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Conserved domains on  [gi|1896069707|gb|QNJ47009|]
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cytochrome c oxidase subunit II, partial (mitochondrion) [Systella rafflesii]

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
 1-223 8.89e-132

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 369.93  E-value: 8.89e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069707   1 MATWTNWSLQDSASPLMEQLSFFHDHTMTIIIMITIIVSYSMMFTFKNKFLMKTMLQEHKLEIMWTTIPTMTLMLIAMPS 80
Cdd:MTH00154    1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069707  81 IQLLYLMDDSTTPLITIKSIGRQWYWSYEYSDFMNIEFDSYMLMNNE--KNSFRLLEVDNRTMMPMNSEIRMLTSASDVL 158
Cdd:MTH00154   81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNEleNNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1896069707 159 HSWTIPSLGIKIDATPGRLNQSTFLINRPGLFFGQCSEICGANHSFMPITLESTSIKLFIKWLMK 223
Cdd:MTH00154  161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKN 225
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-223 8.89e-132

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 369.93  E-value: 8.89e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069707   1 MATWTNWSLQDSASPLMEQLSFFHDHTMTIIIMITIIVSYSMMFTFKNKFLMKTMLQEHKLEIMWTTIPTMTLMLIAMPS 80
Cdd:MTH00154    1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069707  81 IQLLYLMDDSTTPLITIKSIGRQWYWSYEYSDFMNIEFDSYMLMNNE--KNSFRLLEVDNRTMMPMNSEIRMLTSASDVL 158
Cdd:MTH00154   81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNEleNNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1896069707 159 HSWTIPSLGIKIDATPGRLNQSTFLINRPGLFFGQCSEICGANHSFMPITLESTSIKLFIKWLMK 223
Cdd:MTH00154  161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKN 225
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 93-220 4.50e-83

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: 242.86  E-value: 4.50e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069707  93 PLITIKSIGRQWYWSYEYSDFMNIEFDSYMLMNN--EKNSFRLLEVDNRTMMPMNSEIRMLTSASDVLHSWTIPSLGIKI 170
Cdd:cd13912     1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDdlEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1896069707 171 DATPGRLNQSTFLINRPGLFFGQCSEICGANHSFMPITLESTSIKLFIKW 220
Cdd:cd13912    81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-212 4.83e-72

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 214.58  E-value: 4.83e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069707  95 ITIKSIGRQWYWSYEYSDFMNIEFDSYMLMNN--EKNSFRLLEVDNRTMMPMNSEIRMLTSASDVLHSWTIPSLGIKIDA 172
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEdlEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1896069707 173 TPGRLNQSTFLINRPGLFFGQCSEICGANHSFMPITLEST 212
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
59-221 4.84e-43

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 144.59  E-value: 4.84e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069707  59 HKLEIMWTTIPTMTLMLIAMPSIQLLYLMDDSTTPLITIKSIGRQWYWSYEYSDfmniefdsymlmnneKNSfrllEVDN 138
Cdd:COG1622    77 TKLEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPD---------------QGI----ATVN 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069707 139 RTMMPMNSEIRMLTSASDVLHSWTIPSLGIKIDATPGRLNQSTFLINRPGLFFGQCSEICGANHSFMPITLESTSIKLFI 218
Cdd:COG1622   138 ELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFD 217


                  ...
gi 1896069707 219 KWL 221
Cdd:COG1622   218 AWL 220
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 13-221 6.04e-38

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: 130.58  E-value: 6.04e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069707  13 ASPLMEQLSFFHDHTMTIIIMITIIVSYSMMFTF-----KNKFLMKTMLQEH-KLEIMWTTIPTMTLM-LIAMPSIQLLY 85
Cdd:TIGR02866   2 GGEIAQQIAFLFLFVLAVSTLISLLVAALLAYVVwkfrrKGDEEKPSQIHGNrRLEYVWTVIPLIIVVgLFAATAKGLLY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069707  86 LMDDSTTPLITIKSIGRQWYWSYEYSDFmniefdsymlmnneknsfrLLEVDNRTMMPMNSEIRMLTSASDVLHSWTIPS 165
Cdd:TIGR02866  82 LERPIPKDALKVKVTGYQWWWDFEYPES-------------------GFTTVNELVLPAGTPVELQVTSKDVIHSFWVPE 142

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1896069707 166 LGIKIDATPGRLNQSTFLINRPGLFFGQCSEICGANHSFMPITLESTSIKLFIKWL 221
Cdd:TIGR02866 143 LGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYV 198
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-223 8.89e-132

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 369.93  E-value: 8.89e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069707   1 MATWTNWSLQDSASPLMEQLSFFHDHTMTIIIMITIIVSYSMMFTFKNKFLMKTMLQEHKLEIMWTTIPTMTLMLIAMPS 80
Cdd:MTH00154    1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069707  81 IQLLYLMDDSTTPLITIKSIGRQWYWSYEYSDFMNIEFDSYMLMNNE--KNSFRLLEVDNRTMMPMNSEIRMLTSASDVL 158
Cdd:MTH00154   81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNEleNNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1896069707 159 HSWTIPSLGIKIDATPGRLNQSTFLINRPGLFFGQCSEICGANHSFMPITLESTSIKLFIKWLMK 223
Cdd:MTH00154  161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKN 225
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-221 1.51e-106

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 306.26  E-value: 1.51e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069707   1 MATWTNWSLQDSASPLMEQLSFFHDHTMTIIIMITIIVSYSMMFTFKNKFLMKTMLQEHKLEIMWTTIPTMTLMLIAMPS 80
Cdd:MTH00139    1 MAYWGQLGFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069707  81 IQLLYLMDDSTTPLITIKSIGRQWYWSYEYSDFMNIEFDSYMLMNNE--KNSFRLLEVDNRTMMPMNSEIRMLTSASDVL 158
Cdd:MTH00139   81 LRLLYLMDEVSDPYLTFKAVGHQWYWSYEYSDFKNLSFDSYMIPTEDlsSGEFRLLEVDNRLVLPYKSNIRALITAADVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1896069707 159 HSWTIPSLGIKIDATPGRLNQSTFLINRPGLFFGQCSEICGANHSFMPITLESTSIKLFIKWL 221
Cdd:MTH00139  161 HSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEWI 223
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-223 4.36e-105

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 302.22  E-value: 4.36e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069707   1 MATWTNWSLQDSASPLMEQLSFFHDHTMTIIIMITIIVSYSMMFTFKNKFLMKTMLQEHKLEIMWTTIPTMTLMLIAMPS 80
Cdd:MTH00117    1 MANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069707  81 IQLLYLMDDSTTPLITIKSIGRQWYWSYEYSDFMNIEFDSYMLMNNE--KNSFRLLEVDNRTMMPMNSEIRMLTSASDVL 158
Cdd:MTH00117   81 LRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDlpNGHFRLLEVDHRMVIPMESPIRILITAEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1896069707 159 HSWTIPSLGIKIDATPGRLNQSTFLINRPGLFFGQCSEICGANHSFMPITLESTSIKLFIKWLMK 223
Cdd:MTH00117  161 HSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSL 225
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-222 1.36e-103

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 298.78  E-value: 1.36e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069707   1 MATWTNWSLQDSASPLMEQLSFFHDHTMTIIIMITIIVSYSMMFTFKNKFLMKTMLQEHKLEIMWTTIPTMTLMLIAMPS 80
Cdd:MTH00140    1 MSYWGQLGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069707  81 IQLLYLMDDSTTPLITIKSIGRQWYWSYEYSDFMNIEFDSYMLMNNEKNS--FRLLEVDNRTMMPMNSEIRMLTSASDVL 158
Cdd:MTH00140   81 LRLLYLLDETNNPLLTVKAIGHQWYWSYEYSDFSVIEFDSYMVPENELELgdFRLLEVDNRLVLPYSVDTRVLVTSADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1896069707 159 HSWTIPSLGIKIDATPGRLNQSTFLINRPGLFFGQCSEICGANHSFMPITLESTSIKLFIKWLM 222
Cdd:MTH00140  161 HSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWLE 224
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-221 2.07e-98

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 285.34  E-value: 2.07e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069707   1 MATWTNWSLQDSASPLMEQLSFFHDHTMTIIIMITIIVSYSMMFTFKNKFLMKTMLQEHKLEIMWTTIPTMTLMLIAMPS 80
Cdd:MTH00168    1 MATYSQLGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069707  81 IQLLYLMDDSTTPLITIKSIGRQWYWSYEYSDFMNIEFDSYMLMNNEKN--SFRLLEVDNRTMMPMNSEIRMLTSASDVL 158
Cdd:MTH00168   81 LRLLYLMDEIDKPDLTIKAVGHQWYWSYEYTDYNDLEFDSYMVPTQDLSpgQFRLLEVDNRLVLPMDSKIRVLVTSADVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1896069707 159 HSWTIPSLGIKIDATPGRLNQSTFLINRPGLFFGQCSEICGANHSFMPITLESTSIKLFIKWL 221
Cdd:MTH00168  161 HSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENWV 223
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-220 2.86e-98

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 285.06  E-value: 2.86e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069707   1 MATWTNWSLQDSASPLMEQLSFFHDHTMTIIIMITIIVSYSMMFTFKNKFLMKTMLQEHKLEIMWTTIPTMTLMLIAMPS 80
Cdd:MTH00038    1 MATWLQLGLQDASSPLMEELIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069707  81 IQLLYLMDDSTTPLITIKSIGRQWYWSYEYSDFMNIEFDSYMLMNNEKNS--FRLLEVDNRTMMPMNSEIRMLTSASDVL 158
Cdd:MTH00038   81 LQLLYLMDEVNNPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDLSTglPRLLEVDNRLVLPYQTPIRVLVSSADVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1896069707 159 HSWTIPSLGIKIDATPGRLNQSTFLINRPGLFFGQCSEICGANHSFMPITLESTSIKLFIKW 220
Cdd:MTH00038  161 HSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENW 222
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-223 1.59e-96

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 280.97  E-value: 1.59e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069707   1 MATWTNWSLQDSASPLMEQLSFFHDHTMTIIIMITIIVSYSMMFTFKNKFLMKTMLQEHKLEIMWTTIPTMTLMLIAMPS 80
Cdd:MTH00008    1 MPHWGQLMFQDAASPVMLQLISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069707  81 IQLLYLMDDSTTPLITIKSIGRQWYWSYEYSDFMNIEFDSYMLMNNE--KNSFRLLEVDNRTMMPMNSEIRMLTSASDVL 158
Cdd:MTH00008   81 LRLLYLMDEVSNPSITLKTIGHQWYWSYEYSDFSNLEFDSYMLPTSDlsPGQFRLLEVDNRAVLPMQTEIRVLVTAADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1896069707 159 HSWTIPSLGIKIDATPGRLNQSTFLINRPGLFFGQCSEICGANHSFMPITLESTSIKLFIKWLMK 223
Cdd:MTH00008  161 HSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKWVSS 225
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 8-222 9.07e-92

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 269.31  E-value: 9.07e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069707   8 SLQDSASPLMEQLSFFHDHTMTIIIMITIIVSYSMMFTFKNKFLMKTMLQEHKLEIMWTTIPTMTLMLIAMPSIQLLYLM 87
Cdd:MTH00023   17 GFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKLLYLM 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069707  88 DDSTTPLITIKSIGRQWYWSYEYSDFM--NIEFDSYMLMNNEKNS--FRLLEVDNRTMMPMNSEIRMLTSASDVLHSWTI 163
Cdd:MTH00023   97 DEVVSPALTIKAIGHQWYWSYEYSDYEgeTLEFDSYMVPTSDLNSgdFRLLEVDNRLVVPINTHVRILVTGADVLHSFAV 176

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1896069707 164 PSLGIKIDATPGRLNQSTFLINRPGLFFGQCSEICGANHSFMPITLESTSIKLFIKWLM 222
Cdd:MTH00023  177 PSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWLL 235
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 1-220 2.74e-90

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 265.04  E-value: 2.74e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069707   1 MATWTNWSLQDSASPLMEQLSFFHDHTMTIIIMITIIVSYSMMFTFKNKFLMKTMLQEHKLEIMWTTIPTMTLMLIAMPS 80
Cdd:MTH00129    1 MAHPSQLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069707  81 IQLLYLMDDSTTPLITIKSIGRQWYWSYEYSDFMNIEFDSYMLMNNE--KNSFRLLEVDNRTMMPMNSEIRMLTSASDVL 158
Cdd:MTH00129   81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMIPTQDltPGQFRLLEADHRMVVPVESPIRVLVSAEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1896069707 159 HSWTIPSLGIKIDATPGRLNQSTFLINRPGLFFGQCSEICGANHSFMPITLESTSIKLFIKW 220
Cdd:MTH00129  161 HSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFENW 222
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 1-220 7.29e-89

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 261.36  E-value: 7.29e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069707   1 MATWTNWSLQDSASPLMEQLSFFHDHTMTIIIMITIIVSYSMMFTFKNKFLMKTMLQEHKLEIMWTTIPTMTLMLIAMPS 80
Cdd:MTH00185    1 MAHPSQLGLQDAASPVMEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069707  81 IQLLYLMDDSTTPLITIKSIGRQWYWSYEYSDFMNIEFDSYMLMNNEKNS--FRLLEVDNRTMMPMNSEIRMLTSASDVL 158
Cdd:MTH00185   81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEQLEFDSYMTPTQDLTPgqFRLLETDHRMVVPMESPIRVLITAEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1896069707 159 HSWTIPSLGIKIDATPGRLNQSTFLINRPGLFFGQCSEICGANHSFMPITLESTSIKLFIKW 220
Cdd:MTH00185  161 HSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENW 222
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-220 1.32e-88

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 260.81  E-value: 1.32e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069707   1 MATWTNWSLQDSASPLMEQLSFFHDHTMTIIIMITIIVSYSMMFTFKNKFLMKTMLQEHKLEIMWTTIPTMTLMLIAMPS 80
Cdd:MTH00098    1 MAYPFQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069707  81 IQLLYLMDDSTTPLITIKSIGRQWYWSYEYSDFMNIEFDSYMLMNNEKN--SFRLLEVDNRTMMPMNSEIRMLTSASDVL 158
Cdd:MTH00098   81 LRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKpgELRLLEVDNRVVLPMEMPIRMLISSEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1896069707 159 HSWTIPSLGIKIDATPGRLNQSTFLINRPGLFFGQCSEICGANHSFMPITLESTSIKLFIKW 220
Cdd:MTH00098  161 HSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKW 222
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 1-221 4.62e-87

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 256.63  E-value: 4.62e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069707   1 MATWTNWSLQDSASPLMEQLSFFHDHTMTIIIMITIIVSYSMMFTFKNKFLMKTMLQEHKLEIMWTTIPTMTLMLIAMPS 80
Cdd:MTH00076    1 MAHPSQLGFQDAASPIMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069707  81 IQLLYLMDDSTTPLITIKSIGRQWYWSYEYSDFMNIEFDSYMLMNNEKN--SFRLLEVDNRTMMPMNSEIRMLTSASDVL 158
Cdd:MTH00076   81 LRILYLMDEINDPHLTVKAIGHQWYWSYEYTDYEDLSFDSYMIPTQDLTpgQFRLLEVDNRMVVPMESPIRMLITAEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1896069707 159 HSWTIPSLGIKIDATPGRLNQSTFLINRPGLFFGQCSEICGANHSFMPITLESTSIKLFIKWL 221
Cdd:MTH00076  161 HSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLNWS 223
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 7-221 2.26e-86

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 255.09  E-value: 2.26e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069707   7 WSL--QDSASPLMEQLSFFHDHTMTIIIMITIIVSYSMMFTFKNKFLMKTMLQEHKLEIMWTTIPTMTLMLIAMPSIQLL 84
Cdd:MTH00051    7 WQLgfQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSLKLL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069707  85 YLMDDSTTPLITIKSIGRQWYWSYEYSDF--MNIEFDSYMLMNNEKNS--FRLLEVDNRTMMPMNSEIRMLTSASDVLHS 160
Cdd:MTH00051   87 YLMDEVIDPALTIKAIGHQWYWSYEYSDYgtDTIEFDSYMIPTSDLNSgdLRLLEVDNRLIVPIQTQVRVLVTAADVLHS 166

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1896069707 161 WTIPSLGIKIDATPGRLNQSTFLINRPGLFFGQCSEICGANHSFMPITLESTSIKLFIKWL 221
Cdd:MTH00051  167 FAVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINWV 227
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 93-220 4.50e-83

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: 242.86  E-value: 4.50e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069707  93 PLITIKSIGRQWYWSYEYSDFMNIEFDSYMLMNN--EKNSFRLLEVDNRTMMPMNSEIRMLTSASDVLHSWTIPSLGIKI 170
Cdd:cd13912     1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDdlEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1896069707 171 DATPGRLNQSTFLINRPGLFFGQCSEICGANHSFMPITLESTSIKLFIKW 220
Cdd:cd13912    81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-212 4.83e-72

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 214.58  E-value: 4.83e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069707  95 ITIKSIGRQWYWSYEYSDFMNIEFDSYMLMNN--EKNSFRLLEVDNRTMMPMNSEIRMLTSASDVLHSWTIPSLGIKIDA 172
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEdlEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1896069707 173 TPGRLNQSTFLINRPGLFFGQCSEICGANHSFMPITLEST 212
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 7-221 2.18e-66

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 205.64  E-value: 2.18e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069707   7 WSL--QDSASPLMEQLSFFHDHTMTIIIMITIIVSYSMM-FTFKNKFLMK--TMLQEHKLEIMWTTIPTMTLMLIAMPSI 81
Cdd:MTH00027   33 WQLgfQDAGSPVMEEIIMLHDQILFILTIIVGVVLWLIIrILLGNNYYSYywNKLDGSLIEVIWTLIPAFILILIAFPSL 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069707  82 QLLYLMDDST-TPLITIKSIGRQWYWSYEYSDF--MNIEFDSYML--MNNEKNSFRLLEVDNRTMMPMNSEIRMLTSASD 156
Cdd:MTH00027  113 RLLYIMDECGfSANITIKVTGHQWYWSYSYEDYgeKNIEFDSYMIptADLEFGDLRLLEVDNRLILPVDTNVRVLITAAD 192

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1896069707 157 VLHSWTIPSLGIKIDATPGRLNQSTFLINRPGLFFGQCSEICGANHSFMPITLESTSIKLFIKWL 221
Cdd:MTH00027  193 VLHSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYIDWI 257
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 23-221 1.84e-61

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 191.76  E-value: 1.84e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069707  23 FHDHTMTIIIMITIIVSYSMMFTFKNKFLMKTMLQEHKLEIMWTTIPTMTLMLIAMPSIQLLYLMD----DSTtplITIK 98
Cdd:MTH00080   25 FNCSLLFGEFVLAFVVFLFLYLISNNFYFKSKKIEYQFGELLCSVFPVLILLMQMVPSLSLLYYYGlmnlDSN---LTVK 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069707  99 SIGRQWYWSYEYSDFMNIEFDSYMLMNNEKN--SFRLLEVDNRTMMPMNSEIRMLTSASDVLHSWTIPSLGIKIDATPGR 176
Cdd:MTH00080  102 VTGHQWYWSYEFSDIPGLEFDSYMKSLDQLRlgEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDAMSGI 181

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1896069707 177 LNQSTFLINRPGLFFGQCSEICGANHSFMPITLESTSIKLFIKWL 221
Cdd:MTH00080  182 LSTLCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKEWC 226
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
59-221 4.84e-43

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 144.59  E-value: 4.84e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069707  59 HKLEIMWTTIPTMTLMLIAMPSIQLLYLMDDSTTPLITIKSIGRQWYWSYEYSDfmniefdsymlmnneKNSfrllEVDN 138
Cdd:COG1622    77 TKLEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPD---------------QGI----ATVN 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069707 139 RTMMPMNSEIRMLTSASDVLHSWTIPSLGIKIDATPGRLNQSTFLINRPGLFFGQCSEICGANHSFMPITLESTSIKLFI 218
Cdd:COG1622   138 ELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFD 217


                  ...
gi 1896069707 219 KWL 221
Cdd:COG1622   218 AWL 220
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 61-210 3.32e-42

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 141.25  E-value: 3.32e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069707  61 LEIMWTTIPTMtlMLIAMPSIQLLYLMDDS-TTPLITIKSIGRQWYWSYEYSDfmNIEFDSYM--LMNNeknsfrlleVD 137
Cdd:MTH00047   49 LELLWTVVPTL--LVLVLCFLNLNFITSDLdCFSSETIKVIGHQWYWSYEYSF--GGSYDSFMtdDIFG---------VD 115

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1896069707 138 NRTMMPMNSEIRMLTSASDVLHSWTIPSLGIKIDATPGRLNQSTFLINRPGLFFGQCSEICGANHSFMPITLE 210
Cdd:MTH00047  116 KPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCPDRHGVFVGYCSELCGVGHSYMPIVIE 188
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 13-221 6.04e-38

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: 130.58  E-value: 6.04e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069707  13 ASPLMEQLSFFHDHTMTIIIMITIIVSYSMMFTF-----KNKFLMKTMLQEH-KLEIMWTTIPTMTLM-LIAMPSIQLLY 85
Cdd:TIGR02866   2 GGEIAQQIAFLFLFVLAVSTLISLLVAALLAYVVwkfrrKGDEEKPSQIHGNrRLEYVWTVIPLIIVVgLFAATAKGLLY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069707  86 LMDDSTTPLITIKSIGRQWYWSYEYSDFmniefdsymlmnneknsfrLLEVDNRTMMPMNSEIRMLTSASDVLHSWTIPS 165
Cdd:TIGR02866  82 LERPIPKDALKVKVTGYQWWWDFEYPES-------------------GFTTVNELVLPAGTPVELQVTSKDVIHSFWVPE 142

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1896069707 166 LGIKIDATPGRLNQSTFLINRPGLFFGQCSEICGANHSFMPITLESTSIKLFIKWL 221
Cdd:TIGR02866 143 LGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYV 198
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 132-213 5.48e-35

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 121.85  E-value: 5.48e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069707 132 RLLEVDNRTMMPMNSEIRMLTSASDVLHSWTIPSLGIKIDATPGRLNQSTFLINRPGLFFGQCSEICGANHSFMPITLES 211
Cdd:PTZ00047   67 RQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCSEMCGTLHGFMPIVVEA 146


                  ..
gi 1896069707 212 TS 213
Cdd:PTZ00047  147 VS 148
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 95-210 9.77e-27

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: 98.52  E-value: 9.77e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069707  95 ITIKSIGRQWYWSYEYsdfmniefdsymlmnNEKNSFRLLEVdnrtmmPMNSEIRMLTSASDVLHSWTIPSLGIKIDATP 174
Cdd:cd13842     1 LTVYVTGVQWSWTFIY---------------PNVRTPNEIVV------PAGTPVRFRVTSPDVIHGFYIPNLGVKVDAVP 59

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1896069707 175 GRLNQSTFLINRPGLFFGQCSEICGANHSFMPITLE 210
Cdd:cd13842    60 GYTSELWFVADKPGTYTIICAEYCGLGHSYMLGKVE 95
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 95-205 1.20e-21

The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), the terminal oxidase in the respiratory chains of most bacteria, is a multi-chain transmembrane protein located in the inner membrane the cell membrane of prokaryotes. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. Caa3 type of CcO Subunit II contains a copper-copper binuclear site called CuA, which is believed to be involved in electron transfer from cytochrome c to the cytochromes a, a3 and CuB active site in subunit I.


Pssm-ID: 259875 [Multi-domain]  Cd Length: 103  Bit Score: 85.36  E-value: 1.20e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069707  95 ITIKSIGRQWYWSYEYSDfmniefdsymlmnnekNSFRLLEVDNRTMMPMNSEIRMLTSASDVLHSWTIPSLGIKIDATP 174
Cdd:cd04213     2 LTIEVTGHQWWWEFRYPD----------------EPGRGIVTANELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMDMIP 65

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1896069707 175 GRLNQSTFLINRPGLFFGQCSEICGANHSFM 205
Cdd:cd04213    66 GRTNRLWLQADEPGVYRGQCAEFCGASHALM 96
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-205 3.61e-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: 259986 [Multi-domain]  Cd Length: 107  Bit Score: 79.22  E-value: 3.61e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069707  95 ITIKSIGRQWYWSYEYSDfmniefdsymlmNNEKNSFRLLEVDNRTMMPMNSEIRMLTSASDVLHSWTIPSLGIKIDATP 174
Cdd:cd13919     2 LVVEVTAQQWAWTFRYPG------------GDGKLGTDDDVTSPELHLPVGRPVLFNLRSKDVIHSFWVPEFRVKQDAVP 69

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1896069707 175 GRLNQSTFLINRPGLFFGQCSEICGANHSFM 205
Cdd:cd13919    70 GRTTRLWFTPTREGEYEVRCAELCGLGHYRM 100
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-205 4.71e-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: 259982 [Multi-domain]  Cd Length: 98  Bit Score: 78.44  E-value: 4.71e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069707  95 ITIKSIGRQWYWSYEYSdfmniefdsymlmnNEKnsfrllEVDNRTMMPMNSEIRMLTSASDVLHSWTIPSLGIKIDATP 174
Cdd:cd13915     2 LEIQVTGRQWMWEFTYP--------------NGK------REINELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQDVVP 61

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1896069707 175 GRLNQSTFLINRPGLFFGQCSEICGANHSFM 205
Cdd:cd13915    62 GRYTYLWFEATKPGEYDLFCTEYCGTGHSGM 92
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 75-221 2.30e-16

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: 72.87  E-value: 2.30e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069707  75 LIAMPSIQLLYLMDDSTTP---LITIKSIGRQWYWSYEYSdfmniefdsymlmnNEKNSFRLLEVdnrtmmPMNSEIRML 151
Cdd:cd13918    10 LIVWTYGMLLYVEDPPDEAdedALEVEVEGFQFGWQFEYP--------------NGVTTGNTLRV------PADTPIALR 69

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069707 152 TSASDVLHSWTIPSLGIKIDATPGRLNQSTFLINRPGLFFGQCSEICGANHSFMPITLESTSIKLFIKWL 221
Cdd:cd13918    70 VTSTDVFHTFGIPELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEFEAWY 139
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-221 1.45e-14

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


Pssm-ID: 259981 [Multi-domain]  Cd Length: 108  Bit Score: 67.05  E-value: 1.45e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069707  95 ITIKSIGRQWYWSYEYSDFMNIEFdsymlmnneknsfrllevdNRTMMPMNSEIRMLTSASDVLHSWTIPSLGIKIDATP 174
Cdd:cd13914     1 VEIEVEAYQWGWEFSYPEANVTTS-------------------EQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDAFP 61

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1896069707 175 GRLNQSTFLINRPGLFFGQCSEICGANHSFMPITLESTSIKLFIKWL 221
Cdd:cd13914    62 GQYNTIKTEATEEGEYQLYCAEYCGAGHSQMLSTVTVVSQDEYQQWL 108
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-83 1.29e-12

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: 61.58  E-value: 1.29e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069707   1 MATWTNWSLQDSASPLMEQLSFFHDHTMTIIIMITIIVSY---SMMFTF---KNKFLMKTMLQEHKLEIMWTTIPTMTLM 74
Cdd:pfam02790   1 MPTPWGLGFQDAASPLMEGLLELHDYIMFILTLILILVLYilvTCLIRFnrrKNPITARYTTHGQTIEIIWTIIPAVILI 80


                  ....*....
gi 1896069707  75 LIAMPSIQL 83
Cdd:pfam02790  81 LIALPSFKL 89
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 143-205 1.59e-06

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: 45.25  E-value: 1.59e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1896069707 143 PMNSEIRMLTSASDVLHSWTIPSLGIKIDATPGRLNQSTFLINRPGLFFGQCSEICGANHSFM 205
Cdd:cd13913    30 PAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNM 92
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 138-205 1.23e-03

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: 37.14  E-value: 1.23e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1896069707 138 NRTMMPMNSEIRMLTSASDVLHSWTIPSLGIKIDATPGRLNQSTFLINRPGLFFGQCSEICGANHSFM 205
Cdd:cd04212    25 NELVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGTYQGLSANYSGEGFSDM 92
N2OR_C cd04223
The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase ...
 154-205 1.88e-03

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: 36.44  E-value: 1.88e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1896069707 154 ASDVLHSWTIPSLGIKIDATPGRLNQSTFLINRPGLFFGQCSEICGANHSFM 205
Cdd:cd04223    36 DEDITHGFAIPGYNVNLSLEPGETATVTFVADKPGVYPYYCTEFCSALHLEM 87
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 151-210 3.92e-03

Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in inter-molecular electron transfer reactions. Cupredoxins are blue copper proteins, having an intense blue color due to the presence of a mononuclear type 1 (T1) copper site. Structurally, the cupredoxin-like fold consists of a beta-sandwich with 7 strands in 2 beta-sheets, which is arranged in a Greek-key beta-barrel. Some of these proteins have lost the ability to bind copper. The majority of family members contain multiple cupredoxin domain repeats: ceruloplasmin and the coagulation factors V/VIII have six repeats; laccase, ascorbate oxidase, spore coat protein A, and multicopper oxidase CueO contain three repeats; and nitrite reductase has two repeats. Others are mono-domain cupredoxins, such as plastocyanin, pseudoazurin, plantacyanin, azurin, rusticyanin, stellacyanin, quinol oxidase, and the periplasmic domain of cytochrome c oxidase subunit II.


Pssm-ID: 259860 [Multi-domain]  Cd Length: 110  Bit Score: 36.05  E-value: 3.92e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1896069707 151 LTSASDVLHSWTIPSLGIKIDA---------------TPGRLNQSTFLINRPGLFFGQCSEICGaNHSFMPITLE 210
Cdd:cd00920    37 FVNKLGENHSVTIAGFGVPVVAmagganpglvntlviGPGESAEVTFTTDQAGVYWFYCTIPGH-NHAGMVGTIN 110
CuRO_HCO_II_like_4 cd13917
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 145-205 5.31e-03

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: 259984 [Multi-domain]  Cd Length: 88  Bit Score: 35.04  E-value: 5.31e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1896069707 145 NSEIRMLTSASDVLHSWTIPSLGIKIDATPGRLNQSTFLINRPGLFFGQCSEICGANHSFM 205
Cdd:cd13917    21 GKTYRLHLSSLDVQHGFSLQPKNINFQVLPGYEWVITMTPNETGEFHIICNEYCGIGHHTM 81
 
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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