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Conserved domains on  [gi|1896069699|gb|QNJ47005|]
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cytochrome c oxidase subunit II, partial (mitochondrion) [Prosarthria teretrirostris]

Protein Classification

cytochrome c oxidase subunit II( domain architecture ID 11475927)

cytochrome c oxidase subunit II, part of the functional core of the enzyme, transfers the electrons from cytochrome c via its binuclear copper A center to the bimetallic center of the catalytic subunit I

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-225 2.65e-136

cytochrome c oxidase subunit II; Provisional


:

Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 381.48  E-value: 2.65e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069699   1 MATWSELSLQNSSSPIMEQLSFFHDHTMTIIIMITMIVGYSMSSMLLNKYSLNHFLHGHTIEMVWTTLPAMTLMFIALPS 80
Cdd:MTH00154    1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069699  81 LKILYILDDSTESNLTIKTIGRQWYWSYEYSDFENIEFDSYMI--TEMENNNFRLLDVDNRTMVPFNNEIRMLMSASDVI 158
Cdd:MTH00154   81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIptNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1896069699 159 HSWTIPSAGIKIDASPGRINQGMLFMNRPGLFFGQCSEICGANHSFMPITLESTSTNMFIKWLSNMI 225
Cdd:MTH00154  161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNMS 227
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-225 2.65e-136

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 381.48  E-value: 2.65e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069699   1 MATWSELSLQNSSSPIMEQLSFFHDHTMTIIIMITMIVGYSMSSMLLNKYSLNHFLHGHTIEMVWTTLPAMTLMFIALPS 80
Cdd:MTH00154    1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069699  81 LKILYILDDSTESNLTIKTIGRQWYWSYEYSDFENIEFDSYMI--TEMENNNFRLLDVDNRTMVPFNNEIRMLMSASDVI 158
Cdd:MTH00154   81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIptNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1896069699 159 HSWTIPSAGIKIDASPGRINQGMLFMNRPGLFFGQCSEICGANHSFMPITLESTSTNMFIKWLSNMI 225
Cdd:MTH00154  161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNMS 227
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 93-220 2.24e-79

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: 233.62  E-value: 2.24e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069699  93 SNLTIKTIGRQWYWSYEYSDFENIEFDSYMITE--MENNNFRLLDVDNRTMVPFNNEIRMLMSASDVIHSWTIPSAGIKI 170
Cdd:cd13912     1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEddLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1896069699 171 DASPGRINQGMLFMNRPGLFFGQCSEICGANHSFMPITLESTSTNMFIKW 220
Cdd:cd13912    81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-212 8.86e-70

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 209.19  E-value: 8.86e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069699  95 LTIKTIGRQWYWSYEYSDFENIEFDSYMI--TEMENNNFRLLDVDNRTMVPFNNEIRMLMSASDVIHSWTIPSAGIKIDA 172
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIptEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1896069699 173 SPGRINQGMLFMNRPGLFFGQCSEICGANHSFMPITLEST 212
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
54-224 2.93e-44

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 147.67  E-value: 2.93e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069699  54 HFLHGHTIEMVWTTLPAMTLMFIALPSLKILYILDDSTESNLTIKTIGRQWYWSYEYSDfENIEfdsymitemennnfrl 133
Cdd:COG1622    72 QFHHNTKLEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPD-QGIA---------------- 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069699 134 ldVDNRTMVPFNNEIRMLMSASDVIHSWTIPSAGIKIDASPGRINQGMLFMNRPGLFFGQCSEICGANHSFMPITLESTS 213
Cdd:COG1622   135 --TVNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVS 212

                         170
                  ....*....|.
gi 1896069699 214 TNMFIKWLSNM 224
Cdd:COG1622   213 PEEFDAWLAEQ 223
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 57-222 1.69e-34

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: 121.72  E-value: 1.69e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069699  57 HGHT-IEMVWTTLPAMTLM-FIALPSLKILYILDDSTESNLTIKTIGRQWYWSYEYSDFeniefdsymitemennnfrLL 134
Cdd:TIGR02866  51 HGNRrLEYVWTVIPLIIVVgLFAATAKGLLYLERPIPKDALKVKVTGYQWWWDFEYPES-------------------GF 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069699 135 DVDNRTMVPFNNEIRMLMSASDVIHSWTIPSAGIKIDASPGRINQGMLFMNRPGLFFGQCSEICGANHSFMPITLESTST 214
Cdd:TIGR02866 112 TTVNELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPK 191


                  ....*...
gi 1896069699 215 NMFIKWLS 222
Cdd:TIGR02866 192 EEFDAYVE 199
 
Name Accession Description Interval E-value
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 1-225 2.65e-136

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 381.48  E-value: 2.65e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069699   1 MATWSELSLQNSSSPIMEQLSFFHDHTMTIIIMITMIVGYSMSSMLLNKYSLNHFLHGHTIEMVWTTLPAMTLMFIALPS 80
Cdd:MTH00154    1 MATWSNLSFQDSASPLMEQLIFFHDHTMMILIMITILVGYMMISLLFNKFTNRFLLEGQEIEIIWTILPAIILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069699  81 LKILYILDDSTESNLTIKTIGRQWYWSYEYSDFENIEFDSYMI--TEMENNNFRLLDVDNRTMVPFNNEIRMLMSASDVI 158
Cdd:MTH00154   81 LRLLYLLDEVNNPSITLKTIGHQWYWSYEYSDFKNIEFDSYMIptNELENNGFRLLDVDNRLVLPMNTQIRILITAADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1896069699 159 HSWTIPSAGIKIDASPGRINQGMLFMNRPGLFFGQCSEICGANHSFMPITLESTSTNMFIKWLSNMI 225
Cdd:MTH00154  161 HSWTVPSLGVKVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWIKNMS 227
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 1-224 5.23e-110

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 314.93  E-value: 5.23e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069699   1 MATWSELSLQNSSSPIMEQLSFFHDHTMTIIIMITMIVGYSMSSMLLNKYSLNHFLHGHTIEMVWTTLPAMTLMFIALPS 80
Cdd:MTH00117    1 MANPSQLGFQDASSPIMEELLFFHDHALMVALLISSLVLYLLTLMLTTKLTHTNTVDAQEVELIWTILPAIVLILLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069699  81 LKILYILDDSTESNLTIKTIGRQWYWSYEYSDFENIEFDSYMI--TEMENNNFRLLDVDNRTMVPFNNEIRMLMSASDVI 158
Cdd:MTH00117   81 LRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKDLSFDSYMIptQDLPNGHFRLLEVDHRMVIPMESPIRILITAEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1896069699 159 HSWTIPSAGIKIDASPGRINQGMLFMNRPGLFFGQCSEICGANHSFMPITLESTSTNMFIKWLSNM 224
Cdd:MTH00117  161 HSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSSLL 226
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 1-224 3.27e-105

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 303.01  E-value: 3.27e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069699   1 MATWSELSLQNSSSPIMEQLSFFHDHTMTIIIMITMIVGYSMSSMLLNKYSLNHFLHGHTIEMVWTTLPAMTLMFIALPS 80
Cdd:MTH00140    1 MSYWGQLGFQDPASPLMEELIFFHDHAMVVLVLIFSFVMYMLVLLLFNKFSCRTILEAQKLETIWTIVPALILVFLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069699  81 LKILYILDDSTESNLTIKTIGRQWYWSYEYSDFENIEFDSYMITEMENN--NFRLLDVDNRTMVPFNNEIRMLMSASDVI 158
Cdd:MTH00140   81 LRLLYLLDETNNPLLTVKAIGHQWYWSYEYSDFSVIEFDSYMVPENELElgDFRLLEVDNRLVLPYSVDTRVLVTSADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1896069699 159 HSWTIPSAGIKIDASPGRINQGMLFMNRPGLFFGQCSEICGANHSFMPITLESTSTNMFIKWLSNM 224
Cdd:MTH00140  161 HSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWLELM 226
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 1-224 4.49e-104

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 300.10  E-value: 4.49e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069699   1 MATWSELSLQNSSSPIMEQLSFFHDHTMTIIIMITMIVGYSMSSMLLNKYSLNHFLHGHTIEMVWTTLPAMTLMFIALPS 80
Cdd:MTH00139    1 MAYWGQLGFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSRSLLESQEVETIWTVLPAFILLFLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069699  81 LKILYILDDSTESNLTIKTIGRQWYWSYEYSDFENIEFDSYMI--TEMENNNFRLLDVDNRTMVPFNNEIRMLMSASDVI 158
Cdd:MTH00139   81 LRLLYLMDEVSDPYLTFKAVGHQWYWSYEYSDFKNLSFDSYMIptEDLSSGEFRLLEVDNRLVLPYKSNIRALITAADVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1896069699 159 HSWTIPSAGIKIDASPGRINQGMLFMNRPGLFFGQCSEICGANHSFMPITLESTSTNMFIKWLSNM 224
Cdd:MTH00139  161 HSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEWILEK 226
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 1-223 1.22e-100

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 291.37  E-value: 1.22e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069699   1 MATWSELSLQNSSSPIMEQLSFFHDHTMTIIIMITMIVGYSMSSMLLNKYSLNHFLHGHTIEMVWTTLPAMTLMFIALPS 80
Cdd:MTH00008    1 MPHWGQLMFQDAASPVMLQLISFHDHALLILTLVLTVVGYAMTSLMFNKLSNRYILEAQQIETIWTILPALILLFLAFPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069699  81 LKILYILDDSTESNLTIKTIGRQWYWSYEYSDFENIEFDSYMI--TEMENNNFRLLDVDNRTMVPFNNEIRMLMSASDVI 158
Cdd:MTH00008   81 LRLLYLMDEVSNPSITLKTIGHQWYWSYEYSDFSNLEFDSYMLptSDLSPGQFRLLEVDNRAVLPMQTEIRVLVTAADVI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1896069699 159 HSWTIPSAGIKIDASPGRINQGMLFMNRPGLFFGQCSEICGANHSFMPITLESTSTNMFIKWLSN 223
Cdd:MTH00008  161 HSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKWVSS 225
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 1-223 2.33e-100

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 290.34  E-value: 2.33e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069699   1 MATWSELSLQNSSSPIMEQLSFFHDHTMTIIIMITMIVGYSMSSMLLNKYSLNHFLHGHTIEMVWTTLPAMTLMFIALPS 80
Cdd:MTH00168    1 MATYSQLGLQDAASPVMEELILFHDHALLILVLILTLVLYSLLVLVTSKYTNRFLLDSQMIEFVWTIIPAFILISLALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069699  81 LKILYILDDSTESNLTIKTIGRQWYWSYEYSDFENIEFDSYMI--TEMENNNFRLLDVDNRTMVPFNNEIRMLMSASDVI 158
Cdd:MTH00168   81 LRLLYLMDEIDKPDLTIKAVGHQWYWSYEYTDYNDLEFDSYMVptQDLSPGQFRLLEVDNRLVLPMDSKIRVLVTSADVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1896069699 159 HSWTIPSAGIKIDASPGRINQGMLFMNRPGLFFGQCSEICGANHSFMPITLESTSTNMFIKWLSN 223
Cdd:MTH00168  161 HSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENWVDS 225
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 1-225 9.69e-99

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 286.60  E-value: 9.69e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069699   1 MATWSELSLQNSSSPIMEQLSFFHDHTMTIIIMITMIVGYSMSSMLLNKYSLNHFLHGHTIEMVWTTLPAMTLMFIALPS 80
Cdd:MTH00038    1 MATWLQLGLQDASSPLMEELIYFHDYALIILTLITILVFYGLASLLFSSPTNRFFLEGQELETIWTIVPAFILIFIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069699  81 LKILYILDDSTESNLTIKTIGRQWYWSYEYSDFENIEFDSYMI--TEMENNNFRLLDVDNRTMVPFNNEIRMLMSASDVI 158
Cdd:MTH00038   81 LQLLYLMDEVNNPFLTIKAIGHQWYWSYEYTDYNDLEFDSYMVptSDLSTGLPRLLEVDNRLVLPYQTPIRVLVSSADVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1896069699 159 HSWTIPSAGIKIDASPGRINQGMLFMNRPGLFFGQCSEICGANHSFMPITLESTSTNMFIKWLSNMI 225
Cdd:MTH00038  161 HSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWVSNFL 227
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 1-225 6.38e-93

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 271.59  E-value: 6.38e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069699   1 MATWSELSLQNSSSPIMEQLSFFHDHTMTIIIMITMIVGYSMSSMLLNKYSLNHFLHGHTIEMVWTTLPAMTLMFIALPS 80
Cdd:MTH00098    1 MAYPFQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQEVETIWTILPAIILILIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069699  81 LKILYILDDSTESNLTIKTIGRQWYWSYEYSDFENIEFDSYMI--TEMENNNFRLLDVDNRTMVPFNNEIRMLMSASDVI 158
Cdd:MTH00098   81 LRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDSYMIptSDLKPGELRLLEVDNRVVLPMEMPIRMLISSEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1896069699 159 HSWTIPSAGIKIDASPGRINQGMLFMNRPGLFFGQCSEICGANHSFMPITLESTSTNMFIKWLSNMI 225
Cdd:MTH00098  161 HSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKWSASML 227
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 6-225 3.64e-91

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 267.77  E-value: 3.64e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069699   6 ELSLQNSSSPIMEQLSFFHDHTMTIIIMITMIVGYSMSSMLLNKYSLNHFLHGHTIEMVWTTLPAMTLMFIALPSLKILY 85
Cdd:MTH00023   15 QLGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIVEALNGKFYDRFLVDGTFLEIVWTIIPAVILVFIALPSLKLLY 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069699  86 ILDDSTESNLTIKTIGRQWYWSYEYSDF--ENIEFDSYMI--TEMENNNFRLLDVDNRTMVPFNNEIRMLMSASDVIHSW 161
Cdd:MTH00023   95 LMDEVVSPALTIKAIGHQWYWSYEYSDYegETLEFDSYMVptSDLNSGDFRLLEVDNRLVVPINTHVRILVTGADVLHSF 174

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1896069699 162 TIPSAGIKIDASPGRINQGMLFMNRPGLFFGQCSEICGANHSFMPITLESTSTNMFIKWLSNMI 225
Cdd:MTH00023  175 AVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWLLSLS 238
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 1-225 1.66e-89

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 263.11  E-value: 1.66e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069699   1 MATWSELSLQNSSSPIMEQLSFFHDHTMTIIIMITMIVGYSMSSMLLNKYSLNHFLHGHTIEMVWTTLPAMTLMFIALPS 80
Cdd:MTH00129    1 MAHPSQLGFQDAASPVMEELLHFHDHALMIVFLISTLVLYIIVAMVSTKLTNKYILDSQEIEIIWTVLPAVILILIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069699  81 LKILYILDDSTESNLTIKTIGRQWYWSYEYSDFENIEFDSYMI--TEMENNNFRLLDVDNRTMVPFNNEIRMLMSASDVI 158
Cdd:MTH00129   81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEDLGFDSYMIptQDLTPGQFRLLEADHRMVVPVESPIRVLVSAEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1896069699 159 HSWTIPSAGIKIDASPGRINQGMLFMNRPGLFFGQCSEICGANHSFMPITLESTSTNMFIKWLSNMI 225
Cdd:MTH00129  161 HSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLML 227
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 1-225 1.90e-89

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 262.90  E-value: 1.90e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069699   1 MATWSELSLQNSSSPIMEQLSFFHDHTMTIIIMITMIVGYSMSSMLLNKYSLNHFLHGHTIEMVWTTLPAMTLMFIALPS 80
Cdd:MTH00185    1 MAHPSQLGLQDAASPVMEELIHFHDHTLMIVFLISTLVLYIIVAMVTTKLTNKYILDSQEIEIVWTILPAIILIMIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069699  81 LKILYILDDSTESNLTIKTIGRQWYWSYEYSDFENIEFDSYMI--TEMENNNFRLLDVDNRTMVPFNNEIRMLMSASDVI 158
Cdd:MTH00185   81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEQLEFDSYMTptQDLTPGQFRLLETDHRMVVPMESPIRVLITAEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1896069699 159 HSWTIPSAGIKIDASPGRINQGMLFMNRPGLFFGQCSEICGANHSFMPITLESTSTNMFIKWLSNMI 225
Cdd:MTH00185  161 HSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENWSSLML 227
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 1-224 5.52e-89

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 261.64  E-value: 5.52e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069699   1 MATWSELSLQNSSSPIMEQLSFFHDHTMTIIIMITMIVGYSMSSMLLNKYSLNHFLHGHTIEMVWTTLPAMTLMFIALPS 80
Cdd:MTH00076    1 MAHPSQLGFQDAASPIMEELLHFHDHALMAVFLISTLVLYIITIMMTTKLTNTNTMDAQEIEMVWTIMPAIILIVIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069699  81 LKILYILDDSTESNLTIKTIGRQWYWSYEYSDFENIEFDSYMI--TEMENNNFRLLDVDNRTMVPFNNEIRMLMSASDVI 158
Cdd:MTH00076   81 LRILYLMDEINDPHLTVKAIGHQWYWSYEYTDYEDLSFDSYMIptQDLTPGQFRLLEVDNRMVVPMESPIRMLITAEDVL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1896069699 159 HSWTIPSAGIKIDASPGRINQGMLFMNRPGLFFGQCSEICGANHSFMPITLESTSTNMFIKWLSNM 224
Cdd:MTH00076  161 HSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLNWSSSM 226
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 6-224 1.35e-87

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 258.56  E-value: 1.35e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069699   6 ELSLQNSSSPIMEQLSFFHDHTMTIIIMITMIVGYSMSSMLLNKYSLNHFLHGHTIEMVWTTLPAMTLMFIALPSLKILY 85
Cdd:MTH00051    8 QLGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRALTTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPSLKLLY 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069699  86 ILDDSTESNLTIKTIGRQWYWSYEYSDF--ENIEFDSYMI--TEMENNNFRLLDVDNRTMVPFNNEIRMLMSASDVIHSW 161
Cdd:MTH00051   88 LMDEVIDPALTIKAIGHQWYWSYEYSDYgtDTIEFDSYMIptSDLNSGDLRLLEVDNRLIVPIQTQVRVLVTAADVLHSF 167

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1896069699 162 TIPSAGIKIDASPGRINQGMLFMNRPGLFFGQCSEICGANHSFMPITLESTSTNMFIKWLSNM 224
Cdd:MTH00051  168 AVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINWVATQ 230
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 93-220 2.24e-79

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: 233.62  E-value: 2.24e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069699  93 SNLTIKTIGRQWYWSYEYSDFENIEFDSYMITE--MENNNFRLLDVDNRTMVPFNNEIRMLMSASDVIHSWTIPSAGIKI 170
Cdd:cd13912     1 PSLTIKAIGHQWYWSYEYSDFNDLEFDSYMIPEddLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1896069699 171 DASPGRINQGMLFMNRPGLFFGQCSEICGANHSFMPITLESTSTNMFIKW 220
Cdd:cd13912    81 DAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
95-212 8.86e-70

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 209.19  E-value: 8.86e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069699  95 LTIKTIGRQWYWSYEYSDFENIEFDSYMI--TEMENNNFRLLDVDNRTMVPFNNEIRMLMSASDVIHSWTIPSAGIKIDA 172
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTDFGDLEFDSYMIptEDLEEGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPSLGIKTDA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1896069699 173 SPGRINQGMLFMNRPGLFFGQCSEICGANHSFMPITLEST 212
Cdd:pfam00116  81 VPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIEAV 120
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 6-221 8.47e-69

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 211.81  E-value: 8.47e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069699   6 ELSLQNSSSPIMEQLSFFHDHTMTIIIMITMIVGYSMSSMLLNKYSLNHF---LHGHTIEMVWTTLPAMTLMFIALPSLK 82
Cdd:MTH00027   34 QLGFQDAGSPVMEEIIMLHDQILFILTIIVGVVLWLIIRILLGNNYYSYYwnkLDGSLIEVIWTLIPAFILILIAFPSLR 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069699  83 ILYILDDST-ESNLTIKTIGRQWYWSYEYSDF--ENIEFDSYMI--TEMENNNFRLLDVDNRTMVPFNNEIRMLMSASDV 157
Cdd:MTH00027  114 LLYIMDECGfSANITIKVTGHQWYWSYSYEDYgeKNIEFDSYMIptADLEFGDLRLLEVDNRLILPVDTNVRVLITAADV 193

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1896069699 158 IHSWTIPSAGIKIDASPGRINQGMLFMNRPGLFFGQCSEICGANHSFMPITLESTSTNMFIKWL 221
Cdd:MTH00027  194 LHSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYIDWI 257
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 42-225 8.96e-64

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 197.92  E-value: 8.96e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069699  42 MSSMLLNKYSLNHFLHGHTIEMVWTTLPAMTLMFIALPSLKILYILD-DSTESNLTIKTIGRQWYWSYEYSDFENIEFDS 120
Cdd:MTH00080   44 LYLISNNFYFKSKKIEYQFGELLCSVFPVLILLMQMVPSLSLLYYYGlMNLDSNLTVKVTGHQWYWSYEFSDIPGLEFDS 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069699 121 YM--ITEMENNNFRLLDVDNRTMVPFNNEIRMLMSASDVIHSWTIPSAGIKIDASPGRINQGMLFMNRPGLFFGQCSEIC 198
Cdd:MTH00080  124 YMksLDQLRLGEPRLLEVDNRCVLPCDTNIRFCITSSDVIHSWALPSLSIKMDAMSGILSTLCYSFPMPGVFYGQCSEIC 203

                         170       180
                  ....*....|....*....|....*..
gi 1896069699 199 GANHSFMPITLESTSTNMFIKWLSNMI 225
Cdd:MTH00080  204 GANHSFMPIAVEVTLLDNFKEWCKLLL 230
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
54-224 2.93e-44

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 147.67  E-value: 2.93e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069699  54 HFLHGHTIEMVWTTLPAMTLMFIALPSLKILYILDDSTESNLTIKTIGRQWYWSYEYSDfENIEfdsymitemennnfrl 133
Cdd:COG1622    72 QFHHNTKLEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPD-QGIA---------------- 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069699 134 ldVDNRTMVPFNNEIRMLMSASDVIHSWTIPSAGIKIDASPGRINQGMLFMNRPGLFFGQCSEICGANHSFMPITLESTS 213
Cdd:COG1622   135 --TVNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVS 212

                         170
                  ....*....|.
gi 1896069699 214 TNMFIKWLSNM 224
Cdd:COG1622   213 PEEFDAWLAEQ 223
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 60-210 7.13e-44

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 145.87  E-value: 7.13e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069699  60 TIEMVWTTLPamTLMFIALPSLKILYILDDS-TESNLTIKTIGRQWYWSYEYSDfeNIEFDSYMITEMENnnfrlldVDN 138
Cdd:MTH00047   48 VLELLWTVVP--TLLVLVLCFLNLNFITSDLdCFSSETIKVIGHQWYWSYEYSF--GGSYDSFMTDDIFG-------VDK 116

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1896069699 139 RTMVPFNNEIRMLMSASDVIHSWTIPSAGIKIDASPGRINQGMLFMNRPGLFFGQCSEICGANHSFMPITLE 210
Cdd:MTH00047  117 PLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCPDRHGVFVGYCSELCGVGHSYMPIVIE 188
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 57-222 1.69e-34

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: 121.72  E-value: 1.69e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069699  57 HGHT-IEMVWTTLPAMTLM-FIALPSLKILYILDDSTESNLTIKTIGRQWYWSYEYSDFeniefdsymitemennnfrLL 134
Cdd:TIGR02866  51 HGNRrLEYVWTVIPLIIVVgLFAATAKGLLYLERPIPKDALKVKVTGYQWWWDFEYPES-------------------GF 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069699 135 DVDNRTMVPFNNEIRMLMSASDVIHSWTIPSAGIKIDASPGRINQGMLFMNRPGLFFGQCSEICGANHSFMPITLESTST 214
Cdd:TIGR02866 112 TTVNELVLPAGTPVELQVTSKDVIHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPK 191


                  ....*...
gi 1896069699 215 NMFIKWLS 222
Cdd:TIGR02866 192 EEFDAYVE 199
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 118-217 1.83e-33

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 118.00  E-value: 1.83e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069699 118 FDSYMITEME--NNNFRLLDVDNRTMVPFNNEIRMLMSASDVIHSWTIPSAGIKIDASPGRINQGMLFMNRPGLFFGQCS 195
Cdd:PTZ00047   51 FQSNLVTDEDlkPGMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCS 130

                          90       100
                  ....*....|....*....|..
gi 1896069699 196 EICGANHSFMPITLESTSTNMF 217
Cdd:PTZ00047  131 EMCGTLHGFMPIVVEAVSPEAY 152
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 95-210 8.05e-24

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: 90.82  E-value: 8.05e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069699  95 LTIKTIGRQWYWSYEYSDfeniefdsymitemennnfrlLDVDNRTMVPFNNEIRMLMSASDVIHSWTIPSAGIKIDASP 174
Cdd:cd13842     1 LTVYVTGVQWSWTFIYPN---------------------VRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDAVP 59

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1896069699 175 GRINQGMLFMNRPGLFFGQCSEICGANHSFMPITLE 210
Cdd:cd13842    60 GYTSELWFVADKPGTYTIICAEYCGLGHSYMLGKVE 95
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 95-205 2.03e-21

The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), the terminal oxidase in the respiratory chains of most bacteria, is a multi-chain transmembrane protein located in the inner membrane the cell membrane of prokaryotes. It catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. Caa3 type of CcO Subunit II contains a copper-copper binuclear site called CuA, which is believed to be involved in electron transfer from cytochrome c to the cytochromes a, a3 and CuB active site in subunit I.


Pssm-ID: 259875 [Multi-domain]  Cd Length: 103  Bit Score: 84.98  E-value: 2.03e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069699  95 LTIKTIGRQWYWSYEYSDFENIEFDSymitemennnfrlldvDNRTMVPFNNEIRMLMSASDVIHSWTIPSAGIKIDASP 174
Cdd:cd04213     2 LTIEVTGHQWWWEFRYPDEPGRGIVT----------------ANELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMDMIP 65

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1896069699 175 GRINQGMLFMNRPGLFFGQCSEICGANHSFM 205
Cdd:cd04213    66 GRTNRLWLQADEPGVYRGQCAEFCGASHALM 96
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-205 2.91e-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: 259982 [Multi-domain]  Cd Length: 98  Bit Score: 76.51  E-value: 2.91e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069699  95 LTIKTIGRQWYWSYEYSdfeniefdsymitemenNNFRlldVDNRTMVPFNNEIRMLMSASDVIHSWTIPSAGIKIDASP 174
Cdd:cd13915     2 LEIQVTGRQWMWEFTYP-----------------NGKR---EINELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQDVVP 61

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1896069699 175 GRINQGMLFMNRPGLFFGQCSEICGANHSFM 205
Cdd:cd13915    62 GRYTYLWFEATKPGEYDLFCTEYCGTGHSGM 92
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 95-205 3.79e-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: 259986 [Multi-domain]  Cd Length: 107  Bit Score: 76.53  E-value: 3.79e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069699  95 LTIKTIGRQWYWSYEY--SDFENIEFDSYMITEMEnnnfrlldvdnrtmVPFNNEIRMLMSASDVIHSWTIPSAGIKIDA 172
Cdd:cd13919     2 LVVEVTAQQWAWTFRYpgGDGKLGTDDDVTSPELH--------------LPVGRPVLFNLRSKDVIHSFWVPEFRVKQDA 67

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1896069699 173 SPGRINQGMLFMNRPGLFFGQCSEICGANHSFM 205
Cdd:cd13919    68 VPGRTTRLWFTPTREGEYEVRCAELCGLGHYRM 100
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 1-83 1.04e-16

Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C oxidase contains two transmembrane alpha-helices.


Pssm-ID: 397083 [Multi-domain]  Cd Length: 89  Bit Score: 72.36  E-value: 1.04e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069699   1 MATWSELSLQNSSSPIMEQLSFFHDHTMTIIIMITMIVGYSMSSMLL------NKYSLNHFLHGHTIEMVWTTLPAMTLM 74
Cdd:pfam02790   1 MPTPWGLGFQDAASPLMEGLLELHDYIMFILTLILILVLYILVTCLIrfnrrkNPITARYTTHGQTIEIIWTIIPAVILI 80


                  ....*....
gi 1896069699  75 FIALPSLKI 83
Cdd:pfam02790  81 LIALPSFKL 89
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 96-221 1.06e-15

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: 70.13  E-value: 1.06e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069699  96 TIKTIGRQWYWSYEYSDfENIefdsymitemennnfrllDVDNRTMVPFNNEIRMLMSASDVIHSWTIPSAGIKIDASPG 175
Cdd:cd13914     2 EIEVEAYQWGWEFSYPE-ANV------------------TTSEQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDAFPG 62

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1896069699 176 RINQGMLFMNRPGLFFGQCSEICGANHSFMPITLESTSTNMFIKWL 221
Cdd:cd13914    63 QYNTIKTEATEEGEYQLYCAEYCGAGHSQMLSTVTVVSQDEYQQWL 108
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 83-221 1.24e-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: 259985 [Multi-domain]  Cd Length: 139  Bit Score: 65.55  E-value: 1.24e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069699  83 ILYILDDSTESN---LTIKTIGRQWYWSYEYSDfeNIEFDSYMItemennnfrlldvdnrtmVPFNNEIRMLMSASDVIH 159
Cdd:cd13918    18 LLYVEDPPDEADedaLEVEVEGFQFGWQFEYPN--GVTTGNTLR------------------VPADTPIALRVTSTDVFH 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1896069699 160 SWTIPSAGIKIDASPGRINQGMLFMNRPGLFFGQCSEICGANHSFMPITLESTSTNMFIKWL 221
Cdd:cd13918    78 TFGIPELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEFEAWY 139
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 142-205 5.66e-07

C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and some archaea, which catalyze the reduction of O2 and simultaneously pump protons across the membrane. It has been proposed that archaea acquired heme-copper oxidases through gene transfer from gram-positive bacteria. The ba3 family contains oxidases that lack the conserved residues that form the D- and K-pathways in CcO and ubiquinol oxidase. Instead, they contain a potential alternative K-pathway. Additional proton channels have been proposed for this family of oxidases but none have been identified definitively.


Pssm-ID: 259980 [Multi-domain]  Cd Length: 99  Bit Score: 46.41  E-value: 5.66e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1896069699 142 VPFNNEIRMLMSASDVIHSWTIPSAGIKIDASPGRINQGMLFMNRPGLFFGQCSEICGANHSFM 205
Cdd:cd13913    29 VPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNM 92
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 103-210 5.58e-03

Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in inter-molecular electron transfer reactions. Cupredoxins are blue copper proteins, having an intense blue color due to the presence of a mononuclear type 1 (T1) copper site. Structurally, the cupredoxin-like fold consists of a beta-sandwich with 7 strands in 2 beta-sheets, which is arranged in a Greek-key beta-barrel. Some of these proteins have lost the ability to bind copper. The majority of family members contain multiple cupredoxin domain repeats: ceruloplasmin and the coagulation factors V/VIII have six repeats; laccase, ascorbate oxidase, spore coat protein A, and multicopper oxidase CueO contain three repeats; and nitrite reductase has two repeats. Others are mono-domain cupredoxins, such as plastocyanin, pseudoazurin, plantacyanin, azurin, rusticyanin, stellacyanin, quinol oxidase, and the periplasmic domain of cytochrome c oxidase subunit II.


Pssm-ID: 259860 [Multi-domain]  Cd Length: 110  Bit Score: 35.67  E-value: 5.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1896069699 103 QWYWSYEYSDFENIEFDSYMITEMENNNFRLLdvdNRTMVPFNneirMLMSASDVIHSWTIPSAGI----KIDASPGRIN 178
Cdd:cd00920     7 DWGWSFTYNGVLLFGPPVLVVPVGDTVRVQFV---NKLGENHS----VTIAGFGVPVVAMAGGANPglvnTLVIGPGESA 79

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1896069699 179 QGMLFMNRPGLFFGQCSEICGaNHSFMPITLE 210
Cdd:cd00920    80 EVTFTTDQAGVYWFYCTIPGH-NHAGMVGTIN 110
 
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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