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Conserved domains on  [gi|517113694|ref|WP_018302512|]
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cytochrome c oxidase subunit II [Wenxinia marina]

Protein Classification

cytochrome c oxidase subunit II( domain architecture ID 11446855)

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|2.60.40.420
EC:  7.1.1.9
Gene Ontology:  GO:0042773|GO:0004129|GO:0005507
SCOP:  4002011|4002191

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
1-186 1.96e-54

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


:

Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 172.32  E-value: 1.96e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517113694   1 MWWVLLAGASLIFLFVMALVA-VAWRSPARPAAEERPFVVG------LGLAFPLVVLAALLAYGLVVGERLLPRPGPEVv 73
Cdd:COG1622   35 LFWVSLIIMLVIFVLVFGLLLyFAIRYRRRKGDADPAQFHHntkleiVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPL- 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517113694  74 TVRAEASQWRWRFGYEDAPGLeTEGVLHIPAARPIDVEITTTDVVHSFWVPRLAGKLDAMPGHVNVLRIEADAPGEYGGL 153
Cdd:COG1622  114 TVEVTGYQWKWLFRYPDQGIA-TVNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQ 192

                        170       180       190
                 ....*....|....*....|....*....|...
gi 517113694 154 SAEYNGPGYVQHGFVVVAHGPDEWRAFIEGETP 186
Cdd:COG1622  193 CAELCGTGHAGMRFKVVVVSPEEFDAWLAEQKA 225
 
Name Accession Description Interval E-value
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
1-186 1.96e-54

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 172.32  E-value: 1.96e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517113694   1 MWWVLLAGASLIFLFVMALVA-VAWRSPARPAAEERPFVVG------LGLAFPLVVLAALLAYGLVVGERLLPRPGPEVv 73
Cdd:COG1622   35 LFWVSLIIMLVIFVLVFGLLLyFAIRYRRRKGDADPAQFHHntkleiVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPL- 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517113694  74 TVRAEASQWRWRFGYEDAPGLeTEGVLHIPAARPIDVEITTTDVVHSFWVPRLAGKLDAMPGHVNVLRIEADAPGEYGGL 153
Cdd:COG1622  114 TVEVTGYQWKWLFRYPDQGIA-TVNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQ 192

                        170       180       190
                 ....*....|....*....|....*....|...
gi 517113694 154 SAEYNGPGYVQHGFVVVAHGPDEWRAFIEGETP 186
Cdd:COG1622  193 CAELCGTGHAGMRFKVVVVSPEEFDAWLAEQKA 225
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 2-182 7.39e-40

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: 134.05  E-value: 7.39e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517113694    2 WWVLLAGASLIFLFVMALVA-VAWRSPARPAAEERPFVVG------LGLAFPLVVLAALLAYGlVVGERLLPRPGP-EVV 73
Cdd:TIGR02866  13 FLFVLAVSTLISLLVAALLAyVVWKFRRKGDEEKPSQIHGnrrleyVWTVIPLIIVVGLFAAT-AKGLLYLERPIPkDAL 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517113694   74 TVRAEASQWRWRFGYEDApGLETEGVLHIPAARPIDVEITTTDVVHSFWVPRLAGKLDAMPGHVNVLRIEADAPGEYGGL 153
Cdd:TIGR02866  92 KVKVTGYQWWWDFEYPES-GFTTVNELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGF 170

                         170       180
                  ....*....|....*....|....*....
gi 517113694  154 SAEYNGPGYVQHGFVVVAHGPDEWRAFIE 182
Cdd:TIGR02866 171 CAELCGAGHSLMLFKVVVVPKEEFDAYVE 199
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 73-172 4.54e-37

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: 123.88  E-value: 4.54e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517113694  73 VTVRAEASQWRWRFGYEDAP--GLETEGVLHIPAARPIDVEITTTDVVHSFWVPRLAGKLDAMPGHVNVLRIEADAPGEY 150
Cdd:cd04213    2 LTIEVTGHQWWWEFRYPDEPgrGIVTANELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMDMIPGRTNRLWLQADEPGVY 81

                         90       100
                 ....*....|....*....|..
gi 517113694 151 GGLSAEYNGPGYVQHGFVVVAH 172
Cdd:cd04213   82 RGQCAEFCGASHALMRFKVIAL 103
PRK10525 PRK10525
cytochrome o ubiquinol oxidase subunit II; Provisional
 73-179 1.60e-16

cytochrome o ubiquinol oxidase subunit II; Provisional


Pssm-ID: 182518 [Multi-domain]  Cd Length: 315  Bit Score: 75.61  E-value: 1.60e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517113694  73 VTVRAEASQWRWRFGYEDApGLETEGVLHIPAARPIDVEITTTDVVHSFWVPRLAGKLDAMPGHVNVLRIEADAPGEYGG 152
Cdd:PRK10525 127 ITIEVVSMDWKWFFIYPEQ-GIATVNEIAFPANVPVYFKVTSNSVMNSFFIPRLGSQIYAMAGMQTRLHLIANEPGTYDG 205

                         90       100       110
                 ....*....|....*....|....*....|.
gi 517113694 153 LSAEYNGPGYVQHGFVVVA----HGPDEWRA 179
Cdd:PRK10525 206 ISASYSGPGFSGMKFKAIAtpdrAEFDQWVA 236
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
74-167 1.24e-12

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 61.66  E-value: 1.24e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517113694   74 TVRAEASQWRWRFGYED----------------APG----LETEGVLHIPAARPIDVEITTTDVVHSFWVPRLAGKLDAM 133
Cdd:pfam00116   2 TIKAIGHQWYWSYEYTDfgdlefdsymiptedlEEGqlrlLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDAV 81

                          90       100       110
                  ....*....|....*....|....*....|....
gi 517113694  134 PGHVNVLRIEADAPGEYGGLSAEYNGpgyVQHGF 167
Cdd:pfam00116  82 PGRLNQTSFSIDREGVFYGQCSEICG---INHSF 112
 
Name Accession Description Interval E-value
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
1-186 1.96e-54

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 172.32  E-value: 1.96e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517113694   1 MWWVLLAGASLIFLFVMALVA-VAWRSPARPAAEERPFVVG------LGLAFPLVVLAALLAYGLVVGERLLPRPGPEVv 73
Cdd:COG1622   35 LFWVSLIIMLVIFVLVFGLLLyFAIRYRRRKGDADPAQFHHntkleiVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPL- 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517113694  74 TVRAEASQWRWRFGYEDAPGLeTEGVLHIPAARPIDVEITTTDVVHSFWVPRLAGKLDAMPGHVNVLRIEADAPGEYGGL 153
Cdd:COG1622  114 TVEVTGYQWKWLFRYPDQGIA-TVNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQ 192

                        170       180       190
                 ....*....|....*....|....*....|...
gi 517113694 154 SAEYNGPGYVQHGFVVVAHGPDEWRAFIEGETP 186
Cdd:COG1622  193 CAELCGTGHAGMRFKVVVVSPEEFDAWLAEQKA 225
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 2-182 7.39e-40

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: 134.05  E-value: 7.39e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517113694    2 WWVLLAGASLIFLFVMALVA-VAWRSPARPAAEERPFVVG------LGLAFPLVVLAALLAYGlVVGERLLPRPGP-EVV 73
Cdd:TIGR02866  13 FLFVLAVSTLISLLVAALLAyVVWKFRRKGDEEKPSQIHGnrrleyVWTVIPLIIVVGLFAAT-AKGLLYLERPIPkDAL 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517113694   74 TVRAEASQWRWRFGYEDApGLETEGVLHIPAARPIDVEITTTDVVHSFWVPRLAGKLDAMPGHVNVLRIEADAPGEYGGL 153
Cdd:TIGR02866  92 KVKVTGYQWWWDFEYPES-GFTTVNELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGF 170

                         170       180
                  ....*....|....*....|....*....
gi 517113694  154 SAEYNGPGYVQHGFVVVAHGPDEWRAFIE 182
Cdd:TIGR02866 171 CAELCGAGHSLMLFKVVVVPKEEFDAYVE 199
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 73-172 4.54e-37

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: 123.88  E-value: 4.54e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517113694  73 VTVRAEASQWRWRFGYEDAP--GLETEGVLHIPAARPIDVEITTTDVVHSFWVPRLAGKLDAMPGHVNVLRIEADAPGEY 150
Cdd:cd04213    2 LTIEVTGHQWWWEFRYPDEPgrGIVTANELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMDMIPGRTNRLWLQADEPGVY 81

                         90       100
                 ....*....|....*....|..
gi 517113694 151 GGLSAEYNGPGYVQHGFVVVAH 172
Cdd:cd04213   82 RGQCAEFCGASHALMRFKVIAL 103
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 73-171 2.16e-25

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: 93.77  E-value: 2.16e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517113694  73 VTVRAEASQWRWRFGYEDApGLETEGVLHIPAARPIDVEITTTDVVHSFWVPRLAGKLDAMPGHVNVLRIEADAPGEYGG 152
Cdd:cd04212    1 LEIQVVSLDWKWLFIYPEQ-GIATVNELVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGTYQG 79

                         90
                 ....*....|....*....
gi 517113694 153 LSAEYNGPGYVQHGFVVVA 171
Cdd:cd04212   80 LSANYSGEGFSDMKFKVLA 98
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 73-161 3.26e-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: 93.51  E-value: 3.26e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517113694  73 VTVRAEASQWRWRFGYedaPGLETEGVLHIPAARPIDVEITTTDVVHSFWVPRLAGKLDAMPGHVNVLRIEADAPGEYGG 152
Cdd:cd13842    1 LTVYVTGVQWSWTFIY---PNVRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDAVPGYTSELWFVADKPGTYTI 77


                 ....*....
gi 517113694 153 LSAEYNGPG 161
Cdd:cd13842   78 ICAEYCGLG 86
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 73-181 9.76e-25

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: 92.47  E-value: 9.76e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517113694  73 VTVRAEASQWRWRFGYEDApGLETEGVLHIPAARPIDVEITTTDVVHSFWVPRLAGKLDAMPGHVNVLRIEADAPGEYGG 152
Cdd:cd13914    1 VEIEVEAYQWGWEFSYPEA-NVTTSEQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDAFPGQYNTIKTEATEEGEYQL 79

                         90       100
                 ....*....|....*....|....*....
gi 517113694 153 LSAEYNGPGYVQHGFVVVAHGPDEWRAFI 181
Cdd:cd13914   80 YCAEYCGAGHSQMLSTVTVVSQDEYQQWL 108
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 73-172 4.43e-24

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: 90.78  E-value: 4.43e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517113694  73 VTVRAEASQWRWRFGYEDAPGLETE------GVLHIPAARPIDVEITTTDVVHSFWVPRLAGKLDAMPGHVNVLRIEADA 146
Cdd:cd13919    2 LVVEVTAQQWAWTFRYPGGDGKLGTdddvtsPELHLPVGRPVLFNLRSKDVIHSFWVPEFRVKQDAVPGRTTRLWFTPTR 81

                         90       100
                 ....*....|....*....|....*.
gi 517113694 147 PGEYGGLSAEYNGPGYVQHGFVVVAH 172
Cdd:cd13919   82 EGEYEVRCAELCGLGHYRMRATVKVV 107
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 74-159 2.93e-19

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: 78.05  E-value: 2.93e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517113694  74 TVRAEASQWRWRFGYEDapGLETEGVLHIPAARPIDVEITTTDVVHSFWVPRLAGKLDAMPGHVNVLRIEADAPGEYGGL 153
Cdd:cd13915    3 EIQVTGRQWMWEFTYPN--GKREINELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQDVVPGRYTYLWFEATKPGEYDLF 80


                 ....*.
gi 517113694 154 SAEYNG 159
Cdd:cd13915   81 CTEYCG 86
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 66-162 6.47e-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: 73.26  E-value: 6.47e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517113694  66 PRPGPEVVTVRAEASQWRWRFGYEDapGLETEGVLHIPAARPIDVEITTTDVVHSFWVPRLAGKLDAMPGHVNVLRIEAD 145
Cdd:cd13918   26 DEADEDALEVEVEGFQFGWQFEYPN--GVTTGNTLRVPADTPIALRVTSTDVFHTFGIPELRVKADAIPGEYTSTWFEAD 103

                         90
                 ....*....|....*..
gi 517113694 146 APGEYGGLSAEYNGPGY 162
Cdd:cd13918  104 EPGTYEAKCYELCGSGH 120
PRK10525 PRK10525
cytochrome o ubiquinol oxidase subunit II; Provisional
 73-179 1.60e-16

cytochrome o ubiquinol oxidase subunit II; Provisional


Pssm-ID: 182518 [Multi-domain]  Cd Length: 315  Bit Score: 75.61  E-value: 1.60e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517113694  73 VTVRAEASQWRWRFGYEDApGLETEGVLHIPAARPIDVEITTTDVVHSFWVPRLAGKLDAMPGHVNVLRIEADAPGEYGG 152
Cdd:PRK10525 127 ITIEVVSMDWKWFFIYPEQ-GIATVNEIAFPANVPVYFKVTSNSVMNSFFIPRLGSQIYAMAGMQTRLHLIANEPGTYDG 205

                         90       100       110
                 ....*....|....*....|....*....|.
gi 517113694 153 LSAEYNGPGYVQHGFVVVA----HGPDEWRA 179
Cdd:PRK10525 206 ISASYSGPGFSGMKFKAIAtpdrAEFDQWVA 236
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 73-167 2.27e-13

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: 63.74  E-value: 2.27e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517113694  73 VTVRAEASQWRWRFGYED----------------APG----LETEGVLHIPAARPIDVEITTTDVVHSFWVPRLAGKLDA 132
Cdd:cd13912    3 LTIKAIGHQWYWSYEYSDfndlefdsymipeddlEKGqlrlLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKVDA 82

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 517113694 133 MPGHVNVLRIEADAPGEYGGLSAEYNGpgyVQHGF 167
Cdd:cd13912   83 VPGRLNQTSFFIERPGVYYGQCSEICG---ANHSF 114
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
74-167 1.24e-12

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 61.66  E-value: 1.24e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517113694   74 TVRAEASQWRWRFGYED----------------APG----LETEGVLHIPAARPIDVEITTTDVVHSFWVPRLAGKLDAM 133
Cdd:pfam00116   2 TIKAIGHQWYWSYEYTDfgdlefdsymiptedlEEGqlrlLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDAV 81

                          90       100       110
                  ....*....|....*....|....*....|....
gi 517113694  134 PGHVNVLRIEADAPGEYGGLSAEYNGpgyVQHGF 167
Cdd:pfam00116  82 PGRLNQTSFSIDREGVFYGQCSEICG---INHSF 112
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 36-183 6.72e-11

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 58.80  E-value: 6.72e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517113694  36 PFVVGLGLAFPLVVLAallaYglvvgerLLPRPGPEVVTVRAEASQWRWRFGYED----------------APG----LE 95
Cdd:MTH00140  69 PALILVFLALPSLRLL----Y-------LLDETNNPLLTVKAIGHQWYWSYEYSDfsviefdsymvpenelELGdfrlLE 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517113694  96 TEGVLHIPAARPIDVEITTTDVVHSFWVPRLAGKLDAMPGHVNVLRIEADAPGEYGGLSAEYNGpgyVQHGF---VVVAH 172
Cdd:MTH00140 138 VDNRLVLPYSVDTRVLVTSADVIHSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICG---ANHSFmpiVVEAV 214

                        170
                 ....*....|.
gi 517113694 173 GPDEWRAFIEG 183
Cdd:MTH00140 215 PLEDFVKWLEL 225
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 73-171 1.01e-10

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 58.36  E-value: 1.01e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517113694  73 VTVRAEASQWRWRFGYED----------------APG----LETEGVLHIPAARPIDVEITTTDVVHSFWVPRLAGKLDA 132
Cdd:MTH00185  95 LTIKAMGHQWYWSYEYTDyeqlefdsymtptqdlTPGqfrlLETDHRMVVPMESPIRVLITAEDVLHSWTVPALGVKMDA 174

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 517113694 133 MPGHVNVLRIEADAPGEYGGLSAEYNGpgyVQHGFVVVA 171
Cdd:MTH00185 175 VPGRLNQATFIISRPGLYYGQCSEICG---ANHSFMPIV 210
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 73-162 1.30e-10

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


Pssm-ID: 259983 [Multi-domain]  Cd Length: 93  Bit Score: 55.47  E-value: 1.30e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517113694  73 VTVRAEASQWRWRFGyedapglETEgvlhIPAARPIDVEITTTDVVHSFWV----PRLAGKLDAMPGHVNVLRIEADAPG 148
Cdd:cd13916    1 QVVAVTGHQWYWELS-------RTE----IPAGKPVEFRVTSADVNHGFGIydpdMRLLAQTQAMPGYTNVLRYTFDKPG 69

                         90
                 ....*....|....
gi 517113694 149 EYGGLSAEYNGPGY 162
Cdd:cd13916   70 TYTILCLEYCGLAH 83
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 73-159 6.53e-10

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 56.26  E-value: 6.53e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517113694  73 VTVRAEASQWRWRFGYED----------------APG----LETEGVLHIPAARPIDVEITTTDVVHSFWVPRLAGKLDA 132
Cdd:MTH00129  95 LTIKAMGHQWYWSYEYTDyedlgfdsymiptqdlTPGqfrlLEADHRMVVPVESPIRVLVSAEDVLHSWAVPALGVKMDA 174

                         90       100
                 ....*....|....*....|....*..
gi 517113694 133 MPGHVNVLRIEADAPGEYGGLSAEYNG 159
Cdd:MTH00129 175 VPGRLNQTAFIASRPGVFYGQCSEICG 201
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 69-170 9.72e-10

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: 9.72e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517113694  69 GPEVVTVRAEASQWRWrfgyedapgleTEGVLHIPAARPIDVEITTTDVVHSFWVPRLAGKLDAMPGHVNVLRIEADAPG 148
Cdd:cd13913    7 GPNEYEVYVVAQAFAF-----------NPNEIEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPG 75

                         90       100
                 ....*....|....*....|...
gi 517113694 149 EYGGLSAEYNGPGY-VQHGFVVV 170
Cdd:cd13913   76 EYLIICNEYCGAGHhNMYGKIIV 98
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 36-171 1.02e-09

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 55.63  E-value: 1.02e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517113694  36 PFVVGLGLAFPLVVLAALLAYglvvgerlLPRPGpevVTVRAEASQWRWRFGYED----------------APG----LE 95
Cdd:MTH00008  69 PALILLFLAFPSLRLLYLMDE--------VSNPS---ITLKTIGHQWYWSYEYSDfsnlefdsymlptsdlSPGqfrlLE 137

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 517113694  96 TEGVLHIPAARPIDVEITTTDVVHSFWVPRLAGKLDAMPGHVNVLRIEADAPGEYGGLSAEYNGpgyVQHGFVVVA 171
Cdd:MTH00008 138 VDNRAVLPMQTEIRVLVTAADVIHSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICG---ANHSFMPIV 210
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 73-167 1.08e-09

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 55.76  E-value: 1.08e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517113694  73 VTVRAEASQWRWRFGYED----------------APG----LETEGVLHIPAARPIDVEITTTDVVHSFWVPRLAGKLDA 132
Cdd:MTH00168  95 LTIKAVGHQWYWSYEYTDyndlefdsymvptqdlSPGqfrlLEVDNRLVLPMDSKIRVLVTSADVLHSWTLPSLGLKMDA 174

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 517113694 133 MPGHVNVLRIEADAPGEYGGLSAEYNGpgyVQHGF 167
Cdd:MTH00168 175 VPGRLNQLAFLSSRPGSFYGQCSEICG---ANHSF 206
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 73-167 2.06e-09

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 54.72  E-value: 2.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517113694  73 VTVRAEASQWRWRFGYEDAPG--------------------LETEGVLHIPAARPIDVEITTTDVVHSFWVPRLAGKLDA 132
Cdd:MTH00139  95 LTFKAVGHQWYWSYEYSDFKNlsfdsymiptedlssgefrlLEVDNRLVLPYKSNIRALITAADVLHSWTVPSLGVKIDA 174

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 517113694 133 MPGHVNVLRIEADAPGEYGGLSAEYNGpgyVQHGF 167
Cdd:MTH00139 175 VPGRLNQVGFFINRPGVFYGQCSEICG---ANHSF 206
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 73-159 4.88e-09

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 53.95  E-value: 4.88e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517113694  73 VTVRAEASQWRWRFGYED----------------APG----LETEGVLHIPAARPIDVEITTTDVVHSFWVPRLAGKLDA 132
Cdd:MTH00098  95 LTVKTMGHQWYWSYEYTDyedlsfdsymiptsdlKPGelrlLEVDNRVVLPMEMPIRMLISSEDVLHSWAVPSLGLKTDA 174

                         90       100
                 ....*....|....*....|....*..
gi 517113694 133 MPGHVNVLRIEADAPGEYGGLSAEYNG 159
Cdd:MTH00098 175 IPGRLNQTTLMSTRPGLYYGQCSEICG 201
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 73-159 8.60e-09

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 53.24  E-value: 8.60e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517113694  73 VTVRAEASQWRWRFGYED----------------APG----LETEGVLHIPAARPIDVEITTTDVVHSFWVPRLAGKLDA 132
Cdd:MTH00076  95 LTVKAIGHQWYWSYEYTDyedlsfdsymiptqdlTPGqfrlLEVDNRMVVPMESPIRMLITAEDVLHSWAVPSLGIKTDA 174

                         90       100
                 ....*....|....*....|....*..
gi 517113694 133 MPGHVNVLRIEADAPGEYGGLSAEYNG 159
Cdd:MTH00076 175 IPGRLNQTSFIASRPGVYYGQCSEICG 201
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 73-159 1.02e-08

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 52.78  E-value: 1.02e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517113694  73 VTVRAEASQWRWRFGYED----------------APG----LETEGVLHIPAARPIDVEITTTDVVHSFWVPRLAGKLDA 132
Cdd:MTH00038  95 LTIKAIGHQWYWSYEYTDyndlefdsymvptsdlSTGlprlLEVDNRLVLPYQTPIRVLVSSADVLHSWAVPSLGVKMDA 174

                         90       100
                 ....*....|....*....|....*..
gi 517113694 133 MPGHVNVLRIEADAPGEYGGLSAEYNG 159
Cdd:MTH00038 175 VPGRLNQTTFFISRTGLFYGQCSEICG 201
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 73-168 1.17e-08

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 52.83  E-value: 1.17e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517113694  73 VTVRAEASQWRWRFGYEDAPG----------------------LETEGVLHIPAARPIDVEITTTDVVHSFWVPRLAGKL 130
Cdd:MTH00023 104 LTIKAIGHQWYWSYEYSDYEGetlefdsymvptsdlnsgdfrlLEVDNRLVVPINTHVRILVTGADVLHSFAVPSLGLKI 183

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 517113694 131 DAMPGHVNVLRIEADAPGEYGGLSAEYNGpgyVQHGFV 168
Cdd:MTH00023 184 DAVPGRLNQTGFFIKRPGVFYGQCSEICG---ANHSFM 218
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 73-159 1.72e-08

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 52.48  E-value: 1.72e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517113694  73 VTVRAEASQWRWRFGYEDAPG----------------------LETEGVLHIPAARPIDVEITTTDVVHSFWVPRLAGKL 130
Cdd:MTH00051  97 LTIKAIGHQWYWSYEYSDYGTdtiefdsymiptsdlnsgdlrlLEVDNRLIVPIQTQVRVLVTAADVLHSFAVPSLSVKI 176

                         90       100
                 ....*....|....*....|....*....
gi 517113694 131 DAMPGHVNVLRIEADAPGEYGGLSAEYNG 159
Cdd:MTH00051 177 DAVPGRLNQTSFFIKRPGVFYGQCSEICG 205
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 73-162 7.58e-08

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 50.79  E-value: 7.58e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517113694  73 VTVRAEASQWRWRFGYEDAPG----------------------LETEGVLHIPAARPIDVEITTTDVVHSFWVPRLAGKL 130
Cdd:MTH00027 127 ITIKVTGHQWYWSYSYEDYGEkniefdsymiptadlefgdlrlLEVDNRLILPVDTNVRVLITAADVLHSWTVPSLAVKM 206

                         90       100       110
                 ....*....|....*....|....*....|..
gi 517113694 131 DAMPGHVNVLRIEADAPGEYGGLSAEYNGPGY 162
Cdd:MTH00027 207 DAVPGRINETGFLIKRPGIFYGQCSEICGANH 238
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 74-156 1.77e-07

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 49.24  E-value: 1.77e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517113694  74 TVRAEASQWRWRFGYEDAPGLETEGV------LHIPAAR----------PIDVEI----TTTDVVHSFWVPRLAGKLDAM 133
Cdd:MTH00080  99 TVKVTGHQWYWSYEFSDIPGLEFDSYmksldqLRLGEPRllevdnrcvlPCDTNIrfciTSSDVIHSWALPSLSIKMDAM 178

                         90       100
                 ....*....|....*....|...
gi 517113694 134 PGHVNVLRIEADAPGEYGGLSAE 156
Cdd:MTH00080 179 SGILSTLCYSFPMPGVFYGQCSE 201
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 73-152 3.18e-07

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 48.76  E-value: 3.18e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517113694  73 VTVRAEASQWRWRFGYED----------------APG----LETEGVLHIPAARPIDVEITTTDVVHSFWVPRLAGKLDA 132
Cdd:MTH00117  95 LTIKAIGHQWYWSYEYTDykdlsfdsymiptqdlPNGhfrlLEVDHRMVIPMESPIRILITAEDVLHSWAVPSLGVKTDA 174

                         90       100
                 ....*....|....*....|
gi 517113694 133 MPGHVNVLRIEADAPGEYGG 152
Cdd:MTH00117 175 VPGRLNQTSFITTRPGVFYG 194
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 73-152 9.52e-06

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 44.43  E-value: 9.52e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517113694  73 VTVRAEASQWRWRFGYED----------APG----------LETEGVLHIPAARPIDVEITTTDVVHSFWVPRLAGKLDA 132
Cdd:MTH00154  95 ITLKTIGHQWYWSYEYSDfkniefdsymIPTnelenngfrlLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDA 174

                         90       100
                 ....*....|....*....|
gi 517113694 133 MPGHVNVLRIEADAPGEYGG 152
Cdd:MTH00154 175 VPGRLNQLNFLINRPGLFFG 194
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 112-167 2.42e-05

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 43.02  E-value: 2.42e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 517113694 112 ITTTDVVHSFWVPRLAGKLDAMPGHVNVLRIEADAPGEYGGLSAEYNGpgyVQHGF 167
Cdd:MTH00047 130 VTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCPDRHGVFVGYCSELCG---VGHSY 182
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 94-179 3.55e-05

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 42.11  E-value: 3.55e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517113694  94 LETEGVLHIPAARPIDVEITTTDVVHSFWVPRLAGKLDAMPGHVNVLRIEADAPGEYGGLSAEYNGpgyVQHGF---VVV 170
Cdd:PTZ00047  69 LEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCSEMCG---TLHGFmpiVVE 145


                 ....*....
gi 517113694 171 AHGPDEWRA 179
Cdd:PTZ00047 146 AVSPEAYAA 154
CuRO_HCO_II_like_4 cd13917
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 75-170 5.62e-04

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: 37.35  E-value: 5.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 517113694  75 VRAEASQWRWRfgyedapgleteGVLHIPAARPIDVEITTTDVVHSFWVPRLAGKLDAMPGHVNVLRIEADAPGEYGGLS 154
Cdd:cd13917    3 VYLVARAWQWR------------PVLVLKKGKTYRLHLSSLDVQHGFSLQPKNINFQVLPGYEWVITMTPNETGEFHIIC 70

                         90
                 ....*....|....*..
gi 517113694 155 AEYNGPGY-VQHGFVVV 170
Cdd:cd13917   71 NEYCGIGHhTMHGRIIV 87
 
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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