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Conserved domains on  [gi|19857059|sp|P21534|]
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RecName: Full=Cytochrome c oxidase subunit 2; AltName: Full=Cytochrome c oxidase polypeptide II

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
 13-248 4.12e-100

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 290.96  E-value: 4.12e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19857059   13 SSWA-LYFQDGASPSYLGVTHLNDYLMFYLTFIFIGVIYAICKAVIEYNYNshpiaaKYTTHGSIVEFIWTLIPALILIL 91
Cdd:MTH00154   2 ATWSnLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTN------RFLLEGQEIEIIWTILPAIILIF 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19857059   92 VALPSFKLLYLLDEVQKPSMTVKAIGRQWFWTYELNDFVTnenepVSFDSYMVPEEDLEEGSLRQLEVDNRLVLPIDTRI 171
Cdd:MTH00154  76 IALPSLRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKN-----IEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQI 150

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19857059  172 RLILTSGDVIHSWAVPSLGIKCDCIPGRLNQVSLSIDREGLFYGQCSELCGVLHSSMPIVVQGVSLEDFLAWLEENS 248
Cdd:MTH00154 151 RILITAADVIHSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNMS 227
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 13-248 4.12e-100

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 290.96  E-value: 4.12e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19857059   13 SSWA-LYFQDGASPSYLGVTHLNDYLMFYLTFIFIGVIYAICKAVIEYNYNshpiaaKYTTHGSIVEFIWTLIPALILIL 91
Cdd:MTH00154   2 ATWSnLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTN------RFLLEGQEIEIIWTILPAIILIF 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19857059   92 VALPSFKLLYLLDEVQKPSMTVKAIGRQWFWTYELNDFVTnenepVSFDSYMVPEEDLEEGSLRQLEVDNRLVLPIDTRI 171
Cdd:MTH00154  76 IALPSLRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKN-----IEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQI 150

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19857059  172 RLILTSGDVIHSWAVPSLGIKCDCIPGRLNQVSLSIDREGLFYGQCSELCGVLHSSMPIVVQGVSLEDFLAWLEENS 248
Cdd:MTH00154 151 RILITAADVIHSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNMS 227
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 109-243 1.01e-87

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


Pssm-ID: 259979 [Multi-domain]  Cd Length: 130  Bit Score: 255.96  E-value: 1.01e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19857059 109 PSMTVKAIGRQWFWTYELNDFVTnenepVSFDSYMVPEEDLEEGSLRQLEVDNRLVLPIDTRIRLILTSGDVIHSWAVPS 188
Cdd:cd13912   1 PSLTIKAIGHQWYWSYEYSDFND-----LEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPS 75

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 19857059 189 LGIKCDCIPGRLNQVSLSIDREGLFYGQCSELCGVLHSSMPIVVQGVSLEDFLAW 243
Cdd:cd13912  76 LGIKVDAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
111-235 1.08e-80

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 237.69  E-value: 1.08e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19857059   111 MTVKAIGRQWFWTYELNDFVTnenepVSFDSYMVPEEDLEEGSLRQLEVDNRLVLPIDTRIRLILTSGDVIHSWAVPSLG 190
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGD-----LEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLG 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 19857059   191 IKCDCIPGRLNQVSLSIDREGLFYGQCSELCGVLHSSMPIVVQGV 235
Cdd:pfam00116  76 IKTDAVPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
14-246 2.97e-67

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 207.37  E-value: 2.97e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19857059  14 SWALYFQDGASPSYLGVTHLNDYLMFYLTFIFIGVIYAICKAVIEYNYNSHPIAAKYTTHGSIVEFIWTLIPALILILVA 93
Cdd:COG1622  16 SGQLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLLLYFAIRYRRRKGDADPAQFHHNTKLEIVWTVIPIIIVIVLA 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19857059  94 LPSFKLLYLLDEVQKPSMTVKAIGRQWFWTYElndfvtnenepvsfdsYmvpeedLEEGSLrqleVDNRLVLPIDTRIRL 173
Cdd:COG1622  96 VPTLRVLHALDDAPEDPLTVEVTGYQWKWLFR----------------Y------PDQGIA----TVNELVLPVGRPVRF 149

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19857059 174 ILTSGDVIHSWAVPSLGIKCDCIPGRLNQVSLSIDREGLFYGQCSELCGVLHSSMPIVVQGVSLEDFLAWLEE 246
Cdd:COG1622 150 LLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAE 222
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 33-245 2.26e-46

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: 153.31  E-value: 2.26e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19857059    33 LNDYLMFYLTFIFIGVIYAICKAVIEYNYNSHPIAAKYTTHGSIVEFIWTLIPALILI-LVALPSFKLLYLLDEVQKPSM 111
Cdd:TIGR02866  12 LFLFVLAVSTLISLLVAALLAYVVWKFRRKGDEEKPSQIHGNRRLEYVWTVIPLIIVVgLFAATAKGLLYLERPIPKDAL 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19857059   112 TVKAIGRQWFWTYelndfvtnenepvsfdsymvpeeDLEEGSLRqleVDNRLVLPIDTRIRLILTSGDVIHSWAVPSLGI 191
Cdd:TIGR02866  92 KVKVTGYQWWWDF-----------------------EYPESGFT---TVNELVLPAGTPVELQVTSKDVIHSFWVPELGG 145

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 19857059   192 KCDCIPGRLNQVSLSIDREGLFYGQCSELCGVLHSSMPIVVQGVSLEDFLAWLE 245
Cdd:TIGR02866 146 KIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYVE 199
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 13-248 4.12e-100

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 290.96  E-value: 4.12e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19857059   13 SSWA-LYFQDGASPSYLGVTHLNDYLMFYLTFIFIGVIYAICKAVIEYNYNshpiaaKYTTHGSIVEFIWTLIPALILIL 91
Cdd:MTH00154   2 ATWSnLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTN------RFLLEGQEIEIIWTILPAIILIF 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19857059   92 VALPSFKLLYLLDEVQKPSMTVKAIGRQWFWTYELNDFVTnenepVSFDSYMVPEEDLEEGSLRQLEVDNRLVLPIDTRI 171
Cdd:MTH00154  76 IALPSLRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKN-----IEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQI 150

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19857059  172 RLILTSGDVIHSWAVPSLGIKCDCIPGRLNQVSLSIDREGLFYGQCSELCGVLHSSMPIVVQGVSLEDFLAWLEENS 248
Cdd:MTH00154 151 RILITAADVIHSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNMS 227
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 13-245 2.14e-95

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 278.75  E-value: 2.14e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19857059   13 SSW-ALYFQDGASPSYLGVTHLNDYLMFYLTFIFIGVIYAICKAVIeynyNSHpiAAKYTTHGSIVEFIWTLIPALILIL 91
Cdd:MTH00140   2 SYWgQLGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLF----NKF--SCRTILEAQKLETIWTIVPALILVF 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19857059   92 VALPSFKLLYLLDEVQKPSMTVKAIGRQWFWTYELNDFVTnenepVSFDSYMVPEEDLEEGSLRQLEVDNRLVLPIDTRI 171
Cdd:MTH00140  76 LALPSLRLLYLLDETNNPLLTVKAIGHQWYWSYEYSDFSV-----IEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDT 150

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19857059  172 RLILTSGDVIHSWAVPSLGIKCDCIPGRLNQVSLSIDREGLFYGQCSELCGVLHSSMPIVVQGVSLEDFLAWLE 245
Cdd:MTH00140 151 RVLVTSADVIHSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWLE 224
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 17-244 4.61e-95

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 278.02  E-value: 4.61e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19857059   17 LYFQDGASPSYLGVTHLNDYLMFYLTFIFIGVIYAIckAVIeynYNSHPIAAKYTThGSIVEFIWTLIPALILILVALPS 96
Cdd:MTH00168   7 LGLQDAASPVMEELILFHDHALLILVLILTLVLYSL--LVL---VTSKYTNRFLLD-SQMIEFVWTIIPAFILISLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19857059   97 FKLLYLLDEVQKPSMTVKAIGRQWFWTYELNDFvtnenEPVSFDSYMVPEEDLEEGSLRQLEVDNRLVLPIDTRIRLILT 176
Cdd:MTH00168  81 LRLLYLMDEIDKPDLTIKAVGHQWYWSYEYTDY-----NDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVT 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19857059  177 SGDVIHSWAVPSLGIKCDCIPGRLNQVSLSIDREGLFYGQCSELCGVLHSSMPIVVQGVSLEDFLAWL 244
Cdd:MTH00168 156 SADVLHSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENWV 223
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 4-244 7.03e-95

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 278.17  E-value: 7.03e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19857059    4 FNSIL-NDAPSSWALYFQDGASPSYLGVTHLNDYLMFYLTFIFIGVIYAICKAVIEYNYNshpiaaKYTTHGSIVEFIWT 82
Cdd:MTH00023   2 FNNFFyRDIPEPWQLGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYD------RFLVDGTFLEIVWT 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19857059   83 LIPALILILVALPSFKLLYLLDEVQKPSMTVKAIGRQWFWTYELNDFvtnENEPVSFDSYMVPEEDLEEGSLRQLEVDNR 162
Cdd:MTH00023  76 IIPAVILVFIALPSLKLLYLMDEVVSPALTIKAIGHQWYWSYEYSDY---EGETLEFDSYMVPTSDLNSGDFRLLEVDNR 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19857059  163 LVLPIDTRIRLILTSGDVIHSWAVPSLGIKCDCIPGRLNQVSLSIDREGLFYGQCSELCGVLHSSMPIVVQGVSLEDFLA 242
Cdd:MTH00023 153 LVVPINTHVRILVTGADVLHSFAVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYIN 232


                 ..
gi 19857059  243 WL 244
Cdd:MTH00023 233 WL 234
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 17-248 3.32e-94

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 276.02  E-value: 3.32e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19857059   17 LYFQDGASPSYLGVTHLNDYLMFYLTFIFIGVIYAICKAVIEYNYNSHpiaakyTTHGSIVEFIWTLIPALILILVALPS 96
Cdd:MTH00117   7 LGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTN------TVDAQEVELIWTILPAIVLILLALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19857059   97 FKLLYLLDEVQKPSMTVKAIGRQWFWTYELNDFvtnenEPVSFDSYMVPEEDLEEGSLRQLEVDNRLVLPIDTRIRLILT 176
Cdd:MTH00117  81 LRILYLMDEINNPHLTIKAIGHQWYWSYEYTDY-----KDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILIT 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19857059  177 SGDVIHSWAVPSLGIKCDCIPGRLNQVSLSIDREGLFYGQCSELCGVLHSSMPIVVQGVSLEDFLAWLEENS 248
Cdd:MTH00117 156 AEDVLHSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSLLS 227
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 9-245 2.60e-93

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 273.97  E-value: 2.60e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19857059    9 NDAPSSWALYFQDGASPSYLGVTHLNDYLMFYLTFIFIGVIYAICKAVIEYNYNshpiaaKYTTHGSIVEFIWTLIPALI 88
Cdd:MTH00051   1 KDAPEPWQLGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYH------KYLFEGTLIEIIWTLIPAAI 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19857059   89 LILVALPSFKLLYLLDEVQKPSMTVKAIGRQWFWTYELNDFVTnenEPVSFDSYMVPEEDLEEGSLRQLEVDNRLVLPID 168
Cdd:MTH00051  75 LIFIAFPSLKLLYLMDEVIDPALTIKAIGHQWYWSYEYSDYGT---DTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQ 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19857059  169 TRIRLILTSGDVIHSWAVPSLGIKCDCIPGRLNQVSLSIDREGLFYGQCSELCGVLHSSMPIVVQGVSLEDFLAWLE 245
Cdd:MTH00051 152 TQVRVLVTAADVLHSFAVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINWVA 228
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 13-248 9.87e-92

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 269.65  E-value: 9.87e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19857059   13 SSWA-LYFQDGASPSYLGVTHLNDYLMFYLTFIFIGVIYAIckAVIEYNYNSHpiaaKYTTHGSIVEFIWTLIPALILIL 91
Cdd:MTH00038   2 ATWLqLGLQDASSPLMEELIYFHDYALIILTLITILVFYGL--ASLLFSSPTN----RFFLEGQELETIWTIVPAFILIF 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19857059   92 VALPSFKLLYLLDEVQKPSMTVKAIGRQWFWTYELNDFvtNENEpvsFDSYMVPEEDLEEGSLRQLEVDNRLVLPIDTRI 171
Cdd:MTH00038  76 IALPSLQLLYLMDEVNNPFLTIKAIGHQWYWSYEYTDY--NDLE---FDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPI 150

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19857059  172 RLILTSGDVIHSWAVPSLGIKCDCIPGRLNQVSLSIDREGLFYGQCSELCGVLHSSMPIVVQGVSLEDFLAWLEENS 248
Cdd:MTH00038 151 RVLVSSADVLHSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVSNFL 227
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 13-246 1.83e-88

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 261.19  E-value: 1.83e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19857059   13 SSWA-LYFQDGASPSYLGVTHLNDYLMFYLTFIFIGVIYAICKAVieynYNShpIAAKYTTHGSIVEFIWTLIPALILIL 91
Cdd:MTH00139   2 AYWGqLGFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLM----SNK--FTSRSLLESQEVETIWTVLPAFILLF 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19857059   92 VALPSFKLLYLLDEVQKPSMTVKAIGRQWFWTYELNDFvtnenEPVSFDSYMVPEEDLEEGSLRQLEVDNRLVLPIDTRI 171
Cdd:MTH00139  76 LALPSLRLLYLMDEVSDPYLTFKAVGHQWYWSYEYSDF-----KNLSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNI 150

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19857059  172 RLILTSGDVIHSWAVPSLGIKCDCIPGRLNQVSLSIDREGLFYGQCSELCGVLHSSMPIVVQGVSLEDFLAWLEE 246
Cdd:MTH00139 151 RALITAADVLHSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEWILE 225
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 109-243 1.01e-87

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


Pssm-ID: 259979 [Multi-domain]  Cd Length: 130  Bit Score: 255.96  E-value: 1.01e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19857059 109 PSMTVKAIGRQWFWTYELNDFVTnenepVSFDSYMVPEEDLEEGSLRQLEVDNRLVLPIDTRIRLILTSGDVIHSWAVPS 188
Cdd:cd13912   1 PSLTIKAIGHQWYWSYEYSDFND-----LEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPS 75

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 19857059 189 LGIKCDCIPGRLNQVSLSIDREGLFYGQCSELCGVLHSSMPIVVQGVSLEDFLAW 243
Cdd:cd13912  76 LGIKVDAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 17-243 2.64e-84

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 250.79  E-value: 2.64e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19857059   17 LYFQDGASPSYLGVTHLNDYLMFYLTFIFIGVIYAIckavieynynSHPIAAKYTtHGSI-----VEFIWTLIPALILIL 91
Cdd:MTH00098   7 LGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYII----------SLMLTTKLT-HTSTmdaqeVETIWTILPAIILIL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19857059   92 VALPSFKLLYLLDEVQKPSMTVKAIGRQWFWTYELNDFvtnenEPVSFDSYMVPEEDLEEGSLRQLEVDNRLVLPIDTRI 171
Cdd:MTH00098  76 IALPSLRILYMMDEINNPSLTVKTMGHQWYWSYEYTDY-----EDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPI 150

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19857059  172 RLILTSGDVIHSWAVPSLGIKCDCIPGRLNQVSLSIDREGLFYGQCSELCGVLHSSMPIVVQGVSLEDFLAW 243
Cdd:MTH00098 151 RMLISSEDVLHSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKW 222
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 17-244 6.77e-84

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 249.70  E-value: 6.77e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19857059   17 LYFQDGASPSYLGVTHLNDYLMFYLTFIFIGVIYAICKAVIEYNYNSHPIAAKYtthgsiVEFIWTLIPALILILVALPS 96
Cdd:MTH00076   7 LGFQDAASPIMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQE------IEMVWTIMPAIILIVIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19857059   97 FKLLYLLDEVQKPSMTVKAIGRQWFWTYELNDFvtnenEPVSFDSYMVPEEDLEEGSLRQLEVDNRLVLPIDTRIRLILT 176
Cdd:MTH00076  81 LRILYLMDEINDPHLTVKAIGHQWYWSYEYTDY-----EDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLIT 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19857059  177 SGDVIHSWAVPSLGIKCDCIPGRLNQVSLSIDREGLFYGQCSELCGVLHSSMPIVVQGVSLEDFLAWL 244
Cdd:MTH00076 156 AEDVLHSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLNWS 223
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 13-248 1.25e-81

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 244.00  E-value: 1.25e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19857059   13 SSWA-LYFQDGASPSYLGVTHLNDYLMFYLTFIFIGVIYAICKAVIEYNYNshpiaaKYTTHGSIVEFIWTLIPALILIL 91
Cdd:MTH00008   2 PHWGqLMFQDAASPVMLQLISFHDHALLILTLVLTVVGYAMTSLMFNKLSN------RYILEAQQIETIWTILPALILLF 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19857059   92 VALPSFKLLYLLDEVQKPSMTVKAIGRQWFWTYELNDFVTnenepVSFDSYMVPEEDLEEGSLRQLEVDNRLVLPIDTRI 171
Cdd:MTH00008  76 LAFPSLRLLYLMDEVSNPSITLKTIGHQWYWSYEYSDFSN-----LEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEI 150

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19857059  172 RLILTSGDVIHSWAVPSLGIKCDCIPGRLNQVSLSIDREGLFYGQCSELCGVLHSSMPIVVQGVSLEDFLAWLEENS 248
Cdd:MTH00008 151 RVLVTAADVIHSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKWVSSFA 227
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 17-243 3.68e-81

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 243.08  E-value: 3.68e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19857059   17 LYFQDGASPSYLGVTHLNDYLMFYLTFIFIGVIYAICKAVieynynSHPIAAKYTTHGSIVEFIWTLIPALILILVALPS 96
Cdd:MTH00129   7 LGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMV------STKLTNKYILDSQEIEIIWTVLPAVILILIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19857059   97 FKLLYLLDEVQKPSMTVKAIGRQWFWTYELNDFvtnenEPVSFDSYMVPEEDLEEGSLRQLEVDNRLVLPIDTRIRLILT 176
Cdd:MTH00129  81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDY-----EDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVS 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19857059  177 SGDVIHSWAVPSLGIKCDCIPGRLNQVSLSIDREGLFYGQCSELCGVLHSSMPIVVQGVSLEDFLAW 243
Cdd:MTH00129 156 AEDVLHSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFENW 222
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
111-235 1.08e-80

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 237.69  E-value: 1.08e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19857059   111 MTVKAIGRQWFWTYELNDFVTnenepVSFDSYMVPEEDLEEGSLRQLEVDNRLVLPIDTRIRLILTSGDVIHSWAVPSLG 190
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGD-----LEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLG 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 19857059   191 IKCDCIPGRLNQVSLSIDREGLFYGQCSELCGVLHSSMPIVVQGV 235
Cdd:pfam00116  76 IKTDAVPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 17-243 3.64e-78

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 235.16  E-value: 3.64e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19857059   17 LYFQDGASPSYLGVTHLNDYLMFYLTFIFIGVIYAICKAVieynynSHPIAAKYTTHGSIVEFIWTLIPALILILVALPS 96
Cdd:MTH00185   7 LGLQDAASPVMEELIHFHDHTLMIVFLISTLVLYIIVAMV------TTKLTNKYILDSQEIEIVWTILPAIILIMIALPS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19857059   97 FKLLYLLDEVQKPSMTVKAIGRQWFWTYELNDFvtnenEPVSFDSYMVPEEDLEEGSLRQLEVDNRLVLPIDTRIRLILT 176
Cdd:MTH00185  81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDY-----EQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLIT 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19857059  177 SGDVIHSWAVPSLGIKCDCIPGRLNQVSLSIDREGLFYGQCSELCGVLHSSMPIVVQGVSLEDFLAW 243
Cdd:MTH00185 156 AEDVLHSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENW 222
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 6-244 1.13e-73

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 224.90  E-value: 1.13e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19857059    6 SILNDAPSSWALYFQDGASPSYLGVTHLNDYLMFYLTFIFIGVIYAICKAVIEYNYNSHpiaAKYTTHGSIVEFIWTLIP 85
Cdd:MTH00027  24 SMIKDANEPWQLGFQDAGSPVMEEIIMLHDQILFILTIIVGVVLWLIIRILLGNNYYSY---YWNKLDGSLIEVIWTLIP 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19857059   86 ALILILVALPSFKLLYLLDE-VQKPSMTVKAIGRQWFWTYELNDFvtnENEPVSFDSYMVPEEDLEEGSLRQLEVDNRLV 164
Cdd:MTH00027 101 AFILILIAFPSLRLLYIMDEcGFSANITIKVTGHQWYWSYSYEDY---GEKNIEFDSYMIPTADLEFGDLRLLEVDNRLI 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19857059  165 LPIDTRIRLILTSGDVIHSWAVPSLGIKCDCIPGRLNQVSLSIDREGLFYGQCSELCGVLHSSMPIVVQGVSLEDFLAWL 244
Cdd:MTH00027 178 LPVDTNVRVLITAADVLHSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYIDWI 257
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
14-246 2.97e-67

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 207.37  E-value: 2.97e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19857059  14 SWALYFQDGASPSYLGVTHLNDYLMFYLTFIFIGVIYAICKAVIEYNYNSHPIAAKYTTHGSIVEFIWTLIPALILILVA 93
Cdd:COG1622  16 SGQLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLLLYFAIRYRRRKGDADPAQFHHNTKLEIVWTVIPIIIVIVLA 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19857059  94 LPSFKLLYLLDEVQKPSMTVKAIGRQWFWTYElndfvtnenepvsfdsYmvpeedLEEGSLrqleVDNRLVLPIDTRIRL 173
Cdd:COG1622  96 VPTLRVLHALDDAPEDPLTVEVTGYQWKWLFR----------------Y------PDQGIA----TVNELVLPVGRPVRF 149

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19857059 174 ILTSGDVIHSWAVPSLGIKCDCIPGRLNQVSLSIDREGLFYGQCSELCGVLHSSMPIVVQGVSLEDFLAWLEE 246
Cdd:COG1622 150 LLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAE 222
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 15-244 6.65e-60

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 188.68  E-value: 6.65e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19857059   15 WALYFQDGASPSYLGVTHL-NDYLMFYLTFIFIGVIYAICKAVIEYNYNSHPIaakyttHGSIVEFIWTLIPALILILVA 93
Cdd:MTH00080   6 YNLNFSNSLFSSYMDWFHNfNCSLLFGEFVLAFVVFLFLYLISNNFYFKSKKI------EYQFGELLCSVFPVLILLMQM 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19857059   94 LPSFKLLYLLDEVQKPS-MTVKAIGRQWFWTYELNDFVTnenepVSFDSYMVPEEDLEEGSLRQLEVDNRLVLPIDTRIR 172
Cdd:MTH00080  80 VPSLSLLYYYGLMNLDSnLTVKVTGHQWYWSYEFSDIPG-----LEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIR 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19857059  173 LILTSGDVIHSWAVPSLGIKCDCIPGRLNQVSLSIDREGLFYGQCSELCGVLHSSMPIVVQGVSLEDFLAWL 244
Cdd:MTH00080 155 FCITSSDVIHSWALPSLSIKMDAMSGILSTLCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKEWC 226
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 138-242 3.29e-50

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 161.91  E-value: 3.29e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19857059  138 SFDSYMVPEEDLEEGSLRQLEVDNRLVLPIDTRIRLILTSGDVIHSWAVPSLGIKCDCIPGRLNQVSLSIDREGLFYGQC 217
Cdd:PTZ00047  50 SFQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQC 129

                         90       100
                 ....*....|....*....|....*
gi 19857059  218 SELCGVLHSSMPIVVQGVSLEDFLA 242
Cdd:PTZ00047 130 SEMCGTLHGFMPIVVEAVSPEAYAA 154
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 33-245 2.26e-46

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: 153.31  E-value: 2.26e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19857059    33 LNDYLMFYLTFIFIGVIYAICKAVIEYNYNSHPIAAKYTTHGSIVEFIWTLIPALILI-LVALPSFKLLYLLDEVQKPSM 111
Cdd:TIGR02866  12 LFLFVLAVSTLISLLVAALLAYVVWKFRRKGDEEKPSQIHGNRRLEYVWTVIPLIIVVgLFAATAKGLLYLERPIPKDAL 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19857059   112 TVKAIGRQWFWTYelndfvtnenepvsfdsymvpeeDLEEGSLRqleVDNRLVLPIDTRIRLILTSGDVIHSWAVPSLGI 191
Cdd:TIGR02866  92 KVKVTGYQWWWDF-----------------------EYPESGFT---TVNELVLPAGTPVELQVTSKDVIHSFWVPELGG 145

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 19857059   192 KCDCIPGRLNQVSLSIDREGLFYGQCSELCGVLHSSMPIVVQGVSLEDFLAWLE 245
Cdd:TIGR02866 146 KIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYVE 199
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 36-235 1.90e-44

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 148.18  E-value: 1.90e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19857059   36 YLMFYLTFIFIGVIYAICkavieYNYNSHPIAAKYTTHGSIVEFIWTLIPALILILvaLPSFKLLYLL-DEVQKPSMTVK 114
Cdd:MTH00047  13 YILALCVFIPCWVYIMLC-----WQVVSGNGSVNFGSENQVLELLWTVVPTLLVLV--LCFLNLNFITsDLDCFSSETIK 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19857059  115 AIGRQWFWTYELNDfvtnenePVSFDSYMVPEEDLeegslrqleVDNRLVLPIDTRIRLILTSGDVIHSWAVPSLGIKCD 194
Cdd:MTH00047  86 VIGHQWYWSYEYSF-------GGSYDSFMTDDIFG---------VDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMD 149

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 19857059  195 CIPGRLNQVSLSIDREGLFYGQCSELCGVLHSSMPIVVQGV 235
Cdd:MTH00047 150 AIPGRINHLFFCPDRHGVFVGYCSELCGVGHSYMPIVIEVV 190
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 11-99 1.46e-38

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: 129.37  E-value: 1.46e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19857059    11 APSSWALYFQDGASPSYLGVTHLNDYLMFYLTFIFIGVIYAICKAVIEYNYNSHPIAAKYTTHGSIVEFIWTLIPALILI 90
Cdd:pfam02790   1 MPTPWGLGFQDAASPLMEGLLELHDYIMFILTLILILVLYILVTCLIRFNRRKNPITARYTTHGQTIEIIWTIIPAVILI 80


                  ....*....
gi 19857059    91 LVALPSFKL 99
Cdd:pfam02790  81 LIALPSFKL 89
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 111-228 4.00e-26

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: 98.10  E-value: 4.00e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19857059 111 MTVKAIGRQWFWTYelndfvtnenepvsfdSYmvPEEDLEEGSLRQLEVdNRLVLPIDTRIRLILTSGDVIHSWAVPSLG 190
Cdd:cd13919   2 LVVEVTAQQWAWTF----------------RY--PGGDGKLGTDDDVTS-PELHLPVGRPVLFNLRSKDVIHSFWVPEFR 62

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 19857059 191 IKCDCIPGRLNQVSLSIDREGLFYGQCSELCGVLHSSM 228
Cdd:cd13919  63 VKQDAVPGRTTRLWFTPTREGEYEVRCAELCGLGHYRM 100
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 110-228 4.83e-26

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: 97.69  E-value: 4.83e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19857059 110 SMTVKAIGRQWFWTYElndfvtnenepvsfdsYmvPEEDLEEgslrqLEVDNRLVLPIDTRIRLILTSGDVIHSWAVPSL 189
Cdd:cd04213   1 ALTIEVTGHQWWWEFR----------------Y--PDEPGRG-----IVTANELHIPVGRPVRLRLTSADVIHSFWVPSL 57

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 19857059 190 GIKCDCIPGRLNQVSLSIDREGLFYGQCSELCGVLHSSM 228
Cdd:cd04213  58 AGKMDMIPGRTNRLWLQADEPGVYRGQCAEFCGASHALM 96
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 111-232 1.07e-25

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


Pssm-ID: 259911 [Multi-domain]  Cd Length: 95  Bit Score: 96.60  E-value: 1.07e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19857059 111 MTVKAIGRQWFWTYELNDfvtnenepvsfdsymvpeedleegslrqLEVDNRLVLPIDTRIRLILTSGDVIHSWAVPSLG 190
Cdd:cd13842   1 LTVYVTGVQWSWTFIYPN----------------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLG 52

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 19857059 191 IKCDCIPGRLNQVSLSIDREGLFYGQCSELCGVLHSSMPIVV 232
Cdd:cd13842  53 VKVDAVPGYTSELWFVADKPGTYTIICAEYCGLGHSYMLGKV 94
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 110-232 2.67e-22

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: 87.68  E-value: 2.67e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19857059 110 SMTVKAIGRQWFWTYELNDFVTNENEpvsfdsymvpeedleegslrqlevdnrLVLPIDTRIRLILTSGDVIHSWAVPSL 189
Cdd:cd13915   1 ALEIQVTGRQWMWEFTYPNGKREINE---------------------------LHVPVGKPVRLILTSKDVIHSFYVPAF 53

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 19857059 190 GIKCDCIPGRLNQVSLSIDREGLFYGQCSELCGVLHSSMPIVV 232
Cdd:cd13915  54 RIKQDVVPGRYTYLWFEATKPGEYDLFCTEYCGTGHSGMIGKV 96
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 112-244 1.55e-19

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: 80.92  E-value: 1.55e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19857059 112 TVKAIGRQWFWTYelndfvtnenepvsfdSYmvPEEDLEEgslrqlevDNRLVLPIDTRIRLILTSGDVIHSWAVPSLGI 191
Cdd:cd13914   2 EIEVEAYQWGWEF----------------SY--PEANVTT--------SEQLVIPADRPVYFRITSRDVIHAFHVPELGL 55

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 19857059 192 KCDCIPGRLNQVSLSIDREGLFYGQCSELCGVLHSSMPIVVQGVSLEDFLAWL 244
Cdd:cd13914  56 KQDAFPGQYNTIKTEATEEGEYQLYCAEYCGAGHSQMLSTVTVVSQDEYQQWL 108
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 84-244 8.63e-19

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: 79.81  E-value: 8.63e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19857059  84 IPALILI-LVALPSFKLLYLLD---EVQKPSMTVKAIGRQWFWTYELNDFVTNENEpvsfdsymvpeedleegslrqlev 159
Cdd:cd13918   2 LSAIIVIsLIVWTYGMLLYVEDppdEADEDALEVEVEGFQFGWQFEYPNGVTTGNT------------------------ 57

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19857059 160 dnrLVLPIDTRIRLILTSGDVIHSWAVPSLGIKCDCIPGRLNQVSLSIDREGLFYGQCSELCGVLHSSMPIVVQGVSLED 239
Cdd:cd13918  58 ---LRVPADTPIALRVTSTDVFHTFGIPELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEE 134


                ....*
gi 19857059 240 FLAWL 244
Cdd:cd13918 135 FEAWY 139
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 161-228 4.63e-10

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: 55.27  E-value: 4.63e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19857059 161 NRLVLPIDTRIRLILTSGDVIHSWAVPSLGIKCDCIPGRLNQVSLSIDREGLFYGQCSELCGVLHSSM 228
Cdd:cd13913  25 NEIEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNM 92
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 161-222 1.99e-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: 45.23  E-value: 1.99e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19857059 161 NRLVLPIDTRIRLILTSGDVIHSWAVPSLGIKCDCIPGRLNQVSLSIDREGLFYGQCSELCG 222
Cdd:cd04212  25 NELVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGTYQGLSANYSG 86
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 140-233 1.31e-05

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: 42.99  E-value: 1.31e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19857059 140 DSYMVPEEDLEEGslrqlEVDNRLVLPIDTRIRLILTS-GDVIHSWAVPSLGIKCDCI---------------PGRLNQV 203
Cdd:cd00920   7 DWGWSFTYNGVLL-----FGPPVLVVPVGDTVRVQFVNkLGENHSVTIAGFGVPVVAMagganpglvntlvigPGESAEV 81

                        90       100       110
                ....*....|....*....|....*....|
gi 19857059 204 SLSIDREGLFYGQCSELCGVlHSSMPIVVQ 233
Cdd:cd00920  82 TFTTDQAGVYWFYCTIPGHN-HAGMVGTIN 110
CuRO_HCO_II_like_4 cd13917
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 163-228 1.31e-03

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


Pssm-ID: 259984 [Multi-domain]  Cd Length: 88  Bit Score: 36.97  E-value: 1.31e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19857059 163 LVLPIDTRIRLILTSGDVIHSWAVPSLGIKCDCIPGRLNQVSLSIDREGLFYGQCSELCGVLHSSM 228
Cdd:cd13917  16 LVLKKGKTYRLHLSSLDVQHGFSLQPKNINFQVLPGYEWVITMTPNETGEFHIICNEYCGIGHHTM 81
N2OR_C cd04223
The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase ...
 179-228 8.77e-03

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


Pssm-ID: 259885 [Multi-domain]  Cd Length: 95  Bit Score: 34.90  E-value: 8.77e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 19857059 179 DVIHSWAVPSLGIKCDCIPGRLNQVSLSIDREGLFYGQCSELCGVLHSSM 228
Cdd:cd04223  38 DITHGFAIPGYNVNLSLEPGETATVTFVADKPGVYPYYCTEFCSALHLEM 87
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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