NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|970839893|gb|ALU66380|]
View 

cytochrome c oxidase subunit II, partial (mitochondrion) [Sphenarium occidentalis]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-160 9.48e-102

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 291.35  E-value: 9.48e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839893   1 IMITMIVGYTLSYIMLIKFKNRNMLHGHLIETIWTMIPAITLIFIALPSLRLLYMLDDSNNTLITIKSIGRQWYWSYEYS 80
Cdd:MTH00154  32 IMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLYLLDEVNNPSITLKTIGHQWYWSYEYS 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839893  81 DFVNIEFDAYMLP--EEQSNKFRLLDVDNRTLIPMNSEIRMLTSASDVLHSWTIPSMGIKVDATPGRLNQSTFSVNRPGL 158
Cdd:MTH00154 112 DFKNIEFDSYMIPtnELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDAVPGRLNQLNFLINRPGL 191


                 ..
gi 970839893 159 YF 160
Cdd:MTH00154 192 FF 193
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-160 9.48e-102

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 291.35  E-value: 9.48e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839893   1 IMITMIVGYTLSYIMLIKFKNRNMLHGHLIETIWTMIPAITLIFIALPSLRLLYMLDDSNNTLITIKSIGRQWYWSYEYS 80
Cdd:MTH00154  32 IMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLYLLDEVNNPSITLKTIGHQWYWSYEYS 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839893  81 DFVNIEFDAYMLP--EEQSNKFRLLDVDNRTLIPMNSEIRMLTSASDVLHSWTIPSMGIKVDATPGRLNQSTFSVNRPGL 158
Cdd:MTH00154 112 DFKNIEFDSYMIPtnELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDAVPGRLNQLNFLINRPGL 191


                 ..
gi 970839893 159 YF 160
Cdd:MTH00154 192 FF 193
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 64-160 7.43e-60

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: 181.61  E-value: 7.43e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839893  64 ITIKSIGRQWYWSYEYSDFVNIEFDAYMLPEEQSNK--FRLLDVDNRTLIPMNSEIRMLTSASDVLHSWTIPSMGIKVDA 141
Cdd:cd13912    3 LTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKgqLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKVDA 82

                         90
                 ....*....|....*....
gi 970839893 142 TPGRLNQSTFSVNRPGLYF 160
Cdd:cd13912   83 VPGRLNQTSFFIERPGVYY 101
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
64-160 2.41e-55

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 169.90  E-value: 2.41e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839893   64 ITIKSIGRQWYWSYEYSDFVNIEFDAYMLPEE--QSNKFRLLDVDNRTLIPMNSEIRMLTSASDVLHSWTIPSMGIKVDA 141
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEdlEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90
                  ....*....|....*....
gi 970839893  142 TPGRLNQSTFSVNRPGLYF 160
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFY 99
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
26-159 5.92e-31

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 111.07  E-value: 5.92e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839893  26 HGHLIETIWTMIPAITLIFIALPSLRLLYMLDDSNNTLITIKSIGRQWYWSYEYsdfvniefdaymlPEEQSnkfrllDV 105
Cdd:COG1622   75 HNTKLEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRY-------------PDQGI------AT 135

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 970839893 106 DNRTLIPMNSEIRMLTSASDVLHSWTIPSMGIKVDATPGRLNQSTFSVNRPGLY 159
Cdd:COG1622  136 VNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTY 189
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 1-159 1.10e-25

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: 96.68  E-value: 1.10e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839893    1 IMITMIVGytLSYIMLiKFKNRN------MLHGH-LIETIWTMIPA-ITLIFIALPSLRLLYMLDDSNNTLITIKSIGRQ 72
Cdd:TIGR02866  23 ISLLVAAL--LAYVVW-KFRRKGdeekpsQIHGNrRLEYVWTVIPLiIVVGLFAATAKGLLYLERPIPKDALKVKVTGYQ 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839893   73 WYWSYEYSDFvniefdaymlpeeqsnkfrLLDVDNRTLIPMNSEIRMLTSASDVLHSWTIPSMGIKVDATPGRLNQSTFS 152
Cdd:TIGR02866 100 WWWDFEYPES-------------------GFTTVNELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQTNALWFN 160


                  ....*..
gi 970839893  153 VNRPGLY 159
Cdd:TIGR02866 161 ADEPGVY 167
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-160 9.48e-102

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 291.35  E-value: 9.48e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839893   1 IMITMIVGYTLSYIMLIKFKNRNMLHGHLIETIWTMIPAITLIFIALPSLRLLYMLDDSNNTLITIKSIGRQWYWSYEYS 80
Cdd:MTH00154  32 IMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLYLLDEVNNPSITLKTIGHQWYWSYEYS 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839893  81 DFVNIEFDAYMLP--EEQSNKFRLLDVDNRTLIPMNSEIRMLTSASDVLHSWTIPSMGIKVDATPGRLNQSTFSVNRPGL 158
Cdd:MTH00154 112 DFKNIEFDSYMIPtnELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDAVPGRLNQLNFLINRPGL 191


                 ..
gi 970839893 159 YF 160
Cdd:MTH00154 192 FF 193
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-160 4.90e-79

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 233.68  E-value: 4.90e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839893   1 IMITMIVGYTLSYIMLIKFKNRNMLHGHLIETIWTMIPAITLIFIALPSLRLLYMLDDSNNTLITIKSIGRQWYWSYEYS 80
Cdd:MTH00140  32 VLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPSLRLLYLLDETNNPLLTVKAIGHQWYWSYEYS 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839893  81 DFVNIEFDAYMLPEEQSNK--FRLLDVDNRTLIPMNSEIRMLTSASDVLHSWTIPSMGIKVDATPGRLNQSTFSVNRPGL 158
Cdd:MTH00140 112 DFSVIEFDSYMVPENELELgdFRLLEVDNRLVLPYSVDTRVLVTSADVIHSWTVPSLGVKVDAIPGRLNQLSFEPKRPGV 191


                 ..
gi 970839893 159 YF 160
Cdd:MTH00140 192 FY 193
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-160 6.30e-78

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 230.96  E-value: 6.30e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839893   1 IMITMIVGYTLSYIMLIKFKNRNMLHGHLIETIWTMIPAITLIFIALPSLRLLYMLDDSNNTLITIKSIGRQWYWSYEYS 80
Cdd:MTH00117  32 LLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPSLRILYLMDEINNPHLTIKAIGHQWYWSYEYT 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839893  81 DFVNIEFDAYMLPEE--QSNKFRLLDVDNRTLIPMNSEIRMLTSASDVLHSWTIPSMGIKVDATPGRLNQSTFSVNRPGL 158
Cdd:MTH00117 112 DYKDLSFDSYMIPTQdlPNGHFRLLEVDHRMVIPMESPIRILITAEDVLHSWAVPSLGVKTDAVPGRLNQTSFITTRPGV 191


                 ..
gi 970839893 159 YF 160
Cdd:MTH00117 192 FY 193
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-160 3.21e-75

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 223.83  E-value: 3.21e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839893   1 IMITMIVGYTLSYIMLIKFKNRNMLHGHLIETIWTMIPAITLIFIALPSLRLLYMLDDSNNTLITIKSIGRQWYWSYEYS 80
Cdd:MTH00139  32 IMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPSLRLLYLMDEVSDPYLTFKAVGHQWYWSYEYS 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839893  81 DFVNIEFDAYMLPEEQ--SNKFRLLDVDNRTLIPMNSEIRMLTSASDVLHSWTIPSMGIKVDATPGRLNQSTFSVNRPGL 158
Cdd:MTH00139 112 DFKNLSFDSYMIPTEDlsSGEFRLLEVDNRLVLPYKSNIRALITAADVLHSWTVPSLGVKIDAVPGRLNQVGFFINRPGV 191


                 ..
gi 970839893 159 YF 160
Cdd:MTH00139 192 FY 193
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-160 2.97e-73

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 218.96  E-value: 2.97e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839893   1 IMITMIVGYTLSYIMLIKFKNRNMLHGHLIETIWTMIPAITLIFIALPSLRLLYMLDDSNNTLITIKSIGRQWYWSYEYS 80
Cdd:MTH00008  32 TLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPSLRLLYLMDEVSNPSITLKTIGHQWYWSYEYS 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839893  81 DFVNIEFDAYMLPEEQ--SNKFRLLDVDNRTLIPMNSEIRMLTSASDVLHSWTIPSMGIKVDATPGRLNQSTFSVNRPGL 158
Cdd:MTH00008 112 DFSNLEFDSYMLPTSDlsPGQFRLLEVDNRAVLPMQTEIRVLVTAADVIHSWTVPSLGVKVDAVPGRLNQIGFTITRPGV 191


                 ..
gi 970839893 159 YF 160
Cdd:MTH00008 192 FY 193
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-160 2.84e-72

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 216.39  E-value: 2.84e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839893   1 IMITMIVGYTLSYIMLIKFKNRNMLHGHLIETIWTMIPAITLIFIALPSLRLLYMLDDSNNTLITIKSIGRQWYWSYEYS 80
Cdd:MTH00168  32 VLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPSLRLLYLMDEIDKPDLTIKAVGHQWYWSYEYT 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839893  81 DFVNIEFDAYMLPEE--QSNKFRLLDVDNRTLIPMNSEIRMLTSASDVLHSWTIPSMGIKVDATPGRLNQSTFSVNRPGL 158
Cdd:MTH00168 112 DYNDLEFDSYMVPTQdlSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVLHSWTLPSLGLKMDAVPGRLNQLAFLSSRPGS 191


                 ..
gi 970839893 159 YF 160
Cdd:MTH00168 192 FY 193
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-160 6.34e-70

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 210.71  E-value: 6.34e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839893   1 IMITMIVGYTLSYIMLIKFKNRNMLHGHLIETIWTMIPAITLIFIALPSLRLLYMLDDSNNTLITIKSIGRQWYWSYEYS 80
Cdd:MTH00038  32 TLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPSLQLLYLMDEVNNPFLTIKAIGHQWYWSYEYT 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839893  81 DFVNIEFDAYMLPEE--QSNKFRLLDVDNRTLIPMNSEIRMLTSASDVLHSWTIPSMGIKVDATPGRLNQSTFSVNRPGL 158
Cdd:MTH00038 112 DYNDLEFDSYMVPTSdlSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVLHSWAVPSLGVKMDAVPGRLNQTTFFISRTGL 191


                 ..
gi 970839893 159 YF 160
Cdd:MTH00038 192 FY 193
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 1-160 5.54e-67

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 203.09  E-value: 5.54e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839893   1 IMITMIVGYTLSYIMLIKFKNRNMLHGHLIETIWTMIPAITLIFIALPSLRLLYMLDDSNNTLITIKSIGRQWYWSYEYS 80
Cdd:MTH00076  32 FLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPSLRILYLMDEINDPHLTVKAIGHQWYWSYEYT 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839893  81 DFVNIEFDAYMLPEEQSN--KFRLLDVDNRTLIPMNSEIRMLTSASDVLHSWTIPSMGIKVDATPGRLNQSTFSVNRPGL 158
Cdd:MTH00076 112 DYEDLSFDSYMIPTQDLTpgQFRLLEVDNRMVVPMESPIRMLITAEDVLHSWAVPSLGIKTDAIPGRLNQTSFIASRPGV 191


                 ..
gi 970839893 159 YF 160
Cdd:MTH00076 192 YY 193
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 2-160 8.21e-67

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 202.64  E-value: 8.21e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839893   2 MITMIVGYTLSYIMLIKFKNRNMLHGHLIETIWTMIPAITLIFIALPSLRLLYMLDDSNNTLITIKSIGRQWYWSYEYSD 81
Cdd:MTH00098  33 LISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPSLRILYMMDEINNPSLTVKTMGHQWYWSYEYTD 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839893  82 FVNIEFDAYMLPEEQSN--KFRLLDVDNRTLIPMNSEIRMLTSASDVLHSWTIPSMGIKVDATPGRLNQSTFSVNRPGLY 159
Cdd:MTH00098 113 YEDLSFDSYMIPTSDLKpgELRLLEVDNRVVLPMEMPIRMLISSEDVLHSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLY 192


                 .
gi 970839893 160 F 160
Cdd:MTH00098 193 Y 193
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 2-160 3.70e-65

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 198.57  E-value: 3.70e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839893   2 MITMIVGYTLSYIMLIKFKNRNMLHGHLIETIWTMIPAITLIFIALPSLRLLYMLDDSNNTLITIKSIGRQWYWSYEYSD 81
Cdd:MTH00185  33 LISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPSLRILYLMDEINDPHLTIKAMGHQWYWSYEYTD 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839893  82 FVNIEFDAYMLPEEQ--SNKFRLLDVDNRTLIPMNSEIRMLTSASDVLHSWTIPSMGIKVDATPGRLNQSTFSVNRPGLY 159
Cdd:MTH00185 113 YEQLEFDSYMTPTQDltPGQFRLLETDHRMVVPMESPIRVLITAEDVLHSWTVPALGVKMDAVPGRLNQATFIISRPGLY 192


                 .
gi 970839893 160 F 160
Cdd:MTH00185 193 Y 193
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 2-160 7.77e-65

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 197.63  E-value: 7.77e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839893   2 MITMIVGYTLSYIMLIKFKNRNMLHGHLIETIWTMIPAITLIFIALPSLRLLYMLDDSNNTLITIKSIGRQWYWSYEYSD 81
Cdd:MTH00129  33 LISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPSLRILYLMDEINDPHLTIKAMGHQWYWSYEYTD 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839893  82 FVNIEFDAYMLPEEQ--SNKFRLLDVDNRTLIPMNSEIRMLTSASDVLHSWTIPSMGIKVDATPGRLNQSTFSVNRPGLY 159
Cdd:MTH00129 113 YEDLGFDSYMIPTQDltPGQFRLLEADHRMVVPVESPIRVLVSAEDVLHSWAVPALGVKMDAVPGRLNQTAFIASRPGVF 192


                 .
gi 970839893 160 F 160
Cdd:MTH00129 193 Y 193
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 1-160 1.01e-62

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 192.66  E-value: 1.01e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839893   1 IMITMIVGYTLSYIMLIKFKNRNMLHGHLIETIWTMIPAITLIFIALPSLRLLYMLDDSNNTLITIKSIGRQWYWSYEYS 80
Cdd:MTH00023  41 IIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKLLYLMDEVVSPALTIKAIGHQWYWSYEYS 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839893  81 DFV--NIEFDAYMLP--EEQSNKFRLLDVDNRTLIPMNSEIRMLTSASDVLHSWTIPSMGIKVDATPGRLNQSTFSVNRP 156
Cdd:MTH00023 121 DYEgeTLEFDSYMVPtsDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSFAVPSLGLKIDAVPGRLNQTGFFIKRP 200


                 ....
gi 970839893 157 GLYF 160
Cdd:MTH00023 201 GVFY 204
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 1-160 9.73e-61

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 187.68  E-value: 9.73e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839893   1 IMITMIVGYTLSYIMLIKFKNRNMLHGHLIETIWTMIPAITLIFIALPSLRLLYMLDDSNNTLITIKSIGRQWYWSYEYS 80
Cdd:MTH00051  34 TIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSLKLLYLMDEVIDPALTIKAIGHQWYWSYEYS 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839893  81 DF--VNIEFDAYMLPEEQSNK--FRLLDVDNRTLIPMNSEIRMLTSASDVLHSWTIPSMGIKVDATPGRLNQSTFSVNRP 156
Cdd:MTH00051 114 DYgtDTIEFDSYMIPTSDLNSgdLRLLEVDNRLIVPIQTQVRVLVTAADVLHSFAVPSLSVKIDAVPGRLNQTSFFIKRP 193


                 ....
gi 970839893 157 GLYF 160
Cdd:MTH00051 194 GVFY 197
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 64-160 7.43e-60

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: 181.61  E-value: 7.43e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839893  64 ITIKSIGRQWYWSYEYSDFVNIEFDAYMLPEEQSNK--FRLLDVDNRTLIPMNSEIRMLTSASDVLHSWTIPSMGIKVDA 141
Cdd:cd13912    3 LTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEDDLEKgqLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKVDA 82

                         90
                 ....*....|....*....
gi 970839893 142 TPGRLNQSTFSVNRPGLYF 160
Cdd:cd13912   83 VPGRLNQTSFFIERPGVYY 101
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
64-160 2.41e-55

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 169.90  E-value: 2.41e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839893   64 ITIKSIGRQWYWSYEYSDFVNIEFDAYMLPEE--QSNKFRLLDVDNRTLIPMNSEIRMLTSASDVLHSWTIPSMGIKVDA 141
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIPTEdlEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90
                  ....*....|....*....
gi 970839893  142 TPGRLNQSTFSVNRPGLYF 160
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFY 99
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 2-160 3.81e-49

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 159.04  E-value: 3.81e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839893   2 MITMIVGYTLSYIMLIKFKNR------NMLHGHLIETIWTMIPAITLIFIALPSLRLLYMLDDSN-NTLITIKSIGRQWY 74
Cdd:MTH00027  58 ILTIIVGVVLWLIIRILLGNNyysyywNKLDGSLIEVIWTLIPAFILILIAFPSLRLLYIMDECGfSANITIKVTGHQWY 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839893  75 WSYEYSDF--VNIEFDAYMLP--EEQSNKFRLLDVDNRTLIPMNSEIRMLTSASDVLHSWTIPSMGIKVDATPGRLNQST 150
Cdd:MTH00027 138 WSYSYEDYgeKNIEFDSYMIPtaDLEFGDLRLLEVDNRLILPVDTNVRVLITAADVLHSWTVPSLAVKMDAVPGRINETG 217

                        170
                 ....*....|
gi 970839893 151 FSVNRPGLYF 160
Cdd:MTH00027 218 FLIKRPGIFY 227
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 1-160 4.34e-45

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 147.46  E-value: 4.34e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839893   1 IMITMIVGYtLSYIMLIKFKNRNMLHGHLIETIWTMIPAITLIFIALPSLRLLYMLD----DSNntlITIKSIGRQWYWS 76
Cdd:MTH00080  35 VLAFVVFLF-LYLISNNFYFKSKKIEYQFGELLCSVFPVLILLMQMVPSLSLLYYYGlmnlDSN---LTVKVTGHQWYWS 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839893  77 YEYSDFVNIEFDAYMLPEEQSN--KFRLLDVDNRTLIPMNSEIRMLTSASDVLHSWTIPSMGIKVDATPGRLNQSTFSVN 154
Cdd:MTH00080 111 YEFSDIPGLEFDSYMKSLDQLRlgEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDAMSGILSTLCYSFP 190


                 ....*.
gi 970839893 155 RPGLYF 160
Cdd:MTH00080 191 MPGVFY 196
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
26-159 5.92e-31

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 111.07  E-value: 5.92e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839893  26 HGHLIETIWTMIPAITLIFIALPSLRLLYMLDDSNNTLITIKSIGRQWYWSYEYsdfvniefdaymlPEEQSnkfrllDV 105
Cdd:COG1622   75 HNTKLEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRY-------------PDQGI------AT 135

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 970839893 106 DNRTLIPMNSEIRMLTSASDVLHSWTIPSMGIKVDATPGRLNQSTFSVNRPGLY 159
Cdd:COG1622  136 VNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTY 189
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 29-159 5.43e-27

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 100.03  E-value: 5.43e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839893  29 LIETIWTMIPaiTLIFIALPSLRLLYMLDDSN-NTLITIKSIGRQWYWSYEYSDfvNIEFDAYMlpeeqsNKFRLLdVDN 107
Cdd:MTH00047  48 VLELLWTVVP--TLLVLVLCFLNLNFITSDLDcFSSETIKVIGHQWYWSYEYSF--GGSYDSFM------TDDIFG-VDK 116

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 970839893 108 RTLIPMNSEIRMLTSASDVLHSWTIPSMGIKVDATPGRLNQSTFSVNRPGLY 159
Cdd:MTH00047 117 PLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCPDRHGVF 168
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 1-159 1.10e-25

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: 96.68  E-value: 1.10e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839893    1 IMITMIVGytLSYIMLiKFKNRN------MLHGH-LIETIWTMIPA-ITLIFIALPSLRLLYMLDDSNNTLITIKSIGRQ 72
Cdd:TIGR02866  23 ISLLVAAL--LAYVVW-KFRRKGdeekpsQIHGNrRLEYVWTVIPLiIVVGLFAATAKGLLYLERPIPKDALKVKVTGYQ 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839893   73 WYWSYEYSDFvniefdaymlpeeqsnkfrLLDVDNRTLIPMNSEIRMLTSASDVLHSWTIPSMGIKVDATPGRLNQSTFS 152
Cdd:TIGR02866 100 WWWDFEYPES-------------------GFTTVNELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQTNALWFN 160


                  ....*..
gi 970839893  153 VNRPGLY 159
Cdd:TIGR02866 161 ADEPGVY 167
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 101-160 3.35e-18

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 76.40  E-value: 3.35e-18
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839893 101 RLLDVDNRTLIPMNSEIRMLTSASDVLHSWTIPSMGIKVDATPGRLNQSTFSVNRPGLYF 160
Cdd:PTZ00047  67 RQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFY 126
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 64-159 1.69e-15

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: 67.71  E-value: 1.69e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839893  64 ITIKSIGRQWYWSYEYSDfvniefdaymlpeeqsnkfrlLDVDNRTLIPMNSEIRMLTSASDVLHSWTIPSMGIKVDATP 143
Cdd:cd13842    1 LTVYVTGVQWSWTFIYPN---------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDAVP 59

                         90
                 ....*....|....*.
gi 970839893 144 GRLNQSTFSVNRPGLY 159
Cdd:cd13842   60 GYTSELWFVADKPGTY 75
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 64-159 1.40e-14

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: 65.34  E-value: 1.40e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839893  64 ITIKSIGRQWYWSYEYsdfvniefdaymlPEEQSNkfrlldvDNRTLIPMNSEIRMLTSASDVLHSWTIPSMGIKVDATP 143
Cdd:cd13915    2 LEIQVTGRQWMWEFTY-------------PNGKRE-------INELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQDVVP 61

                         90
                 ....*....|....*.
gi 970839893 144 GRLNQSTFSVNRPGLY 159
Cdd:cd13915   62 GRYTYLWFEATKPGEY 77
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 64-160 6.67e-13

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: 61.10  E-value: 6.67e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839893  64 ITIKSIGRQWYWSYEYsdfvniefdaymlPEEQSNKFRLLdvdNRTLIPMNSEIRMLTSASDVLHSWTIPSMGIKVDATP 143
Cdd:cd04213    2 LTIEVTGHQWWWEFRY-------------PDEPGRGIVTA---NELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMDMIP 65

                         90
                 ....*....|....*..
gi 970839893 144 GRLNQSTFSVNRPGLYF 160
Cdd:cd04213   66 GRTNRLWLQADEPGVYR 82
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 64-159 1.68e-12

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: 59.96  E-value: 1.68e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839893  64 ITIKSIGRQWYWSYEYsdfvniefdaymlPEEQSNKFRLLDVDNRTL-IPMNSEIRMLTSASDVLHSWTIPSMGIKVDAT 142
Cdd:cd13919    2 LVVEVTAQQWAWTFRY-------------PGGDGKLGTDDDVTSPELhLPVGRPVLFNLRSKDVIHSFWVPEFRVKQDAV 68

                         90
                 ....*....|....*..
gi 970839893 143 PGRLNQSTFSVNRPGLY 159
Cdd:cd13919   69 PGRTTRLWFTPTREGEY 85
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 64-159 5.95e-10

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


Pssm-ID: 259981 [Multi-domain]  Cd Length: 108  Bit Score: 53.57  E-value: 5.95e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839893  64 ITIKSIGRQWYWSYEYsdfvniefdaymlPEEQsnkfrlLDVDNRTLIPMNSEIRMLTSASDVLHSWTIPSMGIKVDATP 143
Cdd:cd13914    1 VEIEVEAYQWGWEFSY-------------PEAN------VTTSEQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDAFP 61

                         90
                 ....*....|....*.
gi 970839893 144 GRLNQSTFSVNRPGLY 159
Cdd:cd13914   62 GQYNTIKTEATEEGEY 77
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-52 1.01e-09

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: 52.33  E-value: 1.01e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 970839893    1 IMITMIVGYTLSYIML------IKFKNRNMLHGHLIETIWTMIPAITLIFIALPSLRL 52
Cdd:pfam02790  32 TLILILVLYILVTCLIrfnrrkNPITARYTTHGQTIEIIWTIIPAVILILIALPSFKL 89
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 52-159 1.10e-08

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: 50.92  E-value: 1.10e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 970839893  52 LLYMLD---DSNNTLITIKSIGRQWYWSYEYSDFVniefdaymlpeEQSNKFRlldvdnrtlIPMNSEIRMLTSASDVLH 128
Cdd:cd13918   18 LLYVEDppdEADEDALEVEVEGFQFGWQFEYPNGV-----------TTGNTLR---------VPADTPIALRVTSTDVFH 77

                         90       100       110
                 ....*....|....*....|....*....|.
gi 970839893 129 SWTIPSMGIKVDATPGRLNQSTFSVNRPGLY 159
Cdd:cd13918   78 TFGIPELRVKADAIPGEYTSTWFEADEPGTY 108
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 111-159 3.35e-04

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: 37.93  E-value: 3.35e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 970839893 111 IPMNSEIRMLTSASDVLHSWTIPSMGIKVDATPGRLNQSTFSVNRPGLY 159
Cdd:cd13913   29 VPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEY 77
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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