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Conserved domains on  [gi|540361532|gb|AGV08649|]
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cytochrome oxidase subunit II, partial (mitochondrion) [Sasima sp. OR131]

Protein Classification

cytochrome c oxidase subunit II( domain architecture ID 11475927)

cytochrome c oxidase subunit II, part of the functional core of the enzyme, transfers the electrons from cytochrome c via its binuclear copper A center to the bimetallic center of the catalytic subunit I

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-213 5.37e-147

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 408.06  E-value: 5.37e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361532   1 MATWSNLNLQNSASPLMEQLTFFHDHALLILIMITTLVAYIMTAIMFYSYTHRNLLEGQLIEVIWTVLPAVTLIFIALPS 80
Cdd:MTH00154   1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361532  81 LRLLYLLDESMDPSISIKTVGHQWYWSYEYSDFINPhEFDSYMIPYNEMNTNGFRLLDVDNRTVLPMHTQIRMMVSAADV 160
Cdd:MTH00154  81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNI-EFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADV 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 540361532 161 LHSWTVPALGVKVDATPGRLNQTNFFMNRPGLYYGQCSEICGANHSFMPIVIE 213
Cdd:MTH00154 160 IHSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIE 212
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-213 5.37e-147

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 408.06  E-value: 5.37e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361532   1 MATWSNLNLQNSASPLMEQLTFFHDHALLILIMITTLVAYIMTAIMFYSYTHRNLLEGQLIEVIWTVLPAVTLIFIALPS 80
Cdd:MTH00154   1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361532  81 LRLLYLLDESMDPSISIKTVGHQWYWSYEYSDFINPhEFDSYMIPYNEMNTNGFRLLDVDNRTVLPMHTQIRMMVSAADV 160
Cdd:MTH00154  81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNI-EFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADV 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 540361532 161 LHSWTVPALGVKVDATPGRLNQTNFFMNRPGLYYGQCSEICGANHSFMPIVIE 213
Cdd:MTH00154 160 IHSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIE 212
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 93-213 3.48e-83

C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal oxidase in the respiratory chains of eukaryotes and most bacteria, is a multi-chain transmembrane protein located in the inner membrane of mitochondria and the cell membrane of prokaryotes. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. Only subunits I and II are essential for function. Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunit II contains a copper-copper binuclear site called CuA, which is believed to be involved in electron transfer from cytochrome c to the binuclear center (active site) in subunit I.


Pssm-ID: 259979 [Multi-domain]  Cd Length: 130  Bit Score: 242.86  E-value: 3.48e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361532  93 PSISIKTVGHQWYWSYEYSDFiNPHEFDSYMIPYNEMNTNGFRLLDVDNRTVLPMHTQIRMMVSAADVLHSWTVPALGVK 172
Cdd:cd13912    1 PSLTIKAIGHQWYWSYEYSDF-NDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIK 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 540361532 173 VDATPGRLNQTNFFMNRPGLYYGQCSEICGANHSFMPIVIE 213
Cdd:cd13912   80 VDAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVE 120
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-213 2.80e-74

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 219.97  E-value: 2.80e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361532   95 ISIKTVGHQWYWSYEYSDFINPhEFDSYMIPYNEMNTNGFRLLDVDNRTVLPMHTQIRMMVSAADVLHSWTVPALGVKVD 174
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDL-EFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTD 79

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 540361532  175 ATPGRLNQTNFFMNRPGLYYGQCSEICGANHSFMPIVIE 213
Cdd:pfam00116  80 AVPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIE 118
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
6-213 1.68e-45

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 150.36  E-value: 1.68e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361532   6 NLNLQNSASPLMEQLTFFHDHALLILIMITTLVayimTAIMFYS--------------YTHRNLLegqlIEVIWTVLPAV 71
Cdd:COG1622   18 QLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLV----FGLLLYFairyrrrkgdadpaQFHHNTK----LEIVWTVIPII 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361532  72 TLIFIALPSLRLLYLLDESMDPSISIKTVGHQWYWSYEYSDfinphefdsymipYNEmntngfrllDVDNRTVLPMHTQI 151
Cdd:COG1622   90 IVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPD-------------QGI---------ATVNELVLPVGRPV 147

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 540361532 152 RMMVSAADVLHSWTVPALGVKVDATPGRLNQTNFFMNRPGLYYGQCSEICGANHSFMPIVIE 213
Cdd:COG1622  148 RFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVV 209
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 13-213 5.93e-37

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: 127.88  E-value: 5.93e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361532   13 ASPLMEQLTFFHdhalLILIMITTLVAYIMTAIMFY--------------SYTHrnllEGQLIEVIWTVLPAVTLIFIAL 78
Cdd:TIGR02866   2 GGEIAQQIAFLF----LFVLAVSTLISLLVAALLAYvvwkfrrkgdeekpSQIH----GNRRLEYVWTVIPLIIVVGLFA 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361532   79 PSLRLLYLLDESMDP-SISIKTVGHQWYWSYEYSDFinphefdsymipynemntnGFRlldVDNRTVLPMHTQIRMMVSA 157
Cdd:TIGR02866  74 ATAKGLLYLERPIPKdALKVKVTGYQWWWDFEYPES-------------------GFT---TVNELVLPAGTPVELQVTS 131

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 540361532  158 ADVLHSWTVPALGVKVDATPGRLNQTNFFMNRPGLYYGQCSEICGANHSFMPIVIE 213
Cdd:TIGR02866 132 KDVIHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVV 187
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-213 5.37e-147

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 408.06  E-value: 5.37e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361532   1 MATWSNLNLQNSASPLMEQLTFFHDHALLILIMITTLVAYIMTAIMFYSYTHRNLLEGQLIEVIWTVLPAVTLIFIALPS 80
Cdd:MTH00154   1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361532  81 LRLLYLLDESMDPSISIKTVGHQWYWSYEYSDFINPhEFDSYMIPYNEMNTNGFRLLDVDNRTVLPMHTQIRMMVSAADV 160
Cdd:MTH00154  81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNI-EFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADV 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 540361532 161 LHSWTVPALGVKVDATPGRLNQTNFFMNRPGLYYGQCSEICGANHSFMPIVIE 213
Cdd:MTH00154 160 IHSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIE 212
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-213 9.75e-115

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 326.29  E-value: 9.75e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361532   1 MATWSNLNLQNSASPLMEQLTFFHDHALLILIMITTLVAYIMTAIMFYSYTHRNLLEGQLIEVIWTVLPAVTLIFIALPS 80
Cdd:MTH00139   1 MAYWGQLGFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361532  81 LRLLYLLDESMDPSISIKTVGHQWYWSYEYSDFINpHEFDSYMIPYNEMNTNGFRLLDVDNRTVLPMHTQIRMMVSAADV 160
Cdd:MTH00139  81 LRLLYLMDEVSDPYLTFKAVGHQWYWSYEYSDFKN-LSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADV 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 540361532 161 LHSWTVPALGVKVDATPGRLNQTNFFMNRPGLYYGQCSEICGANHSFMPIVIE 213
Cdd:MTH00139 160 LHSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVE 212
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-213 3.31e-113

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 322.66  E-value: 3.31e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361532   1 MATWSNLNLQNSASPLMEQLTFFHDHALLILIMITTLVAYIMTAIMFYSYTHRNLLEGQLIEVIWTVLPAVTLIFIALPS 80
Cdd:MTH00140   1 MSYWGQLGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361532  81 LRLLYLLDESMDPSISIKTVGHQWYWSYEYSDFINpHEFDSYMIPYNEMNTNGFRLLDVDNRTVLPMHTQIRMMVSAADV 160
Cdd:MTH00140  81 LRLLYLLDETNNPLLTVKAIGHQWYWSYEYSDFSV-IEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADV 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 540361532 161 LHSWTVPALGVKVDATPGRLNQTNFFMNRPGLYYGQCSEICGANHSFMPIVIE 213
Cdd:MTH00140 160 IHSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVE 212
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-213 1.37e-109

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 313.39  E-value: 1.37e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361532   1 MATWSNLNLQNSASPLMEQLTFFHDHALLILIMITTLVAYIMTAIMFYSYTHRNLLEGQLIEVIWTVLPAVTLIFIALPS 80
Cdd:MTH00117   1 MANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361532  81 LRLLYLLDESMDPSISIKTVGHQWYWSYEYSDFINPhEFDSYMIPYNEMNTNGFRLLDVDNRTVLPMHTQIRMMVSAADV 160
Cdd:MTH00117  81 LRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKDL-SFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDV 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 540361532 161 LHSWTVPALGVKVDATPGRLNQTNFFMNRPGLYYGQCSEICGANHSFMPIVIE 213
Cdd:MTH00117 160 LHSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVE 212
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-213 2.08e-108

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 310.48  E-value: 2.08e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361532   1 MATWSNLNLQNSASPLMEQLTFFHDHALLILIMITTLVAYIMTAIMFYSYTHRNLLEGQLIEVIWTVLPAVTLIFIALPS 80
Cdd:MTH00038   1 MATWLQLGLQDASSPLMEELIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361532  81 LRLLYLLDESMDPSISIKTVGHQWYWSYEYSDFiNPHEFDSYMIPYNEMNTNGFRLLDVDNRTVLPMHTQIRMMVSAADV 160
Cdd:MTH00038  81 LQLLYLMDEVNNPFLTIKAIGHQWYWSYEYTDY-NDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADV 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 540361532 161 LHSWTVPALGVKVDATPGRLNQTNFFMNRPGLYYGQCSEICGANHSFMPIVIE 213
Cdd:MTH00038 160 LHSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIE 212
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-213 4.39e-108

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 309.60  E-value: 4.39e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361532   1 MATWSNLNLQNSASPLMEQLTFFHDHALLILIMITTLVAYIMTAIMFYSYTHRNLLEGQLIEVIWTVLPAVTLIFIALPS 80
Cdd:MTH00168   1 MATYSQLGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361532  81 LRLLYLLDESMDPSISIKTVGHQWYWSYEYSDFINpHEFDSYMIPYNEMNTNGFRLLDVDNRTVLPMHTQIRMMVSAADV 160
Cdd:MTH00168  81 LRLLYLMDEIDKPDLTIKAVGHQWYWSYEYTDYND-LEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADV 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 540361532 161 LHSWTVPALGVKVDATPGRLNQTNFFMNRPGLYYGQCSEICGANHSFMPIVIE 213
Cdd:MTH00168 160 LHSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVE 212
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-213 1.31e-107

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 308.32  E-value: 1.31e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361532   1 MATWSNLNLQNSASPLMEQLTFFHDHALLILIMITTLVAYIMTAIMFYSYTHRNLLEGQLIEVIWTVLPAVTLIFIALPS 80
Cdd:MTH00008   1 MPHWGQLMFQDAASPVMLQLISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361532  81 LRLLYLLDESMDPSISIKTVGHQWYWSYEYSDFINPhEFDSYMIPYNEMNTNGFRLLDVDNRTVLPMHTQIRMMVSAADV 160
Cdd:MTH00008  81 LRLLYLMDEVSNPSITLKTIGHQWYWSYEYSDFSNL-EFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADV 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 540361532 161 LHSWTVPALGVKVDATPGRLNQTNFFMNRPGLYYGQCSEICGANHSFMPIVIE 213
Cdd:MTH00008 160 IHSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLE 212
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-213 4.10e-99

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 287.00  E-value: 4.10e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361532   1 MATWSNLNLQNSASPLMEQLTFFHDHALLILIMITTLVAYIMTAIMFYSYTHRNLLEGQLIEVIWTVLPAVTLIFIALPS 80
Cdd:MTH00098   1 MAYPFQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361532  81 LRLLYLLDESMDPSISIKTVGHQWYWSYEYSDFINpHEFDSYMIPYNEMNTNGFRLLDVDNRTVLPMHTQIRMMVSAADV 160
Cdd:MTH00098  81 LRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYED-LSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDV 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 540361532 161 LHSWTVPALGVKVDATPGRLNQTNFFMNRPGLYYGQCSEICGANHSFMPIVIE 213
Cdd:MTH00098 160 LHSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLE 212
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 7-213 1.16e-98

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 286.26  E-value: 1.16e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361532   7 LNLQNSASPLMEQLTFFHDHALLILIMITTLVAYIMTAIMFYSYTHRNLLEGQLIEVIWTVLPAVTLIFIALPSLRLLYL 86
Cdd:MTH00023  16 LGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKLLYL 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361532  87 LDESMDPSISIKTVGHQWYWSYEYSDFINPH-EFDSYMIPYNEMNTNGFRLLDVDNRTVLPMHTQIRMMVSAADVLHSWT 165
Cdd:MTH00023  96 MDEVVSPALTIKAIGHQWYWSYEYSDYEGETlEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSFA 175

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 540361532 166 VPALGVKVDATPGRLNQTNFFMNRPGLYYGQCSEICGANHSFMPIVIE 213
Cdd:MTH00023 176 VPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIE 223
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 1-213 1.44e-98

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 285.45  E-value: 1.44e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361532   1 MATWSNLNLQNSASPLMEQLTFFHDHALLILIMITTLVAYIMTAIMFYSYTHRNLLEGQLIEVIWTVLPAVTLIFIALPS 80
Cdd:MTH00129   1 MAHPSQLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361532  81 LRLLYLLDESMDPSISIKTVGHQWYWSYEYSDFINpHEFDSYMIPYNEMNTNGFRLLDVDNRTVLPMHTQIRMMVSAADV 160
Cdd:MTH00129  81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYED-LGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDV 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 540361532 161 LHSWTVPALGVKVDATPGRLNQTNFFMNRPGLYYGQCSEICGANHSFMPIVIE 213
Cdd:MTH00129 160 LHSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVE 212
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 7-213 3.96e-97

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 282.05  E-value: 3.96e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361532   7 LNLQNSASPLMEQLTFFHDHALLILIMITTLVAYIMTAIMFYSYTHRNLLEGQLIEVIWTVLPAVTLIFIALPSLRLLYL 86
Cdd:MTH00051   9 LGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSLKLLYL 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361532  87 LDESMDPSISIKTVGHQWYWSYEYSDF-INPHEFDSYMIPYNEMNTNGFRLLDVDNRTVLPMHTQIRMMVSAADVLHSWT 165
Cdd:MTH00051  89 MDEVIDPALTIKAIGHQWYWSYEYSDYgTDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSFA 168

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 540361532 166 VPALGVKVDATPGRLNQTNFFMNRPGLYYGQCSEICGANHSFMPIVIE 213
Cdd:MTH00051 169 VPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIE 216
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 1-213 1.03e-96

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 281.00  E-value: 1.03e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361532   1 MATWSNLNLQNSASPLMEQLTFFHDHALLILIMITTLVAYIMTAIMFYSYTHRNLLEGQLIEVIWTVLPAVTLIFIALPS 80
Cdd:MTH00185   1 MAHPSQLGLQDAASPVMEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361532  81 LRLLYLLDESMDPSISIKTVGHQWYWSYEYSDFiNPHEFDSYMIPYNEMNTNGFRLLDVDNRTVLPMHTQIRMMVSAADV 160
Cdd:MTH00185  81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDY-EQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDV 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 540361532 161 LHSWTVPALGVKVDATPGRLNQTNFFMNRPGLYYGQCSEICGANHSFMPIVIE 213
Cdd:MTH00185 160 LHSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVE 212
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 1-213 1.86e-96

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 280.13  E-value: 1.86e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361532   1 MATWSNLNLQNSASPLMEQLTFFHDHALLILIMITTLVAYIMTAIMFYSYTHRNLLEGQLIEVIWTVLPAVTLIFIALPS 80
Cdd:MTH00076   1 MAHPSQLGFQDAASPIMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361532  81 LRLLYLLDESMDPSISIKTVGHQWYWSYEYSDFINpHEFDSYMIPYNEMNTNGFRLLDVDNRTVLPMHTQIRMMVSAADV 160
Cdd:MTH00076  81 LRILYLMDEINDPHLTVKAIGHQWYWSYEYTDYED-LSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDV 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 540361532 161 LHSWTVPALGVKVDATPGRLNQTNFFMNRPGLYYGQCSEICGANHSFMPIVIE 213
Cdd:MTH00076 160 LHSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVE 212
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 93-213 3.48e-83

C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal oxidase in the respiratory chains of eukaryotes and most bacteria, is a multi-chain transmembrane protein located in the inner membrane of mitochondria and the cell membrane of prokaryotes. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. Only subunits I and II are essential for function. Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunit II contains a copper-copper binuclear site called CuA, which is believed to be involved in electron transfer from cytochrome c to the binuclear center (active site) in subunit I.


Pssm-ID: 259979 [Multi-domain]  Cd Length: 130  Bit Score: 242.86  E-value: 3.48e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361532  93 PSISIKTVGHQWYWSYEYSDFiNPHEFDSYMIPYNEMNTNGFRLLDVDNRTVLPMHTQIRMMVSAADVLHSWTVPALGVK 172
Cdd:cd13912    1 PSLTIKAIGHQWYWSYEYSDF-NDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIK 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 540361532 173 VDATPGRLNQTNFFMNRPGLYYGQCSEICGANHSFMPIVIE 213
Cdd:cd13912   80 VDAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVE 120
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-213 2.80e-74

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 219.97  E-value: 2.80e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361532   95 ISIKTVGHQWYWSYEYSDFINPhEFDSYMIPYNEMNTNGFRLLDVDNRTVLPMHTQIRMMVSAADVLHSWTVPALGVKVD 174
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDL-EFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTD 79

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 540361532  175 ATPGRLNQTNFFMNRPGLYYGQCSEICGANHSFMPIVIE 213
Cdd:pfam00116  80 AVPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIE 118
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 7-213 2.59e-72

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 220.28  E-value: 2.59e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361532   7 LNLQNSASPLMEQLTFFHDHALLILIMITTLVAYIMTAIMF----YSYtHRNLLEGQLIEVIWTVLPAVTLIFIALPSLR 82
Cdd:MTH00027  35 LGFQDAGSPVMEEIIMLHDQILFILTIIVGVVLWLIIRILLgnnyYSY-YWNKLDGSLIEVIWTLIPAFILILIAFPSLR 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361532  83 LLYLLDES-MDPSISIKTVGHQWYWSYEYSDFINPH-EFDSYMIPYNEMNTNGFRLLDVDNRTVLPMHTQIRMMVSAADV 160
Cdd:MTH00027 114 LLYIMDECgFSANITIKVTGHQWYWSYSYEDYGEKNiEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAADV 193

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 540361532 161 LHSWTVPALGVKVDATPGRLNQTNFFMNRPGLYYGQCSEICGANHSFMPIVIE 213
Cdd:MTH00027 194 LHSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVE 246
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 6-213 9.37e-60

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 187.14  E-value: 9.37e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361532   6 NLNLQNSA-SPLMEQLTFFHDHALLILIMITTLVAYIMTAIMFYSYTHRNLLEGQLIEVIWTVLPAVTLIFIALPSLRLL 84
Cdd:MTH00080   7 NLNFSNSLfSSYMDWFHNFNCSLLFGEFVLAFVVFLFLYLISNNFYFKSKKIEYQFGELLCSVFPVLILLMQMVPSLSLL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361532  85 YLLD-ESMDPSISIKTVGHQWYWSYEYSDFINPhEFDSYMIPYNEMNTNGFRLLDVDNRTVLPMHTQIRMMVSAADVLHS 163
Cdd:MTH00080  87 YYYGlMNLDSNLTVKVTGHQWYWSYEFSDIPGL-EFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHS 165

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 540361532 164 WTVPALGVKVDATPGRLNQTNFFMNRPGLYYGQCSEICGANHSFMPIVIE 213
Cdd:MTH00080 166 WALPSLSIKMDAMSGILSTLCYSFPMPGVFYGQCSEICGANHSFMPIAVE 215
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
6-213 1.68e-45

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 150.36  E-value: 1.68e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361532   6 NLNLQNSASPLMEQLTFFHDHALLILIMITTLVayimTAIMFYS--------------YTHRNLLegqlIEVIWTVLPAV 71
Cdd:COG1622   18 QLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLV----FGLLLYFairyrrrkgdadpaQFHHNTK----LEIVWTVIPII 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361532  72 TLIFIALPSLRLLYLLDESMDPSISIKTVGHQWYWSYEYSDfinphefdsymipYNEmntngfrllDVDNRTVLPMHTQI 151
Cdd:COG1622   90 IVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPD-------------QGI---------ATVNELVLPVGRPV 147

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 540361532 152 RMMVSAADVLHSWTVPALGVKVDATPGRLNQTNFFMNRPGLYYGQCSEICGANHSFMPIVIE 213
Cdd:COG1622  148 RFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVV 209
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 57-213 3.86e-42

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 140.86  E-value: 3.86e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361532  57 EGQLIEVIWTVLPAVtLIFIALPSLRLLYLLDESMDPSISIKTVGHQWYWSYEYSDFInphEFDSYMIPYNEMntngfrl 136
Cdd:MTH00047  45 ENQVLELLWTVVPTL-LVLVLCFLNLNFITSDLDCFSSETIKVIGHQWYWSYEYSFGG---SYDSFMTDDIFG------- 113

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 540361532 137 ldVDNRTVLPMHTQIRMMVSAADVLHSWTVPALGVKVDATPGRLNQTNFFMNRPGLYYGQCSEICGANHSFMPIVIE 213
Cdd:MTH00047 114 --VDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCPDRHGVFVGYCSELCGVGHSYMPIVIE 188
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 119-213 3.05e-38

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 129.94  E-value: 3.05e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361532 119 FDSYMIPYNEMNTNGFRLLDVDNRTVLPMHTQIRMMVSAADVLHSWTVPALGVKVDATPGRLNQTNFFMNRPGLYYGQCS 198
Cdd:PTZ00047  51 FQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCS 130

                         90
                 ....*....|....*
gi 540361532 199 EICGANHSFMPIVIE 213
Cdd:PTZ00047 131 EMCGTLHGFMPIVVE 145
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 13-213 5.93e-37

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: 127.88  E-value: 5.93e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361532   13 ASPLMEQLTFFHdhalLILIMITTLVAYIMTAIMFY--------------SYTHrnllEGQLIEVIWTVLPAVTLIFIAL 78
Cdd:TIGR02866   2 GGEIAQQIAFLF----LFVLAVSTLISLLVAALLAYvvwkfrrkgdeekpSQIH----GNRRLEYVWTVIPLIIVVGLFA 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361532   79 PSLRLLYLLDESMDP-SISIKTVGHQWYWSYEYSDFinphefdsymipynemntnGFRlldVDNRTVLPMHTQIRMMVSA 157
Cdd:TIGR02866  74 ATAKGLLYLERPIPKdALKVKVTGYQWWWDFEYPES-------------------GFT---TVNELVLPAGTPVELQVTS 131

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 540361532  158 ADVLHSWTVPALGVKVDATPGRLNQTNFFMNRPGLYYGQCSEICGANHSFMPIVIE 213
Cdd:TIGR02866 132 KDVIHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVV 187
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 97-213 1.32e-25

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: 95.44  E-value: 1.32e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361532  97 IKTVGHQWYWSYEYSDFINPHEFdsymipynemntngfrlldvdnrtVLPMHTQIRMMVSAADVLHSWTVPALGVKVDAT 176
Cdd:cd13842    3 VYVTGVQWSWTFIYPNVRTPNEI------------------------VVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDAV 58

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 540361532 177 PGRLNQTNFFMNRPGLYYGQCSEICGANHSFMPIVIE 213
Cdd:cd13842   59 PGYTSELWFVADKPGTYTIICAEYCGLGHSYMLGKVE 95
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-77 3.61e-23

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: 88.93  E-value: 3.61e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361532    1 MATWSNLNLQNSASPLMEQLTFFHDHALLILIMITTLVAYIM-TAIMFYSY-----THRNLLEGQLIEVIWTVLPAVTLI 74
Cdd:pfam02790   1 MPTPWGLGFQDAASPLMEGLLELHDYIMFILTLILILVLYILvTCLIRFNRrknpiTARYTTHGQTIEIIWTIIPAVILI 80


                  ...
gi 540361532   75 FIA 77
Cdd:pfam02790  81 LIA 83
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 97-208 2.88e-21

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


Pssm-ID: 259875 [Multi-domain]  Cd Length: 103  Bit Score: 84.21  E-value: 2.88e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361532  97 IKTVGHQWYWSYEYSDfINPHEFDSYmipyNEMntngfrlldvdnrtVLPMHTQIRMMVSAADVLHSWTVPALGVKVDAT 176
Cdd:cd04213    4 IEVTGHQWWWEFRYPD-EPGRGIVTA----NEL--------------HIPVGRPVRLRLTSADVIHSFWVPSLAGKMDMI 64

                         90       100       110
                 ....*....|....*....|....*....|..
gi 540361532 177 PGRLNQTNFFMNRPGLYYGQCSEICGANHSFM 208
Cdd:cd04213   65 PGRTNRLWLQADEPGVYRGQCAEFCGASHALM 96
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 97-208 7.21e-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: 259982 [Multi-domain]  Cd Length: 98  Bit Score: 75.36  E-value: 7.21e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361532  97 IKTVGHQWYWSYEYSdfinphefdsymipynemntNGFRlldVDNRTVLPMHTQIRMMVSAADVLHSWTVPALGVKVDAT 176
Cdd:cd13915    4 IQVTGRQWMWEFTYP--------------------NGKR---EINELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQDVV 60

                         90       100       110
                 ....*....|....*....|....*....|..
gi 540361532 177 PGRLNQTNFFMNRPGLYYGQCSEICGANHSFM 208
Cdd:cd13915   61 PGRYTYLWFEATKPGEYDLFCTEYCGTGHSGM 92
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 97-208 2.28e-17

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: 74.21  E-value: 2.28e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361532  97 IKTVGHQWYWSYEYsdfINPHEfdsymipynemnTNGFRLLDVDNRTVLPMHTQIRMMVSAADVLHSWTVPALGVKVDAT 176
Cdd:cd13919    4 VEVTAQQWAWTFRY---PGGDG------------KLGTDDDVTSPELHLPVGRPVLFNLRSKDVIHSFWVPEFRVKQDAV 68

                         90       100       110
                 ....*....|....*....|....*....|..
gi 540361532 177 PGRLNQTNFFMNRPGLYYGQCSEICGANHSFM 208
Cdd:cd13919   69 PGRTTRLWFTPTREGEYEVRCAELCGLGHYRM 100
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 88-208 7.79e-17

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: 73.64  E-value: 7.79e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361532  88 DESMDPSISIKTVGHQWYWSYEYSdfiNPHEFDSYMipynemntngfrlldvdnrtVLPMHTQIRMMVSAADVLHSWTVP 167
Cdd:cd13918   26 DEADEDALEVEVEGFQFGWQFEYP---NGVTTGNTL--------------------RVPADTPIALRVTSTDVFHTFGIP 82

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 540361532 168 ALGVKVDATPGRLNQTNFFMNRPGLYYGQCSEICGANHSFM 208
Cdd:cd13918   83 ELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLM 123
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 97-208 2.47e-16

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


Pssm-ID: 259981 [Multi-domain]  Cd Length: 108  Bit Score: 71.67  E-value: 2.47e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361532  97 IKTVGHQWYWSYEYsdfinphefdsymipyNEMNTNGFrlldvdNRTVLPMHTQIRMMVSAADVLHSWTVPALGVKVDAT 176
Cdd:cd13914    3 IEVEAYQWGWEFSY----------------PEANVTTS------EQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDAF 60

                         90       100       110
                 ....*....|....*....|....*....|..
gi 540361532 177 PGRLNQTNFFMNRPGLYYGQCSEICGANHSFM 208
Cdd:cd13914   61 PGQYNTIKTEATEEGEYQLYCAEYCGAGHSQM 92
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 141-208 2.06e-07

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: 47.56  E-value: 2.06e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 540361532 141 NRTVLPMHTQIRMMVSAADVLHSWTVPALGVKVDATPGRLNQTNFFMNRPGLYYGQCSEICGANHSFM 208
Cdd:cd13913   25 NEIEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNM 92
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 141-208 1.38e-05

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


Pssm-ID: 259874 [Multi-domain]  Cd Length: 99  Bit Score: 42.54  E-value: 1.38e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 540361532 141 NRTVLPMHTQIRMMVSAADVLHSWTVPALGVKVDATPGRLNQTNFFMNRPGLYYGQCSEICGANHSFM 208
Cdd:cd04212   25 NELVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGTYQGLSANYSGEGFSDM 92
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 121-213 1.13e-04

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: 40.29  E-value: 1.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361532 121 SYMIPYNEMNTNGFrlldVDNRTVLPMHTQIRM-MVSAADVLHSWTVPALGVKVDA---------------TPGRLNQTN 184
Cdd:cd00920    7 DWGWSFTYNGVLLF----GPPVLVVPVGDTVRVqFVNKLGENHSVTIAGFGVPVVAmagganpglvntlviGPGESAEVT 82

                         90       100
                 ....*....|....*....|....*....
gi 540361532 185 FFMNRPGLYYGQCSEICGaNHSFMPIVIE 213
Cdd:cd00920   83 FTTDQAGVYWFYCTIPGH-NHAGMVGTIN 110
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-208 2.79e-04

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: 38.52  E-value: 2.79e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 540361532  95 ISIKTVGHQWYWsyeysdfinphefdsymipynEMNtngfrlldvdnRTVLPMHTQIRMMVSAADVLHSWTV--PALGV- 171
Cdd:cd13916    1 QVVAVTGHQWYW---------------------ELS-----------RTEIPAGKPVEFRVTSADVNHGFGIydPDMRLl 48

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 540361532 172 -KVDATPGRLNQTNFFMNRPGLYYGQCSEICGANHSFM 208
Cdd:cd13916   49 aQTQAMPGYTNVLRYTFDKPGTYTILCLEYCGLAHHVM 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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