NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1671383843|gb|TMH55297|]
View 

cytochrome c oxidase subunit II [Betaproteobacteria bacterium]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 100-197 3.32e-66

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: 202.47  E-value: 3.32e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671383843 100 ALEIAVVAKQWMWKLQHATGQREIDELHVPVGIPVKLVMTSQDAIHSFYVPAFRLKQDVLPGRYTVLWFTATHAGDYHLF 179
Cdd:cd13915     1 ALEIQVTGRQWMWEFTYPNGKREINELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQDVVPGRYTYLWFEATKPGEYDLF 80

                          90
                  ....*....|....*...
gi 1671383843 180 CAEYCGTDHSRMIGRVVA 197
Cdd:cd13915    81 CTEYCGTGHSGMIGKVRV 98
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
3-215 8.63e-61

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


:

Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 193.51  E-value: 8.63e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671383843   3 FLPEAASTLGARVDTLF--------AAVALVTGAVAlavvallvvfalrYRRGSRADRRRAPEAVRLRTERRLEIAWIAV 74
Cdd:COG1622    20 SLPDPAGPIAEEIDDLFwvsliimlVIFVLVFGLLL-------------YFAIRYRRRKGDADPAQFHHNTKLEIVWTVI 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671383843  75 PMLLFSAAFAWAAALYFDHAAPPQGALEIAVVAKQWMWKLQHA-TGQREIDELHVPVGIPVKLVMTSQDAIHSFYVPAFR 153
Cdd:COG1622    87 PIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPdQGIATVNELVLPVGRPVRFLLTSADVIHSFWVPALG 166

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1671383843 154 LKQDVLPGRYTVLWFTATHAGDYHLFCAEYCGTDHSRMIGRVVALDPAQFQRWLAANNAEPT 215
Cdd:COG1622   167 GKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAEQKASAA 228
Cyc7 COG3474
Cytochrome c2 [Energy production and conversion];
217-308 4.65e-15

Cytochrome c2 [Energy production and conversion];


:

Pssm-ID: 442697 [Multi-domain]  Cd Length: 101  Bit Score: 69.91  E-value: 4.65e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671383843 217 AARGEALFGAfGCGGCH---GPGSTVRAPPLEGLYGRPVALADG---------RTVIADERYLRDAILLPaKEVVAGYAp 284
Cdd:COG3474     3 AAAGEKLFNR-KCAACHsvdGGAGNRVGPNLNGVVGRKAGSVEGfaysdalkaSGLVWDEETLDAWLADP-KAFVPGTK- 79

                          90       100
                  ....*....|....*....|....
gi 1671383843 285 vMPsFSGQIPEGDLLDLIAYLKSL 308
Cdd:COG3474    80 -MP-FAGLKDPEDRADLIAYLKTL 101
 
Name Accession Description Interval E-value
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 100-197 3.32e-66

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: 202.47  E-value: 3.32e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671383843 100 ALEIAVVAKQWMWKLQHATGQREIDELHVPVGIPVKLVMTSQDAIHSFYVPAFRLKQDVLPGRYTVLWFTATHAGDYHLF 179
Cdd:cd13915     1 ALEIQVTGRQWMWEFTYPNGKREINELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQDVVPGRYTYLWFEATKPGEYDLF 80

                          90
                  ....*....|....*...
gi 1671383843 180 CAEYCGTDHSRMIGRVVA 197
Cdd:cd13915    81 CTEYCGTGHSGMIGKVRV 98
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
3-215 8.63e-61

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 193.51  E-value: 8.63e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671383843   3 FLPEAASTLGARVDTLF--------AAVALVTGAVAlavvallvvfalrYRRGSRADRRRAPEAVRLRTERRLEIAWIAV 74
Cdd:COG1622    20 SLPDPAGPIAEEIDDLFwvsliimlVIFVLVFGLLL-------------YFAIRYRRRKGDADPAQFHHNTKLEIVWTVI 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671383843  75 PMLLFSAAFAWAAALYFDHAAPPQGALEIAVVAKQWMWKLQHA-TGQREIDELHVPVGIPVKLVMTSQDAIHSFYVPAFR 153
Cdd:COG1622    87 PIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPdQGIATVNELVLPVGRPVRFLLTSADVIHSFWVPALG 166

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1671383843 154 LKQDVLPGRYTVLWFTATHAGDYHLFCAEYCGTDHSRMIGRVVALDPAQFQRWLAANNAEPT 215
Cdd:COG1622   167 GKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAEQKASAA 228
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 65-208 1.41e-44

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: 150.61  E-value: 1.41e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671383843  65 RRLEIAWIAVPMLLF-SAAFAWAAALYFDHAAPPQGALEIAVVAKQWMWKLQHA-TGQREIDELHVPVGIPVKLVMTSQD 142
Cdd:TIGR02866  54 RRLEYVWTVIPLIIVvGLFAATAKGLLYLERPIPKDALKVKVTGYQWWWDFEYPeSGFTTVNELVLPAGTPVELQVTSKD 133

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1671383843 143 AIHSFYVPAFRLKQDVLPGRYTVLWFTATHAGDYHLFCAEYCGTDHSRMIGRVVALDPAQFQRWLA 208
Cdd:TIGR02866 134 VIHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYVE 199
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
128-191 2.01e-16

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 73.98  E-value: 2.01e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1671383843 128 VPVGIPVKLVMTSQDAIHSFYVPAFRLKQDVLPGRYTVLWFTATHAGDYHLFCAEYCGTDHSRM 191
Cdd:pfam00116  50 LPVETHIRVIVTAADVIHSWAVPSLGIKTDAVPGRLNQTSFSIDREGVFYGQCSEICGINHSFM 113
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 65-211 7.96e-16

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 75.28  E-value: 7.96e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671383843  65 RRLEIAWIAVPMLLFSAAFAWAAALYFDHAAPPQGALEIAVVAKQWMWKLQHA------------------TGQ---REI 123
Cdd:MTH00008   59 QQIETIWTILPALILLFLAFPSLRLLYLMDEVSNPSITLKTIGHQWYWSYEYSdfsnlefdsymlptsdlsPGQfrlLEV 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671383843 124 DELHV-PVGIPVKLVMTSQDAIHSFYVPAFRLKQDVLPGRYTVLWFTATHAGDYHLFCAEYCGTDHSRMIGRVVALDPAQ 202
Cdd:MTH00008  139 DNRAVlPMQTEIRVLVTAADVIHSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKS 218


                  ....*....
gi 1671383843 203 FQRWLAANN 211
Cdd:MTH00008  219 FMKWVSSFA 227
Cyc7 COG3474
Cytochrome c2 [Energy production and conversion];
217-308 4.65e-15

Cytochrome c2 [Energy production and conversion];


Pssm-ID: 442697 [Multi-domain]  Cd Length: 101  Bit Score: 69.91  E-value: 4.65e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671383843 217 AARGEALFGAfGCGGCH---GPGSTVRAPPLEGLYGRPVALADG---------RTVIADERYLRDAILLPaKEVVAGYAp 284
Cdd:COG3474     3 AAAGEKLFNR-KCAACHsvdGGAGNRVGPNLNGVVGRKAGSVEGfaysdalkaSGLVWDEETLDAWLADP-KAFVPGTK- 79

                          90       100
                  ....*....|....*....|....
gi 1671383843 285 vMPsFSGQIPEGDLLDLIAYLKSL 308
Cdd:COG3474    80 -MP-FAGLKDPEDRADLIAYLKTL 101
Cytochrom_C pfam00034
Cytochrome c; The Pfam entry does not include all Prosite members. The cytochrome 556 and ...
 218-308 8.52e-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: 54.85  E-value: 8.52e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671383843 218 ARGEALFGAfGCGGCHGP---GSTVRAPPLEGLYGRPVALADGRTVIADERYLRDAillpAKEVVAGYAPVMPSFsGQIP 294
Cdd:pfam00034   1 ARGKKLFAA-NCAACHGVngeGAGAGGPDLAGLAARYPGDALGAIRENKHAIGGGG----VDRAGGPPGTGMPAF-DGLT 74

                          90
                  ....*....|....
gi 1671383843 295 EGDLLDLIAYLKSL 308
Cdd:pfam00034  75 DEEIADLVAYLLSL 88
PTZ00048 PTZ00048
cytochrome c; Provisional
 217-306 3.18e-05

cytochrome c; Provisional


Pssm-ID: 185414  Cd Length: 115  Bit Score: 42.54  E-value: 3.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671383843 217 AARGEALFGAfGCGGCH---GPGSTVRAPPLEGLYGRPVALAD--------GRTVIADERYLRDAILLPaKEVVAGYAPV 285
Cdd:PTZ00048   15 AKKGAKLFKA-KCAQCHtinKGGAVKQGPNLHGFYGRKSGSADfpysdankNSGIVWSDKHLFEYLVNP-KLYIPGTKMV 92

                          90       100
                  ....*....|....*....|.
gi 1671383843 286 mpsFSGQIPEGDLLDLIAYLK 306
Cdd:PTZ00048   93 ---FAGIKKEKERADLIAYLK 110
ccoP TIGR00782
cytochrome c oxidase, cbb3-type, subunit III; This model describes a di-heme subunit of ...
 212-312 3.30e-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: 41.80  E-value: 3.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671383843 212 AEPTMAARGEALFGAfGCGGCHGPGSTvrapPLEGLyGRPVaLADGRTVIADEryLRDAIllpaKEVVAGYAPVMPSFSG 291
Cdd:TIGR00782 198 KDEALAAKGQELFAD-NCTTCHGEDGK----GLQEL-GAPN-LTDDVWLYGGD--LKTIT----TTITNGRGGVMPAWGP 264

                          90       100
                  ....*....|....*....|.
gi 1671383843 292 QIPEGDLLDLIAYLKSLGGRE 312
Cdd:TIGR00782 265 RLSEAQIKALAAYVHSLGGGQ 285
COG4633 COG4633
Plastocyanin domain containing protein [General function prediction only];
128-180 4.92e-04

Plastocyanin domain containing protein [General function prediction only];


Pssm-ID: 443671 [Multi-domain]  Cd Length: 121  Bit Score: 39.13  E-value: 4.92e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1671383843 128 VPVGIPVKLVMTSQDA---IHSFYVPAFRLKQDVLPGRYTVLWFTATHAGDYHLFC 180
Cdd:COG4633    54 VKAGIPVRLNFTRKDPsgcAEEVVFPDLGISQDLPLGKTVTIEFTPLKPGEYPFTC 109
 
Name Accession Description Interval E-value
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 100-197 3.32e-66

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: 202.47  E-value: 3.32e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671383843 100 ALEIAVVAKQWMWKLQHATGQREIDELHVPVGIPVKLVMTSQDAIHSFYVPAFRLKQDVLPGRYTVLWFTATHAGDYHLF 179
Cdd:cd13915     1 ALEIQVTGRQWMWEFTYPNGKREINELHVPVGKPVRLILTSKDVIHSFYVPAFRIKQDVVPGRYTYLWFEATKPGEYDLF 80

                          90
                  ....*....|....*...
gi 1671383843 180 CAEYCGTDHSRMIGRVVA 197
Cdd:cd13915    81 CTEYCGTGHSGMIGKVRV 98
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
3-215 8.63e-61

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 193.51  E-value: 8.63e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671383843   3 FLPEAASTLGARVDTLF--------AAVALVTGAVAlavvallvvfalrYRRGSRADRRRAPEAVRLRTERRLEIAWIAV 74
Cdd:COG1622    20 SLPDPAGPIAEEIDDLFwvsliimlVIFVLVFGLLL-------------YFAIRYRRRKGDADPAQFHHNTKLEIVWTVI 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671383843  75 PMLLFSAAFAWAAALYFDHAAPPQGALEIAVVAKQWMWKLQHA-TGQREIDELHVPVGIPVKLVMTSQDAIHSFYVPAFR 153
Cdd:COG1622    87 PIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPdQGIATVNELVLPVGRPVRFLLTSADVIHSFWVPALG 166

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1671383843 154 LKQDVLPGRYTVLWFTATHAGDYHLFCAEYCGTDHSRMIGRVVALDPAQFQRWLAANNAEPT 215
Cdd:COG1622   167 GKQDAIPGRVTELWFTADKPGTYRGQCAELCGTGHAGMRFKVVVVSPEEFDAWLAEQKASAA 228
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 65-208 1.41e-44

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: 150.61  E-value: 1.41e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671383843  65 RRLEIAWIAVPMLLF-SAAFAWAAALYFDHAAPPQGALEIAVVAKQWMWKLQHA-TGQREIDELHVPVGIPVKLVMTSQD 142
Cdd:TIGR02866  54 RRLEYVWTVIPLIIVvGLFAATAKGLLYLERPIPKDALKVKVTGYQWWWDFEYPeSGFTTVNELVLPAGTPVELQVTSKD 133

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1671383843 143 AIHSFYVPAFRLKQDVLPGRYTVLWFTATHAGDYHLFCAEYCGTDHSRMIGRVVALDPAQFQRWLA 208
Cdd:TIGR02866 134 VIHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYVE 199
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 100-196 1.10e-41

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: 140.08  E-value: 1.10e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671383843 100 ALEIAVVAKQWMWKLQH--------ATGQREIDELHVPVGIPVKLVMTSQDAIHSFYVPAFRLKQDVLPGRYTVLWFTAT 171
Cdd:cd13919     1 ALVVEVTAQQWAWTFRYpggdgklgTDDDVTSPELHLPVGRPVLFNLRSKDVIHSFWVPEFRVKQDAVPGRTTRLWFTPT 80

                          90       100
                  ....*....|....*....|....*
gi 1671383843 172 HAGDYHLFCAEYCGTDHSRMIGRVV 196
Cdd:cd13919    81 REGEYEVRCAELCGLGHYRMRATVK 105
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 101-196 2.14e-35

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: 123.56  E-value: 2.14e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671383843 101 LEIAVVAKQWMWKlQHATGQREIDELHVPVGIPVKLVMTSQDAIHSFYVPAFRLKQDVLPGRYTVLWFTATHAGDYHLFC 180
Cdd:cd13842     1 LTVYVTGVQWSWT-FIYPNVRTPNEIVVPAGTPVRFRVTSPDVIHGFYIPNLGVKVDAVPGYTSELWFVADKPGTYTIIC 79

                          90
                  ....*....|....*.
gi 1671383843 181 AEYCGTDHSRMIGRVV 196
Cdd:cd13842    80 AEYCGLGHSYMLGKVE 95
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 100-198 2.33e-31

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: 113.10  E-value: 2.33e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671383843 100 ALEIAVVAKQWMWKLQ----HATGQREIDELHVPVGIPVKLVMTSQDAIHSFYVPAFRLKQDVLPGRYTVLWFTATHAGD 175
Cdd:cd04213     1 ALTIEVTGHQWWWEFRypdePGRGIVTANELHIPVGRPVRLRLTSADVIHSFWVPSLAGKMDMIPGRTNRLWLQADEPGV 80

                          90       100
                  ....*....|....*....|...
gi 1671383843 176 YHLFCAEYCGTDHSRMIGRVVAL 198
Cdd:cd04213    81 YRGQCAEFCGASHALMRFKVIAL 103
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 102-207 3.33e-29

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


Pssm-ID: 259981 [Multi-domain]  Cd Length: 108  Bit Score: 107.88  E-value: 3.33e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671383843 102 EIAVVAKQWMWKLQHA-TGQREIDELHVPVGIPVKLVMTSQDAIHSFYVPAFRLKQDVLPGRYTVLWFTATHAGDYHLFC 180
Cdd:cd13914     2 EIEVEAYQWGWEFSYPeANVTTSEQLVIPADRPVYFRITSRDVIHAFHVPELGLKQDAFPGQYNTIKTEATEEGEYQLYC 81

                          90       100
                  ....*....|....*....|....*..
gi 1671383843 181 AEYCGTDHSRMIGRVVALDPAQFQRWL 207
Cdd:cd13914    82 AEYCGAGHSQMLSTVTVVSQDEYQQWL 108
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 89-207 1.27e-25

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


Pssm-ID: 259985 [Multi-domain]  Cd Length: 139  Bit Score: 99.45  E-value: 1.27e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671383843  89 LYFDHAAPPQG--ALEIAVVAKQWMWKLQHATGQREIDELHVPVGIPVKLVMTSQDAIHSFYVPAFRLKQDVLPGRYTVL 166
Cdd:cd13918    19 LYVEDPPDEADedALEVEVEGFQFGWQFEYPNGVTTGNTLRVPADTPIALRVTSTDVFHTFGIPELRVKADAIPGEYTST 98

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1671383843 167 WFTATHAGDYHLFCAEYCGTDHSRMIGRVVALDPAQFQRWL 207
Cdd:cd13918    99 WFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEFEAWY 139
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 99-196 1.15e-19

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


Pssm-ID: 259980 [Multi-domain]  Cd Length: 99  Bit Score: 82.23  E-value: 1.15e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671383843  99 GALEIAVVAKQWMWklqhatgqrEIDELHVPVGIPVKLVMTSQDAIHSFYVPAFRLKQDVLPGRYTVLWFTATHAGDYHL 178
Cdd:cd13913     9 NEYEVYVVAQAFAF---------NPNEIEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLI 79

                          90
                  ....*....|....*...
gi 1671383843 179 FCAEYCGTDHSRMIGRVV 196
Cdd:cd13913    80 ICNEYCGAGHHNMYGKII 97
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 100-206 1.12e-18

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: 80.31  E-value: 1.12e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671383843 100 ALEIAVVAKQWMWKLQH------------------ATGQR---EID-ELHVPVGIPVKLVMTSQDAIHSFYVPAFRLKQD 157
Cdd:cd13912     2 SLTIKAIGHQWYWSYEYsdfndlefdsymipeddlEKGQLrllEVDnRLVVPVNTHIRVLVTSADVIHSWAVPSLGIKVD 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1671383843 158 VLPGRYTVLWFTATHAGDYHLFCAEYCGTDHSRM-IG-RVVALDpaQFQRW 206
Cdd:cd13912    82 AVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMpIVvEAVSLE--DFLSW 130
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
128-191 2.01e-16

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 73.98  E-value: 2.01e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1671383843 128 VPVGIPVKLVMTSQDAIHSFYVPAFRLKQDVLPGRYTVLWFTATHAGDYHLFCAEYCGTDHSRM 191
Cdd:pfam00116  50 LPVETHIRVIVTAADVIHSWAVPSLGIKTDAVPGRLNQTSFSIDREGVFYGQCSEICGINHSFM 113
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 65-211 7.96e-16

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 75.28  E-value: 7.96e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671383843  65 RRLEIAWIAVPMLLFSAAFAWAAALYFDHAAPPQGALEIAVVAKQWMWKLQHA------------------TGQ---REI 123
Cdd:MTH00008   59 QQIETIWTILPALILLFLAFPSLRLLYLMDEVSNPSITLKTIGHQWYWSYEYSdfsnlefdsymlptsdlsPGQfrlLEV 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671383843 124 DELHV-PVGIPVKLVMTSQDAIHSFYVPAFRLKQDVLPGRYTVLWFTATHAGDYHLFCAEYCGTDHSRMIGRVVALDPAQ 202
Cdd:MTH00008  139 DNRAVlPMQTEIRVLVTAADVIHSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKS 218


                  ....*....
gi 1671383843 203 FQRWLAANN 211
Cdd:MTH00008  219 FMKWVSSFA 227
Cyc7 COG3474
Cytochrome c2 [Energy production and conversion];
217-308 4.65e-15

Cytochrome c2 [Energy production and conversion];


Pssm-ID: 442697 [Multi-domain]  Cd Length: 101  Bit Score: 69.91  E-value: 4.65e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671383843 217 AARGEALFGAfGCGGCH---GPGSTVRAPPLEGLYGRPVALADG---------RTVIADERYLRDAILLPaKEVVAGYAp 284
Cdd:COG3474     3 AAAGEKLFNR-KCAACHsvdGGAGNRVGPNLNGVVGRKAGSVEGfaysdalkaSGLVWDEETLDAWLADP-KAFVPGTK- 79

                          90       100
                  ....*....|....*....|....
gi 1671383843 285 vMPsFSGQIPEGDLLDLIAYLKSL 308
Cdd:COG3474    80 -MP-FAGLKDPEDRADLIAYLKTL 101
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 66-207 2.96e-14

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 70.74  E-value: 2.96e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671383843  66 RLEIAWIAVPMLLFSAAFAWAAALYF--DHAAPPqgALEIAVVAKQWMWKLQHAT-------------------GQR--E 122
Cdd:MTH00140   60 KLETIWTIVPALILVFLALPSLRLLYllDETNNP--LLTVKAIGHQWYWSYEYSDfsviefdsymvpenelelgDFRllE 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671383843 123 IDE-LHVPVGIPVKLVMTSQDAIHSFYVPAFRLKQDVLPGRYTVLWFTATHAGDYHLFCAEYCGTDHSRMIGRVVALDPA 201
Cdd:MTH00140  138 VDNrLVLPYSVDTRVLVTSADVIHSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLE 217


                  ....*.
gi 1671383843 202 QFQRWL 207
Cdd:MTH00140  218 DFVKWL 223
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 102-196 5.41e-14

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


Pssm-ID: 259983 [Multi-domain]  Cd Length: 93  Bit Score: 66.64  E-value: 5.41e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671383843 102 EIAVVAKQWMWklqhatgqrEIDELHVPVGIPVKLVMTSQDAIHSF--YVPAFRLKQDV--LPGRYTVLWFTATHAGDYH 177
Cdd:cd13916     2 VVAVTGHQWYW---------ELSRTEIPAGKPVEFRVTSADVNHGFgiYDPDMRLLAQTqaMPGYTNVLRYTFDKPGTYT 72

                          90
                  ....*....|....*....
gi 1671383843 178 LFCAEYCGTDHSRMIGRVV 196
Cdd:cd13916    73 ILCLEYCGLAHHVMMAEFT 91
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 128-211 6.74e-14

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 69.81  E-value: 6.74e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671383843 128 VPVGIPVKLVMTSQDAIHSFYVPAFRLKQDVLPGRYTVLWFTATHAGDYHLFCAEYCGTDHSRMIGRVVALDPAQFQRWL 207
Cdd:MTH00076  144 VPMESPIRMLITAEDVLHSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEATPLNNFLNWS 223


                  ....
gi 1671383843 208 AANN 211
Cdd:MTH00076  224 SSML 227
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 65-206 9.53e-14

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 69.53  E-value: 9.53e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671383843  65 RRLEIAWIAVP-MLLFSAAFAWAAALYF-DHAAPPQgaLEIAVVAKQWMWKLQH------------------ATGQ-REI 123
Cdd:MTH00185   59 QEIEIVWTILPaIILIMIALPSLRILYLmDEINDPH--LTIKAMGHQWYWSYEYtdyeqlefdsymtptqdlTPGQfRLL 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671383843 124 DELH---VPVGIPVKLVMTSQDAIHSFYVPAFRLKQDVLPGRYTVLWFTATHAGDYHLFCAEYCGTDHSRMIGRVVALDP 200
Cdd:MTH00185  137 ETDHrmvVPMESPIRVLITAEDVLHSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPL 216


                  ....*.
gi 1671383843 201 AQFQRW 206
Cdd:MTH00185  217 EHFENW 222
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 66-207 1.01e-13

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 69.36  E-value: 1.01e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671383843  66 RLEIAWIAVPML-LFSAAFAWAAALYF-DHAAPPqgALEIAVVAKQWMWKLQHA-------------------TGQR--E 122
Cdd:MTH00139   60 EVETIWTVLPAFiLLFLALPSLRLLYLmDEVSDP--YLTFKAVGHQWYWSYEYSdfknlsfdsymiptedlssGEFRllE 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671383843 123 IDE-LHVPVGIPVKLVMTSQDAIHSFYVPAFRLKQDVLPGRYTVLWFTATHAGDYHLFCAEYCGTDHSRMIGRVVALDPA 201
Cdd:MTH00139  138 VDNrLVLPYKSNIRALITAADVLHSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPK 217


                  ....*.
gi 1671383843 202 QFQRWL 207
Cdd:MTH00139  218 FFLEWI 223
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 103-191 1.28e-13

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 68.06  E-value: 1.28e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671383843 103 IAVVAKQWMWKLQHATGQrEIDE------------LHVPVGIPVKLVMTSQDAIHSFYVPAFRLKQDVLPGRYTVLWFTA 170
Cdd:MTH00047   84 IKVIGHQWYWSYEYSFGG-SYDSfmtddifgvdkpLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDAIPGRINHLFFCP 162

                          90       100
                  ....*....|....*....|.
gi 1671383843 171 THAGDYHLFCAEYCGTDHSRM 191
Cdd:MTH00047  163 DRHGVFVGYCSELCGVGHSYM 183
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 67-209 1.44e-13

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 68.85  E-value: 1.44e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671383843  67 LEIAWIAVPM-LLFSAAFAWAAALYF-DHAAPPQgaLEIAVVAKQWMWKLQH------------------ATGQ-R--EI 123
Cdd:MTH00168   61 IEFVWTIIPAfILISLALPSLRLLYLmDEIDKPD--LTIKAVGHQWYWSYEYtdyndlefdsymvptqdlSPGQfRllEV 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671383843 124 D-ELHVPVGIPVKLVMTSQDAIHSFYVPAFRLKQDVLPGRYTVLWFTATHAGDYHLFCAEYCGTDHSRMIGRVVALDPAQ 202
Cdd:MTH00168  139 DnRLVLPMDSKIRVLVTSADVLHSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWET 218


                  ....*..
gi 1671383843 203 FQRWLAA 209
Cdd:MTH00168  219 FENWVDS 225
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 67-207 3.68e-13

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 67.85  E-value: 3.68e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671383843  67 LEIAWIAVP--MLLFSAAFAWAAALYFDHAAPPqgALEIAVVAKQWMWKLQHATGQREIDE------------------- 125
Cdd:MTH00023   70 LEIVWTIIPavILVFIALPSLKLLYLMDEVVSP--ALTIKAIGHQWYWSYEYSDYEGETLEfdsymvptsdlnsgdfrll 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671383843 126 -----LHVPVGIPVKLVMTSQDAIHSFYVPAFRLKQDVLPGRYTVLWFTATHAGDYHLFCAEYCGTDHSRMIGRVVALDP 200
Cdd:MTH00023  148 evdnrLVVPINTHVRILVTGADVLHSFAVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSL 227


                  ....*..
gi 1671383843 201 AQFQRWL 207
Cdd:MTH00023  228 DKYINWL 234
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 67-213 7.35e-13

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 66.73  E-value: 7.35e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671383843  67 LEIAWIAVP--MLLFSAAFAWAAALYFDHAAPPqgALEIAVVAKQWMWKLQHATGQREIDE------------------- 125
Cdd:MTH00051   63 IEIIWTLIPaaILIFIAFPSLKLLYLMDEVIDP--ALTIKAIGHQWYWSYEYSDYGTDTIEfdsymiptsdlnsgdlrll 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671383843 126 -----LHVPVGIPVKLVMTSQDAIHSFYVPAFRLKQDVLPGRYTVLWFTATHAGDYHLFCAEYCGTDHSRMIGRVVALDP 200
Cdd:MTH00051  141 evdnrLIVPIQTQVRVLVTAADVLHSFAVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSL 220

                         170
                  ....*....|...
gi 1671383843 201 AQFQRWLAANNAE 213
Cdd:MTH00051  221 DKYINWVATQSEE 233
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 101-191 3.50e-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: 3.50e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671383843 101 LEIAVVAKQWMWKL----QH-ATgqreIDELHVPVGIPVKLVMTSQDAIHSFYVPAFRLKQDVLPGRYTVLWFTATHAGD 175
Cdd:cd04212     1 LEIQVVSLDWKWLFiypeQGiAT----VNELVIPVGRPVNFRLTSDSVMNSFFIPQLGGQIYAMAGMQTQLHLIADKPGT 76

                          90
                  ....*....|....*.
gi 1671383843 176 YHLFCAEYCGTDHSRM 191
Cdd:cd04212    77 YQGLSANYSGEGFSDM 92
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 122-208 6.26e-12

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 63.97  E-value: 6.26e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671383843 122 EIDELHV-PVGIPVKLVMTSQDAIHSFYVPAFRLKQDVLPGRYTVLWFTATHAGDYHLFCAEYCGTDHSRM-IgrVVALD 199
Cdd:MTH00098  137 EVDNRVVlPMEMPIRMLISSEDVLHSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMpI--VLELV 214

                          90
                  ....*....|
gi 1671383843 200 PAQ-FQRWLA 208
Cdd:MTH00098  215 PLKyFEKWSA 224
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 128-208 7.13e-12

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 63.78  E-value: 7.13e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671383843 128 VPVGIPVKLVMTSQDAIHSFYVPAFRLKQDVLPGRYTVLWFTATHAGDYHLFCAEYCGTDHSRMIGRVVALDPAQFQRWL 207
Cdd:MTH00117  144 IPMESPIRILITAEDVLHSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWS 223


                  .
gi 1671383843 208 A 208
Cdd:MTH00117  224 S 224
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 67-206 1.11e-11

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 63.58  E-value: 1.11e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671383843  67 LEIAWIAVP-MLLFSAAFAWAAALYF-DHAAPPQgaLEIAVVAKQWMWKLQH------------------ATGQ-REIDE 125
Cdd:MTH00129   61 IEIIWTVLPaVILILIALPSLRILYLmDEINDPH--LTIKAMGHQWYWSYEYtdyedlgfdsymiptqdlTPGQfRLLEA 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671383843 126 LH---VPVGIPVKLVMTSQDAIHSFYVPAFRLKQDVLPGRYTVLWFTATHAGDYHLFCAEYCGTDHSRMIGRVVALDPAQ 202
Cdd:MTH00129  139 DHrmvVPVESPIRVLVSAEDVLHSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVEAVPLEH 218


                  ....
gi 1671383843 203 FQRW 206
Cdd:MTH00129  219 FENW 222
CuRO_HCO_II_like_4 cd13917
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 135-196 3.03e-11

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


Pssm-ID: 259984 [Multi-domain]  Cd Length: 88  Bit Score: 58.92  E-value: 3.03e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1671383843 135 KLVMTSQDAIHSFYVPAFRLKQDVLPGRYTVLWFTATHAGDYHLFCAEYCGTDHSRMIGRVV 196
Cdd:cd13917    25 RLHLSSLDVQHGFSLQPKNINFQVLPGYEWVITMTPNETGEFHIICNEYCGIGHHTMHGRII 86
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 67-213 8.41e-11

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 60.87  E-value: 8.41e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671383843  67 LEIAWIAVP-MLLFSAAFAWAAALYF-DHAAPPQgaLEIAVVAKQWMWKLQHATGQR-EID------------------- 124
Cdd:MTH00038   61 LETIWTIVPaFILIFIALPSLQLLYLmDEVNNPF--LTIKAIGHQWYWSYEYTDYNDlEFDsymvptsdlstglprllev 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671383843 125 --ELHVPVGIPVKLVMTSQDAIHSFYVPAFRLKQDVLPGRYTVLWFTATHAGDYHLFCAEYCGTDHSRMIGRVVALDPAQ 202
Cdd:MTH00038  139 dnRLVLPYQTPIRVLVSSADVLHSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNT 218

                         170
                  ....*....|.
gi 1671383843 203 FQRWLAANNAE 213
Cdd:MTH00038  219 FENWVSNFLEE 229
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 128-191 1.72e-10

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 60.02  E-value: 1.72e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1671383843 128 VPVGIPVKLVMTSQDAIHSFYVPAFRLKQDVLPGRYTVLWFTATHAGDYHLFCAEYCGTDHSRM 191
Cdd:MTH00080  147 LPCDTNIRFCITSSDVIHSWALPSLSIKMDAMSGILSTLCYSFPMPGVFYGQCSEICGANHSFM 210
Cytochrom_C pfam00034
Cytochrome c; The Pfam entry does not include all Prosite members. The cytochrome 556 and ...
 218-308 8.52e-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: 54.85  E-value: 8.52e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671383843 218 ARGEALFGAfGCGGCHGP---GSTVRAPPLEGLYGRPVALADGRTVIADERYLRDAillpAKEVVAGYAPVMPSFsGQIP 294
Cdd:pfam00034   1 ARGKKLFAA-NCAACHGVngeGAGAGGPDLAGLAARYPGDALGAIRENKHAIGGGG----VDRAGGPPGTGMPAF-DGLT 74

                          90
                  ....*....|....
gi 1671383843 295 EGDLLDLIAYLKSL 308
Cdd:pfam00034  75 DEEIADLVAYLLSL 88
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 67-208 1.72e-09

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 57.34  E-value: 1.72e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671383843  67 LEIAWIAVP-MLLFSAAFAWAAALYFDHAAPPQGALEIAVVAKQWMWKLQHAT-GQREID-------------------- 124
Cdd:MTH00027   92 IEVIWTLIPaFILILIAFPSLRLLYIMDECGFSANITIKVTGHQWYWSYSYEDyGEKNIEfdsymiptadlefgdlrlle 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671383843 125 ---ELHVPVGIPVKLVMTSQDAIHSFYVPAFRLKQDVLPGRYTVLWFTATHAGDYHLFCAEYCGTDHSRMIGRVVALDPA 201
Cdd:MTH00027  172 vdnRLILPVDTNVRVLITAADVLHSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLS 251


                  ....*..
gi 1671383843 202 QFQRWLA 208
Cdd:MTH00027  252 KYIDWIG 258
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 126-191 3.47e-09

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 55.99  E-value: 3.47e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1671383843 126 LHVPVGIPVKLVMTSQDAIHSFYVPAFRLKQDVLPGRYTVLWFTATHAGdyhLF---CAEYCGTDHSRM 191
Cdd:MTH00154  142 LVLPMNTQIRILITAADVIHSWTVPSLGVKVDAVPGRLNQLNFLINRPG---LFfgqCSEICGANHSFM 207
Cupredoxin_1 pfam13473
Cupredoxin-like domain; The cupredoxin-like fold consists of a beta-sandwich with 7 strands in ...
 103-180 1.89e-08

Cupredoxin-like domain; The cupredoxin-like fold consists of a beta-sandwich with 7 strands in 2 beta-sheets, which is arranged in a Greek-key beta-barrel.


Pssm-ID: 379208 [Multi-domain]  Cd Length: 104  Bit Score: 51.43  E-value: 1.89e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671383843 103 IAVVAKQWMWKLQHATGQREI-----------DELHVPVGIPVKLVMTSQDA-IHSFYVPAFRLKQDVLPGRYTVLWFTA 170
Cdd:pfam13473   3 AALAVLFWLSKPAAAADDPTVeitvkdggfspSRITVPAGTPVKLEFKNKDKtPAEFESPDLGIEKVLAPGKTSTITIPP 82

                          90
                  ....*....|
gi 1671383843 171 THAGDYHLFC 180
Cdd:pfam13473  83 LKPGEYDFFC 92
CccA COG2010
Cytochrome c, mono- and diheme variants [Energy production and conversion];
185-311 7.15e-08

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


Pssm-ID: 441613 [Multi-domain]  Cd Length: 169  Bit Score: 51.49  E-value: 7.15e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671383843 185 GTDHSRMIGRVVALDPAQFQrwLAANNAEPTMAARGEALFGAFgCGGCHGPGstvrappLEGLYGRPVALADGRTVIADE 264
Cdd:COG2010    59 AAAAALALALLLALLLAAAA--ADAPAADAEALARGKALYEQN-CAACHGAD-------GKGGLGAAPNLTDDALYGGDP 128

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1671383843 265 RYLRDAILLPAKevvagyAPVMPSFSGQIPEGDLLDLIAYLKSLGGR 311
Cdd:COG2010   129 EALVETILNGRP------GGAMPAFGGQLSDEEIAALAAYLRSLSGN 169
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 120-203 1.39e-07

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 50.20  E-value: 1.39e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671383843 120 QREIDE-LHVPVGIPVKLVMTSQDAIHSFYVPAFRLKQDVLPGRYTVLWFTATHAGDYHLFCAEYCGTDHSRMIGRVVAL 198
Cdd:PTZ00047   68 QLEVDKrLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCSEMCGTLHGFMPIVVEAV 147


                  ....*
gi 1671383843 199 DPAQF 203
Cdd:PTZ00047  148 SPEAY 152
PRK10525 PRK10525
cytochrome o ubiquinol oxidase subunit II; Provisional
 103-218 2.00e-06

cytochrome o ubiquinol oxidase subunit II; Provisional


Pssm-ID: 182518 [Multi-domain]  Cd Length: 315  Bit Score: 48.64  E-value: 2.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671383843 103 IAVVAKQWMWKLQHA-TGQREIDELHVPVGIPVKLVMTSQDAIHSFYVPAFRLKQDVLPGRYTVLWFTATHAGDYHLFCA 181
Cdd:PRK10525  129 IEVVSMDWKWFFIYPeQGIATVNEIAFPANVPVYFKVTSNSVMNSFFIPRLGSQIYAMAGMQTRLHLIANEPGTYDGISA 208

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1671383843 182 EYCGTDHSRMIGRVVAL-DPAQFQRWLAANNAEP----TMAA 218
Cdd:PRK10525  209 SYSGPGFSGMKFKAIATpDRAEFDQWVAKAKQSPntmnDMAA 250
N2OR_C cd04223
The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase ...
 124-196 9.30e-06

The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase participates in nitrogen metabolism and catalyzes the last step in dissimilatory nitrate reduction, the two-electron reduction of N2O to N2. It contains copper ions as cofactors in the form of a binuclear CuA center at the site of electron entry and a tetranuclear CuZ centre at the active site. The C-terminus of Nitrous-oxide reductase is a cupredoxin domain.


Pssm-ID: 259885 [Multi-domain]  Cd Length: 95  Bit Score: 43.38  E-value: 9.30e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1671383843 124 DELHVPVGIPVKLVMT----SQDAIHSFYVPAFRLKQDVLPGRYTVLWFTATHAGDYHLFCAEYCGTDHSRMIGRVV 196
Cdd:cd04223    16 DIIEVKEGDEVTVHLTnleqDEDITHGFAIPGYNVNLSLEPGETATVTFVADKPGVYPYYCTEFCSALHLEMQGYLI 92
PTZ00048 PTZ00048
cytochrome c; Provisional
 217-306 3.18e-05

cytochrome c; Provisional


Pssm-ID: 185414  Cd Length: 115  Bit Score: 42.54  E-value: 3.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671383843 217 AARGEALFGAfGCGGCH---GPGSTVRAPPLEGLYGRPVALAD--------GRTVIADERYLRDAILLPaKEVVAGYAPV 285
Cdd:PTZ00048   15 AKKGAKLFKA-KCAQCHtinKGGAVKQGPNLHGFYGRKSGSADfpysdankNSGIVWSDKHLFEYLVNP-KLYIPGTKMV 92

                          90       100
                  ....*....|....*....|.
gi 1671383843 286 mpsFSGQIPEGDLLDLIAYLK 306
Cdd:PTZ00048   93 ---FAGIKKEKERADLIAYLK 110
CytC553 COG2863
Cytochrome c553 [Energy production and conversion];
207-315 3.46e-05

Cytochrome c553 [Energy production and conversion];


Pssm-ID: 442110 [Multi-domain]  Cd Length: 98  Bit Score: 42.02  E-value: 3.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671383843 207 LAANNAEPTMAARGEALFGAfgCGGCHGP----GSTVRAPPLEGLYgrpvaladgrtviadERYLRDAILLPAKEvvAGY 282
Cdd:COG2863     5 LLAAPAAAGDAARGKAYAAA--CAACHGAdgegNPGGGAPRLAGQH---------------AEYLVAQLKAFRSG--ARK 65

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1671383843 283 APVMPSFSGQIPEGDLLDLIAYLKSLGGREPAS 315
Cdd:COG2863    66 NGVMPAIAKGLSDEDIKALAAYIASLKAPPGAA 98
Cytochrome_CBB3 pfam13442
Cytochrome C oxidase, cbb3-type, subunit III;
217-305 1.78e-04

Cytochrome C oxidase, cbb3-type, subunit III;


Pssm-ID: 463879 [Multi-domain]  Cd Length: 67  Bit Score: 39.31  E-value: 1.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671383843 217 AARGEALFGAFgCGGCHGPGstVRAPPLEGLYGRPvaladgrtviadeRYLRDAILlpakevvAGYApVMPSFSGQIPEG 296
Cdd:pfam13442   3 AAAGEALYAAN-CASCHGTG--GAGPSLAGRALPP-------------EALVDIIR-------NGKG-AMPAFGGDLSDE 58


                  ....*....
gi 1671383843 297 DLLDLIAYL 305
Cdd:pfam13442  59 ELEALAAYL 67
ccoP TIGR00782
cytochrome c oxidase, cbb3-type, subunit III; This model describes a di-heme subunit of ...
 212-312 3.30e-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: 41.80  E-value: 3.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671383843 212 AEPTMAARGEALFGAfGCGGCHGPGSTvrapPLEGLyGRPVaLADGRTVIADEryLRDAIllpaKEVVAGYAPVMPSFSG 291
Cdd:TIGR00782 198 KDEALAAKGQELFAD-NCTTCHGEDGK----GLQEL-GAPN-LTDDVWLYGGD--LKTIT----TTITNGRGGVMPAWGP 264

                          90       100
                  ....*....|....*....|.
gi 1671383843 292 QIPEGDLLDLIAYLKSLGGRE 312
Cdd:TIGR00782 265 RLSEAQIKALAAYVHSLGGGQ 285
COG4633 COG4633
Plastocyanin domain containing protein [General function prediction only];
128-180 4.92e-04

Plastocyanin domain containing protein [General function prediction only];


Pssm-ID: 443671 [Multi-domain]  Cd Length: 121  Bit Score: 39.13  E-value: 4.92e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1671383843 128 VPVGIPVKLVMTSQDA---IHSFYVPAFRLKQDVLPGRYTVLWFTATHAGDYHLFC 180
Cdd:COG4633    54 VKAGIPVRLNFTRKDPsgcAEEVVFPDLGISQDLPLGKTVTIEFTPLKPGEYPFTC 109
PetE COG3794
Plastocyanin [Energy production and conversion];
124-196 2.03e-03

Plastocyanin [Energy production and conversion];


Pssm-ID: 443008 [Multi-domain]  Cd Length: 76  Bit Score: 36.51  E-value: 2.03e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1671383843 124 DELHVPVGIPVKLVMTSQDA--IHSFYVPAFRLKQDVLPGRYTVlWFTATHAGDYHLFCaeycgTDHSRMIGRVV 196
Cdd:COG3794     6 ATLTVKPGDTVTWVNTDSVPhnVTSDDGPDGAFDSGLLAPGETF-SVTFDEPGTYDYYC-----TPHPWMVGTIV 74
Cupredoxin cd00920
Cupredoxin superfamily; Cupredoxins contain type I copper centers and are involved in ...
 105-195 5.30e-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: 36.05  E-value: 5.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1671383843 105 VVAKQWMWKLQHATGQREIDE-LHVPVGIPVKLVMTS-QDAIHSFYVPAFRLKQDVL---------------PGRYTVLW 167
Cdd:cd00920     3 VTASDWGWSFTYNGVLLFGPPvLVVPVGDTVRVQFVNkLGENHSVTIAGFGVPVVAMagganpglvntlvigPGESAEVT 82

                          90       100
                  ....*....|....*....|....*...
gi 1671383843 168 FTATHAGDYHLFCAEYCGTdHSRMIGRV 195
Cdd:cd00920    83 FTTDQAGVYWFYCTIPGHN-HAGMVGTI 109
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH