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Conserved domains on  [gi|1252316703|ref|YP_009433694|]
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cytochrome c oxidase subunit 2 (mitochondrion) [Kluyveromyces marxianus DMKU3-1042]

Protein Classification

cytochrome c oxidase subunit II( domain architecture ID 11475927)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 19-245 1.68e-103

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 299.44  E-value: 1.68e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252316703  19 MYFQDSATPNQEGILELHDNIMFYLFIILGLVSWLLFTIVrtysKNPIAYKYIKHGQTIEIIWTIFPAVVLLIIAFPSFI 98
Cdd:MTH00154    7 LSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLL----FNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252316703  99 LLYLCDEVISPAMTIKAIGLQWYWKYEYSDFINdngetVEFESYVIPEDLLEEGQLRLLDTDTSVVVPVDTHIRFVVTAA 178
Cdd:MTH00154   83 LLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKN-----IEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAA 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1252316703 179 DVIHDFAVPSLGIKVDASPGRLNQVSALIQREGVFYGQCSEICGQSHSAMPIKIEAVSLPAFLEWLN 245
Cdd:MTH00154  158 DVIHSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIK 224
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 19-245 1.68e-103

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 299.44  E-value: 1.68e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252316703  19 MYFQDSATPNQEGILELHDNIMFYLFIILGLVSWLLFTIVrtysKNPIAYKYIKHGQTIEIIWTIFPAVVLLIIAFPSFI 98
Cdd:MTH00154    7 LSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLL----FNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252316703  99 LLYLCDEVISPAMTIKAIGLQWYWKYEYSDFINdngetVEFESYVIPEDLLEEGQLRLLDTDTSVVVPVDTHIRFVVTAA 178
Cdd:MTH00154   83 LLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKN-----IEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAA 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1252316703 179 DVIHDFAVPSLGIKVDASPGRLNQVSALIQREGVFYGQCSEICGQSHSAMPIKIEAVSLPAFLEWLN 245
Cdd:MTH00154  158 DVIHSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIK 224
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 109-243 8.37e-82

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: 240.94  E-value: 8.37e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252316703 109 PAMTIKAIGLQWYWKYEYSDFindngETVEFESYVIPEDLLEEGQLRLLDTDTSVVVPVDTHIRFVVTAADVIHDFAVPS 188
Cdd:cd13912     1 PSLTIKAIGHQWYWSYEYSDF-----NDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPS 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1252316703 189 LGIKVDASPGRLNQVSALIQREGVFYGQCSEICGQSHSAMPIKIEAVSLPAFLEW 243
Cdd:cd13912    76 LGIKVDAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
111-235 1.53e-78

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 232.30  E-value: 1.53e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252316703 111 MTIKAIGLQWYWKYEYSDFINdngetVEFESYVIPEDLLEEGQLRLLDTDTSVVVPVDTHIRFVVTAADVIHDFAVPSLG 190
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGD-----LEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLG 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1252316703 191 IKVDASPGRLNQVSALIQREGVFYGQCSEICGQSHSAMPIKIEAV 235
Cdd:pfam00116  76 IKTDAVPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
1-247 9.71e-61

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 190.81  E-value: 9.71e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252316703   1 MFYLLNSIIMNDVPTPYGMYFQDSATPNQEGILELHdNIMFYLFIILGLVSWLL---FTIVRTYSKNPIAYKYIKHGQTI 77
Cdd:COG1622     1 MKRLLLALLLLALLLSGQLSLPDPAGPIAEEIDDLF-WVSLIIMLVIFVLVFGLllyFAIRYRRRKGDADPAQFHHNTKL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252316703  78 EIIWTIFPAVVLLIIAFPSFILLYLCDEVISPAMTIKAIGLQWYWKYEYsdfindngetvefesyvipedlLEEGQLrll 157
Cdd:COG1622    80 EIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRY----------------------PDQGIA--- 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252316703 158 dTDTSVVVPVDTHIRFVVTAADVIHDFAVPSLGIKVDASPGRLNQVSALIQREGVFYGQCSEICGQSHSAMPIKIEAVSL 237
Cdd:COG1622   135 -TVNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSP 213

                         250
                  ....*....|
gi 1252316703 238 PAFLEWLNDQ 247
Cdd:COG1622   214 EEFDAWLAEQ 223
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 25-245 2.24e-42

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: 142.90  E-value: 2.24e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252316703  25 ATPNQEGILELHDNIMFYLFIILGLVSWLLFTIV---RTYSKNPIAyKYIKHGQTIEIIWTIFPAV-VLLIIAFPSFILL 100
Cdd:TIGR02866   2 GGEIAQQIAFLFLFVLAVSTLISLLVAALLAYVVwkfRRKGDEEKP-SQIHGNRRLEYVWTVIPLIiVVGLFAATAKGLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252316703 101 YLCDEVISPAMTIKAIGLQWYWKYEYSDFindngetvefesyvipedlleegqlrLLDTDTSVVVPVDTHIRFVVTAADV 180
Cdd:TIGR02866  81 YLERPIPKDALKVKVTGYQWWWDFEYPES--------------------------GFTTVNELVLPAGTPVELQVTSKDV 134

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1252316703 181 IHDFAVPSLGIKVDASPGRLNQVSALIQREGVFYGQCSEICGQSHSAMPIKIEAVSLPAFLEWLN 245
Cdd:TIGR02866 135 IHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYVE 199
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 19-245 1.68e-103

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 299.44  E-value: 1.68e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252316703  19 MYFQDSATPNQEGILELHDNIMFYLFIILGLVSWLLFTIVrtysKNPIAYKYIKHGQTIEIIWTIFPAVVLLIIAFPSFI 98
Cdd:MTH00154    7 LSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLL----FNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252316703  99 LLYLCDEVISPAMTIKAIGLQWYWKYEYSDFINdngetVEFESYVIPEDLLEEGQLRLLDTDTSVVVPVDTHIRFVVTAA 178
Cdd:MTH00154   83 LLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKN-----IEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILITAA 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1252316703 179 DVIHDFAVPSLGIKVDASPGRLNQVSALIQREGVFYGQCSEICGQSHSAMPIKIEAVSLPAFLEWLN 245
Cdd:MTH00154  158 DVIHSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIK 224
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 4-244 3.70e-101

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 293.97  E-value: 3.70e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252316703   4 LLNSIIMNDVPTPYGMYFQDSATPNQEGILELHDNIMFYLFIILGLVSWLLFTIVrtysKNPIAYKYIKHGQTIEIIWTI 83
Cdd:MTH00023    1 MFNNFFYRDIPEPWQLGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEAL----NGKFYDRFLVDGTFLEIVWTI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252316703  84 FPAVVLLIIAFPSFILLYLCDEVISPAMTIKAIGLQWYWKYEYSDFindNGETVEFESYVIPEDLLEEGQLRLLDTDTSV 163
Cdd:MTH00023   77 IPAVILVFIALPSLKLLYLMDEVVSPALTIKAIGHQWYWSYEYSDY---EGETLEFDSYMVPTSDLNSGDFRLLEVDNRL 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252316703 164 VVPVDTHIRFVVTAADVIHDFAVPSLGIKVDASPGRLNQVSALIQREGVFYGQCSEICGQSHSAMPIKIEAVSLPAFLEW 243
Cdd:MTH00023  154 VVPINTHVRILVTGADVLHSFAVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINW 233


                  .
gi 1252316703 244 L 244
Cdd:MTH00023  234 L 234
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 19-245 6.34e-96

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 280.29  E-value: 6.34e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252316703  19 MYFQDSATPNQEGILELHDNIMFYLFIILGLVSWLLFTIVrtysKNPIAYKYIKHGQTIEIIWTIFPAVVLLIIAFPSFI 98
Cdd:MTH00140    7 LGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLL----FNKFSCRTILEAQKLETIWTIVPALILVFLALPSLR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252316703  99 LLYLCDEVISPAMTIKAIGLQWYWKYEYSDFINdngetVEFESYVIPEDLLEEGQLRLLDTDTSVVVPVDTHIRFVVTAA 178
Cdd:MTH00140   83 LLYLLDETNNPLLTVKAIGHQWYWSYEYSDFSV-----IEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSA 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1252316703 179 DVIHDFAVPSLGIKVDASPGRLNQVSALIQREGVFYGQCSEICGQSHSAMPIKIEAVSLPAFLEWLN 245
Cdd:MTH00140  158 DVIHSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWLE 224
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 11-247 1.80e-94

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 276.66  E-value: 1.80e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252316703  11 NDVPTPYGMYFQDSATPNQEGILELHDNIMFYLFIILGLVSWLlftIVRTYSkNPIAYKYIKHGQTIEIIWTIFPAVVLL 90
Cdd:MTH00051    1 KDAPEPWQLGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWL---IIRALT-TKYYHKYLFEGTLIEIIWTLIPAAILI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252316703  91 IIAFPSFILLYLCDEVISPAMTIKAIGLQWYWKYEYSDFindNGETVEFESYVIPEDLLEEGQLRLLDTDTSVVVPVDTH 170
Cdd:MTH00051   77 FIAFPSLKLLYLMDEVIDPALTIKAIGHQWYWSYEYSDY---GTDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQ 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1252316703 171 IRFVVTAADVIHDFAVPSLGIKVDASPGRLNQVSALIQREGVFYGQCSEICGQSHSAMPIKIEAVSLPAFLEWLNDQ 247
Cdd:MTH00051  154 VRVLVTAADVLHSFAVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINWVATQ 230
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 15-245 2.19e-91

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 268.77  E-value: 2.19e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252316703  15 TPYGMYFQDSATPNQEGILELHDNIMFYLFIILGLVSWLLFTIvrtySKNPIAYKYIKHGQTIEIIWTIFPAVVLLIIAF 94
Cdd:MTH00168    3 TYSQLGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVL----VTSKYTNRFLLDSQMIEFVWTIIPAFILISLAL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252316703  95 PSFILLYLCDEVISPAMTIKAIGLQWYWKYEYSDFINdngetVEFESYVIPEDLLEEGQLRLLDTDTSVVVPVDTHIRFV 174
Cdd:MTH00168   79 PSLRLLYLMDEIDKPDLTIKAVGHQWYWSYEYTDYND-----LEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVL 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1252316703 175 VTAADVIHDFAVPSLGIKVDASPGRLNQVSALIQREGVFYGQCSEICGQSHSAMPIKIEAVSLPAFLEWLN 245
Cdd:MTH00168  154 VTSADVLHSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENWVD 224
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 21-244 2.16e-86

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 256.18  E-value: 2.16e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252316703  21 FQDSATPNQEGILELHDNIMFYLFIILGLVSWLLFTIVrtysKNPIAYKYIKHGQTIEIIWTIFPAVVLLIIAFPSFILL 100
Cdd:MTH00139    9 FQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLM----SNKFTSRSLLESQEVETIWTVLPAFILLFLALPSLRLL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252316703 101 YLCDEVISPAMTIKAIGLQWYWKYEYSDFINdngetVEFESYVIPEDLLEEGQLRLLDTDTSVVVPVDTHIRFVVTAADV 180
Cdd:MTH00139   85 YLMDEVSDPYLTFKAVGHQWYWSYEYSDFKN-----LSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADV 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1252316703 181 IHDFAVPSLGIKVDASPGRLNQVSALIQREGVFYGQCSEICGQSHSAMPIKIEAVSLPAFLEWL 244
Cdd:MTH00139  160 LHSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEWI 223
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 21-245 4.34e-86

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 255.22  E-value: 4.34e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252316703  21 FQDSATPNQEGILELHDNIMFYLFIILGLVSWLLFTIVRTysknPIAYKYIKHGQTIEIIWTIFPAVVLLIIAFPSFILL 100
Cdd:MTH00117    9 FQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTT----KLTHTNTVDAQEVELIWTILPAIVLILLALPSLRIL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252316703 101 YLCDEVISPAMTIKAIGLQWYWKYEYSDFindngETVEFESYVIPEDLLEEGQLRLLDTDTSVVVPVDTHIRFVVTAADV 180
Cdd:MTH00117   85 YLMDEINNPHLTIKAIGHQWYWSYEYTDY-----KDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDV 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1252316703 181 IHDFAVPSLGIKVDASPGRLNQVSALIQREGVFYGQCSEICGQSHSAMPIKIEAVSLPAFLEWLN 245
Cdd:MTH00117  160 LHSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSS 224
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 16-243 2.13e-83

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 248.48  E-value: 2.13e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252316703  16 PYGMYFQDSATPNQEGILELHDNIMFYLFIILGLVSWLLFTIVRTYSKNpiayKYIKHGQTIEIIWTIFPAVVLLIIAFP 95
Cdd:MTH00129    4 PSQLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTN----KYILDSQEIEIIWTVLPAVILILIALP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252316703  96 SFILLYLCDEVISPAMTIKAIGLQWYWKYEYSDFindngETVEFESYVIPEDLLEEGQLRLLDTDTSVVVPVDTHIRFVV 175
Cdd:MTH00129   80 SLRILYLMDEINDPHLTIKAMGHQWYWSYEYTDY-----EDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLV 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1252316703 176 TAADVIHDFAVPSLGIKVDASPGRLNQVSALIQREGVFYGQCSEICGQSHSAMPIKIEAVSLPAFLEW 243
Cdd:MTH00129  155 SAEDVLHSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFENW 222
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 15-246 1.70e-82

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 246.15  E-value: 1.70e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252316703  15 TPYGMYFQDSATPNQEGILELHDNIMFYLFIILGLVSWLLFTIVRTYSKNpiayKYIKHGQTIEIIWTIFPAVVLLIIAF 94
Cdd:MTH00038    3 TWLQLGLQDASSPLMEELIYFHDYALIILTLITILVFYGLASLLFSSPTN----RFFLEGQELETIWTIVPAFILIFIAL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252316703  95 PSFILLYLCDEVISPAMTIKAIGLQWYWKYEYSDFindngETVEFESYVIPEDLLEEGQLRLLDTDTSVVVPVDTHIRFV 174
Cdd:MTH00038   79 PSLQLLYLMDEVNNPFLTIKAIGHQWYWSYEYTDY-----NDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVL 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1252316703 175 VTAADVIHDFAVPSLGIKVDASPGRLNQVSALIQREGVFYGQCSEICGQSHSAMPIKIEAVSLPAFLEWLND 246
Cdd:MTH00038  154 VSSADVLHSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVSN 225
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 21-244 2.45e-82

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 245.92  E-value: 2.45e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252316703  21 FQDSATPNQEGILELHDNIMFYLFIILGLVSWLLFTIVRtyskNPIAYKYIKHGQTIEIIWTIFPAVVLLIIAFPSFILL 100
Cdd:MTH00008    9 FQDAASPVMLQLISFHDHALLILTLVLTVVGYAMTSLMF----NKLSNRYILEAQQIETIWTILPALILLFLAFPSLRLL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252316703 101 YLCDEVISPAMTIKAIGLQWYWKYEYSDFINdngetVEFESYVIPEDLLEEGQLRLLDTDTSVVVPVDTHIRFVVTAADV 180
Cdd:MTH00008   85 YLMDEVSNPSITLKTIGHQWYWSYEYSDFSN-----LEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADV 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1252316703 181 IHDFAVPSLGIKVDASPGRLNQVSALIQREGVFYGQCSEICGQSHSAMPIKIEAVSLPAFLEWL 244
Cdd:MTH00008  160 IHSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKWV 223
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 109-243 8.37e-82

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: 240.94  E-value: 8.37e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252316703 109 PAMTIKAIGLQWYWKYEYSDFindngETVEFESYVIPEDLLEEGQLRLLDTDTSVVVPVDTHIRFVVTAADVIHDFAVPS 188
Cdd:cd13912     1 PSLTIKAIGHQWYWSYEYSDF-----NDLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPS 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1252316703 189 LGIKVDASPGRLNQVSALIQREGVFYGQCSEICGQSHSAMPIKIEAVSLPAFLEW 243
Cdd:cd13912    76 LGIKVDAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 16-243 2.15e-81

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 243.64  E-value: 2.15e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252316703  16 PYGMYFQDSATPNQEGILELHDNIMFYLFIILGLVSWLLFTIVRTYSKNpiayKYIKHGQTIEIIWTIFPAVVLLIIAFP 95
Cdd:MTH00185    4 PSQLGLQDAASPVMEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTN----KYILDSQEIEIVWTILPAIILIMIALP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252316703  96 SFILLYLCDEVISPAMTIKAIGLQWYWKYEYSDFindngETVEFESYVIPEDLLEEGQLRLLDTDTSVVVPVDTHIRFVV 175
Cdd:MTH00185   80 SLRILYLMDEINDPHLTIKAMGHQWYWSYEYTDY-----EQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLI 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1252316703 176 TAADVIHDFAVPSLGIKVDASPGRLNQVSALIQREGVFYGQCSEICGQSHSAMPIKIEAVSLPAFLEW 243
Cdd:MTH00185  155 TAEDVLHSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENW 222
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 14-247 1.19e-80

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 241.61  E-value: 1.19e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252316703  14 PTPYGmyFQDSATPNQEGILELHDNIMFYLFIILGLVSWLLFTIVRTYSKNPIAYKyikhGQTIEIIWTIFPAVVLLIIA 93
Cdd:MTH00076    4 PSQLG--FQDAASPIMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMD----AQEIEMVWTIMPAIILIVIA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252316703  94 FPSFILLYLCDEVISPAMTIKAIGLQWYWKYEYSDFINdngetVEFESYVIPEDLLEEGQLRLLDTDTSVVVPVDTHIRF 173
Cdd:MTH00076   78 LPSLRILYLMDEINDPHLTVKAIGHQWYWSYEYTDYED-----LSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRM 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1252316703 174 VVTAADVIHDFAVPSLGIKVDASPGRLNQVSALIQREGVFYGQCSEICGQSHSAMPIKIEAVSLPAFLEWLNDQ 247
Cdd:MTH00076  153 LITAEDVLHSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLNWSSSM 226
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 14-243 2.47e-79

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 238.08  E-value: 2.47e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252316703  14 PTPYGMYFQDSATPNQEGILELHDNIMFYLFIILGLVSWLLFTIVRTysknPIAYKYIKHGQTIEIIWTIFPAVVLLIIA 93
Cdd:MTH00098    2 AYPFQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTT----KLTHTSTMDAQEVETIWTILPAIILILIA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252316703  94 FPSFILLYLCDEVISPAMTIKAIGLQWYWKYEYSDFindngETVEFESYVIPEDLLEEGQLRLLDTDTSVVVPVDTHIRF 173
Cdd:MTH00098   78 LPSLRILYMMDEINNPSLTVKTMGHQWYWSYEYTDY-----EDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIRM 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252316703 174 VVTAADVIHDFAVPSLGIKVDASPGRLNQVSALIQREGVFYGQCSEICGQSHSAMPIKIEAVSLPAFLEW 243
Cdd:MTH00098  153 LISSEDVLHSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKW 222
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
111-235 1.53e-78

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 232.30  E-value: 1.53e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252316703 111 MTIKAIGLQWYWKYEYSDFINdngetVEFESYVIPEDLLEEGQLRLLDTDTSVVVPVDTHIRFVVTAADVIHDFAVPSLG 190
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGD-----LEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLG 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1252316703 191 IKVDASPGRLNQVSALIQREGVFYGQCSEICGQSHSAMPIKIEAV 235
Cdd:pfam00116  76 IKTDAVPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 9-244 1.32e-73

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 224.90  E-value: 1.32e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252316703   9 IMNDVPTPYGMYFQDSATPNQEGILELHDNIMFYLFIILGLVSWLLFTIVrtYSKNPIAYKYIK-HGQTIEIIWTIFPAV 87
Cdd:MTH00027   25 MIKDANEPWQLGFQDAGSPVMEEIIMLHDQILFILTIIVGVVLWLIIRIL--LGNNYYSYYWNKlDGSLIEVIWTLIPAF 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252316703  88 VLLIIAFPSFILLYLCDE-VISPAMTIKAIGLQWYWKYEYSDFINDNgetVEFESYVIPEDLLEEGQLRLLDTDTSVVVP 166
Cdd:MTH00027  103 ILILIAFPSLRLLYIMDEcGFSANITIKVTGHQWYWSYSYEDYGEKN---IEFDSYMIPTADLEFGDLRLLEVDNRLILP 179

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1252316703 167 VDTHIRFVVTAADVIHDFAVPSLGIKVDASPGRLNQVSALIQREGVFYGQCSEICGQSHSAMPIKIEAVSLPAFLEWL 244
Cdd:MTH00027  180 VDTNVRVLITAADVLHSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYIDWI 257
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
1-247 9.71e-61

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 190.81  E-value: 9.71e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252316703   1 MFYLLNSIIMNDVPTPYGMYFQDSATPNQEGILELHdNIMFYLFIILGLVSWLL---FTIVRTYSKNPIAYKYIKHGQTI 77
Cdd:COG1622     1 MKRLLLALLLLALLLSGQLSLPDPAGPIAEEIDDLF-WVSLIIMLVIFVLVFGLllyFAIRYRRRKGDADPAQFHHNTKL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252316703  78 EIIWTIFPAVVLLIIAFPSFILLYLCDEVISPAMTIKAIGLQWYWKYEYsdfindngetvefesyvipedlLEEGQLrll 157
Cdd:COG1622    80 EIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRY----------------------PDQGIA--- 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252316703 158 dTDTSVVVPVDTHIRFVVTAADVIHDFAVPSLGIKVDASPGRLNQVSALIQREGVFYGQCSEICGQSHSAMPIKIEAVSL 237
Cdd:COG1622   135 -TVNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSP 213

                         250
                  ....*....|
gi 1252316703 238 PAFLEWLNDQ 247
Cdd:COG1622   214 EEFDAWLAEQ 223
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 37-244 1.42e-58

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 185.21  E-value: 1.42e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252316703  37 DNIMFYLFIILGLVSWLLFTIVRTYSknpiaYKYIK-HGQTIEIIWTIFPAVVLLIIAFPSFILLYLCDEV-ISPAMTIK 114
Cdd:MTH00080   27 CSLLFGEFVLAFVVFLFLYLISNNFY-----FKSKKiEYQFGELLCSVFPVLILLMQMVPSLSLLYYYGLMnLDSNLTVK 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252316703 115 AIGLQWYWKYEYSDFINdngetVEFESYVIPEDLLEEGQLRLLDTDTSVVVPVDTHIRFVVTAADVIHDFAVPSLGIKVD 194
Cdd:MTH00080  102 VTGHQWYWSYEFSDIPG-----LEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMD 176

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1252316703 195 ASPGRLNQVSALIQREGVFYGQCSEICGQSHSAMPIKIEAVSLPAFLEWL 244
Cdd:MTH00080  177 AMSGILSTLCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKEWC 226
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 25-245 2.24e-42

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: 142.90  E-value: 2.24e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252316703  25 ATPNQEGILELHDNIMFYLFIILGLVSWLLFTIV---RTYSKNPIAyKYIKHGQTIEIIWTIFPAV-VLLIIAFPSFILL 100
Cdd:TIGR02866   2 GGEIAQQIAFLFLFVLAVSTLISLLVAALLAYVVwkfRRKGDEEKP-SQIHGNRRLEYVWTVIPLIiVVGLFAATAKGLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252316703 101 YLCDEVISPAMTIKAIGLQWYWKYEYSDFindngetvefesyvipedlleegqlrLLDTDTSVVVPVDTHIRFVVTAADV 180
Cdd:TIGR02866  81 YLERPIPKDALKVKVTGYQWWWDFEYPES--------------------------GFTTVNELVLPAGTPVELQVTSKDV 134

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1252316703 181 IHDFAVPSLGIKVDASPGRLNQVSALIQREGVFYGQCSEICGQSHSAMPIKIEAVSLPAFLEWLN 245
Cdd:TIGR02866 135 IHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYVE 199
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 139-240 5.30e-42

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 140.73  E-value: 5.30e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252316703 139 FESYVIPEDLLEEGQLRLLDTDTSVVVPVDTHIRFVVTAADVIHDFAVPSLGIKVDASPGRLNQVSALIQREGVFYGQCS 218
Cdd:PTZ00047   51 FQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCS 130

                          90       100
                  ....*....|....*....|..
gi 1252316703 219 EICGQSHSAMPIKIEAVSLPAF 240
Cdd:PTZ00047  131 EMCGTLHGFMPIVVEAVSPEAY 152
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 13-99 7.97e-39

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: 130.14  E-value: 7.97e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252316703  13 VPTPYGMYFQDSATPNQEGILELHDNIMFYLFIILGLVSWLLFTIVRTY--SKNPIAYKYIKHGQTIEIIWTIFPAVVLL 90
Cdd:pfam02790   1 MPTPWGLGFQDAASPLMEGLLELHDYIMFILTLILILVLYILVTCLIRFnrRKNPITARYTTHGQTIEIIWTIIPAVILI 80


                  ....*....
gi 1252316703  91 IIAFPSFIL 99
Cdd:pfam02790  81 LIALPSFKL 89
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 75-235 1.89e-35

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 124.68  E-value: 1.89e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252316703  75 QTIEIIWTIFPAVVLLIIAFpsFILLYL-CDEVISPAMTIKAIGLQWYWKYEYSDFIndngetvEFESYVIPEDLLEEGQ 153
Cdd:MTH00047   47 QVLELLWTVVPTLLVLVLCF--LNLNFItSDLDCFSSETIKVIGHQWYWSYEYSFGG-------SYDSFMTDDIFGVDKP 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252316703 154 LRLLdtdtsvvvpVDTHIRFVVTAADVIHDFAVPSLGIKVDASPGRLNQVSALIQREGVFYGQCSEICGQSHSAMPIKIE 233
Cdd:MTH00047  118 LRLV---------YGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCPDRHGVFVGYCSELCGVGHSYMPIVIE 188


                  ..
gi 1252316703 234 AV 235
Cdd:MTH00047  189 VV 190
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 110-235 8.40e-26

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


Pssm-ID: 259875 [Multi-domain]  Cd Length: 103  Bit Score: 96.92  E-value: 8.40e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252316703 110 AMTIKAIGLQWYWKYEYSDfinDNGETVEfesyvipedlleegqlrlldTDTSVVVPVDTHIRFVVTAADVIHDFAVPSL 189
Cdd:cd04213     1 ALTIEVTGHQWWWEFRYPD---EPGRGIV--------------------TANELHIPVGRPVRLRLTSADVIHSFWVPSL 57

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1252316703 190 GIKVDASPGRLNQVSALIQREGVFYGQCSEICGQSHSAMPIKIEAV 235
Cdd:cd04213    58 AGKMDMIPGRTNRLWLQADEPGVYRGQCAEFCGASHALMRFKVIAL 103
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 111-233 2.54e-23

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: 90.43  E-value: 2.54e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252316703 111 MTIKAIGLQWYWKYEYSDFINDNgetvefesyvipedlleegqlrlldtdtSVVVPVDTHIRFVVTAADVIHDFAVPSLG 190
Cdd:cd13842     1 LTVYVTGVQWSWTFIYPNVRTPN----------------------------EIVVPAGTPVRFRVTSPDVIHGFYIPNLG 52

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1252316703 191 IKVDASPGRLNQVSALIQREGVFYGQCSEICGQSHSAMPIKIE 233
Cdd:cd13842    53 VKVDAVPGYTSELWFVADKPGTYTIICAEYCGLGHSYMLGKVE 95
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 110-228 1.02e-22

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


Pssm-ID: 259986 [Multi-domain]  Cd Length: 107  Bit Score: 89.24  E-value: 1.02e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252316703 110 AMTIKAIGLQWYWKYEYSdfindnGETVEFesyvIPEDLLEEGQLRLldtdtsvvvPVDTHIRFVVTAADVIHDFAVPSL 189
Cdd:cd13919     1 ALVVEVTAQQWAWTFRYP------GGDGKL----GTDDDVTSPELHL---------PVGRPVLFNLRSKDVIHSFWVPEF 61

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1252316703 190 GIKVDASPGRLNQVSALIQREGVFYGQCSEICGQSHSAM 228
Cdd:cd13919    62 RVKQDAVPGRTTRLWFTPTREGEYEVRCAELCGLGHYRM 100
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 110-234 2.28e-22

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


Pssm-ID: 259982 [Multi-domain]  Cd Length: 98  Bit Score: 88.07  E-value: 2.28e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252316703 110 AMTIKAIGLQWYWKYEYSdfiNDNGETVEfesyvipedlleegqlrlldtdtsVVVPVDTHIRFVVTAADVIHDFAVPSL 189
Cdd:cd13915     1 ALEIQVTGRQWMWEFTYP---NGKREINE------------------------LHVPVGKPVRLILTSKDVIHSFYVPAF 53

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1252316703 190 GIKVDASPGRLNQVSALIQREGVFYGQCSEICGQSHSAMPIKIEA 234
Cdd:cd13915    54 RIKQDVVPGRYTYLWFEATKPGEYDLFCTEYCGTGHSGMIGKVRV 98
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 112-244 2.99e-21

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


Pssm-ID: 259981 [Multi-domain]  Cd Length: 108  Bit Score: 85.15  E-value: 2.99e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252316703 112 TIKAIGLQWYWKYEYsdfindNGETVefesyvipedlleegqlrllDTDTSVVVPVDTHIRFVVTAADVIHDFAVPSLGI 191
Cdd:cd13914     2 EIEVEAYQWGWEFSY------PEANV--------------------TTSEQLVIPADRPVYFRITSRDVIHAFHVPELGL 55

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1252316703 192 KVDASPGRLNQVSALIQREGVFYGQCSEICGQSHSAMPIKIEAVSLPAFLEWL 244
Cdd:cd13914    56 KQDAFPGQYNTIKTEATEEGEYQLYCAEYCGAGHSQMLSTVTVVSQDEYQQWL 108
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 87-244 8.87e-20

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


Pssm-ID: 259985 [Multi-domain]  Cd Length: 139  Bit Score: 82.50  E-value: 8.87e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252316703  87 VVLLIIAFPSFILLYLCD---EVISPAMTIKAIGLQWYWKYEYSdfindNGETvefesyvipedlleegqlrlldTDTSV 163
Cdd:cd13918     6 IVISLIVWTYGMLLYVEDppdEADEDALEVEVEGFQFGWQFEYP-----NGVT----------------------TGNTL 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252316703 164 VVPVDTHIRFVVTAADVIHDFAVPSLGIKVDASPGRLNQVSALIQREGVFYGQCSEICGQSHSAMPIKIEAVSLPAFLEW 243
Cdd:cd13918    59 RVPADTPIALRVTSTDVFHTFGIPELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEFEAW 138


                  .
gi 1252316703 244 L 244
Cdd:cd13918   139 Y 139
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 159-235 3.26e-12

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: 61.05  E-value: 3.26e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1252316703 159 TDTSVVVPVDTHIRFVVTAADVIHDFAVPSLGIKVDASPGRLNQVSALIQREGVFYGQCSEICGQSHSAMPIKIEAV 235
Cdd:cd13913    23 NPNEIEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNMYGKIIVE 99
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 157-235 2.79e-06

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


Pssm-ID: 259983 [Multi-domain]  Cd Length: 93  Bit Score: 44.68  E-value: 2.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252316703 157 LDTDTsvvVPVDTHIRFVVTAADVIHDFAV--PSLGI--KVDASPGRLNQVSALIQREGVFYGQCSEICGQSHSAMPIKI 232
Cdd:cd13916    14 LSRTE---IPAGKPVEFRVTSADVNHGFGIydPDMRLlaQTQAMPGYTNVLRYTFDKPGTYTILCLEYCGLAHHVMMAEF 90


                  ...
gi 1252316703 233 EAV 235
Cdd:cd13916    91 TVV 93
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 111-235 3.45e-06

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


Pssm-ID: 259874 [Multi-domain]  Cd Length: 99  Bit Score: 44.46  E-value: 3.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252316703 111 MTIKAIGLQWYWKYEYSDfinDNGETVEFesyvipedlleegqlrlldtdtsVVVPVDTHIRFVVTAADVIHDFAVPSLG 190
Cdd:cd04212     1 LEIQVVSLDWKWLFIYPE---QGIATVNE-----------------------LVIPVGRPVNFRLTSDSVMNSFFIPQLG 54

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1252316703 191 IKVDASPGRLNQVSALIQREGVFYGQCSEICGQSHSAMPIKIEAV 235
Cdd:cd04212    55 GQIYAMAGMQTQLHLIADKPGTYQGLSANYSGEGFSDMKFKVLAV 99
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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