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Conserved domains on  [gi|1071411983|ref|WP_069837488|]
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cytochrome c oxidase subunit II [Bacillus subtilis]

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];
26-253 8.07e-57

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


:

Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 184.65  E-value: 8.07e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071411983  26 LSTLKPAGEVADKQFDLTVLSTLIMVVVVAVVSVIFFYVIVRFRRSRvgENTIPKQVEGNKFLEITWTvipillliilvi 105
Cdd:COG1622    19 LSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLLLYFAIRYRRRK--GDADPAQFHHNTKLEIVWTvipiii----vi 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071411983 106 pvvlYTLELadTSPMDkkgRKAEDALVVNVRANLYWWEFEYPDYGIITSQELIVPTDQRVYFNLKASDVKHSFWIPSVGG 185
Cdd:COG1622    93 vlavPTLRV--LHALD---DAPEDPLTVEVTGYQWKWLFRYPDQGIATVNELVLPVGRPVRFLLTSADVIHSFWVPALGG 167

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1071411983 186 KLDTNTDNENKFFLTFDskrskEAGDmFFGKCAELCGPSHALMDFKVKTMSAKEFQGWTKEMKNYKST 253
Cdd:COG1622   168 KQDAIPGRVTELWFTAD-----KPGT-YRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAEQKASAAT 229
Cyc7 COG3474
Cytochrome c2 [Energy production and conversion];
259-351 8.26e-17

Cytochrome c2 [Energy production and conversion];


:

Pssm-ID: 442697 [Multi-domain]  Cd Length: 101  Bit Score: 74.92  E-value: 8.26e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071411983 259 AKQGEELFKeKNCLSCHAVEPNDKraeaARTAPNLATFGERTK--VAGVK----------EANKENVKAWLKDPDSIKPG 326
Cdd:COG3474     3 AAAGEKLFN-RKCAACHSVDGGAG----NRVGPNLNGVVGRKAgsVEGFAysdalkasglVWDEETLDAWLADPKAFVPG 77

                          90       100
                  ....*....|....*....|....*.
gi 1071411983 327 NKMtgTYPKLSDSET-DALYEYLKGL 351
Cdd:COG3474    78 TKM--PFAGLKDPEDrADLIAYLKTL 101
 
Name Accession Description Interval E-value
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
26-253 8.07e-57

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 184.65  E-value: 8.07e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071411983  26 LSTLKPAGEVADKQFDLTVLSTLIMVVVVAVVSVIFFYVIVRFRRSRvgENTIPKQVEGNKFLEITWTvipillliilvi 105
Cdd:COG1622    19 LSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLLLYFAIRYRRRK--GDADPAQFHHNTKLEIVWTvipiii----vi 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071411983 106 pvvlYTLELadTSPMDkkgRKAEDALVVNVRANLYWWEFEYPDYGIITSQELIVPTDQRVYFNLKASDVKHSFWIPSVGG 185
Cdd:COG1622    93 vlavPTLRV--LHALD---DAPEDPLTVEVTGYQWKWLFRYPDQGIATVNELVLPVGRPVRFLLTSADVIHSFWVPALGG 167

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1071411983 186 KLDTNTDNENKFFLTFDskrskEAGDmFFGKCAELCGPSHALMDFKVKTMSAKEFQGWTKEMKNYKST 253
Cdd:COG1622   168 KQDAIPGRVTELWFTAD-----KPGT-YRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAEQKASAAT 229
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 130-235 2.32e-49

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: 160.86  E-value: 2.32e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071411983 130 ALVVNVRANLYWWEFEYPDY---GIITSQELIVPTDQRVYFNLKASDVKHSFWIPSVGGKLDTNTDNENKFFLTFDskrs 206
Cdd:cd04213     1 ALTIEVTGHQWWWEFRYPDEpgrGIVTANELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMDMIPGRTNRLWLQAD---- 76

                          90       100
                  ....*....|....*....|....*....
gi 1071411983 207 kEAGdMFFGKCAELCGPSHALMDFKVKTM 235
Cdd:cd04213    77 -EPG-VYRGQCAEFCGASHALMRFKVIAL 103
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 31-243 6.11e-43

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: 147.53  E-value: 6.11e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071411983  31 PAGEVADKQFDLTVLSTLIMVVVVAVVSVIFFYVIVRFRRSrvGENTIPKQVEGNKFLEITWTVIPILLLIILVIPVVLY 110
Cdd:TIGR02866   1 PGGEIAQQIAFLFLFVLAVSTLISLLVAALLAYVVWKFRRK--GDEEKPSQIHGNRRLEYVWTVIPLIIVVGLFAATAKG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071411983 111 TLELadTSPMDKkgrkaeDALVVNVRANLYWWEFEYPDYGIITSQELIVPTDQRVYFNLKASDVKHSFWIPSVGGKLDTN 190
Cdd:TIGR02866  79 LLYL--ERPIPK------DALKVKVTGYQWWWDFEYPESGFTTVNELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAI 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1071411983 191 TDNENKFFLTfdskrSKEAGdMFFGKCAELCGPSHALMDFKVKTMSAKEFQGW 243
Cdd:TIGR02866 151 PGQTNALWFN-----ADEPG-VYYGFCAELCGAGHSLMLFKVVVVPKEEFDAY 197
Cyc7 COG3474
Cytochrome c2 [Energy production and conversion];
259-351 8.26e-17

Cytochrome c2 [Energy production and conversion];


Pssm-ID: 442697 [Multi-domain]  Cd Length: 101  Bit Score: 74.92  E-value: 8.26e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071411983 259 AKQGEELFKeKNCLSCHAVEPNDKraeaARTAPNLATFGERTK--VAGVK----------EANKENVKAWLKDPDSIKPG 326
Cdd:COG3474     3 AAAGEKLFN-RKCAACHSVDGGAG----NRVGPNLNGVVGRKAgsVEGFAysdalkasglVWDEETLDAWLADPKAFVPG 77

                          90       100
                  ....*....|....*....|....*.
gi 1071411983 327 NKMtgTYPKLSDSET-DALYEYLKGL 351
Cdd:COG3474    78 TKM--PFAGLKDPEDrADLIAYLKTL 101
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 128-249 3.30e-13

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 68.27  E-value: 3.30e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071411983 128 EDALVVNVRANLYWWEFEYPDYG----------IITSQ-------------ELIVPTDQRVYFNLKASDVKHSFWIPSVG 184
Cdd:MTH00051   94 DPALTIKAIGHQWYWSYEYSDYGtdtiefdsymIPTSDlnsgdlrllevdnRLIVPIQTQVRVLVTAADVLHSFAVPSLS 173

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1071411983 185 GKLDT--NTDNENKFFLtfdskrsKEAGdMFFGKCAELCGPSHALMDFKVKTMSAKEFQGWTKEMKN 249
Cdd:MTH00051  174 VKIDAvpGRLNQTSFFI-------KRPG-VFYGQCSEICGANHSFMPIVIEGVSLDKYINWVATQSE 232
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
140-233 3.89e-13

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 65.51  E-value: 3.89e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071411983 140 YWWEFEYPDYGII---------------------TSQELIVPTDQRVYFNLKASDVKHSFWIPSVGGKLDTNTDNENKff 198
Cdd:pfam00116  10 WYWSYEYTDFGDLefdsymiptedleegqlrlleVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDAVPGRLNQ-- 87

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1071411983 199 LTFDSKRSkeagDMFFGKCAELCGPSHALMDFKVK 233
Cdd:pfam00116  88 TSFSIDRE----GVFYGQCSEICGINHSFMPIVIE 118
Cytochrom_C pfam00034
Cytochrome c; The Pfam entry does not include all Prosite members. The cytochrome 556 and ...
 262-352 1.75e-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: 56.78  E-value: 1.75e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071411983 262 GEELFKeKNCLSCHAVEPNDkraeAARTAPNLATFGERTKVAGVKEA--NKENVKAWLKDPDSIKPGNKMTGtYPKLSDS 339
Cdd:pfam00034   3 GKKLFA-ANCAACHGVNGEG----AGAGGPDLAGLAARYPGDALGAIreNKHAIGGGGVDRAGGPPGTGMPA-FDGLTDE 76

                          90
                  ....*....|...
gi 1071411983 340 ETDALYEYLKGLK 352
Cdd:pfam00034  77 EIADLVAYLLSLS 89
ccoP TIGR00782
cytochrome c oxidase, cbb3-type, subunit III; This model describes a di-heme subunit of ...
 251-351 5.26e-04

cytochrome c oxidase, cbb3-type, subunit III; This model describes a di-heme subunit of approximately 26 kDa of the cbb3 type copper and heme-containing cytochrome oxidase. [Energy metabolism, Electron transport]


Pssm-ID: 129864 [Multi-domain]  Cd Length: 285  Bit Score: 41.42  E-value: 5.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071411983 251 KSTAESDLAKQGEELFkEKNCLSCHAvepNDKRAEAARTAPNLAtfgertkvagvkeankENVKAWLKDPDSI------K 324
Cdd:TIGR00782 195 GKPKDEALAAKGQELF-ADNCTTCHG---EDGKGLQELGAPNLT----------------DDVWLYGGDLKTItttitnG 254

                          90       100
                  ....*....|....*....|....*..
gi 1071411983 325 PGNKMTGTYPKLSDSETDALYEYLKGL 351
Cdd:TIGR00782 255 RGGVMPAWGPRLSEAQIKALAAYVHSL 281
 
Name Accession Description Interval E-value
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
26-253 8.07e-57

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 184.65  E-value: 8.07e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071411983  26 LSTLKPAGEVADKQFDLTVLSTLIMVVVVAVVSVIFFYVIVRFRRSRvgENTIPKQVEGNKFLEITWTvipillliilvi 105
Cdd:COG1622    19 LSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLLLYFAIRYRRRK--GDADPAQFHHNTKLEIVWTvipiii----vi 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071411983 106 pvvlYTLELadTSPMDkkgRKAEDALVVNVRANLYWWEFEYPDYGIITSQELIVPTDQRVYFNLKASDVKHSFWIPSVGG 185
Cdd:COG1622    93 vlavPTLRV--LHALD---DAPEDPLTVEVTGYQWKWLFRYPDQGIATVNELVLPVGRPVRFLLTSADVIHSFWVPALGG 167

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1071411983 186 KLDTNTDNENKFFLTFDskrskEAGDmFFGKCAELCGPSHALMDFKVKTMSAKEFQGWTKEMKNYKST 253
Cdd:COG1622   168 KQDAIPGRVTELWFTAD-----KPGT-YRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAEQKASAAT 229
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 130-235 2.32e-49

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: 160.86  E-value: 2.32e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071411983 130 ALVVNVRANLYWWEFEYPDY---GIITSQELIVPTDQRVYFNLKASDVKHSFWIPSVGGKLDTNTDNENKFFLTFDskrs 206
Cdd:cd04213     1 ALTIEVTGHQWWWEFRYPDEpgrGIVTANELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMDMIPGRTNRLWLQAD---- 76

                          90       100
                  ....*....|....*....|....*....
gi 1071411983 207 kEAGdMFFGKCAELCGPSHALMDFKVKTM 235
Cdd:cd04213    77 -EPG-VYRGQCAEFCGASHALMRFKVIAL 103
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 31-243 6.11e-43

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: 147.53  E-value: 6.11e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071411983  31 PAGEVADKQFDLTVLSTLIMVVVVAVVSVIFFYVIVRFRRSrvGENTIPKQVEGNKFLEITWTVIPILLLIILVIPVVLY 110
Cdd:TIGR02866   1 PGGEIAQQIAFLFLFVLAVSTLISLLVAALLAYVVWKFRRK--GDEEKPSQIHGNRRLEYVWTVIPLIIVVGLFAATAKG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071411983 111 TLELadTSPMDKkgrkaeDALVVNVRANLYWWEFEYPDYGIITSQELIVPTDQRVYFNLKASDVKHSFWIPSVGGKLDTN 190
Cdd:TIGR02866  79 LLYL--ERPIPK------DALKVKVTGYQWWWDFEYPESGFTTVNELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAI 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1071411983 191 TDNENKFFLTfdskrSKEAGdMFFGKCAELCGPSHALMDFKVKTMSAKEFQGW 243
Cdd:TIGR02866 151 PGQTNALWFN-----ADEPG-VYYGFCAELCGAGHSLMLFKVVVVPKEEFDAY 197
QOXA TIGR01432
cytochrome aa3 quinol oxidase, subunit II; This enzyme catalyzes the oxidation of quinol with ...
 19-248 6.79e-25

cytochrome aa3 quinol oxidase, subunit II; This enzyme catalyzes the oxidation of quinol with the concomitant reduction of molecular oxygen to water. This acts as the terminal electron acceptor in the respiratory chain. This subunit contains two transmembrane helices and a large external domain responsible for the binding and oxidation of quinol. QuoX is (presently) only found in gram positive bacteria of the Bacillus/Staphylococcus group. Like CyoA, the ubiquinol oxidase found in proteobacteria, the residues responsible for the ligation of Cu(a) and cytochrome c (found in the related cyt. c oxidases) are absent. Unlike CyoA, QoxA is in complex with a subunit I which contains cytochromes a similar to the cyt. c oxidases (as opposed to cytochromes b). [Energy metabolism, Electron transport]


Pssm-ID: 273621 [Multi-domain]  Cd Length: 226  Bit Score: 100.76  E-value: 6.79e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071411983  19 SGCGKpfLSTLKPAGEVADKQFDLTVLSTLIMVVVVAVVSVIFFYVIVRFRRSRVGENTIPKqVEGNKFLEITWTV--IP 96
Cdd:TIGR01432  10 SGCSN--IEVLNPKGPVASSQSDLILYSIVFMLVIVFVVFVLFTIFLVKYRYRKDNGAYSPK-MHGNAILETIWTVipII 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071411983  97 ILLLIILVIPVVLYTLELADTSPMDKkgrkaeDALVVNVRANLYWWEFEYPDYGIITSQELIVPTDQRVYFNLKASDVKH 176
Cdd:TIGR01432  87 IVIALAIPTVKTIYDYEKAPKSTKEK------DPMVVYATSADWKWFFSYPDEHIETVNYLNIPKDRPVLFKLQSADTMT 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1071411983 177 SFWIPSVGGKLDTNTDNENKFFLTFDskrskEAGdMFFGKCAELCGPSHALMDFKVKTMSAKEFQGWTKEMK 248
Cdd:TIGR01432 161 SFWIPQLGGQKYAMTGMTMNWYLQAD-----EVG-TYRGRNANFNGEGFADQTFDVNAVSEKDFDKWVKETK 226
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 132-243 5.47e-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: 259981 [Multi-domain]  Cd Length: 108  Bit Score: 89.39  E-value: 5.47e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071411983 132 VVNVRANLYWWEFEYPDYGIITSQELIVPTDQRVYFNLKASDVKHSFWIPSVGGKLDTNTDNENkffltfdSKRSK--EA 209
Cdd:cd13914     2 EIEVEAYQWGWEFSYPEANVTTSEQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDAFPGQYN-------TIKTEatEE 74

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1071411983 210 GDmFFGKCAELCGPSHALMDFKVKTMSAKEFQGW 243
Cdd:cd13914    75 GE-YQLYCAEYCGAGHSQMLSTVTVVSQDEYQQW 107
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 130-235 1.11e-21

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: 88.47  E-value: 1.11e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071411983 130 ALVVNVRANLYWWEFEYPDYGI-------ITSQELIVPTDQRVYFNLKASDVKHSFWIPSVGGKLDTNTDNENKFFLTfd 202
Cdd:cd13919     1 ALVVEVTAQQWAWTFRYPGGDGklgtdddVTSPELHLPVGRPVLFNLRSKDVIHSFWVPEFRVKQDAVPGRTTRLWFT-- 78

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1071411983 203 skrSKEAGdMFFGKCAELCGPSHALMDFKVKTM 235
Cdd:cd13919    79 ---PTREG-EYEVRCAELCGLGHYRMRATVKVV 107
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 131-233 6.29e-21

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: 86.20  E-value: 6.29e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071411983 131 LVVNVRANLYWWEFEYPDygIITSQELIVPTDQRVYFNLKASDVKHSFWIPSVGGKLDTNTDNENKFFLTFDskrskEAG 210
Cdd:cd13842     1 LTVYVTGVQWSWTFIYPN--VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDAVPGYTSELWFVAD-----KPG 73

                          90       100
                  ....*....|....*....|...
gi 1071411983 211 DmFFGKCAELCGPSHALMDFKVK 233
Cdd:cd13842    74 T-YTIICAEYCGLGHSYMLGKVE 95
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 121-243 2.89e-19

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


Pssm-ID: 259985 [Multi-domain]  Cd Length: 139  Bit Score: 82.89  E-value: 2.89e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071411983 121 DKKGRKAEDALVVNVRANLYWWEFEYPDyGIITSQELIVPTDQRVYFNLKASDVKHSFWIPSVGGKLDTNTDNENKFFLT 200
Cdd:cd13918    23 DPPDEADEDALEVEVEGFQFGWQFEYPN-GVTTGNTLRVPADTPIALRVTSTDVFHTFGIPELRVKADAIPGEYTSTWFE 101

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1071411983 201 FDSKRSKEAgdmffgKCAELCGPSHALMDFKVKTMSAKEFQGW 243
Cdd:cd13918   102 ADEPGTYEA------KCYELCGSGHSLMTGDVIVMDEEEFEAW 138
Cyc7 COG3474
Cytochrome c2 [Energy production and conversion];
259-351 8.26e-17

Cytochrome c2 [Energy production and conversion];


Pssm-ID: 442697 [Multi-domain]  Cd Length: 101  Bit Score: 74.92  E-value: 8.26e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071411983 259 AKQGEELFKeKNCLSCHAVEPNDKraeaARTAPNLATFGERTK--VAGVK----------EANKENVKAWLKDPDSIKPG 326
Cdd:COG3474     3 AAAGEKLFN-RKCAACHSVDGGAG----NRVGPNLNGVVGRKAgsVEGFAysdalkasglVWDEETLDAWLADPKAFVPG 77

                          90       100
                  ....*....|....*....|....*.
gi 1071411983 327 NKMtgTYPKLSDSET-DALYEYLKGL 351
Cdd:COG3474    78 TKM--PFAGLKDPEDrADLIAYLKTL 101
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 130-233 1.49e-14

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: 68.81  E-value: 1.49e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071411983 130 ALVVNVRANLYWWEFEYPDyGIITSQELIVPTDQRVYFNLKASDVKHSFWIPSVGGKLDTNTDNENkfFLTFdskRSKEA 209
Cdd:cd13915     1 ALEIQVTGRQWMWEFTYPN-GKREINELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQDVVPGRYT--YLWF---EATKP 74

                          90       100
                  ....*....|....*....|....
gi 1071411983 210 GDmFFGKCAELCGPSHALMDFKVK 233
Cdd:cd13915    75 GE-YDLFCTEYCGTGHSGMIGKVR 97
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 141-243 2.45e-13

C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal oxidase in the respiratory chains of eukaryotes and most bacteria, is a multi-chain transmembrane protein located in the inner membrane of mitochondria and the cell membrane of prokaryotes. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. Only subunits I and II are essential for function. Subunits I, II, and III of mammalian CcO are encoded within the mitochondrial genome and the remaining 10 subunits are encoded within the nuclear genome. Subunit II contains a copper-copper binuclear site called CuA, which is believed to be involved in electron transfer from cytochrome c to the binuclear center (active site) in subunit I.


Pssm-ID: 259979 [Multi-domain]  Cd Length: 130  Bit Score: 66.05  E-value: 2.45e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071411983 141 W-WEFEYPDYGII---------------------TSQELIVPTDQRVYFNLKASDVKHSFWIPSVGGKLD-----TNTdn 193
Cdd:cd13912    12 WyWSYEYSDFNDLefdsymipeddlekgqlrlleVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKVDavpgrLNQ-- 89

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1071411983 194 enkffLTFDSKRSkeaGdMFFGKCAELCGPSHALMDFKVKTMSAKEFQGW 243
Cdd:cd13912    90 -----TSFFIERP---G-VYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 128-249 3.30e-13

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 68.27  E-value: 3.30e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071411983 128 EDALVVNVRANLYWWEFEYPDYG----------IITSQ-------------ELIVPTDQRVYFNLKASDVKHSFWIPSVG 184
Cdd:MTH00051   94 DPALTIKAIGHQWYWSYEYSDYGtdtiefdsymIPTSDlnsgdlrllevdnRLIVPIQTQVRVLVTAADVLHSFAVPSLS 173

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1071411983 185 GKLDT--NTDNENKFFLtfdskrsKEAGdMFFGKCAELCGPSHALMDFKVKTMSAKEFQGWTKEMKN 249
Cdd:MTH00051  174 VKIDAvpGRLNQTSFFI-------KRPG-VFYGQCSEICGANHSFMPIVIEGVSLDKYINWVATQSE 232
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
140-233 3.89e-13

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 65.51  E-value: 3.89e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071411983 140 YWWEFEYPDYGII---------------------TSQELIVPTDQRVYFNLKASDVKHSFWIPSVGGKLDTNTDNENKff 198
Cdd:pfam00116  10 WYWSYEYTDFGDLefdsymiptedleegqlrlleVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDAVPGRLNQ-- 87

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1071411983 199 LTFDSKRSkeagDMFFGKCAELCGPSHALMDFKVK 233
Cdd:pfam00116  88 TSFSIDRE----GVFYGQCSEICGINHSFMPIVIE 118
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 131-235 2.07e-12

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: 62.57  E-value: 2.07e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071411983 131 LVVNVRAnLYW-WEFEYPDYGIITSQELIVPTDQRVYFNLKASDVKHSFWIPSVGGKLDTNTDNENKFFLTFDskrskEA 209
Cdd:cd04212     1 LEIQVVS-LDWkWLFIYPEQGIATVNELVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYAMAGMQTQLHLIAD-----KP 74

                          90       100
                  ....*....|....*....|....*.
gi 1071411983 210 GDmFFGKCAELCGPSHALMDFKVKTM 235
Cdd:cd04212    75 GT-YQGLSANYSGEGFSDMKFKVLAV 99
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 128-249 2.59e-12

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 65.93  E-value: 2.59e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071411983 128 EDALVVNVRANLYWWEFEYPDYG----------IITSQ-------------ELIVPTDQRVYFNLKASDVKHSFWIPSVG 184
Cdd:MTH00023  101 SPALTIKAIGHQWYWSYEYSDYEgetlefdsymVPTSDlnsgdfrllevdnRLVVPINTHVRILVTGADVLHSFAVPSLG 180

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1071411983 185 GKLDT--NTDNENKFFLtfdskrsKEAGdMFFGKCAELCGPSHALMDFKVKTMSAKEFQGWTKEMKN 249
Cdd:MTH00023  181 LKIDAvpGRLNQTGFFI-------KRPG-VFYGQCSEICGANHSFMPIVIEAVSLDKYINWLLSLSN 239
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 131-247 1.57e-11

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 63.37  E-value: 1.57e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071411983 131 LVVNVRANLYWWEFEYPDYG-------IITSQEL--------------IVPTDQRVYFNLKASDVKHSFWIPSVGGKLDT 189
Cdd:MTH00185   95 LTIKAMGHQWYWSYEYTDYEqlefdsyMTPTQDLtpgqfrlletdhrmVVPMESPIRVLITAEDVLHSWTVPALGVKMDA 174

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1071411983 190 NTDNENKffLTFDSKRSkeagDMFFGKCAELCGPSHALMDFKVKTMSAKEFQGWTKEM 247
Cdd:MTH00185  175 VPGRLNQ--ATFIISRP----GLYYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLM 226
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 140-247 9.10e-11

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 61.27  E-value: 9.10e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071411983 140 YWWEFEYPDYG-------IITSQEL--------------IVPTDQRVYFNLKASDVKHSFWIPSVGGKLDTNTDNENKff 198
Cdd:MTH00129  104 WYWSYEYTDYEdlgfdsyMIPTQDLtpgqfrlleadhrmVVPVESPIRVLVSAEDVLHSWAVPALGVKMDAVPGRLNQ-- 181

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1071411983 199 LTFDSKRSkeagDMFFGKCAELCGPSHALMDFKVKTMSAKEFQGWTKEM 247
Cdd:MTH00129  182 TAFIASRP----GVFYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLM 226
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 120-243 1.37e-10

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 61.19  E-value: 1.37e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071411983 120 MDKKGRKAEdaLVVNVRANLYWWEFEYPDYG-----------------------IITSQELIVPTDQRVYFNLKASDVKH 176
Cdd:MTH00027  118 MDECGFSAN--ITIKVTGHQWYWSYSYEDYGekniefdsymiptadlefgdlrlLEVDNRLILPVDTNVRVLITAADVLH 195

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1071411983 177 SFWIPSVGGKLDT--NTDNENKFFLtfdskrsKEAGdMFFGKCAELCGPSHALMDFKVKTMSAKEFQGW 243
Cdd:MTH00027  196 SWTVPSLAVKMDAvpGRINETGFLI-------KRPG-IFYGQCSEICGANHSFMPIVVESVSLSKYIDW 256
Cytochrom_C pfam00034
Cytochrome c; The Pfam entry does not include all Prosite members. The cytochrome 556 and ...
 262-352 1.75e-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: 56.78  E-value: 1.75e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071411983 262 GEELFKeKNCLSCHAVEPNDkraeAARTAPNLATFGERTKVAGVKEA--NKENVKAWLKDPDSIKPGNKMTGtYPKLSDS 339
Cdd:pfam00034   3 GKKLFA-ANCAACHGVNGEG----AGAGGPDLAGLAARYPGDALGAIreNKHAIGGGGVDRAGGPPGTGMPA-FDGLTDE 76

                          90
                  ....*....|...
gi 1071411983 340 ETDALYEYLKGLK 352
Cdd:pfam00034  77 EIADLVAYLLSLS 89
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 140-247 3.01e-10

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 59.54  E-value: 3.01e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071411983 140 YWWEFEYPDYGIITSQELIVPT-------------DQRVYFNLK--------ASDVKHSFWIPSVGGKLDTNTDNENKff 198
Cdd:MTH00117  104 WYWSYEYTDYKDLSFDSYMIPTqdlpnghfrllevDHRMVIPMEspirilitAEDVLHSWAVPSLGVKTDAVPGRLNQ-- 181

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1071411983 199 LTFDSKRSkeagDMFFGKCAELCGPSHALMDFKVKTMSAKEFQGWTKEM 247
Cdd:MTH00117  182 TSFITTRP----GVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSLL 226
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 130-247 3.27e-10

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 59.35  E-value: 3.27e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071411983 130 ALVVNVRANLYWWEFEYPDYGIITSQELIVPT-------------DQRVYFNLK--------ASDVKHSFWIPSVGGKLD 188
Cdd:MTH00139   94 YLTFKAVGHQWYWSYEYSDFKNLSFDSYMIPTedlssgefrllevDNRLVLPYKsniralitAADVLHSWTVPSLGVKID 173

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1071411983 189 TNTDNENKffLTFDSKRSkeagDMFFGKCAELCGPSHALMDFKVKTMSAKEFQGWTKEM 247
Cdd:MTH00139  174 AVPGRLNQ--VGFFINRP----GVFYGQCSEICGANHSFMPIVVEAISPKFFLEWILEK 226
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 140-249 4.82e-10

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 59.02  E-value: 4.82e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071411983 140 YWWEFEYPDYG-------IITSQEL--------------IVPTDQRVYFNLKASDVKHSFWIPSVGGKLDTNTDNENKff 198
Cdd:MTH00076  104 WYWSYEYTDYEdlsfdsyMIPTQDLtpgqfrllevdnrmVVPMESPIRMLITAEDVLHSWAVPSLGIKTDAIPGRLNQ-- 181

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1071411983 199 LTFDSKRSkeagDMFFGKCAELCGPSHALMDFKVKTMSAKEFQGWTKEMKN 249
Cdd:MTH00076  182 TSFIASRP----GVYYGQCSEICGANHSFMPIVVEATPLNNFLNWSSSMLE 228
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 141-247 8.84e-10

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 58.30  E-value: 8.84e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071411983 141 W-WEFEYPDYG-------IITSQEL------IVPTDQRVY--FNLK------ASDVKHSFWIPSVGGKLDTNTDNENKFF 198
Cdd:MTH00154  104 WyWSYEYSDFKniefdsyMIPTNELenngfrLLDVDNRLVlpMNTQirilitAADVIHSWTVPSLGVKVDAVPGRLNQLN 183

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1071411983 199 LTfdSKRSkeaGdMFFGKCAELCGPSHALMDFKVKTMSAKEFQGWTKEM 247
Cdd:MTH00154  184 FL--INRP---G-LFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNM 226
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 140-247 1.24e-09

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 57.81  E-value: 1.24e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071411983 140 YWWEFEYPDYG-------IITSQEL--------------IVPTDQRVYFNLKASDVKHSFWIPSVGGKLDTNTDNENKff 198
Cdd:MTH00098  104 WYWSYEYTDYEdlsfdsyMIPTSDLkpgelrllevdnrvVLPMEMPIRMLISSEDVLHSWAVPSLGLKTDAIPGRLNQ-- 181

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1071411983 199 LTFDSKRSkeagDMFFGKCAELCGPSHALMDFKVKTMSAKEFQGWTKEM 247
Cdd:MTH00098  182 TTLMSTRP----GLYYGQCSEICGSNHSFMPIVLELVPLKYFEKWSASM 226
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 140-243 1.70e-09

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 57.30  E-value: 1.70e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071411983 140 YWWEFEYPDYGII---------------------TSQELIVPTDQRVYFNLKASDVKHSFWIPSVGGKLDT-----NTdn 193
Cdd:MTH00168  104 WYWSYEYTDYNDLefdsymvptqdlspgqfrlleVDNRLVLPMDSKIRVLVTSADVLHSWTLPSLGLKMDAvpgrlNQ-- 181

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1071411983 194 enkffLTFDSKRSkeagDMFFGKCAELCGPSHALMDFKVKTMSAKEFQGW 243
Cdd:MTH00168  182 -----LAFLSSRP----GSFYGQCSEICGANHSFMPIVVEFVPWETFENW 222
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 131-251 2.64e-09

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 56.94  E-value: 2.64e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071411983 131 LVVNVRANLYWWEFEYPDYGII---------------------TSQELIVPTDQRVYFNLKASDVKHSFWIPSVGGKLDT 189
Cdd:MTH00080   98 LTVKVTGHQWYWSYEFSDIPGLefdsymksldqlrlgeprlleVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDA 177

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1071411983 190 NTDNENKFFLTFDSKrskeagDMFFGKCAELCGPSHALMDFKVKTMSAKEFQGWtkeMKNYK 251
Cdd:MTH00080  178 MSGILSTLCYSFPMP------GVFYGQCSEICGANHSFMPIAVEVTLLDNFKEW---CKLLL 230
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 140-249 9.36e-09

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 55.09  E-value: 9.36e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071411983 140 YWWEFEYPDYGIITSQELIVPT-------------DQRVYFNLK--------ASDVKHSFWIPSVGGKLDTNTDNENKff 198
Cdd:MTH00038  104 WYWSYEYTDYNDLEFDSYMVPTsdlstglprllevDNRLVLPYQtpirvlvsSADVLHSWAVPSLGVKMDAVPGRLNQ-- 181

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1071411983 199 LTFDSKRSkeagDMFFGKCAELCGPSHALMDFKVKTMSAKEFQGWTKEMKN 249
Cdd:MTH00038  182 TTFFISRT----GLFYGQCSEICGANHSFMPIVIESVPFNTFENWVSNFLE 228
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 140-244 9.94e-09

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 55.25  E-value: 9.94e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071411983 140 YWWEFEYPD--------YGIITSQ-------------ELIVPTDQRVYFNLKASDVKHSFWIPSVGGKLDTNTDNENKFF 198
Cdd:MTH00008  104 WYWSYEYSDfsnlefdsYMLPTSDlspgqfrllevdnRAVLPMQTEIRVLVTAADVIHSWTVPSLGVKVDAVPGRLNQIG 183

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1071411983 199 LTFDSKrskeagDMFFGKCAELCGPSHALMDFKVKTMSAKEFQGWT 244
Cdd:MTH00008  184 FTITRP------GVFYGQCSEICGANHSFMPIVLEAVDTKSFMKWV 223
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 140-228 1.46e-07

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 51.11  E-value: 1.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071411983 140 YWWEFEYPDYGIITSqeliVPTDQ--------RVYFNL------KASDVKHSFWIPSVGGKLDTNTDNENKFFLTFDSKR 205
Cdd:MTH00047   91 WYWSYEYSFGGSYDS----FMTDDifgvdkplRLVYGVpyhllvTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCPDRHG 166

                          90       100
                  ....*....|....*....|...
gi 1071411983 206 SkeagdmFFGKCAELCGPSHALM 228
Cdd:MTH00047  167 V------FVGYCSELCGVGHSYM 183
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 157-251 2.24e-07

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 49.82  E-value: 2.24e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071411983 157 LIVPTDQRVYFNLKASDVKHSFWIPSVGGKLDT---NTDNENKFFLtfdskrsKEAgdMFFGKCAELCGPSHALMDFKVK 233
Cdd:PTZ00047   75 LTLPTRTHIRFLITATDVIHSWSVPSLGIKADAipgRLHKINTFIL-------REG--VFYGQCSEMCGTLHGFMPIVVE 145

                          90
                  ....*....|....*...
gi 1071411983 234 TMSAKEFQGWTKemKNYK 251
Cdd:PTZ00047  146 AVSPEAYAAHAK--KYYK 161
PRK10525 PRK10525
cytochrome o ubiquinol oxidase subunit II; Provisional
 142-263 2.89e-07

cytochrome o ubiquinol oxidase subunit II; Provisional


Pssm-ID: 182518 [Multi-domain]  Cd Length: 315  Bit Score: 51.34  E-value: 2.89e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071411983 142 WEFEYPDYGIITSQELIVPTDQRVYFNLKASDVKHSFWIPSVGGKLDTNTDNENKFFLTFDskrskEAGDmFFGKCAELC 221
Cdd:PRK10525  138 WFFIYPEQGIATVNEIAFPANVPVYFKVTSNSVMNSFFIPRLGSQIYAMAGMQTRLHLIAN-----EPGT-YDGISASYS 211

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1071411983 222 GPSHALMDFK-VKTMSAKEFQGWTKEMKNYKST-----AESDLAKQGE 263
Cdd:PRK10525  212 GPGFSGMKFKaIATPDRAEFDQWVAKAKQSPNTmndmaAFEKLAAPSE 259
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 141-247 4.11e-07

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 50.32  E-value: 4.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071411983 141 W-WEFEYPDYGIITSQELIVPT-------------DQR--VYFNLK------ASDVKHSFWIPSVGGKLDT-----NTdn 193
Cdd:MTH00140  104 WyWSYEYSDFSVIEFDSYMVPEnelelgdfrllevDNRlvLPYSVDtrvlvtSADVIHSWTVPSLGVKVDAipgrlNQ-- 181

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1071411983 194 enkffLTFDSKRSkeagDMFFGKCAELCGPSHALMDFKVKTMSAKEFQGWTKEM 247
Cdd:MTH00140  182 -----LSFEPKRP----GVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWLELM 226
CytC552 COG4654
Cytochrome c551/c552 [Energy production and conversion];
256-352 1.25e-06

Cytochrome c551/c552 [Energy production and conversion];


Pssm-ID: 443692 [Multi-domain]  Cd Length: 88  Bit Score: 46.05  E-value: 1.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071411983 256 SDLAKQGEELFKEKNCLSCHAVepnDKRaeaaRTAPNLatfgerTKVAGVKEANKENVK---AWLKDPDSIKPGNKMTGT 332
Cdd:COG4654     1 AADAAAGKALAKKSGCLACHAV---DKK----LVGPSY------KDVAKKYKGKADAVAklaKKIKKGGSGVWGDVPMPP 67

                          90       100
                  ....*....|....*....|
gi 1071411983 333 YPKLSDSETDALYEYLKGLK 352
Cdd:COG4654    68 HPQLSDAEAKALVKWILSLK 87
CccA COG2010
Cytochrome c, mono- and diheme variants [Energy production and conversion];
253-354 4.95e-05

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


Pssm-ID: 441613 [Multi-domain]  Cd Length: 169  Bit Score: 43.40  E-value: 4.95e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071411983 253 TAESDLAKQGEELFkEKNCLSCHAVEpndkRAEAARTAPNLATfgertkvAGVKEANKENVKAWLKDPdsiKPGNKMTGT 332
Cdd:COG2010    83 AADAEALARGKALY-EQNCAACHGAD----GKGGLGAAPNLTD-------DALYGGDPEALVETILNG---RPGGAMPAF 147

                          90       100
                  ....*....|....*....|..
gi 1071411983 333 YPKLSDSETDALYEYLKGLKAE 354
Cdd:COG2010   148 GGQLSDEEIAALAAYLRSLSGN 169
ccoP TIGR00782
cytochrome c oxidase, cbb3-type, subunit III; This model describes a di-heme subunit of ...
 251-351 5.26e-04

cytochrome c oxidase, cbb3-type, subunit III; This model describes a di-heme subunit of approximately 26 kDa of the cbb3 type copper and heme-containing cytochrome oxidase. [Energy metabolism, Electron transport]


Pssm-ID: 129864 [Multi-domain]  Cd Length: 285  Bit Score: 41.42  E-value: 5.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071411983 251 KSTAESDLAKQGEELFkEKNCLSCHAvepNDKRAEAARTAPNLAtfgertkvagvkeankENVKAWLKDPDSI------K 324
Cdd:TIGR00782 195 GKPKDEALAAKGQELF-ADNCTTCHG---EDGKGLQELGAPNLT----------------DDVWLYGGDLKTItttitnG 254

                          90       100
                  ....*....|....*....|....*..
gi 1071411983 325 PGNKMTGTYPKLSDSETDALYEYLKGL 351
Cdd:TIGR00782 255 RGGVMPAWGPRLSEAQIKALAAYVHSL 281
thiosulf_SoxX TIGR04485
sulfur oxidation c-type cytochrome SoxX; Members of this family are SoxX, a c-type cytochrome ...
 270-351 8.07e-04

sulfur oxidation c-type cytochrome SoxX; Members of this family are SoxX, a c-type cytochrome with a CxxCH motif, part of a heterodimer with SoxA. SoxXA, SoxYZ, and SoxB contribute to thiosulfate oxidation to sulfate.


Pssm-ID: 275278 [Multi-domain]  Cd Length: 78  Bit Score: 37.57  E-value: 8.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071411983 270 NCLSCHAVEPNdkrAEAART-APNLATFGER--------TKVAGVKEANkenvkawlkdPDSIKPGNKMTGtypKLSDSE 340
Cdd:TIGR04485   4 NCLACHQIPGS---EVFPGNiGPSLTGYGARypdeaylrAKIADAKAVN----------PCTVMPRFGKNG---ILTEQE 67

                          90
                  ....*....|.
gi 1071411983 341 TDALYEYLKGL 351
Cdd:TIGR04485  68 IEDVVAYLLTL 78
CytC553 COG2863
Cytochrome c553 [Energy production and conversion];
252-353 1.41e-03

Cytochrome c553 [Energy production and conversion];


Pssm-ID: 442110 [Multi-domain]  Cd Length: 98  Bit Score: 37.79  E-value: 1.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071411983 252 STAESDLAKQGEElfKEKNCLSCHAVepnDKRAEAARTAPNLAtfGErtkvagvkeaNKENVKAWLKDP-DSIKPGNKMT 330
Cdd:COG2863     8 APAAAGDAARGKA--YAAACAACHGA---DGEGNPGGGAPRLA--GQ----------HAEYLVAQLKAFrSGARKNGVMP 70

                          90       100
                  ....*....|....*....|...
gi 1071411983 331 GTYPKLSDSETDALYEYLKGLKA 353
Cdd:COG2863    71 AIAKGLSDEDIKALAAYIASLKA 93
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 132-232 8.67e-03

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: 35.05  E-value: 8.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1071411983 132 VVNVRANLYWWEfeypdygIITSQeliVPTDQRVYFNLKASDVKHSFWIPSVGGKLDTNT----DNENKFFLTFDskrsk 207
Cdd:cd13916     2 VVAVTGHQWYWE-------LSRTE---IPAGKPVEFRVTSADVNHGFGIYDPDMRLLAQTqampGYTNVLRYTFD----- 66

                          90       100
                  ....*....|....*....|....*..
gi 1071411983 208 EAGdMFFGKCAELCGPSHALM--DFKV 232
Cdd:cd13916    67 KPG-TYTILCLEYCGLAHHVMmaEFTV 92
 
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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