NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2127873173|ref|YP_010204180|]
View 

cytochrome c oxidase subunit 2 (mitochondrion) [Ahnfeltia fastigiata]

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
 13-254 5.86e-115

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: 329.40  E-value: 5.86e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127873173  13 FSDAAENWQLGFQDPATPIMEGIINLHHDLMFFICVVSIFVSWMLGRTLWHFEYKQNpvpstLAHGTLIEMIWTITPAFI 92
Cdd:MTH00023    7 YRDIPEPWQLGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRF-----LVDGTFLEIVWTIIPAVI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127873173  93 LLVIAIPSFSLLYAMDEVISPAITVKTLGHQWYWSYEYSDYvneDDESIAFDSYMIPEEDLELGQLRLLEVDNHMVVPVN 172
Cdd:MTH00023   82 LVFIALPSLKLLYLMDEVVSPALTIKAIGHQWYWSYEYSDY---EGETLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPIN 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127873173 173 THIRVIVSAADVLHSWAVPSLGVKCDAIPGRLNQTSLFIKREGLYYGQCSEICGINHGFMPIVVEAVSLPNYVTWISNKL 252
Cdd:MTH00023  159 THVRILVTGADVLHSFAVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWLLSLS 238


                  ..
gi 2127873173 253 SE 254
Cdd:MTH00023  239 ND 240
 
Name Accession Description Interval E-value
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 13-254 5.86e-115

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 329.40  E-value: 5.86e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127873173  13 FSDAAENWQLGFQDPATPIMEGIINLHHDLMFFICVVSIFVSWMLGRTLWHFEYKQNpvpstLAHGTLIEMIWTITPAFI 92
Cdd:MTH00023    7 YRDIPEPWQLGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRF-----LVDGTFLEIVWTIIPAVI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127873173  93 LLVIAIPSFSLLYAMDEVISPAITVKTLGHQWYWSYEYSDYvneDDESIAFDSYMIPEEDLELGQLRLLEVDNHMVVPVN 172
Cdd:MTH00023   82 LVFIALPSLKLLYLMDEVVSPALTIKAIGHQWYWSYEYSDY---EGETLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPIN 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127873173 173 THIRVIVSAADVLHSWAVPSLGVKCDAIPGRLNQTSLFIKREGLYYGQCSEICGINHGFMPIVVEAVSLPNYVTWISNKL 252
Cdd:MTH00023  159 THVRILVTGADVLHSFAVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWLLSLS 238


                  ..
gi 2127873173 253 SE 254
Cdd:MTH00023  239 ND 240
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 113-247 6.72e-96

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: 276.76  E-value: 6.72e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127873173 113 PAITVKTLGHQWYWSYEYSDYVNeddesIAFDSYMIPEEDLELGQLRLLEVDNHMVVPVNTHIRVIVSAADVLHSWAVPS 192
Cdd:cd13912     1 PSLTIKAIGHQWYWSYEYSDFND-----LEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPS 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2127873173 193 LGVKCDAIPGRLNQTSLFIKREGLYYGQCSEICGINHGFMPIVVEAVSLPNYVTW 247
Cdd:cd13912    76 LGIKVDAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
115-239 6.42e-82

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 241.16  E-value: 6.42e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127873173 115 ITVKTLGHQWYWSYEYSDYVNeddesIAFDSYMIPEEDLELGQLRLLEVDNHMVVPVNTHIRVIVSAADVLHSWAVPSLG 194
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGD-----LEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLG 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2127873173 195 VKCDAIPGRLNQTSLFIKREGLYYGQCSEICGINHGFMPIVVEAV 239
Cdd:pfam00116  76 IKTDAVPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
20-251 6.27e-65

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 201.60  E-value: 6.27e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127873173  20 WQLGFQDPATPIMEGIINLHHDLMFFICVVSIFVSWMLGRTLWHFEYKQNP-VPSTLAHGTLIEMIWTITPAFILLVIAI 98
Cdd:COG1622    17 GQLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLLLYFAIRYRRRKGDaDPAQFHHNTKLEIVWTVIPIIIVIVLAV 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127873173  99 PSFSLLYAMDEVISPAITVKTLGHQWYWSYEYsdyvneddesiafdsymiPEEDLElgqlrlleVDNHMVVPVNTHIRVI 178
Cdd:COG1622    97 PTLRVLHALDDAPEDPLTVEVTGYQWKWLFRY------------------PDQGIA--------TVNELVLPVGRPVRFL 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2127873173 179 VSAADVLHSWAVPSLGVKCDAIPGRLNQTSLFIKREGLYYGQCSEICGINHGFMPIVVEAVSLPNYVTWISNK 251
Cdd:COG1622   151 LTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAEQ 223
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 27-249 2.41e-49

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: 161.01  E-value: 2.41e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127873173  27 PATPIMEGIINLHHDLMFFICVVSIFVSWMLGRTLWHFEYK-QNPVPSTLAHGTLIEMIWTITPAFILLVIAIPSFS-LL 104
Cdd:TIGR02866   1 PGGEIAQQIAFLFLFVLAVSTLISLLVAALLAYVVWKFRRKgDEEKPSQIHGNRRLEYVWTVIPLIIVVGLFAATAKgLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127873173 105 YAMDEVISPAITVKTLGHQWYWSYEYSDYvneddesiafdsymipeedlelgqlrLLEVDNHMVVPVNTHIRVIVSAADV 184
Cdd:TIGR02866  81 YLERPIPKDALKVKVTGYQWWWDFEYPES--------------------------GFTTVNELVLPAGTPVELQVTSKDV 134

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2127873173 185 LHSWAVPSLGVKCDAIPGRLNQTSLFIKREGLYYGQCSEICGINHGFMPIVVEAVSLPNYVTWIS 249
Cdd:TIGR02866 135 IHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYVE 199
 
Name Accession Description Interval E-value
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 13-254 5.86e-115

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 329.40  E-value: 5.86e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127873173  13 FSDAAENWQLGFQDPATPIMEGIINLHHDLMFFICVVSIFVSWMLGRTLWHFEYKQNpvpstLAHGTLIEMIWTITPAFI 92
Cdd:MTH00023    7 YRDIPEPWQLGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRF-----LVDGTFLEIVWTIIPAVI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127873173  93 LLVIAIPSFSLLYAMDEVISPAITVKTLGHQWYWSYEYSDYvneDDESIAFDSYMIPEEDLELGQLRLLEVDNHMVVPVN 172
Cdd:MTH00023   82 LVFIALPSLKLLYLMDEVVSPALTIKAIGHQWYWSYEYSDY---EGETLEFDSYMVPTSDLNSGDFRLLEVDNRLVVPIN 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127873173 173 THIRVIVSAADVLHSWAVPSLGVKCDAIPGRLNQTSLFIKREGLYYGQCSEICGINHGFMPIVVEAVSLPNYVTWISNKL 252
Cdd:MTH00023  159 THVRILVTGADVLHSFAVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWLLSLS 238


                  ..
gi 2127873173 253 SE 254
Cdd:MTH00023  239 ND 240
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 19-250 2.11e-114

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 327.17  E-value: 2.11e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127873173  19 NW-QLGFQDPATPIMEGIINLHHDLMFFICVVSIFVSWMLGRTLWHFEYKQNpvpstLAHGTLIEMIWTITPAFILLVIA 97
Cdd:MTH00154    3 TWsNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRF-----LLEGQEIEIIWTILPAIILIFIA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127873173  98 IPSFSLLYAMDEVISPAITVKTLGHQWYWSYEYSDYVNeddesIAFDSYMIPEEDLELGQLRLLEVDNHMVVPVNTHIRV 177
Cdd:MTH00154   78 LPSLRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKN-----IEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRI 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2127873173 178 IVSAADVLHSWAVPSLGVKCDAIPGRLNQTSLFIKREGLYYGQCSEICGINHGFMPIVVEAVSLPNYVTWISN 250
Cdd:MTH00154  153 LITAADVIHSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKN 225
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 15-254 1.92e-110

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 317.49  E-value: 1.92e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127873173  15 DAAENWQLGFQDPATPIMEGIINLHHDLMFFICVVSIFVSWMLGRTLWHFEYKQnpvpsTLAHGTLIEMIWTITPAFILL 94
Cdd:MTH00051    2 DAPEPWQLGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHK-----YLFEGTLIEIIWTLIPAAILI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127873173  95 VIAIPSFSLLYAMDEVISPAITVKTLGHQWYWSYEYSDYvneDDESIAFDSYMIPEEDLELGQLRLLEVDNHMVVPVNTH 174
Cdd:MTH00051   77 FIAFPSLKLLYLMDEVIDPALTIKAIGHQWYWSYEYSDY---GTDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQ 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127873173 175 IRVIVSAADVLHSWAVPSLGVKCDAIPGRLNQTSLFIKREGLYYGQCSEICGINHGFMPIVVEAVSLPNYVTWISNKLSE 254
Cdd:MTH00051  154 VRVLVTAADVLHSFAVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINWVATQSEE 233
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 17-250 5.08e-110

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 316.09  E-value: 5.08e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127873173  17 AENWQLGFQDPATPIMEGIINLH-HDLM--FFIC-VVSIFVSWMLGRTLWHfeykqnpvpSTLAHGTLIEMIWTITPAFI 92
Cdd:MTH00117    2 ANPSQLGFQDASSPIMEELLFFHdHALMvaLLISsLVLYLLTLMLTTKLTH---------TNTVDAQEVELIWTILPAIV 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127873173  93 LLVIAIPSFSLLYAMDEVISPAITVKTLGHQWYWSYEYSDYVNeddesIAFDSYMIPEEDLELGQLRLLEVDNHMVVPVN 172
Cdd:MTH00117   73 LILLALPSLRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKD-----LSFDSYMIPTQDLPNGHFRLLEVDHRMVIPME 147

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2127873173 173 THIRVIVSAADVLHSWAVPSLGVKCDAIPGRLNQTSLFIKREGLYYGQCSEICGINHGFMPIVVEAVSLPNYVTWISN 250
Cdd:MTH00117  148 SPIRILITAEDVLHSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSL 225
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 21-250 4.65e-106

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 306.09  E-value: 4.65e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127873173  21 QLGFQDPATPIMEGIINLHHDLMFFICVVSIFVSWMLgrTLWHFEYKQNpvpSTLAHGTLIEMIWTITPAFILLVIAIPS 100
Cdd:MTH00140    6 QLGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYML--VLLLFNKFSC---RTILEAQKLETIWTIVPALILVFLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127873173 101 FSLLYAMDEVISPAITVKTLGHQWYWSYEYSDYVNeddesIAFDSYMIPEEDLELGQLRLLEVDNHMVVPVNTHIRVIVS 180
Cdd:MTH00140   81 LRLLYLLDETNNPLLTVKAIGHQWYWSYEYSDFSV-----IEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVT 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127873173 181 AADVLHSWAVPSLGVKCDAIPGRLNQTSLFIKREGLYYGQCSEICGINHGFMPIVVEAVSLPNYVTWISN 250
Cdd:MTH00140  156 SADVIHSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWLEL 225
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 19-254 3.63e-105

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 303.93  E-value: 3.63e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127873173  19 NW-QLGFQDPATPIMEGIINLHHDLMFFICVVSIFVSWMLGR------TLWHFEYKQNpvpstlahgtlIEMIWTITPAF 91
Cdd:MTH00038    3 TWlQLGLQDASSPLMEELIYFHDYALIILTLITILVFYGLASllfsspTNRFFLEGQE-----------LETIWTIVPAF 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127873173  92 ILLVIAIPSFSLLYAMDEVISPAITVKTLGHQWYWSYEYSDYvneddESIAFDSYMIPEEDLELGQLRLLEVDNHMVVPV 171
Cdd:MTH00038   72 ILIFIALPSLQLLYLMDEVNNPFLTIKAIGHQWYWSYEYTDY-----NDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPY 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127873173 172 NTHIRVIVSAADVLHSWAVPSLGVKCDAIPGRLNQTSLFIKREGLYYGQCSEICGINHGFMPIVVEAVSLPNYVTWISNK 251
Cdd:MTH00038  147 QTPIRVLVSSADVLHSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVSNF 226


                  ...
gi 2127873173 252 LSE 254
Cdd:MTH00038  227 LEE 229
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 21-250 2.09e-102

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 296.89  E-value: 2.09e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127873173  21 QLGFQDPATPIMEGIInLHHD----LMFFICVVSIFVSWMLgrtlwhfeYKQNPVPSTLAHGTLIEMIWTITPAFILLVI 96
Cdd:MTH00168    6 QLGLQDAASPVMEELI-LFHDhallILVLILTLVLYSLLVL--------VTSKYTNRFLLDSQMIEFVWTIIPAFILISL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127873173  97 AIPSFSLLYAMDEVISPAITVKTLGHQWYWSYEYSDYVNeddesIAFDSYMIPEEDLELGQLRLLEVDNHMVVPVNTHIR 176
Cdd:MTH00168   77 ALPSLRLLYLMDEIDKPDLTIKAVGHQWYWSYEYTDYND-----LEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIR 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2127873173 177 VIVSAADVLHSWAVPSLGVKCDAIPGRLNQTSLFIKREGLYYGQCSEICGINHGFMPIVVEAVSLPNYVTWISN 250
Cdd:MTH00168  152 VLVTSADVLHSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENWVDS 225
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 21-251 5.40e-99

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 288.15  E-value: 5.40e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127873173  21 QLGFQDPATPIMEGIINLHHDLMFFICVVSIFVSWMLGRTLWHfeykqNPVPSTLAHGTLIEMIWTITPAFILLVIAIPS 100
Cdd:MTH00139    6 QLGFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMSN-----KFTSRSLLESQEVETIWTVLPAFILLFLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127873173 101 FSLLYAMDEVISPAITVKTLGHQWYWSYEYSDYVNeddesIAFDSYMIPEEDLELGQLRLLEVDNHMVVPVNTHIRVIVS 180
Cdd:MTH00139   81 LRLLYLMDEVSDPYLTFKAVGHQWYWSYEYSDFKN-----LSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALIT 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2127873173 181 AADVLHSWAVPSLGVKCDAIPGRLNQTSLFIKREGLYYGQCSEICGINHGFMPIVVEAVSLPNYVTWISNK 251
Cdd:MTH00139  156 AADVLHSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEWILEK 226
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 21-253 7.04e-99

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 288.22  E-value: 7.04e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127873173  21 QLGFQDPATPIMEGIINLH-HDLM--FFICVVSIFVSWMLGRTlwhfeykqNPVPSTLAHGTLIEMIWTITPAFILLVIA 97
Cdd:MTH00076    6 QLGFQDAASPIMEELLHFHdHALMavFLISTLVLYIITIMMTT--------KLTNTNTMDAQEIEMVWTIMPAIILIVIA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127873173  98 IPSFSLLYAMDEVISPAITVKTLGHQWYWSYEYSDYvneddESIAFDSYMIPEEDLELGQLRLLEVDNHMVVPVNTHIRV 177
Cdd:MTH00076   78 LPSLRILYLMDEINDPHLTVKAIGHQWYWSYEYTDY-----EDLSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRM 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2127873173 178 IVSAADVLHSWAVPSLGVKCDAIPGRLNQTSLFIKREGLYYGQCSEICGINHGFMPIVVEAVSLPNYVTWISNKLS 253
Cdd:MTH00076  153 LITAEDVLHSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLNWSSSMLE 228
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 21-249 1.54e-98

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 287.00  E-value: 1.54e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127873173  21 QLGFQDPATPIMEGIINLH-HDLM--FFICVVSIFV-SWMLGRTLWHfeykqnpvPSTLaHGTLIEMIWTITPAFILLVI 96
Cdd:MTH00098    6 QLGFQDATSPIMEELLHFHdHTLMivFLISSLVLYIiSLMLTTKLTH--------TSTM-DAQEVETIWTILPAIILILI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127873173  97 AIPSFSLLYAMDEVISPAITVKTLGHQWYWSYEYSDYvneddESIAFDSYMIPEEDLELGQLRLLEVDNHMVVPVNTHIR 176
Cdd:MTH00098   77 ALPSLRILYMMDEINNPSLTVKTMGHQWYWSYEYTDY-----EDLSFDSYMIPTSDLKPGELRLLEVDNRVVLPMEMPIR 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2127873173 177 VIVSAADVLHSWAVPSLGVKCDAIPGRLNQTSLFIKREGLYYGQCSEICGINHGFMPIVVEAVSLPNYVTWIS 249
Cdd:MTH00098  152 MLISSEDVLHSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKWSA 224
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 113-247 6.72e-96

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: 276.76  E-value: 6.72e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127873173 113 PAITVKTLGHQWYWSYEYSDYVNeddesIAFDSYMIPEEDLELGQLRLLEVDNHMVVPVNTHIRVIVSAADVLHSWAVPS 192
Cdd:cd13912     1 PSLTIKAIGHQWYWSYEYSDFND-----LEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPS 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2127873173 193 LGVKCDAIPGRLNQTSLFIKREGLYYGQCSEICGINHGFMPIVVEAVSLPNYVTW 247
Cdd:cd13912    76 LGIKVDAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 21-254 1.80e-93

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 274.28  E-value: 1.80e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127873173  21 QLGFQDPATPIMEGIINLHHDLMFFICVVSIFVSWMLGRTlwhfeykqnpVPSTLAHGTL-----IEMIWTITPAFILLV 95
Cdd:MTH00129    6 QLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAM----------VSTKLTNKYIldsqeIEIIWTVLPAVILIL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127873173  96 IAIPSFSLLYAMDEVISPAITVKTLGHQWYWSYEYSDYvneddESIAFDSYMIPEEDLELGQLRLLEVDNHMVVPVNTHI 175
Cdd:MTH00129   76 IALPSLRILYLMDEINDPHLTIKAMGHQWYWSYEYTDY-----EDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPI 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2127873173 176 RVIVSAADVLHSWAVPSLGVKCDAIPGRLNQTSLFIKREGLYYGQCSEICGINHGFMPIVVEAVSLPNYVTWISNKLSE 254
Cdd:MTH00129  151 RVLVSAEDVLHSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLMLED 229
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 19-250 2.35e-91

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 269.03  E-value: 2.35e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127873173  19 NW-QLGFQDPATPIMEGIINLH-HDLMFFICVVSIFVSWMLGRTLwhfeykQNPVPSTLAHGTLIEMIWTITPAFILLVI 96
Cdd:MTH00008    3 HWgQLMFQDAASPVMLQLISFHdHALLILTLVLTVVGYAMTSLMF------NKLSNRYILEAQQIETIWTILPALILLFL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127873173  97 AIPSFSLLYAMDEVISPAITVKTLGHQWYWSYEYSDYVNeddesIAFDSYMIPEEDLELGQLRLLEVDNHMVVPVNTHIR 176
Cdd:MTH00008   77 AFPSLRLLYLMDEVSNPSITLKTIGHQWYWSYEYSDFSN-----LEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIR 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2127873173 177 VIVSAADVLHSWAVPSLGVKCDAIPGRLNQTSLFIKREGLYYGQCSEICGINHGFMPIVVEAVSLPNYVTWISN 250
Cdd:MTH00008  152 VLVTAADVIHSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKWVSS 225
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 15-248 1.01e-90

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 268.82  E-value: 1.01e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127873173  15 DAAENWQLGFQDPATPIMEGIINLHHDLMFFICVVSIFVSWMLGRTLW---HFEYKQNPVpstlaHGTLIEMIWTITPAF 91
Cdd:MTH00027   28 DANEPWQLGFQDAGSPVMEEIIMLHDQILFILTIIVGVVLWLIIRILLgnnYYSYYWNKL-----DGSLIEVIWTLIPAF 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127873173  92 ILLVIAIPSFSLLYAMDE-VISPAITVKTLGHQWYWSYEYSDYvneDDESIAFDSYMIPEEDLELGQLRLLEVDNHMVVP 170
Cdd:MTH00027  103 ILILIAFPSLRLLYIMDEcGFSANITIKVTGHQWYWSYSYEDY---GEKNIEFDSYMIPTADLEFGDLRLLEVDNRLILP 179

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2127873173 171 VNTHIRVIVSAADVLHSWAVPSLGVKCDAIPGRLNQTSLFIKREGLYYGQCSEICGINHGFMPIVVEAVSLPNYVTWI 248
Cdd:MTH00027  180 VDTNVRVLITAADVLHSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYIDWI 257
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 17-254 2.80e-88

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 261.36  E-value: 2.80e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127873173  17 AENWQLGFQDPATPIMEGIINLH-HDLM--FFICVVSIFVSWMLGRTLWHFEYkqnpvpstLAHGTLIEMIWTITPAFIL 93
Cdd:MTH00185    2 AHPSQLGLQDAASPVMEELIHFHdHTLMivFLISTLVLYIIVAMVTTKLTNKY--------ILDSQEIEIVWTILPAIIL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127873173  94 LVIAIPSFSLLYAMDEVISPAITVKTLGHQWYWSYEYSDYvneddESIAFDSYMIPEEDLELGQLRLLEVDNHMVVPVNT 173
Cdd:MTH00185   74 IMIALPSLRILYLMDEINDPHLTIKAMGHQWYWSYEYTDY-----EQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMES 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127873173 174 HIRVIVSAADVLHSWAVPSLGVKCDAIPGRLNQTSLFIKREGLYYGQCSEICGINHGFMPIVVEAVSLPNYVTWISNKLS 253
Cdd:MTH00185  149 PIRVLITAEDVLHSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLMLE 228


                  .
gi 2127873173 254 E 254
Cdd:MTH00185  229 E 229
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
115-239 6.42e-82

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 241.16  E-value: 6.42e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127873173 115 ITVKTLGHQWYWSYEYSDYVNeddesIAFDSYMIPEEDLELGQLRLLEVDNHMVVPVNTHIRVIVSAADVLHSWAVPSLG 194
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGD-----LEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLG 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2127873173 195 VKCDAIPGRLNQTSLFIKREGLYYGQCSEICGINHGFMPIVVEAV 239
Cdd:pfam00116  76 IKTDAVPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 44-252 4.53e-65

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 202.16  E-value: 4.53e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127873173  44 FFICVVSIFVSWMLGrtlwHFEYKQNpvpstLAHGTLIEMIWTITPAFILLVIAIPSFSLLYAMDEV-ISPAITVKTLGH 122
Cdd:MTH00080   35 VLAFVVFLFLYLISN----NFYFKSK-----KIEYQFGELLCSVFPVLILLMQMVPSLSLLYYYGLMnLDSNLTVKVTGH 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127873173 123 QWYWSYEYSDYVNeddesIAFDSYMIPEEDLELGQLRLLEVDNHMVVPVNTHIRVIVSAADVLHSWAVPSLGVKCDAIPG 202
Cdd:MTH00080  106 QWYWSYEFSDIPG-----LEFDSYMKSLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDAMSG 180

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2127873173 203 RLNQTSLFIKREGLYYGQCSEICGINHGFMPIVVEAVSLPNYVTWISNKL 252
Cdd:MTH00080  181 ILSTLCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKEWCKLLL 230
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
20-251 6.27e-65

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 201.60  E-value: 6.27e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127873173  20 WQLGFQDPATPIMEGIINLHHDLMFFICVVSIFVSWMLGRTLWHFEYKQNP-VPSTLAHGTLIEMIWTITPAFILLVIAI 98
Cdd:COG1622    17 GQLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLLLYFAIRYRRRKGDaDPAQFHHNTKLEIVWTVIPIIIVIVLAV 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127873173  99 PSFSLLYAMDEVISPAITVKTLGHQWYWSYEYsdyvneddesiafdsymiPEEDLElgqlrlleVDNHMVVPVNTHIRVI 178
Cdd:COG1622    97 PTLRVLHALDDAPEDPLTVEVTGYQWKWLFRY------------------PDQGIA--------TVNELVLPVGRPVRFL 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2127873173 179 VSAADVLHSWAVPSLGVKCDAIPGRLNQTSLFIKREGLYYGQCSEICGINHGFMPIVVEAVSLPNYVTWISNK 251
Cdd:COG1622   151 LTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAEQ 223
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 136-244 2.30e-50

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 162.30  E-value: 2.30e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127873173 136 EDDESI----AFDSYMIPEEDLELGQLRLLEVDNHMVVPVNTHIRVIVSAADVLHSWAVPSLGVKCDAIPGRLNQTSLFI 211
Cdd:PTZ00047   40 EDPDLIpkyySFQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFI 119

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2127873173 212 KREGLYYGQCSEICGINHGFMPIVVEAVSLPNY 244
Cdd:PTZ00047  120 LREGVFYGQCSEMCGTLHGFMPIVVEAVSPEAY 152
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 27-249 2.41e-49

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: 161.01  E-value: 2.41e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127873173  27 PATPIMEGIINLHHDLMFFICVVSIFVSWMLGRTLWHFEYK-QNPVPSTLAHGTLIEMIWTITPAFILLVIAIPSFS-LL 104
Cdd:TIGR02866   1 PGGEIAQQIAFLFLFVLAVSTLISLLVAALLAYVVWKFRRKgDEEKPSQIHGNRRLEYVWTVIPLIIVVGLFAATAKgLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127873173 105 YAMDEVISPAITVKTLGHQWYWSYEYSDYvneddesiafdsymipeedlelgqlrLLEVDNHMVVPVNTHIRVIVSAADV 184
Cdd:TIGR02866  81 YLERPIPKDALKVKVTGYQWWWDFEYPES--------------------------GFTTVNELVLPAGTPVELQVTSKDV 134

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2127873173 185 LHSWAVPSLGVKCDAIPGRLNQTSLFIKREGLYYGQCSEICGINHGFMPIVVEAVSLPNYVTWIS 249
Cdd:TIGR02866 135 IHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYVE 199
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 80-239 3.58e-40

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 137.39  E-value: 3.58e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127873173  80 LIEMIWTITPAFILLVIAIPSFSLLYAmDEVISPAITVKTLGHQWYWSYEYSDyvneddeSIAFDSYMIPEEDLelgqlr 159
Cdd:MTH00047   48 VLELLWTVVPTLLVLVLCFLNLNFITS-DLDCFSSETIKVIGHQWYWSYEYSF-------GGSYDSFMTDDIFG------ 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127873173 160 lleVDNHMVVPVNTHIRVIVSAADVLHSWAVPSLGVKCDAIPGRLNQTSLFIKREGLYYGQCSEICGINHGFMPIVVEAV 239
Cdd:MTH00047  114 ---VDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCPDRHGVFVGYCSELCGVGHSYMPIVIEVV 190
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 16-103 1.11e-29

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: 106.65  E-value: 1.11e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127873173  16 AAENWQLGFQDPATPIMEGIINLHHDLMFFICVVSIFVSWMLGRTLWHFEYKQNPVPST-LAHGTLIEMIWTITPAFILL 94
Cdd:pfam02790   1 MPTPWGLGFQDAASPLMEGLLELHDYIMFILTLILILVLYILVTCLIRFNRRKNPITARyTTHGQTIEIIWTIIPAVILI 80


                  ....*....
gi 2127873173  95 VIAIPSFSL 103
Cdd:pfam02790  81 LIALPSFKL 89
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 115-237 3.63e-25

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


Pssm-ID: 259911 [Multi-domain]  Cd Length: 95  Bit Score: 95.44  E-value: 3.63e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127873173 115 ITVKTLGHQWYWSYEYSDyvneddesiafdsymipeedlelgqlrlLEVDNHMVVPVNTHIRVIVSAADVLHSWAVPSLG 194
Cdd:cd13842     1 LTVYVTGVQWSWTFIYPN----------------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLG 52

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2127873173 195 VKCDAIPGRLNQTSLFIKREGLYYGQCSEICGINHGFMPIVVE 237
Cdd:cd13842    53 VKVDAVPGYTSELWFVADKPGTYTIICAEYCGLGHSYMLGKVE 95
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 114-239 5.15e-23

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: 89.99  E-value: 5.15e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127873173 114 AITVKTLGHQWYWSYEYSDYvneddesiafdsymiPEEDLELGqlrllevdNHMVVPVNTHIRVIVSAADVLHSWAVPSL 193
Cdd:cd04213     1 ALTIEVTGHQWWWEFRYPDE---------------PGRGIVTA--------NELHIPVGRPVRLRLTSADVIHSFWVPSL 57

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2127873173 194 GVKCDAIPGRLNQTSLFIKREGLYYGQCSEICGINHGFMPIVVEAV 239
Cdd:cd04213    58 AGKMDMIPGRTNRLWLQADEPGVYRGQCAEFCGASHALMRFKVIAL 103
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 114-237 7.76e-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: 86.93  E-value: 7.76e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127873173 114 AITVKTLGHQWYWSYEYSDYvneddesiafDSYMIPEEDLELGQLRLlevdnhmvvPVNTHIRVIVSAADVLHSWAVPSL 193
Cdd:cd13919     1 ALVVEVTAQQWAWTFRYPGG----------DGKLGTDDDVTSPELHL---------PVGRPVLFNLRSKDVIHSFWVPEF 61

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2127873173 194 GVKCDAIPGRLNQTSLFIKREGLYYGQCSEICGINHGFM--PIVVE 237
Cdd:cd13919    62 RVKQDAVPGRTTRLWFTPTREGEYEVRCAELCGLGHYRMraTVKVV 107
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 114-238 2.80e-18

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


Pssm-ID: 259982 [Multi-domain]  Cd Length: 98  Bit Score: 77.28  E-value: 2.80e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127873173 114 AITVKTLGHQWYWSYEYSDYVNEDDEsiafdsymipeedlelgqlrllevdnhMVVPVNTHIRVIVSAADVLHSWAVPSL 193
Cdd:cd13915     1 ALEIQVTGRQWMWEFTYPNGKREINE---------------------------LHVPVGKPVRLILTSKDVIHSFYVPAF 53

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2127873173 194 GVKCDAIPGRLNQTSLFIKREGLYYGQCSEICGINHGFMPIVVEA 238
Cdd:cd13915    54 RIKQDVVPGRYTYLWFEATKPGEYDLFCTEYCGTGHSGMIGKVRV 98
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 115-248 7.18e-17

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


Pssm-ID: 259981 [Multi-domain]  Cd Length: 108  Bit Score: 73.98  E-value: 7.18e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127873173 115 ITVKTLGHQWYWSYEYSDYVNEDDESiafdsymipeedlelgqlrllevdnhMVVPVNTHIRVIVSAADVLHSWAVPSLG 194
Cdd:cd13914     1 VEIEVEAYQWGWEFSYPEANVTTSEQ--------------------------LVIPADRPVYFRITSRDVIHAFHVPELG 54

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2127873173 195 VKCDAIPGRLNQTSLFIKREGLYYGQCSEICGINHGFMPIVVEAVSLPNYVTWI 248
Cdd:cd13914    55 LKQDAFPGQYNTIKTEATEEGEYQLYCAEYCGAGHSQMLSTVTVVSQDEYQQWL 108
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 90-247 8.80e-17

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


Pssm-ID: 259985 [Multi-domain]  Cd Length: 139  Bit Score: 74.41  E-value: 8.80e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127873173  90 AFILL-VIAIPSFSLLYAMD---EVISPAITVKTLGHQWYWSYEYSDYVNEDDEsiafdsymipeedlelgqlrllevdn 165
Cdd:cd13918     4 AIIVIsLIVWTYGMLLYVEDppdEADEDALEVEVEGFQFGWQFEYPNGVTTGNT-------------------------- 57

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127873173 166 hMVVPVNTHIRVIVSAADVLHSWAVPSLGVKCDAIPGRLNQTSLFIKREGLYYGQCSEICGINHGFMPIVVEAVSLPNYV 245
Cdd:cd13918    58 -LRVPADTPIALRVTSTDVFHTFGIPELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEFE 136


                  ..
gi 2127873173 246 TW 247
Cdd:cd13918   137 AW 138
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 165-237 2.19e-09

C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and some archaea, which catalyze the reduction of O2 and simultaneously pump protons across the membrane. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. The ba3 family contains oxidases that lack the conserved residues that form the D- and K-pathways in CcO and ubiquinol oxidase. Instead, they contain a potential alternative K-pathway. Additional proton channels have been proposed for this family of oxidases but none have been identified definitively.


Pssm-ID: 259980 [Multi-domain]  Cd Length: 99  Bit Score: 53.34  E-value: 2.19e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2127873173 165 NHMVVPVNTHIRVIVSAADVLHSWAVPSLGVKCDAIPGRLNQTSLFIKREGLYYGQCSEICGINHGFM--PIVVE 237
Cdd:cd13913    25 NEIEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNMygKIIVE 99
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 158-237 1.04e-05

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


Pssm-ID: 259860 [Multi-domain]  Cd Length: 110  Bit Score: 43.37  E-value: 1.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127873173 158 LRLLEVDNHMVVPVNTHIRV-IVSAADVLHSWAVPSLGVKCDAI---------------PGRLNQTSLFIKREGLYYGQC 221
Cdd:cd00920    16 GVLLFGPPVLVVPVGDTVRVqFVNKLGENHSVTIAGFGVPVVAMagganpglvntlvigPGESAEVTFTTDQAGVYWFYC 95

                          90
                  ....*....|....*.
gi 2127873173 222 SEICGINHGfMPIVVE 237
Cdd:cd00920    96 TIPGHNHAG-MVGTIN 110
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 165-239 2.23e-03

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: 36.37  E-value: 2.23e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2127873173 165 NHMVVPVNTHIRVIVSAADVLHSWAVPSLGVKCDAIPGRLNQTSLFIKREGLYYGQCSEICGinHGF--MPIVVEAV 239
Cdd:cd04212    25 NELVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGTYQGLSANYSG--EGFsdMKFKVLAV 99
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 115-232 4.58e-03

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


Pssm-ID: 259983 [Multi-domain]  Cd Length: 93  Bit Score: 35.44  E-value: 4.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2127873173 115 ITVKTLGHQWYWSyeysdyvneddesiafdsyMIPEEdlelgqlrllevdnhmvVPVNTHIRVIVSAADVLHSWAVPS-- 192
Cdd:cd13916     1 QVVAVTGHQWYWE-------------------LSRTE-----------------IPAGKPVEFRVTSADVNHGFGIYDpd 44

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2127873173 193 --LGVKCDAIPGRLNQTSLFIKREGLYYGQCSEICGINHGFM 232
Cdd:cd13916    45 mrLLAQTQAMPGYTNVLRYTFDKPGTYTILCLEYCGLAHHVM 86
FimT COG4970
Type IV pilus assembly protein FimT [Cell motility, Extracellular structures];
79-106 9.39e-03

Type IV pilus assembly protein FimT [Cell motility, Extracellular structures];


Pssm-ID: 443996 [Multi-domain]  Cd Length: 73  Bit Score: 34.05  E-value: 9.39e-03
                          10        20
                  ....*....|....*....|....*...
gi 2127873173  79 TLIEMIWTITPAFILLVIAIPSFSLLYA 106
Cdd:COG4970    12 TLIELLVVLAILAILAAIAVPSFSSLIA 39
 
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