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Conserved domains on  [gi|10441718|gb|AAG17161|]
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cytochrome c oxidase subunit II, partial (mitochondrion) [Polyrhachis arachne]

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
 1-179 4.46e-95

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 275.17  E-value: 4.46e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10441718    1 MNTWL-ISLQNANSPSSEMMIFFHDFAMLILMLITSIILFIMILMPFNKFTDRFLLQSHYMEMIWTISPMIILIFIAIPS 79
Cdd:MTH00154   1 MATWSnLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10441718   80 LKILYTIEESHFNKLTIKCIGHQWYWSYEYSDFMNIEFNSYMIPSNELQLNEFRLLDTDNRCILPFNFPIRILTTSIDVI 159
Cdd:MTH00154  81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                        170       180
                 ....*....|....*....|
gi 10441718  160 HSWTVPSLGIKMDSTPGRLN 179
Cdd:MTH00154 161 HSWTVPSLGVKVDAVPGRLN 180
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-179 4.46e-95

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 275.17  E-value: 4.46e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10441718    1 MNTWL-ISLQNANSPSSEMMIFFHDFAMLILMLITSIILFIMILMPFNKFTDRFLLQSHYMEMIWTISPMIILIFIAIPS 79
Cdd:MTH00154   1 MATWSnLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10441718   80 LKILYTIEESHFNKLTIKCIGHQWYWSYEYSDFMNIEFNSYMIPSNELQLNEFRLLDTDNRCILPFNFPIRILTTSIDVI 159
Cdd:MTH00154  81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                        170       180
                 ....*....|....*....|
gi 10441718  160 HSWTVPSLGIKMDSTPGRLN 179
Cdd:MTH00154 161 HSWTVPSLGVKVDAVPGRLN 180
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 94-179 4.85e-54

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: 167.75  E-value: 4.85e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10441718  94 LTIKCIGHQWYWSYEYSDFMNIEFNSYMIPSNELQLNEFRLLDTDNRCILPFNFPIRILTTSIDVIHSWTVPSLGIKMDS 173
Cdd:cd13912   3 LTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKVDA 82


                ....*.
gi 10441718 174 TPGRLN 179
Cdd:cd13912  83 VPGRLN 88
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
94-179 1.95e-48

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 153.33  E-value: 1.95e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10441718    94 LTIKCIGHQWYWSYEYSDFMNIEFNSYMIPSNELQLNEFRLLDTDNRCILPFNFPIRILTTSIDVIHSWTVPSLGIKMDS 173
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80


                  ....*.
gi 10441718   174 TPGRLN 179
Cdd:pfam00116  81 VPGRLN 86
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
3-179 2.07e-31

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 113.00  E-value: 2.07e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10441718   3 TWLISLQNANSPSSEMMIFFHDFaMLILMLItsIILFIMILMPFN------KFTDRFLLQSHY---MEMIWTISPMIILI 73
Cdd:COG1622  16 SGQLSLPDPAGPIAEEIDDLFWV-SLIIMLV--IFVLVFGLLLYFairyrrRKGDADPAQFHHntkLEIVWTVIPIIIVI 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10441718  74 FIAIPSLKILYTIEESHFNKLTIKCIGHQWYWSYEYSDfmniefnsymipSNELQLNEFRlldtdnrciLPFNFPIRILT 153
Cdd:COG1622  93 VLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPD------------QGIATVNELV---------LPVGRPVRFLL 151

                       170       180
                ....*....|....*....|....*.
gi 10441718 154 TSIDVIHSWTVPSLGIKMDSTPGRLN 179
Cdd:COG1622 152 TSADVIHSFWVPALGGKQDAIPGRVT 177
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 25-179 2.58e-25

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: 96.68  E-value: 2.58e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10441718    25 FAMLILMLITSIILFIMILMPFNKFTDRFLLQSHY---MEMIWTISPMIILIFIAIPSLKILYTIEES-HFNKLTIKCIG 100
Cdd:TIGR02866  18 AVSTLISLLVAALLAYVVWKFRRKGDEEKPSQIHGnrrLEYVWTVIPLIIVVGLFAATAKGLLYLERPiPKDALKVKVTG 97

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 10441718   101 HQWYWSYEYSDFmniefnsymipsnelqlnefrLLDTDNRCILPFNFPIRILTTSIDVIHSWTVPSLGIKMDSTPGRLN 179
Cdd:TIGR02866  98 YQWWWDFEYPES---------------------GFTTVNELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQTN 155
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-179 4.46e-95

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 275.17  E-value: 4.46e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10441718    1 MNTWL-ISLQNANSPSSEMMIFFHDFAMLILMLITSIILFIMILMPFNKFTDRFLLQSHYMEMIWTISPMIILIFIAIPS 79
Cdd:MTH00154   1 MATWSnLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10441718   80 LKILYTIEESHFNKLTIKCIGHQWYWSYEYSDFMNIEFNSYMIPSNELQLNEFRLLDTDNRCILPFNFPIRILTTSIDVI 159
Cdd:MTH00154  81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                        170       180
                 ....*....|....*....|
gi 10441718  160 HSWTVPSLGIKMDSTPGRLN 179
Cdd:MTH00154 161 HSWTVPSLGVKVDAVPGRLN 180
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-179 1.45e-83

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 246.00  E-value: 1.45e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10441718    1 MNTW-LISLQNANSPSSEMMIFFHDFAMLILMLITSIILFIMILMPFNKFTDRFLLQSHYMEMIWTISPMIILIFIAIPS 79
Cdd:MTH00140   1 MSYWgQLGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10441718   80 LKILYTIEESHFNKLTIKCIGHQWYWSYEYSDFMNIEFNSYMIPSNELQLNEFRLLDTDNRCILPFNFPIRILTTSIDVI 159
Cdd:MTH00140  81 LRLLYLLDETNNPLLTVKAIGHQWYWSYEYSDFSVIEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVI 160

                        170       180
                 ....*....|....*....|
gi 10441718  160 HSWTVPSLGIKMDSTPGRLN 179
Cdd:MTH00140 161 HSWTVPSLGVKVDAIPGRLN 180
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-179 4.76e-80

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 237.19  E-value: 4.76e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10441718    1 MNTWL-ISLQNANSPSSEMMIFFHDFAMLILMLITSIILFIMILMPFNKFTDRFLLQSHYMEMIWTISPMIILIFIAIPS 79
Cdd:MTH00168   1 MATYSqLGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10441718   80 LKILYTIEESHFNKLTIKCIGHQWYWSYEYSDFMNIEFNSYMIPSNELQLNEFRLLDTDNRCILPFNFPIRILTTSIDVI 159
Cdd:MTH00168  81 LRLLYLMDEIDKPDLTIKAVGHQWYWSYEYTDYNDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVL 160

                        170       180
                 ....*....|....*....|
gi 10441718  160 HSWTVPSLGIKMDSTPGRLN 179
Cdd:MTH00168 161 HSWTLPSLGLKMDAVPGRLN 180
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-179 2.89e-76

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 227.66  E-value: 2.89e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10441718    1 MNTWL-ISLQNANSPSSEMMIFFHDFAMLILMLITSIILFIMILMPFNKFTDRFLLQSHYMEMIWTISPMIILIFIAIPS 79
Cdd:MTH00038   1 MATWLqLGLQDASSPLMEELIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10441718   80 LKILYTIEESHFNKLTIKCIGHQWYWSYEYSDFMNIEFNSYMIPSNELQLNEFRLLDTDNRCILPFNFPIRILTTSIDVI 159
Cdd:MTH00038  81 LQLLYLMDEVNNPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVL 160

                        170       180
                 ....*....|....*....|
gi 10441718  160 HSWTVPSLGIKMDSTPGRLN 179
Cdd:MTH00038 161 HSWAVPSLGVKMDAVPGRLN 180
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-179 3.13e-76

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 227.29  E-value: 3.13e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10441718    1 MNTW-LISLQNANSPSSEMMIFFHDFAMLILMLITSIILFIMILMPFNKFTDRFLLQSHYMEMIWTISPMIILIFIAIPS 79
Cdd:MTH00139   1 MAYWgQLGFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10441718   80 LKILYTIEESHFNKLTIKCIGHQWYWSYEYSDFMNIEFNSYMIPSNELQLNEFRLLDTDNRCILPFNFPIRILTTSIDVI 159
Cdd:MTH00139  81 LRLLYLMDEVSDPYLTFKAVGHQWYWSYEYSDFKNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVL 160

                        170       180
                 ....*....|....*....|
gi 10441718  160 HSWTVPSLGIKMDSTPGRLN 179
Cdd:MTH00139 161 HSWTVPSLGVKIDAVPGRLN 180
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 7-179 4.68e-76

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 227.10  E-value: 4.68e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10441718    7 SLQNANSPSSEMMIFFHDFAMLILMLITSIILFIMILMPFNKFTDRFLLQSHYMEMIWTISPMIILIFIAIPSLKILYTI 86
Cdd:MTH00117   8 GFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPSLRILYLM 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10441718   87 EESHFNKLTIKCIGHQWYWSYEYSDFMNIEFNSYMIPSNELQLNEFRLLDTDNRCILPFNFPIRILTTSIDVIHSWTVPS 166
Cdd:MTH00117  88 DEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVLHSWAVPS 167

                        170
                 ....*....|...
gi 10441718  167 LGIKMDSTPGRLN 179
Cdd:MTH00117 168 LGVKTDAVPGRLN 180
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 8-179 3.65e-71

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 214.58  E-value: 3.65e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10441718    8 LQNANSPSSEMMIFFHDFAMLILMLITSIILFIMILMPFNKFTDRFLLQSHYMEMIWTISPMIILIFIAIPSLKILYTIE 87
Cdd:MTH00129   9 FQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPSLRILYLMD 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10441718   88 ESHFNKLTIKCIGHQWYWSYEYSDFMNIEFNSYMIPSNELQLNEFRLLDTDNRCILPFNFPIRILTTSIDVIHSWTVPSL 167
Cdd:MTH00129  89 EINDPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVLHSWAVPAL 168

                        170
                 ....*....|..
gi 10441718  168 GIKMDSTPGRLN 179
Cdd:MTH00129 169 GVKMDAVPGRLN 180
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 6-179 2.26e-69

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 210.13  E-value: 2.26e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10441718    6 ISLQNANSPSSEMMIFFHDFAMLILMLITSIILFIMILMPFNKFTDRFLLQSHYMEMIWTISPMIILIFIAIPSLKILYT 85
Cdd:MTH00185   7 LGLQDAASPVMEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPSLRILYL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10441718   86 IEESHFNKLTIKCIGHQWYWSYEYSDFMNIEFNSYMIPSNELQLNEFRLLDTDNRCILPFNFPIRILTTSIDVIHSWTVP 165
Cdd:MTH00185  87 MDEINDPHLTIKAMGHQWYWSYEYTDYEQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVLHSWTVP 166

                        170
                 ....*....|....
gi 10441718  166 SLGIKMDSTPGRLN 179
Cdd:MTH00185 167 ALGVKMDAVPGRLN 180
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 3-179 5.44e-69

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 209.61  E-value: 5.44e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10441718    3 TWLISLQNANSPSSEMMIFFHDFAMLILMLITSIILFIMILMPFNKFTDRFLLQSHYMEMIWTISPMIILIFIAIPSLKI 82
Cdd:MTH00023  13 PWQLGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKL 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10441718   83 LYTIEESHFNKLTIKCIGHQWYWSYEYSDFM--NIEFNSYMIPSNELQLNEFRLLDTDNRCILPFNFPIRILTTSIDVIH 160
Cdd:MTH00023  93 LYLMDEVVSPALTIKAIGHQWYWSYEYSDYEgeTLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLH 172

                        170
                 ....*....|....*....
gi 10441718  161 SWTVPSLGIKMDSTPGRLN 179
Cdd:MTH00023 173 SFAVPSLGLKIDAVPGRLN 191
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 6-179 2.24e-68

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 207.65  E-value: 2.24e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10441718    6 ISLQNANSPSSEMMIFFHDFAMLILMLITSIILFIMILMPFNKFTDRFLLQSHYMEMIWTISPMIILIFIAIPSLKILYT 85
Cdd:MTH00098   7 LGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPSLRILYM 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10441718   86 IEESHFNKLTIKCIGHQWYWSYEYSDFMNIEFNSYMIPSNELQLNEFRLLDTDNRCILPFNFPIRILTTSIDVIHSWTVP 165
Cdd:MTH00098  87 MDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVLHSWAVP 166

                        170
                 ....*....|....
gi 10441718  166 SLGIKMDSTPGRLN 179
Cdd:MTH00098 167 SLGLKTDAIPGRLN 180
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 6-179 2.79e-68

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 207.40  E-value: 2.79e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10441718    6 ISLQNANSPSSEMMIFFHDFAMLILMLITSIILFIMILMPFNKFTDRFLLQSHYMEMIWTISPMIILIFIAIPSLKILYT 85
Cdd:MTH00008   7 LMFQDAASPVMLQLISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPSLRLLYL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10441718   86 IEESHFNKLTIKCIGHQWYWSYEYSDFMNIEFNSYMIPSNELQLNEFRLLDTDNRCILPFNFPIRILTTSIDVIHSWTVP 165
Cdd:MTH00008  87 MDEVSNPSITLKTIGHQWYWSYEYSDFSNLEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVIHSWTVP 166

                        170
                 ....*....|....
gi 10441718  166 SLGIKMDSTPGRLN 179
Cdd:MTH00008 167 SLGVKVDAVPGRLN 180
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 4-179 1.52e-63

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 195.38  E-value: 1.52e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10441718    4 WLISLQNANSPSSEMMIFFHDFAMLILMLITSIILFIMILMPFNKFTDRFLLQSHYMEMIWTISPMIILIFIAIPSLKIL 83
Cdd:MTH00051   7 WQLGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSLKLL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10441718   84 YTIEESHFNKLTIKCIGHQWYWSYEYSDF--MNIEFNSYMIPSNELQLNEFRLLDTDNRCILPFNFPIRILTTSIDVIHS 161
Cdd:MTH00051  87 YLMDEVIDPALTIKAIGHQWYWSYEYSDYgtDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHS 166

                        170
                 ....*....|....*...
gi 10441718  162 WTVPSLGIKMDSTPGRLN 179
Cdd:MTH00051 167 FAVPSLSVKIDAVPGRLN 184
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 8-179 6.08e-63

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 193.84  E-value: 6.08e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10441718    8 LQNANSPSSEMMIFFHDFAMLILMLITSIILFIMILMPFNKFTDRFLLQSHYMEMIWTISPMIILIFIAIPSLKILYTIE 87
Cdd:MTH00076   9 FQDAASPIMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPSLRILYLMD 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10441718   88 ESHFNKLTIKCIGHQWYWSYEYSDFMNIEFNSYMIPSNELQLNEFRLLDTDNRCILPFNFPIRILTTSIDVIHSWTVPSL 167
Cdd:MTH00076  89 EINDPHLTVKAIGHQWYWSYEYTDYEDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVLHSWAVPSL 168

                        170
                 ....*....|..
gi 10441718  168 GIKMDSTPGRLN 179
Cdd:MTH00076 169 GIKTDAIPGRLN 180
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 94-179 4.85e-54

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: 167.75  E-value: 4.85e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10441718  94 LTIKCIGHQWYWSYEYSDFMNIEFNSYMIPSNELQLNEFRLLDTDNRCILPFNFPIRILTTSIDVIHSWTVPSLGIKMDS 173
Cdd:cd13912   3 LTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKVDA 82


                ....*.
gi 10441718 174 TPGRLN 179
Cdd:cd13912  83 VPGRLN 88
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 4-179 7.45e-50

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 161.35  E-value: 7.45e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10441718    4 WLISLQNANSPSSEMMIFFHDFAMLILMLITSIILFIMILMPF-NKFTDRFL--LQSHYMEMIWTISPMIILIFIAIPSL 80
Cdd:MTH00027  33 WQLGFQDAGSPVMEEIIMLHDQILFILTIIVGVVLWLIIRILLgNNYYSYYWnkLDGSLIEVIWTLIPAFILILIAFPSL 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10441718   81 KILYTIEESHFN-KLTIKCIGHQWYWSYEYSDF--MNIEFNSYMIPSNELQLNEFRLLDTDNRCILPFNFPIRILTTSID 157
Cdd:MTH00027 113 RLLYIMDECGFSaNITIKVTGHQWYWSYSYEDYgeKNIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAAD 192

                        170       180
                 ....*....|....*....|..
gi 10441718  158 VIHSWTVPSLGIKMDSTPGRLN 179
Cdd:MTH00027 193 VLHSWTVPSLAVKMDAVPGRIN 214
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 8-179 5.85e-49

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 158.25  E-value: 5.85e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10441718    8 LQNANSPSSEMMIFFHDF---AMLILMLITSIILFIMILMPFNKFTDRFLLQSHYMEMIWTISPMIILIFIAIPSLKILY 84
Cdd:MTH00080   8 LNFSNSLFSSYMDWFHNFncsLLFGEFVLAFVVFLFLYLISNNFYFKSKKIEYQFGELLCSVFPVLILLMQMVPSLSLLY 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10441718   85 TIEESHF-NKLTIKCIGHQWYWSYEYSDFMNIEFNSYMIPSNELQLNEFRLLDTDNRCILPFNFPIRILTTSIDVIHSWT 163
Cdd:MTH00080  88 YYGLMNLdSNLTVKVTGHQWYWSYEFSDIPGLEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWA 167

                        170
                 ....*....|....*.
gi 10441718  164 VPSLGIKMDSTPGRLN 179
Cdd:MTH00080 168 LPSLSIKMDAMSGILS 183
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
94-179 1.95e-48

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 153.33  E-value: 1.95e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10441718    94 LTIKCIGHQWYWSYEYSDFMNIEFNSYMIPSNELQLNEFRLLDTDNRCILPFNFPIRILTTSIDVIHSWTVPSLGIKMDS 173
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80


                  ....*.
gi 10441718   174 TPGRLN 179
Cdd:pfam00116  81 VPGRLN 86
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
3-179 2.07e-31

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 113.00  E-value: 2.07e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10441718   3 TWLISLQNANSPSSEMMIFFHDFaMLILMLItsIILFIMILMPFN------KFTDRFLLQSHY---MEMIWTISPMIILI 73
Cdd:COG1622  16 SGQLSLPDPAGPIAEEIDDLFWV-SLIIMLV--IFVLVFGLLLYFairyrrRKGDADPAQFHHntkLEIVWTVIPIIIVI 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10441718  74 FIAIPSLKILYTIEESHFNKLTIKCIGHQWYWSYEYSDfmniefnsymipSNELQLNEFRlldtdnrciLPFNFPIRILT 153
Cdd:COG1622  93 VLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPD------------QGIATVNELV---------LPVGRPVRFLL 151

                       170       180
                ....*....|....*....|....*.
gi 10441718 154 TSIDVIHSWTVPSLGIKMDSTPGRLN 179
Cdd:COG1622 152 TSADVIHSFWVPALGGKQDAIPGRVT 177
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 22-179 1.53e-26

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 99.64  E-value: 1.53e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10441718   22 FHDFAMLILMLITSIILFIMILMPFNKFTDR----FLLQSHYMEMIWTISPMIILIFIAipSLKILYTIEESHFN-KLTI 96
Cdd:MTH00047   7 YYDIVCYILALCVFIPCWVYIMLCWQVVSGNgsvnFGSENQVLELLWTVVPTLLVLVLC--FLNLNFITSDLDCFsSETI 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10441718   97 KCIGHQWYWSYEYSDfmNIEFNSYMIPSNELQLNEFRLLdtdnrcilpFNFPIRILTTSIDVIHSWTVPSLGIKMDSTPG 176
Cdd:MTH00047  85 KVIGHQWYWSYEYSF--GGSYDSFMTDDIFGVDKPLRLV---------YGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPG 153


                 ...
gi 10441718  177 RLN 179
Cdd:MTH00047 154 RIN 156
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 25-179 2.58e-25

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: 96.68  E-value: 2.58e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10441718    25 FAMLILMLITSIILFIMILMPFNKFTDRFLLQSHY---MEMIWTISPMIILIFIAIPSLKILYTIEES-HFNKLTIKCIG 100
Cdd:TIGR02866  18 AVSTLISLLVAALLAYVVWKFRRKGDEEKPSQIHGnrrLEYVWTVIPLIIVVGLFAATAKGLLYLERPiPKDALKVKVTG 97

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 10441718   101 HQWYWSYEYSDFmniefnsymipsnelqlnefrLLDTDNRCILPFNFPIRILTTSIDVIHSWTVPSLGIKMDSTPGRLN 179
Cdd:TIGR02866  98 YQWWWDFEYPES---------------------GFTTVNELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQTN 155
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 117-178 6.97e-17

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 73.70  E-value: 6.97e-17
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 10441718  117 FNSYMIPSNELQLNEFRLLDTDNRCILPFNFPIRILTTSIDVIHSWTVPSLGIKMDSTPGRL 178
Cdd:PTZ00047  51 FQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRL 112
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 94-179 3.77e-16

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: 69.96  E-value: 3.77e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10441718  94 LTIKCIGHQWYWSYEYSDFMNIEFNSymipSNELqlnefrlldtdnrcILPFNFPIRILTTSIDVIHSWTVPSLGIKMDS 173
Cdd:cd04213   2 LTIEVTGHQWWWEFRYPDEPGRGIVT----ANEL--------------HIPVGRPVRLRLTSADVIHSFWVPSLAGKMDM 63


                ....*.
gi 10441718 174 TPGRLN 179
Cdd:cd04213  64 IPGRTN 69
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 4-82 1.91e-13

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: 62.73  E-value: 1.91e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10441718     4 WLISLQNANSPSSEMMIFFHDFAMLILMLITSIILFIMILMPF------NKFTDRFLLQSHYMEMIWTISPMIILIFIAI 77
Cdd:pfam02790   5 WGLGFQDAASPLMEGLLELHDYIMFILTLILILVLYILVTCLIrfnrrkNPITARYTTHGQTIEIIWTIIPAVILILIAL 84


                  ....*
gi 10441718    78 PSLKI 82
Cdd:pfam02790  85 PSFKL 89
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 94-179 3.92e-12

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: 59.58  E-value: 3.92e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10441718  94 LTIKCIGHQWYWSYEYSDFMNIEFNSYMIPSNELQLnefrlldtdnrcilPFNFPIRILTTSIDVIHSWTVPSLGIKMDS 173
Cdd:cd13919   2 LVVEVTAQQWAWTFRYPGGDGKLGTDDDVTSPELHL--------------PVGRPVLFNLRSKDVIHSFWVPEFRVKQDA 67


                ....*.
gi 10441718 174 TPGRLN 179
Cdd:cd13919  68 VPGRTT 73
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 94-179 5.07e-12

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: 59.18  E-value: 5.07e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10441718  94 LTIKCIGHQWYWSYEYsdfmniefnsymipsnelqLNEFRlldTDNRCILPFNFPIRILTTSIDVIHSWTVPSLGIKMDS 173
Cdd:cd13915   2 LEIQVTGRQWMWEFTY-------------------PNGKR---EINELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQDV 59


                ....*.
gi 10441718 174 TPGRLN 179
Cdd:cd13915  60 VPGRYT 65
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-179 1.14e-11

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: 58.57  E-value: 1.14e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10441718  95 TIKCIGHQWYWSYEYSDfmniefnsymipSNelqlnefrlLDTDNRCILPFNFPIRILTTSIDVIHSWTVPSLGIKMDST 174
Cdd:cd13914   2 EIEVEAYQWGWEFSYPE------------AN---------VTTSEQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDAF 60


                ....*
gi 10441718 175 PGRLN 179
Cdd:cd13914  61 PGQYN 65
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 94-179 1.33e-11

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: 58.08  E-value: 1.33e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10441718  94 LTIKCIGHQWYWSYEYSDfmniefnsymipsnelqlnefrlLDTDNRCILPFNFPIRILTTSIDVIHSWTVPSLGIKMDS 173
Cdd:cd13842   1 LTVYVTGVQWSWTFIYPN-----------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDA 57


                ....*.
gi 10441718 174 TPGRLN 179
Cdd:cd13842  58 VPGYTS 63
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 66-179 1.18e-06

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: 45.91  E-value: 1.18e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10441718  66 ISPMIILIFIAIPSLKILYtIE----ESHFNKLTIKCIGHQWYWSYEYsdfmniefnsymiPSNELQLNEFRlldtdnrc 141
Cdd:cd13918   2 LSAIIVISLIVWTYGMLLY-VEdppdEADEDALEVEVEGFQFGWQFEY-------------PNGVTTGNTLR-------- 59

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 10441718 142 iLPFNFPIRILTTSIDVIHSWTVPSLGIKMDSTPGRLN 179
Cdd:cd13918  60 -VPADTPIALRVTSTDVFHTFGIPELRVKADAIPGEYT 96
 
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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