NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2554488869|ref|YP_010890643|]
View 

cytochrome c oxidase subunit II (mitochondrion) [Amazona vinacea]

Protein Classification

cytochrome c oxidase subunit II( domain architecture ID 11475905)

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-225 1.41e-162

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 447.82  E-value: 1.41e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554488869   1 MANHSQLGFQDASSPIMEELIEFHDHALMVALTICSLVLYLLTLMLMEKLS-SNTVDAQEVELIWTILPAIVLILLALPS 79
Cdd:MTH00117    1 MANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLThTNTVDAQEVELIWTILPAIVLILLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554488869  80 LQILYMMDEVDEPDLTLKAIGHQWYWSYEYTDFKDLSFDSYMTPSTELPMGYFRLLEVDHRVIIPMESPIRMIITADDVL 159
Cdd:MTH00117   81 LRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2554488869 160 HSWAVPTLGVKTDAIPGRLNQTSFITTRPGIFYGQCSEICGANHSFMPIVVESIPLTHFETWSSLL 225
Cdd:MTH00117  161 HSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSLL 226
 
Name Accession Description Interval E-value
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-225 1.41e-162

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 447.82  E-value: 1.41e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554488869   1 MANHSQLGFQDASSPIMEELIEFHDHALMVALTICSLVLYLLTLMLMEKLS-SNTVDAQEVELIWTILPAIVLILLALPS 79
Cdd:MTH00117    1 MANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLThTNTVDAQEVELIWTILPAIVLILLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554488869  80 LQILYMMDEVDEPDLTLKAIGHQWYWSYEYTDFKDLSFDSYMTPSTELPMGYFRLLEVDHRVIIPMESPIRMIITADDVL 159
Cdd:MTH00117   81 LRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2554488869 160 HSWAVPTLGVKTDAIPGRLNQTSFITTRPGIFYGQCSEICGANHSFMPIVVESIPLTHFETWSSLL 225
Cdd:MTH00117  161 HSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSLL 226
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 92-221 5.42e-92

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: 265.59  E-value: 5.42e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554488869  92 PDLTLKAIGHQWYWSYEYTDFKDLSFDSYMTPSTELPMGYFRLLEVDHRVIIPMESPIRMIITADDVLHSWAVPTLGVKT 171
Cdd:cd13912     1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2554488869 172 DAIPGRLNQTSFITTRPGIFYGQCSEICGANHSFMPIVVESIPLTHFETW 221
Cdd:cd13912    81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
94-213 1.05e-83

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 244.63  E-value: 1.05e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554488869  94 LTLKAIGHQWYWSYEYTDFKDLSFDSYMTPSTELPMGYFRLLEVDHRVIIPMESPIRMIITADDVLHSWAVPTLGVKTDA 173
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2554488869 174 IPGRLNQTSFITTRPGIFYGQCSEICGANHSFMPIVVESI 213
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
60-221 6.93e-54

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 172.71  E-value: 6.93e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554488869  60 VELIWTILPAIVLILLALPSLQILYMMDEVDEPDLTLKAIGHQWYWSYEYTDFKDLsfdsymtpstelpmgyfrlleVDH 139
Cdd:COG1622    79 LEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIA---------------------TVN 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554488869 140 RVIIPMESPIRMIITADDVLHSWAVPTLGVKTDAIPGRLNQTSFITTRPGIFYGQCSEICGANHSFMPIVVESIPLTHFE 219
Cdd:COG1622   138 ELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFD 217


                  ..
gi 2554488869 220 TW 221
Cdd:COG1622   218 AW 219
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 12-221 5.20e-42

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: 141.36  E-value: 5.20e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554488869  12 ASSPIMEELIEFHDHALMVALTICSLVLYLLTLMLM-------EKLSSNTVDAQEVELIWTILPA-IVLILLALPSLQIL 83
Cdd:TIGR02866   1 PGGEIAQQIAFLFLFVLAVSTLISLLVAALLAYVVWkfrrkgdEEKPSQIHGNRRLEYVWTVIPLiIVVGLFAATAKGLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554488869  84 YMMDEVDEPDLTLKAIGHQWYWSYEYtdfkdlsfdsymtpstelPMGYFRlleVDHRVIIPMESPIRMIITADDVLHSWA 163
Cdd:TIGR02866  81 YLERPIPKDALKVKVTGYQWWWDFEY------------------PESGFT---TVNELVLPAGTPVELQVTSKDVIHSFW 139

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2554488869 164 VPTLGVKTDAIPGRLNQTSFITTRPGIFYGQCSEICGANHSFMPIVVESIPLTHFETW 221
Cdd:TIGR02866 140 VPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAY 197
 
Name Accession Description Interval E-value
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-225 1.41e-162

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 447.82  E-value: 1.41e-162
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554488869   1 MANHSQLGFQDASSPIMEELIEFHDHALMVALTICSLVLYLLTLMLMEKLS-SNTVDAQEVELIWTILPAIVLILLALPS 79
Cdd:MTH00117    1 MANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLThTNTVDAQEVELIWTILPAIVLILLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554488869  80 LQILYMMDEVDEPDLTLKAIGHQWYWSYEYTDFKDLSFDSYMTPSTELPMGYFRLLEVDHRVIIPMESPIRMIITADDVL 159
Cdd:MTH00117   81 LRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2554488869 160 HSWAVPTLGVKTDAIPGRLNQTSFITTRPGIFYGQCSEICGANHSFMPIVVESIPLTHFETWSSLL 225
Cdd:MTH00117  161 HSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSLL 226
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 1-226 2.50e-131

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 369.04  E-value: 2.50e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554488869   1 MANHSQLGFQDASSPIMEELIEFHDHALMVALTICSLVLYLLTLMLMEKLSS-NTVDAQEVELIWTILPAIVLILLALPS 79
Cdd:MTH00129    1 MAHPSQLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNkYILDSQEIEIIWTVLPAVILILIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554488869  80 LQILYMMDEVDEPDLTLKAIGHQWYWSYEYTDFKDLSFDSYMTPSTELPMGYFRLLEVDHRVIIPMESPIRMIITADDVL 159
Cdd:MTH00129   81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2554488869 160 HSWAVPTLGVKTDAIPGRLNQTSFITTRPGIFYGQCSEICGANHSFMPIVVESIPLTHFETWSSLLM 226
Cdd:MTH00129  161 HSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLML 227
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-226 7.15e-131

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 367.89  E-value: 7.15e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554488869   1 MANHSQLGFQDASSPIMEELIEFHDHALMVALTICSLVLYLLTLMLMEKLS-SNTVDAQEVELIWTILPAIVLILLALPS 79
Cdd:MTH00098    1 MAYPFQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLThTSTMDAQEVETIWTILPAIILILIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554488869  80 LQILYMMDEVDEPDLTLKAIGHQWYWSYEYTDFKDLSFDSYMTPSTELPMGYFRLLEVDHRVIIPMESPIRMIITADDVL 159
Cdd:MTH00098   81 LRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2554488869 160 HSWAVPTLGVKTDAIPGRLNQTSFITTRPGIFYGQCSEICGANHSFMPIVVESIPLTHFETWSSLLM 226
Cdd:MTH00098  161 HSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKWSASML 227
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 1-224 3.12e-130

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 366.41  E-value: 3.12e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554488869   1 MANHSQLGFQDASSPIMEELIEFHDHALMVALTICSLVLYLLTLMLMEKLSS-NTVDAQEVELIWTILPAIVLILLALPS 79
Cdd:MTH00076    1 MAHPSQLGFQDAASPIMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNtNTMDAQEIEMVWTIMPAIILIVIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554488869  80 LQILYMMDEVDEPDLTLKAIGHQWYWSYEYTDFKDLSFDSYMTPSTELPMGYFRLLEVDHRVIIPMESPIRMIITADDVL 159
Cdd:MTH00076   81 LRILYLMDEINDPHLTVKAIGHQWYWSYEYTDYEDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2554488869 160 HSWAVPTLGVKTDAIPGRLNQTSFITTRPGIFYGQCSEICGANHSFMPIVVESIPLTHFETWSSL 224
Cdd:MTH00076  161 HSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLNWSSS 225
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-226 2.15e-129

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 364.15  E-value: 2.15e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554488869   1 MANHSQLGFQDASSPIMEELIEFHDHALMVALTICSLVLYLLTLMLMEKLSS-NTVDAQEVELIWTILPAIVLILLALPS 79
Cdd:MTH00154    1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNrFLLEGQEIEIIWTILPAIILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554488869  80 LQILYMMDEVDEPDLTLKAIGHQWYWSYEYTDFKDLSFDSYMTPSTELPMGYFRLLEVDHRVIIPMESPIRMIITADDVL 159
Cdd:MTH00154   81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2554488869 160 HSWAVPTLGVKTDAIPGRLNQTSFITTRPGIFYGQCSEICGANHSFMPIVVESIPLTHFETWSSLLM 226
Cdd:MTH00154  161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNMS 227
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 1-226 1.24e-122

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 347.26  E-value: 1.24e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554488869   1 MANHSQLGFQDASSPIMEELIEFHDHALMVALTICSLVLYLLTLMLMEKLSSN-TVDAQEVELIWTILPAIVLILLALPS 79
Cdd:MTH00185    1 MAHPSQLGLQDAASPVMEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKyILDSQEIEIVWTILPAIILIMIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554488869  80 LQILYMMDEVDEPDLTLKAIGHQWYWSYEYTDFKDLSFDSYMTPSTELPMGYFRLLEVDHRVIIPMESPIRMIITADDVL 159
Cdd:MTH00185   81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2554488869 160 HSWAVPTLGVKTDAIPGRLNQTSFITTRPGIFYGQCSEICGANHSFMPIVVESIPLTHFETWSSLLM 226
Cdd:MTH00185  161 HSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLML 227
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-223 9.77e-122

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 344.66  E-value: 9.77e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554488869   1 MANHSQLGFQDASSPIMEELIEFHDHALMVALTICSLVLYLLTLMLMEKLSSNTV-DAQEVELIWTILPAIVLILLALPS 79
Cdd:MTH00168    1 MATYSQLGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLlDSQMIEFVWTIIPAFILISLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554488869  80 LQILYMMDEVDEPDLTLKAIGHQWYWSYEYTDFKDLSFDSYMTPSTELPMGYFRLLEVDHRVIIPMESPIRMIITADDVL 159
Cdd:MTH00168   81 LRLLYLMDEIDKPDLTIKAVGHQWYWSYEYTDYNDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2554488869 160 HSWAVPTLGVKTDAIPGRLNQTSFITTRPGIFYGQCSEICGANHSFMPIVVESIPLTHFETWSS 223
Cdd:MTH00168  161 HSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENWVD 224
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-221 1.15e-117

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 334.60  E-value: 1.15e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554488869   1 MANHSQLGFQDASSPIMEELIEFHDHALMVALTICSLVLYLLTLMLMEKLSSNTV-DAQEVELIWTILPAIVLILLALPS 79
Cdd:MTH00140    1 MSYWGQLGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTIlEAQKLETIWTIVPALILVFLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554488869  80 LQILYMMDEVDEPDLTLKAIGHQWYWSYEYTDFKDLSFDSYMTPSTELPMGYFRLLEVDHRVIIPMESPIRMIITADDVL 159
Cdd:MTH00140   81 LRLLYLLDETNNPLLTVKAIGHQWYWSYEYSDFSVIEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2554488869 160 HSWAVPTLGVKTDAIPGRLNQTSFITTRPGIFYGQCSEICGANHSFMPIVVESIPLTHFETW 221
Cdd:MTH00140  161 HSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKW 222
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-223 2.33e-117

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 333.59  E-value: 2.33e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554488869   1 MANHSQLGFQDASSPIMEELIEFHDHALMVaLTICSLVLYLLTLMLMekLSSNT----VDAQEVELIWTILPAIVLILLA 76
Cdd:MTH00038    1 MATWLQLGLQDASSPLMEELIYFHDYALII-LTLITILVFYGLASLL--FSSPTnrffLEGQELETIWTIVPAFILIFIA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554488869  77 LPSLQILYMMDEVDEPDLTLKAIGHQWYWSYEYTDFKDLSFDSYMTPSTELPMGYFRLLEVDHRVIIPMESPIRMIITAD 156
Cdd:MTH00038   78 LPSLQLLYLMDEVNNPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSA 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2554488869 157 DVLHSWAVPTLGVKTDAIPGRLNQTSFITTRPGIFYGQCSEICGANHSFMPIVVESIPLTHFETWSS 223
Cdd:MTH00038  158 DVLHSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVS 224
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-221 2.06e-113

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 323.59  E-value: 2.06e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554488869   1 MANHSQLGFQDASSPIMEELIEFHDHALMVALTICSLVLYLLTLMLMEKLSSNT-VDAQEVELIWTILPAIVLILLALPS 79
Cdd:MTH00139    1 MAYWGQLGFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSlLESQEVETIWTVLPAFILLFLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554488869  80 LQILYMMDEVDEPDLTLKAIGHQWYWSYEYTDFKDLSFDSYMTPSTELPMGYFRLLEVDHRVIIPMESPIRMIITADDVL 159
Cdd:MTH00139   81 LRLLYLMDEVSDPYLTFKAVGHQWYWSYEYSDFKNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2554488869 160 HSWAVPTLGVKTDAIPGRLNQTSFITTRPGIFYGQCSEICGANHSFMPIVVESIPLTHFETW 221
Cdd:MTH00139  161 HSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEW 222
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-223 5.60e-109

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 312.56  E-value: 5.60e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554488869   1 MANHSQLGFQDASSPIMEELIEFHDHALMVALTICSLVLYLLTLMLMEKLSSNTV-DAQEVELIWTILPAIVLILLALPS 79
Cdd:MTH00008    1 MPHWGQLMFQDAASPVMLQLISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYIlEAQQIETIWTILPALILLFLAFPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554488869  80 LQILYMMDEVDEPDLTLKAIGHQWYWSYEYTDFKDLSFDSYMTPSTELPMGYFRLLEVDHRVIIPMESPIRMIITADDVL 159
Cdd:MTH00008   81 LRLLYLMDEVSNPSITLKTIGHQWYWSYEYSDFSNLEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2554488869 160 HSWAVPTLGVKTDAIPGRLNQTSFITTRPGIFYGQCSEICGANHSFMPIVVESIPLTHFETWSS 223
Cdd:MTH00008  161 HSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKWVS 224
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 6-227 1.58e-97

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 283.95  E-value: 1.58e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554488869   6 QLGFQDASSPIMEELIEFHDHALMVALTICSLVLYLLTLMLMEK-LSSNTVDAQEVELIWTILPAIVLILLALPSLQILY 84
Cdd:MTH00023   15 QLGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKfYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKLLY 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554488869  85 MMDEVDEPDLTLKAIGHQWYWSYEYTDFKD--LSFDSYMTPSTELPMGYFRLLEVDHRVIIPMESPIRMIITADDVLHSW 162
Cdd:MTH00023   95 LMDEVVSPALTIKAIGHQWYWSYEYSDYEGetLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSF 174

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2554488869 163 AVPTLGVKTDAIPGRLNQTSFITTRPGIFYGQCSEICGANHSFMPIVVESIPLTHFETWSSLLMS 227
Cdd:MTH00023  175 AVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWLLSLSN 239
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 6-221 1.84e-93

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 273.58  E-value: 1.84e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554488869   6 QLGFQDASSPIMEELIEFHDHALMVALTICSLVLYLLTLMLMEKLSSNTV-DAQEVELIWTILPAIVLILLALPSLQILY 84
Cdd:MTH00051    8 QLGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLfEGTLIEIIWTLIPAAILIFIAFPSLKLLY 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554488869  85 MMDEVDEPDLTLKAIGHQWYWSYEYTDF--KDLSFDSYMTPSTELPMGYFRLLEVDHRVIIPMESPIRMIITADDVLHSW 162
Cdd:MTH00051   88 LMDEVIDPALTIKAIGHQWYWSYEYSDYgtDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSF 167

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2554488869 163 AVPTLGVKTDAIPGRLNQTSFITTRPGIFYGQCSEICGANHSFMPIVVESIPLTHFETW 221
Cdd:MTH00051  168 AVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINW 226
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 92-221 5.42e-92

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: 265.59  E-value: 5.42e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554488869  92 PDLTLKAIGHQWYWSYEYTDFKDLSFDSYMTPSTELPMGYFRLLEVDHRVIIPMESPIRMIITADDVLHSWAVPTLGVKT 171
Cdd:cd13912     1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2554488869 172 DAIPGRLNQTSFITTRPGIFYGQCSEICGANHSFMPIVVESIPLTHFETW 221
Cdd:cd13912    81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
94-213 1.05e-83

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 244.63  E-value: 1.05e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554488869  94 LTLKAIGHQWYWSYEYTDFKDLSFDSYMTPSTELPMGYFRLLEVDHRVIIPMESPIRMIITADDVLHSWAVPTLGVKTDA 173
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2554488869 174 IPGRLNQTSFITTRPGIFYGQCSEICGANHSFMPIVVESI 213
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 6-221 7.28e-81

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 242.62  E-value: 7.28e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554488869   6 QLGFQDASSPIMEELIEFHDHALMVALTICSLVLYLLTLMLM----EKLSSNTVDAQEVELIWTILPAIVLILLALPSLQ 81
Cdd:MTH00027   34 QLGFQDAGSPVMEEIIMLHDQILFILTIIVGVVLWLIIRILLgnnyYSYYWNKLDGSLIEVIWTLIPAFILILIAFPSLR 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554488869  82 ILYMMDE-VDEPDLTLKAIGHQWYWSYEYTDF--KDLSFDSYMTPSTELPMGYFRLLEVDHRVIIPMESPIRMIITADDV 158
Cdd:MTH00027  114 LLYIMDEcGFSANITIKVTGHQWYWSYSYEDYgeKNIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAADV 193

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2554488869 159 LHSWAVPTLGVKTDAIPGRLNQTSFITTRPGIFYGQCSEICGANHSFMPIVVESIPLTHFETW 221
Cdd:MTH00027  194 LHSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYIDW 256
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 49-226 8.18e-71

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 215.64  E-value: 8.18e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554488869  49 KLSSNTVDAQEVELIWTILPAIVLILLALPSLQILYMMDEVD-EPDLTLKAIGHQWYWSYEYTDFKDLSFDSYMTPSTEL 127
Cdd:MTH00080   52 YFKSKKIEYQFGELLCSVFPVLILLMQMVPSLSLLYYYGLMNlDSNLTVKVTGHQWYWSYEFSDIPGLEFDSYMKSLDQL 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554488869 128 PMGYFRLLEVDHRVIIPMESPIRMIITADDVLHSWAVPTLGVKTDAIPGRLNQTSFITTRPGIFYGQCSEICGANHSFMP 207
Cdd:MTH00080  132 RLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDAMSGILSTLCYSFPMPGVFYGQCSEICGANHSFMP 211

                         170
                  ....*....|....*....
gi 2554488869 208 IVVESIPLTHFETWSSLLM 226
Cdd:MTH00080  212 IAVEVTLLDNFKEWCKLLL 230
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
60-221 6.93e-54

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 172.71  E-value: 6.93e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554488869  60 VELIWTILPAIVLILLALPSLQILYMMDEVDEPDLTLKAIGHQWYWSYEYTDFKDLsfdsymtpstelpmgyfrlleVDH 139
Cdd:COG1622    79 LEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIA---------------------TVN 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554488869 140 RVIIPMESPIRMIITADDVLHSWAVPTLGVKTDAIPGRLNQTSFITTRPGIFYGQCSEICGANHSFMPIVVESIPLTHFE 219
Cdd:COG1622   138 ELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFD 217


                  ..
gi 2554488869 220 TW 221
Cdd:COG1622   218 AW 219
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 56-213 1.64e-46

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 152.42  E-value: 1.64e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554488869  56 DAQEVELIWTILPA-IVLILLALPSLQILYmmDEVDEPDLTLKAIGHQWYWSYEYTDfkDLSFDSYMTP---STELPMgy 131
Cdd:MTH00047   45 ENQVLELLWTVVPTlLVLVLCFLNLNFITS--DLDCFSSETIKVIGHQWYWSYEYSF--GGSYDSFMTDdifGVDKPL-- 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554488869 132 frllevdhRVIIPMesPIRMIITADDVLHSWAVPTLGVKTDAIPGRLNQTSFITTRPGIFYGQCSEICGANHSFMPIVVE 211
Cdd:MTH00047  119 --------RLVYGV--PYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCPDRHGVFVGYCSELCGVGHSYMPIVIE 188


                  ..
gi 2554488869 212 SI 213
Cdd:MTH00047  189 VV 190
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 12-221 5.20e-42

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: 141.36  E-value: 5.20e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554488869  12 ASSPIMEELIEFHDHALMVALTICSLVLYLLTLMLM-------EKLSSNTVDAQEVELIWTILPA-IVLILLALPSLQIL 83
Cdd:TIGR02866   1 PGGEIAQQIAFLFLFVLAVSTLISLLVAALLAYVVWkfrrkgdEEKPSQIHGNRRLEYVWTVIPLiIVVGLFAATAKGLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554488869  84 YMMDEVDEPDLTLKAIGHQWYWSYEYtdfkdlsfdsymtpstelPMGYFRlleVDHRVIIPMESPIRMIITADDVLHSWA 163
Cdd:TIGR02866  81 YLERPIPKDALKVKVTGYQWWWDFEY------------------PESGFT---TVNELVLPAGTPVELQVTSKDVIHSFW 139

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2554488869 164 VPTLGVKTDAIPGRLNQTSFITTRPGIFYGQCSEICGANHSFMPIVVESIPLTHFETW 221
Cdd:TIGR02866 140 VPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAY 197
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 116-213 1.23e-37

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 128.78  E-value: 1.23e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554488869 116 SFDSYMTPSTELPMGYFRLLEVDHRVIIPMESPIRMIITADDVLHSWAVPTLGVKTDAIPGRLNQTSFITTRPGIFYGQC 195
Cdd:PTZ00047   50 SFQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQC 129

                          90
                  ....*....|....*...
gi 2554488869 196 SEICGANHSFMPIVVESI 213
Cdd:PTZ00047  130 SEMCGTLHGFMPIVVEAV 147
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 94-211 1.02e-30

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: 108.92  E-value: 1.02e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554488869  94 LTLKAIGHQWYWSYEYTDfkdlsfdsymtpstelpmgyfrlLEVDHRVIIPMESPIRMIITADDVLHSWAVPTLGVKTDA 173
Cdd:cd13842     1 LTVYVTGVQWSWTFIYPN-----------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDA 57

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2554488869 174 IPGRLNQTSFITTRPGIFYGQCSEICGANHSFMPIVVE 211
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), ...
 93-206 2.42e-28

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: 103.08  E-value: 2.42e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554488869  93 DLTLKAIGHQWYWSYEYTDFKDLSFdsymTPSTELpmgyfrllevdhrvIIPMESPIRMIITADDVLHSWAVPTLGVKTD 172
Cdd:cd04213     1 ALTIEVTGHQWWWEFRYPDEPGRGI----VTANEL--------------HIPVGRPVRLRLTSADVIHSFWVPSLAGKMD 62

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2554488869 173 AIPGRLNQTSFITTRPGIFYGQCSEICGANHSFM 206
Cdd:cd04213    63 MIPGRTNRLWLQADEPGVYRGQCAEFCGASHALM 96
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 70-221 8.70e-24

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


Pssm-ID: 259985 [Multi-domain]  Cd Length: 139  Bit Score: 92.52  E-value: 8.70e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554488869  70 IVLILLALPSLQILYMMD---EVDEPDLTLKAIGHQWYWSYEYTDfkdlsfdSYMTPSTelpmgyfrllevdhrVIIPME 146
Cdd:cd13918     6 IVISLIVWTYGMLLYVEDppdEADEDALEVEVEGFQFGWQFEYPN-------GVTTGNT---------------LRVPAD 63

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2554488869 147 SPIRMIITADDVLHSWAVPTLGVKTDAIPGRLNQTSFITTRPGIFYGQCSEICGANHSFMPIVVESIPLTHFETW 221
Cdd:cd13918    64 TPIALRVTSTDVFHTFGIPELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEFEAW 138
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 93-211 4.33e-23

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: 89.62  E-value: 4.33e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554488869  93 DLTLKAIGHQWYWSYEY--TDFKDLSFDSYMTPSTELPMGyfrllevdhrviipmeSPIRMIITADDVLHSWAVPTLGVK 170
Cdd:cd13919     1 ALVVEVTAQQWAWTFRYpgGDGKLGTDDDVTSPELHLPVG----------------RPVLFNLRSKDVIHSFWVPEFRVK 64

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2554488869 171 TDAIPGRLNQTSFITTRPGIFYGQCSEICGANHSFM--PIVVE 211
Cdd:cd13919    65 QDAVPGRTTRLWFTPTREGEYEVRCAELCGLGHYRMraTVKVV 107
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-82 5.83e-22

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: 86.23  E-value: 5.83e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554488869   1 MANHSQLGFQDASSPIMEELIEFHDHALMVALTICSLVLYLLTLMLMEKLSS-------NTVDAQEVELIWTILPAIVLI 73
Cdd:pfam02790   1 MPTPWGLGFQDAASPLMEGLLELHDYIMFILTLILILVLYILVTCLIRFNRRknpitarYTTHGQTIEIIWTIIPAVILI 80


                  ....*....
gi 2554488869  74 LLALPSLQI 82
Cdd:pfam02790  81 LIALPSFKL 89
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 93-210 1.12e-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: 259982 [Multi-domain]  Cd Length: 98  Bit Score: 83.06  E-value: 1.12e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554488869  93 DLTLKAIGHQWYWSYEYTDFKdlsfdsymTPSTELpmgyfrllevdhrvIIPMESPIRMIITADDVLHSWAVPTLGVKTD 172
Cdd:cd13915     1 ALEIQVTGRQWMWEFTYPNGK--------REINEL--------------HVPVGKPVRLILTSKDVIHSFYVPAFRIKQD 58

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2554488869 173 AIPGRLNQTSFITTRPGIFYGQCSEICGANHSFMPIVV 210
Cdd:cd13915    59 VVPGRYTYLWFEATKPGEYDLFCTEYCGTGHSGMIGKV 96
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-221 1.65e-18

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


Pssm-ID: 259981 [Multi-domain]  Cd Length: 108  Bit Score: 77.45  E-value: 1.65e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554488869  95 TLKAIGHQWYWSYEYTDfkdlsfdSYMTPSTELpmgyfrllevdhrvIIPMESPIRMIITADDVLHSWAVPTLGVKTDAI 174
Cdd:cd13914     2 EIEVEAYQWGWEFSYPE-------ANVTTSEQL--------------VIPADRPVYFRITSRDVIHAFHVPELGLKQDAF 60

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2554488869 175 PGRLNQTSFITTRPGIFYGQCSEICGANHSFMPIVVESIPLTHFETW 221
Cdd:cd13914    61 PGQYNTIKTEATEEGEYQLYCAEYCGAGHSQMLSTVTVVSQDEYQQW 107
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 143-211 4.62e-08

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: 49.49  E-value: 4.62e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2554488869 143 IPMESPIRMIITADDVLHSWAVPTLGVKTDAIPGRLNQTSFITTRPGIFYGQCSEICGANHSFM--PIVVE 211
Cdd:cd13913    29 VPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNMygKIIVE 99
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-206 1.96e-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: 41.98  E-value: 1.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554488869  95 TLKAIGHQWYWSyeytdfkdlsfdsyMTPSTelpmgyfrllevdhrviIPMESPIRMIITADDVLHSWAV----PTLGVK 170
Cdd:cd13916     2 VVAVTGHQWYWE--------------LSRTE-----------------IPAGKPVEFRVTSADVNHGFGIydpdMRLLAQ 50

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2554488869 171 TDAIPGRLNQTSFITTRPGIFYGQCSEICGANHSFM 206
Cdd:cd13916    51 TQAMPGYTNVLRYTFDKPGTYTILCLEYCGLAHHVM 86
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 143-206 1.05e-04

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: 40.22  E-value: 1.05e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2554488869 143 IPMESPIRMIITADDVLHSWAVPTLGVKTDAIPGRLNQTSFITTRPGIFYGQCSEICGANHSFM 206
Cdd:cd04212    29 IPVGRPVNFRLTSDSVMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGTYQGLSANYSGEGFSDM 92
N2OR_C cd04223
The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase ...
 149-206 3.69e-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: 38.37  E-value: 3.69e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2554488869 149 IRMIIT----ADDVLHSWAVPTLGVKTDAIPGRLNQTSFITTRPGIFYGQCSEICGANHSFM 206
Cdd:cd04223    26 VTVHLTnleqDEDITHGFAIPGYNVNLSLEPGETATVTFVADKPGVYPYYCTEFCSALHLEM 87
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 132-211 2.83e-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: 36.44  E-value: 2.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2554488869 132 FRLLEVDHRVIIPMESPIRMIIT-ADDVLHSWAVPTLGVKTDAI---------------PGRLNQTSFITTRPGIFYGQC 195
Cdd:cd00920    16 GVLLFGPPVLVVPVGDTVRVQFVnKLGENHSVTIAGFGVPVVAMagganpglvntlvigPGESAEVTFTTDQAGVYWFYC 95

                          90
                  ....*....|....*.
gi 2554488869 196 SEICGaNHSFMPIVVE 211
Cdd:cd00920    96 TIPGH-NHAGMVGTIN 110
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH