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Conserved domains on  [gi|1905978993|ref|WP_188758016|]
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cytochrome C oxidase subunit II [Edaphobacter acidisoli]

Protein Classification

cupredoxin domain-containing protein; multicopper oxidase( domain architecture ID 10195321)

cupredoxin domain-containing protein may contain a type I copper center and be involved in inter-molecular electron transfer reactions; multicopper oxidase (MCO) that couples the oxidation of a substrate with a four-electron reduction of molecular oxygen to water, and which may contain three cupredoxin domains that include one mononuclear and one trinuclear copper center; similar to Pleurotus ostreatus laccase-2 that may be involved in lignin degradation and detoxification of lignin-derived products

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 98-227 3.30e-52

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: 164.74  E-value: 3.30e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905978993  98 ALQVEVTGVQFAWYFRYPGVDGTFGRvrpelvapgegnplgldpadshsADDVVSSQLMLPVGREVDLAIRSQDVIHGFS 177
Cdd:cd13919     1 ALVVEVTAQQWAWTFRYPGGDGKLGT-----------------------DDDVTSPELHLPVGRPVLFNLRSKDVIHSFW 57

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1905978993 178 VPEMRLKQNAVPGETIHIHFTPTKTGTYAILCTQVCGLGHYRMNANLRVV 227
Cdd:cd13919    58 VPEFRVKQDAVPGRTTRLWFTPTREGEYEVRCAELCGLGHYRMRATVKVV 107
 
Name Accession Description Interval E-value
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 98-227 3.30e-52

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: 164.74  E-value: 3.30e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905978993  98 ALQVEVTGVQFAWYFRYPGVDGTFGRvrpelvapgegnplgldpadshsADDVVSSQLMLPVGREVDLAIRSQDVIHGFS 177
Cdd:cd13919     1 ALVVEVTAQQWAWTFRYPGGDGKLGT-----------------------DDDVTSPELHLPVGRPVLFNLRSKDVIHSFW 57

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1905978993 178 VPEMRLKQNAVPGETIHIHFTPTKTGTYAILCTQVCGLGHYRMNANLRVV 227
Cdd:cd13919    58 VPEFRVKQDAVPGRTTRLWFTPTREGEYEVRCAELCGLGHYRMRATVKVV 107
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
12-242 3.08e-51

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 166.54  E-value: 3.08e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905978993  12 LPVDASAHGPALDRQLLLSLWIVLALFTLAHVILLGGLAARRHHPQKSV-------WQIEYLPLVALAALFAVLTIRAER 84
Cdd:COG1622    21 LPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLLLYFAIRYRRRKGDADpaqfhhnTKLEIVWTVIPIIIVIVLAVPTLR 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905978993  85 LWAATRYTGASltALQVEVTGVQFAWYFRYPGvdgtfgrvrpelvapgegnplgldpadshsADDVVSSQLMLPVGREVD 164
Cdd:COG1622   101 VLHALDDAPED--PLTVEVTGYQWKWLFRYPD------------------------------QGIATVNELVLPVGRPVR 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1905978993 165 LAIRSQDVIHGFSVPEMRLKQNAVPGETIHIHFTPTKTGTYAILCTQVCGLGHYRMNANLRVVTPEEFDSWLAAREKA 242
Cdd:COG1622   149 FLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAEQKAS 226
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 20-237 1.57e-33

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: 119.79  E-value: 1.57e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905978993  20 GPALDRQLLLSLWIVLALFTLAHVILLGGLA-------ARRHHPQKSVWQ----IEYLPLVALAALFAVLTIRaerLWAA 88
Cdd:TIGR02866   2 GGEIAQQIAFLFLFVLAVSTLISLLVAALLAyvvwkfrRKGDEEKPSQIHgnrrLEYVWTVIPLIIVVGLFAA---TAKG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905978993  89 TRYTGASL--TALQVEVTGVQFAWYFRYPgvDGTFgrvrpelvapgegnplgldpadshsaddVVSSQLMLPVGREVDLA 166
Cdd:TIGR02866  79 LLYLERPIpkDALKVKVTGYQWWWDFEYP--ESGF----------------------------TTVNELVLPAGTPVELQ 128

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1905978993 167 IRSQDVIHGFSVPEMRLKQNAVPGETIHIHFTPTKTGTYAILCTQVCGLGHYRMNANLRVVTPEEFDSWLA 237
Cdd:TIGR02866 129 VTSKDVIHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYVE 199
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 143-220 3.67e-13

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 65.75  E-value: 3.67e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905978993 143 DSHSADDV--VSSQLMLPVGREVDLAIRSQDVIHGFSVPEMRLKQNAVPGETIHIHFTPTKTGTYAILCTQVCGLGHYRM 220
Cdd:MTH00047  104 DSFMTDDIfgVDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCPDRHGVFVGYCSELCGVGHSYM 183
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
99-220 1.73e-12

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 62.43  E-value: 1.73e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905978993  99 LQVEVTGVQFAWYFRYPG-VDGTFGR--VRPELVAPGEGNPLGLDpadshsaddvvsSQLMLPVGREVDLAIRSQDVIHG 175
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDfGDLEFDSymIPTEDLEEGQLRLLEVD------------NRVVLPVETHIRVIVTAADVIHS 68

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1905978993 176 FSVPEMRLKQNAVPGETIHIHFTPTKTGTYAILCTQVCGLGHYRM 220
Cdd:pfam00116  69 WAVPSLGIKTDAVPGRLNQTSFSIDREGVFYGQCSEICGINHSFM 113
 
Name Accession Description Interval E-value
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 98-227 3.30e-52

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: 164.74  E-value: 3.30e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905978993  98 ALQVEVTGVQFAWYFRYPGVDGTFGRvrpelvapgegnplgldpadshsADDVVSSQLMLPVGREVDLAIRSQDVIHGFS 177
Cdd:cd13919     1 ALVVEVTAQQWAWTFRYPGGDGKLGT-----------------------DDDVTSPELHLPVGRPVLFNLRSKDVIHSFW 57

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1905978993 178 VPEMRLKQNAVPGETIHIHFTPTKTGTYAILCTQVCGLGHYRMNANLRVV 227
Cdd:cd13919    58 VPEFRVKQDAVPGRTTRLWFTPTREGEYEVRCAELCGLGHYRMRATVKVV 107
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
12-242 3.08e-51

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 166.54  E-value: 3.08e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905978993  12 LPVDASAHGPALDRQLLLSLWIVLALFTLAHVILLGGLAARRHHPQKSV-------WQIEYLPLVALAALFAVLTIRAER 84
Cdd:COG1622    21 LPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLLLYFAIRYRRRKGDADpaqfhhnTKLEIVWTVIPIIIVIVLAVPTLR 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905978993  85 LWAATRYTGASltALQVEVTGVQFAWYFRYPGvdgtfgrvrpelvapgegnplgldpadshsADDVVSSQLMLPVGREVD 164
Cdd:COG1622   101 VLHALDDAPED--PLTVEVTGYQWKWLFRYPD------------------------------QGIATVNELVLPVGRPVR 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1905978993 165 LAIRSQDVIHGFSVPEMRLKQNAVPGETIHIHFTPTKTGTYAILCTQVCGLGHYRMNANLRVVTPEEFDSWLAAREKA 242
Cdd:COG1622   149 FLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAEQKAS 226
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 98-226 1.85e-34

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: 119.27  E-value: 1.85e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905978993  98 ALQVEVTGVQFAWYFRYPGVDGTfgrvrpelvapgegnplgldpadshsaddvvSSQLMLPVGREVDLAIRSQDVIHGFS 177
Cdd:cd13915     1 ALEIQVTGRQWMWEFTYPNGKRE-------------------------------INELHVPVGKPVRLILTSKDVIHSFY 49

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1905978993 178 VPEMRLKQNAVPGETIHIHFTPTKTGTYAILCTQVCGLGHYRMNANLRV 226
Cdd:cd13915    50 VPAFRIKQDVVPGRYTYLWFEATKPGEYDLFCTEYCGTGHSGMIGKVRV 98
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 20-237 1.57e-33

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: 119.79  E-value: 1.57e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905978993  20 GPALDRQLLLSLWIVLALFTLAHVILLGGLA-------ARRHHPQKSVWQ----IEYLPLVALAALFAVLTIRaerLWAA 88
Cdd:TIGR02866   2 GGEIAQQIAFLFLFVLAVSTLISLLVAALLAyvvwkfrRKGDEEKPSQIHgnrrLEYVWTVIPLIIVVGLFAA---TAKG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905978993  89 TRYTGASL--TALQVEVTGVQFAWYFRYPgvDGTFgrvrpelvapgegnplgldpadshsaddVVSSQLMLPVGREVDLA 166
Cdd:TIGR02866  79 LLYLERPIpkDALKVKVTGYQWWWDFEYP--ESGF----------------------------TTVNELVLPAGTPVELQ 128

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1905978993 167 IRSQDVIHGFSVPEMRLKQNAVPGETIHIHFTPTKTGTYAILCTQVCGLGHYRMNANLRVVTPEEFDSWLA 237
Cdd:TIGR02866 129 VTSKDVIHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYVE 199
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 100-236 1.29e-30

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: 109.42  E-value: 1.29e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905978993 100 QVEVTGVQFAWYFRYPGvdgtfgrvrpelvapgegnplgldpadshsADDVVSSQLMLPVGREVDLAIRSQDVIHGFSVP 179
Cdd:cd13914     2 EIEVEAYQWGWEFSYPE------------------------------ANVTTSEQLVIPADRPVYFRITSRDVIHAFHVP 51

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1905978993 180 EMRLKQNAVPGETIHIHFTPTKTGTYAILCTQVCGLGHYRMNANLRVVTPEEFDSWL 236
Cdd:cd13914    52 ELGLKQDAFPGQYNTIKTEATEEGEYQLYCAEYCGAGHSQMLSTVTVVSQDEYQQWL 108
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 99-220 8.25e-26

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: 96.60  E-value: 8.25e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905978993  99 LQVEVTGVQFAWYFRYPGVdgtfgRVRPELVapgegnplgldpadshsaddvvssqlmLPVGREVDLAIRSQDVIHGFSV 178
Cdd:cd13842     1 LTVYVTGVQWSWTFIYPNV-----RTPNEIV---------------------------VPAGTPVRFRVTSPDVIHGFYI 48

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1905978993 179 PEMRLKQNAVPGETIHIHFTPTKTGTYAILCTQVCGLGHYRM 220
Cdd:cd13842    49 PNLGVKVDAVPGYTSELWFVADKPGTYTIICAEYCGLGHSYM 90
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 98-236 5.37e-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: 259985 [Multi-domain]  Cd Length: 139  Bit Score: 95.99  E-value: 5.37e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905978993  98 ALQVEVTGVQFAWYFRYPGVDGTfgrvrpelvapgegnplgldpadshsaddvvSSQLMLPVGREVDLAIRSQDVIHGFS 177
Cdd:cd13918    32 ALEVEVEGFQFGWQFEYPNGVTT-------------------------------GNTLRVPADTPIALRVTSTDVFHTFG 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1905978993 178 VPEMRLKQNAVPGETIHIHFTPTKTGTYAILCTQVCGLGHYRMNANLRVVTPEEFDSWL 236
Cdd:cd13918    81 IPELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEFEAWY 139
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 98-227 2.95e-21

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: 84.98  E-value: 2.95e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905978993  98 ALQVEVTGVQFAWYFRYPGVDGTfgrvrpelvapgegnplgldpadshsadDVVSSQ-LMLPVGREVDLAIRSQDVIHGF 176
Cdd:cd04213     1 ALTIEVTGHQWWWEFRYPDEPGR----------------------------GIVTANeLHIPVGRPVRLRLTSADVIHSF 52

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1905978993 177 SVPEMRLKQNAVPGETIHIHFTPTKTGTYAILCTQVCGLGHYRMnaNLRVV 227
Cdd:cd04213    53 WVPSLAGKMDMIPGRTNRLWLQADEPGVYRGQCAEFCGASHALM--RFKVI 101
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 151-227 2.35e-16

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: 72.03  E-value: 2.35e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905978993 151 VSSQLMLPVGREVDLAIRSQDVIHGFSV--PEMRL--KQNAVPGETIHIHFTPTKTGTYAILCTQVCGLGHYRMNANLRV 226
Cdd:cd13916    13 ELSRTEIPAGKPVEFRVTSADVNHGFGIydPDMRLlaQTQAMPGYTNVLRYTFDKPGTYTILCLEYCGLAHHVMMAEFTV 92


                  .
gi 1905978993 227 V 227
Cdd:cd13916    93 V 93
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 153-227 8.93e-16

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: 70.68  E-value: 8.93e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1905978993 153 SQLMLPVGREVDLAIRSQDVIHGFSVPEMRLKQNAVPGETIHIHFTPTKTGTYAILCTQVCGLGHYRMNANLRVV 227
Cdd:cd13913    25 NEIEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNMYGKIIVE 99
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 151-235 6.00e-14

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: 66.44  E-value: 6.00e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905978993 151 VSSQLMLPVGREVDLAIRSQDVIHGFSVPEMRLKQNAVPGETIHIHFTPTKTGTYAILCTQVCGLGHYRMNANLRVVTPE 230
Cdd:cd13912    46 VDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKVDAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLE 125


                  ....*
gi 1905978993 231 EFDSW 235
Cdd:cd13912   126 DFLSW 130
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 143-220 3.67e-13

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 65.75  E-value: 3.67e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905978993 143 DSHSADDV--VSSQLMLPVGREVDLAIRSQDVIHGFSVPEMRLKQNAVPGETIHIHFTPTKTGTYAILCTQVCGLGHYRM 220
Cdd:MTH00047  104 DSFMTDDIfgVDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCPDRHGVFVGYCSELCGVGHSYM 183
CuRO_HCO_II_like_4 cd13917
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 155-227 1.05e-12

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: 62.00  E-value: 1.05e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1905978993 155 LMLPVGREVDLAIRSQDVIHGFSVPEMRLKQNAVPGETIHIHFTPTKTGTYAILCTQVCGLGHYRMNANLRVV 227
Cdd:cd13917    16 LVLKKGKTYRLHLSSLDVQHGFSLQPKNINFQVLPGYEWVITMTPNETGEFHIICNEYCGIGHHTMHGRIIVE 88
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
99-220 1.73e-12

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 62.43  E-value: 1.73e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905978993  99 LQVEVTGVQFAWYFRYPG-VDGTFGR--VRPELVAPGEGNPLGLDpadshsaddvvsSQLMLPVGREVDLAIRSQDVIHG 175
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDfGDLEFDSymIPTEDLEEGQLRLLEVD------------NRVVLPVETHIRVIVTAADVIHS 68

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1905978993 176 FSVPEMRLKQNAVPGETIHIHFTPTKTGTYAILCTQVCGLGHYRM 220
Cdd:pfam00116  69 WAVPSLGIKTDAVPGRLNQTSFSIDREGVFYGQCSEICGINHSFM 113
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 151-236 2.60e-12

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 64.11  E-value: 2.60e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905978993 151 VSSQLMLPVGREVDLAIRSQDVIHGFSVPEMRLKQNAVPGETIHIHFTPTKTGTYAILCTQVCGLGHYRMNANLRVVTPE 230
Cdd:MTH00008  138 VDNRAVLPMQTEIRVLVTAADVIHSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTK 217


                  ....*.
gi 1905978993 231 EFDSWL 236
Cdd:MTH00008  218 SFMKWV 223
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 151-241 1.56e-11

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 62.11  E-value: 1.56e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905978993 151 VSSQLMLPVGREVDLAIRSQDVIHGFSVPEMRLKQNAVPGETIHIHFTPTKTGTYAILCTQVCGLGHYRMNANLRVVTPE 230
Cdd:MTH00051  142 VDNRLIVPIQTQVRVLVTAADVLHSFAVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLD 221

                          90
                  ....*....|.
gi 1905978993 231 EFDSWLAAREK 241
Cdd:MTH00051  222 KYINWVATQSE 232
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 151-236 3.42e-11

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 61.11  E-value: 3.42e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905978993 151 VSSQLMLPVGREVDLAIRSQDVIHGFSVPEMRLKQNAVPGETIHIHFTPTKTGTYAILCTQVCGLGHYRMNANLRVVTPE 230
Cdd:MTH00140  138 VDNRLVLPYSVDTRVLVTSADVIHSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLE 217


                  ....*.
gi 1905978993 231 EFDSWL 236
Cdd:MTH00140  218 DFVKWL 223
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 151-237 4.17e-11

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 60.89  E-value: 4.17e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905978993 151 VSSQLMLPVGREVDLAIRSQDVIHGFSVPEMRLKQNAVPGETIHIHFTPTKTGTYAILCTQVCGLGHYRMNANLRVVTPE 230
Cdd:MTH00098  138 VDNRVVLPMEMPIRMLISSEDVLHSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLK 217


                  ....*..
gi 1905978993 231 EFDSWLA 237
Cdd:MTH00098  218 YFEKWSA 224
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 151-238 4.48e-11

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 60.76  E-value: 4.48e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905978993 151 VSSQLMLPVGREVDLAIRSQDVIHGFSVPEMRLKQNAVPGETIHIHFTPTKTGTYAILCTQVCGLGHYRMNANLRVVTPE 230
Cdd:MTH00168  138 VDNRLVLPMDSKIRVLVTSADVLHSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWE 217


                  ....*...
gi 1905978993 231 EFDSWLAA 238
Cdd:MTH00168  218 TFENWVDS 225
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 151-236 5.19e-10

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 57.80  E-value: 5.19e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905978993 151 VSSQLMLPVGREVDLAIRSQDVIHGFSVPEMRLKQNAVPGETIHIHFTPTKTGTYAILCTQVCGLGHYRMNANLRVVTPE 230
Cdd:MTH00139  138 VDNRLVLPYKSNIRALITAADVLHSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPK 217


                  ....*.
gi 1905978993 231 EFDSWL 236
Cdd:MTH00139  218 FFLEWI 223
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 98-236 5.36e-10

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 57.84  E-value: 5.36e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905978993  98 ALQVEVTGVQFAWYFRYPGVDGTFGRVRPELVAPGEgnplgLDPADSHSADdvVSSQLMLPVGREVDLAIRSQDVIHGFS 177
Cdd:MTH00023  103 ALTIKAIGHQWYWSYEYSDYEGETLEFDSYMVPTSD-----LNSGDFRLLE--VDNRLVVPINTHVRILVTGADVLHSFA 175

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1905978993 178 VPEMRLKQNAVPGETIHIHFTPTKTGTYAILCTQVCGLGHYRMNANLRVVTPEEFDSWL 236
Cdd:MTH00023  176 VPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWL 234
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 151-237 8.81e-10

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 57.02  E-value: 8.81e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905978993 151 VSSQLMLPVGREVDLAIRSQDVIHGFSVPEMRLKQNAVPGETIHIHFTPTKTGTYAILCTQVCGLGHYRMNANLRVVTPE 230
Cdd:MTH00038  138 VDNRLVLPYQTPIRVLVSSADVLHSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFN 217


                  ....*..
gi 1905978993 231 EFDSWLA 237
Cdd:MTH00038  218 TFENWVS 224
N2OR_C cd04223
The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase ...
 159-226 8.96e-10

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: 54.16  E-value: 8.96e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1905978993 159 VGREVDLAI----RSQDVIHGFSVPEMRLKQNAVPGETIHIHFTPTKTGTYAILCTQVCGLGHYRMNANLRV 226
Cdd:cd04223    22 EGDEVTVHLtnleQDEDITHGFAIPGYNVNLSLEPGETATVTFVADKPGVYPYYCTEFCSALHLEMQGYLIV 93
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 151-235 1.48e-09

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 56.43  E-value: 1.48e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905978993 151 VSSQLMLPVGREVDLAIRSQDVIHGFSVPEMRLKQNAVPGETIHIHFTPTKTGTYAILCTQVCGLGHYRMNANLRVVTPE 230
Cdd:MTH00185  138 TDHRMVVPMESPIRVLITAEDVLHSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLE 217


                  ....*
gi 1905978993 231 EFDSW 235
Cdd:MTH00185  218 HFENW 222
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 151-236 1.81e-09

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 55.99  E-value: 1.81e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905978993 151 VSSQLMLPVGREVDLAIRSQDVIHGFSVPEMRLKQNAVPGETIHIHFTPTKTGTYAILCTQVCGLGHYRMNANLRVVTPE 230
Cdd:MTH00154  138 VDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVN 217


                  ....*.
gi 1905978993 231 EFDSWL 236
Cdd:MTH00154  218 NFINWI 223
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 151-240 4.71e-09

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 54.79  E-value: 4.71e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905978993 151 VSSQLMLPVGREVDLAIRSQDVIHGFSVPEMRLKQNAVPGETIHIHFTPTKTGTYAILCTQVCGLGHYRMNANLRVVTPE 230
Cdd:MTH00076  138 VDNRMVVPMESPIRMLITAEDVLHSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLN 217

                          90
                  ....*....|
gi 1905978993 231 EFDSWLAARE 240
Cdd:MTH00076  218 NFLNWSSSML 227
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 151-237 1.34e-08

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 53.88  E-value: 1.34e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905978993 151 VSSQLMLPVGREVDLAIRSQDVIHGFSVPEMRLKQNAVPGETIHIHFTPTKTGTYAILCTQVCGLGHYRMNANLRVVTPE 230
Cdd:MTH00027  172 VDNRLILPVDTNVRVLITAADVLHSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLS 251


                  ....*..
gi 1905978993 231 EFDSWLA 237
Cdd:MTH00027  252 KYIDWIG 258
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 151-232 4.12e-08

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 51.36  E-value: 4.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905978993 151 VSSQLMLPVGREVDLAIRSQDVIHGFSVPEMRLKQNAVPGETIHIHFTPTKTGTYAILCTQVCGLGHYRMNANLRVVTPE 230
Cdd:PTZ00047   71 VDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCSEMCGTLHGFMPIVVEAVSPE 150


                  ..
gi 1905978993 231 EF 232
Cdd:PTZ00047  151 AY 152
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 154-235 9.16e-08

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 51.25  E-value: 9.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905978993 154 QLMLPVGREVDLAIRSQDVIHGFSVPEMRLKQNAVPGETIHIHFTPTKTGTYAILCTQVCGLGHYRMNANLRVVTPEEFD 233
Cdd:MTH00129  141 RMVVPVESPIRVLVSAEDVLHSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFE 220


                  ..
gi 1905978993 234 SW 235
Cdd:MTH00129  221 NW 222
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 99-236 4.93e-07

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 49.24  E-value: 4.93e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905978993  99 LQVEVTGVQFAWYFRYPGVDG----TFGRVRPELVApGEGNPLGLDpadshsaddvvsSQLMLPVGREVDLAIRSQDVIH 174
Cdd:MTH00080   98 LTVKVTGHQWYWSYEFSDIPGlefdSYMKSLDQLRL-GEPRLLEVD------------NRCVLPCDTNIRFCITSSDVIH 164

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1905978993 175 GFSVPEMRLKQNAVPGETIHIHFTPTKTGTYAILCTQVCGLGHYRMNANLRVVTPEEFDSWL 236
Cdd:MTH00080  165 SWALPSLSIKMDAMSGILSTLCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKEWC 226
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 99-227 9.89e-06

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


Pssm-ID: 259874 [Multi-domain]  Cd Length: 99  Bit Score: 43.31  E-value: 9.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905978993  99 LQVEVTGVQFAWYFRYPGvdgtfgrvrpelvapgegnplgldpadshsaDDVVS-SQLMLPVGREVDLAIRSQDVIHGFS 177
Cdd:cd04212     1 LEIQVVSLDWKWLFIYPE-------------------------------QGIATvNELVIPVGRPVNFRLTSDSVMNSFF 49

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1905978993 178 VPEMRLKQNAVPGETIHIHFTPTKTGTYAILCTQVCGLGHYRMNANLRVV 227
Cdd:cd04212    50 IPQLGGQIYAMAGMQTQLHLIADKPGTYQGLSANYSGEGFSDMKFKVLAV 99
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 151-237 1.60e-05

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 44.52  E-value: 1.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905978993 151 VSSQLMLPVGREVDLAIRSQDVIHGFSVPEMRLKQNAVPGETIHIHFTPTKTGTYAILCTQVCGLGHYRMNANLRVVTPE 230
Cdd:MTH00117  138 VDHRMVIPMESPIRILITAEDVLHSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLK 217


                  ....*..
gi 1905978993 231 EFDSWLA 237
Cdd:MTH00117  218 HFENWSS 224
Cupredoxin_1 pfam13473
Cupredoxin-like domain; The cupredoxin-like fold consists of a beta-sandwich with 7 strands in ...
 153-209 3.59e-04

Cupredoxin-like domain; The cupredoxin-like fold consists of a beta-sandwich with 7 strands in 2 beta-sheets, which is arranged in a Greek-key beta-barrel.


Pssm-ID: 379208 [Multi-domain]  Cd Length: 104  Bit Score: 38.72  E-value: 3.59e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1905978993 153 SQLMLPVGREVDLAIRSQD-VIHGFSVPEMRLKQNAVPGETIHIHFTPTKTGTYAILC 209
Cdd:pfam13473  35 SRITVPAGTPVKLEFKNKDkTPAEFESPDLGIEKVLAPGKTSTITIPPLKPGEYDFFC 92
COG4633 COG4633
Plastocyanin domain containing protein [General function prediction only];
153-219 1.01e-03

Plastocyanin domain containing protein [General function prediction only];


Pssm-ID: 443671 [Multi-domain]  Cd Length: 121  Bit Score: 37.97  E-value: 1.01e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1905978993 153 SQLMLPVGREVDLAIRSQDV---IHGFSVPEMRLKQNAVPGETIHIHFTPTKTGTYAILctqvCGLGHYR 219
Cdd:COG4633    50 SRITVKAGIPVRLNFTRKDPsgcAEEVVFPDLGISQDLPLGKTVTIEFTPLKPGEYPFT----CGMGMYR 115
 
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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