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Conserved domains on  [gi|2496356954|ref|WP_280142393|]
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cytochrome c oxidase subunit II [Rhizobium sp. NFR03]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
4-233 3.28e-74

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


:

Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 228.17  E-value: 3.28e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496356954   4 RSAVLPGCVFLSGCSGKQSALDPAGVEATSVHHLFIVMVVGGAIIWALVVGLLLYAGHARREPITARKA-----SWLILG 78
Cdd:COG1622     2 KRLLLALLLLALLLSGQLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLLLYFAIRYRRRKGDADPaqfhhNTKLEI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496356954  79 GGVAFPVIVLFCLLAYAVWLMPQIRPFMPALMdnkpQIEATGEQFWWRLRYLDDGGntafETANELRLPVGERTTFRLKA 158
Cdd:COG1622    82 VWTVIPIIIVIVLAVPTLRVLHALDDAPEDPL----TVEVTGYQWKWLFRYPDQGI----ATVNELVLPVGRPVRFLLTS 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2496356954 159 ADVIHSFWIPSLGGKMDMIPGRDNVLSLEPTKTGVYRAPCAEFCGTSHALMAFSVIVMERPDFDAWRQSRIEAAA 233
Cdd:COG1622   154 ADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAEQKASAA 228
Cyc7 COG3474
Cytochrome c2 [Energy production and conversion];
241-324 4.38e-16

Cytochrome c2 [Energy production and conversion];


:

Pssm-ID: 442697 [Multi-domain]  Cd Length: 101  Bit Score: 72.61  E-value: 4.38e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496356954 241 GRDLFFRhGCAACHTIAGTPAiGRIGPDLTRIGERQTIA-----------AGTLANTKDNIARFIREPDAIKPGVEMPAF 309
Cdd:COG3474     6 GEKLFNR-KCAACHSVDGGAG-NRVGPNLNGVVGRKAGSvegfaysdalkASGLVWDEETLDAWLADPKAFVPGTKMPFA 83

                          90
                  ....*....|....*
gi 2496356954 310 GMLPDGDIEAIAAWL 324
Cdd:COG3474    84 GLKDPEDRADLIAYL 98
 
Name Accession Description Interval E-value
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
4-233 3.28e-74

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 228.17  E-value: 3.28e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496356954   4 RSAVLPGCVFLSGCSGKQSALDPAGVEATSVHHLFIVMVVGGAIIWALVVGLLLYAGHARREPITARKA-----SWLILG 78
Cdd:COG1622     2 KRLLLALLLLALLLSGQLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLLLYFAIRYRRRKGDADPaqfhhNTKLEI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496356954  79 GGVAFPVIVLFCLLAYAVWLMPQIRPFMPALMdnkpQIEATGEQFWWRLRYLDDGGntafETANELRLPVGERTTFRLKA 158
Cdd:COG1622    82 VWTVIPIIIVIVLAVPTLRVLHALDDAPEDPL----TVEVTGYQWKWLFRYPDQGI----ATVNELVLPVGRPVRFLLTS 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2496356954 159 ADVIHSFWIPSLGGKMDMIPGRDNVLSLEPTKTGVYRAPCAEFCGTSHALMAFSVIVMERPDFDAWRQSRIEAAA 233
Cdd:COG1622   154 ADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAEQKASAA 228
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 116-216 4.27e-56

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: 177.43  E-value: 4.27e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496356954 116 IEATGEQFWWRLRYLDDGGnTAFETANELRLPVGERTTFRLKAADVIHSFWIPSLGGKMDMIPGRDNVLSLEPTKTGVYR 195
Cdd:cd04213     4 IEVTGHQWWWEFRYPDEPG-RGIVTANELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMDMIPGRTNRLWLQADEPGVYR 82

                          90       100
                  ....*....|....*....|.
gi 2496356954 196 APCAEFCGTSHALMAFSVIVM 216
Cdd:cd04213    83 GQCAEFCGASHALMRFKVIAL 103
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 26-224 1.87e-49

cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of mitochondria (and one of several possible acceptors in prokaryotes) in the electron transport chain of aerobic respiration. The enzyme couples the oxidation of reduced cytochrome c with the reduction of molecular oxygen to water. This process results in the pumping of four protons across the membrane which are used in the proton gradient powered synthesis of ATP. The oxidase contains two heme a cofactors and three copper atoms as well as other bound ions. [Energy metabolism, Electron transport]


Pssm-ID: 274329 [Multi-domain]  Cd Length: 199  Bit Score: 163.71  E-value: 1.87e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496356954  26 PAGVEATSVHHLFIVMVVGGAIIWALVVGLLLYAGHARREPITARKAS------WLILGGGVAfPVIVLFCLLAyavWLM 99
Cdd:TIGR02866   1 PGGEIAQQIAFLFLFVLAVSTLISLLVAALLAYVVWKFRRKGDEEKPSqihgnrRLEYVWTVI-PLIIVVGLFA---ATA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496356954 100 PQIRPFMPALMDNKPQIEATGEQFWWRLRYlddgGNTAFETANELRLPVGERTTFRLKAADVIHSFWIPSLGGKMDMIPG 179
Cdd:TIGR02866  77 KGLLYLERPIPKDALKVKVTGYQWWWDFEY----PESGFTTVNELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPG 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2496356954 180 RDNVLSLEPTKTGVYRAPCAEFCGTSHALMAFSVIVMERPDFDAW 224
Cdd:TIGR02866 153 QTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAY 197
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
116-217 2.07e-22

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 90.55  E-value: 2.07e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496356954 116 IEATGEQFWWRLRYLDDGgNTAF------------------ETANELRLPVGERTTFRLKAADVIHSFWIPSLGGKMDMI 177
Cdd:pfam00116   3 IKAIGHQWYWSYEYTDFG-DLEFdsymiptedleegqlrllEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDAV 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2496356954 178 PGRDNVLSLEPTKTGVYRAPCAEFCGTSHALMAfsvIVME 217
Cdd:pfam00116  82 PGRLNQTSFSIDREGVFYGQCSEICGINHSFMP---IVIE 118
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 19-217 5.38e-21

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 89.84  E-value: 5.38e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496356954  19 GKQSALDPAGVEATSVHH--LFIVMVVGGAIIWALVVGLLLYAGHARREPITARKASWLILGGGV----AFPVIVLfcll 92
Cdd:MTH00051   10 GFQDAASPVMEEIIFFHDqiMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAIlifiAFPSLKL---- 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496356954  93 ayaVWLMPQIrpFMPALmdnkpQIEATGEQFWWRLRYLDDGGNTA-------------------FETANELRLPVGERTT 153
Cdd:MTH00051   86 ---LYLMDEV--IDPAL-----TIKAIGHQWYWSYEYSDYGTDTIefdsymiptsdlnsgdlrlLEVDNRLIVPIQTQVR 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2496356954 154 FRLKAADVIHSFWIPSLGGKMDMIPGRDNVLSLEPTKTGVYRAPCAEFCGTSHALMAfsvIVME 217
Cdd:MTH00051  156 VLVTAADVLHSFAVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMP---IVIE 216
Cyc7 COG3474
Cytochrome c2 [Energy production and conversion];
241-324 4.38e-16

Cytochrome c2 [Energy production and conversion];


Pssm-ID: 442697 [Multi-domain]  Cd Length: 101  Bit Score: 72.61  E-value: 4.38e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496356954 241 GRDLFFRhGCAACHTIAGTPAiGRIGPDLTRIGERQTIA-----------AGTLANTKDNIARFIREPDAIKPGVEMPAF 309
Cdd:COG3474     6 GEKLFNR-KCAACHSVDGGAG-NRVGPNLNGVVGRKAGSvegfaysdalkASGLVWDEETLDAWLADPKAFVPGTKMPFA 83

                          90
                  ....*....|....*
gi 2496356954 310 GMLPDGDIEAIAAWL 324
Cdd:COG3474    84 GLKDPEDRADLIAYL 98
Cytochrom_C pfam00034
Cytochrome c; The Pfam entry does not include all Prosite members. The cytochrome 556 and ...
 241-328 2.53e-10

Cytochrome c; The Pfam entry does not include all Prosite members. The cytochrome 556 and cytochrome c' families are not included. All these are now in a new clan together. The C-terminus of DUF989, pfam06181, has now been merged into this family.


Pssm-ID: 459641 [Multi-domain]  Cd Length: 89  Bit Score: 56.39  E-value: 2.53e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496356954 241 GRDLFFRHgCAACHTIAGTPAiGRIGPDLTRIGERQTIAAGTLANT-KDNIARFIREPDAIKPGVEMPAFGMLPDGDIEA 319
Cdd:pfam00034   3 GKKLFAAN-CAACHGVNGEGA-GAGGPDLAGLAARYPGDALGAIREnKHAIGGGGVDRAGGPPGTGMPAFDGLTDEEIAD 80


                  ....*....
gi 2496356954 320 IAAWLGGLK 328
Cdd:pfam00034  81 LVAYLLSLS 89
PRK14486 PRK14486
putative bifunctional cbb3-type cytochrome c oxidase subunit II/cytochrome c; Provisional
 230-328 1.57e-03

putative bifunctional cbb3-type cytochrome c oxidase subunit II/cytochrome c; Provisional


Pssm-ID: 184704 [Multi-domain]  Cd Length: 294  Bit Score: 39.80  E-value: 1.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496356954 230 EAAAMPQpahpGRDLFFRHgCAACHtiaGTPAIGRIGPDLTRIGERQTIAAGTLANTKDNIArfirepdaikpGVEMPAF 309
Cdd:PRK14486  211 DVAAIAK----GKALYDAN-CAACH---GDEAQGQEGVALNDIDDGDLPDAAYFGMIKGGSD-----------AKGMPGF 271

                          90       100
                  ....*....|....*....|
gi 2496356954 310 G-MLPDGDIEAIAAWLGGLK 328
Cdd:PRK14486  272 GgDLSDDDIWAIVAYIRSQK 291
 
Name Accession Description Interval E-value
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
4-233 3.28e-74

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 228.17  E-value: 3.28e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496356954   4 RSAVLPGCVFLSGCSGKQSALDPAGVEATSVHHLFIVMVVGGAIIWALVVGLLLYAGHARREPITARKA-----SWLILG 78
Cdd:COG1622     2 KRLLLALLLLALLLSGQLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLLLYFAIRYRRRKGDADPaqfhhNTKLEI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496356954  79 GGVAFPVIVLFCLLAYAVWLMPQIRPFMPALMdnkpQIEATGEQFWWRLRYLDDGGntafETANELRLPVGERTTFRLKA 158
Cdd:COG1622    82 VWTVIPIIIVIVLAVPTLRVLHALDDAPEDPL----TVEVTGYQWKWLFRYPDQGI----ATVNELVLPVGRPVRFLLTS 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2496356954 159 ADVIHSFWIPSLGGKMDMIPGRDNVLSLEPTKTGVYRAPCAEFCGTSHALMAFSVIVMERPDFDAWRQSRIEAAA 233
Cdd:COG1622   154 ADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAEQKASAA 228
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 116-216 4.27e-56

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: 177.43  E-value: 4.27e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496356954 116 IEATGEQFWWRLRYLDDGGnTAFETANELRLPVGERTTFRLKAADVIHSFWIPSLGGKMDMIPGRDNVLSLEPTKTGVYR 195
Cdd:cd04213     4 IEVTGHQWWWEFRYPDEPG-RGIVTANELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMDMIPGRTNRLWLQADEPGVYR 82

                          90       100
                  ....*....|....*....|.
gi 2496356954 196 APCAEFCGTSHALMAFSVIVM 216
Cdd:cd04213    83 GQCAEFCGASHALMRFKVIAL 103
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 26-224 1.87e-49

cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of mitochondria (and one of several possible acceptors in prokaryotes) in the electron transport chain of aerobic respiration. The enzyme couples the oxidation of reduced cytochrome c with the reduction of molecular oxygen to water. This process results in the pumping of four protons across the membrane which are used in the proton gradient powered synthesis of ATP. The oxidase contains two heme a cofactors and three copper atoms as well as other bound ions. [Energy metabolism, Electron transport]


Pssm-ID: 274329 [Multi-domain]  Cd Length: 199  Bit Score: 163.71  E-value: 1.87e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496356954  26 PAGVEATSVHHLFIVMVVGGAIIWALVVGLLLYAGHARREPITARKAS------WLILGGGVAfPVIVLFCLLAyavWLM 99
Cdd:TIGR02866   1 PGGEIAQQIAFLFLFVLAVSTLISLLVAALLAYVVWKFRRKGDEEKPSqihgnrRLEYVWTVI-PLIIVVGLFA---ATA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496356954 100 PQIRPFMPALMDNKPQIEATGEQFWWRLRYlddgGNTAFETANELRLPVGERTTFRLKAADVIHSFWIPSLGGKMDMIPG 179
Cdd:TIGR02866  77 KGLLYLERPIPKDALKVKVTGYQWWWDFEY----PESGFTTVNELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPG 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2496356954 180 RDNVLSLEPTKTGVYRAPCAEFCGTSHALMAFSVIVMERPDFDAW 224
Cdd:TIGR02866 153 QTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAY 197
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 115-216 5.00e-38

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: 130.84  E-value: 5.00e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496356954 115 QIEATGEQFWWRLRYLDDG---GNTAFETANELRLPVGERTTFRLKAADVIHSFWIPSLGGKMDMIPGRDNVLSLEPTKT 191
Cdd:cd13919     3 VVEVTAQQWAWTFRYPGGDgklGTDDDVTSPELHLPVGRPVLFNLRSKDVIHSFWVPEFRVKQDAVPGRTTRLWFTPTRE 82

                          90       100
                  ....*....|....*....|....*
gi 2496356954 192 GVYRAPCAEFCGTSHALMAFSVIVM 216
Cdd:cd13919    83 GEYEVRCAELCGLGHYRMRATVKVV 107
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 115-215 3.19e-31

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: 113.11  E-value: 3.19e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496356954 115 QIEATGEQFWWRLRYLDDGGNTafetaNELRLPVGERTTFRLKAADVIHSFWIPSLGGKMDMIPGRDNVLSLEPTKTGVY 194
Cdd:cd13915     3 EIQVTGRQWMWEFTYPNGKREI-----NELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQDVVPGRYTYLWFEATKPGEY 77

                          90       100
                  ....*....|....*....|.
gi 2496356954 195 RAPCAEFCGTSHALMAFSVIV 215
Cdd:cd13915    78 DLFCTEYCGTGHSGMIGKVRV 98
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 115-224 2.41e-28

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: 105.95  E-value: 2.41e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496356954 115 QIEATGEQFWWRLRYlDDGGNTafeTANELRLPVGERTTFRLKAADVIHSFWIPSLGGKMDMIPGRDNVLSLEPTKTGVY 194
Cdd:cd13914     2 EIEVEAYQWGWEFSY-PEANVT---TSEQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDAFPGQYNTIKTEATEEGEY 77

                          90       100       110
                  ....*....|....*....|....*....|
gi 2496356954 195 RAPCAEFCGTSHALMAFSVIVMERPDFDAW 224
Cdd:cd13914    78 QLYCAEYCGAGHSQMLSTVTVVSQDEYQQW 107
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 115-214 6.46e-28

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: 104.30  E-value: 6.46e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496356954 115 QIEATGEQFWWRLRYLDDGgntafeTANELRLPVGERTTFRLKAADVIHSFWIPSLGGKMDMIPGRDNVLSLEPTKTGVY 194
Cdd:cd13842     2 TVYVTGVQWSWTFIYPNVR------TPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDAVPGYTSELWFVADKPGTY 75

                          90       100
                  ....*....|....*....|
gi 2496356954 195 RAPCAEFCGTSHALMAFSVI 214
Cdd:cd13842    76 TIICAEYCGLGHSYMLGKVE 95
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 116-224 1.85e-26

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: 101.49  E-value: 1.85e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496356954 116 IEATGEQFWWRLRYLDD-----------------GGNTAFETANELRLPVGERTTFRLKAADVIHSFWIPSLGGKMDMIP 178
Cdd:cd13912     5 IKAIGHQWYWSYEYSDFndlefdsymipeddlekGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKVDAVP 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2496356954 179 GRDNVLSLEPTKTGVYRAPCAEFCGTSHALMAFSVIVMERPDFDAW 224
Cdd:cd13912    85 GRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
116-217 2.07e-22

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 90.55  E-value: 2.07e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496356954 116 IEATGEQFWWRLRYLDDGgNTAF------------------ETANELRLPVGERTTFRLKAADVIHSFWIPSLGGKMDMI 177
Cdd:pfam00116   3 IKAIGHQWYWSYEYTDFG-DLEFdsymiptedleegqlrllEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDAV 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2496356954 178 PGRDNVLSLEPTKTGVYRAPCAEFCGTSHALMAfsvIVME 217
Cdd:pfam00116  82 PGRLNQTSFSIDREGVFYGQCSEICGINHSFMP---IVIE 118
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 116-224 4.52e-22

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


Pssm-ID: 259985 [Multi-domain]  Cd Length: 139  Bit Score: 90.21  E-value: 4.52e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496356954 116 IEATGEQFWWRLRYLDDGgntafETANELRLPVGERTTFRLKAADVIHSFWIPSLGGKMDMIPGRDNVLSLEPTKTGVYR 195
Cdd:cd13918    35 VEVEGFQFGWQFEYPNGV-----TTGNTLRVPADTPIALRVTSTDVFHTFGIPELRVKADAIPGEYTSTWFEADEPGTYE 109

                          90       100
                  ....*....|....*....|....*....
gi 2496356954 196 APCAEFCGTSHALMAFSVIVMERPDFDAW 224
Cdd:cd13918   110 AKCYELCGSGHSLMTGDVIVMDEEEFEAW 138
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 19-217 5.38e-21

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 89.84  E-value: 5.38e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496356954  19 GKQSALDPAGVEATSVHH--LFIVMVVGGAIIWALVVGLLLYAGHARREPITARKASWLILGGGV----AFPVIVLfcll 92
Cdd:MTH00051   10 GFQDAASPVMEEIIFFHDqiMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAIlifiAFPSLKL---- 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496356954  93 ayaVWLMPQIrpFMPALmdnkpQIEATGEQFWWRLRYLDDGGNTA-------------------FETANELRLPVGERTT 153
Cdd:MTH00051   86 ---LYLMDEV--IDPAL-----TIKAIGHQWYWSYEYSDYGTDTIefdsymiptsdlnsgdlrlLEVDNRLIVPIQTQVR 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2496356954 154 FRLKAADVIHSFWIPSLGGKMDMIPGRDNVLSLEPTKTGVYRAPCAEFCGTSHALMAfsvIVME 217
Cdd:MTH00051  156 VLVTAADVLHSFAVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMP---IVIE 216
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 109-224 2.76e-20

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 87.69  E-value: 2.76e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496356954 109 LMD--NKPQIE--ATGEQFWWRLRY-----------------LDDGGNTAFETANELRLPVGERTTFRLKAADVIHSFWI 167
Cdd:MTH00140   86 LLDetNNPLLTvkAIGHQWYWSYEYsdfsviefdsymvpeneLELGDFRLLEVDNRLVLPYSVDTRVLVTSADVIHSWTV 165

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2496356954 168 PSLGGKMDMIPGRDNVLSLEPTKTGVYRAPCAEFCGTSHALMAFSVIVMERPDFDAW 224
Cdd:MTH00140  166 PSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKW 222
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 35-224 5.55e-19

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 84.20  E-value: 5.55e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496356954  35 HHLFIVMVVGGAIIWALVVGLLLYAGHARREPITARKASWLILgggvafPVIVLFcLLAyavwlMPQIRPFMpaLMD--N 112
Cdd:MTH00117   26 HALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTIL------PAIVLI-LLA-----LPSLRILY--LMDeiN 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496356954 113 KPQ--IEATGEQFWWRLRYlDDGGNTAF------------------ETANELRLPVGERTTFRLKAADVIHSFWIPSLGG 172
Cdd:MTH00117   92 NPHltIKAIGHQWYWSYEY-TDYKDLSFdsymiptqdlpnghfrllEVDHRMVIPMESPIRILITAEDVLHSWAVPSLGV 170

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2496356954 173 KMDMIPGRDNVLSLEPTKTGVYRAPCAEFCGTSHALMAfsvIVMER---PDFDAW 224
Cdd:MTH00117  171 KTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMP---IVVESvplKHFENW 222
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 116-217 5.89e-19

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 83.08  E-value: 5.89e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496356954 116 IEATGEQFWWRLRYLDDGGNTAFETA------NELRLPVGERTTFRLKAADVIHSFWIPSLGGKMDMIPGRDNVLSLEPT 189
Cdd:MTH00047   84 IKVIGHQWYWSYEYSFGGSYDSFMTDdifgvdKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCPD 163

                          90       100
                  ....*....|....*....|....*...
gi 2496356954 190 KTGVYRAPCAEFCGTSHALMAfsvIVME 217
Cdd:MTH00047  164 RHGVFVGYCSELCGVGHSYMP---IVIE 188
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 83-224 1.32e-18

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 83.11  E-value: 1.32e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496356954  83 FPVIVLFCLlayAVwlmPQIrpFMPALMD--NKPQ--IEATGEQFWWRLRYLD-----------------DGGNTAFETA 141
Cdd:MTH00168   68 IPAFILISL---AL---PSL--RLLYLMDeiDKPDltIKAVGHQWYWSYEYTDyndlefdsymvptqdlsPGQFRLLEVD 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496356954 142 NELRLPVGERTTFRLKAADVIHSFWIPSLGGKMDMIPGRDNVLSLEPTKTGVYRAPCAEFCGTSHALMAFSVIVMERPDF 221
Cdd:MTH00168  140 NRLVLPMDSKIRVLVTSADVLHSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETF 219


                  ...
gi 2496356954 222 DAW 224
Cdd:MTH00168  220 ENW 222
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 17-213 1.64e-17

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 80.18  E-value: 1.64e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496356954  17 CSGKQSALDPAGVEATSVHH--LFIVMVVGGAIIWALVVGLLLYAGHARREPITARKASWLILgggvafPVIVLFCLLAY 94
Cdd:MTH00023   15 QLGFQDAADPVMEEIIFFHDqiMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTII------PAVILVFIALP 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496356954  95 AVWLMPqirpFMPALMDNKPQIEATGEQFWWRLRY-------------------LDDGGNTAFETANELRLPVGERTTFR 155
Cdd:MTH00023   89 SLKLLY----LMDEVVSPALTIKAIGHQWYWSYEYsdyegetlefdsymvptsdLNSGDFRLLEVDNRLVVPINTHVRIL 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2496356954 156 LKAADVIHSFWIPSLGGKMDMIPGRDNVLSLEPTKTGVYRAPCAEFCGTSHALMAFSV 213
Cdd:MTH00023  165 VTGADVLHSFAVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVI 222
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 96-232 2.55e-17

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 79.54  E-value: 2.55e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496356954  96 VW-LMPQIRPFMPAL--------MD--NKPQ--IEATGEQFWWRLRYLD-----------------DGGNTAFETANELR 145
Cdd:MTH00185   64 VWtILPAIILIMIALpslrilylMDeiNDPHltIKAMGHQWYWSYEYTDyeqlefdsymtptqdltPGQFRLLETDHRMV 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496356954 146 LPVGERTTFRLKAADVIHSFWIPSLGGKMDMIPGRDNVLSLEPTKTGVYRAPCAEFCGTSHALMAFSVIVMERPDFDAWR 225
Cdd:MTH00185  144 VPMESPIRVLITAEDVLHSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENWS 223


                  ....*..
gi 2496356954 226 QSRIEAA 232
Cdd:MTH00185  224 SLMLEEA 230
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 109-224 6.01e-17

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 78.36  E-value: 6.01e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496356954 109 LMDNKPQ----IEATGEQFWWRLRYLD-----------------DGGNTAFETANELRLPVGERTTFRLKAADVIHSFWI 167
Cdd:MTH00008   86 LMDEVSNpsitLKTIGHQWYWSYEYSDfsnlefdsymlptsdlsPGQFRLLEVDNRAVLPMQTEIRVLVTAADVIHSWTV 165

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2496356954 168 PSLGGKMDMIPGRDNVLSLEPTKTGVYRAPCAEFCGTSHALMAFSVIVMERPDFDAW 224
Cdd:MTH00008  166 PSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKW 222
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 109-230 7.36e-17

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 78.28  E-value: 7.36e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496356954 109 LMD--NKPQ--IEATGEQFWWRLRYlDDGGNTAF------------------ETANELRLPVGERTTFRLKAADVIHSFW 166
Cdd:MTH00076   86 LMDeiNDPHltVKAIGHQWYWSYEY-TDYEDLSFdsymiptqdltpgqfrllEVDNRMVVPMESPIRMLITAEDVLHSWA 164

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2496356954 167 IPSLGGKMDMIPGRDNVLSLEPTKTGVYRAPCAEFCGTSHALMAFSVIVMERPDFDAWRQSRIE 230
Cdd:MTH00076  165 VPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLNWSSSMLE 228
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 37-217 1.05e-16

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 77.84  E-value: 1.05e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496356954  37 LFIVMVVGGAIIWalvvglLLYAGHARREPITAR--KASWLILgggvafPVIVLFCLLayavwlMPQIRPFMpaLMDNKP 114
Cdd:MTH00139   32 IMILSFVGYISLS------LMSNKFTSRSLLESQevETIWTVL------PAFILLFLA------LPSLRLLY--LMDEVS 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496356954 115 Q----IEATGEQFWWRLRYLD-----------------DGGNTAFETANELRLPVGERTTFRLKAADVIHSFWIPSLGGK 173
Cdd:MTH00139   92 DpyltFKAVGHQWYWSYEYSDfknlsfdsymiptedlsSGEFRLLEVDNRLVLPYKSNIRALITAADVLHSWTVPSLGVK 171

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2496356954 174 MDMIPGRDNVLSLEPTKTGVYRAPCAEFCGTSHALMAfsvIVME 217
Cdd:MTH00139  172 IDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMP---IVVE 212
Cyc7 COG3474
Cytochrome c2 [Energy production and conversion];
241-324 4.38e-16

Cytochrome c2 [Energy production and conversion];


Pssm-ID: 442697 [Multi-domain]  Cd Length: 101  Bit Score: 72.61  E-value: 4.38e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496356954 241 GRDLFFRhGCAACHTIAGTPAiGRIGPDLTRIGERQTIA-----------AGTLANTKDNIARFIREPDAIKPGVEMPAF 309
Cdd:COG3474     6 GEKLFNR-KCAACHSVDGGAG-NRVGPNLNGVVGRKAGSvegfaysdalkASGLVWDEETLDAWLADPKAFVPGTKMPFA 83

                          90
                  ....*....|....*
gi 2496356954 310 GMLPDGDIEAIAAWL 324
Cdd:COG3474    84 GLKDPEDRADLIAYL 98
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 109-224 6.16e-16

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 75.64  E-value: 6.16e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496356954 109 LMD--NKPQI--EATGEQFWWRLRYLD--------------DGGNTAF---ETANELRLPVGERTTFRLKAADVIHSFWI 167
Cdd:MTH00154   86 LLDevNNPSItlKTIGHQWYWSYEYSDfkniefdsymiptnELENNGFrllDVDNRLVLPMNTQIRILITAADVIHSWTV 165

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496356954 168 PSLGGKMDMIPGRDNVLSLEPTKTGVYRAPCAEFCGTSHALMAfsvIVME---RPDFDAW 224
Cdd:MTH00154  166 PSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMP---IVIEsvsVNNFINW 222
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 140-215 9.08e-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: 71.83  E-value: 9.08e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2496356954 140 TANELRLPVGERTTFRLKAADVIHSFWIPSLGGKMDMIPGRDNVLSLEPTKTGVYRAPCAEFCGTSHALMAFSVIV 215
Cdd:cd13913    23 NPNEIEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNMYGKIIV 98
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 109-231 1.21e-15

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 74.74  E-value: 1.21e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496356954 109 LMD--NKP--QIEATGEQFWWRLRYLDD-----------------GGNTAFETANELRLPVGERTTFRLKAADVIHSFWI 167
Cdd:MTH00038   86 LMDevNNPflTIKAIGHQWYWSYEYTDYndlefdsymvptsdlstGLPRLLEVDNRLVLPYQTPIRVLVSSADVLHSWAV 165

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2496356954 168 PSLGGKMDMIPGRDNVLSLEPTKTGVYRAPCAEFCGTSHALMAfsvIVME---RPDFDAWRQSRIEA 231
Cdd:MTH00038  166 PSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMP---IVIEsvpFNTFENWVSNFLEE 229
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 109-232 1.50e-15

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 74.75  E-value: 1.50e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496356954 109 LMD--NKPQ--IEATGEQFWWRLRYLD-----------------DGGNTAFETANELRLPVGERTTFRLKAADVIHSFWI 167
Cdd:MTH00129   86 LMDeiNDPHltIKAMGHQWYWSYEYTDyedlgfdsymiptqdltPGQFRLLEADHRMVVPVESPIRVLVSAEDVLHSWAV 165

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2496356954 168 PSLGGKMDMIPGRDNVLSLEPTKTGVYRAPCAEFCGTSHALMAFSVIVMERPDFDAWRQSRIEAA 232
Cdd:MTH00129  166 PALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLMLEDA 230
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 83-224 3.31e-15

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 73.51  E-value: 3.31e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496356954  83 FPVIVLFCLLAYAVWLMpqirpFMPALM--DNKPQIEATGEQFWWRLRYLDDGG-----------------NTAFETANE 143
Cdd:MTH00080   70 FPVLILLMQMVPSLSLL-----YYYGLMnlDSNLTVKVTGHQWYWSYEFSDIPGlefdsymksldqlrlgePRLLEVDNR 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496356954 144 LRLPVGERTTFRLKAADVIHSFWIPSLGGKMDMIPGRDNVLSLEPTKTGVYRAPCAEFCGTSHALMAFSVIVMERPDFDA 223
Cdd:MTH00080  145 CVLPCDTNIRFCITSSDVIHSWALPSLSIKMDAMSGILSTLCYSFPMPGVFYGQCSEICGANHSFMPIAVEVTLLDNFKE 224


                  .
gi 2496356954 224 W 224
Cdd:MTH00080  225 W 225
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 35-227 5.05e-15

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 73.21  E-value: 5.05e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496356954  35 HHLFIVMVVGGAIIWALVVGLLLYAGHARREPITARKASWLILgggvafPVIVLFcLLAyavwlMPQIRPFMpaLMD--N 112
Cdd:MTH00098   26 HTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTIL------PAIILI-LIA-----LPSLRILY--MMDeiN 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496356954 113 KPQ--IEATGEQFWWRLRYLDDGG--------NTAFETANELRL-PVGERTTFRLKAA--------DVIHSFWIPSLGGK 173
Cdd:MTH00098   92 NPSltVKTMGHQWYWSYEYTDYEDlsfdsymiPTSDLKPGELRLlEVDNRVVLPMEMPirmlisseDVLHSWAVPSLGLK 171

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2496356954 174 MDMIPGRDNVLSLEPTKTGVYRAPCAEFCGTSHALMAfsvIVMER---PDFDAWRQS 227
Cdd:MTH00098  172 TDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMP---IVLELvplKYFEKWSAS 225
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 19-224 2.53e-14

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 71.60  E-value: 2.53e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496356954  19 GKQSALDPAGVEATSVHH--LFIVMVVGGAIIWaLVVGLLLYAGHarrepitaRKASWLILGGG---VAFPVIVLFCLLA 93
Cdd:MTH00027   36 GFQDAGSPVMEEIIMLHDqiLFILTIIVGVVLW-LIIRILLGNNY--------YSYYWNKLDGSlieVIWTLIPAFILIL 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496356954  94 YAvwlMPQIRpfMPALMDN-----KPQIEATGEQFWWRLRYLDDG-GNTAF------------------ETANELRLPVG 149
Cdd:MTH00027  107 IA---FPSLR--LLYIMDEcgfsaNITIKVTGHQWYWSYSYEDYGeKNIEFdsymiptadlefgdlrllEVDNRLILPVD 181

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2496356954 150 ERTTFRLKAADVIHSFWIPSLGGKMDMIPGRDNVLSLEPTKTGVYRAPCAEFCGTSHALMAFSVIVMERPDFDAW 224
Cdd:MTH00027  182 TNVRVLITAADVLHSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYIDW 256
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 115-216 1.05e-13

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: 66.03  E-value: 1.05e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496356954 115 QIEATGEQFWWRLRYLDDGgntaFETANELRLPVGERTTFRLKAADVIHSFWIPSLGGKMDMIPGRDNVLSLEPTKTGVY 194
Cdd:cd04212     2 EIQVVSLDWKWLFIYPEQG----IATVNELVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGTY 77

                          90       100
                  ....*....|....*....|..
gi 2496356954 195 RAPCAEFCGTSHALMAFSVIVM 216
Cdd:cd04212    78 QGLSANYSGEGFSDMKFKVLAV 99
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 139-217 3.38e-13

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 66.38  E-value: 3.38e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2496356954 139 ETANELRLPVGERTTFRLKAADVIHSFWIPSLGGKMDMIPGRDNVLSLEPTKTGVYRAPCAEFCGTSHALMAfsvIVME 217
Cdd:PTZ00047   70 EVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCSEMCGTLHGFMP---IVVE 145
CytC552 COG4654
Cytochrome c551/c552 [Energy production and conversion];
237-328 1.01e-11

Cytochrome c551/c552 [Energy production and conversion];


Pssm-ID: 443692 [Multi-domain]  Cd Length: 88  Bit Score: 60.30  E-value: 1.01e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496356954 237 PAHPGRDLFFRHGCAACHTIAGTpaigRIGPDLTRIGERQTIAAGtlanTKDNIARFIREPDAIKPG-VEMPAFGMLPDG 315
Cdd:COG4654     3 DAAAGKALAKKSGCLACHAVDKK----LVGPSYKDVAKKYKGKAD----AVAKLAKKIKKGGSGVWGdVPMPPHPQLSDA 74

                          90
                  ....*....|...
gi 2496356954 316 DIEAIAAWLGGLK 328
Cdd:COG4654    75 EAKALVKWILSLK 87
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 115-215 1.13e-10

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


Pssm-ID: 259983 [Multi-domain]  Cd Length: 93  Bit Score: 57.39  E-value: 1.13e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496356954 115 QIEATGEQFWWRLrylddGGNTafetanelrLPVGERTTFRLKAADVIHSFWIPSLGGKM----DMIPGRDNVLSLEPTK 190
Cdd:cd13916     2 VVAVTGHQWYWEL-----SRTE---------IPAGKPVEFRVTSADVNHGFGIYDPDMRLlaqtQAMPGYTNVLRYTFDK 67

                          90       100
                  ....*....|....*....|....*
gi 2496356954 191 TGVYRAPCAEFCGTSHALMAFSVIV 215
Cdd:cd13916    68 PGTYTILCLEYCGLAHHVMMAEFTV 92
Cytochrom_C pfam00034
Cytochrome c; The Pfam entry does not include all Prosite members. The cytochrome 556 and ...
 241-328 2.53e-10

Cytochrome c; The Pfam entry does not include all Prosite members. The cytochrome 556 and cytochrome c' families are not included. All these are now in a new clan together. The C-terminus of DUF989, pfam06181, has now been merged into this family.


Pssm-ID: 459641 [Multi-domain]  Cd Length: 89  Bit Score: 56.39  E-value: 2.53e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496356954 241 GRDLFFRHgCAACHTIAGTPAiGRIGPDLTRIGERQTIAAGTLANT-KDNIARFIREPDAIKPGVEMPAFGMLPDGDIEA 319
Cdd:pfam00034   3 GKKLFAAN-CAACHGVNGEGA-GAGGPDLAGLAARYPGDALGAIREnKHAIGGGGVDRAGGPPGTGMPAFDGLTDEEIAD 80


                  ....*....
gi 2496356954 320 IAAWLGGLK 328
Cdd:pfam00034  81 LVAYLLSLS 89
PRK10525 PRK10525
cytochrome o ubiquinol oxidase subunit II; Provisional
 86-224 3.06e-09

cytochrome o ubiquinol oxidase subunit II; Provisional


Pssm-ID: 182518 [Multi-domain]  Cd Length: 315  Bit Score: 57.12  E-value: 3.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496356954  86 IVLFCLLAYAVW-LMPQIRPFMPALMDNKP-QIEATGEQFWWRLRYLDDGgntaFETANELRLPVGERTTFRLKAADVIH 163
Cdd:PRK10525   97 ILIIIFLAVLTWkTTHALEPSKPLAHDEKPiTIEVVSMDWKWFFIYPEQG----IATVNEIAFPANVPVYFKVTSNSVMN 172

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2496356954 164 SFWIPSLGGKMDMIPGRDNVLSLEPTKTGVYRAPCAEFCGTSHALMAFSVIVM-ERPDFDAW 224
Cdd:PRK10525  173 SFFIPRLGSQIYAMAGMQTRLHLIANEPGTYDGISASYSGPGFSGMKFKAIATpDRAEFDQW 234
CuRO_HCO_II_like_4 cd13917
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 144-215 7.87e-09

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: 51.99  E-value: 7.87e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2496356954 144 LRLPVGERTTFRLKAADVIHSFWIPSLGGKMDMIPGRDNVLSLEPTKTGVYRAPCAEFCGTSHALMAFSVIV 215
Cdd:cd13917    16 LVLKKGKTYRLHLSSLDVQHGFSLQPKNINFQVLPGYEWVITMTPNETGEFHIICNEYCGIGHHTMHGRIIV 87
CccA COG2010
Cytochrome c, mono- and diheme variants [Energy production and conversion];
223-324 1.61e-08

Cytochrome c, mono- and diheme variants [Energy production and conversion];


Pssm-ID: 441613 [Multi-domain]  Cd Length: 169  Bit Score: 53.41  E-value: 1.61e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496356954 223 AWRQSRIEAAAMPQPAHPGRDLFFRHgCAACHTIAGTPAIGRIgPDLTRigerqtiaAGTLANTKDNIARFIREPdaiKP 302
Cdd:COG2010    74 LAAAAADAPAADAEALARGKALYEQN-CAACHGADGKGGLGAA-PNLTD--------DALYGGDPEALVETILNG---RP 140

                          90       100
                  ....*....|....*....|...
gi 2496356954 303 GVEMPAFG-MLPDGDIEAIAAWL 324
Cdd:COG2010   141 GGAMPAFGgQLSDEEIAALAAYL 163
CytC553 COG2863
Cytochrome c553 [Energy production and conversion];
231-328 6.30e-06

Cytochrome c553 [Energy production and conversion];


Pssm-ID: 442110 [Multi-domain]  Cd Length: 98  Bit Score: 44.33  E-value: 6.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496356954 231 AAAMPQPAHPGRDlfFRHGCAACHTIAGTPAIGRIGPDLTRIGErqtiaagtlantkDNIARFIREP-DAIKPGVEMPAF 309
Cdd:COG2863     8 APAAAGDAARGKA--YAAACAACHGADGEGNPGGGAPRLAGQHA-------------EYLVAQLKAFrSGARKNGVMPAI 72

                          90       100
                  ....*....|....*....|
gi 2496356954 310 -GMLPDGDIEAIAAWLGGLK 328
Cdd:COG2863    73 aKGLSDEDIKALAAYIASLK 92
Cytochrome_CBB3 pfam13442
Cytochrome C oxidase, cbb3-type, subunit III;
236-324 2.55e-05

Cytochrome C oxidase, cbb3-type, subunit III;


Pssm-ID: 463879 [Multi-domain]  Cd Length: 67  Bit Score: 41.62  E-value: 2.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496356954 236 QPAHPGRDLFFRHgCAACHtiagtpAIGRIGPDLTRIgerqtiaagtlANTKDNIARFIREpdaIKPGveMPAFG-MLPD 314
Cdd:pfam13442   1 AAAAAGEALYAAN-CASCH------GTGGAGPSLAGR-----------ALPPEALVDIIRN---GKGA--MPAFGgDLSD 57

                          90
                  ....*....|
gi 2496356954 315 GDIEAIAAWL 324
Cdd:pfam13442  58 EELEALAAYL 67
N2OR_C cd04223
The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase ...
 140-215 1.27e-04

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: 40.30  E-value: 1.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496356954 140 TANELRLPVGERTTFRL----KAADVIHSFWIPSLGGKMDMIPGRDNVLSLEPTKTGVYRAPCAEFCGTSHALMAFSVIV 215
Cdd:cd04223    14 TPDIIEVKEGDEVTVHLtnleQDEDITHGFAIPGYNVNLSLEPGETATVTFVADKPGVYPYYCTEFCSALHLEMQGYLIV 93
PRK14486 PRK14486
putative bifunctional cbb3-type cytochrome c oxidase subunit II/cytochrome c; Provisional
 230-328 1.57e-03

putative bifunctional cbb3-type cytochrome c oxidase subunit II/cytochrome c; Provisional


Pssm-ID: 184704 [Multi-domain]  Cd Length: 294  Bit Score: 39.80  E-value: 1.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2496356954 230 EAAAMPQpahpGRDLFFRHgCAACHtiaGTPAIGRIGPDLTRIGERQTIAAGTLANTKDNIArfirepdaikpGVEMPAF 309
Cdd:PRK14486  211 DVAAIAK----GKALYDAN-CAACH---GDEAQGQEGVALNDIDDGDLPDAAYFGMIKGGSD-----------AKGMPGF 271

                          90       100
                  ....*....|....*....|
gi 2496356954 310 G-MLPDGDIEAIAAWLGGLK 328
Cdd:PRK14486  272 GgDLSDDDIWAIVAYIRSQK 291
NosZ COG4263
Nitrous oxide reductase [Inorganic ion transport and metabolism];
142-208 6.75e-03

Nitrous oxide reductase [Inorganic ion transport and metabolism];


Pssm-ID: 443405 [Multi-domain]  Cd Length: 621  Bit Score: 38.35  E-value: 6.75e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2496356954 142 NELRLPVGERTTFRL----KAADVIHSFWIPSLGGKMDMIPGRDNVLSLEPTKTGVYRAPCAEFCgtsHAL 208
Cdd:COG4263   542 DEFEVKQGDEVTVHVtnldQVEDLTHGFAIPGYNINMEIMPQETASVTFVADKPGVYWYYCTWFC---HAL 609
 
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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