NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1931495831|ref|XP_037418163|]
View 

cytochrome c oxidase subunit 2-like [Triticum dicoccoides]

Protein Classification

cytochrome c oxidase subunit II( domain architecture ID 1001525)

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

CATH:  1.10.287.90
EC:  7.1.1.9
Gene Ontology:  GO:0004129|GO:0005507
PubMed:  6307356|8083153
TCDB:  3.D.4.6.2

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 super family cl33345
cytochrome c oxidase subunit II; Validated
 17-253 1.29e-92

cytochrome c oxidase subunit II; Validated


The actual alignment was detected with superfamily member MTH00023:

Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 272.78  E-value: 1.29e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931495831  17 DAAEPWQLGSKDAATPMMQGIIDLHHDIFFFLILILVFVSRMLVRALwhfneqTNPIPQR-IVHGSTIEIIRTIFPSVIL 95
Cdd:MTH00023    9 DIPEPWQLGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEAL------NGKFYDRfLVDGTFLEIVWTIIPAVIL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931495831  96 LFIAIPSFALLYSMDGVlVDPAITIKAIGHQWYRTYEYSDYNSSdeqSLTFDSYMIPEDDPELGQSRLLEVDNRVVVPSK 175
Cdd:MTH00023   83 VFIALPSLKLLYLMDEV-VSPALTIKAIGHQWYWSYEYSDYEGE---TLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPIN 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1931495831 176 THLRMIVTPADVPHSWVVPSSGVKCDAVPGHSNLTSISVQREGVYYGQCSEIRGTNHAFTPIVLEAVTLKDYADWVSN 253
Cdd:MTH00023  159 THVRILVTGADVLHSFAVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWLLS 236
 
Name Accession Description Interval E-value
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 17-253 1.29e-92

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 272.78  E-value: 1.29e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931495831  17 DAAEPWQLGSKDAATPMMQGIIDLHHDIFFFLILILVFVSRMLVRALwhfneqTNPIPQR-IVHGSTIEIIRTIFPSVIL 95
Cdd:MTH00023    9 DIPEPWQLGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEAL------NGKFYDRfLVDGTFLEIVWTIIPAVIL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931495831  96 LFIAIPSFALLYSMDGVlVDPAITIKAIGHQWYRTYEYSDYNSSdeqSLTFDSYMIPEDDPELGQSRLLEVDNRVVVPSK 175
Cdd:MTH00023   83 VFIALPSLKLLYLMDEV-VSPALTIKAIGHQWYWSYEYSDYEGE---TLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPIN 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1931495831 176 THLRMIVTPADVPHSWVVPSSGVKCDAVPGHSNLTSISVQREGVYYGQCSEIRGTNHAFTPIVLEAVTLKDYADWVSN 253
Cdd:MTH00023  159 THVRILVTGADVLHSFAVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWLLS 236
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 116-250 8.81e-77

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: 228.61  E-value: 8.81e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931495831 116 PAITIKAIGHQWYRTYEYSDYNSsdeqsLTFDSYMIPEDDPELGQSRLLEVDNRVVVPSKTHLRMIVTPADVPHSWVVPS 195
Cdd:cd13912     1 PSLTIKAIGHQWYWSYEYSDFND-----LEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPS 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1931495831 196 SGVKCDAVPGHSNLTSISVQREGVYYGQCSEIRGTNHAFTPIVLEAVTLKDYADW 250
Cdd:cd13912    76 LGIKVDAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
118-242 1.31e-65

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 199.94  E-value: 1.31e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931495831 118 ITIKAIGHQWYRTYEYSDYNSsdeqsLTFDSYMIPEDDPELGQSRLLEVDNRVVVPSKTHLRMIVTPADVPHSWVVPSSG 197
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGD-----LEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLG 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1931495831 198 VKCDAVPGHSNLTSISVQREGVYYGQCSEIRGTNHAFTPIVLEAV 242
Cdd:pfam00116  76 IKTDAVPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
1-254 2.33e-47

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 156.91  E-value: 2.33e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931495831   1 MILRSLSCRFLTIALCdaaepWQLGSKDAATPMMQGIIDLHHDIFFFLILILVFVSRMLVRALWHFNEQTNP-IPQRIVH 79
Cdd:COG1622     1 MKRLLLALLLLALLLS-----GQLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLLLYFAIRYRRRKGDaDPAQFHH 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931495831  80 GSTIEIIRTIFPSVILLFIAIPSFALLYSMDGVlVDPAITIKAIGHQWYRTYEYSDYNSsdeqsltfdsymipeddpelg 159
Cdd:COG1622    76 NTKLEIVWTVIPIIIVIVLAVPTLRVLHALDDA-PEDPLTVEVTGYQWKWLFRYPDQGI--------------------- 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931495831 160 qsrllEVDNRVVVPSKTHLRMIVTPADVPHSWVVPSSGVKCDAVPGHSNLTSISVQREGVYYGQCSEIRGTNHAFTPIVL 239
Cdd:COG1622   134 -----ATVNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKV 208

                         250
                  ....*....|....*
gi 1931495831 240 EAVTLKDYADWVSNQ 254
Cdd:COG1622   209 VVVSPEEFDAWLAEQ 223
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 29-252 2.16e-39

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: 135.59  E-value: 2.16e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931495831  29 AATPMMQGIIDLHHDIFFFLILILVFVSRMLVRALWHF-NEQTNPIPQRIVHGSTIEIIRTIFPSVILLFIAIPSFALLY 107
Cdd:TIGR02866   1 PGGEIAQQIAFLFLFVLAVSTLISLLVAALLAYVVWKFrRKGDEEKPSQIHGNRRLEYVWTVIPLIIVVGLFAATAKGLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931495831 108 SMDGVLVDPAITIKAIGHQWYRTYEYSDYnssdeqsltfdsymipeddpelgqsrLLEVDNRVVVPSKTHLRMIVTPADV 187
Cdd:TIGR02866  81 YLERPIPKDALKVKVTGYQWWWDFEYPES--------------------------GFTTVNELVLPAGTPVELQVTSKDV 134

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1931495831 188 PHSWVVPSSGVKCDAVPGHSNLTSISVQREGVYYGQCSEIRGTNHAFTPIVLEAVTLKDYADWVS 252
Cdd:TIGR02866 135 IHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYVE 199
 
Name Accession Description Interval E-value
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 17-253 1.29e-92

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 272.78  E-value: 1.29e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931495831  17 DAAEPWQLGSKDAATPMMQGIIDLHHDIFFFLILILVFVSRMLVRALwhfneqTNPIPQR-IVHGSTIEIIRTIFPSVIL 95
Cdd:MTH00023    9 DIPEPWQLGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEAL------NGKFYDRfLVDGTFLEIVWTIIPAVIL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931495831  96 LFIAIPSFALLYSMDGVlVDPAITIKAIGHQWYRTYEYSDYNSSdeqSLTFDSYMIPEDDPELGQSRLLEVDNRVVVPSK 175
Cdd:MTH00023   83 VFIALPSLKLLYLMDEV-VSPALTIKAIGHQWYWSYEYSDYEGE---TLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPIN 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1931495831 176 THLRMIVTPADVPHSWVVPSSGVKCDAVPGHSNLTSISVQREGVYYGQCSEIRGTNHAFTPIVLEAVTLKDYADWVSN 253
Cdd:MTH00023  159 THVRILVTGADVLHSFAVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWLLS 236
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 17-254 2.47e-92

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 272.04  E-value: 2.47e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931495831  17 DAAEPWQLGSKDAATPMMQGIIDLHHDIFFFLILILVFVSRMLVRALwhfneqTNPIPQR-IVHGSTIEIIRTIFPSVIL 95
Cdd:MTH00051    2 DAPEPWQLGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRAL------TTKYYHKyLFEGTLIEIIWTLIPAAIL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931495831  96 LFIAIPSFALLYSMDGVlVDPAITIKAIGHQWYRTYEYSDYNSsdeQSLTFDSYMIPEDDPELGQSRLLEVDNRVVVPSK 175
Cdd:MTH00051   76 IFIAFPSLKLLYLMDEV-IDPALTIKAIGHQWYWSYEYSDYGT---DTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQ 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1931495831 176 THLRMIVTPADVPHSWVVPSSGVKCDAVPGHSNLTSISVQREGVYYGQCSEIRGTNHAFTPIVLEAVTLKDYADWVSNQ 254
Cdd:MTH00051  152 TQVRVLVTAADVLHSFAVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINWVATQ 230
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 23-253 1.67e-89

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 264.38  E-value: 1.67e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931495831  23 QLGSKDAATPMMQGIIDLHHDIFFFLILILVFVSRMLVRALwhFNEQTNpipQRIVHGSTIEIIRTIFPSVILLFIAIPS 102
Cdd:MTH00154    6 NLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLL--FNKFTN---RFLLEGQEIEIIWTILPAIILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931495831 103 FALLYSMDGVlVDPAITIKAIGHQWYRTYEYSDYNSsdeqsLTFDSYMIPEDDPELGQSRLLEVDNRVVVPSKTHLRMIV 182
Cdd:MTH00154   81 LRLLYLLDEV-NNPSITLKTIGHQWYWSYEYSDFKN-----IEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILI 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1931495831 183 TPADVPHSWVVPSSGVKCDAVPGHSNLTSISVQREGVYYGQCSEIRGTNHAFTPIVLEAVTLKDYADWVSN 253
Cdd:MTH00154  155 TAADVIHSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKN 225
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 23-253 2.95e-85

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 253.49  E-value: 2.95e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931495831  23 QLGSKDAATPMMQGIIDLHHDIFFFLILILVFVSRMLVRALWhfNEQTNpipQRIVHGSTIEIIRTIFPSVILLFIAIPS 102
Cdd:MTH00139    6 QLGFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMS--NKFTS---RSLLESQEVETIWTVLPAFILLFLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931495831 103 FALLYSMDGVLvDPAITIKAIGHQWYRTYEYSDYNSsdeqsLTFDSYMIPEDDPELGQSRLLEVDNRVVVPSKTHLRMIV 182
Cdd:MTH00139   81 LRLLYLMDEVS-DPYLTFKAVGHQWYWSYEYSDFKN-----LSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALI 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1931495831 183 TPADVPHSWVVPSSGVKCDAVPGHSNLTSISVQREGVYYGQCSEIRGTNHAFTPIVLEAVTLKDYADWVSN 253
Cdd:MTH00139  155 TAADVLHSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEWILE 225
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 19-255 6.13e-85

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 252.91  E-value: 6.13e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931495831  19 AEPWQLGSKDAATPMMQGIIDLH-HDIFF-FLI--LILVFVSRMLVRALWHFNeqtnpipqrIVHGSTIEIIRTIFPSVI 94
Cdd:MTH00117    2 ANPSQLGFQDASSPIMEELLFFHdHALMVaLLIssLVLYLLTLMLTTKLTHTN---------TVDAQEVELIWTILPAIV 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931495831  95 LLFIAIPSFALLYSMDGVLvDPAITIKAIGHQWYRTYEYSDYNSsdeqsLTFDSYMIPEDDPELGQSRLLEVDNRVVVPS 174
Cdd:MTH00117   73 LILLALPSLRILYLMDEIN-NPHLTIKAIGHQWYWSYEYTDYKD-----LSFDSYMIPTQDLPNGHFRLLEVDHRMVIPM 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931495831 175 KTHLRMIVTPADVPHSWVVPSSGVKCDAVPGHSNLTSISVQREGVYYGQCSEIRGTNHAFTPIVLEAVTLKDYADWVSNQ 254
Cdd:MTH00117  147 ESPIRILITAEDVLHSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSLL 226


                  .
gi 1931495831 255 L 255
Cdd:MTH00117  227 S 227
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 19-255 2.40e-84

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 251.54  E-value: 2.40e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931495831  19 AEPWQLGSKDAATPMMQGIIDLHHDIFFFLILILVFVSRMLVRALwhFNEQTNpipQRIVHGSTIEIIRTIFPSVILLFI 98
Cdd:MTH00038    2 ATWLQLGLQDASSPLMEELIYFHDYALIILTLITILVFYGLASLL--FSSPTN---RFFLEGQELETIWTIVPAFILIFI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931495831  99 AIPSFALLYSMDGVlVDPAITIKAIGHQWYRTYEYSDYNSsdeqsLTFDSYMIPEDDPELGQSRLLEVDNRVVVPSKTHL 178
Cdd:MTH00038   77 ALPSLQLLYLMDEV-NNPFLTIKAIGHQWYWSYEYTDYND-----LEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPI 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1931495831 179 RMIVTPADVPHSWVVPSSGVKCDAVPGHSNLTSISVQREGVYYGQCSEIRGTNHAFTPIVLEAVTLKDYADWVSNQL 255
Cdd:MTH00038  151 RVLVSSADVLHSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVSNFL 227
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 23-253 3.14e-84

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 251.05  E-value: 3.14e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931495831  23 QLGSKDAATPMMQGIIDLHHDIFFFLILILVFVSRMLVRALwhfneQTNPIPQRIVHGSTIEIIRTIFPSVILLFIAIPS 102
Cdd:MTH00168    6 QLGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVLV-----TSKYTNRFLLDSQMIEFVWTIIPAFILISLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931495831 103 FALLYSMDGvLVDPAITIKAIGHQWYRTYEYSDYNSsdeqsLTFDSYMIPEDDPELGQSRLLEVDNRVVVPSKTHLRMIV 182
Cdd:MTH00168   81 LRLLYLMDE-IDKPDLTIKAVGHQWYWSYEYTDYND-----LEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLV 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1931495831 183 TPADVPHSWVVPSSGVKCDAVPGHSNLTSISVQREGVYYGQCSEIRGTNHAFTPIVLEAVTLKDYADWVSN 253
Cdd:MTH00168  155 TSADVLHSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENWVDS 225
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 23-253 8.37e-84

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 249.86  E-value: 8.37e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931495831  23 QLGSKDAATPMMQGIIDLHHDIFFFLILILVFVSRMLVRALwhFNEQTNpipQRIVHGSTIEIIRTIFPSVILLFIAIPS 102
Cdd:MTH00140    6 QLGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLL--FNKFSC---RTILEAQKLETIWTIVPALILVFLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931495831 103 FALLYSMDgVLVDPAITIKAIGHQWYRTYEYSDYNSsdeqsLTFDSYMIPEDDPELGQSRLLEVDNRVVVPSKTHLRMIV 182
Cdd:MTH00140   81 LRLLYLLD-ETNNPLLTVKAIGHQWYWSYEYSDFSV-----IEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLV 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1931495831 183 TPADVPHSWVVPSSGVKCDAVPGHSNLTSISVQREGVYYGQCSEIRGTNHAFTPIVLEAVTLKDYADWVSN 253
Cdd:MTH00140  155 TSADVIHSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWLEL 225
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 19-255 2.22e-80

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 241.16  E-value: 2.22e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931495831  19 AEPWQLGSKDAATPMMQGIIDLHHDIFF--FLI--LILVFVSRMLVRALWHFNeqtnpipqrIVHGSTIEIIRTIFPSVI 94
Cdd:MTH00098    2 AYPFQLGFQDATSPIMEELLHFHDHTLMivFLIssLVLYIISLMLTTKLTHTS---------TMDAQEVETIWTILPAII 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931495831  95 LLFIAIPSFALLYSMDGVlVDPAITIKAIGHQWYRTYEYSDYnssdeQSLTFDSYMIPEDDPELGQSRLLEVDNRVVVPS 174
Cdd:MTH00098   73 LILIALPSLRILYMMDEI-NNPSLTVKTMGHQWYWSYEYTDY-----EDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPM 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931495831 175 KTHLRMIVTPADVPHSWVVPSSGVKCDAVPGHSNLTSISVQREGVYYGQCSEIRGTNHAFTPIVLEAVTLKDYADWVSNQ 254
Cdd:MTH00098  147 EMPIRMLISSEDVLHSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKWSASM 226


                  .
gi 1931495831 255 L 255
Cdd:MTH00098  227 L 227
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 19-255 6.87e-77

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 232.68  E-value: 6.87e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931495831  19 AEPWQLGSKDAATPMMQGIIDLHHDIFFFLILILVFVSRMLVRALwhfneQTNPIPQRIVHGSTIEIIRTIFPSVILLFI 98
Cdd:MTH00129    2 AHPSQLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMV-----STKLTNKYILDSQEIEIIWTVLPAVILILI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931495831  99 AIPSFALLYSMDGVlVDPAITIKAIGHQWYRTYEYSDYnssdeQSLTFDSYMIPEDDPELGQSRLLEVDNRVVVPSKTHL 178
Cdd:MTH00129   77 ALPSLRILYLMDEI-NDPHLTIKAMGHQWYWSYEYTDY-----EDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPI 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1931495831 179 RMIVTPADVPHSWVVPSSGVKCDAVPGHSNLTSISVQREGVYYGQCSEIRGTNHAFTPIVLEAVTLKDYADWVSNQL 255
Cdd:MTH00129  151 RVLVSAEDVLHSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLML 227
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 116-250 8.81e-77

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: 228.61  E-value: 8.81e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931495831 116 PAITIKAIGHQWYRTYEYSDYNSsdeqsLTFDSYMIPEDDPELGQSRLLEVDNRVVVPSKTHLRMIVTPADVPHSWVVPS 195
Cdd:cd13912     1 PSLTIKAIGHQWYWSYEYSDFND-----LEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPS 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1931495831 196 SGVKCDAVPGHSNLTSISVQREGVYYGQCSEIRGTNHAFTPIVLEAVTLKDYADW 250
Cdd:cd13912    76 LGIKVDAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 19-255 1.50e-76

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 231.59  E-value: 1.50e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931495831  19 AEPWQLGSKDAATPMMQGIIDLH-HDIF-FFLI--LILVFVSRMLVRALwhfnEQTNPIpqrivHGSTIEIIRTIFPSVI 94
Cdd:MTH00076    2 AHPSQLGFQDAASPIMEELLHFHdHALMaVFLIstLVLYIITIMMTTKL----TNTNTM-----DAQEIEMVWTIMPAII 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931495831  95 LLFIAIPSFALLYSMDGVlVDPAITIKAIGHQWYRTYEYSDYNSsdeqsLTFDSYMIPEDDPELGQSRLLEVDNRVVVPS 174
Cdd:MTH00076   73 LIVIALPSLRILYLMDEI-NDPHLTVKAIGHQWYWSYEYTDYED-----LSFDSYMIPTQDLTPGQFRLLEVDNRMVVPM 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931495831 175 KTHLRMIVTPADVPHSWVVPSSGVKCDAVPGHSNLTSISVQREGVYYGQCSEIRGTNHAFTPIVLEAVTLKDYADWVSNQ 254
Cdd:MTH00076  147 ESPIRMLITAEDVLHSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLNWSSSM 226


                  .
gi 1931495831 255 L 255
Cdd:MTH00076  227 L 227
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 23-253 5.62e-76

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 230.13  E-value: 5.62e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931495831  23 QLGSKDAATPMMQGIIDLHHDIFFFLILILVFVSRMLVRALwhFNEQTNpipQRIVHGSTIEIIRTIFPSVILLFIAIPS 102
Cdd:MTH00008    6 QLMFQDAASPVMLQLISFHDHALLILTLVLTVVGYAMTSLM--FNKLSN---RYILEAQQIETIWTILPALILLFLAFPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931495831 103 FALLYSMDGVLvDPAITIKAIGHQWYRTYEYSDYNSsdeqsLTFDSYMIPEDDPELGQSRLLEVDNRVVVPSKTHLRMIV 182
Cdd:MTH00008   81 LRLLYLMDEVS-NPSITLKTIGHQWYWSYEYSDFSN-----LEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLV 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1931495831 183 TPADVPHSWVVPSSGVKCDAVPGHSNLTSISVQREGVYYGQCSEIRGTNHAFTPIVLEAVTLKDYADWVSN 253
Cdd:MTH00008  155 TAADVIHSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKWVSS 225
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 17-254 1.28e-74

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 227.99  E-value: 1.28e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931495831  17 DAAEPWQLGSKDAATPMMQGIIDLHHDIFFFLILILVFVSRMLVRALWHFNEQTNPIPQriVHGSTIEIIRTIFPSVILL 96
Cdd:MTH00027   28 DANEPWQLGFQDAGSPVMEEIIMLHDQILFILTIIVGVVLWLIIRILLGNNYYSYYWNK--LDGSLIEVIWTLIPAFILI 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931495831  97 FIAIPSFALLYSMDGVLVDPAITIKAIGHQWYRTYEYSDYNssdEQSLTFDSYMIPEDDPELGQSRLLEVDNRVVVPSKT 176
Cdd:MTH00027  106 LIAFPSLRLLYIMDECGFSANITIKVTGHQWYWSYSYEDYG---EKNIEFDSYMIPTADLEFGDLRLLEVDNRLILPVDT 182

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1931495831 177 HLRMIVTPADVPHSWVVPSSGVKCDAVPGHSNLTSISVQREGVYYGQCSEIRGTNHAFTPIVLEAVTLKDYADWVSNQ 254
Cdd:MTH00027  183 NVRVLITAADVLHSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYIDWIGRE 260
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 19-255 2.54e-73

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 223.61  E-value: 2.54e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931495831  19 AEPWQLGSKDAATPMMQGIIDLHHDIFFFLILILVFVSRMLVRALwhfneQTNPIPQRIVHGSTIEIIRTIFPSVILLFI 98
Cdd:MTH00185    2 AHPSQLGLQDAASPVMEELIHFHDHTLMIVFLISTLVLYIIVAMV-----TTKLTNKYILDSQEIEIVWTILPAIILIMI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931495831  99 AIPSFALLYSMDGVlVDPAITIKAIGHQWYRTYEYSDYNSsdeqsLTFDSYMIPEDDPELGQSRLLEVDNRVVVPSKTHL 178
Cdd:MTH00185   77 ALPSLRILYLMDEI-NDPHLTIKAMGHQWYWSYEYTDYEQ-----LEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPI 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1931495831 179 RMIVTPADVPHSWVVPSSGVKCDAVPGHSNLTSISVQREGVYYGQCSEIRGTNHAFTPIVLEAVTLKDYADWVSNQL 255
Cdd:MTH00185  151 RVLITAEDVLHSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLML 227
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
118-242 1.31e-65

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 199.94  E-value: 1.31e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931495831 118 ITIKAIGHQWYRTYEYSDYNSsdeqsLTFDSYMIPEDDPELGQSRLLEVDNRVVVPSKTHLRMIVTPADVPHSWVVPSSG 197
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGD-----LEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLG 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1931495831 198 VKCDAVPGHSNLTSISVQREGVYYGQCSEIRGTNHAFTPIVLEAV 242
Cdd:pfam00116  76 IKTDAVPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 38-256 4.90e-58

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 184.44  E-value: 4.90e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931495831  38 IDLHHDIFFFLILILVFVSR---MLVRALWHFNeqtnpipQRIVHGSTIEIIRTIFPSVILLFIAIPSFALLYSMDGVLV 114
Cdd:MTH00080   22 FHNFNCSLLFGEFVLAFVVFlflYLISNNFYFK-------SKKIEYQFGELLCSVFPVLILLMQMVPSLSLLYYYGLMNL 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931495831 115 DPAITIKAIGHQWYRTYEYSDYnssdeQSLTFDSYMIPEDDPELGQSRLLEVDNRVVVPSKTHLRMIVTPADVPHSWVVP 194
Cdd:MTH00080   95 DSNLTVKVTGHQWYWSYEFSDI-----PGLEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALP 169

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1931495831 195 SSGVKCDAVPGHSNLTSISVQREGVYYGQCSEIRGTNHAFTPIVLEAVTLKDYADWVSNQLI 256
Cdd:MTH00080  170 SLSIKMDAMSGILSTLCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKEWCKLLLD 231
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
1-254 2.33e-47

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 156.91  E-value: 2.33e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931495831   1 MILRSLSCRFLTIALCdaaepWQLGSKDAATPMMQGIIDLHHDIFFFLILILVFVSRMLVRALWHFNEQTNP-IPQRIVH 79
Cdd:COG1622     1 MKRLLLALLLLALLLS-----GQLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLLLYFAIRYRRRKGDaDPAQFHH 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931495831  80 GSTIEIIRTIFPSVILLFIAIPSFALLYSMDGVlVDPAITIKAIGHQWYRTYEYSDYNSsdeqsltfdsymipeddpelg 159
Cdd:COG1622    76 NTKLEIVWTVIPIIIVIVLAVPTLRVLHALDDA-PEDPLTVEVTGYQWKWLFRYPDQGI--------------------- 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931495831 160 qsrllEVDNRVVVPSKTHLRMIVTPADVPHSWVVPSSGVKCDAVPGHSNLTSISVQREGVYYGQCSEIRGTNHAFTPIVL 239
Cdd:COG1622   134 -----ATVNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKV 208

                         250
                  ....*....|....*
gi 1931495831 240 EAVTLKDYADWVSNQ 254
Cdd:COG1622   209 VVVSPEEFDAWLAEQ 223
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 29-252 2.16e-39

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: 135.59  E-value: 2.16e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931495831  29 AATPMMQGIIDLHHDIFFFLILILVFVSRMLVRALWHF-NEQTNPIPQRIVHGSTIEIIRTIFPSVILLFIAIPSFALLY 107
Cdd:TIGR02866   1 PGGEIAQQIAFLFLFVLAVSTLISLLVAALLAYVVWKFrRKGDEEKPSQIHGNRRLEYVWTVIPLIIVVGLFAATAKGLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931495831 108 SMDGVLVDPAITIKAIGHQWYRTYEYSDYnssdeqsltfdsymipeddpelgqsrLLEVDNRVVVPSKTHLRMIVTPADV 187
Cdd:TIGR02866  81 YLERPIPKDALKVKVTGYQWWWDFEYPES--------------------------GFTTVNELVLPAGTPVELQVTSKDV 134

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1931495831 188 PHSWVVPSSGVKCDAVPGHSNLTSISVQREGVYYGQCSEIRGTNHAFTPIVLEAVTLKDYADWVS 252
Cdd:TIGR02866 135 IHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYVE 199
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 145-248 2.99e-38

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 131.48  E-value: 2.99e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931495831 145 TFDSYMIPEDDPELGQSRLLEVDNRVVVPSKTHLRMIVTPADVPHSWVVPSSGVKCDAVPGHSNLTSISVQREGVYYGQC 224
Cdd:PTZ00047   50 SFQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQC 129

                          90       100
                  ....*....|....*....|....
gi 1931495831 225 SEIRGTNHAFTPIVLEAVTLKDYA 248
Cdd:PTZ00047  130 SEMCGTLHGFMPIVVEAVSPEAYA 153
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 18-105 1.81e-30

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: 108.96  E-value: 1.81e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931495831  18 AAEPWQLGSKDAATPMMQGIIDLHHDIFFFLILILVFVSRMLVRALWHFNEQTNPIPQR-IVHGSTIEIIRTIFPSVILL 96
Cdd:pfam02790   1 MPTPWGLGFQDAASPLMEGLLELHDYIMFILTLILILVLYILVTCLIRFNRRKNPITARyTTHGQTIEIIWTIIPAVILI 80


                  ....*....
gi 1931495831  97 FIAIPSFAL 105
Cdd:pfam02790  81 LIALPSFKL 89
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 39-242 1.31e-26

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 102.34  E-value: 1.31e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931495831  39 DLHHDIFFFLILILVFVSRMLvraLWhfneQTNPIPQRIVHGS---TIEIIRTIFPSVILLFIAipSFALLYSMDGVLVD 115
Cdd:MTH00047    9 DIVCYILALCVFIPCWVYIML---CW----QVVSGNGSVNFGSenqVLELLWTVVPTLLVLVLC--FLNLNFITSDLDCF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931495831 116 PAITIKAIGHQWYRTYEYSDynssdeqSLTFDSYMIpeDDpelgqsrLLEVDNRVVVPSKTHLRMIVTPADVPHSWVVPS 195
Cdd:MTH00047   80 SSETIKVIGHQWYWSYEYSF-------GGSYDSFMT--DD-------IFGVDKPLRLVYGVPYHLLVTSSDVIHSFSVPD 143

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1931495831 196 SGVKCDAVPGHSNLTSISVQREGVYYGQCSEIRGTNHAFTPIVLEAV 242
Cdd:MTH00047  144 LNLKMDAIPGRINHLFFCPDRHGVFVGYCSELCGVGHSYMPIVIEVV 190
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 117-239 4.72e-17

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: 74.19  E-value: 4.72e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931495831 117 AITIKAIGHQWYRTYEYsdynssdeqsltfdsymiPEDDPelgqsRLLEVDNRVVVPSKTHLRMIVTPADVPHSWVVPSS 196
Cdd:cd04213     1 ALTIEVTGHQWWWEFRY------------------PDEPG-----RGIVTANELHIPVGRPVRLRLTSADVIHSFWVPSL 57

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1931495831 197 GVKCDAVPGHSNLTSISVQREGVYYGQCSEIRGTNHA---FTPIVL 239
Cdd:cd04213    58 AGKMDMIPGRTNRLWLQADEPGVYRGQCAEFCGASHAlmrFKVIAL 103
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 118-240 2.13e-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: 69.63  E-value: 2.13e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931495831 118 ITIKAIGHQWYRTYEYSDYNSSDEqsltfdsymipeddpelgqsrllevdnrVVVPSKTHLRMIVTPADVPHSWVVPSSG 197
Cdd:cd13842     1 LTVYVTGVQWSWTFIYPNVRTPNE----------------------------IVVPAGTPVRFRVTSPDVIHGFYIPNLG 52

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1931495831 198 VKCDAVPGHSNLTSISVQREGVYYGQCSEIRGTNHAFTPIVLE 240
Cdd:cd13842    53 VKVDAVPGYTSELWFVADKPGTYTIICAEYCGLGHSYMLGKVE 95
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 117-233 1.82e-11

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


Pssm-ID: 259986 [Multi-domain]  Cd Length: 107  Bit Score: 59.58  E-value: 1.82e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931495831 117 AITIKAIGHQWYRTYEYsdynssdeqsltfdsymiPEDDPELGQSRLLEVdNRVVVPSKTHLRMIVTPADVPHSWVVPSS 196
Cdd:cd13919     1 ALVVEVTAQQWAWTFRY------------------PGGDGKLGTDDDVTS-PELHLPVGRPVLFNLRSKDVIHSFWVPEF 61

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1931495831 197 GVKCDAVPGHSNLTSISVQREGVYYGQCSEIRGTNHA 233
Cdd:cd13919    62 RVKQDAVPGRTTRLWFTPTREGEYEVRCAELCGLGHY 98
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 103-251 8.84e-10

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


Pssm-ID: 259985 [Multi-domain]  Cd Length: 139  Bit Score: 55.54  E-value: 8.84e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931495831 103 FALLYSMDGVL--VDPAITIKAIGHQWYRTYEYSDYNSSdeqsltfdsymipeddpelgqsrllevDNRVVVPSKTHLRM 180
Cdd:cd13918    16 GMLLYVEDPPDeaDEDALEVEVEGFQFGWQFEYPNGVTT---------------------------GNTLRVPADTPIAL 68

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1931495831 181 IVTPADVPHSWVVPSSGVKCDAVPGHSNLTSISVQREGVYYGQCSEIRGTNHAFTPIVLEAVTLKDYADWV 251
Cdd:cd13918    69 RVTSTDVFHTFGIPELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEFEAWY 139
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 117-233 1.31e-09

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: 54.17  E-value: 1.31e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931495831 117 AITIKAIGHQWYRTYEYSDynssdeqsltfdsymipeddpelGQSRllevDNRVVVPSKTHLRMIVTPADVPHSWVVPSS 196
Cdd:cd13915     1 ALEIQVTGRQWMWEFTYPN-----------------------GKRE----INELHVPVGKPVRLILTSKDVIHSFYVPAF 53

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1931495831 197 GVKCDAVPGHSNLTSISVQREGVYYGQCSEIRGTNHA 233
Cdd:cd13915    54 RIKQDVVPGRYTYLWFEATKPGEYDLFCTEYCGTGHS 90
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 163-240 1.16e-03

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: 37.60  E-value: 1.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931495831 163 LLEVDNRVVVPSKTHLRMIVT-PADVPHSWVVPSSGVKCDAVPGHSNL-------------TSISVQ--REGVYYGQCSe 226
Cdd:cd00920    18 LLFGPPVLVVPVGDTVRVQFVnKLGENHSVTIAGFGVPVVAMAGGANPglvntlvigpgesAEVTFTtdQAGVYWFYCT- 96

                          90
                  ....*....|....
gi 1931495831 227 IRGTNHAFTPIVLE 240
Cdd:cd00920    97 IPGHNHAGMVGTIN 110
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 168-232 3.12e-03

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: 36.01  E-value: 3.12e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1931495831 168 NRVVVPSKTHLRMIVTPADVPHSWVVPSSGVKCDAVPGHSNLTSISVQREGVYYGQCSEIRGTNH 232
Cdd:cd13913    25 NEIEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGH 89
 
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