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Conserved domains on  [gi|1219684130|gb|ASM93615|]
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cytochrome oxidase subunit II, partial (mitochondrion) [Saga sp. OR732]

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
 1-218 1.98e-150

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 416.92  E-value: 1.98e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219684130   1 MATWSNLNLQNSASPLMEQLTFFHDHALLILLMITVLVAYIMISLFFNKYTHRFLLEGQTIEVIWTILPAVTLIFIALPS 80
Cdd:MTH00154    1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219684130  81 LRLLYLLDESMDPIVTIKTIGHQWYWSYEYTDFVTPhEFDAYMTPYNELNINGFRLLDVDNRTVLPMSSQ*RVLVTAADV 160
Cdd:MTH00154   81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNI-EFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADV 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1219684130 161 LHSWTVPSLGVKVDASPGRLNQTSFFMNRPGLFYGQCSEICGANHSFMPIVIESVNTN 218
Cdd:MTH00154  160 IHSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVN 217
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-218 1.98e-150

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 416.92  E-value: 1.98e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219684130   1 MATWSNLNLQNSASPLMEQLTFFHDHALLILLMITVLVAYIMISLFFNKYTHRFLLEGQTIEVIWTILPAVTLIFIALPS 80
Cdd:MTH00154    1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219684130  81 LRLLYLLDESMDPIVTIKTIGHQWYWSYEYTDFVTPhEFDAYMTPYNELNINGFRLLDVDNRTVLPMSSQ*RVLVTAADV 160
Cdd:MTH00154   81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNI-EFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADV 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1219684130 161 LHSWTVPSLGVKVDASPGRLNQTSFFMNRPGLFYGQCSEICGANHSFMPIVIESVNTN 218
Cdd:MTH00154  160 IHSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVN 217
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 93-216 9.96e-84

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: 244.40  E-value: 9.96e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219684130  93 PIVTIKTIGHQWYWSYEYTDFVTpHEFDAYMTPYNELNINGFRLLDVDNRTVLPMSSQ*RVLVTAADVLHSWTVPSLGVK 172
Cdd:cd13912     1 PSLTIKAIGHQWYWSYEYSDFND-LEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIK 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1219684130 173 VDASPGRLNQTSFFMNRPGLFYGQCSEICGANHSFMPIVIESVN 216
Cdd:cd13912    80 VDAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVS 123
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
96-215 1.85e-76

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 225.75  E-value: 1.85e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219684130  96 TIKTIGHQWYWSYEYTDFVTPhEFDAYMTPYNELNINGFRLLDVDNRTVLPMSSQ*RVLVTAADVLHSWTVPSLGVKVDA 175
Cdd:pfam00116   2 TIKAIGHQWYWSYEYTDFGDL-EFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1219684130 176 SPGRLNQTSFFMNRPGLFYGQCSEICGANHSFMPIVIESV 215
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
6-215 1.90e-45

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 150.75  E-value: 1.90e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219684130   6 NLNLQNSASPLMEQLTFFHDHALLILLMITVLV-AYIMISLFF-----NKYTHRFLLEGQTIEVIWTILPAVTLIFIALP 79
Cdd:COG1622    18 QLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVfGLLLYFAIRyrrrkGDADPAQFHHNTKLEIVWTVIPIIIVIVLAVP 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219684130  80 SLRLLYLLDESMDPIVTIKTIGHQWYWSYEYTDfvtphefdaymtpYNELningfrlldVDNRTVLPMSSQ*RVLVTAAD 159
Cdd:COG1622    98 TLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPD-------------QGIA---------TVNELVLPVGRPVRFLLTSAD 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1219684130 160 VLHSWTVPSLGVKVDASPGRLNQTSFFMNRPGLFYGQCSEICGANHSFMPIVIESV 215
Cdd:COG1622   156 VIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVV 211
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 13-215 1.32e-36

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: 127.11  E-value: 1.32e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219684130  13 ASPLMEQLTFFHDHALLILLMITVLVAYIMISLFFnKYTHR-------FLLEGQTIEVIWTILPAVTLIFIALPSLRLLY 85
Cdd:TIGR02866   2 GGEIAQQIAFLFLFVLAVSTLISLLVAALLAYVVW-KFRRKgdeekpsQIHGNRRLEYVWTVIPLIIVVGLFAATAKGLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219684130  86 LLDESMDP-IVTIKTIGHQWYWSYEYTDFvtphefdaymtpynelninGFRlldVDNRTVLPMSSQ*RVLVTAADVLHSW 164
Cdd:TIGR02866  81 YLERPIPKdALKVKVTGYQWWWDFEYPES-------------------GFT---TVNELVLPAGTPVELQVTSKDVIHSF 138

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1219684130 165 TVPSLGVKVDASPGRLNQTSFFMNRPGLFYGQCSEICGANHSFMPIVIESV 215
Cdd:TIGR02866 139 WVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVV 189
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-218 1.98e-150

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 416.92  E-value: 1.98e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219684130   1 MATWSNLNLQNSASPLMEQLTFFHDHALLILLMITVLVAYIMISLFFNKYTHRFLLEGQTIEVIWTILPAVTLIFIALPS 80
Cdd:MTH00154    1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219684130  81 LRLLYLLDESMDPIVTIKTIGHQWYWSYEYTDFVTPhEFDAYMTPYNELNINGFRLLDVDNRTVLPMSSQ*RVLVTAADV 160
Cdd:MTH00154   81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNI-EFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADV 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1219684130 161 LHSWTVPSLGVKVDASPGRLNQTSFFMNRPGLFYGQCSEICGANHSFMPIVIESVNTN 218
Cdd:MTH00154  160 IHSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVN 217
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-219 1.23e-117

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 333.83  E-value: 1.23e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219684130   1 MATWSNLNLQNSASPLMEQLTFFHDHALLILLMITVLVAYIMISLFFNKYTHRFLLEGQTIEVIWTILPAVTLIFIALPS 80
Cdd:MTH00140    1 MSYWGQLGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219684130  81 LRLLYLLDESMDPIVTIKTIGHQWYWSYEYTDFVTpHEFDAYMTPYNELNINGFRLLDVDNRTVLPMSSQ*RVLVTAADV 160
Cdd:MTH00140   81 LRLLYLLDETNNPLLTVKAIGHQWYWSYEYSDFSV-IEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADV 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1219684130 161 LHSWTVPSLGVKVDASPGRLNQTSFFMNRPGLFYGQCSEICGANHSFMPIVIESVNTNT 219
Cdd:MTH00140  160 IHSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLED 218
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-216 8.54e-116

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 329.37  E-value: 8.54e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219684130   1 MATWSNLNLQNSASPLMEQLTFFHDHALLILLMITVLVAYIMISLFFNKYTHRFLLEGQTIEVIWTILPAVTLIFIALPS 80
Cdd:MTH00139    1 MAYWGQLGFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219684130  81 LRLLYLLDESMDPIVTIKTIGHQWYWSYEYTDFvTPHEFDAYMTPYNELNINGFRLLDVDNRTVLPMSSQ*RVLVTAADV 160
Cdd:MTH00139   81 LRLLYLMDEVSDPYLTFKAVGHQWYWSYEYSDF-KNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADV 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1219684130 161 LHSWTVPSLGVKVDASPGRLNQTSFFMNRPGLFYGQCSEICGANHSFMPIVIESVN 216
Cdd:MTH00139  160 LHSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAIS 215
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-219 8.27e-114

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 324.35  E-value: 8.27e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219684130   1 MATWSNLNLQNSASPLMEQLTFFHDHALLILLMITVLVAYIMISLFFNKYTHRFLLEGQTIEVIWTILPAVTLIFIALPS 80
Cdd:MTH00038    1 MATWLQLGLQDASSPLMEELIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219684130  81 LRLLYLLDESMDPIVTIKTIGHQWYWSYEYTDFvTPHEFDAYMTPYNELNINGFRLLDVDNRTVLPMSSQ*RVLVTAADV 160
Cdd:MTH00038   81 LQLLYLMDEVNNPFLTIKAIGHQWYWSYEYTDY-NDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADV 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1219684130 161 LHSWTVPSLGVKVDASPGRLNQTSFFMNRPGLFYGQCSEICGANHSFMPIVIESVNTNT 219
Cdd:MTH00038  160 LHSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNT 218
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-218 3.31e-113

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 322.63  E-value: 3.31e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219684130   1 MATWSNLNLQNSASPLMEQLTFFHDHALLILLMITVLVAYIMISLFFNKYTHRFLLEGQTIEVIWTILPAVTLIFIALPS 80
Cdd:MTH00117    1 MANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219684130  81 LRLLYLLDESMDPIVTIKTIGHQWYWSYEYTDFvTPHEFDAYMTPYNELNINGFRLLDVDNRTVLPMSSQ*RVLVTAADV 160
Cdd:MTH00117   81 LRILYLMDEINNPHLTIKAIGHQWYWSYEYTDY-KDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDV 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1219684130 161 LHSWTVPSLGVKVDASPGRLNQTSFFMNRPGLFYGQCSEICGANHSFMPIVIESVNTN 218
Cdd:MTH00117  160 LHSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLK 217
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-219 3.00e-111

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 317.95  E-value: 3.00e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219684130   1 MATWSNLNLQNSASPLMEQLTFFHDHALLILLMITVLVAYIMISLFFNKYTHRFLLEGQTIEVIWTILPAVTLIFIALPS 80
Cdd:MTH00008    1 MPHWGQLMFQDAASPVMLQLISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219684130  81 LRLLYLLDESMDPIVTIKTIGHQWYWSYEYTDFVTPhEFDAYMTPYNELNINGFRLLDVDNRTVLPMSSQ*RVLVTAADV 160
Cdd:MTH00008   81 LRLLYLMDEVSNPSITLKTIGHQWYWSYEYSDFSNL-EFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADV 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1219684130 161 LHSWTVPSLGVKVDASPGRLNQTSFFMNRPGLFYGQCSEICGANHSFMPIVIESVNTNT 219
Cdd:MTH00008  160 IHSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKS 218
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-219 1.33e-110

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 316.15  E-value: 1.33e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219684130   1 MATWSNLNLQNSASPLMEQLTFFHDHALLILLMITVLVAYIMISLFFNKYTHRFLLEGQTIEVIWTILPAVTLIFIALPS 80
Cdd:MTH00168    1 MATYSQLGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219684130  81 LRLLYLLDESMDPIVTIKTIGHQWYWSYEYTDFVTpHEFDAYMTPYNELNINGFRLLDVDNRTVLPMSSQ*RVLVTAADV 160
Cdd:MTH00168   81 LRLLYLMDEIDKPDLTIKAVGHQWYWSYEYTDYND-LEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADV 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1219684130 161 LHSWTVPSLGVKVDASPGRLNQTSFFMNRPGLFYGQCSEICGANHSFMPIVIESVNTNT 219
Cdd:MTH00168  160 LHSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWET 218
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 1-215 2.35e-102

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 295.47  E-value: 2.35e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219684130   1 MATWSNLNLQNSASPLMEQLTFFHDHALLILLMITVLVAYIMISLFFNKYTHRFLLEGQTIEVIWTILPAVTLIFIALPS 80
Cdd:MTH00129    1 MAHPSQLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219684130  81 LRLLYLLDESMDPIVTIKTIGHQWYWSYEYTDFvTPHEFDAYMTPYNELNINGFRLLDVDNRTVLPMSSQ*RVLVTAADV 160
Cdd:MTH00129   81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDY-EDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDV 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1219684130 161 LHSWTVPSLGVKVDASPGRLNQTSFFMNRPGLFYGQCSEICGANHSFMPIVIESV 215
Cdd:MTH00129  160 LHSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAV 214
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 7-218 1.13e-101

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 293.97  E-value: 1.13e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219684130   7 LNLQNSASPLMEQLTFFHDHALLILLMITVLVAYIMISLFFNKYTHRFLLEGQTIEVIWTILPAVTLIFIALPSLRLLYL 86
Cdd:MTH00023   16 LGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKLLYL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219684130  87 LDESMDPIVTIKTIGHQWYWSYEYTDFVTPH-EFDAYMTPYNELNINGFRLLDVDNRTVLPMSSQ*RVLVTAADVLHSWT 165
Cdd:MTH00023   96 MDEVVSPALTIKAIGHQWYWSYEYSDYEGETlEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSFA 175

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1219684130 166 VPSLGVKVDASPGRLNQTSFFMNRPGLFYGQCSEICGANHSFMPIVIESVNTN 218
Cdd:MTH00023  176 VPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLD 228
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 1-215 1.67e-99

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 288.32  E-value: 1.67e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219684130   1 MATWSNLNLQNSASPLMEQLTFFHDHALLILLMITVLVAYIMISLFFNKYTHRFLLEGQTIEVIWTILPAVTLIFIALPS 80
Cdd:MTH00185    1 MAHPSQLGLQDAASPVMEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219684130  81 LRLLYLLDESMDPIVTIKTIGHQWYWSYEYTDFVTpHEFDAYMTPYNELNINGFRLLDVDNRTVLPMSSQ*RVLVTAADV 160
Cdd:MTH00185   81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEQ-LEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDV 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1219684130 161 LHSWTVPSLGVKVDASPGRLNQTSFFMNRPGLFYGQCSEICGANHSFMPIVIESV 215
Cdd:MTH00185  160 LHSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAV 214
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 7-216 3.15e-99

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 287.83  E-value: 3.15e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219684130   7 LNLQNSASPLMEQLTFFHDHALLILLMITVLVAYIMISLFFNKYTHRFLLEGQTIEVIWTILPAVTLIFIALPSLRLLYL 86
Cdd:MTH00051    9 LGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSLKLLYL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219684130  87 LDESMDPIVTIKTIGHQWYWSYEYTDFVTPH-EFDAYMTPYNELNINGFRLLDVDNRTVLPMSSQ*RVLVTAADVLHSWT 165
Cdd:MTH00051   89 MDEVIDPALTIKAIGHQWYWSYEYSDYGTDTiEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSFA 168

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1219684130 166 VPSLGVKVDASPGRLNQTSFFMNRPGLFYGQCSEICGANHSFMPIVIESVN 216
Cdd:MTH00051  169 VPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVS 219
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-215 8.46e-99

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 286.23  E-value: 8.46e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219684130   1 MATWSNLNLQNSASPLMEQLTFFHDHALLILLMITVLVAYIMISLFFNKYTHRFLLEGQTIEVIWTILPAVTLIFIALPS 80
Cdd:MTH00098    1 MAYPFQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219684130  81 LRLLYLLDESMDPIVTIKTIGHQWYWSYEYTDFvTPHEFDAYMTPYNELNINGFRLLDVDNRTVLPMSSQ*RVLVTAADV 160
Cdd:MTH00098   81 LRILYMMDEINNPSLTVKTMGHQWYWSYEYTDY-EDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDV 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1219684130 161 LHSWTVPSLGVKVDASPGRLNQTSFFMNRPGLFYGQCSEICGANHSFMPIVIESV 215
Cdd:MTH00098  160 LHSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELV 214
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 1-215 9.32e-96

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 278.59  E-value: 9.32e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219684130   1 MATWSNLNLQNSASPLMEQLTFFHDHALLILLMITVLVAYIMISLFFNKYTHRFLLEGQTIEVIWTILPAVTLIFIALPS 80
Cdd:MTH00076    1 MAHPSQLGFQDAASPIMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219684130  81 LRLLYLLDESMDPIVTIKTIGHQWYWSYEYTDFvTPHEFDAYMTPYNELNINGFRLLDVDNRTVLPMSSQ*RVLVTAADV 160
Cdd:MTH00076   81 LRILYLMDEINDPHLTVKAIGHQWYWSYEYTDY-EDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDV 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1219684130 161 LHSWTVPSLGVKVDASPGRLNQTSFFMNRPGLFYGQCSEICGANHSFMPIVIESV 215
Cdd:MTH00076  160 LHSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEAT 214
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 93-216 9.96e-84

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: 244.40  E-value: 9.96e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219684130  93 PIVTIKTIGHQWYWSYEYTDFVTpHEFDAYMTPYNELNINGFRLLDVDNRTVLPMSSQ*RVLVTAADVLHSWTVPSLGVK 172
Cdd:cd13912     1 PSLTIKAIGHQWYWSYEYSDFND-LEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIK 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1219684130 173 VDASPGRLNQTSFFMNRPGLFYGQCSEICGANHSFMPIVIESVN 216
Cdd:cd13912    80 VDAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVS 123
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
96-215 1.85e-76

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 225.75  E-value: 1.85e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219684130  96 TIKTIGHQWYWSYEYTDFVTPhEFDAYMTPYNELNINGFRLLDVDNRTVLPMSSQ*RVLVTAADVLHSWTVPSLGVKVDA 175
Cdd:pfam00116   2 TIKAIGHQWYWSYEYTDFGDL-EFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1219684130 176 SPGRLNQTSFFMNRPGLFYGQCSEICGANHSFMPIVIESV 215
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 7-216 4.10e-72

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 219.90  E-value: 4.10e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219684130   7 LNLQNSASPLMEQLTFFHDHALLILLMITVLVAYIMISLFF--NKYTHRF-LLEGQTIEVIWTILPAVTLIFIALPSLRL 83
Cdd:MTH00027   35 LGFQDAGSPVMEEIIMLHDQILFILTIIVGVVLWLIIRILLgnNYYSYYWnKLDGSLIEVIWTLIPAFILILIAFPSLRL 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219684130  84 LYLLDES-MDPIVTIKTIGHQWYWSYEYTDFVTPH-EFDAYMTPYNELNINGFRLLDVDNRTVLPMSSQ*RVLVTAADVL 161
Cdd:MTH00027  115 LYIMDECgFSANITIKVTGHQWYWSYSYEDYGEKNiEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAADVL 194

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1219684130 162 HSWTVPSLGVKVDASPGRLNQTSFFMNRPGLFYGQCSEICGANHSFMPIVIESVN 216
Cdd:MTH00027  195 HSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVS 249
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 6-218 5.10e-62

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 192.92  E-value: 5.10e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219684130   6 NLNLQNSA-SPLMEQLTFFHDHALLILLMITVLVAYIMISLFFNKYTHRFLLEGQTIEVIWTILPAVTLIFIALPSLRLL 84
Cdd:MTH00080    7 NLNFSNSLfSSYMDWFHNFNCSLLFGEFVLAFVVFLFLYLISNNFYFKSKKIEYQFGELLCSVFPVLILLMQMVPSLSLL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219684130  85 YLLD-ESMDPIVTIKTIGHQWYWSYEYTDFVTPhEFDAYMTPYNELNINGFRLLDVDNRTVLPMSSQ*RVLVTAADVLHS 163
Cdd:MTH00080   87 YYYGlMNLDSNLTVKVTGHQWYWSYEFSDIPGL-EFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHS 165

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1219684130 164 WTVPSLGVKVDASPGRLNQTSFFMNRPGLFYGQCSEICGANHSFMPIVIESVNTN 218
Cdd:MTH00080  166 WALPSLSIKMDAMSGILSTLCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLD 220
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
6-215 1.90e-45

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 150.75  E-value: 1.90e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219684130   6 NLNLQNSASPLMEQLTFFHDHALLILLMITVLV-AYIMISLFF-----NKYTHRFLLEGQTIEVIWTILPAVTLIFIALP 79
Cdd:COG1622    18 QLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVfGLLLYFAIRyrrrkGDADPAQFHHNTKLEIVWTVIPIIIVIVLAVP 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219684130  80 SLRLLYLLDESMDPIVTIKTIGHQWYWSYEYTDfvtphefdaymtpYNELningfrlldVDNRTVLPMSSQ*RVLVTAAD 159
Cdd:COG1622    98 TLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPD-------------QGIA---------TVNELVLPVGRPVRFLLTSAD 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1219684130 160 VLHSWTVPSLGVKVDASPGRLNQTSFFMNRPGLFYGQCSEICGANHSFMPIVIESV 215
Cdd:COG1622   156 VIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVV 211
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 17-218 4.25e-43

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 143.56  E-value: 4.25e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219684130  17 MEQLTFFHDHALLILLMITVLVAYIMISLFFNKY----THRFLLEGQTIEVIWTILPAVtLIFIALPSLRLLYLLDESMD 92
Cdd:MTH00047    1 MNLSLLYYDIVCYILALCVFIPCWVYIMLCWQVVsgngSVNFGSENQVLELLWTVVPTL-LVLVLCFLNLNFITSDLDCF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219684130  93 PIVTIKTIGHQWYWSYEYTDfvtPHEFDAYMTPYnelnINGfrlldVDNRTVLPMSSQ*RVLVTAADVLHSWTVPSLGVK 172
Cdd:MTH00047   80 SSETIKVIGHQWYWSYEYSF---GGSYDSFMTDD----IFG-----VDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLK 147

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1219684130 173 VDASPGRLNQTSFFMNRPGLFYGQCSEICGANHSFMPIVIESVNTN 218
Cdd:MTH00047  148 MDAIPGRINHLFFCPDRHGVFVGYCSELCGVGHSYMPIVIEVVDVD 193
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 135-215 3.89e-37

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 127.24  E-value: 3.89e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219684130 135 RLLDVDNRTVLPMSSQ*RVLVTAADVLHSWTVPSLGVKVDASPGRLNQTSFFMNRPGLFYGQCSEICGANHSFMPIVIES 214
Cdd:PTZ00047   67 RQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCSEMCGTLHGFMPIVVEA 146


                  .
gi 1219684130 215 V 215
Cdd:PTZ00047  147 V 147
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 13-215 1.32e-36

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: 127.11  E-value: 1.32e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219684130  13 ASPLMEQLTFFHDHALLILLMITVLVAYIMISLFFnKYTHR-------FLLEGQTIEVIWTILPAVTLIFIALPSLRLLY 85
Cdd:TIGR02866   2 GGEIAQQIAFLFLFVLAVSTLISLLVAALLAYVVW-KFRRKgdeekpsQIHGNRRLEYVWTVIPLIIVVGLFAATAKGLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219684130  86 LLDESMDP-IVTIKTIGHQWYWSYEYTDFvtphefdaymtpynelninGFRlldVDNRTVLPMSSQ*RVLVTAADVLHSW 164
Cdd:TIGR02866  81 YLERPIPKdALKVKVTGYQWWWDFEYPES-------------------GFT---TVNELVLPAGTPVELQVTSKDVIHSF 138

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1219684130 165 TVPSLGVKVDASPGRLNQTSFFMNRPGLFYGQCSEICGANHSFMPIVIESV 215
Cdd:TIGR02866 139 WVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVV 189
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 95-213 9.37e-27

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


Pssm-ID: 259911 [Multi-domain]  Cd Length: 95  Bit Score: 98.52  E-value: 9.37e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219684130  95 VTIKTIGHQWYWSYEYTDFVTPHEFdaymtpynelningfrlldvdnrtVLPMSSQ*RVLVTAADVLHSWTVPSLGVKVD 174
Cdd:cd13842     1 LTVYVTGVQWSWTFIYPNVRTPNEI------------------------VVPAGTPVRFRVTSPDVIHGFYIPNLGVKVD 56

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1219684130 175 ASPGRLNQTSFFMNRPGLFYGQCSEICGANHSFMPIVIE 213
Cdd:cd13842    57 AVPGYTSELWFVADKPGTYTIICAEYCGLGHSYMLGKVE 95
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-77 2.74e-25

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: 94.32  E-value: 2.74e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219684130   1 MATWSNLNLQNSASPLMEQLTFFHDHALLILLMITVLVAYIMISLFF------NKYTHRFLLEGQTIEVIWTILPAVTLI 74
Cdd:pfam02790   1 MPTPWGLGFQDAASPLMEGLLELHDYIMFILTLILILVLYILVTCLIrfnrrkNPITARYTTHGQTIEIIWTIIPAVILI 80


                  ...
gi 1219684130  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), ...
 95-208 7.13e-24

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: 91.14  E-value: 7.13e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219684130  95 VTIKTIGHQWYWSYEYTD-----FVTPhefdaymtpyNELningfrlldvdnrtVLPMSSQ*RVLVTAADVLHSWTVPSL 169
Cdd:cd04213     2 LTIEVTGHQWWWEFRYPDepgrgIVTA----------NEL--------------HIPVGRPVRLRLTSADVIHSFWVPSL 57

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1219684130 170 GVKVDASPGRLNQTSFFMNRPGLFYGQCSEICGANHSFM 208
Cdd:cd04213    58 AGKMDMIPGRTNRLWLQADEPGVYRGQCAEFCGASHALM 96
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-208 2.57e-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: 81.92  E-value: 2.57e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219684130  95 VTIKTIGHQWYWSYEYTDFVTPHEFDAYMTpYNELningfrlldvdnrtVLPMSSQ*RVLVTAADVLHSWTVPSLGVKVD 174
Cdd:cd13919     2 LVVEVTAQQWAWTFRYPGGDGKLGTDDDVT-SPEL--------------HLPVGRPVLFNLRSKDVIHSFWVPEFRVKQD 66

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1219684130 175 ASPGRLNQTSFFMNRPGLFYGQCSEICGANHSFM 208
Cdd:cd13919    67 AVPGRTTRLWFTPTREGEYEVRCAELCGLGHYRM 100
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 96-208 1.12e-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: 259982 [Multi-domain]  Cd Length: 98  Bit Score: 72.28  E-value: 1.12e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219684130  96 TIKTIGHQWYWSYEYTdfvtphefdaymtpynelniNGFRlldVDNRTVLPMSSQ*RVLVTAADVLHSWTVPSLGVKVDA 175
Cdd:cd13915     3 EIQVTGRQWMWEFTYP--------------------NGKR---EINELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQDV 59

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1219684130 176 SPGRLNQTSFFMNRPGLFYGQCSEICGANHSFM 208
Cdd:cd13915    60 VPGRYTYLWFEATKPGEYDLFCTEYCGTGHSGM 92
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 88-208 5.10e-16

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


Pssm-ID: 259985 [Multi-domain]  Cd Length: 139  Bit Score: 71.72  E-value: 5.10e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219684130  88 DESMDPIVTIKTIGHQWYWSYEYTDFVTphefdaymtpynelNINGFRLldvdnrtvlPMSSQ*RVLVTAADVLHSWTVP 167
Cdd:cd13918    26 DEADEDALEVEVEGFQFGWQFEYPNGVT--------------TGNTLRV---------PADTPIALRVTSTDVFHTFGIP 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1219684130 168 SLGVKVDASPGRLNQTSFFMNRPGLFYGQCSEICGANHSFM 208
Cdd:cd13918    83 ELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLM 123
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-216 8.79e-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: 70.13  E-value: 8.79e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219684130  95 VTIKTIGHQWYWSYEYtdfvtphefdaymtpyNELNINGFrlldvdNRTVLPMSSQ*RVLVTAADVLHSWTVPSLGVKVD 174
Cdd:cd13914     1 VEIEVEAYQWGWEFSY----------------PEANVTTS------EQLVIPADRPVYFRITSRDVIHAFHVPELGLKQD 58

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1219684130 175 ASPGRLNQTSFFMNRPGLFYGQCSEICGANHSFMPIVIESVN 216
Cdd:cd13914    59 AFPGQYNTIKTEATEEGEYQLYCAEYCGAGHSQMLSTVTVVS 100
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 141-208 6.94e-08

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


Pssm-ID: 259980 [Multi-domain]  Cd Length: 99  Bit Score: 48.72  E-value: 6.94e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1219684130 141 NRTVLPMSSQ*RVLVTAADVLHSWTVPSLGVKVDASPGRLNQTSFFMNRPGLFYGQCSEICGANHSFM 208
Cdd:cd13913    25 NEIEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNM 92
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 121-213 4.94e-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: 38.37  E-value: 4.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219684130 121 AYMTPYNELNINGFrlldVDNRTVLPMSSQ*RV-LVTAADVLHSWTVPSLGVKVDAS---------------PGRLNQTS 184
Cdd:cd00920     7 DWGWSFTYNGVLLF----GPPVLVVPVGDTVRVqFVNKLGENHSVTIAGFGVPVVAMagganpglvntlvigPGESAEVT 82

                          90       100
                  ....*....|....*....|....*....
gi 1219684130 185 FFMNRPGLFYGQCSEICGaNHSFMPIVIE 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 1.77e-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: 36.59  E-value: 1.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1219684130  95 VTIKTIGHQWYWSYEYTDFVT--PHEFDaymtpynelningfrlldvdnrtvlpmssq*rvlVTAADVLHSWTVPS---- 168
Cdd:cd13916     1 QVVAVTGHQWYWELSRTEIPAgkPVEFR----------------------------------VTSADVNHGFGIYDpdmr 46

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1219684130 169 LGVKVDASPGRLNQTSFFMNRPGLFYGQCSEICGANHSFM 208
Cdd:cd13916    47 LLAQTQAMPGYTNVLRYTFDKPGTYTILCLEYCGLAHHVM 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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