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Conserved domains on  [gi|1150150970|ref|YP_009349950|]
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cytochrome c oxidase subunit 2 (mitochondrion) [Lipotactes tripyrga]

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
 1-226 5.35e-147

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 408.83  E-value: 5.35e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150970   1 MATWSNLNLQNSVTPLMEQLIFFHDHTLMILLTITTLVGYIMSTLFFNTLTHRFLLEGQIIEIIWTILPAITLIFIALPS 80
Cdd:MTH00154    1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150970  81 LRLLYLLDESMKPIITLKTMGHQWYWNYEYTDFTNpYEFDSYMIPSNEMPLNNHRLLDVDNRTILPMNTQIRMLITAADV 160
Cdd:MTH00154   81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKN-IEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADV 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1150150970 161 LHSWTIPAFGVKADATPGRLNQTNFLINRPGLFYGQCSEICGANHSFMPILIESINIKTFIKWMNN 226
Cdd:MTH00154  160 IHSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKN 225
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-226 5.35e-147

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 408.83  E-value: 5.35e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150970   1 MATWSNLNLQNSVTPLMEQLIFFHDHTLMILLTITTLVGYIMSTLFFNTLTHRFLLEGQIIEIIWTILPAITLIFIALPS 80
Cdd:MTH00154    1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150970  81 LRLLYLLDESMKPIITLKTMGHQWYWNYEYTDFTNpYEFDSYMIPSNEMPLNNHRLLDVDNRTILPMNTQIRMLITAADV 160
Cdd:MTH00154   81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKN-IEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADV 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1150150970 161 LHSWTIPAFGVKADATPGRLNQTNFLINRPGLFYGQCSEICGANHSFMPILIESINIKTFIKWMNN 226
Cdd:MTH00154  160 IHSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKN 225
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 93-223 5.73e-87

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: 253.26  E-value: 5.73e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150970  93 PIITLKTMGHQWYWNYEYTDFtNPYEFDSYMIPSNEMPLNNHRLLDVDNRTILPMNTQIRMLITAADVLHSWTIPAFGVK 172
Cdd:cd13912     1 PSLTIKAIGHQWYWSYEYSDF-NDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIK 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1150150970 173 ADATPGRLNQTNFLINRPGLFYGQCSEICGANHSFMPILIESINIKTFIKW 223
Cdd:cd13912    80 VDAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-215 2.55e-75

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 223.44  E-value: 2.55e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150970  95 ITLKTMGHQWYWNYEYTDFTNpYEFDSYMIPSNEMPLNNHRLLDVDNRTILPMNTQIRMLITAADVLHSWTIPAFGVKAD 174
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGD-LEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTD 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1150150970 175 ATPGRLNQTNFLINRPGLFYGQCSEICGANHSFMPILIESI 215
Cdd:pfam00116  80 AVPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
6-226 5.80e-45

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 149.98  E-value: 5.80e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150970   6 NLNLQNSVTPLMEQLiffhDHTLMILLTITTLVG-YIMSTLFFNTLTHR---------FLLEGQIIEIIWTILPAITLIF 75
Cdd:COG1622    18 QLSLPDPAGPIAEEI----DDLFWVSLIIMLVIFvLVFGLLLYFAIRYRrrkgdadpaQFHHNTKLEIVWTVIPIIIVIV 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150970  76 IALPSLRLLYLLDESMKPIITLKTMGHQWYWNYEYtdftnpyefdsymipsnempLNNHRLldVDNRTILPMNTQIRMLI 155
Cdd:COG1622    94 LAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRY--------------------PDQGIA--TVNELVLPVGRPVRFLL 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1150150970 156 TAADVLHSWTIPAFGVKADATPGRLNQTNFLINRPGLFYGQCSEICGANHSFMPILIESINIKTFIKWMNN 226
Cdd:COG1622   152 TSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAE 222
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 14-225 1.24e-35

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: 124.80  E-value: 1.24e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150970  14 TPLMEQLIFFHDHTLMILLTITTLV-GYIMSTLF------FNTLTHRfLLEGQIIEIIWTILPAITLIFIALPSLRLLYL 86
Cdd:TIGR02866   3 GEIAQQIAFLFLFVLAVSTLISLLVaALLAYVVWkfrrkgDEEKPSQ-IHGNRRLEYVWTVIPLIIVVGLFAATAKGLLY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150970  87 LDESM-KPIITLKTMGHQWYWNYEYTDFTnpyefdsymipsnemplnnhrlLDVDNRTILPMNTQIRMLITAADVLHSWT 165
Cdd:TIGR02866  82 LERPIpKDALKVKVTGYQWWWDFEYPESG----------------------FTTVNELVLPAGTPVELQVTSKDVIHSFW 139

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150970 166 IPAFGVKADATPGRLNQTNFLINRPGLFYGQCSEICGANHSFMPILIESINIKTFIKWMN 225
Cdd:TIGR02866 140 VPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYVE 199
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-226 5.35e-147

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 408.83  E-value: 5.35e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150970   1 MATWSNLNLQNSVTPLMEQLIFFHDHTLMILLTITTLVGYIMSTLFFNTLTHRFLLEGQIIEIIWTILPAITLIFIALPS 80
Cdd:MTH00154    1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150970  81 LRLLYLLDESMKPIITLKTMGHQWYWNYEYTDFTNpYEFDSYMIPSNEMPLNNHRLLDVDNRTILPMNTQIRMLITAADV 160
Cdd:MTH00154   81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKN-IEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADV 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1150150970 161 LHSWTIPAFGVKADATPGRLNQTNFLINRPGLFYGQCSEICGANHSFMPILIESINIKTFIKWMNN 226
Cdd:MTH00154  160 IHSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKN 225
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-227 7.86e-117

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 332.29  E-value: 7.86e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150970   1 MATWSNLNLQNSVTPLMEQLIFFHDHTLMILLTITTLVGYIMSTLFFNTLTHRFLLEGQIIEIIWTILPAITLIFIALPS 80
Cdd:MTH00140    1 MSYWGQLGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150970  81 LRLLYLLDESMKPIITLKTMGHQWYWNYEYTDFTNpYEFDSYMIPSNEMPLNNHRLLDVDNRTILPMNTQIRMLITAADV 160
Cdd:MTH00140   81 LRLLYLLDETNNPLLTVKAIGHQWYWSYEYSDFSV-IEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADV 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1150150970 161 LHSWTIPAFGVKADATPGRLNQTNFLINRPGLFYGQCSEICGANHSFMPILIESINIKTFIKWMNNT 227
Cdd:MTH00140  160 IHSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWLELM 226
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-223 4.95e-115

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 327.83  E-value: 4.95e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150970   1 MATWSNLNLQNSVTPLMEQLIFFHDHTLMILLTITTLVGYIMSTLFFNTLTHRFLLEGQIIEIIWTILPAITLIFIALPS 80
Cdd:MTH00139    1 MAYWGQLGFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150970  81 LRLLYLLDESMKPIITLKTMGHQWYWNYEYTDFTNpYEFDSYMIPSNEMPLNNHRLLDVDNRTILPMNTQIRMLITAADV 160
Cdd:MTH00139   81 LRLLYLMDEVSDPYLTFKAVGHQWYWSYEYSDFKN-LSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADV 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1150150970 161 LHSWTIPAFGVKADATPGRLNQTNFLINRPGLFYGQCSEICGANHSFMPILIESINIKTFIKW 223
Cdd:MTH00139  160 LHSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEW 222
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-226 3.58e-112

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 320.71  E-value: 3.58e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150970   1 MATWSNLNLQNSVTPLMEQLIFFHDHTLMILLTITTLVGYIMSTLFFNTLTHRFLLEGQIIEIIWTILPAITLIFIALPS 80
Cdd:MTH00117    1 MANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150970  81 LRLLYLLDESMKPIITLKTMGHQWYWNYEYTDFTNpYEFDSYMIPSNEMPLNNHRLLDVDNRTILPMNTQIRMLITAADV 160
Cdd:MTH00117   81 LRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKD-LSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDV 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1150150970 161 LHSWTIPAFGVKADATPGRLNQTNFLINRPGLFYGQCSEICGANHSFMPILIESINIKTFIKWMNN 226
Cdd:MTH00117  160 LHSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSL 225
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-226 1.32e-110

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 316.54  E-value: 1.32e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150970   1 MATWSNLNLQNSVTPLMEQLIFFHDHTLMILLTITTLVGYIMSTLFFNTLTHRFLLEGQIIEIIWTILPAITLIFIALPS 80
Cdd:MTH00168    1 MATYSQLGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150970  81 LRLLYLLDESMKPIITLKTMGHQWYWNYEYTDFtNPYEFDSYMIPSNEMPLNNHRLLDVDNRTILPMNTQIRMLITAADV 160
Cdd:MTH00168   81 LRLLYLMDEIDKPDLTIKAVGHQWYWSYEYTDY-NDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADV 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1150150970 161 LHSWTIPAFGVKADATPGRLNQTNFLINRPGLFYGQCSEICGANHSFMPILIESINIKTFIKWMNN 226
Cdd:MTH00168  160 LHSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENWVDS 225
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-228 5.13e-110

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 315.10  E-value: 5.13e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150970   1 MATWSNLNLQNSVTPLMEQLIFFHDHTLMILLTITTLVGYIMSTLFFNTLTHRFLLEGQIIEIIWTILPAITLIFIALPS 80
Cdd:MTH00038    1 MATWLQLGLQDASSPLMEELIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150970  81 LRLLYLLDESMKPIITLKTMGHQWYWNYEYTDFtNPYEFDSYMIPSNEMPLNNHRLLDVDNRTILPMNTQIRMLITAADV 160
Cdd:MTH00038   81 LQLLYLMDEVNNPFLTIKAIGHQWYWSYEYTDY-NDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADV 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1150150970 161 LHSWTIPAFGVKADATPGRLNQTNFLINRPGLFYGQCSEICGANHSFMPILIESINIKTFIKWMNNTI 228
Cdd:MTH00038  160 LHSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVSNFL 227
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-226 5.54e-110

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 315.26  E-value: 5.54e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150970   1 MATWSNLNLQNSVTPLMEQLIFFHDHTLMILLTITTLVGYIMSTLFFNTLTHRFLLEGQIIEIIWTILPAITLIFIALPS 80
Cdd:MTH00008    1 MPHWGQLMFQDAASPVMLQLISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150970  81 LRLLYLLDESMKPIITLKTMGHQWYWNYEYTDFTNpYEFDSYMIPSNEMPLNNHRLLDVDNRTILPMNTQIRMLITAADV 160
Cdd:MTH00008   81 LRLLYLMDEVSNPSITLKTIGHQWYWSYEYSDFSN-LEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADV 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1150150970 161 LHSWTIPAFGVKADATPGRLNQTNFLINRPGLFYGQCSEICGANHSFMPILIESINIKTFIKWMNN 226
Cdd:MTH00008  160 IHSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKWVSS 225
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-223 1.70e-100

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 291.24  E-value: 1.70e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150970   1 MATWSNLNLQNSVTPLMEQLIFFHDHTLMILLTITTLVGYIMSTLFFNTLTHRFLLEGQIIEIIWTILPAITLIFIALPS 80
Cdd:MTH00098    1 MAYPFQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150970  81 LRLLYLLDESMKPIITLKTMGHQWYWNYEYTDFTNpYEFDSYMIPSNEMPLNNHRLLDVDNRTILPMNTQIRMLITAADV 160
Cdd:MTH00098   81 LRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYED-LSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDV 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1150150970 161 LHSWTIPAFGVKADATPGRLNQTNFLINRPGLFYGQCSEICGANHSFMPILIESINIKTFIKW 223
Cdd:MTH00098  160 LHSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKW 222
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 1-223 3.99e-99

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 287.77  E-value: 3.99e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150970   1 MATWSNLNLQNSVTPLMEQLIFFHDHTLMILLTITTLVGYIMSTLFFNTLTHRFLLEGQIIEIIWTILPAITLIFIALPS 80
Cdd:MTH00129    1 MAHPSQLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150970  81 LRLLYLLDESMKPIITLKTMGHQWYWNYEYTDFTNpYEFDSYMIPSNEMPLNNHRLLDVDNRTILPMNTQIRMLITAADV 160
Cdd:MTH00129   81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYED-LGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDV 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1150150970 161 LHSWTIPAFGVKADATPGRLNQTNFLINRPGLFYGQCSEICGANHSFMPILIESINIKTFIKW 223
Cdd:MTH00129  160 LHSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFENW 222
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 7-226 3.58e-96

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 280.48  E-value: 3.58e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150970   7 LNLQNSVTPLMEQLIFFHDHTLMILLTITTLVGYIMSTLFFNTLTHRFLLEGQIIEIIWTILPAITLIFIALPSLRLLYL 86
Cdd:MTH00023   16 LGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKLLYL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150970  87 LDESMKPIITLKTMGHQWYWNYEYTDFTNP-YEFDSYMIPSNEMPLNNHRLLDVDNRTILPMNTQIRMLITAADVLHSWT 165
Cdd:MTH00023   96 MDEVVSPALTIKAIGHQWYWSYEYSDYEGEtLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSFA 175

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1150150970 166 IPAFGVKADATPGRLNQTNFLINRPGLFYGQCSEICGANHSFMPILIESINIKTFIKWMNN 226
Cdd:MTH00023  176 VPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWLLS 236
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 1-226 1.67e-95

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 278.59  E-value: 1.67e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150970   1 MATWSNLNLQNSVTPLMEQLIFFHDHTLMILLTITTLVGYIMSTLFFNTLTHRFLLEGQIIEIIWTILPAITLIFIALPS 80
Cdd:MTH00076    1 MAHPSQLGFQDAASPIMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150970  81 LRLLYLLDESMKPIITLKTMGHQWYWNYEYTDFTNpYEFDSYMIPSNEMPLNNHRLLDVDNRTILPMNTQIRMLITAADV 160
Cdd:MTH00076   81 LRILYLMDEINDPHLTVKAIGHQWYWSYEYTDYED-LSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDV 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1150150970 161 LHSWTIPAFGVKADATPGRLNQTNFLINRPGLFYGQCSEICGANHSFMPILIESINIKTFIKWMNN 226
Cdd:MTH00076  160 LHSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLNWSSS 225
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 1-223 2.26e-95

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 278.31  E-value: 2.26e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150970   1 MATWSNLNLQNSVTPLMEQLIFFHDHTLMILLTITTLVGYIMSTLFFNTLTHRFLLEGQIIEIIWTILPAITLIFIALPS 80
Cdd:MTH00185    1 MAHPSQLGLQDAASPVMEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150970  81 LRLLYLLDESMKPIITLKTMGHQWYWNYEYTDFTNpYEFDSYMIPSNEMPLNNHRLLDVDNRTILPMNTQIRMLITAADV 160
Cdd:MTH00185   81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEQ-LEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDV 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1150150970 161 LHSWTIPAFGVKADATPGRLNQTNFLINRPGLFYGQCSEICGANHSFMPILIESINIKTFIKW 223
Cdd:MTH00185  160 LHSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENW 222
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 7-224 2.47e-95

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 278.20  E-value: 2.47e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150970   7 LNLQNSVTPLMEQLIFFHDHTLMILLTITTLVGYIMSTLFFNTLTHRFLLEGQIIEIIWTILPAITLIFIALPSLRLLYL 86
Cdd:MTH00051    9 LGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSLKLLYL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150970  87 LDESMKPIITLKTMGHQWYWNYEYTDF-TNPYEFDSYMIPSNEMPLNNHRLLDVDNRTILPMNTQIRMLITAADVLHSWT 165
Cdd:MTH00051   89 MDEVIDPALTIKAIGHQWYWSYEYSDYgTDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSFA 168

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1150150970 166 IPAFGVKADATPGRLNQTNFLINRPGLFYGQCSEICGANHSFMPILIESINIKTFIKWM 224
Cdd:MTH00051  169 VPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINWV 227
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 93-223 5.73e-87

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: 253.26  E-value: 5.73e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150970  93 PIITLKTMGHQWYWNYEYTDFtNPYEFDSYMIPSNEMPLNNHRLLDVDNRTILPMNTQIRMLITAADVLHSWTIPAFGVK 172
Cdd:cd13912     1 PSLTIKAIGHQWYWSYEYSDF-NDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIK 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1150150970 173 ADATPGRLNQTNFLINRPGLFYGQCSEICGANHSFMPILIESINIKTFIKW 223
Cdd:cd13912    80 VDAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-215 2.55e-75

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 223.44  E-value: 2.55e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150970  95 ITLKTMGHQWYWNYEYTDFTNpYEFDSYMIPSNEMPLNNHRLLDVDNRTILPMNTQIRMLITAADVLHSWTIPAFGVKAD 174
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGD-LEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTD 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1150150970 175 ATPGRLNQTNFLINRPGLFYGQCSEICGANHSFMPILIESI 215
Cdd:pfam00116  80 AVPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 7-224 9.69e-74

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 224.52  E-value: 9.69e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150970   7 LNLQNSVTPLMEQLIFFHDHTLMILLTITTLVGYIMSTLFFNTLTHRFL---LEGQIIEIIWTILPAITLIFIALPSLRL 83
Cdd:MTH00027   35 LGFQDAGSPVMEEIIMLHDQILFILTIIVGVVLWLIIRILLGNNYYSYYwnkLDGSLIEVIWTLIPAFILILIAFPSLRL 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150970  84 LYLLDES-MKPIITLKTMGHQWYWNYEYTDFTNP-YEFDSYMIPSNEMPLNNHRLLDVDNRTILPMNTQIRMLITAADVL 161
Cdd:MTH00027  115 LYIMDECgFSANITIKVTGHQWYWSYSYEDYGEKnIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAADVL 194

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1150150970 162 HSWTIPAFGVKADATPGRLNQTNFLINRPGLFYGQCSEICGANHSFMPILIESINIKTFIKWM 224
Cdd:MTH00027  195 HSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYIDWI 257
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 6-226 6.75e-62

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 193.30  E-value: 6.75e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150970   6 NLNLQNSV-TPLMEQLIFFHDHTLMILLTITTLVGYIMSTLFFNTLTHRFLLEGQIIEIIWTILPAITLIFIALPSLRLL 84
Cdd:MTH00080    7 NLNFSNSLfSSYMDWFHNFNCSLLFGEFVLAFVVFLFLYLISNNFYFKSKKIEYQFGELLCSVFPVLILLMQMVPSLSLL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150970  85 YLLD-ESMKPIITLKTMGHQWYWNYEYTDFTNpYEFDSYMIPSNEMPLNNHRLLDVDNRTILPMNTQIRMLITAADVLHS 163
Cdd:MTH00080   87 YYYGlMNLDSNLTVKVTGHQWYWSYEFSDIPG-LEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHS 165

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1150150970 164 WTIPAFGVKADATPGRLNQTNFLINRPGLFYGQCSEICGANHSFMPILIESINIKTFIKWMNN 226
Cdd:MTH00080  166 WALPSLSIKMDAMSGILSTLCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKEWCKL 228
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
6-226 5.80e-45

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 149.98  E-value: 5.80e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150970   6 NLNLQNSVTPLMEQLiffhDHTLMILLTITTLVG-YIMSTLFFNTLTHR---------FLLEGQIIEIIWTILPAITLIF 75
Cdd:COG1622    18 QLSLPDPAGPIAEEI----DDLFWVSLIIMLVIFvLVFGLLLYFAIRYRrrkgdadpaQFHHNTKLEIVWTVIPIIIVIV 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150970  76 IALPSLRLLYLLDESMKPIITLKTMGHQWYWNYEYtdftnpyefdsymipsnempLNNHRLldVDNRTILPMNTQIRMLI 155
Cdd:COG1622    94 LAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRY--------------------PDQGIA--TVNELVLPVGRPVRFLL 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1150150970 156 TAADVLHSWTIPAFGVKADATPGRLNQTNFLINRPGLFYGQCSEICGANHSFMPILIESINIKTFIKWMNN 226
Cdd:COG1622   152 TSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAE 222
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 117-220 1.18e-39

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 134.18  E-value: 1.18e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150970 117 YEFDSYMIPSNEMPLNNHRLLDVDNRTILPMNTQIRMLITAADVLHSWTIPAFGVKADATPGRLNQTNFLINRPGLFYGQ 196
Cdd:PTZ00047   49 YSFQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQ 128

                          90       100
                  ....*....|....*....|....
gi 1150150970 197 CSEICGANHSFMPILIESINIKTF 220
Cdd:PTZ00047  129 CSEMCGTLHGFMPIVVEAVSPEAY 152
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 57-215 5.76e-38

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 130.84  E-value: 5.76e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150970  57 EGQIIEIIWTILPA-ITLIFIALPSLRLLYLLDESMKPIItlKTMGHQWYWNYEYTDFTnpyEFDSYMIPSNEMplnnhr 135
Cdd:MTH00047   45 ENQVLELLWTVVPTlLVLVLCFLNLNFITSDLDCFSSETI--KVIGHQWYWSYEYSFGG---SYDSFMTDDIFG------ 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150970 136 lldVDNRTILPMNTQIRMLITAADVLHSWTIPAFGVKADATPGRLNQTNFLINRPGLFYGQCSEICGANHSFMPILIESI 215
Cdd:MTH00047  114 ---VDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCPDRHGVFVGYCSELCGVGHSYMPIVIEVV 190
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 14-225 1.24e-35

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: 124.80  E-value: 1.24e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150970  14 TPLMEQLIFFHDHTLMILLTITTLV-GYIMSTLF------FNTLTHRfLLEGQIIEIIWTILPAITLIFIALPSLRLLYL 86
Cdd:TIGR02866   3 GEIAQQIAFLFLFVLAVSTLISLLVaALLAYVVWkfrrkgDEEKPSQ-IHGNRRLEYVWTVIPLIIVVGLFAATAKGLLY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150970  87 LDESM-KPIITLKTMGHQWYWNYEYTDFTnpyefdsymipsnemplnnhrlLDVDNRTILPMNTQIRMLITAADVLHSWT 165
Cdd:TIGR02866  82 LERPIpKDALKVKVTGYQWWWDFEYPESG----------------------FTTVNELVLPAGTPVELQVTSKDVIHSFW 139

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150970 166 IPAFGVKADATPGRLNQTNFLINRPGLFYGQCSEICGANHSFMPILIESINIKTFIKWMN 225
Cdd:TIGR02866 140 VPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYVE 199
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 95-213 1.49e-26

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: 98.14  E-value: 1.49e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150970  95 ITLKTMGHQWYWNYEYTDFTNPyefdsymipsnemplnnhrlldvdNRTILPMNTQIRMLITAADVLHSWTIPAFGVKAD 174
Cdd:cd13842     1 LTVYVTGVQWSWTFIYPNVRTP------------------------NEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVD 56

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1150150970 175 ATPGRLNQTNFLINRPGLFYGQCSEICGANHSFMPILIE 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 5.21e-22

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


Pssm-ID: 397083 [Multi-domain]  Cd Length: 89  Bit Score: 86.23  E-value: 5.21e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150970   1 MATWSNLNLQNSVTPLMEQLIFFHDHTLMILLTITTLVGYIMSTLFF------NTLTHRFLLEGQIIEIIWTILPAITLI 74
Cdd:pfam02790   1 MPTPWGLGFQDAASPLMEGLLELHDYIMFILTLILILVLYILVTCLIrfnrrkNPITARYTTHGQTIEIIWTIIPAVILI 80


                  ...
gi 1150150970  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 6.59e-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: 83.82  E-value: 6.59e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150970  95 ITLKTMGHQWYWNYEYTDftnpyEFDSYMIPSNEMplnnhrlldvdnrtILPMNTQIRMLITAADVLHSWTIPAFGVKAD 174
Cdd:cd04213     2 LTIEVTGHQWWWEFRYPD-----EPGRGIVTANEL--------------HIPVGRPVRLRLTSADVIHSFWVPSLAGKMD 62

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1150150970 175 ATPGRLNQTNFLINRPGLFYGQCSEICGANHSFM 208
Cdd:cd04213    63 MIPGRTNRLWLQADEPGVYRGQCAEFCGASHALM 96
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-208 1.24e-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: 83.07  E-value: 1.24e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150970  95 ITLKTMGHQWYWNYEYTDfTNPYEFDSYMIPSNEMplnnHrlldvdnrtiLPMNTQIRMLITAADVLHSWTIPAFGVKAD 174
Cdd:cd13919     2 LVVEVTAQQWAWTFRYPG-GDGKLGTDDDVTSPEL----H----------LPVGRPVLFNLRSKDVIHSFWVPEFRVKQD 66

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1150150970 175 ATPGRLNQTNFLINRPGLFYGQCSEICGANHSFM 208
Cdd:cd13919    67 AVPGRTTRLWFTPTREGEYEVRCAELCGLGHYRM 100
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 101-208 1.07e-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: 78.05  E-value: 1.07e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150970 101 GHQWYWNYEYtdftnpyefdsymipsnempLNNHRlldVDNRTILPMNTQIRMLITAADVLHSWTIPAFGVKADATPGRL 180
Cdd:cd13915     8 GRQWMWEFTY--------------------PNGKR---EINELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQDVVPGRY 64

                          90       100
                  ....*....|....*....|....*...
gi 1150150970 181 NQTNFLINRPGLFYGQCSEICGANHSFM 208
Cdd:cd13915    65 TYLWFEATKPGEYDLFCTEYCGTGHSGM 92
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-224 2.02e-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: 259985 [Multi-domain]  Cd Length: 139  Bit Score: 78.27  E-value: 2.02e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150970  95 ITLKTMGHQWYWNYEYTdftNPYEFDSYMIpsnemplnnhrlldvdnrtiLPMNTQIRMLITAADVLHSWTIPAFGVKAD 174
Cdd:cd13918    33 LEVEVEGFQFGWQFEYP---NGVTTGNTLR--------------------VPADTPIALRVTSTDVFHTFGIPELRVKAD 89

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1150150970 175 ATPGRLNQTNFLINRPGLFYGQCSEICGANHSFMPILIESINIKTFIKWM 224
Cdd:cd13918    90 AIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEFEAWY 139
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 101-224 3.06e-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: 3.06e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150970 101 GHQWYWNYEYTDftnpyefdsymipSNemplnnhrlLDVDNRTILPMNTQIRMLITAADVLHSWTIPAFGVKADATPGRL 180
Cdd:cd13914     7 AYQWGWEFSYPE-------------AN---------VTTSEQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDAFPGQY 64

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1150150970 181 NQTNFLINRPGLFYGQCSEICGANHSFMPILIESINIKTFIKWM 224
Cdd:cd13914    65 NTIKTEATEEGEYQLYCAEYCGAGHSQMLSTVTVVSQDEYQQWL 108
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 145-208 6.55e-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: 46.41  E-value: 6.55e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1150150970 145 LPMNTQIRMLITAADVLHSWTIPAFGVKADATPGRLNQTNFLINRPGLFYGQCSEICGANHSFM 208
Cdd:cd13913    29 VPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNM 92
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 141-208 1.23e-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: 1.23e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1150150970 141 NRTILPMNTQIRMLITAADVLHSWTIPAFGVKADATPGRLNQTNFLINRPGLFYGQCSEICGANHSFM 208
Cdd:cd04212    25 NELVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGTYQGLSANYSGEGFSDM 92
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-208 4.08e-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: 35.44  E-value: 4.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1150150970  95 ITLKTMGHQWYWnyeytdftnpyefdsymipsnEMplnnhrlldvdNRTILPMNTQIRMLITAADVLHswtipAFGV--- 171
Cdd:cd13916     1 QVVAVTGHQWYW---------------------EL-----------SRTEIPAGKPVEFRVTSADVNH-----GFGIydp 43

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1150150970 172 ------KADATPGRLNQTNFLINRPGLFYGQCSEICGANHSFM 208
Cdd:cd13916    44 dmrllaQTQAMPGYTNVLRYTFDKPGTYTILCLEYCGLAHHVM 86
N2OR_C cd04223
The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase ...
 159-208 6.81e-03

The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase participates in nitrogen metabolism and catalyzes the last step in dissimilatory nitrate reduction, the two-electron reduction of N2O to N2. It contains copper ions as cofactors in the form of a binuclear CuA center at the site of electron entry and a tetranuclear CuZ centre at the active site. The C-terminus of Nitrous-oxide reductase is a cupredoxin domain.


Pssm-ID: 259885 [Multi-domain]  Cd Length: 95  Bit Score: 34.90  E-value: 6.81e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1150150970 159 DVLHSWTIPAFGVKADATPGRLNQTNFLINRPGLFYGQCSEICGANHSFM 208
Cdd:cd04223    38 DITHGFAIPGYNVNLSLEPGETATVTFVADKPGVYPYYCTEFCSALHLEM 87
 
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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