NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2250083844|gb|URW97390|]
View 

cytochrome c oxidase subunit II (mitochondrion) [Crocidura cf. neglecta EBD31643M]

Protein Classification

cytochrome c oxidase subunit II( domain architecture ID 11475897)

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-227 3.63e-148

cytochrome c oxidase subunit II; Validated


:

Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 411.42  E-value: 3.63e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250083844   1 MAYPFQLGLQDATSPIMEELMNFHDHALMIVFLISSLVLYIISAMLTTKLTHTSTMDAQAVETIWTI*******MIALPS 80
Cdd:MTH00098    1 MAYPFQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250083844  81 LRILYMMDEINNPTLTIKTVGHQWYWSYEYTDYDELNFDSYMIPTSELKPGNLRLLEVDNRAVLPMEMTIRVLVTSEDVL 160
Cdd:MTH00098   81 LRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2250083844 161 HSWAIPSLGLKT*******NQTTLLATRPGLYYGQCSEICGS******IVLELVPLKIFEKWSSSMI 227
Cdd:MTH00098  161 HSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKWSASML 227
 
Name Accession Description Interval E-value
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-227 3.63e-148

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 411.42  E-value: 3.63e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250083844   1 MAYPFQLGLQDATSPIMEELMNFHDHALMIVFLISSLVLYIISAMLTTKLTHTSTMDAQAVETIWTI*******MIALPS 80
Cdd:MTH00098    1 MAYPFQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250083844  81 LRILYMMDEINNPTLTIKTVGHQWYWSYEYTDYDELNFDSYMIPTSELKPGNLRLLEVDNRAVLPMEMTIRVLVTSEDVL 160
Cdd:MTH00098   81 LRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2250083844 161 HSWAIPSLGLKT*******NQTTLLATRPGLYYGQCSEICGS******IVLELVPLKIFEKWSSSMI 227
Cdd:MTH00098  161 HSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKWSASML 227
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 93-222 9.41e-73

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: 217.05  E-value: 9.41e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250083844  93 PTLTIKTVGHQWYWSYEYTDYDELNFDSYMIPTSELKPGNLRLLEVDNRAVLPMEMTIRVLVTSEDVLHSWAIPSLGLKT 172
Cdd:cd13912     1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2250083844 173 *******NQTTLLATRPGLYYGQCSEICGS******IVLELVPLKIFEKW 222
Cdd:cd13912    81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-214 1.95e-65

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 198.02  E-value: 1.95e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250083844  95 LTIKTVGHQWYWSYEYTDYDELNFDSYMIPTSELKPGNLRLLEVDNRAVLPMEMTIRVLVTSEDVLHSWAIPSLGLKT** 174
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2250083844 175 *****NQTTLLATRPGLYYGQCSEICGS******IVLELV 214
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
6-222 3.20e-32

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 116.85  E-value: 3.20e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250083844   6 QLGLQDATSPIMEELMNFHdhalMIVFLISSLVLYIISAML--------------TTKLTHTSTmdaqAVETIWTI**** 71
Cdd:COG1622    18 QLSLPDPAGPIAEEIDDLF----WVSLIIMLVIFVLVFGLLlyfairyrrrkgdaDPAQFHHNT----KLEIVWTVIPII 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250083844  72 ***MIALPSLRILYMMDEINNPTLTIKTVGHQWYWSYEYTDYDELnfdsymiptselkpgnlrlleVDNRAVLPMEMTIR 151
Cdd:COG1622    90 IVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIA---------------------TVNELVLPVGRPVR 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2250083844 152 VLVTSEDVLHSWAIPSLGLKT*******NQTTLLATRPGLYYGQCSEICGS******IVLELVPLKIFEKW 222
Cdd:COG1622   149 FLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAW 219
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 12-222 1.35e-27

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: 104.00  E-value: 1.35e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250083844  12 ATSPIMEELMNFHDHALMIVFLISSLVL-YIISAML----------TTKLTHTStmdaqAVETIWT-I*******MIALP 79
Cdd:TIGR02866   1 PGGEIAQQIAFLFLFVLAVSTLISLLVAaLLAYVVWkfrrkgdeekPSQIHGNR-----RLEYVWTvIPLIIVVGLFAAT 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250083844  80 SLRILYMMDEINNPTLTIKTVGHQWYWSYEYTDYdelnfdsymiptselkpgnlrLLEVDNRAVLPMEMTIRVLVTSEDV 159
Cdd:TIGR02866  76 AKGLLYLERPIPKDALKVKVTGYQWWWDFEYPES---------------------GFTTVNELVLPAGTPVELQVTSKDV 134

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2250083844 160 LHSWAIPSLGLKT*******NQTTLLATRPGLYYGQCSEICGS******IVLELVPLKIFEKW 222
Cdd:TIGR02866 135 IHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAY 197
 
Name Accession Description Interval E-value
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-227 3.63e-148

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 411.42  E-value: 3.63e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250083844   1 MAYPFQLGLQDATSPIMEELMNFHDHALMIVFLISSLVLYIISAMLTTKLTHTSTMDAQAVETIWTI*******MIALPS 80
Cdd:MTH00098    1 MAYPFQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250083844  81 LRILYMMDEINNPTLTIKTVGHQWYWSYEYTDYDELNFDSYMIPTSELKPGNLRLLEVDNRAVLPMEMTIRVLVTSEDVL 160
Cdd:MTH00098   81 LRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2250083844 161 HSWAIPSLGLKT*******NQTTLLATRPGLYYGQCSEICGS******IVLELVPLKIFEKWSSSMI 227
Cdd:MTH00098  161 HSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKWSASML 227
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-226 4.78e-134

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 375.79  E-value: 4.78e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250083844   1 MAYPFQLGLQDATSPIMEELMNFHDHALMIVFLISSLVLYIISAMLTTKLTHTSTMDAQAVETIWTI*******MIALPS 80
Cdd:MTH00117    1 MANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250083844  81 LRILYMMDEINNPTLTIKTVGHQWYWSYEYTDYDELNFDSYMIPTSELKPGNLRLLEVDNRAVLPMEMTIRVLVTSEDVL 160
Cdd:MTH00117   81 LRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2250083844 161 HSWAIPSLGLKT*******NQTTLLATRPGLYYGQCSEICGS******IVLELVPLKIFEKWSSSM 226
Cdd:MTH00117  161 HSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSLL 226
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 1-227 5.44e-122

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 345.55  E-value: 5.44e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250083844   1 MAYPFQLGLQDATSPIMEELMNFHDHALMIVFLISSLVLYIISAMLTTKLTHTSTMDAQAVETIWTI*******MIALPS 80
Cdd:MTH00129    1 MAHPSQLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250083844  81 LRILYMMDEINNPTLTIKTVGHQWYWSYEYTDYDELNFDSYMIPTSELKPGNLRLLEVDNRAVLPMEMTIRVLVTSEDVL 160
Cdd:MTH00129   81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2250083844 161 HSWAIPSLGLKT*******NQTTLLATRPGLYYGQCSEICGS******IVLELVPLKIFEKWSSSMI 227
Cdd:MTH00129  161 HSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLML 227
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 1-226 4.78e-121

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 342.91  E-value: 4.78e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250083844   1 MAYPFQLGLQDATSPIMEELMNFHDHALMIVFLISSLVLYIISAMLTTKLTHTSTMDAQAVETIWTI*******MIALPS 80
Cdd:MTH00076    1 MAHPSQLGFQDAASPIMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250083844  81 LRILYMMDEINNPTLTIKTVGHQWYWSYEYTDYDELNFDSYMIPTSELKPGNLRLLEVDNRAVLPMEMTIRVLVTSEDVL 160
Cdd:MTH00076   81 LRILYLMDEINDPHLTVKAIGHQWYWSYEYTDYEDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2250083844 161 HSWAIPSLGLKT*******NQTTLLATRPGLYYGQCSEICGS******IVLELVPLKIFEKWSSSM 226
Cdd:MTH00076  161 HSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLNWSSSM 226
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 1-227 5.29e-114

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 325.30  E-value: 5.29e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250083844   1 MAYPFQLGLQDATSPIMEELMNFHDHALMIVFLISSLVLYIISAMLTTKLTHTSTMDAQAVETIWTI*******MIALPS 80
Cdd:MTH00185    1 MAHPSQLGLQDAASPVMEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250083844  81 LRILYMMDEINNPTLTIKTVGHQWYWSYEYTDYDELNFDSYMIPTSELKPGNLRLLEVDNRAVLPMEMTIRVLVTSEDVL 160
Cdd:MTH00185   81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2250083844 161 HSWAIPSLGLKT*******NQTTLLATRPGLYYGQCSEICGS******IVLELVPLKIFEKWSSSMI 227
Cdd:MTH00185  161 HSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLML 227
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-227 3.24e-106

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 305.21  E-value: 3.24e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250083844   1 MAYPFQLGLQDATSPIMEELMNFHDHALMIVFLISSLVLYIISAMLTTKLTHTSTMDAQAVETIWTI*******MIALPS 80
Cdd:MTH00154    1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250083844  81 LRILYMMDEINNPTLTIKTVGHQWYWSYEYTDYDELNFDSYMIPTSELKPGNLRLLEVDNRAVLPMEMTIRVLVTSEDVL 160
Cdd:MTH00154   81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2250083844 161 HSWAIPSLGLKT*******NQTTLLATRPGLYYGQCSEICGS******IVLELVPLKIFEKWSSSMI 227
Cdd:MTH00154  161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNMS 227
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-227 1.15e-104

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 301.62  E-value: 1.15e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250083844   1 MAYPFQLGLQDATSPIMEELMNFHDHALMIVFLISSLVLYIISAMLTTKLTHTSTMDAQAVETIWTI*******MIALPS 80
Cdd:MTH00038    1 MATWLQLGLQDASSPLMEELIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250083844  81 LRILYMMDEINNPTLTIKTVGHQWYWSYEYTDYDELNFDSYMIPTSELKPGNLRLLEVDNRAVLPMEMTIRVLVTSEDVL 160
Cdd:MTH00038   81 LQLLYLMDEVNNPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2250083844 161 HSWAIPSLGLKT*******NQTTLLATRPGLYYGQCSEICGS******IVLELVPLKIFEKWSSSMI 227
Cdd:MTH00038  161 HSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVSNFL 227
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-225 4.47e-104

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 299.97  E-value: 4.47e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250083844   1 MAYPFQLGLQDATSPIMEELMNFHDHALMIVFLISSLVLYIISAMLTTKLTHTSTMDAQAVETIWTI*******MIALPS 80
Cdd:MTH00168    1 MATYSQLGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250083844  81 LRILYMMDEINNPTLTIKTVGHQWYWSYEYTDYDELNFDSYMIPTSELKPGNLRLLEVDNRAVLPMEMTIRVLVTSEDVL 160
Cdd:MTH00168   81 LRLLYLMDEIDKPDLTIKAVGHQWYWSYEYTDYNDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2250083844 161 HSWAIPSLGLKT*******NQTTLLATRPGLYYGQCSEICGS******IVLELVPLKIFEKWSSS 225
Cdd:MTH00168  161 HSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENWVDS 225
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-226 1.08e-99

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 288.76  E-value: 1.08e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250083844   1 MAYPFQLGLQDATSPIMEELMNFHDHALMIVFLISSLVLYIISAMLTTKLTHTSTMDAQAVETIWTI*******MIALPS 80
Cdd:MTH00140    1 MSYWGQLGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250083844  81 LRILYMMDEINNPTLTIKTVGHQWYWSYEYTDYDELNFDSYMIPTSELKPGNLRLLEVDNRAVLPMEMTIRVLVTSEDVL 160
Cdd:MTH00140   81 LRLLYLLDETNNPLLTVKAIGHQWYWSYEYSDFSVIEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2250083844 161 HSWAIPSLGLKT*******NQTTLLATRPGLYYGQCSEICGS******IVLELVPLKIFEKWSSSM 226
Cdd:MTH00140  161 HSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWLELM 226
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-225 5.65e-94

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 274.43  E-value: 5.65e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250083844   1 MAYPFQLGLQDATSPIMEELMNFHDHALMIVFLISSLVLYIISAMLTTKLTHTSTMDAQAVETIWTI*******MIALPS 80
Cdd:MTH00008    1 MPHWGQLMFQDAASPVMLQLISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250083844  81 LRILYMMDEINNPTLTIKTVGHQWYWSYEYTDYDELNFDSYMIPTSELKPGNLRLLEVDNRAVLPMEMTIRVLVTSEDVL 160
Cdd:MTH00008   81 LRLLYLMDEVSNPSITLKTIGHQWYWSYEYSDFSNLEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2250083844 161 HSWAIPSLGLKT*******NQTTLLATRPGLYYGQCSEICGS******IVLELVPLKIFEKWSSS 225
Cdd:MTH00008  161 HSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKWVSS 225
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-226 1.08e-93

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 273.52  E-value: 1.08e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250083844   1 MAYPFQLGLQDATSPIMEELMNFHDHALMIVFLISSLVLYIISAMLTTKLTHTSTMDAQAVETIWTI*******MIALPS 80
Cdd:MTH00139    1 MAYWGQLGFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250083844  81 LRILYMMDEINNPTLTIKTVGHQWYWSYEYTDYDELNFDSYMIPTSELKPGNLRLLEVDNRAVLPMEMTIRVLVTSEDVL 160
Cdd:MTH00139   81 LRLLYLMDEVSDPYLTFKAVGHQWYWSYEYSDFKNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2250083844 161 HSWAIPSLGLKT*******NQTTLLATRPGLYYGQCSEICGS******IVLELVPLKIFEKWSSSM 226
Cdd:MTH00139  161 HSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEWILEK 226
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 4-226 1.50e-86

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 255.86  E-value: 1.50e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250083844   4 PFQLGLQDATSPIMEELMNFHDHALMIVFLISSLVLYIISAMLTTKLTHTSTMDAQAVETIWTI*******MIALPSLRI 83
Cdd:MTH00051    6 PWQLGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSLKL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250083844  84 LYMMDEINNPTLTIKTVGHQWYWSYEYTDY--DELNFDSYMIPTSELKPGNLRLLEVDNRAVLPMEMTIRVLVTSEDVLH 161
Cdd:MTH00051   86 LYLMDEVIDPALTIKAIGHQWYWSYEYSDYgtDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLH 165

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2250083844 162 SWAIPSLGLKT*******NQTTLLATRPGLYYGQCSEICGS******IVLELVPLKIFEKWSSSM 226
Cdd:MTH00051  166 SFAVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINWVATQ 230
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 4-227 1.01e-85

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 253.90  E-value: 1.01e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250083844   4 PFQLGLQDATSPIMEELMNFHDHALMIVFLISSLVLYIISAMLTTKLTHTSTMDAQAVETIWTI*******MIALPSLRI 83
Cdd:MTH00023   13 PWQLGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKL 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250083844  84 LYMMDEINNPTLTIKTVGHQWYWSYEYTDYDE--LNFDSYMIPTSELKPGNLRLLEVDNRAVLPMEMTIRVLVTSEDVLH 161
Cdd:MTH00023   93 LYLMDEVVSPALTIKAIGHQWYWSYEYSDYEGetLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLH 172

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2250083844 162 SWAIPSLGLKT*******NQTTLLATRPGLYYGQCSEICGS******IVLELVPLKIFEKWSSSMI 227
Cdd:MTH00023  173 SFAVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWLLSLS 238
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 93-222 9.41e-73

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: 217.05  E-value: 9.41e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250083844  93 PTLTIKTVGHQWYWSYEYTDYDELNFDSYMIPTSELKPGNLRLLEVDNRAVLPMEMTIRVLVTSEDVLHSWAIPSLGLKT 172
Cdd:cd13912     1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2250083844 173 *******NQTTLLATRPGLYYGQCSEICGS******IVLELVPLKIFEKW 222
Cdd:cd13912    81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 4-222 3.52e-67

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 207.57  E-value: 3.52e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250083844   4 PFQLGLQDATSPIMEELMNFHDHALMIVFLISSLVLYIISAMLTTKLTHT---STMDAQAVETIWTI*******MIALPS 80
Cdd:MTH00027   32 PWQLGFQDAGSPVMEEIIMLHDQILFILTIIVGVVLWLIIRILLGNNYYSyywNKLDGSLIEVIWTLIPAFILILIAFPS 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250083844  81 LRILYMMDE-INNPTLTIKTVGHQWYWSYEYTDYDELN--FDSYMIPTSELKPGNLRLLEVDNRAVLPMEMTIRVLVTSE 157
Cdd:MTH00027  112 LRLLYIMDEcGFSANITIKVTGHQWYWSYSYEDYGEKNieFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAA 191

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2250083844 158 DVLHSWAIPSLGLKT*******NQTTLLATRPGLYYGQCSEICGS******IVLELVPLKIFEKW 222
Cdd:MTH00027  192 DVLHSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYIDW 256
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-214 1.95e-65

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 198.02  E-value: 1.95e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250083844  95 LTIKTVGHQWYWSYEYTDYDELNFDSYMIPTSELKPGNLRLLEVDNRAVLPMEMTIRVLVTSEDVLHSWAIPSLGLKT** 174
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2250083844 175 *****NQTTLLATRPGLYYGQCSEICGS******IVLELV 214
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 17-223 4.51e-56

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 178.28  E-value: 4.51e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250083844  17 MEELMNFHDHALMIVFLISSLVLYIISAMLTTKLTHTSTMDAQAVETIWTI*******MIALPSLRILYMMDEIN-NPTL 95
Cdd:MTH00080   19 MDWFHNFNCSLLFGEFVLAFVVFLFLYLISNNFYFKSKKIEYQFGELLCSVFPVLILLMQMVPSLSLLYYYGLMNlDSNL 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250083844  96 TIKTVGHQWYWSYEYTDYDELNFDSYMIPTSELKPGNLRLLEVDNRAVLPMEMTIRVLVTSEDVLHSWAIPSLGLKT*** 175
Cdd:MTH00080   99 TVKVTGHQWYWSYEFSDIPGLEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDAM 178

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2250083844 176 ****NQTTLLATRPGLYYGQCSEICGS******IVLELVPLKIFEKWS 223
Cdd:MTH00080  179 SGILSTLCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKEWC 226
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
6-222 3.20e-32

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 116.85  E-value: 3.20e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250083844   6 QLGLQDATSPIMEELMNFHdhalMIVFLISSLVLYIISAML--------------TTKLTHTSTmdaqAVETIWTI**** 71
Cdd:COG1622    18 QLSLPDPAGPIAEEIDDLF----WVSLIIMLVIFVLVFGLLlyfairyrrrkgdaDPAQFHHNT----KLEIVWTVIPII 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250083844  72 ***MIALPSLRILYMMDEINNPTLTIKTVGHQWYWSYEYTDYDELnfdsymiptselkpgnlrlleVDNRAVLPMEMTIR 151
Cdd:COG1622    90 IVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIA---------------------TVNELVLPVGRPVR 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2250083844 152 VLVTSEDVLHSWAIPSLGLKT*******NQTTLLATRPGLYYGQCSEICGS******IVLELVPLKIFEKW 222
Cdd:COG1622   149 FLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAW 219
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 12-222 1.35e-27

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: 104.00  E-value: 1.35e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250083844  12 ATSPIMEELMNFHDHALMIVFLISSLVL-YIISAML----------TTKLTHTStmdaqAVETIWT-I*******MIALP 79
Cdd:TIGR02866   1 PGGEIAQQIAFLFLFVLAVSTLISLLVAaLLAYVVWkfrrkgdeekPSQIHGNR-----RLEYVWTvIPLIIVVGLFAAT 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250083844  80 SLRILYMMDEINNPTLTIKTVGHQWYWSYEYTDYdelnfdsymiptselkpgnlrLLEVDNRAVLPMEMTIRVLVTSEDV 159
Cdd:TIGR02866  76 AKGLLYLERPIPKDALKVKVTGYQWWWDFEYPES---------------------GFTTVNELVLPAGTPVELQVTSKDV 134

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2250083844 160 LHSWAIPSLGLKT*******NQTTLLATRPGLYYGQCSEICGS******IVLELVPLKIFEKW 222
Cdd:TIGR02866 135 IHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAY 197
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 118-214 1.47e-26

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 100.28  E-value: 1.47e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250083844 118 FDSYMIPTSELKPGNLRLLEVDNRAVLPMEMTIRVLVTSEDVLHSWAIPSLGLKT*******NQTTLLATRPGLYYGQCS 197
Cdd:PTZ00047   51 FQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCS 130

                          90
                  ....*....|....*..
gi 2250083844 198 EICGS******IVLELV 214
Cdd:PTZ00047  131 EMCGTLHGFMPIVVEAV 147
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 57-214 7.10e-23

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 91.55  E-value: 7.10e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250083844  57 DAQAVETIWTI*******miaLPSLRILYM---------MDEINNPTLTIKTVGHQWYWSYEYTDydELNFDSYMIptse 127
Cdd:MTH00047   45 ENQVLELLWTV----------VPTLLVLVLcflnlnfitSDLDCFSSETIKVIGHQWYWSYEYSF--GGSYDSFMT---- 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250083844 128 lKPGNLrlleVDNRAVLPMEMTIRVLVTSEDVLHSWAIPSLGLKT*******NQTTLLATRPGLYYGQCSEICGS***** 207
Cdd:MTH00047  109 -DDIFG----VDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCPDRHGVFVGYCSELCGVGHSYM 183


                  ....*..
gi 2250083844 208 *IVLELV 214
Cdd:MTH00047  184 PIVIEVV 190
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-83 8.38e-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: 85.46  E-value: 8.38e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250083844   1 MAYPFQLGLQDATSPIMEELMNFHDHALMIVFLISSLVLYIISAMLTT------KLTHTSTMDAQAVETIWTI******* 74
Cdd:pfam02790   1 MPTPWGLGFQDAASPLMEGLLELHDYIMFILTLILILVLYILVTCLIRfnrrknPITARYTTHGQTIEIIWTIIPAVILI 80


                  ....*....
gi 2250083844  75 MIALPSLRI 83
Cdd:pfam02790  81 LIALPSFKL 89
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 95-202 1.32e-21

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: 85.43  E-value: 1.32e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250083844  95 LTIKTVGHQWYWSYEYTDydelnfdsymiptselkpgnlrlLEVDNRAVLPMEMTIRVLVTSEDVLHSWAIPSLGLKT** 174
Cdd:cd13842     1 LTVYVTGVQWSWTFIYPN-----------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDA 57

                          90       100
                  ....*....|....*....|....*...
gi 2250083844 175 *****NQTTLLATRPGLYYGQCSEICGS 202
Cdd:cd13842    58 VPGYTSELWFVADKPGTYTIICAEYCGL 85
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 94-201 2.87e-20

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: 81.90  E-value: 2.87e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250083844  94 TLTIKTVGHQWYWSYEYTDYDELNFDSymipTSELkpgnlrllevdnraVLPMEMTIRVLVTSEDVLHSWAIPSLGLKT* 173
Cdd:cd04213     1 ALTIEVTGHQWWWEFRYPDEPGRGIVT----ANEL--------------HIPVGRPVRLRLTSADVIHSFWVPSLAGKMD 62

                          90       100
                  ....*....|....*....|....*...
gi 2250083844 174 ******NQTTLLATRPGLYYGQCSEICG 201
Cdd:cd04213    63 MIPGRTNRLWLQADEPGVYRGQCAEFCG 90
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 94-201 1.50e-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: 259986 [Multi-domain]  Cd Length: 107  Bit Score: 72.29  E-value: 1.50e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250083844  94 TLTIKTVGHQWYWSYEYTDYDELNFDSYMIPTSELkpgnlrllevdnraVLPMEMTIRVLVTSEDVLHSWAIPSLGLKT* 173
Cdd:cd13919     1 ALVVEVTAQQWAWTFRYPGGDGKLGTDDDVTSPEL--------------HLPVGRPVLFNLRSKDVIHSFWVPEFRVKQD 66

                          90       100
                  ....*....|....*....|....*...
gi 2250083844 174 ******NQTTLLATRPGLYYGQCSEICG 201
Cdd:cd13919    67 AVPGRTTRLWFTPTREGEYEVRCAELCG 94
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 96-222 1.16e-11

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: 59.34  E-value: 1.16e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250083844  96 TIKTVGHQWYWSYEYTDYDELNFDSYMIPTselkpgnlrllevdNRAVlpmemTIRVlvTSEDVLHSWAIPSLGLKT*** 175
Cdd:cd13914     2 EIEVEAYQWGWEFSYPEANVTTSEQLVIPA--------------DRPV-----YFRI--TSRDVIHAFHVPELGLKQDAF 60

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2250083844 176 ****NQTTLLATRPGLYYGQCSEICGS******IVLELVPLKIFEKW 222
Cdd:cd13914    61 PGQYNTIKTEATEEGEYQLYCAEYCGAGHSQMLSTVTVVSQDEYQQW 107
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 94-201 7.89e-11

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: 56.87  E-value: 7.89e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250083844  94 TLTIKTVGHQWYWSYEYtdydelnfdsymiptselkPGNLRlleVDNRAVLPMEMTIRVLVTSEDVLHSWAIPSLGLKT* 173
Cdd:cd13915     1 ALEIQVTGRQWMWEFTY-------------------PNGKR---EINELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQD 58

                          90       100
                  ....*....|....*....|....*...
gi 2250083844 174 ******NQTTLLATRPGLYYGQCSEICG 201
Cdd:cd13915    59 VVPGRYTYLWFEATKPGEYDLFCTEYCG 86
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 88-222 1.60e-10

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: 57.08  E-value: 1.60e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2250083844  88 DEINNPTLTIKTVGHQWYWSYEYTD-YDELNfdsYMiptselkpgnlrllevdnraVLPMEMTIRVLVTSEDVLHSWAIP 166
Cdd:cd13918    26 DEADEDALEVEVEGFQFGWQFEYPNgVTTGN---TL--------------------RVPADTPIALRVTSTDVFHTFGIP 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2250083844 167 SLGLKT*******NQTTLLATRPGLYYGQCSEICGS******IVLELVPLKIFEKW 222
Cdd:cd13918    83 ELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEFEAW 138
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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