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Conserved domains on  [gi|1892043850|ref|WP_184258688|]
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cupredoxin domain-containing protein [Granulicella mallensis]

Protein Classification

CuRO_HCO_II_like_5 domain-containing protein( domain architecture ID 10195321)

CuRO_HCO_II_like_5 domain-containing protein

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; ...
 103-231 3.45e-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: 165.12  E-value: 3.45e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892043850 103 AMQVEVTGMQFAWYFRYPGADAAFGetkptlvapgegnplgldpadrhGADDLVTSQLVLPAGREVDLALHAQDVIHGFS 182
Cdd:cd13919     1 ALVVEVTAQQWAWTFRYPGGDGKLG-----------------------TDDDVTSPELHLPVGRPVLFNLRSKDVIHSFW 57

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1892043850 183 VPEMRLKQNAVPGQTAHIHFTPTQPGSYAILCTQLCGLGHYRMQATMLV 231
Cdd:cd13919    58 VPEFRVKQDAVPGRTTRLWFTPTREGEYEVRCAELCGLGHYRMRATVKV 106
 
Name Accession Description Interval E-value
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 103-231 3.45e-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: 165.12  E-value: 3.45e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892043850 103 AMQVEVTGMQFAWYFRYPGADAAFGetkptlvapgegnplgldpadrhGADDLVTSQLVLPAGREVDLALHAQDVIHGFS 182
Cdd:cd13919     1 ALVVEVTAQQWAWTFRYPGGDGKLG-----------------------TDDDVTSPELHLPVGRPVLFNLRSKDVIHSFW 57

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1892043850 183 VPEMRLKQNAVPGQTAHIHFTPTQPGSYAILCTQLCGLGHYRMQATMLV 231
Cdd:cd13919    58 VPEFRVKQDAVPGRTTRLWFTPTREGEYEVRCAELCGLGHYRMRATVKV 106
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
55-248 8.89e-49

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 160.38  E-value: 8.89e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892043850  55 FRRRASRPV-----HTLLLEYLPLAALTLLFAFLAARAQQLWAAQRYTGASltAMQVEVTGMQFAWYFRYPGADAAfget 129
Cdd:COG1622    61 YRRRKGDADpaqfhHNTKLEIVWTVIPIIIVIVLAVPTLRVLHALDDAPED--PLTVEVTGYQWKWLFRYPDQGIA---- 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892043850 130 kptlvapgegnplgldpadrhgaddlVTSQLVLPAGREVDLALHAQDVIHGFSVPEMRLKQNAVPGQTAHIHFTPTQPGS 209
Cdd:COG1622   135 --------------------------TVNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGT 188

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1892043850 210 YAILCTQLCGLGHYRMQATMLVLPPAAFDTWLQAHEAAA 248
Cdd:COG1622   189 YRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAEQKASA 227
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 55-241 9.31e-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: 118.25  E-value: 9.31e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892043850  55 FRRRASRPV-----HTLLLEYL-PLAALTLLFAFLAARAQQLWAAQRytGASLTAMQVEVTGMQFAWYFRYPGAdaafge 128
Cdd:TIGR02866  38 FRRKGDEEKpsqihGNRRLEYVwTVIPLIIVVGLFAATAKGLLYLER--PIPKDALKVKVTGYQWWWDFEYPES------ 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892043850 129 tkptlvapgegnplgldpadrhgadDLVTSQ-LVLPAGREVDLALHAQDVIHGFSVPEMRLKQNAVPGQTAHIHFTPTQP 207
Cdd:TIGR02866 110 -------------------------GFTTVNeLVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQTNALWFNADEP 164

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1892043850 208 GSYAILCTQLCGLGHYRMQATMLVLPPAAFDTWL 241
Cdd:TIGR02866 165 GVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYV 198
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
104-225 1.64e-14

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 67.82  E-value: 1.64e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892043850 104 MQVEVTGMQFAWYFRYPG-ADAAFGE--TKPTLVAPGEGNPLGLDpadrhgaddlvtSQLVLPAGREVDLALHAQDVIHG 180
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDfGDLEFDSymIPTEDLEEGQLRLLEVD------------NRVVLPVETHIRVIVTAADVIHS 68

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1892043850 181 FSVPEMRLKQNAVPGQTAHIHFTPTQPGSYAILCTQLCGLGHYRM 225
Cdd:pfam00116  69 WAVPSLGIKTDAVPGRLNQTSFSIDREGVFYGQCSEICGINHSFM 113
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 73-241 4.90e-14

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 69.11  E-value: 4.90e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892043850  73 LAALTLLF-AFLAARAqqLWAAQRYTGASLTamqVEVTGMQfaWYFRYPGADAAFGE-----TKPTLVAPGEGNPLGLDp 146
Cdd:MTH00008   68 LPALILLFlAFPSLRL--LYLMDEVSNPSIT---LKTIGHQ--WYWSYEYSDFSNLEfdsymLPTSDLSPGQFRLLEVD- 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892043850 147 adrhgaddlvtSQLVLPAGREVDLALHAQDVIHGFSVPEMRLKQNAVPGQTAHIHFTPTQPGSYAILCTQLCGLGHYRMQ 226
Cdd:MTH00008  140 -----------NRAVLPMQTEIRVLVTAADVIHSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMP 208

                         170
                  ....*....|....*
gi 1892043850 227 ATMLVLPPAAFDTWL 241
Cdd:MTH00008  209 IVLEAVDTKSFMKWV 223
 
Name Accession Description Interval E-value
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 103-231 3.45e-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: 165.12  E-value: 3.45e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892043850 103 AMQVEVTGMQFAWYFRYPGADAAFGetkptlvapgegnplgldpadrhGADDLVTSQLVLPAGREVDLALHAQDVIHGFS 182
Cdd:cd13919     1 ALVVEVTAQQWAWTFRYPGGDGKLG-----------------------TDDDVTSPELHLPVGRPVLFNLRSKDVIHSFW 57

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1892043850 183 VPEMRLKQNAVPGQTAHIHFTPTQPGSYAILCTQLCGLGHYRMQATMLV 231
Cdd:cd13919    58 VPEFRVKQDAVPGRTTRLWFTPTREGEYEVRCAELCGLGHYRMRATVKV 106
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
55-248 8.89e-49

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 160.38  E-value: 8.89e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892043850  55 FRRRASRPV-----HTLLLEYLPLAALTLLFAFLAARAQQLWAAQRYTGASltAMQVEVTGMQFAWYFRYPGADAAfget 129
Cdd:COG1622    61 YRRRKGDADpaqfhHNTKLEIVWTVIPIIIVIVLAVPTLRVLHALDDAPED--PLTVEVTGYQWKWLFRYPDQGIA---- 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892043850 130 kptlvapgegnplgldpadrhgaddlVTSQLVLPAGREVDLALHAQDVIHGFSVPEMRLKQNAVPGQTAHIHFTPTQPGS 209
Cdd:COG1622   135 --------------------------TVNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGT 188

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1892043850 210 YAILCTQLCGLGHYRMQATMLVLPPAAFDTWLQAHEAAA 248
Cdd:COG1622   189 YRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAEQKASA 227
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 103-231 1.32e-35

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: 122.35  E-value: 1.32e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892043850 103 AMQVEVTGMQFAWYFRYPGADAAFGEtkptlvapgegnplgldpadrhgaddlvtsqLVLPAGREVDLALHAQDVIHGFS 182
Cdd:cd13915     1 ALEIQVTGRQWMWEFTYPNGKREINE-------------------------------LHVPVGKPVRLILTSKDVIHSFY 49

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1892043850 183 VPEMRLKQNAVPGQTAHIHFTPTQPGSYAILCTQLCGLGHYRMQATMLV 231
Cdd:cd13915    50 VPAFRIKQDVVPGRYTYLWFEATKPGEYDLFCTEYCGTGHSGMIGKVRV 98
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 55-241 9.31e-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: 118.25  E-value: 9.31e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892043850  55 FRRRASRPV-----HTLLLEYL-PLAALTLLFAFLAARAQQLWAAQRytGASLTAMQVEVTGMQFAWYFRYPGAdaafge 128
Cdd:TIGR02866  38 FRRKGDEEKpsqihGNRRLEYVwTVIPLIIVVGLFAATAKGLLYLER--PIPKDALKVKVTGYQWWWDFEYPES------ 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892043850 129 tkptlvapgegnplgldpadrhgadDLVTSQ-LVLPAGREVDLALHAQDVIHGFSVPEMRLKQNAVPGQTAHIHFTPTQP 207
Cdd:TIGR02866 110 -------------------------GFTTVNeLVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQTNALWFNADEP 164

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1892043850 208 GSYAILCTQLCGLGHYRMQATMLVLPPAAFDTWL 241
Cdd:TIGR02866 165 GVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYV 198
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 105-241 7.48e-29

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: 105.18  E-value: 7.48e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892043850 105 QVEVTGMQFAWYFRYPGADAAFGEtkptlvapgegnplgldpadrhgaddlvtsQLVLPAGREVDLALHAQDVIHGFSVP 184
Cdd:cd13914     2 EIEVEAYQWGWEFSYPEANVTTSE------------------------------QLVIPADRPVYFRITSRDVIHAFHVP 51

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1892043850 185 EMRLKQNAVPGQTAHIHFTPTQPGSYAILCTQLCGLGHYRMQATMLVLPPAAFDTWL 241
Cdd:cd13914    52 ELGLKQDAFPGQYNTIKTEATEEGEYQLYCAEYCGAGHSQMLSTVTVVSQDEYQQWL 108
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 104-229 3.39e-27

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


Pssm-ID: 259911 [Multi-domain]  Cd Length: 95  Bit Score: 100.45  E-value: 3.39e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892043850 104 MQVEVTGMQFAWYFRYPGadaafGETKPTLVapgegnplgldpadrhgaddlvtsqlvLPAGREVDLALHAQDVIHGFSV 183
Cdd:cd13842     1 LTVYVTGVQWSWTFIYPN-----VRTPNEIV---------------------------VPAGTPVRFRVTSPDVIHGFYI 48

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1892043850 184 PEMRLKQNAVPGQTAHIHFTPTQPGSYAILCTQLCGLGHYRMQATM 229
Cdd:cd13842    49 PNLGVKVDAVPGYTSELWFVADKPGTYTIICAEYCGLGHSYMLGKV 94
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 103-241 1.32e-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: 97.91  E-value: 1.32e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892043850 103 AMQVEVTGMQFAWYFRYPGAdaafGETKPTlvapgegnplgldpadrhgaddlvtsqLVLPAGREVDLALHAQDVIHGFS 182
Cdd:cd13918    32 ALEVEVEGFQFGWQFEYPNG----VTTGNT---------------------------LRVPADTPIALRVTSTDVFHTFG 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1892043850 183 VPEMRLKQNAVPGQTAHIHFTPTQPGSYAILCTQLCGLGHYRMQATMLVLPPAAFDTWL 241
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), ...
 103-232 2.93e-24

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: 93.07  E-value: 2.93e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892043850 103 AMQVEVTGMQFAWYFRYPGADAafgetkptlvapgegnplgldpadrhgaDDLVTSQ-LVLPAGREVDLALHAQDVIHGF 181
Cdd:cd04213     1 ALTIEVTGHQWWWEFRYPDEPG----------------------------RGIVTANeLHIPVGRPVRLRLTSADVIHSF 52

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1892043850 182 SVPEMRLKQNAVPGQTAHIHFTPTQPGSYAILCTQLCGLGHYRMQATMLVL 232
Cdd:cd04213    53 WVPSLAGKMDMIPGRTNRLWLQADEPGVYRGQCAEFCGASHALMRFKVIAL 103
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 158-231 9.55e-19

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: 78.38  E-value: 9.55e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1892043850 158 SQLVLPAGREVDLALHAQDVIHGFSVPEMRLKQNAVPGQTAHIHFTPTQPGSYAILCTQLCGLGHYRMQATMLV 231
Cdd:cd13913    25 NEIEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNMYGKIIV 98
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 158-231 1.94e-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: 72.41  E-value: 1.94e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1892043850 158 SQLVLPAGREVDLALHAQDVIHGFSV--PEMRL--KQNAVPGQTAHIHFTPTQPGSYAILCTQLCGLGHYRMQATMLV 231
Cdd:cd13916    15 SRTEIPAGKPVEFRVTSADVNHGFGIydPDMRLlaQTQAMPGYTNVLRYTFDKPGTYTILCLEYCGLAHHVMMAEFTV 92
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 103-240 1.50e-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: 68.37  E-value: 1.50e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892043850 103 AMQVEVTGMQfaWYFRYPGADAAFGETKPTLVAPGE---GNPLGLDpadrhgaddlVTSQLVLPAGREVDLALHAQDVIH 179
Cdd:cd13912     2 SLTIKAIGHQ--WYWSYEYSDFNDLEFDSYMIPEDDlekGQLRLLE----------VDNRLVVPVNTHIRVLVTSADVIH 69

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1892043850 180 GFSVPEMRLKQNAVPGQTAHIHFTPTQPGSYAILCTQLCGLGHYRMQATMLVLPPAAFDTW 240
Cdd:cd13912    70 SWAVPSLGIKVDAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
104-225 1.64e-14

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 67.82  E-value: 1.64e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892043850 104 MQVEVTGMQFAWYFRYPG-ADAAFGE--TKPTLVAPGEGNPLGLDpadrhgaddlvtSQLVLPAGREVDLALHAQDVIHG 180
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDfGDLEFDSymIPTEDLEEGQLRLLEVD------------NRVVLPVETHIRVIVTAADVIHS 68

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1892043850 181 FSVPEMRLKQNAVPGQTAHIHFTPTQPGSYAILCTQLCGLGHYRM 225
Cdd:pfam00116  69 WAVPSLGIKTDAVPGRLNQTSFSIDREGVFYGQCSEICGINHSFM 113
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 73-241 4.90e-14

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 69.11  E-value: 4.90e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892043850  73 LAALTLLF-AFLAARAqqLWAAQRYTGASLTamqVEVTGMQfaWYFRYPGADAAFGE-----TKPTLVAPGEGNPLGLDp 146
Cdd:MTH00008   68 LPALILLFlAFPSLRL--LYLMDEVSNPSIT---LKTIGHQ--WYWSYEYSDFSNLEfdsymLPTSDLSPGQFRLLEVD- 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892043850 147 adrhgaddlvtSQLVLPAGREVDLALHAQDVIHGFSVPEMRLKQNAVPGQTAHIHFTPTQPGSYAILCTQLCGLGHYRMQ 226
Cdd:MTH00008  140 -----------NRAVLPMQTEIRVLVTAADVIHSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMP 208

                         170
                  ....*....|....*
gi 1892043850 227 ATMLVLPPAAFDTWL 241
Cdd:MTH00008  209 IVLEAVDTKSFMKWV 223
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 170-225 1.26e-13

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 67.29  E-value: 1.26e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1892043850 170 LALHAQDVIHGFSVPEMRLKQNAVPGQTAHIHFTPTQPGSYAILCTQLCGLGHYRM 225
Cdd:MTH00047  128 LLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCPDRHGVFVGYCSELCGVGHSYM 183
CuRO_HCO_II_like_4 cd13917
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 160-231 8.65e-13

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: 62.39  E-value: 8.65e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1892043850 160 LVLPAGREVDLALHAQDVIHGFSVPEMRLKQNAVPGQTAHIHFTPTQPGSYAILCTQLCGLGHYRMQATMLV 231
Cdd:cd13917    16 LVLKKGKTYRLHLSSLDVQHGFSLQPKNINFQVLPGYEWVITMTPNETGEFHIICNEYCGIGHHTMHGRIIV 87
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 104-245 1.30e-12

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 65.19  E-value: 1.30e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892043850 104 MQVEVTGMQFAWYFRYPG-ADAAFGE--TKPTLVAPGEGNPLGLDpadrhgaddlvtSQLVLPAGREVDLALHAQDVIHG 180
Cdd:MTH00076   95 LTVKAIGHQWYWSYEYTDyEDLSFDSymIPTQDLTPGQFRLLEVD------------NRMVVPMESPIRMLITAEDVLHS 162

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1892043850 181 FSVPEMRLKQNAVPGQTAHIHFTPTQPGSYAILCTQLCGLGHYRMQATMLVLPPAAFDTWLQAHE 245
Cdd:MTH00076  163 WAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLNWSSSML 227
N2OR_C cd04223
The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase ...
 174-233 6.52e-12

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: 60.33  E-value: 6.52e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892043850 174 AQDVIHGFSVPEMRLKQNAVPGQTAHIHFTPTQPGSYAILCTQLCGLGHYRMQATMLVLP 233
Cdd:cd04223    36 DEDITHGFAIPGYNVNLSLEPGETATVTFVADKPGVYPYYCTEFCSALHLEMQGYLIVEP 95
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 160-241 1.59e-11

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 62.26  E-value: 1.59e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892043850 160 LVLPAGREVDLALHAQDVIHGFSVPEMRLKQNAVPGQTAHIHFTPTQPGSYAILCTQLCGLGHYRMQATMLVLPPAAFDT 239
Cdd:MTH00140  142 LVLPYSVDTRVLVTSADVIHSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVK 221


                  ..
gi 1892043850 240 WL 241
Cdd:MTH00140  222 WL 223
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 103-241 4.02e-11

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 60.89  E-value: 4.02e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892043850 103 AMQVEVTGMQfaWYFRYPGADAAFGETKPTLVAPGEgnpLGLDPADRHGADdlvtSQLVLPAGREVDLALHAQDVIHGFS 182
Cdd:MTH00139   94 YLTFKAVGHQ--WYWSYEYSDFKNLSFDSYMIPTED---LSSGEFRLLEVD----NRLVLPYKSNIRALITAADVLHSWT 164

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1892043850 183 VPEMRLKQNAVPGQTAHIHFTPTQPGSYAILCTQLCGLGHYRMQATMLVLPPAAFDTWL 241
Cdd:MTH00139  165 VPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEWI 223
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 106-241 9.27e-11

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 59.99  E-value: 9.27e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892043850 106 VEVTGMQfaWYFRYPGADaaFGE------TKPTLVAPGEGNPLgLDpadrhgaddlVTSQLVLPAGREVDLALHAQDVIH 179
Cdd:MTH00168   97 IKAVGHQ--WYWSYEYTD--YNDlefdsyMVPTQDLSPGQFRL-LE----------VDNRLVLPMDSKIRVLVTSADVLH 161

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1892043850 180 GFSVPEMRLKQNAVPGQTAHIHFTPTQPGSYAILCTQLCGLGHYRMQATMLVLPPAAFDTWL 241
Cdd:MTH00168  162 SWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENWV 223
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 156-240 1.06e-10

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 59.73  E-value: 1.06e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892043850 156 VTSQLVLPAGREVDLALHAQDVIHGFSVPEMRLKQNAVPGQTAHIHFTPTQPGSYAILCTQLCGLGHYRMQATMLVLPPA 235
Cdd:MTH00098  138 VDNRVVLPMEMPIRMLISSEDVLHSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLK 217


                  ....*
gi 1892043850 236 AFDTW 240
Cdd:MTH00098  218 YFEKW 222
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 103-246 1.23e-10

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 59.79  E-value: 1.23e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892043850 103 AMQVEVTGMQFAWYFRYPGADAAFGETKPTLVapgegnplgldPADRHGADDL----VTSQLVLPAGREVDLALHAQDVI 178
Cdd:MTH00051   96 ALTIKAIGHQWYWSYEYSDYGTDTIEFDSYMI-----------PTSDLNSGDLrlleVDNRLIVPIQTQVRVLVTAADVL 164

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1892043850 179 HGFSVPEMRLKQNAVPGQTAHIHFTPTQPGSYAILCTQLCGLGHYRMQATMLVLPPAAFDTWLQAHEA 246
Cdd:MTH00051  165 HSFAVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINWVATQSE 232
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 159-240 1.87e-10

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 59.13  E-value: 1.87e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892043850 159 QLVLPAGREVDLALHAQDVIHGFSVPEMRLKQNAVPGQTAHIHFTPTQPGSYAILCTQLCGLGHYRMQATMLVLPPAAFD 238
Cdd:MTH00185  141 RMVVPMESPIRVLITAEDVLHSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFE 220


                  ..
gi 1892043850 239 TW 240
Cdd:MTH00185  221 NW 222
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 104-241 1.90e-09

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 56.57  E-value: 1.90e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892043850 104 MQVEVTGMQfaWYFRYPGADaaFGETKPtlvapgEGNPLGLDPADRHGADDL---VTSQLVLPAGREVDLALHAQDVIHG 180
Cdd:MTH00027  127 ITIKVTGHQ--WYWSYSYED--YGEKNI------EFDSYMIPTADLEFGDLRlleVDNRLILPVDTNVRVLITAADVLHS 196

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1892043850 181 FSVPEMRLKQNAVPGQTAHIHFTPTQPGSYAILCTQLCGLGHYRMQATMLVLPPAAFDTWL 241
Cdd:MTH00027  197 WTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYIDWI 257
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 103-225 3.48e-09

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 55.53  E-value: 3.48e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892043850 103 AMQVEVTGMQFAWYFRYPGADAAFGETKPTLVAPGEGNPlgldpadrhGADDL--VTSQLVLPAGREVDLALHAQDVIHG 180
Cdd:MTH00023  103 ALTIKAIGHQWYWSYEYSDYEGETLEFDSYMVPTSDLNS---------GDFRLleVDNRLVVPINTHVRILVTGADVLHS 173

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1892043850 181 FSVPEMRLKQNAVPGQTAHIHFTPTQPGSYAILCTQLCGLGHYRM 225
Cdd:MTH00023  174 FAVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFM 218
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 156-240 3.65e-09

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 55.48  E-value: 3.65e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892043850 156 VTSQLVLPAGREVDLALHAQDVIHGFSVPEMRLKQNAVPGQTAHIHFTPTQPGSYAILCTQLCGLGHYRMQATMLVLPPA 235
Cdd:MTH00038  138 VDNRLVLPYQTPIRVLVSSADVLHSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFN 217


                  ....*
gi 1892043850 236 AFDTW 240
Cdd:MTH00038  218 TFENW 222
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 159-240 4.47e-09

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 55.11  E-value: 4.47e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892043850 159 QLVLPAGREVDLALHAQDVIHGFSVPEMRLKQNAVPGQTAHIHFTPTQPGSYAILCTQLCGLGHYRMQATMLVLPPAAFD 238
Cdd:MTH00129  141 RMVVPVESPIRVLVSAEDVLHSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFE 220


                  ..
gi 1892043850 239 TW 240
Cdd:MTH00129  221 NW 222
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 156-241 8.71e-09

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 54.45  E-value: 8.71e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892043850 156 VTSQLVLPAGREVDLALHAQDVIHGFSVPEMRLKQNAVPGQTAHIHFTPTQPGSYAILCTQLCGLGHYRMQATMLVLPPA 235
Cdd:MTH00154  138 VDNRLVLPMNTQIRILITAADVIHSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVN 217


                  ....*.
gi 1892043850 236 AFDTWL 241
Cdd:MTH00154  218 NFINWI 223
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 156-241 2.40e-08

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 52.99  E-value: 2.40e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892043850 156 VTSQLVLPAGREVDLALHAQDVIHGFSVPEMRLKQNAVPGQTAHIHFTPTQPGSYAILCTQLCGLGHYRMQATMLVLPPA 235
Cdd:MTH00117  138 VDHRMVIPMESPIRILITAEDVLHSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLK 217


                  ....*.
gi 1892043850 236 AFDTWL 241
Cdd:MTH00117  218 HFENWS 223
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 156-237 1.26e-06

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 47.12  E-value: 1.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892043850 156 VTSQLVLPAGREVDLALHAQDVIHGFSVPEMRLKQNAVPGQTAHIHFTPTQPGSYAILCTQLCGLGHYRMQATMLVLPPA 235
Cdd:PTZ00047   71 VDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCSEMCGTLHGFMPIVVEAVSPE 150


                  ..
gi 1892043850 236 AF 237
Cdd:PTZ00047  151 AY 152
PRK02888 PRK02888
nitrous-oxide reductase; Validated
 175-233 2.41e-06

nitrous-oxide reductase; Validated


Pssm-ID: 235082 [Multi-domain]  Cd Length: 635  Bit Score: 48.05  E-value: 2.41e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1892043850 175 QDVIHGFSVPEMRLKQNAVPGQTAHIHFTPTQPGSYAILCTQLCGLGHYRMQATMLVLP 233
Cdd:PRK02888  576 EDLTHGFAIPNYGVNMEVAPQATASVTFTADKPGVYWYYCTWFCHALHMEMRGRMLVEP 634
Cupredoxin_1 pfam13473
Cupredoxin-like domain; The cupredoxin-like fold consists of a beta-sandwich with 7 strands in ...
 158-214 5.58e-06

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: 44.11  E-value: 5.58e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1892043850 158 SQLVLPAGREVDLALHAQD-VIHGFSVPEMRLKQNAVPGQTAHIHFTPTQPGSYAILC 214
Cdd:pfam13473  35 SRITVPAGTPVKLEFKNKDkTPAEFESPDLGIEKVLAPGKTSTITIPPLKPGEYDFFC 92
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 156-225 7.95e-06

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 45.77  E-value: 7.95e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892043850 156 VTSQLVLPAGREVDLALHAQDVIHGFSVPEMRLKQNAVPGQTAHIHFTPTQPGSYAILCTQLCGLGHYRM 225
Cdd:MTH00080  141 VDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDAMSGILSTLCYSFPMPGVFYGQCSEICGANHSFM 210
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 104-225 7.70e-05

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: 40.61  E-value: 7.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892043850 104 MQVEVTGMQFAWYFRYPGADAAfgetkpTLvapgegnplgldpadrhgaddlvtSQLVLPAGREVDLALHAQDVIHGFSV 183
Cdd:cd04212     1 LEIQVVSLDWKWLFIYPEQGIA------TV------------------------NELVIPVGRPVNFRLTSDSVMNSFFI 50

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1892043850 184 PEMRLKQNAVPGQTAHIHFTPTQPGSYAILCTQLCGLGHYRM 225
Cdd:cd04212    51 PQLGGQIYAMAGMQTQLHLIADKPGTYQGLSANYSGEGFSDM 92
Auracyanin cd04233
Auracyanins A and B and similar proteins; This subfamily includes both auracyanins A and B ...
 194-231 1.73e-04

Auracyanins A and B and similar proteins; This subfamily includes both auracyanins A and B from the photosynthetic bacterium Chloroflexus aurantiacus and similar proteins. Auracyanins A and B are very similar blue copper proteins with 38% sequence identity and are homologous to the bacterial redox protein Azurin. However, auracyanin A is expressed only when C. aurantiacus cells are grown in light, whereas auracyanin B is expressed in both dark and light conditions. Thus, auracyanin A may function as a redox partner in photosynthesis, while auracyanin B may function in aerobic respiration.


Pssm-ID: 259895 [Multi-domain]  Cd Length: 121  Bit Score: 40.31  E-value: 1.73e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1892043850 194 PGQTAHIHFT-PTQPGSYAILCTQlcgLGHYR-MQATMLV 231
Cdd:cd04233    85 PGETETLTFTaPTEPGTYPYVCTY---PGHWAiMKGVLIV 121
COG4633 COG4633
Plastocyanin domain containing protein [General function prediction only];
158-224 6.93e-04

Plastocyanin domain containing protein [General function prediction only];


Pssm-ID: 443671 [Multi-domain]  Cd Length: 121  Bit Score: 38.36  E-value: 6.93e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1892043850 158 SQLVLPAGREVDLALHAQDV---IHGFSVPEMRLKQNAVPGQTAHIHFTPTQPGSYAIlctqLCGLGHYR 224
Cdd:COG4633    50 SRITVKAGIPVRLNFTRKDPsgcAEEVVFPDLGISQDLPLGKTVTIEFTPLKPGEYPF----TCGMGMYR 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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