223.99  E-value: 4.18e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509724777  81 PSITLKSIGHQWYWSYEYSDFLNLEFDSYMIPTNELDMNGFRLLDVDNRIILPMNNQIRILVTATDVLHSWTVPSLGVKV 160
Cdd:cd13912     1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                          90       100
                  ....*....|....*....|....*...
gi 2509724777 161 DATPGRLNQINFLINRPGLFFGQCSEIC 188
Cdd:cd13912    81 DAVPGRLNQTSFFIERPGVYYGQCSEIC 108
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
83-188 3.30e-69

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 206.11  E-value: 3.30e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509724777  83 ITLKSIGHQWYWSYEYSDFLNLEFDSYMIPTNELDMNGFRLLDVDNRIILPMNNQIRILVTATDVLHSWTVPSLGVKVDA 162
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100
                  ....*....|....*....|....*.
gi 2509724777 163 TPGRLNQINFLINRPGLFFGQCSEIC 188
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEIC 106
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
2-188 7.48e-44

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 145.36  E-value: 7.48e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509724777   2 SPLMEQLNFFHDHTLLILTMITILVgyiMGMLMF---------NKFTNRYLLHGQTIEIIWTVLPAIILMFIAFPSLRLL 72
Cdd:COG1622    26 GPIAEEIDDLFWVSLIIMLVIFVLV---FGLLLYfairyrrrkGDADPAQFHHNTKLEIVWTVIPIIIVIVLAVPTLRVL 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509724777  73 YLMDEINTPSITLKSIGHQWYWSYEYSDflnlefdsymipTNELdmngfrlldVDNRIILPMNNQIRILVTATDVLHSWT 152
Cdd:COG1622   103 HALDDAPEDPLTVEVTGYQWKWLFRYPD------------QGIA---------TVNELVLPVGRPVRFLLTSADVIHSFW 161

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2509724777 153 VPSLGVKVDATPGRLNQINFLINRPGLFFGQCSEIC 188
Cdd:COG1622   162 VPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELC 197
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 2-188 1.71e-39

cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of mitochondria (and one of several possible acceptors in prokaryotes) in the electron transport chain of aerobic respiration. The enzyme couples the oxidation of reduced cytochrome c with the reduction of molecular oxygen to water. This process results in the pumping of four protons across the membrane which are used in the proton gradient powered synthesis of ATP. The oxidase contains two heme a cofactors and three copper atoms as well as other bound ions. [Energy metabolism, Electron transport]


Pssm-ID: 274329 [Multi-domain]  Cd Length: 199  Bit Score: 133.27  E-value: 1.71e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509724777   2 SPLMEQLNFFHDHTLLILTMITILVGYIMGMLMFnKFTNR-------YLLHGQTIEIIWTVLPAIILM-FIAFPSLRLLY 73
Cdd:TIGR02866   3 GEIAQQIAFLFLFVLAVSTLISLLVAALLAYVVW-KFRRKgdeekpsQIHGNRRLEYVWTVIPLIIVVgLFAATAKGLLY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509724777  74 LMDEINTPSITLKSIGHQWYWSYEYSDFlnlefdsymiptneldmnGFRlldVDNRIILPMNNQIRILVTATDVLHSWTV 153
Cdd:TIGR02866  82 LERPIPKDALKVKVTGYQWWWDFEYPES------------------GFT---TVNELVLPAGTPVELQVTSKDVIHSFWV 140

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2509724777 154 PSLGVKVDATPGRLNQINFLINRPGLFFGQCSEIC 188
Cdd:TIGR02866 141 PELGGKIDAIPGQTNALWFNADEPGVYYGFCAELC 175
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-188 4.34e-140

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 389.19  E-value: 4.34e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509724777   1 SSPLMEQLNFFHDHTLLILTMITILVGYIMGMLMFNKFTNRYLLHGQTIEIIWTVLPAIILMFIAFPSLRLLYLMDEINT 80
Cdd:MTH00154   13 ASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLYLLDEVNN 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509724777  81 PSITLKSIGHQWYWSYEYSDFLNLEFDSYMIPTNELDMNGFRLLDVDNRIILPMNNQIRILVTATDVLHSWTVPSLGVKV 160
Cdd:MTH00154   93 PSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKV 172

                         170       180
                  ....*....|....*....|....*...
gi 2509724777 161 DATPGRLNQINFLINRPGLFFGQCSEIC 188
Cdd:MTH00154  173 DAVPGRLNQLNFLINRPGLFFGQCSEIC 200
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-188 9.18e-114

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 323.04  E-value: 9.18e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509724777   1 SSPLMEQLNFFHDHTLLILTMITILVGYIMGMLMFNKFTNRYLLHGQTIEIIWTVLPAIILMFIAFPSLRLLYLMDEINT 80
Cdd:MTH00140   13 ASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPSLRLLYLLDETNN 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509724777  81 PSITLKSIGHQWYWSYEYSDFLNLEFDSYMIPTNELDMNGFRLLDVDNRIILPMNNQIRILVTATDVLHSWTVPSLGVKV 160
Cdd:MTH00140   93 PLLTVKAIGHQWYWSYEYSDFSVIEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVIHSWTVPSLGVKV 172

                         170       180
                  ....*....|....*....|....*...
gi 2509724777 161 DATPGRLNQINFLINRPGLFFGQCSEIC 188
Cdd:MTH00140  173 DAIPGRLNQLSFEPKRPGVFYGQCSEIC 200
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-188 1.49e-110

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 314.73  E-value: 1.49e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509724777   1 SSPLMEQLNFFHDHTLLILTMITILVGYIMGMLMFNKFTNRYLLHGQTIEIIWTVLPAIILMFIAFPSLRLLYLMDEINT 80
Cdd:MTH00139   13 ASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPSLRLLYLMDEVSD 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509724777  81 PSITLKSIGHQWYWSYEYSDFLNLEFDSYMIPTNELDMNGFRLLDVDNRIILPMNNQIRILVTATDVLHSWTVPSLGVKV 160
Cdd:MTH00139   93 PYLTFKAVGHQWYWSYEYSDFKNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVLHSWTVPSLGVKI 172

                         170       180
                  ....*....|....*....|....*...
gi 2509724777 161 DATPGRLNQINFLINRPGLFFGQCSEIC 188
Cdd:MTH00139  173 DAVPGRLNQVGFFINRPGVFYGQCSEIC 200
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-188 3.66e-108

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 308.71  E-value: 3.66e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509724777   1 SSPLMEQLNFFHDHTLLILTMITILVGYIMGMLMFNKFTNRYLLHGQTIEIIWTVLPAIILMFIAFPSLRLLYLMDEINT 80
Cdd:MTH00008   13 ASPVMLQLISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPSLRLLYLMDEVSN 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509724777  81 PSITLKSIGHQWYWSYEYSDFLNLEFDSYMIPTNELDMNGFRLLDVDNRIILPMNNQIRILVTATDVLHSWTVPSLGVKV 160
Cdd:MTH00008   93 PSITLKTIGHQWYWSYEYSDFSNLEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVIHSWTVPSLGVKV 172

                         170       180
                  ....*....|....*....|....*...
gi 2509724777 161 DATPGRLNQINFLINRPGLFFGQCSEIC 188
Cdd:MTH00008  173 DAVPGRLNQIGFTITRPGVFYGQCSEIC 200
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-188 4.06e-108

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 308.38  E-value: 4.06e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509724777   1 SSPLMEQLNFFHDHTLLILTMITILVGYIMGMLMFNKFTNRYLLHGQTIEIIWTVLPAIILMFIAFPSLRLLYLMDEINT 80
Cdd:MTH00117   13 SSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPSLRILYLMDEINN 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509724777  81 PSITLKSIGHQWYWSYEYSDFLNLEFDSYMIPTNELDMNGFRLLDVDNRIILPMNNQIRILVTATDVLHSWTVPSLGVKV 160
Cdd:MTH00117   93 PHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVLHSWAVPSLGVKT 172

                         170       180
                  ....*....|....*....|....*...
gi 2509724777 161 DATPGRLNQINFLINRPGLFFGQCSEIC 188
Cdd:MTH00117  173 DAVPGRLNQTSFITTRPGVFYGQCSEIC 200
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-188 1.64e-107

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 307.01  E-value: 1.64e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509724777   1 SSPLMEQLNFFHDHTLLILTMITILVGYIMGMLMFNKFTNRYLLHGQTIEIIWTVLPAIILMFIAFPSLRLLYLMDEINT 80
Cdd:MTH00038   13 SSPLMEELIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPSLQLLYLMDEVNN 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509724777  81 PSITLKSIGHQWYWSYEYSDFLNLEFDSYMIPTNELDMNGFRLLDVDNRIILPMNNQIRILVTATDVLHSWTVPSLGVKV 160
Cdd:MTH00038   93 PFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVLHSWAVPSLGVKM 172

                         170       180
                  ....*....|....*....|....*...
gi 2509724777 161 DATPGRLNQINFLINRPGLFFGQCSEIC 188
Cdd:MTH00038  173 DAVPGRLNQTTFFISRTGLFYGQCSEIC 200
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-188 1.22e-105

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 302.28  E-value: 1.22e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509724777   1 SSPLMEQLNFFHDHTLLILTMITILVGYIMGMLMFNKFTNRYLLHGQTIEIIWTVLPAIILMFIAFPSLRLLYLMDEINT 80
Cdd:MTH00168   13 ASPVMEELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPSLRLLYLMDEIDK 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509724777  81 PSITLKSIGHQWYWSYEYSDFLNLEFDSYMIPTNELDMNGFRLLDVDNRIILPMNNQIRILVTATDVLHSWTVPSLGVKV 160
Cdd:MTH00168   93 PDLTIKAVGHQWYWSYEYTDYNDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVLHSWTLPSLGLKM 172

                         170       180
                  ....*....|....*....|....*...
gi 2509724777 161 DATPGRLNQINFLINRPGLFFGQCSEIC 188
Cdd:MTH00168  173 DAVPGRLNQLAFLSSRPGSFYGQCSEIC 200
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 1-188 1.03e-99

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 287.38  E-value: 1.03e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509724777   1 SSPLMEQLNFFHDHTLLILTMITILVGYIMGMLMFNKFTNRYLLHGQTIEIIWTVLPAIILMFIAFPSLRLLYLMDEINT 80
Cdd:MTH00129   13 ASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPSLRILYLMDEIND 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509724777  81 PSITLKSIGHQWYWSYEYSDFLNLEFDSYMIPTNELDMNGFRLLDVDNRIILPMNNQIRILVTATDVLHSWTVPSLGVKV 160
Cdd:MTH00129   93 PHLTIKAMGHQWYWSYEYTDYEDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVLHSWAVPALGVKM 172

                         170       180
                  ....*....|....*....|....*...
gi 2509724777 161 DATPGRLNQINFLINRPGLFFGQCSEIC 188
Cdd:MTH00129  173 DAVPGRLNQTAFIASRPGVFYGQCSEIC 200
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 1-188 2.36e-98

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 284.09  E-value: 2.36e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509724777   1 SSPLMEQLNFFHDHTLLILTMITILVGYIMGMLMFNKFTNRYLLHGQTIEIIWTVLPAIILMFIAFPSLRLLYLMDEINT 80
Cdd:MTH00185   13 ASPVMEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPSLRILYLMDEIND 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509724777  81 PSITLKSIGHQWYWSYEYSDFLNLEFDSYMIPTNELDMNGFRLLDVDNRIILPMNNQIRILVTATDVLHSWTVPSLGVKV 160
Cdd:MTH00185   93 PHLTIKAMGHQWYWSYEYTDYEQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVLHSWTVPALGVKM 172

                         170       180
                  ....*....|....*....|....*...
gi 2509724777 161 DATPGRLNQINFLINRPGLFFGQCSEIC 188
Cdd:MTH00185  173 DAVPGRLNQATFIISRPGLYYGQCSEIC 200
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-188 1.90e-97

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 281.61  E-value: 1.90e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509724777   1 SSPLMEQLNFFHDHTLLILTMITILVGYIMGMLMFNKFTNRYLLHGQTIEIIWTVLPAIILMFIAFPSLRLLYLMDEINT 80
Cdd:MTH00098   13 TSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPSLRILYMMDEINN 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509724777  81 PSITLKSIGHQWYWSYEYSDFLNLEFDSYMIPTNELDMNGFRLLDVDNRIILPMNNQIRILVTATDVLHSWTVPSLGVKV 160
Cdd:MTH00098   93 PSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVLHSWAVPSLGLKT 172

                         170       180
                  ....*....|....*....|....*...
gi 2509724777 161 DATPGRLNQINFLINRPGLFFGQCSEIC 188
Cdd:MTH00098  173 DAIPGRLNQTTLMSTRPGLYYGQCSEIC 200
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 2-188 2.13e-95

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 276.27  E-value: 2.13e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509724777   2 SPLMEQLNFFHDHTLLILTMITILVGYIMGMLMFNKFTNRYLLHGQTIEIIWTVLPAIILMFIAFPSLRLLYLMDEINTP 81
Cdd:MTH00076   14 SPIMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPSLRILYLMDEINDP 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509724777  82 SITLKSIGHQWYWSYEYSDFLNLEFDSYMIPTNELDMNGFRLLDVDNRIILPMNNQIRILVTATDVLHSWTVPSLGVKVD 161
Cdd:MTH00076   94 HLTVKAIGHQWYWSYEYTDYEDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVLHSWAVPSLGIKTD 173

                         170       180
                  ....*....|....*....|....*..
gi 2509724777 162 ATPGRLNQINFLINRPGLFFGQCSEIC 188
Cdd:MTH00076  174 AIPGRLNQTSFIASRPGVYYGQCSEIC 200
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 1-188 4.62e-95

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 275.86  E-value: 4.62e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509724777   1 SSPLMEQLNFFHDHTLLILTMITILVGYIMGMLMFNKFTNRYLLHGQTIEIIWTVLPAIILMFIAFPSLRLLYLMDEINT 80
Cdd:MTH00023   22 ADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKLLYLMDEVVS 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509724777  81 PSITLKSIGHQWYWSYEYSDFL--NLEFDSYMIPTNELDMNGFRLLDVDNRIILPMNNQIRILVTATDVLHSWTVPSLGV 158
Cdd:MTH00023  102 PALTIKAIGHQWYWSYEYSDYEgeTLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSFAVPSLGL 181

                         170       180       190
                  ....*....|....*....|....*....|
gi 2509724777 159 KVDATPGRLNQINFLINRPGLFFGQCSEIC 188
Cdd:MTH00023  182 KIDAVPGRLNQTGFFIKRPGVFYGQCSEIC 211
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 1-188 4.77e-91

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 265.49  E-value: 4.77e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509724777   1 SSPLMEQLNFFHDHTLLILTMITILVGYIMGMLMFNKFTNRYLLHGQTIEIIWTVLPAIILMFIAFPSLRLLYLMDEINT 80
Cdd:MTH00051   15 ASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSLKLLYLMDEVID 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509724777  81 PSITLKSIGHQWYWSYEYSDF--LNLEFDSYMIPTNELDMNGFRLLDVDNRIILPMNNQIRILVTATDVLHSWTVPSLGV 158
Cdd:MTH00051   95 PALTIKAIGHQWYWSYEYSDYgtDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSFAVPSLSV 174

                         170       180       190
                  ....*....|....*....|....*....|
gi 2509724777 159 KVDATPGRLNQINFLINRPGLFFGQCSEIC 188
Cdd:MTH00051  175 KIDAVPGRLNQTSFFIKRPGVFYGQCSEIC 204
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 81-188 4.18e-76

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: 223.99  E-value: 4.18e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509724777  81 PSITLKSIGHQWYWSYEYSDFLNLEFDSYMIPTNELDMNGFRLLDVDNRIILPMNNQIRILVTATDVLHSWTVPSLGVKV 160
Cdd:cd13912     1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                          90       100
                  ....*....|....*....|....*...
gi 2509724777 161 DATPGRLNQINFLINRPGLFFGQCSEIC 188
Cdd:cd13912    81 DAVPGRLNQTSFFIERPGVYYGQCSEIC 108
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 2-188 1.00e-70

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 215.27  E-value: 1.00e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509724777   2 SPLMEQLNFFHDHTLLILTMIT-ILVGYIMGMLMFNKFTNRYL--LHGQTIEIIWTVLPAIILMFIAFPSLRLLYLMDE- 77
Cdd:MTH00027   42 SPVMEEIIMLHDQILFILTIIVgVVLWLIIRILLGNNYYSYYWnkLDGSLIEVIWTLIPAFILILIAFPSLRLLYIMDEc 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509724777  78 INTPSITLKSIGHQWYWSYEYSDF--LNLEFDSYMIPTNELDMNGFRLLDVDNRIILPMNNQIRILVTATDVLHSWTVPS 155
Cdd:MTH00027  122 GFSANITIKVTGHQWYWSYSYEDYgeKNIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAADVLHSWTVPS 201

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2509724777 156 LGVKVDATPGRLNQINFLINRPGLFFGQCSEIC 188
Cdd:MTH00027  202 LAVKMDAVPGRINETGFLIKRPGIFYGQCSEIC 234
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
83-188 3.30e-69

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 206.11  E-value: 3.30e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509724777  83 ITLKSIGHQWYWSYEYSDFLNLEFDSYMIPTNELDMNGFRLLDVDNRIILPMNNQIRILVTATDVLHSWTVPSLGVKVDA 162
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100
                  ....*....|....*....|....*.
gi 2509724777 163 TPGRLNQINFLINRPGLFFGQCSEIC 188
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEIC 106
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 2-188 3.27e-62

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 192.15  E-value: 3.27e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509724777   2 SPLMEQLNFFHDHTLLILTMITILVGYIMGMLMFNKFTNRYLLHGQTIEIIWTVLPAIILMFIAFPSLRLLYLMDEINTP 81
Cdd:MTH00080   16 SSYMDWFHNFNCSLLFGEFVLAFVVFLFLYLISNNFYFKSKKIEYQFGELLCSVFPVLILLMQMVPSLSLLYYYGLMNLD 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509724777  82 S-ITLKSIGHQWYWSYEYSDFLNLEFDSYMIPTNELDMNGFRLLDVDNRIILPMNNQIRILVTATDVLHSWTVPSLGVKV 160
Cdd:MTH00080   96 SnLTVKVTGHQWYWSYEFSDIPGLEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKM 175

                         170       180
                  ....*....|....*....|....*...
gi 2509724777 161 DATPGRLNQINFLINRPGLFFGQCSEIC 188
Cdd:MTH00080  176 DAMSGILSTLCYSFPMPGVFYGQCSEIC 203
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
2-188 7.48e-44

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 145.36  E-value: 7.48e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509724777   2 SPLMEQLNFFHDHTLLILTMITILVgyiMGMLMF---------NKFTNRYLLHGQTIEIIWTVLPAIILMFIAFPSLRLL 72
Cdd:COG1622    26 GPIAEEIDDLFWVSLIIMLVIFVLV---FGLLLYfairyrrrkGDADPAQFHHNTKLEIVWTVIPIIIVIVLAVPTLRVL 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509724777  73 YLMDEINTPSITLKSIGHQWYWSYEYSDflnlefdsymipTNELdmngfrlldVDNRIILPMNNQIRILVTATDVLHSWT 152
Cdd:COG1622   103 HALDDAPEDPLTVEVTGYQWKWLFRYPD------------QGIA---------TVNELVLPVGRPVRFLLTSADVIHSFW 161

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2509724777 153 VPSLGVKVDATPGRLNQINFLINRPGLFFGQCSEIC 188
Cdd:COG1622   162 VPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELC 197
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 2-188 1.71e-39

cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of mitochondria (and one of several possible acceptors in prokaryotes) in the electron transport chain of aerobic respiration. The enzyme couples the oxidation of reduced cytochrome c with the reduction of molecular oxygen to water. This process results in the pumping of four protons across the membrane which are used in the proton gradient powered synthesis of ATP. The oxidase contains two heme a cofactors and three copper atoms as well as other bound ions. [Energy metabolism, Electron transport]


Pssm-ID: 274329 [Multi-domain]  Cd Length: 199  Bit Score: 133.27  E-value: 1.71e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509724777   2 SPLMEQLNFFHDHTLLILTMITILVGYIMGMLMFnKFTNR-------YLLHGQTIEIIWTVLPAIILM-FIAFPSLRLLY 73
Cdd:TIGR02866   3 GEIAQQIAFLFLFVLAVSTLISLLVAALLAYVVW-KFRRKgdeekpsQIHGNRRLEYVWTVIPLIIVVgLFAATAKGLLY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509724777  74 LMDEINTPSITLKSIGHQWYWSYEYSDFlnlefdsymiptneldmnGFRlldVDNRIILPMNNQIRILVTATDVLHSWTV 153
Cdd:TIGR02866  82 LERPIPKDALKVKVTGYQWWWDFEYPES------------------GFT---TVNELVLPAGTPVELQVTSKDVIHSFWV 140

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2509724777 154 PSLGVKVDATPGRLNQINFLINRPGLFFGQCSEIC 188
Cdd:TIGR02866 141 PELGGKIDAIPGQTNALWFNADEPGVYYGFCAELC 175
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 47-188 6.67e-36

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 123.91  E-value: 6.67e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509724777  47 QTIEIIWTVLPAIILMFIAFpsLRLLYLMDEIN-TPSITLKSIGHQWYWSYEYSDflNLEFDSYMIPtnelDMNGfrlld 125
Cdd:MTH00047   47 QVLELLWTVVPTLLVLVLCF--LNLNFITSDLDcFSSETIKVIGHQWYWSYEYSF--GGSYDSFMTD----DIFG----- 113

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2509724777 126 VDNRIILPMNNQIRILVTATDVLHSWTVPSLGVKVDATPGRLNQINFLINRPGLFFGQCSEIC 188
Cdd:MTH00047  114 VDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCPDRHGVFVGYCSELC 176
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 106-188 2.41e-32

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 113.76  E-value: 2.41e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509724777 106 FDSYMIPTNELDMNGFRLLDVDNRIILPMNNQIRILVTATDVLHSWTVPSLGVKVDATPGRLNQINFLINRPGLFFGQCS 185
Cdd:PTZ00047   51 FQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCS 130


                  ...
gi 2509724777 186 EIC 188
Cdd:PTZ00047  131 EMC 133
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-71 1.10e-25

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: 94.32  E-value: 1.10e-25
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2509724777   1 SSPLMEQLNFFHDHTLLILTMITILVGYIMGMLMF------NKFTNRYLLHGQTIEIIWTVLPAIILMFIAFPSLRL 71
Cdd:pfam02790  13 ASPLMEGLLELHDYIMFILTLILILVLYILVTCLIrfnrrkNPITARYTTHGQTIEIIWTIIPAVILILIALPSFKL 89
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 83-188 3.06e-21

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: 83.11  E-value: 3.06e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509724777  83 ITLKSIGHQWYWSYEYSDflnlefdsymiptneldmngfrlLDVDNRIILPMNNQIRILVTATDVLHSWTVPSLGVKVDA 162
Cdd:cd13842     1 LTVYVTGVQWSWTFIYPN-----------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDA 57

                          90       100
                  ....*....|....*....|....*.
gi 2509724777 163 TPGRLNQINFLINRPGLFFGQCSEIC 188
Cdd:cd13842    58 VPGYTSELWFVADKPGTYTIICAEYC 83
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 82-188 4.37e-21

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: 83.05  E-value: 4.37e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509724777  82 SITLKSIGHQWYWSYEYSDflnlefdsymiptneLDMNGFRLLdvdNRIILPMNNQIRILVTATDVLHSWTVPSLGVKVD 161
Cdd:cd04213     1 ALTIEVTGHQWWWEFRYPD---------------EPGRGIVTA---NELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMD 62

                          90       100
                  ....*....|....*....|....*..
gi 2509724777 162 ATPGRLNQINFLINRPGLFFGQCSEIC 188
Cdd:cd04213    63 MIPGRTNRLWLQADEPGVYRGQCAEFC 89
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 83-188 2.53e-18

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


Pssm-ID: 259986 [Multi-domain]  Cd Length: 107  Bit Score: 76.14  E-value: 2.53e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509724777  83 ITLKSIGHQWYWSYEYSDFLNLEFDSYMIPTNELdmngfrlldvdnriILPMNNQIRILVTATDVLHSWTVPSLGVKVDA 162
Cdd:cd13919     2 LVVEVTAQQWAWTFRYPGGDGKLGTDDDVTSPEL--------------HLPVGRPVLFNLRSKDVIHSFWVPEFRVKQDA 67

                          90       100
                  ....*....|....*....|....*.
gi 2509724777 163 TPGRLNQINFLINRPGLFFGQCSEIC 188
Cdd:cd13919    68 VPGRTTRLWFTPTREGEYEVRCAELC 93
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 82-188 1.78e-15

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


Pssm-ID: 259982 [Multi-domain]  Cd Length: 98  Bit Score: 68.42  E-value: 1.78e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509724777  82 SITLKSIGHQWYWSYEYSdflnlefdsymiptneldmNGFRlldVDNRIILPMNNQIRILVTATDVLHSWTVPSLGVKVD 161
Cdd:cd13915     1 ALEIQVTGRQWMWEFTYP-------------------NGKR---EINELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQD 58

                          90       100
                  ....*....|....*....|....*..
gi 2509724777 162 ATPGRLNQINFLINRPGLFFGQCSEIC 188
Cdd:cd13915    59 VVPGRYTYLWFEATKPGEYDLFCTEYC 85
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 56-188 3.56e-14

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


Pssm-ID: 259985 [Multi-domain]  Cd Length: 139  Bit Score: 66.32  E-value: 3.56e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509724777  56 LPAIILM-FIAFPSLRLLYLMD---EINTPSITLKSIGHQWYWSYEYSdflnlefdsymiptneldmNGFRLLdvdNRII 131
Cdd:cd13918     2 LSAIIVIsLIVWTYGMLLYVEDppdEADEDALEVEVEGFQFGWQFEYP-------------------NGVTTG---NTLR 59

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2509724777 132 LPMNNQIRILVTATDVLHSWTVPSLGVKVDATPGRLNQINFLINRPGLFFGQCSEIC 188
Cdd:cd13918    60 VPADTPIALRVTSTDVFHTFGIPELRVKADAIPGEYTSTWFEADEPGTYEAKCYELC 116
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 89-188 1.81e-13

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: 63.58  E-value: 1.81e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2509724777  89 GHQWYWSYEYSDFLNLEFdsymiptneldmngfrlldvdNRIILPMNNQIRILVTATDVLHSWTVPSLGVKVDATPGRLN 168
Cdd:cd13914     7 AYQWGWEFSYPEANVTTS---------------------EQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDAFPGQYN 65

                          90       100
                  ....*....|....*....|
gi 2509724777 169 QINFLINRPGLFFGQCSEIC 188
Cdd:cd13914    66 TIKTEATEEGEYQLYCAEYC 85
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 128-183 5.22e-06

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: 43.31  E-value: 5.22e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2509724777 128 NRIILPMNNQIRILVTATDVLHSWTVPSLGVKVDATPGRLNQINFLINRPGLFFGQ 183
Cdd:cd04212    25 NELVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGTYQGL 80
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 128-188 2.40e-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: 41.40  E-value: 2.40e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2509724777 128 NRIILPMNNQIRILVTATDVLHSWTVPSLGVKVDATPGRLNQINFLINRPGLFFGQCSEIC 188
Cdd:cd13913    25 NEIEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYC 85
 
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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