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Conserved domains on  [gi|1041576102|gb|ANO59330|]
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cytochrome oxidase subunit II, partial (mitochondrion) [Ateloplus schwarzi]

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
 1-198 6.40e-137

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 381.87  E-value: 6.40e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041576102   1 LMEQLIFFHDHTLFILLMITILVAYIMCSLMFNKFTHRYLLEGQTIEVIWTILPAITLIFIALPSLRLLYLLDESMDPLI 80
Cdd:MTH00154   16 LMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLYLLDEVNNPSI 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041576102  81 TVKTVGHQWYWSYEYTDFMNpYEFDSYMLPYNEMTSDGFRLLDVDNRTILPMNTPIRMLITAADVLHSWTVPALGVKVDA 160
Cdd:MTH00154   96 TLKTIGHQWYWSYEYSDFKN-IEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDA 174

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1041576102 161 TPGRLNQTSFFMNRPGLFYGQCSEICGANHSFMPIVIE 198
Cdd:MTH00154  175 VPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIE 212
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-198 6.40e-137

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 381.87  E-value: 6.40e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041576102   1 LMEQLIFFHDHTLFILLMITILVAYIMCSLMFNKFTHRYLLEGQTIEVIWTILPAITLIFIALPSLRLLYLLDESMDPLI 80
Cdd:MTH00154   16 LMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLYLLDEVNNPSI 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041576102  81 TVKTVGHQWYWSYEYTDFMNpYEFDSYMLPYNEMTSDGFRLLDVDNRTILPMNTPIRMLITAADVLHSWTVPALGVKVDA 160
Cdd:MTH00154   96 TLKTIGHQWYWSYEYSDFKN-IEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDA 174

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1041576102 161 TPGRLNQTSFFMNRPGLFYGQCSEICGANHSFMPIVIE 198
Cdd:MTH00154  175 VPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIE 212
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 78-198 8.02e-85

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: 246.33  E-value: 8.02e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041576102  78 PLITVKTVGHQWYWSYEYTDFmNPYEFDSYMLPYNEMTSDGFRLLDVDNRTILPMNTPIRMLITAADVLHSWTVPALGVK 157
Cdd:cd13912     1 PSLTIKAIGHQWYWSYEYSDF-NDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIK 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1041576102 158 VDATPGRLNQTSFFMNRPGLFYGQCSEICGANHSFMPIVIE 198
Cdd:cd13912    80 VDAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVE 120
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
80-198 8.14e-77

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 225.75  E-value: 8.14e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041576102  80 ITVKTVGHQWYWSYEYTDFMNpYEFDSYMLPYNEMTSDGFRLLDVDNRTILPMNTPIRMLITAADVLHSWTVPALGVKVD 159
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGD-LEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTD 79

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1041576102 160 ATPGRLNQTSFFMNRPGLFYGQCSEICGANHSFMPIVIE 198
Cdd:pfam00116  80 AVPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIE 118
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
11-198 1.21e-44

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 147.67  E-value: 1.21e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041576102  11 HTLFILLMITILVAYI-MCSLMF----------NKFTHRYLLEGQTIEVIWTILPAITLIFIALPSLRLLYLLDESMDPL 79
Cdd:COG1622    33 DDLFWVSLIIMLVIFVlVFGLLLyfairyrrrkGDADPAQFHHNTKLEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDP 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041576102  80 ITVKTVGHQWYWSYEYTDfmnpyefdsymlpYNEMTsdgfrlldvDNRTILPMNTPIRMLITAADVLHSWTVPALGVKVD 159
Cdd:COG1622   113 LTVEVTGYQWKWLFRYPD-------------QGIAT---------VNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQD 170

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1041576102 160 ATPGRLNQTSFFMNRPGLFYGQCSEICGANHSFMPIVIE 198
Cdd:COG1622   171 AIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVV 209
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 1-198 2.23e-37

cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of mitochondria (and one of several possible acceptors in prokaryotes) in the electron transport chain of aerobic respiration. The enzyme couples the oxidation of reduced cytochrome c with the reduction of molecular oxygen to water. This process results in the pumping of four protons across the membrane which are used in the proton gradient powered synthesis of ATP. The oxidase contains two heme a cofactors and three copper atoms as well as other bound ions. [Energy metabolism, Electron transport]


Pssm-ID: 274329 [Multi-domain]  Cd Length: 199  Bit Score: 128.27  E-value: 2.23e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041576102   1 LMEQLIFFHDHTLFILLMITILVAYIMCSLMFnKFTHR-------YLLEGQTIEVIWTILPAITLIFIALPSLRLLYLLD 73
Cdd:TIGR02866   5 IAQQIAFLFLFVLAVSTLISLLVAALLAYVVW-KFRRKgdeekpsQIHGNRRLEYVWTVIPLIIVVGLFAATAKGLLYLE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041576102  74 ESMDP-LITVKTVGHQWYWSYEYTDFmnpyefdsymlpynemtsdGFRlldVDNRTILPMNTPIRMLITAADVLHSWTVP 152
Cdd:TIGR02866  84 RPIPKdALKVKVTGYQWWWDFEYPES-------------------GFT---TVNELVLPAGTPVELQVTSKDVIHSFWVP 141

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1041576102 153 ALGVKVDATPGRLNQTSFFMNRPGLFYGQCSEICGANHSFMPIVIE 198
Cdd:TIGR02866 142 ELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVV 187
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-198 6.40e-137

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 381.87  E-value: 6.40e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041576102   1 LMEQLIFFHDHTLFILLMITILVAYIMCSLMFNKFTHRYLLEGQTIEVIWTILPAITLIFIALPSLRLLYLLDESMDPLI 80
Cdd:MTH00154   16 LMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLYLLDEVNNPSI 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041576102  81 TVKTVGHQWYWSYEYTDFMNpYEFDSYMLPYNEMTSDGFRLLDVDNRTILPMNTPIRMLITAADVLHSWTVPALGVKVDA 160
Cdd:MTH00154   96 TLKTIGHQWYWSYEYSDFKN-IEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDA 174

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1041576102 161 TPGRLNQTSFFMNRPGLFYGQCSEICGANHSFMPIVIE 198
Cdd:MTH00154  175 VPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIE 212
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-198 6.12e-110

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 313.80  E-value: 6.12e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041576102   1 LMEQLIFFHDHTLFILLMITILVAYIMCSLMFNKFTHRYLLEGQTIEVIWTILPAITLIFIALPSLRLLYLLDESMDPLI 80
Cdd:MTH00140   16 LMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPSLRLLYLLDETNNPLL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041576102  81 TVKTVGHQWYWSYEYTDFMNpYEFDSYMLPYNEMTSDGFRLLDVDNRTILPMNTPIRMLITAADVLHSWTVPALGVKVDA 160
Cdd:MTH00140   96 TVKAIGHQWYWSYEYSDFSV-IEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSADVIHSWTVPSLGVKVDA 174

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1041576102 161 TPGRLNQTSFFMNRPGLFYGQCSEICGANHSFMPIVIE 198
Cdd:MTH00140  175 IPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVE 212
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-198 7.24e-110

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 313.58  E-value: 7.24e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041576102   1 LMEQLIFFHDHTLFILLMITILVAYIMCSLMFNKFTHRYLLEGQTIEVIWTILPAITLIFIALPSLRLLYLLDESMDPLI 80
Cdd:MTH00139   16 LMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPSLRLLYLMDEVSDPYL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041576102  81 TVKTVGHQWYWSYEYTDFMNpYEFDSYMLPYNEMTSDGFRLLDVDNRTILPMNTPIRMLITAADVLHSWTVPALGVKVDA 160
Cdd:MTH00139   96 TFKAVGHQWYWSYEYSDFKN-LSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVLHSWTVPSLGVKIDA 174

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1041576102 161 TPGRLNQTSFFMNRPGLFYGQCSEICGANHSFMPIVIE 198
Cdd:MTH00139  175 VPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVE 212
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-198 1.04e-105

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 302.99  E-value: 1.04e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041576102   1 LMEQLIFFHDHTLFILLMITILVAYIMCSLMFNKFTHRYLLEGQTIEVIWTILPAITLIFIALPSLRLLYLLDESMDPLI 80
Cdd:MTH00117   16 IMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPSLRILYLMDEINNPHL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041576102  81 TVKTVGHQWYWSYEYTDFMNpYEFDSYMLPYNEMTSDGFRLLDVDNRTILPMNTPIRMLITAADVLHSWTVPALGVKVDA 160
Cdd:MTH00117   96 TIKAIGHQWYWSYEYTDYKD-LSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVLHSWAVPSLGVKTDA 174

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1041576102 161 TPGRLNQTSFFMNRPGLFYGQCSEICGANHSFMPIVIE 198
Cdd:MTH00117  175 VPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVE 212
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-198 1.38e-105

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 302.78  E-value: 1.38e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041576102   1 LMEQLIFFHDHTLFILLMITILVAYIMCSLMFNKFTHRYLLEGQTIEVIWTILPAITLIFIALPSLRLLYLLDESMDPLI 80
Cdd:MTH00038   16 LMEELIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPSLQLLYLMDEVNNPFL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041576102  81 TVKTVGHQWYWSYEYTDFmNPYEFDSYMLPYNEMTSDGFRLLDVDNRTILPMNTPIRMLITAADVLHSWTVPALGVKVDA 160
Cdd:MTH00038   96 TIKAIGHQWYWSYEYTDY-NDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVLHSWAVPSLGVKMDA 174

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1041576102 161 TPGRLNQTSFFMNRPGLFYGQCSEICGANHSFMPIVIE 198
Cdd:MTH00038  175 VPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIE 212
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-198 2.30e-104

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 299.46  E-value: 2.30e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041576102   1 LMEQLIFFHDHTLFILLMITILVAYIMCSLMFNKFTHRYLLEGQTIEVIWTILPAITLIFIALPSLRLLYLLDESMDPLI 80
Cdd:MTH00008   16 VMLQLISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPSLRLLYLMDEVSNPSI 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041576102  81 TVKTVGHQWYWSYEYTDFMNpYEFDSYMLPYNEMTSDGFRLLDVDNRTILPMNTPIRMLITAADVLHSWTVPALGVKVDA 160
Cdd:MTH00008   96 TLKTIGHQWYWSYEYSDFSN-LEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVIHSWTVPSLGVKVDA 174

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1041576102 161 TPGRLNQTSFFMNRPGLFYGQCSEICGANHSFMPIVIE 198
Cdd:MTH00008  175 VPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLE 212
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-198 7.92e-100

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 288.03  E-value: 7.92e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041576102   1 LMEQLIFFHDHTLFILLMITILVAYIMCSLMFNKFTHRYLLEGQTIEVIWTILPAITLIFIALPSLRLLYLLDESMDPLI 80
Cdd:MTH00168   16 VMEELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPSLRLLYLMDEIDKPDL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041576102  81 TVKTVGHQWYWSYEYTDFmNPYEFDSYMLPYNEMTSDGFRLLDVDNRTILPMNTPIRMLITAADVLHSWTVPALGVKVDA 160
Cdd:MTH00168   96 TIKAVGHQWYWSYEYTDY-NDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVLHSWTLPSLGLKMDA 174

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1041576102 161 TPGRLNQTSFFMNRPGLFYGQCSEICGANHSFMPIVIE 198
Cdd:MTH00168  175 VPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVE 212
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 2-198 5.77e-98

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 283.95  E-value: 5.77e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041576102   2 MEQLIFFHDHTLFILLMITILVAYIMCSLMFNKFTHRYLLEGQTIEVIWTILPAITLIFIALPSLRLLYLLDESMDPLIT 81
Cdd:MTH00023   26 MEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKLLYLMDEVVSPALT 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041576102  82 VKTVGHQWYWSYEYTDFMNP-YEFDSYMLPYNEMTSDGFRLLDVDNRTILPMNTPIRMLITAADVLHSWTVPALGVKVDA 160
Cdd:MTH00023  106 IKAIGHQWYWSYEYSDYEGEtLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSFAVPSLGLKIDA 185

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1041576102 161 TPGRLNQTSFFMNRPGLFYGQCSEICGANHSFMPIVIE 198
Cdd:MTH00023  186 VPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIE 223
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 1-198 1.35e-96

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 280.06  E-value: 1.35e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041576102   1 LMEQLIFFHDHTLFILLMITILVAYIMCSLMFNKFTHRYLLEGQTIEVIWTILPAITLIFIALPSLRLLYLLDESMDPLI 80
Cdd:MTH00129   16 VMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPSLRILYLMDEINDPHL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041576102  81 TVKTVGHQWYWSYEYTDFMNpYEFDSYMLPYNEMTSDGFRLLDVDNRTILPMNTPIRMLITAADVLHSWTVPALGVKVDA 160
Cdd:MTH00129   96 TIKAMGHQWYWSYEYTDYED-LGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVLHSWAVPALGVKMDA 174

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1041576102 161 TPGRLNQTSFFMNRPGLFYGQCSEICGANHSFMPIVIE 198
Cdd:MTH00129  175 VPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVE 212
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 1-198 1.49e-95

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 277.54  E-value: 1.49e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041576102   1 LMEQLIFFHDHTLFILLMITILVAYIMCSLMFNKFTHRYLLEGQTIEVIWTILPAITLIFIALPSLRLLYLLDESMDPLI 80
Cdd:MTH00185   16 VMEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPSLRILYLMDEINDPHL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041576102  81 TVKTVGHQWYWSYEYTDFmNPYEFDSYMLPYNEMTSDGFRLLDVDNRTILPMNTPIRMLITAADVLHSWTVPALGVKVDA 160
Cdd:MTH00185   96 TIKAMGHQWYWSYEYTDY-EQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVLHSWTVPALGVKMDA 174

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1041576102 161 TPGRLNQTSFFMNRPGLFYGQCSEICGANHSFMPIVIE 198
Cdd:MTH00185  175 VPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVE 212
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-198 2.42e-95

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 276.60  E-value: 2.42e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041576102   1 LMEQLIFFHDHTLFILLMITILVAYIMCSLMFNKFTHRYLLEGQTIEVIWTILPAITLIFIALPSLRLLYLLDESMDPLI 80
Cdd:MTH00098   16 IMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPSLRILYMMDEINNPSL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041576102  81 TVKTVGHQWYWSYEYTDFMNpYEFDSYMLPYNEMTSDGFRLLDVDNRTILPMNTPIRMLITAADVLHSWTVPALGVKVDA 160
Cdd:MTH00098   96 TVKTMGHQWYWSYEYTDYED-LSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVLHSWAVPSLGLKTDA 174

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1041576102 161 TPGRLNQTSFFMNRPGLFYGQCSEICGANHSFMPIVIE 198
Cdd:MTH00098  175 IPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLE 212
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 2-198 8.92e-94

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 272.81  E-value: 8.92e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041576102   2 MEQLIFFHDHTLFILLMITILVAYIMCSLMFNKFTHRYLLEGQTIEVIWTILPAITLIFIALPSLRLLYLLDESMDPLIT 81
Cdd:MTH00051   19 MEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSLKLLYLMDEVIDPALT 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041576102  82 VKTVGHQWYWSYEYTDF-MNPYEFDSYMLPYNEMTSDGFRLLDVDNRTILPMNTPIRMLITAADVLHSWTVPALGVKVDA 160
Cdd:MTH00051   99 IKAIGHQWYWSYEYSDYgTDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSFAVPSLSVKIDA 178

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1041576102 161 TPGRLNQTSFFMNRPGLFYGQCSEICGANHSFMPIVIE 198
Cdd:MTH00051  179 VPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIE 216
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 1-198 2.25e-93

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 271.65  E-value: 2.25e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041576102   1 LMEQLIFFHDHTLFILLMITILVAYIMCSLMFNKFTHRYLLEGQTIEVIWTILPAITLIFIALPSLRLLYLLDESMDPLI 80
Cdd:MTH00076   16 IMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPSLRILYLMDEINDPHL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041576102  81 TVKTVGHQWYWSYEYTDFMNpYEFDSYMLPYNEMTSDGFRLLDVDNRTILPMNTPIRMLITAADVLHSWTVPALGVKVDA 160
Cdd:MTH00076   96 TVKAIGHQWYWSYEYTDYED-LSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVLHSWAVPSLGIKTDA 174

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1041576102 161 TPGRLNQTSFFMNRPGLFYGQCSEICGANHSFMPIVIE 198
Cdd:MTH00076  175 IPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVE 212
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 78-198 8.02e-85

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: 246.33  E-value: 8.02e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041576102  78 PLITVKTVGHQWYWSYEYTDFmNPYEFDSYMLPYNEMTSDGFRLLDVDNRTILPMNTPIRMLITAADVLHSWTVPALGVK 157
Cdd:cd13912     1 PSLTIKAIGHQWYWSYEYSDF-NDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIK 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1041576102 158 VDATPGRLNQTSFFMNRPGLFYGQCSEICGANHSFMPIVIE 198
Cdd:cd13912    80 VDAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVE 120
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
80-198 8.14e-77

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 225.75  E-value: 8.14e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041576102  80 ITVKTVGHQWYWSYEYTDFMNpYEFDSYMLPYNEMTSDGFRLLDVDNRTILPMNTPIRMLITAADVLHSWTVPALGVKVD 159
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGD-LEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTD 79

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1041576102 160 ATPGRLNQTSFFMNRPGLFYGQCSEICGANHSFMPIVIE 198
Cdd:pfam00116  80 AVPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIE 118
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 1-198 4.39e-69

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 211.42  E-value: 4.39e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041576102   1 LMEQLIFFHDHTLFILLMITILVAYIMCSLMFNKFTHRYL---LEGQTIEVIWTILPAITLIFIALPSLRLLYLLDES-M 76
Cdd:MTH00027   44 VMEEIIMLHDQILFILTIIVGVVLWLIIRILLGNNYYSYYwnkLDGSLIEVIWTLIPAFILILIAFPSLRLLYIMDECgF 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041576102  77 DPLITVKTVGHQWYWSYEYTDFMNP-YEFDSYMLPYNEMTSDGFRLLDVDNRTILPMNTPIRMLITAADVLHSWTVPALG 155
Cdd:MTH00027  124 SANITIKVTGHQWYWSYSYEDYGEKnIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAADVLHSWTVPSLA 203

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1041576102 156 VKVDATPGRLNQTSFFMNRPGLFYGQCSEICGANHSFMPIVIE 198
Cdd:MTH00027  204 VKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVE 246
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 8-198 1.32e-59

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 185.98  E-value: 1.32e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041576102   8 FHDHTLFILLMITILVAYIMCSLMFNKFTHRYLLEGQTIEVIWTILPAITLIFIALPSLRLLYLLD-ESMDPLITVKTVG 86
Cdd:MTH00080   25 FNCSLLFGEFVLAFVVFLFLYLISNNFYFKSKKIEYQFGELLCSVFPVLILLMQMVPSLSLLYYYGlMNLDSNLTVKVTG 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041576102  87 HQWYWSYEYTDFMNpYEFDSYMLPYNEMTSDGFRLLDVDNRTILPMNTPIRMLITAADVLHSWTVPALGVKVDATPGRLN 166
Cdd:MTH00080  105 HQWYWSYEFSDIPG-LEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDAMSGILS 183

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1041576102 167 QTSFFMNRPGLFYGQCSEICGANHSFMPIVIE 198
Cdd:MTH00080  184 TLCYSFPMPGVFYGQCSEICGANHSFMPIAVE 215
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
11-198 1.21e-44

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 147.67  E-value: 1.21e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041576102  11 HTLFILLMITILVAYI-MCSLMF----------NKFTHRYLLEGQTIEVIWTILPAITLIFIALPSLRLLYLLDESMDPL 79
Cdd:COG1622    33 DDLFWVSLIIMLVIFVlVFGLLLyfairyrrrkGDADPAQFHHNTKLEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDP 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041576102  80 ITVKTVGHQWYWSYEYTDfmnpyefdsymlpYNEMTsdgfrlldvDNRTILPMNTPIRMLITAADVLHSWTVPALGVKVD 159
Cdd:COG1622   113 LTVEVTGYQWKWLFRYPD-------------QGIAT---------VNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQD 170

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1041576102 160 ATPGRLNQTSFFMNRPGLFYGQCSEICGANHSFMPIVIE 198
Cdd:COG1622   171 AIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVV 209
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 14-198 2.52e-44

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 145.87  E-value: 2.52e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041576102  14 FILLMITILVAYIMC----SLMFNKfthryllEGQTIEVIWTILPAItLIFIALPSLRLLYLLDESMDPLITVKTVGHQW 89
Cdd:MTH00047   20 FIPCWVYIMLCWQVVsgngSVNFGS-------ENQVLELLWTVVPTL-LVLVLCFLNLNFITSDLDCFSSETIKVIGHQW 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041576102  90 YWSYEYTdfmNPYEFDSYMlpynemTSDGFrllDVDNRTILPMNTPIRMLITAADVLHSWTVPALGVKVDATPGRLNQTS 169
Cdd:MTH00047   92 YWSYEYS---FGGSYDSFM------TDDIF---GVDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLF 159

                         170       180
                  ....*....|....*....|....*....
gi 1041576102 170 FFMNRPGLFYGQCSEICGANHSFMPIVIE 198
Cdd:MTH00047  160 FCPDRHGVFVGYCSELCGVGHSYMPIVIE 188
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 102-198 7.90e-39

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 130.71  E-value: 7.90e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041576102 102 YEFDSYMLPYNEMTSDGFRLLDVDNRTILPMNTPIRMLITAADVLHSWTVPALGVKVDATPGRLNQTSFFMNRPGLFYGQ 181
Cdd:PTZ00047   49 YSFQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQ 128

                          90
                  ....*....|....*..
gi 1041576102 182 CSEICGANHSFMPIVIE 198
Cdd:PTZ00047  129 CSEMCGTLHGFMPIVVE 145
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 1-198 2.23e-37

cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of mitochondria (and one of several possible acceptors in prokaryotes) in the electron transport chain of aerobic respiration. The enzyme couples the oxidation of reduced cytochrome c with the reduction of molecular oxygen to water. This process results in the pumping of four protons across the membrane which are used in the proton gradient powered synthesis of ATP. The oxidase contains two heme a cofactors and three copper atoms as well as other bound ions. [Energy metabolism, Electron transport]


Pssm-ID: 274329 [Multi-domain]  Cd Length: 199  Bit Score: 128.27  E-value: 2.23e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041576102   1 LMEQLIFFHDHTLFILLMITILVAYIMCSLMFnKFTHR-------YLLEGQTIEVIWTILPAITLIFIALPSLRLLYLLD 73
Cdd:TIGR02866   5 IAQQIAFLFLFVLAVSTLISLLVAALLAYVVW-KFRRKgdeekpsQIHGNRRLEYVWTVIPLIIVVGLFAATAKGLLYLE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041576102  74 ESMDP-LITVKTVGHQWYWSYEYTDFmnpyefdsymlpynemtsdGFRlldVDNRTILPMNTPIRMLITAADVLHSWTVP 152
Cdd:TIGR02866  84 RPIPKdALKVKVTGYQWWWDFEYPES-------------------GFT---TVNELVLPAGTPVELQVTSKDVIHSFWVP 141

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1041576102 153 ALGVKVDATPGRLNQTSFFMNRPGLFYGQCSEICGANHSFMPIVIE 198
Cdd:TIGR02866 142 ELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVV 187
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 80-198 9.87e-29

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: 102.76  E-value: 9.87e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041576102  80 ITVKTVGHQWYWSYEYTDfmnpyefdsymlpynemtsdgfrlLDVDNRTILPMNTPIRMLITAADVLHSWTVPALGVKVD 159
Cdd:cd13842     1 LTVYVTGVQWSWTFIYPN------------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVD 56

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1041576102 160 ATPGRLNQTSFFMNRPGLFYGQCSEICGANHSFMPIVIE 198
Cdd:cd13842    57 AVPGYTSELWFVADKPGTYTIICAEYCGLGHSYMLGKVE 95
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 80-193 1.82e-24

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


Pssm-ID: 259875 [Multi-domain]  Cd Length: 103  Bit Score: 91.91  E-value: 1.82e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041576102  80 ITVKTVGHQWYWSYEYTDfmnpyefdsymlpynemtSDGFRLLDVdNRTILPMNTPIRMLITAADVLHSWTVPALGVKVD 159
Cdd:cd04213     2 LTIEVTGHQWWWEFRYPD------------------EPGRGIVTA-NELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMD 62

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1041576102 160 ATPGRLNQTSFFMNRPGLFYGQCSEICGANHSFM 193
Cdd:cd04213    63 MIPGRTNRLWLQADEPGVYRGQCAEFCGASHALM 96
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 80-193 4.89e-21

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


Pssm-ID: 259982 [Multi-domain]  Cd Length: 98  Bit Score: 83.06  E-value: 4.89e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041576102  80 ITVKTVGHQWYWSYEYtdfmnpyefdsymlpynemtSDGFRlldVDNRTILPMNTPIRMLITAADVLHSWTVPALGVKVD 159
Cdd:cd13915     2 LEIQVTGRQWMWEFTY--------------------PNGKR---EINELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQD 58

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1041576102 160 ATPGRLNQTSFFMNRPGLFYGQCSEICGANHSFM 193
Cdd:cd13915    59 VVPGRYTYLWFEATKPGEYDLFCTEYCGTGHSGM 92
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 80-193 1.16e-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: 82.30  E-value: 1.16e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041576102  80 ITVKTVGHQWYWSYEYtdfmnpyefdsymlPyNEMTSDGFRLLDVDNRTILPMNTPIRMLITAADVLHSWTVPALGVKVD 159
Cdd:cd13919     2 LVVEVTAQQWAWTFRY--------------P-GGDGKLGTDDDVTSPELHLPVGRPVLFNLRSKDVIHSFWVPEFRVKQD 66

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1041576102 160 ATPGRLNQTSFFMNRPGLFYGQCSEICGANHSFM 193
Cdd:cd13919    67 AVPGRTTRLWFTPTREGEYEVRCAELCGLGHYRM 100
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-62 3.80e-19

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: 78.14  E-value: 3.80e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1041576102   1 LMEQLIFFHDHTLFILLMITILVAYIMCSLMF------NKFTHRYLLEGQTIEVIWTILPAITLIFIA 62
Cdd:pfam02790  16 LMEGLLELHDYIMFILTLILILVLYILVTCLIrfnrrkNPITARYTTHGQTIEIIWTIIPAVILILIA 83
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 77-193 4.19e-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: 76.73  E-value: 4.19e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041576102  77 DPLiTVKTVGHQWYWSYEYTdfmNPYEFDSYMlpynemtsdgfrlldvdnrtILPMNTPIRMLITAADVLHSWTVPALGV 156
Cdd:cd13918    31 DAL-EVEVEGFQFGWQFEYP---NGVTTGNTL--------------------RVPADTPIALRVTSTDVFHTFGIPELRV 86

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1041576102 157 KVDATPGRLNQTSFFMNRPGLFYGQCSEICGANHSFM 193
Cdd:cd13918    87 KADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLM 123
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 80-193 4.19e-17

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


Pssm-ID: 259981 [Multi-domain]  Cd Length: 108  Bit Score: 73.21  E-value: 4.19e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041576102  80 ITVKTVGHQWYWSYEYTDFMNpyefdsymlpynemtsdgfrllDVDNRTILPMNTPIRMLITAADVLHSWTVPALGVKVD 159
Cdd:cd13914     1 VEIEVEAYQWGWEFSYPEANV----------------------TTSEQLVIPADRPVYFRITSRDVIHAFHVPELGLKQD 58

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1041576102 160 ATPGRLNQTSFFMNRPGLFYGQCSEICGANHSFM 193
Cdd:cd13914    59 AFPGQYNTIKTEATEEGEYQLYCAEYCGAGHSQM 92
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 130-193 7.72e-09

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: 51.03  E-value: 7.72e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1041576102 130 LPMNTPIRMLITAADVLHSWTVPALGVKVDATPGRLNQTSFFMNRPGLFYGQCSEICGANHSFM 193
Cdd:cd13913    29 VPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNM 92
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 126-193 2.14e-06

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


Pssm-ID: 259874 [Multi-domain]  Cd Length: 99  Bit Score: 44.46  E-value: 2.14e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1041576102 126 NRTILPMNTPIRMLITAADVLHSWTVPALGVKVDATPGRLNQTSFFMNRPGLFYGQCSEICGANHSFM 193
Cdd:cd04212    25 NELVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGTYQGLSANYSGEGFSDM 92
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 80-193 8.44e-06

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: 42.75  E-value: 8.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041576102  80 ITVKTVGHQWYWsyeytdfmnpyefdsymlpynEMTsdgfrlldvdnRTILPMNTPIRMLITAADVLHSWTV--PALGV- 156
Cdd:cd13916     1 QVVAVTGHQWYW---------------------ELS-----------RTEIPAGKPVEFRVTSADVNHGFGIydPDMRLl 48

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1041576102 157 -KVDATPGRLNQTSFFMNRPGLFYGQCSEICGANHSFM 193
Cdd:cd13916    49 aQTQAMPGYTNVLRYTFDKPGTYTILCLEYCGLAHHVM 86
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 107-198 1.21e-04

Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in inter-molecular electron transfer reactions. Cupredoxins are blue copper proteins, having an intense blue color due to the presence of a mononuclear type 1 (T1) copper site. Structurally, the cupredoxin-like fold consists of a beta-sandwich with 7 strands in 2 beta-sheets, which is arranged in a Greek-key beta-barrel. Some of these proteins have lost the ability to bind copper. The majority of family members contain multiple cupredoxin domain repeats: ceruloplasmin and the coagulation factors V/VIII have six repeats; laccase, ascorbate oxidase, spore coat protein A, and multicopper oxidase CueO contain three repeats; and nitrite reductase has two repeats. Others are mono-domain cupredoxins, such as plastocyanin, pseudoazurin, plantacyanin, azurin, rusticyanin, stellacyanin, quinol oxidase, and the periplasmic domain of cytochrome c oxidase subunit II.


Pssm-ID: 259860 [Multi-domain]  Cd Length: 110  Bit Score: 39.91  E-value: 1.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041576102 107 YMLPYNEMTSDGFRLLDVDNRTILPMNTPIRMLIT-AADVLHSWTVPALGVKVDA---------------TPGRLNQTSF 170
Cdd:cd00920     4 TASDWGWSFTYNGVLLFGPPVLVVPVGDTVRVQFVnKLGENHSVTIAGFGVPVVAmagganpglvntlviGPGESAEVTF 83

                          90       100
                  ....*....|....*....|....*...
gi 1041576102 171 FMNRPGLFYGQCSEICGaNHSFMPIVIE 198
Cdd:cd00920    84 TTDQAGVYWFYCTIPGH-NHAGMVGTIN 110
PRK10525 PRK10525
cytochrome o ubiquinol oxidase subunit II; Provisional
 48-193 1.83e-03

cytochrome o ubiquinol oxidase subunit II; Provisional


Pssm-ID: 182518 [Multi-domain]  Cd Length: 315  Bit Score: 38.24  E-value: 1.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1041576102  48 VIWTIlPAITLIFIALPSLRLLYLLDESmDPL------ITVKTVGHQWYWSYEYTDfmnpyefdSYMLPYNEMTsdgfrl 121
Cdd:PRK10525   91 VVWTV-PILIIIFLAVLTWKTTHALEPS-KPLahdekpITIEVVSMDWKWFFIYPE--------QGIATVNEIA------ 154

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1041576102 122 ldvdnrtiLPMNTPIRMLITAADVLHSWTVPALGVKVDATPGRLNQTSFFMNRPGLFYGQCSEICGANHSFM 193
Cdd:PRK10525  155 --------FPANVPVYFKVTSNSVMNSFFIPRLGSQIYAMAGMQTRLHLIANEPGTYDGISASYSGPGFSGM 218
 
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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