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Conserved domains on  [gi|504292607|ref|WP_014479709|]
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MULTISPECIES: cytochrome c oxidase subunit II [Bacillus]

Protein Classification

CuRO_CcO_Caa3_II and CYT1 domain-containing protein( domain architecture ID 11446895)

CuRO_CcO_Caa3_II and CYT1 domain-containing protein

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 2.61e-56

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


:

Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 183.11  E-value: 2.61e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504292607  26 LSTLKPAGEVADKQFDLTVLSTLIMVVVVAVVSVIFFYVIVRFRRSRvgENTIPKQVEGNKFLEITWTvipillliilvi 105
Cdd:COG1622   19 LSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLLLYFAIRYRRRK--GDADPAQFHHNTKLEIVWTvipiii----vi 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504292607 106 pvvlYTLELadTSPMDkkgRKAEDALVVNVRANLYWWEFEYPDYDIITSQELIVPTDQRVYFNLKASDVKHSFWIPSVGG 185
Cdd:COG1622   93 vlavPTLRV--LHALD---DAPEDPLTVEVTGYQWKWLFRYPDQGIATVNELVLPVGRPVRFLLTSADVIHSFWVPALGG 167

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504292607 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 504292607 259 AKQGEELFKeKNCLSCHAVEPNDKraeaARTAPNLATFGERTK--VAGVK----------EANKENVKAWLKDPDSIKPG 326
Cdd:COG3474    3 AAAGEKLFN-RKCAACHSVDGGAG----NRVGPNLNGVVGRKAgsVEGFAysdalkasglVWDEETLDAWLADPKAFVPG 77

                         90       100
                 ....*....|....*....|....*.
gi 504292607 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 2.61e-56

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 183.11  E-value: 2.61e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504292607  26 LSTLKPAGEVADKQFDLTVLSTLIMVVVVAVVSVIFFYVIVRFRRSRvgENTIPKQVEGNKFLEITWTvipillliilvi 105
Cdd:COG1622   19 LSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLLLYFAIRYRRRK--GDADPAQFHHNTKLEIVWTvipiii----vi 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504292607 106 pvvlYTLELadTSPMDkkgRKAEDALVVNVRANLYWWEFEYPDYDIITSQELIVPTDQRVYFNLKASDVKHSFWIPSVGG 185
Cdd:COG1622   93 vlavPTLRV--LHALD---DAPEDPLTVEVTGYQWKWLFRYPDQGIATVNELVLPVGRPVRFLLTSADVIHSFWVPALGG 167

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504292607 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 3.76e-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: 160.48  E-value: 3.76e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504292607 130 ALVVNVRANLYWWEFEYPDYD---IITSQELIVPTDQRVYFNLKASDVKHSFWIPSVGGKLDTNTDNENKFFLTFDskrs 206
Cdd:cd04213    1 ALTIEVTGHQWWWEFRYPDEPgrgIVTANELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMDMIPGRTNRLWLQAD---- 76

                         90       100
                 ....*....|....*....|....*....
gi 504292607 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 5.53e-42

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: 145.22  E-value: 5.53e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504292607   31 PAGEVADKQFDLTVLSTLIMVVVVAVVSVIFFYVIVRFRRSrvGENTIPKQVEGNKFLEITWTVIPILLLIILVIPVVLY 110
Cdd:TIGR02866   1 PGGEIAQQIAFLFLFVLAVSTLISLLVAALLAYVVWKFRRK--GDEEKPSQIHGNRRLEYVWTVIPLIIVVGLFAATAKG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504292607  111 TLELadTSPMDKkgrkaeDALVVNVRANLYWWEFEYPDYDIITSQELIVPTDQRVYFNLKASDVKHSFWIPSVGGKLDTN 190
Cdd:TIGR02866  79 LLYL--ERPIPK------DALKVKVTGYQWWWDFEYPESGFTTVNELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAI 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 504292607  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 504292607 259 AKQGEELFKeKNCLSCHAVEPNDKraeaARTAPNLATFGERTK--VAGVK----------EANKENVKAWLKDPDSIKPG 326
Cdd:COG3474    3 AAAGEKLFN-RKCAACHSVDGGAG----NRVGPNLNGVVGRKAgsVEGFAysdalkasglVWDEETLDAWLADPKAFVPG 77

                         90       100
                 ....*....|....*....|....*.
gi 504292607 327 NKMtgTYPKLSDSET-DALYEYLKGL 351
Cdd:COG3474   78 TKM--PFAGLKDPEDrADLIAYLKTL 101
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 128-249 1.34e-12

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 66.70  E-value: 1.34e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504292607 128 EDALVVNVRANLYWWEFEYPDYD----------IITSQ-------------ELIVPTDQRVYFNLKASDVKHSFWIPSVG 184
Cdd:MTH00023 101 SPALTIKAIGHQWYWSYEYSDYEgetlefdsymVPTSDlnsgdfrllevdnRLVVPINTHVRILVTGADVLHSFAVPSLG 180

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504292607 185 GKLDT--NTDNENKFFLtfdskrsKEAGdMFFGKCAELCGPSHALMDFKVKTMSAKEFQGWTKEMKN 249
Cdd:MTH00023 181 LKIDAvpGRLNQTGFFI-------KRPG-VFYGQCSEICGANHSFMPIVIEAVSLDKYINWLLSLSN 239
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
140-233 1.64e-12

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 63.58  E-value: 1.64e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504292607  140 YWWEFEYPDYDII---------------------TSQELIVPTDQRVYFNLKASDVKHSFWIPSVGGKLDTNTDNENKff 198
Cdd:pfam00116  10 WYWSYEYTDFGDLefdsymiptedleegqlrlleVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDAVPGRLNQ-- 87

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 504292607  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 504292607  262 GEELFKeKNCLSCHAVEPNDkraeAARTAPNLATFGERTKVAGVKEA--NKENVKAWLKDPDSIKPGNKMTGtYPKLSDS 339
Cdd:pfam00034   3 GKKLFA-ANCAACHGVNGEG----AGAGGPDLAGLAARYPGDALGAIreNKHAIGGGGVDRAGGPPGTGMPA-FDGLTDE 76

                          90
                  ....*....|...
gi 504292607  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 504292607  251 KSTAESDLAKQGEELFkEKNCLSCHAvepNDKRAEAARTAPNLAtfgertkvagvkeankENVKAWLKDPDSI------K 324
Cdd:TIGR00782 195 GKPKDEALAAKGQELF-ADNCTTCHG---EDGKGLQELGAPNLT----------------DDVWLYGGDLKTItttitnG 254

                          90       100
                  ....*....|....*....|....*..
gi 504292607  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 2.61e-56

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 183.11  E-value: 2.61e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504292607  26 LSTLKPAGEVADKQFDLTVLSTLIMVVVVAVVSVIFFYVIVRFRRSRvgENTIPKQVEGNKFLEITWTvipillliilvi 105
Cdd:COG1622   19 LSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLLLYFAIRYRRRK--GDADPAQFHHNTKLEIVWTvipiii----vi 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504292607 106 pvvlYTLELadTSPMDkkgRKAEDALVVNVRANLYWWEFEYPDYDIITSQELIVPTDQRVYFNLKASDVKHSFWIPSVGG 185
Cdd:COG1622   93 vlavPTLRV--LHALD---DAPEDPLTVEVTGYQWKWLFRYPDQGIATVNELVLPVGRPVRFLLTSADVIHSFWVPALGG 167

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504292607 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 3.76e-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: 160.48  E-value: 3.76e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504292607 130 ALVVNVRANLYWWEFEYPDYD---IITSQELIVPTDQRVYFNLKASDVKHSFWIPSVGGKLDTNTDNENKFFLTFDskrs 206
Cdd:cd04213    1 ALTIEVTGHQWWWEFRYPDEPgrgIVTANELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMDMIPGRTNRLWLQAD---- 76

                         90       100
                 ....*....|....*....|....*....
gi 504292607 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 5.53e-42

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: 145.22  E-value: 5.53e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504292607   31 PAGEVADKQFDLTVLSTLIMVVVVAVVSVIFFYVIVRFRRSrvGENTIPKQVEGNKFLEITWTVIPILLLIILVIPVVLY 110
Cdd:TIGR02866   1 PGGEIAQQIAFLFLFVLAVSTLISLLVAALLAYVVWKFRRK--GDEEKPSQIHGNRRLEYVWTVIPLIIVVGLFAATAKG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504292607  111 TLELadTSPMDKkgrkaeDALVVNVRANLYWWEFEYPDYDIITSQELIVPTDQRVYFNLKASDVKHSFWIPSVGGKLDTN 190
Cdd:TIGR02866  79 LLYL--ERPIPK------DALKVKVTGYQWWWDFEYPESGFTTVNELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAI 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 504292607  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 1.22e-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: 102.68  E-value: 1.22e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504292607   19 SGCGKpfLSTLKPAGEVADKQFDLTVLSTLIMVVVVAVVSVIFFYVIVRFRRSRVGENTIPKqVEGNKFLEITWTV--IP 96
Cdd:TIGR01432  10 SGCSN--IEVLNPKGPVASSQSDLILYSIVFMLVIVFVVFVLFTIFLVKYRYRKDNGAYSPK-MHGNAILETIWTVipII 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504292607   97 ILLLIILVIPVVLYTLELADTSPMDKkgrkaeDALVVNVRANLYWWEFEYPDYDIITSQELIVPTDQRVYFNLKASDVKH 176
Cdd:TIGR01432  87 IVIALAIPTVKTIYDYEKAPKSTKEK------DPMVVYATSADWKWFFSYPDEHIETVNYLNIPKDRPVLFKLQSADTMT 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504292607  177 SFWIPSVGGKLDTNTDNENKFFLTFDskrskEAGdMFFGKCAELCGPSHALMDFKVKTMSAKEFQGWTKEMK 248
Cdd:TIGR01432 161 SFWIPQLGGQKYAMTGMTMNWYLQAD-----EVG-TYRGRNANFNGEGFADQTFDVNAVSEKDFDKWVKETK 226
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 130-235 6.63e-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: 259986 [Multi-domain]  Cd Length: 107  Bit Score: 89.24  E-value: 6.63e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504292607 130 ALVVNVRANLYWWEFEYPDYDI-------ITSQELIVPTDQRVYFNLKASDVKHSFWIPSVGGKLDTNTDNENKFFLTfd 202
Cdd:cd13919    1 ALVVEVTAQQWAWTFRYPGGDGklgtdddVTSPELHLPVGRPVLFNLRSKDVIHSFWVPEFRVKQDAVPGRTTRLWFT-- 78

                         90       100       110
                 ....*....|....*....|....*....|...
gi 504292607 203 skrSKEAGdMFFGKCAELCGPSHALMDFKVKTM 235
Cdd:cd13919   79 ---PTREG-EYEVRCAELCGLGHYRMRATVKVV 107
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 132-243 2.16e-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: 259981 [Multi-domain]  Cd Length: 108  Bit Score: 87.85  E-value: 2.16e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504292607 132 VVNVRANLYWWEFEYPDYDIITSQELIVPTDQRVYFNLKASDVKHSFWIPSVGGKLDTNTDNENkffltfdSKRSK--EA 209
Cdd:cd13914    2 EIEVEAYQWGWEFSYPEANVTTSEQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDAFPGQYN-------TIKTEatEE 74

                         90       100       110
                 ....*....|....*....|....*....|....
gi 504292607 210 GDmFFGKCAELCGPSHALMDFKVKTMSAKEFQGW 243
Cdd:cd13914   75 GE-YQLYCAEYCGAGHSQMLSTVTVVSQDEYQQW 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 504292607 131 LVVNVRANLYWWEFEYPDydIITSQELIVPTDQRVYFNLKASDVKHSFWIPSVGGKLDTNTDNENKFFLTFDskrskEAG 210
Cdd:cd13842    1 LTVYVTGVQWSWTFIYPN--VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDAVPGYTSELWFVAD-----KPG 73

                         90       100
                 ....*....|....*....|...
gi 504292607 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 2.36e-18

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: 80.58  E-value: 2.36e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504292607 121 DKKGRKAEDALVVNVRANLYWWEFEYPDyDIITSQELIVPTDQRVYFNLKASDVKHSFWIPSVGGKLDTNTDNENKFFLT 200
Cdd:cd13918   23 DPPDEADEDALEVEVEGFQFGWQFEYPN-GVTTGNTLRVPADTPIALRVTSTDVFHTFGIPELRVKADAIPGEYTSTWFE 101

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 504292607 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 504292607 259 AKQGEELFKeKNCLSCHAVEPNDKraeaARTAPNLATFGERTK--VAGVK----------EANKENVKAWLKDPDSIKPG 326
Cdd:COG3474    3 AAAGEKLFN-RKCAACHSVDGGAG----NRVGPNLNGVVGRKAgsVEGFAysdalkasglVWDEETLDAWLADPKAFVPG 77

                         90       100
                 ....*....|....*....|....*.
gi 504292607 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 1.19e-13

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


Pssm-ID: 259982 [Multi-domain]  Cd Length: 98  Bit Score: 66.11  E-value: 1.19e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504292607 130 ALVVNVRANLYWWEFEYPDYDIITSqELIVPTDQRVYFNLKASDVKHSFWIPSVGGKLDTNTDNENkfFLTFdskRSKEA 209
Cdd:cd13915    1 ALEIQVTGRQWMWEFTYPNGKREIN-ELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQDVVPGRYT--YLWF---EATKP 74

                         90       100
                 ....*....|....*....|....
gi 504292607 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 3.64e-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: 65.67  E-value: 3.64e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504292607 141 W-WEFEYPDYDII---------------------TSQELIVPTDQRVYFNLKASDVKHSFWIPSVGGKLD-----TNTdn 193
Cdd:cd13912   12 WyWSYEYSDFNDLefdsymipeddlekgqlrlleVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKVDavpgrLNQ-- 89

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 504292607 194 enkffLTFDSKRSkeaGdMFFGKCAELCGPSHALMDFKVKTMSAKEFQGW 243
Cdd:cd13912   90 -----TSFFIERP---G-VYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 128-249 1.34e-12

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 66.70  E-value: 1.34e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504292607 128 EDALVVNVRANLYWWEFEYPDYD----------IITSQ-------------ELIVPTDQRVYFNLKASDVKHSFWIPSVG 184
Cdd:MTH00023 101 SPALTIKAIGHQWYWSYEYSDYEgetlefdsymVPTSDlnsgdfrllevdnRLVVPINTHVRILVTGADVLHSFAVPSLG 180

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504292607 185 GKLDT--NTDNENKFFLtfdskrsKEAGdMFFGKCAELCGPSHALMDFKVKTMSAKEFQGWTKEMKN 249
Cdd:MTH00023 181 LKIDAvpGRLNQTGFFI-------KRPG-VFYGQCSEICGANHSFMPIVIEAVSLDKYINWLLSLSN 239
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
140-233 1.64e-12

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 63.58  E-value: 1.64e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504292607  140 YWWEFEYPDYDII---------------------TSQELIVPTDQRVYFNLKASDVKHSFWIPSVGGKLDTNTDNENKff 198
Cdd:pfam00116  10 WYWSYEYTDFGDLefdsymiptedleegqlrlleVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDAVPGRLNQ-- 87

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 504292607  199 LTFDSKRSkeagDMFFGKCAELCGPSHALMDFKVK 233
Cdd:pfam00116  88 TSFSIDRE----GVFYGQCSEICGINHSFMPIVIE 118
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 128-249 2.23e-12

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 65.96  E-value: 2.23e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504292607 128 EDALVVNVRANLYWWEFEYPDY--DII--------TSQ-------------ELIVPTDQRVYFNLKASDVKHSFWIPSVG 184
Cdd:MTH00051  94 DPALTIKAIGHQWYWSYEYSDYgtDTIefdsymipTSDlnsgdlrllevdnRLIVPIQTQVRVLVTAADVLHSFAVPSLS 173

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504292607 185 GKLDT--NTDNENKFFLtfdskrsKEAGdMFFGKCAELCGPSHALMDFKVKTMSAKEFQGWTKEMKN 249
Cdd:MTH00051 174 VKIDAvpGRLNQTSFFI-------KRPG-VFYGQCSEICGANHSFMPIVIEGVSLDKYINWVATQSE 232
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 131-235 4.79e-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: 61.80  E-value: 4.79e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504292607 131 LVVNVRAnLYW-WEFEYPDYDIITSQELIVPTDQRVYFNLKASDVKHSFWIPSVGGKLDTNTDNENKFFLTFDskrskEA 209
Cdd:cd04212    1 LEIQVVS-LDWkWLFIYPEQGIATVNELVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYAMAGMQTQLHLIAD-----KP 74

                         90       100
                 ....*....|....*....|....*.
gi 504292607 210 GDmFFGKCAELCGPSHALMDFKVKTM 235
Cdd:cd04212   75 GT-YQGLSANYSGEGFSDMKFKVLAV 99
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 131-247 5.89e-12

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 64.52  E-value: 5.89e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504292607 131 LVVNVRANLYWWEFEYPDYD-------IITSQEL--------------IVPTDQRVYFNLKASDVKHSFWIPSVGGKLDT 189
Cdd:MTH00185  95 LTIKAMGHQWYWSYEYTDYEqlefdsyMTPTQDLtpgqfrlletdhrmVVPMESPIRVLITAEDVLHSWTVPALGVKMDA 174

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 504292607 190 NTDNENKffLTFDSKRSkeagDMFFGKCAELCGPSHALMDFKVKTMSAKEFQGWTKEM 247
Cdd:MTH00185 175 VPGRLNQ--ATFIISRP----GLYYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLM 226
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 140-247 2.30e-11

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 62.81  E-value: 2.30e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504292607 140 YWWEFEYPDYD-------IITSQEL--------------IVPTDQRVYFNLKASDVKHSFWIPSVGGKLDTNTDNENKff 198
Cdd:MTH00129 104 WYWSYEYTDYEdlgfdsyMIPTQDLtpgqfrlleadhrmVVPVESPIRVLVSAEDVLHSWAVPALGVKMDAVPGRLNQ-- 181

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 504292607 199 LTFDSKRSkeagDMFFGKCAELCGPSHALMDFKVKTMSAKEFQGWTKEM 247
Cdd:MTH00129 182 TAFIASRP----GVFYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLM 226
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 130-247 7.14e-11

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 61.27  E-value: 7.14e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504292607 130 ALVVNVRANLYWWEFEYPDYDIITSQELIVPT-------------DQRVYFNLK--------ASDVKHSFWIPSVGGKLD 188
Cdd:MTH00139  94 YLTFKAVGHQWYWSYEYSDFKNLSFDSYMIPTedlssgefrllevDNRLVLPYKsniralitAADVLHSWTVPSLGVKID 173

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 504292607 189 TNTDNENKffLTFDSKRSkeagDMFFGKCAELCGPSHALMDFKVKTMSAKEFQGWTKEM 247
Cdd:MTH00139 174 AVPGRLNQ--VGFFINRP----GVFYGQCSEICGANHSFMPIVVEAISPKFFLEWILEK 226
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 140-247 1.05e-10

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 60.70  E-value: 1.05e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504292607 140 YWWEFEYPDYDIITSQELIVPT-------------DQRVYFNLK--------ASDVKHSFWIPSVGGKLDTNTDNENKff 198
Cdd:MTH00117 104 WYWSYEYTDYKDLSFDSYMIPTqdlpnghfrllevDHRMVIPMEspirilitAEDVLHSWAVPSLGVKTDAVPGRLNQ-- 181

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 504292607 199 LTFDSKRSkeagDMFFGKCAELCGPSHALMDFKVKTMSAKEFQGWTKEM 247
Cdd:MTH00117 182 TSFITTRP----GVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSLL 226
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 140-249 1.66e-10

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 60.18  E-value: 1.66e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504292607 140 YWWEFEYPDYD-------IITSQEL--------------IVPTDQRVYFNLKASDVKHSFWIPSVGGKLDTNTDNENKff 198
Cdd:MTH00076 104 WYWSYEYTDYEdlsfdsyMIPTQDLtpgqfrllevdnrmVVPMESPIRMLITAEDVLHSWAVPSLGIKTDAIPGRLNQ-- 181

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 504292607 199 LTFDSKRSkeagDMFFGKCAELCGPSHALMDFKVKTMSAKEFQGWTKEMKN 249
Cdd:MTH00076 182 TSFIASRP----GVYYGQCSEICGANHSFMPIVVEATPLNNFLNWSSSMLE 228
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 504292607  262 GEELFKeKNCLSCHAVEPNDkraeAARTAPNLATFGERTKVAGVKEA--NKENVKAWLKDPDSIKPGNKMTGtYPKLSDS 339
Cdd:pfam00034   3 GKKLFA-ANCAACHGVNGEG----AGAGGPDLAGLAARYPGDALGAIreNKHAIGGGGVDRAGGPPGTGMPA-FDGLTDE 76

                          90
                  ....*....|...
gi 504292607  340 ETDALYEYLKGLK 352
Cdd:pfam00034  77 EIADLVAYLLSLS 89
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 141-247 7.97e-10

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 58.30  E-value: 7.97e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504292607 141 W-WEFEYPD-----YD--IITSQEL------IVPTDQRVY--FNLK------ASDVKHSFWIPSVGGKLDTNTDNENKFF 198
Cdd:MTH00154 104 WyWSYEYSDfknieFDsyMIPTNELenngfrLLDVDNRLVlpMNTQirilitAADVIHSWTVPSLGVKVDAVPGRLNQLN 183

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 504292607 199 LTfdSKRSkeaGdMFFGKCAELCGPSHALMDFKVKTMSAKEFQGWTKEM 247
Cdd:MTH00154 184 FL--INRP---G-LFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNM 226
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 140-247 9.08e-10

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 58.19  E-value: 9.08e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504292607 140 YWWEFEYPDYD-------IITSQEL--------------IVPTDQRVYFNLKASDVKHSFWIPSVGGKLDTNTDNENKff 198
Cdd:MTH00098 104 WYWSYEYTDYEdlsfdsyMIPTSDLkpgelrllevdnrvVLPMEMPIRMLISSEDVLHSWAVPSLGLKTDAIPGRLNQ-- 181

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 504292607 199 LTFDSKRSkeagDMFFGKCAELCGPSHALMDFKVKTMSAKEFQGWTKEM 247
Cdd:MTH00098 182 TTLMSTRP----GLYYGQCSEICGSNHSFMPIVLELVPLKYFEKWSASM 226
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 120-243 1.34e-09

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 58.11  E-value: 1.34e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504292607 120 MDKKGRKAEdaLVVNVRANLYWWEFEYPDYD-----------------------IITSQELIVPTDQRVYFNLKASDVKH 176
Cdd:MTH00027 118 MDECGFSAN--ITIKVTGHQWYWSYSYEDYGekniefdsymiptadlefgdlrlLEVDNRLILPVDTNVRVLITAADVLH 195

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504292607 177 SFWIPSVGGKLDT--NTDNENKFFLtfdskrsKEAGdMFFGKCAELCGPSHALMDFKVKTMSAKEFQGW 243
Cdd:MTH00027 196 SWTVPSLAVKMDAvpGRINETGFLI-------KRPG-IFYGQCSEICGANHSFMPIVVESVSLSKYIDW 256
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 140-249 2.47e-09

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 57.02  E-value: 2.47e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504292607 140 YWWEFEYPDY-------------DIITSQ--------ELIVPTDQRVYFNLKASDVKHSFWIPSVGGKLDTNTDNENKff 198
Cdd:MTH00038 104 WYWSYEYTDYndlefdsymvptsDLSTGLprllevdnRLVLPYQTPIRVLVSSADVLHSWAVPSLGVKMDAVPGRLNQ-- 181

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 504292607 199 LTFDSKRSkeagDMFFGKCAELCGPSHALMDFKVKTMSAKEFQGWTKEMKN 249
Cdd:MTH00038 182 TTFFISRT----GLFYGQCSEICGANHSFMPIVIESVPFNTFENWVSNFLE 228
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 140-244 4.74e-09

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 56.02  E-value: 4.74e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504292607 140 YWWEFEYPDY-------------DIITSQ--------ELIVPTDQRVYFNLKASDVKHSFWIPSVGGKLDTNTDNENKFF 198
Cdd:MTH00008 104 WYWSYEYSDFsnlefdsymlptsDLSPGQfrllevdnRAVLPMQTEIRVLVTAADVIHSWTVPSLGVKVDAVPGRLNQIG 183

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 504292607 199 LTFDSKrskeagDMFFGKCAELCGPSHALMDFKVKTMSAKEFQGWT 244
Cdd:MTH00008 184 FTITRP------GVFYGQCSEICGANHSFMPIVLEAVDTKSFMKWV 223
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 140-243 5.09e-09

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 55.76  E-value: 5.09e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504292607 140 YWWEFEYPDY-------------DIITSQ--------ELIVPTDQRVYFNLKASDVKHSFWIPSVGGKLDT-----NTdn 193
Cdd:MTH00168 104 WYWSYEYTDYndlefdsymvptqDLSPGQfrllevdnRLVLPMDSKIRVLVTSADVLHSWTLPSLGLKMDAvpgrlNQ-- 181

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 504292607 194 enkffLTFDSKRSkeagDMFFGKCAELCGPSHALMDFKVKTMSAKEFQGW 243
Cdd:MTH00168 182 -----LAFLSSRP----GSFYGQCSEICGANHSFMPIVVEFVPWETFENW 222
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 131-251 6.56e-09

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 55.79  E-value: 6.56e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504292607 131 LVVNVRANLYWWEFEYPDYDII---------------------TSQELIVPTDQRVYFNLKASDVKHSFWIPSVGGKLDT 189
Cdd:MTH00080  98 LTVKVTGHQWYWSYEFSDIPGLefdsymksldqlrlgeprlleVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDA 177

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504292607 190 NTDNENKFFLTFDSKrskeagDMFFGKCAELCGPSHALMDFKVKTMSAKEFQGWtkeMKNYK 251
Cdd:MTH00080 178 MSGILSTLCYSFPMP------GVFYGQCSEICGANHSFMPIAVEVTLLDNFKEW---CKLLL 230
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 141-247 1.82e-07

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 51.48  E-value: 1.82e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504292607 141 W-WEFEYPDYDIITSQELIVPT-------------DQR--VYFNLK------ASDVKHSFWIPSVGGKLDT-----NTdn 193
Cdd:MTH00140 104 WyWSYEYSDFSVIEFDSYMVPEnelelgdfrllevDNRlvLPYSVDtrvlvtSADVIHSWTVPSLGVKVDAipgrlNQ-- 181

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 504292607 194 enkffLTFDSKRSkeagDMFFGKCAELCGPSHALMDFKVKTMSAKEFQGWTKEM 247
Cdd:MTH00140 182 -----LSFEPKRP----GVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWLELM 226
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 157-251 2.35e-07

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 49.82  E-value: 2.35e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504292607 157 LIVPTDQRVYFNLKASDVKHSFWIPSVGGKLDT---NTDNENKFFLtfdskrsKEAgdMFFGKCAELCGPSHALMDFKVK 233
Cdd:PTZ00047  75 LTLPTRTHIRFLITATDVIHSWSVPSLGIKADAipgRLHKINTFIL-------REG--VFYGQCSEMCGTLHGFMPIVVE 145

                         90
                 ....*....|....*...
gi 504292607 234 TMSAKEFQGWTKemKNYK 251
Cdd:PTZ00047 146 AVSPEAYAAHAK--KYYK 161
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 140-228 3.64e-07

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 49.95  E-value: 3.64e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504292607 140 YWWEFEYPD---YD-IITSQELIVPTDQRVYFNL------KASDVKHSFWIPSVGGKLDTNTDNENKFFLTFDSKRSkea 209
Cdd:MTH00047  91 WYWSYEYSFggsYDsFMTDDIFGVDKPLRLVYGVpyhllvTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCPDRHGV--- 167

                         90
                 ....*....|....*....
gi 504292607 210 gdmFFGKCAELCGPSHALM 228
Cdd:MTH00047 168 ---FVGYCSELCGVGHSYM 183
CytC552 COG4654
Cytochrome c551/c552 [Energy production and conversion];
256-352 1.24e-06

Cytochrome c551/c552 [Energy production and conversion];


Pssm-ID: 443692 [Multi-domain]  Cd Length: 88  Bit Score: 46.05  E-value: 1.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504292607 256 SDLAKQGEELFKEKNCLSCHAVepnDKRaeaaRTAPNLatfgerTKVAGVKEANKENVK---AWLKDPDSIKPGNKMTGT 332
Cdd:COG4654    1 AADAAAGKALAKKSGCLACHAV---DKK----LVGPSY------KDVAKKYKGKADAVAklaKKIKKGGSGVWGDVPMPP 67

                         90       100
                 ....*....|....*....|
gi 504292607 333 YPKLSDSETDALYEYLKGLK 352
Cdd:COG4654   68 HPQLSDAEAKALVKWILSLK 87
PRK10525 PRK10525
cytochrome o ubiquinol oxidase subunit II; Provisional
 142-263 3.35e-06

cytochrome o ubiquinol oxidase subunit II; Provisional


Pssm-ID: 182518 [Multi-domain]  Cd Length: 315  Bit Score: 48.26  E-value: 3.35e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504292607 142 WEFEYPDYDIITSQELIVPTDQRVYFNLKASDVKHSFWIPSVGGKLDTNTDNENKFFLTFDskrskEAGDmFFGKCAELC 221
Cdd:PRK10525 138 WFFIYPEQGIATVNEIAFPANVPVYFKVTSNSVMNSFFIPRLGSQIYAMAGMQTRLHLIAN-----EPGT-YDGISASYS 211

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 504292607 222 GPSHALMDFK-VKTMSAKEFQGWTKEMKNYKST-----AESDLAKQGE 263
Cdd:PRK10525 212 GPGFSGMKFKaIATPDRAEFDQWVAKAKQSPNTmndmaAFEKLAAPSE 259
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 504292607 253 TAESDLAKQGEELFkEKNCLSCHAVEpndkRAEAARTAPNLATfgertkvAGVKEANKENVKAWLKDPdsiKPGNKMTGT 332
Cdd:COG2010   83 AADAEALARGKALY-EQNCAACHGAD----GKGGLGAAPNLTD-------DALYGGDPEALVETILNG---RPGGAMPAF 147

                         90       100
                 ....*....|....*....|..
gi 504292607 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 504292607  251 KSTAESDLAKQGEELFkEKNCLSCHAvepNDKRAEAARTAPNLAtfgertkvagvkeankENVKAWLKDPDSI------K 324
Cdd:TIGR00782 195 GKPKDEALAAKGQELF-ADNCTTCHG---EDGKGLQELGAPNLT----------------DDVWLYGGDLKTItttitnG 254

                          90       100
                  ....*....|....*....|....*..
gi 504292607  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 504292607  270 NCLSCHAVEPNdkrAEAART-APNLATFGER--------TKVAGVKEANkenvkawlkdPDSIKPGNKMTGtypKLSDSE 340
Cdd:TIGR04485   4 NCLACHQIPGS---EVFPGNiGPSLTGYGARypdeaylrAKIADAKAVN----------PCTVMPRFGKNG---ILTEQE 67

                          90
                  ....*....|.
gi 504292607  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 504292607 252 STAESDLAKQGEElfKEKNCLSCHAVepnDKRAEAARTAPNLAtfGErtkvagvkeaNKENVKAWLKDP-DSIKPGNKMT 330
Cdd:COG2863    8 APAAAGDAARGKA--YAAACAACHGA---DGEGNPGGGAPRLA--GQ----------HAEYLVAQLKAFrSGARKNGVMP 70

                         90       100
                 ....*....|....*....|...
gi 504292607 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 504292607 132 VVNVRANLYWWEfeypdydIITSQeliVPTDQRVYFNLKASDVKHSFWIPSVGGKLDTNT----DNENKFFLTFDskrsk 207
Cdd:cd13916    2 VVAVTGHQWYWE-------LSRTE---IPAGKPVEFRVTSADVNHGFGIYDPDMRLLAQTqampGYTNVLRYTFD----- 66

                         90       100
                 ....*....|....*....|....*..
gi 504292607 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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