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Conserved domains on  [gi|1747250639|ref|YP_009689211|]
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cytochrome c oxidase subunit II (mitochondrion) [Geoemyda spengleri]

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

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List of domain hits

 Name Accession Description Interval E-value
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-227 1.70e-173

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 475.56  E-value: 1.70e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747250639   1 MAHPLQLGFQDAMSPIMEELHHFHDHTLMIVFLISTLVLYIITMMMTTKLTYTNTMNAQEVEMIWTILPAIVLITIALPS 80
Cdd:MTH00117    1 MANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747250639  81 LRVLYLMDEINDPYLTIKAVGHQWYWTYEYTDYKDLEFDSYMIPTQNLPDGHFRLLEVDHRVVMPMESPIRMLISAEDVL 160
Cdd:MTH00117   81 LRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1747250639 161 HSWAVPSLGVKADAVPGRLNQSTFIVMHPGVFYGQCSEICGANHSFMPIVVESVPLKHFEDWSSLVL 227
Cdd:MTH00117  161 HSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSLLS 227
 
Name Accession Description Interval E-value
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-227 1.70e-173

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 475.56  E-value: 1.70e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747250639   1 MAHPLQLGFQDAMSPIMEELHHFHDHTLMIVFLISTLVLYIITMMMTTKLTYTNTMNAQEVEMIWTILPAIVLITIALPS 80
Cdd:MTH00117    1 MANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747250639  81 LRVLYLMDEINDPYLTIKAVGHQWYWTYEYTDYKDLEFDSYMIPTQNLPDGHFRLLEVDHRVVMPMESPIRMLISAEDVL 160
Cdd:MTH00117   81 LRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1747250639 161 HSWAVPSLGVKADAVPGRLNQSTFIVMHPGVFYGQCSEICGANHSFMPIVVESVPLKHFEDWSSLVL 227
Cdd:MTH00117  161 HSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSLLS 227
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 93-222 1.72e-90

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: 262.12  E-value: 1.72e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747250639  93 PYLTIKAVGHQWYWTYEYTDYKDLEFDSYMIPTQNLPDGHFRLLEVDHRVVMPMESPIRMLISAEDVLHSWAVPSLGVKA 172
Cdd:cd13912     1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1747250639 173 DAVPGRLNQSTFIVMHPGVFYGQCSEICGANHSFMPIVVESVPLKHFEDW 222
Cdd:cd13912    81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-214 5.64e-83

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 242.70  E-value: 5.64e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747250639  95 LTIKAVGHQWYWTYEYTDYKDLEFDSYMIPTQNLPDGHFRLLEVDHRVVMPMESPIRMLISAEDVLHSWAVPSLGVKADA 174
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1747250639 175 VPGRLNQSTFIVMHPGVFYGQCSEICGANHSFMPIVVESV 214
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
6-222 2.66e-53

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 171.16  E-value: 2.66e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747250639   6 QLGFQDAMSPIMEELHHfhdhtLMIVFLISTLVLYIITMMMT----------------TKLTYTNTmnaqeVEMIWTILP 69
Cdd:COG1622    18 QLSLPDPAGPIAEEIDD-----LFWVSLIIMLVIFVLVFGLLlyfairyrrrkgdadpAQFHHNTK-----LEIVWTVIP 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747250639  70 AIVLITIALPSLRVLYLMDEINDPYLTIKAVGHQWYWTYEYTDYKDLefdsymiptqnlpdghfrlleVDHRVVMPMESP 149
Cdd:COG1622    88 IIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIA---------------------TVNELVLPVGRP 146

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1747250639 150 IRMLISAEDVLHSWAVPSLGVKADAVPGRLNQSTFIVMHPGVFYGQCSEICGANHSFMPIVVESVPLKHFEDW 222
Cdd:COG1622   147 VRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAW 219
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 61-222 1.30e-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: 132.50  E-value: 1.30e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747250639  61 VEMIWTILPA-IVLITIALPSLRVLYLMDEINDPYLTIKAVGHQWYWTYEYtdykdlefdsymiptqnlPDGHFRlleVD 139
Cdd:TIGR02866  56 LEYVWTVIPLiIVVGLFAATAKGLLYLERPIPKDALKVKVTGYQWWWDFEY------------------PESGFT---TV 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747250639 140 HRVVMPMESPIRMLISAEDVLHSWAVPSLGVKADAVPGRLNQSTFIVMHPGVFYGQCSEICGANHSFMPIVVESVPLKHF 219
Cdd:TIGR02866 115 NELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEF 194


                  ...
gi 1747250639 220 EDW 222
Cdd:TIGR02866 195 DAY 197
 
Name Accession Description Interval E-value
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-227 1.70e-173

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 475.56  E-value: 1.70e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747250639   1 MAHPLQLGFQDAMSPIMEELHHFHDHTLMIVFLISTLVLYIITMMMTTKLTYTNTMNAQEVEMIWTILPAIVLITIALPS 80
Cdd:MTH00117    1 MANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747250639  81 LRVLYLMDEINDPYLTIKAVGHQWYWTYEYTDYKDLEFDSYMIPTQNLPDGHFRLLEVDHRVVMPMESPIRMLISAEDVL 160
Cdd:MTH00117   81 LRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1747250639 161 HSWAVPSLGVKADAVPGRLNQSTFIVMHPGVFYGQCSEICGANHSFMPIVVESVPLKHFEDWSSLVL 227
Cdd:MTH00117  161 HSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSLLS 227
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-227 4.99e-155

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 428.75  E-value: 4.99e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747250639   1 MAHPLQLGFQDAMSPIMEELHHFHDHTLMIVFLISTLVLYIITMMMTTKLTYTNTMNAQEVEMIWTILPAIVLITIALPS 80
Cdd:MTH00098    1 MAYPFQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747250639  81 LRVLYLMDEINDPYLTIKAVGHQWYWTYEYTDYKDLEFDSYMIPTQNLPDGHFRLLEVDHRVVMPMESPIRMLISAEDVL 160
Cdd:MTH00098   81 LRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1747250639 161 HSWAVPSLGVKADAVPGRLNQSTFIVMHPGVFYGQCSEICGANHSFMPIVVESVPLKHFEDWSSLVL 227
Cdd:MTH00098  161 HSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKWSASML 227
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 1-227 3.49e-153

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 424.51  E-value: 3.49e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747250639   1 MAHPLQLGFQDAMSPIMEELHHFHDHTLMIVFLISTLVLYIITMMMTTKLTYTNTMNAQEVEMIWTILPAIVLITIALPS 80
Cdd:MTH00129    1 MAHPSQLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747250639  81 LRVLYLMDEINDPYLTIKAVGHQWYWTYEYTDYKDLEFDSYMIPTQNLPDGHFRLLEVDHRVVMPMESPIRMLISAEDVL 160
Cdd:MTH00129   81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1747250639 161 HSWAVPSLGVKADAVPGRLNQSTFIVMHPGVFYGQCSEICGANHSFMPIVVESVPLKHFEDWSSLVL 227
Cdd:MTH00129  161 HSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLML 227
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 1-227 4.05e-149

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 414.18  E-value: 4.05e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747250639   1 MAHPLQLGFQDAMSPIMEELHHFHDHTLMIVFLISTLVLYIITMMMTTKLTYTNTMNAQEVEMIWTILPAIVLITIALPS 80
Cdd:MTH00076    1 MAHPSQLGFQDAASPIMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747250639  81 LRVLYLMDEINDPYLTIKAVGHQWYWTYEYTDYKDLEFDSYMIPTQNLPDGHFRLLEVDHRVVMPMESPIRMLISAEDVL 160
Cdd:MTH00076   81 LRILYLMDEINDPHLTVKAIGHQWYWSYEYTDYEDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1747250639 161 HSWAVPSLGVKADAVPGRLNQSTFIVMHPGVFYGQCSEICGANHSFMPIVVESVPLKHFEDWSSLVL 227
Cdd:MTH00076  161 HSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLNWSSSML 227
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 1-227 6.01e-142

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 396.18  E-value: 6.01e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747250639   1 MAHPLQLGFQDAMSPIMEELHHFHDHTLMIVFLISTLVLYIITMMMTTKLTYTNTMNAQEVEMIWTILPAIVLITIALPS 80
Cdd:MTH00185    1 MAHPSQLGLQDAASPVMEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747250639  81 LRVLYLMDEINDPYLTIKAVGHQWYWTYEYTDYKDLEFDSYMIPTQNLPDGHFRLLEVDHRVVMPMESPIRMLISAEDVL 160
Cdd:MTH00185   81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1747250639 161 HSWAVPSLGVKADAVPGRLNQSTFIVMHPGVFYGQCSEICGANHSFMPIVVESVPLKHFEDWSSLVL 227
Cdd:MTH00185  161 HSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLML 227
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-224 3.63e-134

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 376.09  E-value: 3.63e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747250639   1 MAHPLQLGFQDAMSPIMEELHHFHDHTLMIVFLISTLVLYIITMMMTTKLTYTNTMNAQEVEMIWTILPAIVLITIALPS 80
Cdd:MTH00154    1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747250639  81 LRVLYLMDEINDPYLTIKAVGHQWYWTYEYTDYKDLEFDSYMIPTQNLPDGHFRLLEVDHRVVMPMESPIRMLISAEDVL 160
Cdd:MTH00154   81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1747250639 161 HSWAVPSLGVKADAVPGRLNQSTFIVMHPGVFYGQCSEICGANHSFMPIVVESVPLKHFEDWSS 224
Cdd:MTH00154  161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIK 224
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-224 1.82e-132

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 371.62  E-value: 1.82e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747250639   1 MAHPLQLGFQDAMSPIMEELHHFHDHTLMIVFLISTLVLYIITMMMTTKLTYTNTMNAQEVEMIWTILPAIVLITIALPS 80
Cdd:MTH00168    1 MATYSQLGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747250639  81 LRVLYLMDEINDPYLTIKAVGHQWYWTYEYTDYKDLEFDSYMIPTQNLPDGHFRLLEVDHRVVMPMESPIRMLISAEDVL 160
Cdd:MTH00168   81 LRLLYLMDEIDKPDLTIKAVGHQWYWSYEYTDYNDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1747250639 161 HSWAVPSLGVKADAVPGRLNQSTFIVMHPGVFYGQCSEICGANHSFMPIVVESVPLKHFEDWSS 224
Cdd:MTH00168  161 HSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENWVD 224
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-224 6.06e-128

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 360.56  E-value: 6.06e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747250639   1 MAHPLQLGFQDAMSPIMEELHHFHDHTLMIVFLISTLVLYIITMMMTTKLTYTNTMNAQEVEMIWTILPAIVLITIALPS 80
Cdd:MTH00038    1 MATWLQLGLQDASSPLMEELIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747250639  81 LRVLYLMDEINDPYLTIKAVGHQWYWTYEYTDYKDLEFDSYMIPTQNLPDGHFRLLEVDHRVVMPMESPIRMLISAEDVL 160
Cdd:MTH00038   81 LQLLYLMDEVNNPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1747250639 161 HSWAVPSLGVKADAVPGRLNQSTFIVMHPGVFYGQCSEICGANHSFMPIVVESVPLKHFEDWSS 224
Cdd:MTH00038  161 HSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVS 224
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 6-222 4.54e-123

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 348.08  E-value: 4.54e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747250639   6 QLGFQDAMSPIMEELHHFHDHTLMIVFLISTLVLYIITMMMTTKLTYTNTMNAQEVEMIWTILPAIVLITIALPSLRVLY 85
Cdd:MTH00140    6 QLGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPSLRLLY 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747250639  86 LMDEINDPYLTIKAVGHQWYWTYEYTDYKDLEFDSYMIPTQNLPDGHFRLLEVDHRVVMPMESPIRMLISAEDVLHSWAV 165
Cdd:MTH00140   86 LLDETNNPLLTVKAIGHQWYWSYEYSDFSVIEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVIHSWTV 165

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1747250639 166 PSLGVKADAVPGRLNQSTFIVMHPGVFYGQCSEICGANHSFMPIVVESVPLKHFEDW 222
Cdd:MTH00140  166 PSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKW 222
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-222 4.74e-122

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 345.55  E-value: 4.74e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747250639   1 MAHPLQLGFQDAMSPIMEELHHFHDHTLMIVFLISTLVLYIITMMMTTKLTYTNTMNAQEVEMIWTILPAIVLITIALPS 80
Cdd:MTH00139    1 MAYWGQLGFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747250639  81 LRVLYLMDEINDPYLTIKAVGHQWYWTYEYTDYKDLEFDSYMIPTQNLPDGHFRLLEVDHRVVMPMESPIRMLISAEDVL 160
Cdd:MTH00139   81 LRLLYLMDEVSDPYLTFKAVGHQWYWSYEYSDFKNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1747250639 161 HSWAVPSLGVKADAVPGRLNQSTFIVMHPGVFYGQCSEICGANHSFMPIVVESVPLKHFEDW 222
Cdd:MTH00139  161 HSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEW 222
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-224 2.38e-110

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 316.03  E-value: 2.38e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747250639   1 MAHPLQLGFQDAMSPIMEELHHFHDHTLMIVFLISTLVLYIITMMMTTKLTYTNTMNAQEVEMIWTILPAIVLITIALPS 80
Cdd:MTH00008    1 MPHWGQLMFQDAASPVMLQLISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747250639  81 LRVLYLMDEINDPYLTIKAVGHQWYWTYEYTDYKDLEFDSYMIPTQNLPDGHFRLLEVDHRVVMPMESPIRMLISAEDVL 160
Cdd:MTH00008   81 LRLLYLMDEVSNPSITLKTIGHQWYWSYEYSDFSNLEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1747250639 161 HSWAVPSLGVKADAVPGRLNQSTFIVMHPGVFYGQCSEICGANHSFMPIVVESVPLKHFEDWSS 224
Cdd:MTH00008  161 HSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKWVS 224
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 2-222 3.94e-105

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 302.86  E-value: 3.94e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747250639   2 AHPLQLGFQDAMSPIMEELHHFHDHTLMIVFLISTLVLYIITMMMTTKLTYTNTMNAQEVEMIWTILPAIVLITIALPSL 81
Cdd:MTH00051    4 PEPWQLGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747250639  82 RVLYLMDEINDPYLTIKAVGHQWYWTYEYTDY--KDLEFDSYMIPTQNLPDGHFRLLEVDHRVVMPMESPIRMLISAEDV 159
Cdd:MTH00051   84 KLLYLMDEVIDPALTIKAIGHQWYWSYEYSDYgtDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADV 163

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1747250639 160 LHSWAVPSLGVKADAVPGRLNQSTFIVMHPGVFYGQCSEICGANHSFMPIVVESVPLKHFEDW 222
Cdd:MTH00051  164 LHSFAVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINW 226
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 2-224 3.74e-104

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 300.90  E-value: 3.74e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747250639   2 AHPLQLGFQDAMSPIMEELHHFHDHTLMIVFLISTLVLYIITMMMTTKLTYTNTMNAQEVEMIWTILPAIVLITIALPSL 81
Cdd:MTH00023   11 PEPWQLGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSL 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747250639  82 RVLYLMDEINDPYLTIKAVGHQWYWTYEYTDYKD--LEFDSYMIPTQNLPDGHFRLLEVDHRVVMPMESPIRMLISAEDV 159
Cdd:MTH00023   91 KLLYLMDEVVSPALTIKAIGHQWYWSYEYSDYEGetLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADV 170

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1747250639 160 LHSWAVPSLGVKADAVPGRLNQSTFIVMHPGVFYGQCSEICGANHSFMPIVVESVPLKHFEDWSS 224
Cdd:MTH00023  171 LHSFAVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWLL 235
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 93-222 1.72e-90

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: 262.12  E-value: 1.72e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747250639  93 PYLTIKAVGHQWYWTYEYTDYKDLEFDSYMIPTQNLPDGHFRLLEVDHRVVMPMESPIRMLISAEDVLHSWAVPSLGVKA 172
Cdd:cd13912     1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1747250639 173 DAVPGRLNQSTFIVMHPGVFYGQCSEICGANHSFMPIVVESVPLKHFEDW 222
Cdd:cd13912    81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 4-222 1.41e-85

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 254.56  E-value: 1.41e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747250639   4 PLQLGFQDAMSPIMEELHHFHDHTLMIVFLISTLVLYIITMMMTTKLTYT---NTMNAQEVEMIWTILPAIVLITIALPS 80
Cdd:MTH00027   32 PWQLGFQDAGSPVMEEIIMLHDQILFILTIIVGVVLWLIIRILLGNNYYSyywNKLDGSLIEVIWTLIPAFILILIAFPS 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747250639  81 LRVLYLMDE-INDPYLTIKAVGHQWYWTYEYTDY--KDLEFDSYMIPTQNLPDGHFRLLEVDHRVVMPMESPIRMLISAE 157
Cdd:MTH00027  112 LRLLYIMDEcGFSANITIKVTGHQWYWSYSYEDYgeKNIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAA 191

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1747250639 158 DVLHSWAVPSLGVKADAVPGRLNQSTFIVMHPGVFYGQCSEICGANHSFMPIVVESVPLKHFEDW 222
Cdd:MTH00027  192 DVLHSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYIDW 256
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-214 5.64e-83

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 242.70  E-value: 5.64e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747250639  95 LTIKAVGHQWYWTYEYTDYKDLEFDSYMIPTQNLPDGHFRLLEVDHRVVMPMESPIRMLISAEDVLHSWAVPSLGVKADA 174
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1747250639 175 VPGRLNQSTFIVMHPGVFYGQCSEICGANHSFMPIVVESV 214
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 7-228 6.50e-74

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 223.73  E-value: 6.50e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747250639   7 LGFQDAMSPI-MEELHHFHDHTLMIVFLISTLVLYIITMMMTTKLTYTNTMNAQEVEMIWTILPAIVLITIALPSLRVLY 85
Cdd:MTH00080    8 LNFSNSLFSSyMDWFHNFNCSLLFGEFVLAFVVFLFLYLISNNFYFKSKKIEYQFGELLCSVFPVLILLMQMVPSLSLLY 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747250639  86 LMDEIN-DPYLTIKAVGHQWYWTYEYTDYKDLEFDSYMIPTQNLPDGHFRLLEVDHRVVMPMESPIRMLISAEDVLHSWA 164
Cdd:MTH00080   88 YYGLMNlDSNLTVKVTGHQWYWSYEFSDIPGLEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWA 167

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1747250639 165 VPSLGVKADAVPGRLNQSTFIVMHPGVFYGQCSEICGANHSFMPIVVESVPLKHFEDWSSLVLI 228
Cdd:MTH00080  168 LPSLSIKMDAMSGILSTLCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKEWCKLLLD 231
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
6-222 2.66e-53

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 171.16  E-value: 2.66e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747250639   6 QLGFQDAMSPIMEELHHfhdhtLMIVFLISTLVLYIITMMMT----------------TKLTYTNTmnaqeVEMIWTILP 69
Cdd:COG1622    18 QLSLPDPAGPIAEEIDD-----LFWVSLIIMLVIFVLVFGLLlyfairyrrrkgdadpAQFHHNTK-----LEIVWTVIP 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747250639  70 AIVLITIALPSLRVLYLMDEINDPYLTIKAVGHQWYWTYEYTDYKDLefdsymiptqnlpdghfrlleVDHRVVMPMESP 149
Cdd:COG1622    88 IIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIA---------------------TVNELVLPVGRP 146

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1747250639 150 IRMLISAEDVLHSWAVPSLGVKADAVPGRLNQSTFIVMHPGVFYGQCSEICGANHSFMPIVVESVPLKHFEDW 222
Cdd:COG1622   147 VRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAW 219
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 23-214 1.44e-42

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 142.40  E-value: 1.44e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747250639  23 FHDHTLMIVFLISTLVLYIITMMMTTKLTYTNTMN----AQEVEMIWTILPAivLITIALPSLRVLYLMDEIND-PYLTI 97
Cdd:MTH00047    7 YYDIVCYILALCVFIPCWVYIMLCWQVVSGNGSVNfgseNQVLELLWTVVPT--LLVLVLCFLNLNFITSDLDCfSSETI 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747250639  98 KAVGHQWYWTYEYTDykDLEFDSYMIPTQNLpdghfrlleVDHRVVMPMESPIRMLISAEDVLHSWAVPSLGVKADAVPG 177
Cdd:MTH00047   85 KVIGHQWYWSYEYSF--GGSYDSFMTDDIFG---------VDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPG 153

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1747250639 178 RLNQSTFIVMHPGVFYGQCSEICGANHSFMPIVVESV 214
Cdd:MTH00047  154 RINHLFFCPDRHGVFVGYCSELCGVGHSYMPIVIEVV 190
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 118-214 1.58e-39

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 133.79  E-value: 1.58e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747250639 118 FDSYMIPTQNLPDGHFRLLEVDHRVVMPMESPIRMLISAEDVLHSWAVPSLGVKADAVPGRLNQSTFIVMHPGVFYGQCS 197
Cdd:PTZ00047   51 FQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCS 130

                          90
                  ....*....|....*..
gi 1747250639 198 EICGANHSFMPIVVESV 214
Cdd:PTZ00047  131 EMCGTLHGFMPIVVEAV 147
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 61-222 1.30e-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: 132.50  E-value: 1.30e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747250639  61 VEMIWTILPA-IVLITIALPSLRVLYLMDEINDPYLTIKAVGHQWYWTYEYtdykdlefdsymiptqnlPDGHFRlleVD 139
Cdd:TIGR02866  56 LEYVWTVIPLiIVVGLFAATAKGLLYLERPIPKDALKVKVTGYQWWWDFEY------------------PESGFT---TV 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747250639 140 HRVVMPMESPIRMLISAEDVLHSWAVPSLGVKADAVPGRLNQSTFIVMHPGVFYGQCSEICGANHSFMPIVVESVPLKHF 219
Cdd:TIGR02866 115 NELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEF 194


                  ...
gi 1747250639 220 EDW 222
Cdd:TIGR02866 195 DAY 197
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 95-212 5.79e-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: 99.29  E-value: 5.79e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747250639  95 LTIKAVGHQWYWTYEYTDykdlefdsymiptqnlpdghfrlLEVDHRVVMPMESPIRMLISAEDVLHSWAVPSLGVKADA 174
Cdd:cd13842     1 LTVYVTGVQWSWTFIYPN-----------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDA 57

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1747250639 175 VPGRLNQSTFIVMHPGVFYGQCSEICGANHSFMPIVVE 212
Cdd:cd13842    58 VPGYTSELWFVADKPGTYTIICAEYCGLGHSYMLGKVE 95
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-83 3.16e-26

Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C oxidase contains two transmembrane alpha-helices.


Pssm-ID: 397083 [Multi-domain]  Cd Length: 89  Bit Score: 97.02  E-value: 3.16e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747250639   1 MAHPLQLGFQDAMSPIMEELHHFHDHTLMIVFLISTLVLYIITMMMTT------KLTYTNTMNAQEVEMIWTILPAIVLI 74
Cdd:pfam02790   1 MPTPWGLGFQDAASPLMEGLLELHDYIMFILTLILILVLYILVTCLIRfnrrknPITARYTTHGQTIEIIWTIIPAVILI 80


                  ....*....
gi 1747250639  75 TIALPSLRV 83
Cdd:pfam02790  81 LIALPSFKL 89
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 95-207 5.59e-25

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: 94.22  E-value: 5.59e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747250639  95 LTIKAVGHQWYWTYEYtdykdlefdsymiptqnlPDGHFRLLEVDHRVVMPMESPIRMLISAEDVLHSWAVPSLGVKADA 174
Cdd:cd04213     2 LTIEVTGHQWWWEFRY------------------PDEPGRGIVTANELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMDM 63

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1747250639 175 VPGRLNQSTFIVMHPGVFYGQCSEICGANHSFM 207
Cdd:cd04213    64 IPGRTNRLWLQADEPGVYRGQCAEFCGASHALM 96
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-211 2.82e-21

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


Pssm-ID: 259982 [Multi-domain]  Cd Length: 98  Bit Score: 84.60  E-value: 2.82e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747250639  95 LTIKAVGHQWYWTYEYtdykdlefdsymiptqnlPDGhfrlLEVDHRVVMPMESPIRMLISAEDVLHSWAVPSLGVKADA 174
Cdd:cd13915     2 LEIQVTGRQWMWEFTY------------------PNG----KREINELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQDV 59

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1747250639 175 VPGRLNQSTFIVMHPGVFYGQCSEICGANHSFMPIVV 211
Cdd:cd13915    60 VPGRYTYLWFEATKPGEYDLFCTEYCGTGHSGMIGKV 96
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 67-222 2.26e-20

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


Pssm-ID: 259985 [Multi-domain]  Cd Length: 139  Bit Score: 83.66  E-value: 2.26e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747250639  67 ILPAIVLIT-IALPSLRVLYLMD---EINDPYLTIKAVGHQWYWTYEYTDykDLEFDSYMiptqnlpdghfrllevdhrv 142
Cdd:cd13918     1 GLSAIIVISlIVWTYGMLLYVEDppdEADEDALEVEVEGFQFGWQFEYPN--GVTTGNTL-------------------- 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747250639 143 VMPMESPIRMLISAEDVLHSWAVPSLGVKADAVPGRLNQSTFIVMHPGVFYGQCSEICGANHSFMPIVVESVPLKHFEDW 222
Cdd:cd13918    59 RVPADTPIALRVTSTDVFHTFGIPELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEFEAW 138
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-212 4.53e-20

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


Pssm-ID: 259986 [Multi-domain]  Cd Length: 107  Bit Score: 81.53  E-value: 4.53e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747250639  95 LTIKAVGHQWYWTYEYtdykdlefdsymiptqnlPDGHFRLLEVDHRV----VMPMESPIRMLISAEDVLHSWAVPSLGV 170
Cdd:cd13919     2 LVVEVTAQQWAWTFRY------------------PGGDGKLGTDDDVTspelHLPVGRPVLFNLRSKDVIHSFWVPEFRV 63

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1747250639 171 KADAVPGRLNQSTFIVMHPGVFYGQCSEICGANHSFM--PIVVE 212
Cdd:cd13919    64 KQDAVPGRTTRLWFTPTREGEYEVRCAELCGLGHYRMraTVKVV 107
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 96-222 3.76e-19

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


Pssm-ID: 259981 [Multi-domain]  Cd Length: 108  Bit Score: 79.37  E-value: 3.76e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747250639  96 TIKAVGHQWYWTYEYTDYKDLEFDSYMIPTqnlpdghfrllevdhrvvmpmESPIRMLISAEDVLHSWAVPSLGVKADAV 175
Cdd:cd13914     2 EIEVEAYQWGWEFSYPEANVTTSEQLVIPA---------------------DRPVYFRITSRDVIHAFHVPELGLKQDAF 60

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1747250639 176 PGRLNQSTFIVMHPGVFYGQCSEICGANHSFMPIVVESVPLKHFEDW 222
Cdd:cd13914    61 PGQYNTIKTEATEEGEYQLYCAEYCGAGHSQMLSTVTVVSQDEYQQW 107
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 95-214 1.98e-06

The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase in the respiratory chains of aerobic bacteria, is a multi-chain transmembrane protein located in the cell membrane. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits in ubiquinol oxidase varies from two to five. Although subunit II of ubiquinol oxidase lacks the binuclear CuA site found in cytochrome c oxidases, the structure is conserved.


Pssm-ID: 259874 [Multi-domain]  Cd Length: 99  Bit Score: 44.85  E-value: 1.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747250639  95 LTIKAVGHQWYWTYEYTDYKdlefdsymIPTQNlpdghfrllevdhRVVMPMESPIRMLISAEDVLHSWAVPSLGVKADA 174
Cdd:cd04212     1 LEIQVVSLDWKWLFIYPEQG--------IATVN-------------ELVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYA 59

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1747250639 175 VPGRLNQSTFIVMHPGVFYGQCSEICGANHSFMPIVVESV 214
Cdd:cd04212    60 MAGMQTQLHLIADKPGTYQGLSANYSGEGFSDMKFKVLAV 99
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 142-212 1.47e-05

C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and some archaea, which catalyze the reduction of O2 and simultaneously pump protons across the membrane. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. The ba3 family contains oxidases that lack the conserved residues that form the D- and K-pathways in CcO and ubiquinol oxidase. Instead, they contain a potential alternative K-pathway. Additional proton channels have been proposed for this family of oxidases but none have been identified definitively.


Pssm-ID: 259980 [Multi-domain]  Cd Length: 99  Bit Score: 42.56  E-value: 1.47e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1747250639 142 VVMPMESPIRMLISAEDVLHSWAVPSLGVKADAVPGRLNQSTFIVMHPGVFYGQCSEICGANHSFM--PIVVE 212
Cdd:cd13913    27 IEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNMygKIIVE 99
N2OR_C cd04223
The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase ...
 156-207 3.30e-05

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: 41.45  E-value: 3.30e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1747250639 156 AEDVLHSWAVPSLGVKADAVPGRLNQSTFIVMHPGVFYGQCSEICGANHSFM 207
Cdd:cd04223    36 DEDITHGFAIPGYNVNLSLEPGETATVTFVADKPGVYPYYCTEFCSALHLEM 87
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 96-207 2.24e-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: 259983 [Multi-domain]  Cd Length: 93  Bit Score: 36.21  E-value: 2.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1747250639  96 TIKAVGHQWYWTYEytdykdlefdsymiptqnlpdghfrllevdhRVVMPMESPIRMLISAEDVLHSWAVPS----LGVK 171
Cdd:cd13916     2 VVAVTGHQWYWELS-------------------------------RTEIPAGKPVEFRVTSADVNHGFGIYDpdmrLLAQ 50

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1747250639 172 ADAVPGRLNQSTFIVMHPGVFYGQCSEICGANHSFM 207
Cdd:cd13916    51 TQAMPGYTNVLRYTFDKPGTYTILCLEYCGLAHHVM 86
 
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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