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Conserved domains on  [gi|1810945087|gb|QIC19436|]
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cytochrome c oxidase subunit II (mitochondrion) [Koreoleptoxis nodifila]

Protein Classification

cytochrome c oxidase subunit II( domain architecture ID 11475917)

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 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-227 2.10e-149

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 414.72  E-value: 2.10e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810945087   1 MSFWGQLGFQDAASPLMEELIFFHDHAMMILVMIISLVGYAALSLMLNKLTCRSLVEGQEIETIWTILPAVILIFLALPS 80
Cdd:MTH00140    1 MSYWGQLGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810945087  81 LRLLYLLDEVGDCSLTLKSIGHQWYWSYEYSDFLNIEFDSYMIPTNELNDGDFRLLEVDHRVVIPTETDIRVLVTSADVI 160
Cdd:MTH00140   81 LRLLYLLDETNNPLLTVKAIGHQWYWSYEYSDFSVIEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1810945087 161 HSWAVPSLGVKADAVPGRLNQLSFFVKHPGIFYGQCSEICGANHSFMPIVLEAIPLKNFMNWIVHVS 227
Cdd:MTH00140  161 HSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWLELMS 227
 
Name Accession Description Interval E-value
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-227 2.10e-149

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 414.72  E-value: 2.10e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810945087   1 MSFWGQLGFQDAASPLMEELIFFHDHAMMILVMIISLVGYAALSLMLNKLTCRSLVEGQEIETIWTILPAVILIFLALPS 80
Cdd:MTH00140    1 MSYWGQLGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810945087  81 LRLLYLLDEVGDCSLTLKSIGHQWYWSYEYSDFLNIEFDSYMIPTNELNDGDFRLLEVDHRVVIPTETDIRVLVTSADVI 160
Cdd:MTH00140   81 LRLLYLLDETNNPLLTVKAIGHQWYWSYEYSDFSVIEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1810945087 161 HSWAVPSLGVKADAVPGRLNQLSFFVKHPGIFYGQCSEICGANHSFMPIVLEAIPLKNFMNWIVHVS 227
Cdd:MTH00140  161 HSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWLELMS 227
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 94-222 7.21e-96

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: 275.60  E-value: 7.21e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810945087  94 SLTLKSIGHQWYWSYEYSDFLNIEFDSYMIPTNELNDGDFRLLEVDHRVVIPTETDIRVLVTSADVIHSWAVPSLGVKAD 173
Cdd:cd13912     2 SLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKVD 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1810945087 174 AVPGRLNQLSFFVKHPGIFYGQCSEICGANHSFMPIVLEAIPLKNFMNW 222
Cdd:cd13912    82 AVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-214 1.04e-82

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 241.93  E-value: 1.04e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810945087  95 LTLKSIGHQWYWSYEYSDFLNIEFDSYMIPTNELNDGDFRLLEVDHRVVIPTETDIRVLVTSADVIHSWAVPSLGVKADA 174
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1810945087 175 VPGRLNQLSFFVKHPGIFYGQCSEICGANHSFMPIVLEAI 214
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
1-223 9.56e-48

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 156.91  E-value: 9.56e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810945087   1 MSFWGQLGFQDAASPLMEELIFFHDhAMMILVMIISLVGYAALSLML-------NKLTCRSLVEGQEIETIWTILPAVIL 73
Cdd:COG1622    13 LLLSGQLSLPDPAGPIAEEIDDLFW-VSLIIMLVIFVLVFGLLLYFAiryrrrkGDADPAQFHHNTKLEIVWTVIPIIIV 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810945087  74 IFLALPSLRLLYLLDEVGDCSLTLKSIGHQWYWSYEYsdflniefdsymiptneLNDGDfrllEVDHRVVIPTETDIRVL 153
Cdd:COG1622    92 IVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRY-----------------PDQGI----ATVNELVLPVGRPVRFL 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810945087 154 VTSADVIHSWAVPSLGVKADAVPGRLNQLSFFVKHPGIFYGQCSEICGANHSFMPIVLEAIPLKNFMNWI 223
Cdd:COG1622   151 LTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWL 220
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 12-223 8.12e-40

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: 135.59  E-value: 8.12e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810945087  12 AASPLMEElIFFHDHAMMILVMIISLVGYAALSLMLNKLTCRSLVE-------GQEIETIWTILPAVILIFLALPSLRLL 84
Cdd:TIGR02866   1 PGGEIAQQ-IAFLFLFVLAVSTLISLLVAALLAYVVWKFRRKGDEEkpsqihgNRRLEYVWTVIPLIIVVGLFAATAKGL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810945087  85 YLLDEVGDC-SLTLKSIGHQWYWSYEYSDFLniefdsymiptnelndgdfrlLEVDHRVVIPTETDIRVLVTSADVIHSW 163
Cdd:TIGR02866  80 LYLERPIPKdALKVKVTGYQWWWDFEYPESG---------------------FTTVNELVLPAGTPVELQVTSKDVIHSF 138

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810945087 164 AVPSLGVKADAVPGRLNQLSFFVKHPGIFYGQCSEICGANHSFMPIVLEAIPLKNFMNWI 223
Cdd:TIGR02866 139 WVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYV 198
 
Name Accession Description Interval E-value
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-227 2.10e-149

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 414.72  E-value: 2.10e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810945087   1 MSFWGQLGFQDAASPLMEELIFFHDHAMMILVMIISLVGYAALSLMLNKLTCRSLVEGQEIETIWTILPAVILIFLALPS 80
Cdd:MTH00140    1 MSYWGQLGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810945087  81 LRLLYLLDEVGDCSLTLKSIGHQWYWSYEYSDFLNIEFDSYMIPTNELNDGDFRLLEVDHRVVIPTETDIRVLVTSADVI 160
Cdd:MTH00140   81 LRLLYLLDETNNPLLTVKAIGHQWYWSYEYSDFSVIEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1810945087 161 HSWAVPSLGVKADAVPGRLNQLSFFVKHPGIFYGQCSEICGANHSFMPIVLEAIPLKNFMNWIVHVS 227
Cdd:MTH00140  161 HSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWLELMS 227
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-223 6.71e-147

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 408.45  E-value: 6.71e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810945087   1 MSFWGQLGFQDAASPLMEELIFFHDHAMMILVMIISLVGYAALSLMLNKLTCRSLVEGQEIETIWTILPAVILIFLALPS 80
Cdd:MTH00154    1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810945087  81 LRLLYLLDEVGDCSLTLKSIGHQWYWSYEYSDFLNIEFDSYMIPTNELNDGDFRLLEVDHRVVIPTETDIRVLVTSADVI 160
Cdd:MTH00154   81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1810945087 161 HSWAVPSLGVKADAVPGRLNQLSFFVKHPGIFYGQCSEICGANHSFMPIVLEAIPLKNFMNWI 223
Cdd:MTH00154  161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWI 223
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-223 1.89e-136

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 381.76  E-value: 1.89e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810945087   1 MSFWGQLGFQDAASPLMEELIFFHDHAMMILVMIISLVGYAALSLMLNKLTCRSLVEGQEIETIWTILPAVILIFLALPS 80
Cdd:MTH00139    1 MAYWGQLGFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810945087  81 LRLLYLLDEVGDCSLTLKSIGHQWYWSYEYSDFLNIEFDSYMIPTNELNDGDFRLLEVDHRVVIPTETDIRVLVTSADVI 160
Cdd:MTH00139   81 LRLLYLMDEVSDPYLTFKAVGHQWYWSYEYSDFKNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1810945087 161 HSWAVPSLGVKADAVPGRLNQLSFFVKHPGIFYGQCSEICGANHSFMPIVLEAIPLKNFMNWI 223
Cdd:MTH00139  161 HSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEWI 223
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-223 2.41e-135

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 379.26  E-value: 2.41e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810945087   1 MSFWGQLGFQDAASPLMEELIFFHDHAMMILVMIISLVGYAALSLMLNKLTCRSLVEGQEIETIWTILPAVILIFLALPS 80
Cdd:MTH00117    1 MANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810945087  81 LRLLYLLDEVGDCSLTLKSIGHQWYWSYEYSDFLNIEFDSYMIPTNELNDGDFRLLEVDHRVVIPTETDIRVLVTSADVI 160
Cdd:MTH00117   81 LRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1810945087 161 HSWAVPSLGVKADAVPGRLNQLSFFVKHPGIFYGQCSEICGANHSFMPIVLEAIPLKNFMNWI 223
Cdd:MTH00117  161 HSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWS 223
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-223 9.72e-129

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 362.64  E-value: 9.72e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810945087   1 MSFWGQLGFQDAASPLMEELIFFHDHAMMILVMIISLVGYAALSLMLNKLTCRSLVEGQEIETIWTILPAVILIFLALPS 80
Cdd:MTH00008    1 MPHWGQLMFQDAASPVMLQLISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810945087  81 LRLLYLLDEVGDCSLTLKSIGHQWYWSYEYSDFLNIEFDSYMIPTNELNDGDFRLLEVDHRVVIPTETDIRVLVTSADVI 160
Cdd:MTH00008   81 LRLLYLMDEVSNPSITLKTIGHQWYWSYEYSDFSNLEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1810945087 161 HSWAVPSLGVKADAVPGRLNQLSFFVKHPGIFYGQCSEICGANHSFMPIVLEAIPLKNFMNWI 223
Cdd:MTH00008  161 HSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKWV 223
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-223 1.50e-124

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 352.08  E-value: 1.50e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810945087   1 MSFWGQLGFQDAASPLMEELIFFHDHAMMILVMIISLVGYAALSLMLNKLTCRSLVEGQEIETIWTILPAVILIFLALPS 80
Cdd:MTH00038    1 MATWLQLGLQDASSPLMEELIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810945087  81 LRLLYLLDEVGDCSLTLKSIGHQWYWSYEYSDFLNIEFDSYMIPTNELNDGDFRLLEVDHRVVIPTETDIRVLVTSADVI 160
Cdd:MTH00038   81 LQLLYLMDEVNNPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1810945087 161 HSWAVPSLGVKADAVPGRLNQLSFFVKHPGIFYGQCSEICGANHSFMPIVLEAIPLKNFMNWI 223
Cdd:MTH00038  161 HSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWV 223
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-223 3.37e-124

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 350.82  E-value: 3.37e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810945087   1 MSFWGQLGFQDAASPLMEELIFFHDHAMMILVMIISLVGYAALSLMLNKLTCRSLVEGQEIETIWTILPAVILIFLALPS 80
Cdd:MTH00168    1 MATYSQLGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810945087  81 LRLLYLLDEVGDCSLTLKSIGHQWYWSYEYSDFLNIEFDSYMIPTNELNDGDFRLLEVDHRVVIPTETDIRVLVTSADVI 160
Cdd:MTH00168   81 LRLLYLMDEIDKPDLTIKAVGHQWYWSYEYTDYNDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1810945087 161 HSWAVPSLGVKADAVPGRLNQLSFFVKHPGIFYGQCSEICGANHSFMPIVLEAIPLKNFMNWI 223
Cdd:MTH00168  161 HSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENWV 223
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-222 1.22e-121

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 344.39  E-value: 1.22e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810945087   1 MSFWGQLGFQDAASPLMEELIFFHDHAMMILVMIISLVGYAALSLMLNKLTCRSLVEGQEIETIWTILPAVILIFLALPS 80
Cdd:MTH00098    1 MAYPFQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810945087  81 LRLLYLLDEVGDCSLTLKSIGHQWYWSYEYSDFLNIEFDSYMIPTNELNDGDFRLLEVDHRVVIPTETDIRVLVTSADVI 160
Cdd:MTH00098   81 LRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1810945087 161 HSWAVPSLGVKADAVPGRLNQLSFFVKHPGIFYGQCSEICGANHSFMPIVLEAIPLKNFMNW 222
Cdd:MTH00098  161 HSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKW 222
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 1-223 3.75e-117

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 333.28  E-value: 3.75e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810945087   1 MSFWGQLGFQDAASPLMEELIFFHDHAMMILVMIISLVGYAALSLMLNKLTCRSLVEGQEIETIWTILPAVILIFLALPS 80
Cdd:MTH00076    1 MAHPSQLGFQDAASPIMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810945087  81 LRLLYLLDEVGDCSLTLKSIGHQWYWSYEYSDFLNIEFDSYMIPTNELNDGDFRLLEVDHRVVIPTETDIRVLVTSADVI 160
Cdd:MTH00076   81 LRILYLMDEINDPHLTVKAIGHQWYWSYEYTDYEDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1810945087 161 HSWAVPSLGVKADAVPGRLNQLSFFVKHPGIFYGQCSEICGANHSFMPIVLEAIPLKNFMNWI 223
Cdd:MTH00076  161 HSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLNWS 223
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 1-222 9.57e-117

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 332.45  E-value: 9.57e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810945087   1 MSFWGQLGFQDAASPLMEELIFFHDHAMMILVMIISLVGYAALSLMLNKLTCRSLVEGQEIETIWTILPAVILIFLALPS 80
Cdd:MTH00129    1 MAHPSQLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810945087  81 LRLLYLLDEVGDCSLTLKSIGHQWYWSYEYSDFLNIEFDSYMIPTNELNDGDFRLLEVDHRVVIPTETDIRVLVTSADVI 160
Cdd:MTH00129   81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1810945087 161 HSWAVPSLGVKADAVPGRLNQLSFFVKHPGIFYGQCSEICGANHSFMPIVLEAIPLKNFMNW 222
Cdd:MTH00129  161 HSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFENW 222
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 1-222 7.68e-112

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 319.91  E-value: 7.68e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810945087   1 MSFWGQLGFQDAASPLMEELIFFHDHAMMILVMIISLVGYAALSLMLNKLTCRSLVEGQEIETIWTILPAVILIFLALPS 80
Cdd:MTH00185    1 MAHPSQLGLQDAASPVMEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810945087  81 LRLLYLLDEVGDCSLTLKSIGHQWYWSYEYSDFLNIEFDSYMIPTNELNDGDFRLLEVDHRVVIPTETDIRVLVTSADVI 160
Cdd:MTH00185   81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1810945087 161 HSWAVPSLGVKADAVPGRLNQLSFFVKHPGIFYGQCSEICGANHSFMPIVLEAIPLKNFMNW 222
Cdd:MTH00185  161 HSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENW 222
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 6-228 1.14e-111

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 319.77  E-value: 1.14e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810945087   6 QLGFQDAASPLMEELIFFHDHAMMILVMIISLVGYAALSLMLNKLTCRSLVEGQEIETIWTILPAVILIFLALPSLRLLY 85
Cdd:MTH00023   15 QLGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKLLY 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810945087  86 LLDEVGDCSLTLKSIGHQWYWSYEYSDFL--NIEFDSYMIPTNELNDGDFRLLEVDHRVVIPTETDIRVLVTSADVIHSW 163
Cdd:MTH00023   95 LMDEVVSPALTIKAIGHQWYWSYEYSDYEgeTLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSF 174

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1810945087 164 AVPSLGVKADAVPGRLNQLSFFVKHPGIFYGQCSEICGANHSFMPIVLEAIPLKNFMNWIVHVSA 228
Cdd:MTH00023  175 AVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWLLSLSN 239
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 6-223 4.24e-107

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 307.86  E-value: 4.24e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810945087   6 QLGFQDAASPLMEELIFFHDHAMMILVMIISLVGYAALSLMLNKLTCRSLVEGQEIETIWTILPAVILIFLALPSLRLLY 85
Cdd:MTH00051    8 QLGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSLKLLY 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810945087  86 LLDEVGDCSLTLKSIGHQWYWSYEYSDF--LNIEFDSYMIPTNELNDGDFRLLEVDHRVVIPTETDIRVLVTSADVIHSW 163
Cdd:MTH00051   88 LMDEVIDPALTIKAIGHQWYWSYEYSDYgtDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSF 167

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810945087 164 AVPSLGVKADAVPGRLNQLSFFVKHPGIFYGQCSEICGANHSFMPIVLEAIPLKNFMNWI 223
Cdd:MTH00051  168 AVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINWV 227
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 94-222 7.21e-96

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: 275.60  E-value: 7.21e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810945087  94 SLTLKSIGHQWYWSYEYSDFLNIEFDSYMIPTNELNDGDFRLLEVDHRVVIPTETDIRVLVTSADVIHSWAVPSLGVKAD 173
Cdd:cd13912     2 SLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKVD 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1810945087 174 AVPGRLNQLSFFVKHPGIFYGQCSEICGANHSFMPIVLEAIPLKNFMNW 222
Cdd:cd13912    82 AVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-214 1.04e-82

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 241.93  E-value: 1.04e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810945087  95 LTLKSIGHQWYWSYEYSDFLNIEFDSYMIPTNELNDGDFRLLEVDHRVVIPTETDIRVLVTSADVIHSWAVPSLGVKADA 174
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1810945087 175 VPGRLNQLSFFVKHPGIFYGQCSEICGANHSFMPIVLEAI 214
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 6-223 8.44e-82

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 244.93  E-value: 8.44e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810945087   6 QLGFQDAASPLMEELIFFHDHAMMILVMIISLVGYAALSLML---------NKLtcrslvEGQEIETIWTILPAVILIFL 76
Cdd:MTH00027   34 QLGFQDAGSPVMEEIIMLHDQILFILTIIVGVVLWLIIRILLgnnyysyywNKL------DGSLIEVIWTLIPAFILILI 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810945087  77 ALPSLRLLYLLDEVG-DCSLTLKSIGHQWYWSYEYSDF--LNIEFDSYMIPTNELNDGDFRLLEVDHRVVIPTETDIRVL 153
Cdd:MTH00027  108 AFPSLRLLYIMDECGfSANITIKVTGHQWYWSYSYEDYgeKNIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVL 187

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810945087 154 VTSADVIHSWAVPSLGVKADAVPGRLNQLSFFVKHPGIFYGQCSEICGANHSFMPIVLEAIPLKNFMNWI 223
Cdd:MTH00027  188 ITAADVLHSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYIDWI 257
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 23-224 2.29e-70

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 214.87  E-value: 2.29e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810945087  23 FHDHAMMILVMIISLVGYAALSLMLNKLTCRSLVEGQEIETIWTILPAVILIFLALPSLRLLYLLDEVG-DCSLTLKSIG 101
Cdd:MTH00080   25 FNCSLLFGEFVLAFVVFLFLYLISNNFYFKSKKIEYQFGELLCSVFPVLILLMQMVPSLSLLYYYGLMNlDSNLTVKVTG 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810945087 102 HQWYWSYEYSDFLNIEFDSYMIPTNELNDGDFRLLEVDHRVVIPTETDIRVLVTSADVIHSWAVPSLGVKADAVPGRLNQ 181
Cdd:MTH00080  105 HQWYWSYEFSDIPGLEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDAMSGILST 184

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1810945087 182 LSFFVKHPGIFYGQCSEICGANHSFMPIVLEAIPLKNFMNWIV 224
Cdd:MTH00080  185 LCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKEWCK 227
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
1-223 9.56e-48

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 156.91  E-value: 9.56e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810945087   1 MSFWGQLGFQDAASPLMEELIFFHDhAMMILVMIISLVGYAALSLML-------NKLTCRSLVEGQEIETIWTILPAVIL 73
Cdd:COG1622    13 LLLSGQLSLPDPAGPIAEEIDDLFW-VSLIIMLVIFVLVFGLLLYFAiryrrrkGDADPAQFHHNTKLEIVWTVIPIIIV 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810945087  74 IFLALPSLRLLYLLDEVGDCSLTLKSIGHQWYWSYEYsdflniefdsymiptneLNDGDfrllEVDHRVVIPTETDIRVL 153
Cdd:COG1622    92 IVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRY-----------------PDQGI----ATVNELVLPVGRPVRFL 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810945087 154 VTSADVIHSWAVPSLGVKADAVPGRLNQLSFFVKHPGIFYGQCSEICGANHSFMPIVLEAIPLKNFMNWI 223
Cdd:COG1622   151 LTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWL 220
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 57-214 1.44e-44

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 147.79  E-value: 1.44e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810945087  57 EGQEIETIWTILPAVILIFLALPSLRLLYLlDEVGDCSLTLKSIGHQWYWSYEYSDflNIEFDSYMiptNELNDGdfrll 136
Cdd:MTH00047   45 ENQVLELLWTVVPTLLVLVLCFLNLNFITS-DLDCFSSETIKVIGHQWYWSYEYSF--GGSYDSFM---TDDIFG----- 113

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1810945087 137 eVDHRVVIPTETDIRVLVTSADVIHSWAVPSLGVKADAVPGRLNQLSFFVKHPGIFYGQCSEICGANHSFMPIVLEAI 214
Cdd:MTH00047  114 -VDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCPDRHGVFVGYCSELCGVGHSYMPIVIEVV 190
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 118-214 6.61e-44

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 144.96  E-value: 6.61e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810945087 118 FDSYMIPTNELNDGDFRLLEVDHRVVIPTETDIRVLVTSADVIHSWAVPSLGVKADAVPGRLNQLSFFVKHPGIFYGQCS 197
Cdd:PTZ00047   51 FQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCS 130

                          90
                  ....*....|....*..
gi 1810945087 198 EICGANHSFMPIVLEAI 214
Cdd:PTZ00047  131 EMCGTLHGFMPIVVEAV 147
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 12-223 8.12e-40

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: 135.59  E-value: 8.12e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810945087  12 AASPLMEElIFFHDHAMMILVMIISLVGYAALSLMLNKLTCRSLVE-------GQEIETIWTILPAVILIFLALPSLRLL 84
Cdd:TIGR02866   1 PGGEIAQQ-IAFLFLFVLAVSTLISLLVAALLAYVVWKFRRKGDEEkpsqihgNRRLEYVWTVIPLIIVVGLFAATAKGL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810945087  85 YLLDEVGDC-SLTLKSIGHQWYWSYEYSDFLniefdsymiptnelndgdfrlLEVDHRVVIPTETDIRVLVTSADVIHSW 163
Cdd:TIGR02866  80 LYLERPIPKdALKVKVTGYQWWWDFEYPESG---------------------FTTVNELVLPAGTPVELQVTSKDVIHSF 138

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810945087 164 AVPSLGVKADAVPGRLNQLSFFVKHPGIFYGQCSEICGANHSFMPIVLEAIPLKNFMNWI 223
Cdd:TIGR02866 139 WVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYV 198
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 95-212 6.60e-29

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


Pssm-ID: 259911 [Multi-domain]  Cd Length: 95  Bit Score: 104.30  E-value: 6.60e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810945087  95 LTLKSIGHQWYWSYEYSDflniefdsymiptnelndgdfrlLEVDHRVVIPTETDIRVLVTSADVIHSWAVPSLGVKADA 174
Cdd:cd13842     1 LTVYVTGVQWSWTFIYPN-----------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDA 57

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1810945087 175 VPGRLNQLSFFVKHPGIFYGQCSEICGANHSFMPIVLE 212
Cdd:cd13842    58 VPGYTSELWFVADKPGTYTIICAEYCGLGHSYMLGKVE 95
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 94-207 1.27e-27

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: 101.16  E-value: 1.27e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810945087  94 SLTLKSIGHQWYWSYEYSDFLNIEFDSymipTNELndgdfrllevdhrvVIPTETDIRVLVTSADVIHSWAVPSLGVKAD 173
Cdd:cd04213     1 ALTIEVTGHQWWWEFRYPDEPGRGIVT----ANEL--------------HIPVGRPVRLRLTSADVIHSFWVPSLAGKMD 62

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1810945087 174 AVPGRLNQLSFFVKHPGIFYGQCSEICGANHSFM 207
Cdd:cd04213    63 MIPGRTNRLWLQADEPGVYRGQCAEFCGASHALM 96
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-77 3.09e-26

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: 97.02  E-value: 3.09e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810945087   1 MSFWGQLGFQDAASPLMEELIFFHDHAMMILVMIISLVGYAALSLML------NKLTCRSLVEGQEIETIWTILPAVILI 74
Cdd:pfam02790   1 MPTPWGLGFQDAASPLMEGLLELHDYIMFILTLILILVLYILVTCLIrfnrrkNPITARYTTHGQTIEIIWTIIPAVILI 80


                  ...
gi 1810945087  75 FLA 77
Cdd:pfam02790  81 LIA 83
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 94-207 8.27e-21

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: 83.45  E-value: 8.27e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810945087  94 SLTLKSIGHQWYWSYEYSDFLNIefdsymipTNELndgdfrllevdhrvVIPTETDIRVLVTSADVIHSWAVPSLGVKAD 173
Cdd:cd13915     1 ALEIQVTGRQWMWEFTYPNGKRE--------INEL--------------HVPVGKPVRLILTSKDVIHSFYVPAFRIKQD 58

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1810945087 174 AVPGRLNQLSFFVKHPGIFYGQCSEICGANHSFM 207
Cdd:cd13915    59 VVPGRYTYLWFEATKPGEYDLFCTEYCGTGHSGM 92
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-207 1.37e-20

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


Pssm-ID: 259986 [Multi-domain]  Cd Length: 107  Bit Score: 83.07  E-value: 1.37e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810945087  95 LTLKSIGHQWYWSYEYSDFLNIEFDSYMIPTNELNdgdfrlLEVDHRVviptetdiRVLVTSADVIHSWAVPSLGVKADA 174
Cdd:cd13919     2 LVVEVTAQQWAWTFRYPGGDGKLGTDDDVTSPELH------LPVGRPV--------LFNLRSKDVIHSFWVPEFRVKQDA 67

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1810945087 175 VPGRLNQLSFFVKHPGIFYGQCSEICGANHSFM 207
Cdd:cd13919    68 VPGRTTRLWFTPTREGEYEVRCAELCGLGHYRM 100
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 88-222 2.12e-20

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


Pssm-ID: 259985 [Multi-domain]  Cd Length: 139  Bit Score: 83.66  E-value: 2.12e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810945087  88 DEVGDCSLTLKSIGHQWYWSYEYSdflniefdsymiptNELNDGDFrllevdhrVVIPTETDIRVLVTSADVIHSWAVPS 167
Cdd:cd13918    26 DEADEDALEVEVEGFQFGWQFEYP--------------NGVTTGNT--------LRVPADTPIALRVTSTDVFHTFGIPE 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1810945087 168 LGVKADAVPGRLNQLSFFVKHPGIFYGQCSEICGANHSFMPIVLEAIPLKNFMNW 222
Cdd:cd13918    84 LRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEFEAW 138
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 101-223 1.03e-19

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: 80.92  E-value: 1.03e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810945087 101 GHQWYWSYEYSDFLNIEFDsymiptnelndgdfrllevdhRVVIPTETDIRVLVTSADVIHSWAVPSLGVKADAVPGRLN 180
Cdd:cd13914     7 AYQWGWEFSYPEANVTTSE---------------------QLVIPADRPVYFRITSRDVIHAFHVPELGLKQDAFPGQYN 65

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1810945087 181 QLSFFVKHPGIFYGQCSEICGANHSFMPIVLEAIPLKNFMNWI 223
Cdd:cd13914    66 TIKTEATEEGEYQLYCAEYCGAGHSQMLSTVTVVSQDEYQQWL 108
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 142-207 5.07e-10

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: 54.88  E-value: 5.07e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1810945087 142 VVIPTETDIRVLVTSADVIHSWAVPSLGVKADAVPGRLNQLSFFVKHPGIFYGQCSEICGANHSFM 207
Cdd:cd13913    27 IEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNM 92
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 142-207 2.05e-05

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: 42.15  E-value: 2.05e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1810945087 142 VVIPTETDIRVLVTSADVIHSWAVPSLGVKADAVPGRLNQLSFFVKHPGIFYGQCSEICGANHSFM 207
Cdd:cd04212    27 LVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGTYQGLSANYSGEGFSDM 92
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 101-207 5.33e-05

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


Pssm-ID: 259983 [Multi-domain]  Cd Length: 93  Bit Score: 40.83  E-value: 5.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1810945087 101 GHQWYWsyeysdflniEFDSYMIPTNELndGDFRllevdhrvviptetdirvlVTSADVIHSWAVPS----LGVKADAVP 176
Cdd:cd13916     7 GHQWYW----------ELSRTEIPAGKP--VEFR-------------------VTSADVNHGFGIYDpdmrLLAQTQAMP 55

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1810945087 177 GRLNQLSFFVKHPGIFYGQCSEICGANHSFM 207
Cdd:cd13916    56 GYTNVLRYTFDKPGTYTILCLEYCGLAHHVM 86
N2OR_C cd04223
The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase ...
 158-207 2.93e-04

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


Pssm-ID: 259885 [Multi-domain]  Cd Length: 95  Bit Score: 38.76  E-value: 2.93e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1810945087 158 DVIHSWAVPSLGVKADAVPGRLNQLSFFVKHPGIFYGQCSEICGANHSFM 207
Cdd:cd04223    38 DITHGFAIPGYNVNLSLEPGETATVTFVADKPGVYPYYCTEFCSALHLEM 87
 
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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