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Conserved domains on  [gi|15100103|gb|AAK84264|]
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cytochrome c oxidase subunit 2 (mitochondrion) [Rhizophydium sp. 136]

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

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List of domain hits

 Name Accession Description Interval E-value
COX2 super family cl33345
cytochrome c oxidase subunit II; Validated
 8-253 1.19e-95

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: 280.10  E-value: 1.19e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15100103    8 FACLLFSDYPINYSYSFQDPASDWLLGIINLHDNIIFYLIIILTVVLWLLTSALLNPDHLFNLHHGNLIELIWTITPAAI 87
Cdd:MTH00023   2 FNNFFYRDIPEPWQLGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15100103   88 LWMIGLPSLKLLYLMDEILSPEITVKAIGNQWYWSFEYGDHvfdnengePKETIAFDSFMVAEDDLELGEQRNLAVDNYL 167
Cdd:MTH00023  82 LVFIALPSLKLLYLMDEVVSPALTIKAIGHQWYWSYEYSDY--------EGETLEFDSYMVPTSDLNSGDFRLLEVDNRL 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15100103  168 VLPINTSIRMLVTANDVIHSFSINSLGIKVDALPGRINALGFIINRPGQFYGQCSELCGSLHGFMPIGLKAVSLSSYLSF 247
Cdd:MTH00023 154 VVPINTHVRILVTGADVLHSFAVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINW 233


                 ....*.
gi 15100103  248 INSFQE 253
Cdd:MTH00023 234 LLSLSN 239
 
Name Accession Description Interval E-value
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 8-253 1.19e-95

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 280.10  E-value: 1.19e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15100103    8 FACLLFSDYPINYSYSFQDPASDWLLGIINLHDNIIFYLIIILTVVLWLLTSALLNPDHLFNLHHGNLIELIWTITPAAI 87
Cdd:MTH00023   2 FNNFFYRDIPEPWQLGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15100103   88 LWMIGLPSLKLLYLMDEILSPEITVKAIGNQWYWSFEYGDHvfdnengePKETIAFDSFMVAEDDLELGEQRNLAVDNYL 167
Cdd:MTH00023  82 LVFIALPSLKLLYLMDEVVSPALTIKAIGHQWYWSYEYSDY--------EGETLEFDSYMVPTSDLNSGDFRLLEVDNRL 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15100103  168 VLPINTSIRMLVTANDVIHSFSINSLGIKVDALPGRINALGFIINRPGQFYGQCSELCGSLHGFMPIGLKAVSLSSYLSF 247
Cdd:MTH00023 154 VVPINTHVRILVTGADVLHSFAVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINW 233


                 ....*.
gi 15100103  248 INSFQE 253
Cdd:MTH00023 234 LLSLSN 239
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 108-247 7.44e-79

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: 233.62  E-value: 7.44e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15100103 108 PEITVKAIGNQWYWSFEYGDHVfdnengepkeTIAFDSFMVAEDDLELGEQRNLAVDNYLVLPINTSIRMLVTANDVIHS 187
Cdd:cd13912   1 PSLTIKAIGHQWYWSYEYSDFN----------DLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHS 70

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15100103 188 FSINSLGIKVDALPGRINALGFIINRPGQFYGQCSELCGSLHGFMPIGLKAVSLSSYLSF 247
Cdd:cd13912  71 WAVPSLGIKVDAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
110-239 2.85e-61

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 188.77  E-value: 2.85e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15100103   110 ITVKAIGNQWYWSFEYGDHVfdnengepkeTIAFDSFMVAEDDLELGEQRNLAVDNYLVLPINTSIRMLVTANDVIHSFS 189
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFG----------DLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWA 70

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 15100103   190 INSLGIKVDALPGRINALGFIINRPGQFYGQCSELCGSLHGFMPIGLKAV 239
Cdd:pfam00116  71 VPSLGIKTDAVPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
8-240 7.37e-56

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 178.48  E-value: 7.37e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15100103   8 FACLLFSDYPINYSYSFQDPASDWLLGIINLHdNIIFYLIIILTVVLWLLT-------SALLNPDHLFNLHHGNLIELIW 80
Cdd:COG1622   5 LLALLLLALLLSGQLSLPDPAGPIAEEIDDLF-WVSLIIMLVIFVLVFGLLlyfairyRRRKGDADPAQFHHNTKLEIVW 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15100103  81 TITPAAILWMIGLPSLKLLYLMDEILSPEITVKAIGNQWYWSFEYGDHvfdnengepketiafdsfmvaeddlelgeqrN 160
Cdd:COG1622  84 TVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQ-------------------------------G 132

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15100103 161 LAVDNYLVLPINTSIRMLVTANDVIHSFSINSLGIKVDALPGRINALGFIINRPGQFYGQCSELCGSLHGFMPIGLKAVS 240
Cdd:COG1622 133 IATVNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVS 212
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 71-249 8.18e-41

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: 139.05  E-value: 8.18e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15100103    71 HHGNLIELIWTITPAAILW-MIGLPSLKLLYLMDEILSPEITVKAIGNQWYWSFEYGDHVFDNengepketiafdsfmva 149
Cdd:TIGR02866  51 HGNRRLEYVWTVIPLIIVVgLFAATAKGLLYLERPIPKDALKVKVTGYQWWWDFEYPESGFTT----------------- 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15100103   150 eddlelgeqrnlavDNYLVLPINTSIRMLVTANDVIHSFSINSLGIKVDALPGRINALGFIINRPGQFYGQCSELCGSLH 229
Cdd:TIGR02866 114 --------------VNELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGH 179

                         170       180
                  ....*....|....*....|
gi 15100103   230 GFMPIGLKAVSLSSYLSFIN 249
Cdd:TIGR02866 180 SLMLFKVVVVPKEEFDAYVE 199
 
Name Accession Description Interval E-value
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 8-253 1.19e-95

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 280.10  E-value: 1.19e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15100103    8 FACLLFSDYPINYSYSFQDPASDWLLGIINLHDNIIFYLIIILTVVLWLLTSALLNPDHLFNLHHGNLIELIWTITPAAI 87
Cdd:MTH00023   2 FNNFFYRDIPEPWQLGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15100103   88 LWMIGLPSLKLLYLMDEILSPEITVKAIGNQWYWSFEYGDHvfdnengePKETIAFDSFMVAEDDLELGEQRNLAVDNYL 167
Cdd:MTH00023  82 LVFIALPSLKLLYLMDEVVSPALTIKAIGHQWYWSYEYSDY--------EGETLEFDSYMVPTSDLNSGDFRLLEVDNRL 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15100103  168 VLPINTSIRMLVTANDVIHSFSINSLGIKVDALPGRINALGFIINRPGQFYGQCSELCGSLHGFMPIGLKAVSLSSYLSF 247
Cdd:MTH00023 154 VVPINTHVRILVTGADVLHSFAVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINW 233


                 ....*.
gi 15100103  248 INSFQE 253
Cdd:MTH00023 234 LLSLSN 239
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 15-253 5.68e-92

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 270.88  E-value: 5.68e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15100103   15 DYPINYSYSFQDPASDWLLGIINLHDNIIFYLIIILTVVLWLLTSALLNPDHLFNLHHGNLIELIWTITPAAILWMIGLP 94
Cdd:MTH00051   2 DAPEPWQLGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15100103   95 SLKLLYLMDEILSPEITVKAIGNQWYWSFEYGDHvfdnengePKETIAFDSFMVAEDDLELGEQRNLAVDNYLVLPINTS 174
Cdd:MTH00051  82 SLKLLYLMDEVIDPALTIKAIGHQWYWSYEYSDY--------GTDTIEFDSYMIPTSDLNSGDLRLLEVDNRLIVPIQTQ 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15100103  175 IRMLVTANDVIHSFSINSLGIKVDALPGRINALGFIINRPGQFYGQCSELCGSLHGFMPIGLKAVSLSSYLSFINSFQE 253
Cdd:MTH00051 154 VRVLVTAADVLHSFAVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINWVATQSE 232
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 21-251 4.01e-91

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 268.24  E-value: 4.01e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15100103   21 SYSFQDPASDWLLGIINLHDNIIFYLIIILTVVLWLLTSALLNPDHLFNLHHGNLIELIWTITPAAILWMIGLPSLKLLY 100
Cdd:MTH00154   6 NLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPSLRLLY 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15100103  101 LMDEILSPEITVKAIGNQWYWSFEYGDhvFDNengepketIAFDSFMVAEDDLELGEQRNLAVDNYLVLPINTSIRMLVT 180
Cdd:MTH00154  86 LLDEVNNPSITLKTIGHQWYWSYEYSD--FKN--------IEFDSYMIPTNELENNGFRLLDVDNRLVLPMNTQIRILIT 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15100103  181 ANDVIHSFSINSLGIKVDALPGRINALGFIINRPGQFYGQCSELCGSLHGFMPIGLKAVSLSSYLSFINSF 251
Cdd:MTH00154 156 AADVIHSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNM 226
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 23-253 9.74e-90

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 264.88  E-value: 9.74e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15100103   23 SFQDPASDWLLGIINLHDNIIFYLIIILTVVLWLLTSALLNPDHLFNLHHGNLIELIWTITPAAILWMIGLPSLKLLYLM 102
Cdd:MTH00140   8 GFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPSLRLLYLL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15100103  103 DEILSPEITVKAIGNQWYWSFEYGDhvFDNengepketIAFDSFMVAEDDLELGEQRNLAVDNYLVLPINTSIRMLVTAN 182
Cdd:MTH00140  88 DETNNPLLTVKAIGHQWYWSYEYSD--FSV--------IEFDSYMVPENELELGDFRLLEVDNRLVLPYSVDTRVLVTSA 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15100103  183 DVIHSFSINSLGIKVDALPGRINALGFIINRPGQFYGQCSELCGSLHGFMPIGLKAVSLSSYLSFINSFQE 253
Cdd:MTH00140 158 DVIHSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWLELMSE 228
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 21-250 3.34e-82

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 245.66  E-value: 3.34e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15100103   21 SYSFQDPASDWLLGIINLHDNIIFYLIIILTVVLWLLTSALLNPDHLFNLHHGNLIELIWTITPAAILWMIGLPSLKLLY 100
Cdd:MTH00168   6 QLGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPSLRLLY 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15100103  101 LMDEILSPEITVKAIGNQWYWSFEYGDHvfdnengepkETIAFDSFMVAEDDLELGEQRNLAVDNYLVLPINTSIRMLVT 180
Cdd:MTH00168  86 LMDEIDKPDLTIKAVGHQWYWSYEYTDY----------NDLEFDSYMVPTQDLSPGQFRLLEVDNRLVLPMDSKIRVLVT 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15100103  181 ANDVIHSFSINSLGIKVDALPGRINALGFIINRPGQFYGQCSELCGSLHGFMPIGLKAVSLSSYLSFINS 250
Cdd:MTH00168 156 SADVLHSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENWVDS 225
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 23-252 7.52e-82

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 244.82  E-value: 7.52e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15100103   23 SFQDPASDWLLGIINLHDNIIFYLIIILTVVLWLLTSALLNpdhlfNLHHGNL-----IELIWTITPAAILWMIGLPSLK 97
Cdd:MTH00117   8 GFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTT-----KLTHTNTvdaqeVELIWTILPAIVLILLALPSLR 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15100103   98 LLYLMDEILSPEITVKAIGNQWYWSFEYGDHvfdnengepkETIAFDSFMVAEDDLELGEQRNLAVDNYLVLPINTSIRM 177
Cdd:MTH00117  83 ILYLMDEINNPHLTIKAIGHQWYWSYEYTDY----------KDLSFDSYMIPTQDLPNGHFRLLEVDHRMVIPMESPIRI 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15100103  178 LVTANDVIHSFSINSLGIKVDALPGRINALGFIINRPGQFYGQCSELCGSLHGFMPIGLKAVSLSSYLSFINSFQ 252
Cdd:MTH00117 153 LITAEDVLHSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSLLS 227
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 23-253 8.98e-82

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 244.77  E-value: 8.98e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15100103   23 SFQDPASDWLLGIINLHDNIIFYLIIILTVVLWLLTSALLNPDHLFNLHHGNLIELIWTITPAAILWMIGLPSLKLLYLM 102
Cdd:MTH00008   8 MFQDAASPVMLQLISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPSLRLLYLM 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15100103  103 DEILSPEITVKAIGNQWYWSFEYGDhvFDNengepketIAFDSFMVAEDDLELGEQRNLAVDNYLVLPINTSIRMLVTAN 182
Cdd:MTH00008  88 DEVSNPSITLKTIGHQWYWSYEYSD--FSN--------LEFDSYMLPTSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAA 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15100103  183 DVIHSFSINSLGIKVDALPGRINALGFIINRPGQFYGQCSELCGSLHGFMPIGLKAVSLSSYLSFINSFQE 253
Cdd:MTH00008 158 DVIHSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKWVSSFAE 228
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 23-251 1.20e-80

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 241.54  E-value: 1.20e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15100103   23 SFQDPASDWLLGIINLHDNIIFYLIIILTVVLWLLTSALLNPDHLFNLHHGNLIELIWTITPAAILWMIGLPSLKLLYLM 102
Cdd:MTH00139   8 GFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPSLRLLYLM 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15100103  103 DEILSPEITVKAIGNQWYWSFEYGDhvFDNengepketIAFDSFMVAEDDLELGEQRNLAVDNYLVLPINTSIRMLVTAN 182
Cdd:MTH00139  88 DEVSDPYLTFKAVGHQWYWSYEYSD--FKN--------LSFDSYMIPTEDLSSGEFRLLEVDNRLVLPYKSNIRALITAA 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15100103  183 DVIHSFSINSLGIKVDALPGRINALGFIINRPGQFYGQCSELCGSLHGFMPIGLKAVSLSSYLSFINSF 251
Cdd:MTH00139 158 DVLHSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEWILEK 226
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 23-253 6.23e-79

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 237.29  E-value: 6.23e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15100103   23 SFQDPASDWLLGIINLHDNIIFYLIIILTVVLWLLTSALLN-PDHLFNLHhGNLIELIWTITPAAILWMIGLPSLKLLYL 101
Cdd:MTH00038   8 GLQDASSPLMEELIYFHDYALIILTLITILVFYGLASLLFSsPTNRFFLE-GQELETIWTIVPAFILIFIALPSLQLLYL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15100103  102 MDEILSPEITVKAIGNQWYWSFEYGDHvfdnengepkETIAFDSFMVAEDDLELGEQRNLAVDNYLVLPINTSIRMLVTA 181
Cdd:MTH00038  87 MDEVNNPFLTIKAIGHQWYWSYEYTDY----------NDLEFDSYMVPTSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSS 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15100103  182 NDVIHSFSINSLGIKVDALPGRINALGFIINRPGQFYGQCSELCGSLHGFMPIGLKAVSLSSYLSFINSFQE 253
Cdd:MTH00038 157 ADVLHSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVSNFLE 228
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 108-247 7.44e-79

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: 233.62  E-value: 7.44e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15100103 108 PEITVKAIGNQWYWSFEYGDHVfdnengepkeTIAFDSFMVAEDDLELGEQRNLAVDNYLVLPINTSIRMLVTANDVIHS 187
Cdd:cd13912   1 PSLTIKAIGHQWYWSYEYSDFN----------DLEFDSYMIPEDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHS 70

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15100103 188 FSINSLGIKVDALPGRINALGFIINRPGQFYGQCSELCGSLHGFMPIGLKAVSLSSYLSF 247
Cdd:cd13912  71 WAVPSLGIKVDAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 24-253 8.17e-77

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 231.98  E-value: 8.17e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15100103   24 FQDPASDWLLGIINLHDNIIFYLIIILTVVLWLLTSALLNPDHLFNLHHGNLIELIWTITPAAILWMIGLPSLKLLYLMD 103
Cdd:MTH00076   9 FQDAASPIMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPSLRILYLMD 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15100103  104 EILSPEITVKAIGNQWYWSFEYGDhvFDNengepketIAFDSFMVAEDDLELGEQRNLAVDNYLVLPINTSIRMLVTAND 183
Cdd:MTH00076  89 EINDPHLTVKAIGHQWYWSYEYTD--YED--------LSFDSYMIPTQDLTPGQFRLLEVDNRMVVPMESPIRMLITAED 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15100103  184 VIHSFSINSLGIKVDALPGRINALGFIINRPGQFYGQCSELCGSLHGFMPIGLKAVSLSSYLSFINSFQE 253
Cdd:MTH00076 159 VLHSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLNWSSSMLE 228
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 16-244 1.86e-74

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 226.14  E-value: 1.86e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15100103   16 YPINYSysFQDPASDWLLGIINLHDNIIFYLIIILTVVLWLLTSALLNpdhlfNLHHGNL-----IELIWTITPAAILWM 90
Cdd:MTH00098   3 YPFQLG--FQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTT-----KLTHTSTmdaqeVETIWTILPAIILIL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15100103   91 IGLPSLKLLYLMDEILSPEITVKAIGNQWYWSFEYGDHvfdnengepkETIAFDSFMVAEDDLELGEQRNLAVDNYLVLP 170
Cdd:MTH00098  76 IALPSLRILYMMDEINNPSLTVKTMGHQWYWSYEYTDY----------EDLSFDSYMIPTSDLKPGELRLLEVDNRVVLP 145

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15100103  171 INTSIRMLVTANDVIHSFSINSLGIKVDALPGRINALGFIINRPGQFYGQCSELCGSLHGFMPIGLKAVSLSSY 244
Cdd:MTH00098 146 MEMPIRMLISSEDVLHSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYF 219
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 24-253 1.96e-73

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 223.44  E-value: 1.96e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15100103   24 FQDPASDWLLGIINLHDNIIFYLIIILTVVLWLLTSALLNPDHLFNLHHGNLIELIWTITPAAILWMIGLPSLKLLYLMD 103
Cdd:MTH00129   9 FQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPSLRILYLMD 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15100103  104 EILSPEITVKAIGNQWYWSFEYGDHvfdnengepkETIAFDSFMVAEDDLELGEQRNLAVDNYLVLPINTSIRMLVTAND 183
Cdd:MTH00129  89 EINDPHLTIKAMGHQWYWSYEYTDY----------EDLGFDSYMIPTQDLTPGQFRLLEADHRMVVPVESPIRVLVSAED 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15100103  184 VIHSFSINSLGIKVDALPGRINALGFIINRPGQFYGQCSELCGSLHGFMPIGLKAVSLSSYLSFINSFQE 253
Cdd:MTH00129 159 VLHSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLMLE 228
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 7-248 3.72e-72

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 221.44  E-value: 3.72e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15100103    7 NFACLLFSD------YPINYSYSFQDPASDWLLG-----------IINLHDNIIFYLIIILTVVLWLLTSALLNPDHL-- 67
Cdd:MTH00027   3 NVYCLTIVNweggalYPMNVASMIKDANEPWQLGfqdagspvmeeIIMLHDQILFILTIIVGVVLWLIIRILLGNNYYsy 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15100103   68 -FNLHHGNLIELIWTITPAAILWMIGLPSLKLLYLMDE-ILSPEITVKAIGNQWYWSFEYGDHvfdnenGEpkETIAFDS 145
Cdd:MTH00027  83 yWNKLDGSLIEVIWTLIPAFILILIAFPSLRLLYIMDEcGFSANITIKVTGHQWYWSYSYEDY------GE--KNIEFDS 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15100103  146 FMVAEDDLELGEQRNLAVDNYLVLPINTSIRMLVTANDVIHSFSINSLGIKVDALPGRINALGFIINRPGQFYGQCSELC 225
Cdd:MTH00027 155 YMIPTADLEFGDLRLLEVDNRLILPVDTNVRVLITAADVLHSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEIC 234

                        250       260
                 ....*....|....*....|...
gi 15100103  226 GSLHGFMPIGLKAVSLSSYLSFI 248
Cdd:MTH00027 235 GANHSFMPIVVESVSLSKYIDWI 257
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 24-253 5.43e-72

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 219.76  E-value: 5.43e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15100103   24 FQDPASDWLLGIINLHDNIIFYLIIILTVVLWLLT---SALLNPDHLFNLHHgnlIELIWTITPAAILWMIGLPSLKLLY 100
Cdd:MTH00185   9 LQDAASPVMEELIHFHDHTLMIVFLISTLVLYIIVamvTTKLTNKYILDSQE---IEIVWTILPAIILIMIALPSLRILY 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15100103  101 LMDEILSPEITVKAIGNQWYWSFEYGDHvfdnengepkETIAFDSFMVAEDDLELGEQRNLAVDNYLVLPINTSIRMLVT 180
Cdd:MTH00185  86 LMDEINDPHLTIKAMGHQWYWSYEYTDY----------EQLEFDSYMTPTQDLTPGQFRLLETDHRMVVPMESPIRVLIT 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15100103  181 ANDVIHSFSINSLGIKVDALPGRINALGFIINRPGQFYGQCSELCGSLHGFMPIGLKAVSLSSYLSFINSFQE 253
Cdd:MTH00185 156 AEDVLHSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLMLE 228
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
110-239 2.85e-61

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 188.77  E-value: 2.85e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15100103   110 ITVKAIGNQWYWSFEYGDHVfdnengepkeTIAFDSFMVAEDDLELGEQRNLAVDNYLVLPINTSIRMLVTANDVIHSFS 189
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFG----------DLEFDSYMIPTEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWA 70

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 15100103   190 INSLGIKVDALPGRINALGFIINRPGQFYGQCSELCGSLHGFMPIGLKAV 239
Cdd:pfam00116  71 VPSLGIKTDAVPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 1-253 1.85e-58

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 185.21  E-value: 1.85e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15100103    1 MFSVNFNFACLLFSDYpinysysfqdpaSDWllgIINLHDNIIFYLIIILTVVLWLLTSALLNPDHLFNLHHGNLIELIW 80
Cdd:MTH00080   3 FQGYNLNFSNSLFSSY------------MDW---FHNFNCSLLFGEFVLAFVVFLFLYLISNNFYFKSKKIEYQFGELLC 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15100103   81 TITPAAILWMIGLPSLKLLYLMDEI-LSPEITVKAIGNQWYWSFEYGDHvfdnengepkETIAFDSFMVAEDDLELGEQR 159
Cdd:MTH00080  68 SVFPVLILLMQMVPSLSLLYYYGLMnLDSNLTVKVTGHQWYWSYEFSDI----------PGLEFDSYMKSLDQLRLGEPR 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15100103  160 NLAVDNYLVLPINTSIRMLVTANDVIHSFSINSLGIKVDALPGRINALGFIINRPGQFYGQCSELCGSLHGFMPIGLKAV 239
Cdd:MTH00080 138 LLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDAMSGILSTLCYSFPMPGVFYGQCSEICGANHSFMPIAVEVT 217

                        250
                 ....*....|....
gi 15100103  240 SLSSYLSFINSFQE 253
Cdd:MTH00080 218 LLDNFKEWCKLLLD 231
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
8-240 7.37e-56

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 178.48  E-value: 7.37e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15100103   8 FACLLFSDYPINYSYSFQDPASDWLLGIINLHdNIIFYLIIILTVVLWLLT-------SALLNPDHLFNLHHGNLIELIW 80
Cdd:COG1622   5 LLALLLLALLLSGQLSLPDPAGPIAEEIDDLF-WVSLIIMLVIFVLVFGLLlyfairyRRRKGDADPAQFHHNTKLEIVW 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15100103  81 TITPAAILWMIGLPSLKLLYLMDEILSPEITVKAIGNQWYWSFEYGDHvfdnengepketiafdsfmvaeddlelgeqrN 160
Cdd:COG1622  84 TVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQ-------------------------------G 132

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15100103 161 LAVDNYLVLPINTSIRMLVTANDVIHSFSINSLGIKVDALPGRINALGFIINRPGQFYGQCSELCGSLHGFMPIGLKAVS 240
Cdd:COG1622 133 IATVNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVS 212
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 142-244 3.77e-41

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 138.80  E-value: 3.77e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15100103  142 AFDSFMVAEDDLELGEQRNLAVDNYLVLPINTSIRMLVTANDVIHSFSINSLGIKVDALPGRINALGFIINRPGQFYGQC 221
Cdd:PTZ00047  50 SFQSNLVTDEDLKPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQC 129

                         90       100
                 ....*....|....*....|...
gi 15100103  222 SELCGSLHGFMPIGLKAVSLSSY 244
Cdd:PTZ00047 130 SEMCGTLHGFMPIVVEAVSPEAY 152
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 71-249 8.18e-41

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: 139.05  E-value: 8.18e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15100103    71 HHGNLIELIWTITPAAILW-MIGLPSLKLLYLMDEILSPEITVKAIGNQWYWSFEYGDHVFDNengepketiafdsfmva 149
Cdd:TIGR02866  51 HGNRRLEYVWTVIPLIIVVgLFAATAKGLLYLERPIPKDALKVKVTGYQWWWDFEYPESGFTT----------------- 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15100103   150 eddlelgeqrnlavDNYLVLPINTSIRMLVTANDVIHSFSINSLGIKVDALPGRINALGFIINRPGQFYGQCSELCGSLH 229
Cdd:TIGR02866 114 --------------VNELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGH 179

                         170       180
                  ....*....|....*....|
gi 15100103   230 GFMPIGLKAVSLSSYLSFIN 249
Cdd:TIGR02866 180 SLMLFKVVVVPKEEFDAYVE 199
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 74-234 3.95e-39

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 134.70  E-value: 3.95e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15100103   74 NLIELIWTITPAAILwmIGLPSLKLLYLMDEI-LSPEITVKAIGNQWYWSFEYgdhvfdNENGEpketiaFDSFMVAEDD 152
Cdd:MTH00047  47 QVLELLWTVVPTLLV--LVLCFLNLNFITSDLdCFSSETIKVIGHQWYWSYEY------SFGGS------YDSFMTDDIF 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15100103  153 LelgeqrnlaVDNYLVLPINTSIRMLVTANDVIHSFSINSLGIKVDALPGRINALGFIINRPGQFYGQCSELCGSLHGFM 232
Cdd:MTH00047 113 G---------VDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCPDRHGVFVGYCSELCGVGHSYM 183


                 ..
gi 15100103  233 PI 234
Cdd:MTH00047 184 PI 185
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 109-232 2.42e-27

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: 101.18  E-value: 2.42e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15100103 109 EITVKAIGNQWYWSFEYgdhvfdnengePKETIAFDsfmvAEDDLELGEqrnlavdnyLVLPINTSIRMLVTANDVIHSF 188
Cdd:cd13919   1 ALVVEVTAQQWAWTFRY-----------PGGDGKLG----TDDDVTSPE---------LHLPVGRPVLFNLRSKDVIHSF 56

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 15100103 189 SINSLGIKVDALPGRINALGFIINRPGQFYGQCSELCGSLHGFM 232
Cdd:cd13919  57 WVPEFRVKQDAVPGRTTRLWFTPTREGEYEVRCAELCGLGHYRM 100
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 110-233 9.84e-27

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: 99.29  E-value: 9.84e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15100103 110 ITVKAIGNQWYWSFEYGDHVFDNEngepketiafdsfmvaeddlelgeqrnlavdnyLVLPINTSIRMLVTANDVIHSFS 189
Cdd:cd13842   1 LTVYVTGVQWSWTFIYPNVRTPNE---------------------------------IVVPAGTPVRFRVTSPDVIHGFY 47

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 15100103 190 INSLGIKVDALPGRINALGFIINRPGQFYGQCSELCGSLHGFMP 233
Cdd:cd13842  48 IPNLGVKVDAVPGYTSELWFVADKPGTYTIICAEYCGLGHSYML 91
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 109-232 1.15e-25

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: 1.15e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15100103 109 EITVKAIGNQWYWSFEYGDhvfdnENGEPKETIafdsfmvaeddlelgeqrnlavdNYLVLPINTSIRMLVTANDVIHSF 188
Cdd:cd04213   1 ALTIEVTGHQWWWEFRYPD-----EPGRGIVTA-----------------------NELHIPVGRPVRLRLTSADVIHSF 52

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 15100103 189 SINSLGIKVDALPGRINALGFIINRPGQFYGQCSELCGSLHGFM 232
Cdd:cd04213  53 WVPSLAGKMDMIPGRTNRLWLQADEPGVYRGQCAEFCGASHALM 96
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 110-232 3.38e-22

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


Pssm-ID: 259982 [Multi-domain]  Cd Length: 98  Bit Score: 87.68  E-value: 3.38e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15100103 110 ITVKAIGNQWYWSFEYGDhvfdnengePKETIafdsfmvaeddlelgeqrnlavdNYLVLPINTSIRMLVTANDVIHSFS 189
Cdd:cd13915   2 LEIQVTGRQWMWEFTYPN---------GKREI-----------------------NELHVPVGKPVRLILTSKDVIHSFY 49

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 15100103 190 INSLGIKVDALPGRINALGFIINRPGQFYGQCSELCGSLHGFM 232
Cdd:cd13915  50 VPAFRIKQDVVPGRYTYLWFEATKPGEYDLFCTEYCGTGHSGM 92
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 87-232 2.73e-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: 259985 [Multi-domain]  Cd Length: 139  Bit Score: 78.65  E-value: 2.73e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15100103  87 ILWMIGLpslkLLYLMDEILSPE---ITVKAIGNQWYWSFEYgdhvfdnENGepketiafdsfmvaeddlelGEQRNlav 163
Cdd:cd13918  11 IVWTYGM----LLYVEDPPDEADedaLEVEVEGFQFGWQFEY-------PNG--------------------VTTGN--- 56

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15100103 164 dnYLVLPINTSIRMLVTANDVIHSFSINSLGIKVDALPGRINALGFIINRPGQFYGQCSELCGSLHGFM 232
Cdd:cd13918  57 --TLRVPADTPIALRVTSTDVFHTFGIPELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLM 123
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 109-244 7.17e-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: 259981 [Multi-domain]  Cd Length: 108  Bit Score: 76.68  E-value: 7.17e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15100103 109 EITVKAIgnQWYWSFEYGDhvfdnengepketiafdsfmvaeddlelgeqRNLAVDNYLVLPINTSIRMLVTANDVIHSF 188
Cdd:cd13914   2 EIEVEAY--QWGWEFSYPE-------------------------------ANVTTSEQLVIPADRPVYFRITSRDVIHAF 48

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15100103 189 SINSLGIKVDALPGRINALGFIINRPGQFYGQCSELCGSLHGFMPIGLKAVSLSSY 244
Cdd:cd13914  49 HVPELGLKQDAFPGQYNTIKTEATEEGEYQLYCAEYCGAGHSQMLSTVTVVSQDEY 104
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 17-98 2.41e-17

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: 74.68  E-value: 2.41e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15100103    17 PINYSYSFQDPASDWLLGIINLHDNIIFYLIIILTVVLWLLTSALLNPDHLFN------LHHGNLIELIWTITPAAILWM 90
Cdd:pfam02790   2 PTPWGLGFQDAASPLMEGLLELHDYIMFILTLILILVLYILVTCLIRFNRRKNpitaryTTHGQTIEIIWTIIPAVILIL 81


                  ....*...
gi 15100103    91 IGLPSLKL 98
Cdd:pfam02790  82 IALPSFKL 89
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 165-232 7.35e-11

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: 57.58  E-value: 7.35e-11
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15100103 165 NYLVLPINTSIRMLVTANDVIHSFSINSLGIKVDALPGRINALGFIINRPGQFYGQCSELCGSLHGFM 232
Cdd:cd13913  25 NEIEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNM 92
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 110-231 1.60e-10

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: 56.40  E-value: 1.60e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15100103 110 ITVKAIGNQWYWSFEYgdhvfdnengePKETIAfdsfmvaeddlelgeqrnlAVdNYLVLPINTSIRMLVTANDVIHSFS 189
Cdd:cd04212   1 LEIQVVSLDWKWLFIY-----------PEQGIA-------------------TV-NELVIPVGRPVNFRLTSDSVMNSFF 49

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 15100103 190 INSLGIKVDALPGRINALGFIINRPGQFYGQCSELCGslHGF 231
Cdd:cd04212  50 IPQLGGQIYAMAGMQTQLHLIADKPGTYQGLSANYSG--EGF 89
PRK10525 PRK10525
cytochrome o ubiquinol oxidase subunit II; Provisional
 69-240 2.14e-06

cytochrome o ubiquinol oxidase subunit II; Provisional


Pssm-ID: 182518 [Multi-domain]  Cd Length: 315  Bit Score: 47.87  E-value: 2.14e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15100103   69 NLHHGNLIELI-WTItPAAILWMIGLPSLKLLYLMDE---ILSPE--ITVKAIGNQWYWSFEYgdhvfdnengePKETIA 142
Cdd:PRK10525  81 NWSHSNKVEAVvWTV-PILIIIFLAVLTWKTTHALEPskpLAHDEkpITIEVVSMDWKWFFIY-----------PEQGIA 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15100103  143 fdsfmvaeddlelgeqrnlaVDNYLVLPINTSIRMLVTANDVIHSFSINSLGIKVDALPGRINALGFIINRPGQFYGQCS 222
Cdd:PRK10525 149 --------------------TVNEIAFPANVPVYFKVTSNSVMNSFFIPRLGSQIYAMAGMQTRLHLIANEPGTYDGISA 208

                        170
                 ....*....|....*...
gi 15100103  223 ELCGslHGFMPIGLKAVS 240
Cdd:PRK10525 209 SYSG--PGFSGMKFKAIA 224
CuRO_HCO_II_like_4 cd13917
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 167-232 3.93e-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: 259984 [Multi-domain]  Cd Length: 88  Bit Score: 43.90  E-value: 3.93e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15100103 167 LVLPINTSIRMLVTANDVIHSFSINSLGIKVDALPGRINALGFIINRPGQFYGQCSELCGSLHGFM 232
Cdd:cd13917  16 LVLKKGKTYRLHLSSLDVQHGFSLQPKNINFQVLPGYEWVITMTPNETGEFHIICNEYCGIGHHTM 81
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 168-232 1.05e-05

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: 43.14  E-value: 1.05e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15100103 168 VLPINTSIRMLVTANDVIHSFSINS----LGIKVDALPGRINALGFIINRPGQFYGQCSELCGSLHGFM 232
Cdd:cd13916  18 EIPAGKPVEFRVTSADVNHGFGIYDpdmrLLAQTQAMPGYTNVLRYTFDKPGTYTILCLEYCGLAHHVM 86
N2OR_C cd04223
The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase ...
 183-229 1.30e-03

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


Pssm-ID: 259885 [Multi-domain]  Cd Length: 95  Bit Score: 37.21  E-value: 1.30e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 15100103 183 DVIHSFSINSLGIKVDALPGRINALGFIINRPGQFYGQCSELCGSLH 229
Cdd:cd04223  38 DITHGFAIPGYNVNLSLEPGETATVTFVADKPGVYPYYCTEFCSALH 84
 
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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