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Conserved domains on  [gi|1337428508|ref|WP_103272010|]
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cytochrome c oxidase subunit II [Achromobacter sp. AONIH1]

Protein Classification

cytochrome c oxidase subunit II( domain architecture ID 11446856)

cytochrome c oxidase subunit II, together with subunit I, forms the functional core of the enzyme that catalyzes the reduction of O2 and simultaneously pump protons across the membrane

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
1-272 4.72e-98

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


:

Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 290.96  E-value: 4.72e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428508   1 MKKWRGILGACAMLIGGmagaqvqdmpggpkvnQLNLHEGVTQIARDVMWLHWMLLTICIVIFIGVFGVMFYSIWAHRKS 80
Cdd:COG1622     1 MKRLLLALLLLALLLSG----------------QLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLLLYFAIRYRRR 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428508  81 RGH-KAATFHEHLGVEVAWTVIPFIIVIAMALPATKTVVAMKDTSSADLTVKVTGYQWKWGYEYLDGSAAgvkflstlst 159
Cdd:COG1622    65 KGDaDPAQFHHNTKLEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIA---------- 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428508 160 praqienrepkgqfylmeVDNHMVVPVDKKVRVVLTAADVIHSWMIPDFGVKQDAIPGFLRDAWFRAEQPGIYRGQCAEL 239
Cdd:COG1622   135 ------------------TVNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAEL 196

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1337428508 240 CGKDHAFMPIVVEVLAQADYDKWVEDQKKRMAA 272
Cdd:COG1622   197 CGTGHAGMRFKVVVVSPEEFDAWLAEQKASAAT 229
CccA COG2010
Cytochrome c, mono- and diheme variants [Energy production and conversion];
270-367 3.48e-26

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


:

Pssm-ID: 441613 [Multi-domain]  Cd Length: 169  Bit Score: 103.11  E-value: 3.48e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428508 270 MAASADDPNKEWTEAELVARGEKVFAANCVACHQANGKGIPGSFPALDGDKVVLGPKAAQINTVLKGKPGTAMAAFGGQL 349
Cdd:COG2010    72 LLLAAAAADAPAADAEALARGKALYEQNCAACHGADGKGGLGAAPNLTDDALYGGDPEALVETILNGRPGGAMPAFGGQL 151

                          90
                  ....*....|....*...
gi 1337428508 350 NDVEIAAVISYTRHAWSN 367
Cdd:COG2010   152 SDEEIAALAAYLRSLSGN 169
 
Name Accession Description Interval E-value
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
1-272 4.72e-98

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 290.96  E-value: 4.72e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428508   1 MKKWRGILGACAMLIGGmagaqvqdmpggpkvnQLNLHEGVTQIARDVMWLHWMLLTICIVIFIGVFGVMFYSIWAHRKS 80
Cdd:COG1622     1 MKRLLLALLLLALLLSG----------------QLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLLLYFAIRYRRR 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428508  81 RGH-KAATFHEHLGVEVAWTVIPFIIVIAMALPATKTVVAMKDTSSADLTVKVTGYQWKWGYEYLDGSAAgvkflstlst 159
Cdd:COG1622    65 KGDaDPAQFHHNTKLEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIA---------- 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428508 160 praqienrepkgqfylmeVDNHMVVPVDKKVRVVLTAADVIHSWMIPDFGVKQDAIPGFLRDAWFRAEQPGIYRGQCAEL 239
Cdd:COG1622   135 ------------------TVNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAEL 196

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1337428508 240 CGKDHAFMPIVVEVLAQADYDKWVEDQKKRMAA 272
Cdd:COG1622   197 CGTGHAGMRFKVVVVSPEEFDAWLAEQKASAAT 229
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 127-262 2.88e-69

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: 213.97  E-value: 2.88e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428508 127 DLTVKVTGYQWKWGYEYLDGSaaGVKFLSTLSTpraqiENREPKGQFYLMEVDNHMVVPVDKKVRVVLTAADVIHSWMIP 206
Cdd:cd13912     2 SLTIKAIGHQWYWSYEYSDFN--DLEFDSYMIP-----EDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVP 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1337428508 207 DFGVKQDAIPGFLRDAWFRAEQPGIYRGQCAELCGKDHAFMPIVVEVLAQADYDKW 262
Cdd:cd13912    75 SLGIKVDAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 33-264 2.22e-65

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 207.48  E-value: 2.22e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428508  33 NQLNLHEGVTQIARDVMWLH--WMLLTICIVIFIGVFGVMFY--SIWAHrksrghkaaTFHEHLGVEVAWTVIPFIIVIA 108
Cdd:MTH00140    5 GQLGFQDPASPLMEELIFFHdhAMVVLVLIFSFVMYMLVLLLfnKFSCR---------TILEAQKLETIWTIVPALILVF 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428508 109 MALPATKTVVAMKDTSSADLTVKVTGYQWKWGYEYLDGSaaGVKFLSTLsTPRAQIEnrepKGQFYLMEVDNHMVVPVDK 188
Cdd:MTH00140   76 LALPSLRLLYLLDETNNPLLTVKAIGHQWYWSYEYSDFS--VIEFDSYM-VPENELE----LGDFRLLEVDNRLVLPYSV 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1337428508 189 KVRVVLTAADVIHSWMIPDFGVKQDAIPGFLRDAWFRAEQPGIYRGQCAELCGKDHAFMPIVVEVLAQADYDKWVE 264
Cdd:MTH00140  149 DTRVLVTSADVIHSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWLE 224
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 42-264 3.22e-53

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: 175.26  E-value: 3.22e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428508  42 TQIARDVMWLHWMLLTICIVIFIGVFGVMFYSIWAHR-KSRGHKAATFHEHLGVEVAWTVIPFIIVIAM-ALPATKTVVA 119
Cdd:TIGR02866   3 GEIAQQIAFLFLFVLAVSTLISLLVAALLAYVVWKFRrKGDEEKPSQIHGNRRLEYVWTVIPLIIVVGLfAATAKGLLYL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428508 120 MKDTSSADLTVKVTGYQWKWGYEYLDGsaagvkflstlstpraqienrepkgqfyLMEVDNHMVVPVDKKVRVVLTAADV 199
Cdd:TIGR02866  83 ERPIPKDALKVKVTGYQWWWDFEYPES----------------------------GFTTVNELVLPAGTPVELQVTSKDV 134

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1337428508 200 IHSWMIPDFGVKQDAIPGFLRDAWFRAEQPGIYRGQCAELCGKDHAFMPIVVEVLAQADYDKWVE 264
Cdd:TIGR02866 135 IHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYVE 199
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
128-252 6.18e-48

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 158.73  E-value: 6.18e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428508 128 LTVKVTGYQWKWGYEYLDgsAAGVKFLSTLsTPRAQIEnrepKGQFYLMEVDNHMVVPVDKKVRVVLTAADVIHSWMIPD 207
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTD--FGDLEFDSYM-IPTEDLE----EGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPS 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1337428508 208 FGVKQDAIPGFLRDAWFRAEQPGIYRGQCAELCGKDHAFMPIVVE 252
Cdd:pfam00116  74 LGIKTDAVPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIE 118
CccA COG2010
Cytochrome c, mono- and diheme variants [Energy production and conversion];
270-367 3.48e-26

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


Pssm-ID: 441613 [Multi-domain]  Cd Length: 169  Bit Score: 103.11  E-value: 3.48e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428508 270 MAASADDPNKEWTEAELVARGEKVFAANCVACHQANGKGIPGSFPALDGDKVVLGPKAAQINTVLKGKPGTAMAAFGGQL 349
Cdd:COG2010    72 LLLAAAAADAPAADAEALARGKALYEQNCAACHGADGKGGLGAAPNLTDDALYGGDPEALVETILNGRPGGAMPAFGGQL 151

                          90
                  ....*....|....*...
gi 1337428508 350 NDVEIAAVISYTRHAWSN 367
Cdd:COG2010   152 SDEEIAALAAYLRSLSGN 169
Cytochrom_C pfam00034
Cytochrome c; The Pfam entry does not include all Prosite members. The cytochrome 556 and ...
 288-365 3.72e-14

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: 67.56  E-value: 3.72e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428508 288 ARGEKVFAANCVACHQANGKGIPGSFPALDG----------DKVVLGPKAAQINTVLK--GKPGTAMAAFGGqLNDVEIA 355
Cdd:pfam00034   1 ARGKKLFAANCAACHGVNGEGAGAGGPDLAGlaarypgdalGAIRENKHAIGGGGVDRagGPPGTGMPAFDG-LTDEEIA 79

                          90
                  ....*....|
gi 1337428508 356 AVISYTRHAW 365
Cdd:pfam00034  80 DLVAYLLSLS 89
ccoP TIGR00782
cytochrome c oxidase, cbb3-type, subunit III; This model describes a di-heme subunit of ...
 247-370 7.15e-10

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: 59.52  E-value: 7.15e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428508 247 MPIVVEVLAQADYDKWVEDQKKRMAASADDPnkewteaELVARGEKVFAANCVACHQANGKGIPG-SFPALDGDKVVLGP 325
Cdd:TIGR00782 170 MPAFGPLLEEADIKDVASYVMSLSSGKPKDE-------ALAAKGQELFADNCTTCHGEDGKGLQElGAPNLTDDVWLYGG 242

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1337428508 326 KAAQINTVLKGKPGTAMAAFGGQLNDVEIAAVISYTrhaWSNAGK 370
Cdd:TIGR00782 243 DLKTITTTITNGRGGVMPAWGPRLSEAQIKALAAYV---HSLGGG 284
petJ CHL00183
cytochrome c553; Provisional
 282-360 3.58e-08

cytochrome c553; Provisional


Pssm-ID: 177085  Cd Length: 108  Bit Score: 50.93  E-value: 3.58e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428508 282 TEAELVARGEKVFAANCVACHqANGKGipgsfpALDGDKvVLGPKA----------AQINTVLKGKpgTAMAAFGGQLND 351
Cdd:CHL00183   21 AFAADLDNGEQIFSANCAACH-AGGNN------VIMPEK-TLKKDAleansmnsieAITYQVTNGK--NAMPAFGGRLSD 90


                  ....*....
gi 1337428508 352 VEIAAVISY 360
Cdd:CHL00183   91 EDIEDVANY 99
 
Name Accession Description Interval E-value
CyoA COG1622
Heme/copper-type cytochrome/quinol oxidase, subunit 2 [Energy production and conversion];
1-272 4.72e-98

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


Pssm-ID: 441229 [Multi-domain]  Cd Length: 229  Bit Score: 290.96  E-value: 4.72e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428508   1 MKKWRGILGACAMLIGGmagaqvqdmpggpkvnQLNLHEGVTQIARDVMWLHWMLLTICIVIFIGVFGVMFYSIWAHRKS 80
Cdd:COG1622     1 MKRLLLALLLLALLLSG----------------QLSLPDPAGPIAEEIDDLFWVSLIIMLVIFVLVFGLLLYFAIRYRRR 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428508  81 RGH-KAATFHEHLGVEVAWTVIPFIIVIAMALPATKTVVAMKDTSSADLTVKVTGYQWKWGYEYLDGSAAgvkflstlst 159
Cdd:COG1622    65 KGDaDPAQFHHNTKLEIVWTVIPIIIVIVLAVPTLRVLHALDDAPEDPLTVEVTGYQWKWLFRYPDQGIA---------- 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428508 160 praqienrepkgqfylmeVDNHMVVPVDKKVRVVLTAADVIHSWMIPDFGVKQDAIPGFLRDAWFRAEQPGIYRGQCAEL 239
Cdd:COG1622   135 ------------------TVNELVLPVGRPVRFLLTSADVIHSFWVPALGGKQDAIPGRVTELWFTADKPGTYRGQCAEL 196

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1337428508 240 CGKDHAFMPIVVEVLAQADYDKWVEDQKKRMAA 272
Cdd:COG1622   197 CGTGHAGMRFKVVVVSPEEFDAWLAEQKASAAT 229
CcO_II_C cd13912
C-terminal domain of Cytochrome c Oxidase subunit II; Cytochrome c Oxidase (CcO), the terminal ...
 127-262 2.88e-69

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: 213.97  E-value: 2.88e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428508 127 DLTVKVTGYQWKWGYEYLDGSaaGVKFLSTLSTpraqiENREPKGQFYLMEVDNHMVVPVDKKVRVVLTAADVIHSWMIP 206
Cdd:cd13912     2 SLTIKAIGHQWYWSYEYSDFN--DLEFDSYMIP-----EDDLEKGQLRLLEVDNRLVVPVNTHIRVLVTSADVIHSWAVP 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1337428508 207 DFGVKQDAIPGFLRDAWFRAEQPGIYRGQCAELCGKDHAFMPIVVEVLAQADYDKW 262
Cdd:cd13912    75 SLGIKVDAVPGRLNQTSFFIERPGVYYGQCSEICGANHSFMPIVVEAVSLEDFLSW 130
COX2 MTH00140
cytochrome c oxidase subunit II; Provisional
 33-264 2.22e-65

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214430 [Multi-domain]  Cd Length: 228  Bit Score: 207.48  E-value: 2.22e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428508  33 NQLNLHEGVTQIARDVMWLH--WMLLTICIVIFIGVFGVMFY--SIWAHrksrghkaaTFHEHLGVEVAWTVIPFIIVIA 108
Cdd:MTH00140    5 GQLGFQDPASPLMEELIFFHdhAMVVLVLIFSFVMYMLVLLLfnKFSCR---------TILEAQKLETIWTIVPALILVF 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428508 109 MALPATKTVVAMKDTSSADLTVKVTGYQWKWGYEYLDGSaaGVKFLSTLsTPRAQIEnrepKGQFYLMEVDNHMVVPVDK 188
Cdd:MTH00140   76 LALPSLRLLYLLDETNNPLLTVKAIGHQWYWSYEYSDFS--VIEFDSYM-VPENELE----LGDFRLLEVDNRLVLPYSV 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1337428508 189 KVRVVLTAADVIHSWMIPDFGVKQDAIPGFLRDAWFRAEQPGIYRGQCAELCGKDHAFMPIVVEVLAQADYDKWVE 264
Cdd:MTH00140  149 DTRVLVTSADVIHSWTVPSLGVKVDAIPGRLNQLSFEPKRPGVFYGQCSEICGANHSFMPIVVEAVPLEDFVKWLE 224
COX2 MTH00117
cytochrome c oxidase subunit II; Provisional
 34-264 8.93e-58

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177178 [Multi-domain]  Cd Length: 227  Bit Score: 187.81  E-value: 8.93e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428508  34 QLNLHEGVTQIARDVMWLH----WMLLTICIVIFIGVFGVMFYSIWahrksrgHKAATFHEHLgvEVAWTVIPFIIVIAM 109
Cdd:MTH00117    6 QLGFQDASSPIMEELLFFHdhalMVALLISSLVLYLLTLMLTTKLT-------HTNTVDAQEV--ELIWTILPAIVLILL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428508 110 ALPATKTVVAMKDTSSADLTVKVTGYQWKWGYEYLDGSAagVKFLSTLsTPRAQIenrePKGQFYLMEVDNHMVVPVDKK 189
Cdd:MTH00117   77 ALPSLRILYLMDEINNPHLTIKAIGHQWYWSYEYTDYKD--LSFDSYM-IPTQDL----PNGHFRLLEVDHRMVIPMESP 149

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1337428508 190 VRVVLTAADVIHSWMIPDFGVKQDAIPGFLRDAWFRAEQPGIYRGQCAELCGKDHAFMPIVVEVLAQADYDKWVE 264
Cdd:MTH00117  150 IRILITAEDVLHSWAVPSLGVKTDAVPGRLNQTSFITTRPGVFYGQCSEICGANHSFMPIVVESVPLKHFENWSS 224
COX2 MTH00139
cytochrome c oxidase subunit II; Provisional
 30-263 1.43e-57

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214429 [Multi-domain]  Cd Length: 226  Bit Score: 187.23  E-value: 1.43e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428508  30 PKVNQLNLHEGVTQIARDVMWLHWMLLTICIVIFIGVFGVMFYSIWAHRKSRghkaaTFHEHLGVEVAWTVIPFIIVIAM 109
Cdd:MTH00139    2 AYWGQLGFQDSASPLMEQLIFFHDHAMVILIMILSFVGYISLSLMSNKFTSR-----SLLESQEVETIWTVLPAFILLFL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428508 110 ALPATKTVVAMKDTSSADLTVKVTGYQWKWGYEYLDgsaagvkfLSTLSTPRAQIENRE-PKGQFYLMEVDNHMVVPVDK 188
Cdd:MTH00139   77 ALPSLRLLYLMDEVSDPYLTFKAVGHQWYWSYEYSD--------FKNLSFDSYMIPTEDlSSGEFRLLEVDNRLVLPYKS 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1337428508 189 KVRVVLTAADVIHSWMIPDFGVKQDAIPGFLRDAWFRAEQPGIYRGQCAELCGKDHAFMPIVVEVLAQADYDKWV 263
Cdd:MTH00139  149 NIRALITAADVLHSWTVPSLGVKIDAVPGRLNQVGFFINRPGVFYGQCSEICGANHSFMPIVVEAISPKFFLEWI 223
COX2 MTH00168
cytochrome c oxidase subunit II; Provisional
 33-263 4.97e-57

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177223 [Multi-domain]  Cd Length: 225  Bit Score: 185.95  E-value: 4.97e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428508  33 NQLNLHEGVTQIARDVMWLHWMLLTICIVIFIGVFgVMFYSIwahrKSRGHKAATFHEHLGVEVAWTVIPFIIVIAMALP 112
Cdd:MTH00168    5 SQLGLQDAASPVMEELILFHDHALLILVLILTLVL-YSLLVL----VTSKYTNRFLLDSQMIEFVWTIIPAFILISLALP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428508 113 ATKTVVAMKDTSSADLTVKVTGYQWKWGYEYLDGSaaGVKFLSTLsTPRAQIENrepkGQFYLMEVDNHMVVPVDKKVRV 192
Cdd:MTH00168   80 SLRLLYLMDEIDKPDLTIKAVGHQWYWSYEYTDYN--DLEFDSYM-VPTQDLSP----GQFRLLEVDNRLVLPMDSKIRV 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1337428508 193 VLTAADVIHSWMIPDFGVKQDAIPGFLRDAWFRAEQPGIYRGQCAELCGKDHAFMPIVVEVLAQADYDKWV 263
Cdd:MTH00168  153 LVTSADVLHSWTLPSLGLKMDAVPGRLNQLAFLSSRPGSFYGQCSEICGANHSFMPIVVEFVPWETFENWV 223
COX2 MTH00154
cytochrome c oxidase subunit II; Provisional
 52-263 1.23e-56

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214438 [Multi-domain]  Cd Length: 227  Bit Score: 185.03  E-value: 1.23e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428508  52 HWMLLTICIVIFIGVFGV-MFYSIWAHRKSrghkaatFHEHLgVEVAWTVIPFIIVIAMALPATKTVVAMKDTSSADLTV 130
Cdd:MTH00154   26 HTMMILIMITILVGYMMIsLLFNKFTNRFL-------LEGQE-IEIIWTILPAIILIFIALPSLRLLYLLDEVNNPSITL 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428508 131 KVTGYQWKWGYEYLDgsAAGVKFLSTLsTPraqiENREPKGQFYLMEVDNHMVVPVDKKVRVVLTAADVIHSWMIPDFGV 210
Cdd:MTH00154   98 KTIGHQWYWSYEYSD--FKNIEFDSYM-IP----TNELENNGFRLLDVDNRLVLPMNTQIRILITAADVIHSWTVPSLGV 170

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1337428508 211 KQDAIPGFLRDAWFRAEQPGIYRGQCAELCGKDHAFMPIVVEVLAQADYDKWV 263
Cdd:MTH00154  171 KVDAVPGRLNQLNFLINRPGLFFGQCSEICGANHSFMPIVIESVSVNNFINWI 223
COX2 MTH00023
cytochrome c oxidase subunit II; Validated
 29-263 4.75e-55

cytochrome c oxidase subunit II; Validated


Pssm-ID: 214402 [Multi-domain]  Cd Length: 240  Bit Score: 181.49  E-value: 4.75e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428508  29 GPKVNQLNLHEGVTQIARDVMWLHWMLLTICIVIFIGVFGVMFysiwahrksRGHKAATFHEHL----GVEVAWTVIPFI 104
Cdd:MTH00023   10 IPEPWQLGFQDAADPVMEEIIFFHDQIMFLLIIIITVVLWLIV---------EALNGKFYDRFLvdgtFLEIVWTIIPAV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428508 105 IVIAMALPATKTVVAMKDTSSADLTVKVTGYQWKWGYEYLDGSAAGVKFLSTLsTPRAQIEnrepKGQFYLMEVDNHMVV 184
Cdd:MTH00023   81 ILVFIALPSLKLLYLMDEVVSPALTIKAIGHQWYWSYEYSDYEGETLEFDSYM-VPTSDLN----SGDFRLLEVDNRLVV 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1337428508 185 PVDKKVRVVLTAADVIHSWMIPDFGVKQDAIPGFLRDAWFRAEQPGIYRGQCAELCGKDHAFMPIVVEVLAQADYDKWV 263
Cdd:MTH00023  156 PINTHVRILVTGADVLHSFAVPSLGLKIDAVPGRLNQTGFFIKRPGVFYGQCSEICGANHSFMPIVIEAVSLDKYINWL 234
COX2 MTH00038
cytochrome c oxidase subunit II; Provisional
 34-263 1.84e-54

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177113 [Multi-domain]  Cd Length: 229  Bit Score: 179.51  E-value: 1.84e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428508  34 QLNLHEGVTQIARDVMWLH----WMLLTICIVIFIGVFGVMFySIWAHRKsrghkaatFHEHLGVEVAWTVIPFIIVIAM 109
Cdd:MTH00038    6 QLGLQDASSPLMEELIYFHdyalIILTLITILVFYGLASLLF-SSPTNRF--------FLEGQELETIWTIVPAFILIFI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428508 110 ALPATKTVVAMKDTSSADLTVKVTGYQWKWGYEYLDGSAagVKFLSTLsTPRAQIENREPKgqfyLMEVDNHMVVPVDKK 189
Cdd:MTH00038   77 ALPSLQLLYLMDEVNNPFLTIKAIGHQWYWSYEYTDYND--LEFDSYM-VPTSDLSTGLPR----LLEVDNRLVLPYQTP 149

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1337428508 190 VRVVLTAADVIHSWMIPDFGVKQDAIPGFLRDAWFRAEQPGIYRGQCAELCGKDHAFMPIVVEVLAQADYDKWV 263
Cdd:MTH00038  150 IRVLVSSADVLHSWAVPSLGVKMDAVPGRLNQTTFFISRTGLFYGQCSEICGANHSFMPIVIESVPFNTFENWV 223
COX2 MTH00008
cytochrome c oxidase subunit II; Validated
 34-263 4.42e-54

cytochrome c oxidase subunit II; Validated


Pssm-ID: 164584 [Multi-domain]  Cd Length: 228  Bit Score: 178.51  E-value: 4.42e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428508  34 QLNLHEGVTQIARDVMWLHWMLLTICIVIfIGVFGVMFYSIWAHRKSrghkAATFHEHLGVEVAWTVIPFIIVIAMALPA 113
Cdd:MTH00008    6 QLMFQDAASPVMLQLISFHDHALLILTLV-LTVVGYAMTSLMFNKLS----NRYILEAQQIETIWTILPALILLFLAFPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428508 114 TKTVVAMKDTSSADLTVKVTGYQWKWGYEYLDGSaaGVKFLSTLsTPRAQIEnrepKGQFYLMEVDNHMVVPVDKKVRVV 193
Cdd:MTH00008   81 LRLLYLMDEVSNPSITLKTIGHQWYWSYEYSDFS--NLEFDSYM-LPTSDLS----PGQFRLLEVDNRAVLPMQTEIRVL 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428508 194 LTAADVIHSWMIPDFGVKQDAIPGFLRDAWFRAEQPGIYRGQCAELCGKDHAFMPIVVEVLAQADYDKWV 263
Cdd:MTH00008  154 VTAADVIHSWTVPSLGVKVDAVPGRLNQIGFTITRPGVFYGQCSEICGANHSFMPIVLEAVDTKSFMKWV 223
COX2 MTH00076
cytochrome c oxidase subunit II; Provisional
 94-262 8.06e-54

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164646 [Multi-domain]  Cd Length: 228  Bit Score: 177.66  E-value: 8.06e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428508  94 VEVAWTVIPFIIVIAMALPATKTVVAMKDTSSADLTVKVTGYQWKWGYEYLDgsAAGVKFLSTLsTPRAQIEnrepKGQF 173
Cdd:MTH00076   61 IEMVWTIMPAIILIVIALPSLRILYLMDEINDPHLTVKAIGHQWYWSYEYTD--YEDLSFDSYM-IPTQDLT----PGQF 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428508 174 YLMEVDNHMVVPVDKKVRVVLTAADVIHSWMIPDFGVKQDAIPGFLRDAWFRAEQPGIYRGQCAELCGKDHAFMPIVVEV 253
Cdd:MTH00076  134 RLLEVDNRMVVPMESPIRMLITAEDVLHSWAVPSLGIKTDAIPGRLNQTSFIASRPGVYYGQCSEICGANHSFMPIVVEA 213


                  ....*....
gi 1337428508 254 LAQADYDKW 262
Cdd:MTH00076  214 TPLNNFLNW 222
CoxB TIGR02866
cytochrome c oxidase, subunit II; Cytochrome c oxidase is the terminal electron acceptor of ...
 42-264 3.22e-53

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: 175.26  E-value: 3.22e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428508  42 TQIARDVMWLHWMLLTICIVIFIGVFGVMFYSIWAHR-KSRGHKAATFHEHLGVEVAWTVIPFIIVIAM-ALPATKTVVA 119
Cdd:TIGR02866   3 GEIAQQIAFLFLFVLAVSTLISLLVAALLAYVVWKFRrKGDEEKPSQIHGNRRLEYVWTVIPLIIVVGLfAATAKGLLYL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428508 120 MKDTSSADLTVKVTGYQWKWGYEYLDGsaagvkflstlstpraqienrepkgqfyLMEVDNHMVVPVDKKVRVVLTAADV 199
Cdd:TIGR02866  83 ERPIPKDALKVKVTGYQWWWDFEYPES----------------------------GFTTVNELVLPAGTPVELQVTSKDV 134

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1337428508 200 IHSWMIPDFGVKQDAIPGFLRDAWFRAEQPGIYRGQCAELCGKDHAFMPIVVEVLAQADYDKWVE 264
Cdd:TIGR02866 135 IHSFWVPELGGKIDAIPGQTNALWFNADEPGVYYGFCAELCGAGHSLMLFKVVVVPKEEFDAYVE 199
COX2 MTH00051
cytochrome c oxidase subunit II; Provisional
 34-268 2.83e-52

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177126 [Multi-domain]  Cd Length: 234  Bit Score: 173.81  E-value: 2.83e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428508  34 QLNLHEGVTQIARDVMWLHWMLLTICIVIFIGVFGVMFYSIwahrkSRGHKAATFHEHLGVEVAWTVIPFIIVIAMALPA 113
Cdd:MTH00051    8 QLGFQDAASPVMEEIIFFHDQIMFILTIIITTVLWLIIRAL-----TTKYYHKYLFEGTLIEIIWTLIPAAILIFIAFPS 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428508 114 TKTVVAMKDTSSADLTVKVTGYQWKWGYEYLDGSAAGVKFLSTLsTPRAQIENrepkGQFYLMEVDNHMVVPVDKKVRVV 193
Cdd:MTH00051   83 LKLLYLMDEVIDPALTIKAIGHQWYWSYEYSDYGTDTIEFDSYM-IPTSDLNS----GDLRLLEVDNRLIVPIQTQVRVL 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1337428508 194 LTAADVIHSWMIPDFGVKQDAIPGFLRDAWFRAEQPGIYRGQCAELCGKDHAFMPIVVEVLAQADYDKWVEDQKK 268
Cdd:MTH00051  158 VTAADVLHSFAVPSLSVKIDAVPGRLNQTSFFIKRPGVFYGQCSEICGANHSFMPIVIEGVSLDKYINWVATQSE 232
COX2 MTH00185
cytochrome c oxidase subunit II; Provisional
 34-262 1.55e-51

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 164736 [Multi-domain]  Cd Length: 230  Bit Score: 171.99  E-value: 1.55e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428508  34 QLNLHEGVTQIARDVMWLHWMLLTICIVIFIgvfgVMFYSIWAHRKSRGHKAATFhEHLGVEVAWTVIPFIIVIAMALPA 113
Cdd:MTH00185    6 QLGLQDAASPVMEELIHFHDHTLMIVFLIST----LVLYIIVAMVTTKLTNKYIL-DSQEIEIVWTILPAIILIMIALPS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428508 114 TKTVVAMKDTSSADLTVKVTGYQWKWGYEYLDGSAagVKFLSTLStpraQIENREPkGQFYLMEVDNHMVVPVDKKVRVV 193
Cdd:MTH00185   81 LRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEQ--LEFDSYMT----PTQDLTP-GQFRLLETDHRMVVPMESPIRVL 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1337428508 194 LTAADVIHSWMIPDFGVKQDAIPGFLRDAWFRAEQPGIYRGQCAELCGKDHAFMPIVVEVLAQADYDKW 262
Cdd:MTH00185  154 ITAEDVLHSWTVPALGVKMDAVPGRLNQATFIISRPGLYYGQCSEICGANHSFMPIVVEAVPLEHFENW 222
COX2 MTH00098
cytochrome c oxidase subunit II; Validated
 94-262 5.72e-51

cytochrome c oxidase subunit II; Validated


Pssm-ID: 177160 [Multi-domain]  Cd Length: 227  Bit Score: 170.28  E-value: 5.72e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428508  94 VEVAWTVIPFIIVIAMALPATKTVVAMKDTSSADLTVKVTGYQWKWGYEYLDgsAAGVKFLSTLSTPraqiENREPkGQF 173
Cdd:MTH00098   61 VETIWTILPAIILILIALPSLRILYMMDEINNPSLTVKTMGHQWYWSYEYTD--YEDLSFDSYMIPT----SDLKP-GEL 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428508 174 YLMEVDNHMVVPVDKKVRVVLTAADVIHSWMIPDFGVKQDAIPGFLRDAWFRAEQPGIYRGQCAELCGKDHAFMPIVVEV 253
Cdd:MTH00098  134 RLLEVDNRVVLPMEMPIRMLISSEDVLHSWAVPSLGLKTDAIPGRLNQTTLMSTRPGLYYGQCSEICGSNHSFMPIVLEL 213


                  ....*....
gi 1337428508 254 LAQADYDKW 262
Cdd:MTH00098  214 VPLKYFEKW 222
COX2 MTH00129
cytochrome c oxidase subunit II; Provisional
 93-262 2.59e-50

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177187 [Multi-domain]  Cd Length: 230  Bit Score: 168.74  E-value: 2.59e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428508  93 GVEVAWTVIPFIIVIAMALPATKTVVAMKDTSSADLTVKVTGYQWKWGYEYLDGSAAGvkFLSTLsTPRAQIEnrepKGQ 172
Cdd:MTH00129   60 EIEIIWTVLPAVILILIALPSLRILYLMDEINDPHLTIKAMGHQWYWSYEYTDYEDLG--FDSYM-IPTQDLT----PGQ 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428508 173 FYLMEVDNHMVVPVDKKVRVVLTAADVIHSWMIPDFGVKQDAIPGFLRDAWFRAEQPGIYRGQCAELCGKDHAFMPIVVE 252
Cdd:MTH00129  133 FRLLEADHRMVVPVESPIRVLVSAEDVLHSWAVPALGVKMDAVPGRLNQTAFIASRPGVFYGQCSEICGANHSFMPIVVE 212

                         170
                  ....*....|
gi 1337428508 253 VLAQADYDKW 262
Cdd:MTH00129  213 AVPLEHFENW 222
COX2 MTH00027
cytochrome c oxidase subunit II; Provisional
 34-263 7.68e-49

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214405 [Multi-domain]  Cd Length: 262  Bit Score: 165.97  E-value: 7.68e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428508  34 QLNLHEGVTQIARDVMWLHWMLLTIcIVIFIGV---------FGVMFYSIWAHRKSrghkaATFhehlgVEVAWTVIPFI 104
Cdd:MTH00027   34 QLGFQDAGSPVMEEIIMLHDQILFI-LTIIVGVvlwliirilLGNNYYSYYWNKLD-----GSL-----IEVIWTLIPAF 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428508 105 IVIAMALPATKTVVAMKDTS-SADLTVKVTGYQWKWGYEYLDGSAAGVKFLSTLsTPRAQIEnrepKGQFYLMEVDNHMV 183
Cdd:MTH00027  103 ILILIAFPSLRLLYIMDECGfSANITIKVTGHQWYWSYSYEDYGEKNIEFDSYM-IPTADLE----FGDLRLLEVDNRLI 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428508 184 VPVDKKVRVVLTAADVIHSWMIPDFGVKQDAIPGFLRDAWFRAEQPGIYRGQCAELCGKDHAFMPIVVEVLAQADYDKWV 263
Cdd:MTH00027  178 LPVDTNVRVLITAADVLHSWTVPSLAVKMDAVPGRINETGFLIKRPGIFYGQCSEICGANHSFMPIVVESVSLSKYIDWI 257
COX2 pfam00116
Cytochrome C oxidase subunit II, periplasmic domain;
128-252 6.18e-48

Cytochrome C oxidase subunit II, periplasmic domain;


Pssm-ID: 395066 [Multi-domain]  Cd Length: 120  Bit Score: 158.73  E-value: 6.18e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428508 128 LTVKVTGYQWKWGYEYLDgsAAGVKFLSTLsTPRAQIEnrepKGQFYLMEVDNHMVVPVDKKVRVVLTAADVIHSWMIPD 207
Cdd:pfam00116   1 LTIKAIGHQWYWSYEYTD--FGDLEFDSYM-IPTEDLE----EGQLRLLEVDNRVVLPVETHIRVIVTAADVIHSWAVPS 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1337428508 208 FGVKQDAIPGFLRDAWFRAEQPGIYRGQCAELCGKDHAFMPIVVE 252
Cdd:pfam00116  74 LGIKTDAVPGRLNQTSFSIDREGVFYGQCSEICGINHSFMPIVIE 118
COX2 MTH00080
cytochrome c oxidase subunit II; Provisional
 51-253 5.15e-45

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 177149 [Multi-domain]  Cd Length: 231  Bit Score: 154.78  E-value: 5.15e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428508  51 LHWMLLTICIVIFIG---VFGVMFY-----SIWAHRKSRGHKAAtfhehlgVEVAWTVIPFIIVIAMALPATKTVVAMKD 122
Cdd:MTH00080   19 MDWFHNFNCSLLFGEfvlAFVVFLFlylisNNFYFKSKKIEYQF-------GELLCSVFPVLILLMQMVPSLSLLYYYGL 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428508 123 TS-SADLTVKVTGYQWKWGYEYLDgsAAGVKFLSTLStPRAQIENREPKgqfyLMEVDNHMVVPVDKKVRVVLTAADVIH 201
Cdd:MTH00080   92 MNlDSNLTVKVTGHQWYWSYEFSD--IPGLEFDSYMK-SLDQLRLGEPR----LLEVDNRCVLPCDTNIRFCITSSDVIH 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1337428508 202 SWMIPDFGVKQDAIPGFLRDAWFRAEQPGIYRGQCAELCGKDHAFMPIVVEV 253
Cdd:MTH00080  165 SWALPSLSIKMDAMSGILSTLCYSFPMPGVFYGQCSEICGANHSFMPIAVEV 216
COX2 MTH00047
cytochrome c oxidase subunit II; Provisional
 55-253 3.23e-33

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 214412 [Multi-domain]  Cd Length: 194  Bit Score: 122.76  E-value: 3.23e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428508  55 LLTICIVIFIGVFGVMFYSIwahrKSRGHKAATFHEHLGVEVAWTVIPFIIVIAMALPATKTVVAMKDTSSADlTVKVTG 134
Cdd:MTH00047   14 ILALCVFIPCWVYIMLCWQV----VSGNGSVNFGSENQVLELLWTVVPTLLVLVLCFLNLNFITSDLDCFSSE-TIKVIG 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428508 135 YQWKWGYEYLDGSaagvKFLSTLStpraqienrepkgQFYLMeVDNHMVVPVDKKVRVVLTAADVIHSWMIPDFGVKQDA 214
Cdd:MTH00047   89 HQWYWSYEYSFGG----SYDSFMT-------------DDIFG-VDKPLRLVYGVPYHLLVTSSDVIHSFSVPDLNLKMDA 150

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1337428508 215 IPGFLRDAWFRAEQPGIYRGQCAELCGKDHAFMPIVVEV 253
Cdd:MTH00047  151 IPGRINHLFFCPDRHGVFVGYCSELCGVGHSYMPIVIEV 189
CuRO_HCO_II_like_2 cd13915
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 127-253 8.92e-31

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


Pssm-ID: 259982 [Multi-domain]  Cd Length: 98  Bit Score: 113.11  E-value: 8.92e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428508 127 DLTVKVTGYQWKWGYEYLDGsaagvkflstlstpraqieNREpkgqfylmevDNHMVVPVDKKVRVVLTAADVIHSWMIP 206
Cdd:cd13915     1 ALEIQVTGRQWMWEFTYPNG-------------------KRE----------INELHVPVGKPVRLILTSKDVIHSFYVP 51

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1337428508 207 DFGVKQDAIPGFLRDAWFRAEQPGIYRGQCAELCGKDHAFMPIVVEV 253
Cdd:cd13915    52 AFRIKQDVVPGRYTYLWFEATKPGEYDLFCTEYCGTGHSGMIGKVRV 98
CuRO_CcO_Caa3_II cd04213
The cupredoxin domain of Caa3 type Cytochrome c oxidase subunit II; Cytochrome c oxidase (CcO), ...
 127-254 1.42e-30

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: 112.71  E-value: 1.42e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428508 127 DLTVKVTGYQWKWGYEYLDGSAAGVkflstlstpraqienrepkgqfylmEVDNHMVVPVDKKVRVVLTAADVIHSWMIP 206
Cdd:cd04213     1 ALTIEVTGHQWWWEFRYPDEPGRGI-------------------------VTANELHIPVGRPVRLRLTSADVIHSFWVP 55

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1337428508 207 DFGVKQDAIPGFLRDAWFRAEQPGIYRGQCAELCGKDHAFMPIVVEVL 254
Cdd:cd04213    56 SLAGKMDMIPGRTNRLWLQADEPGVYRGQCAEFCGASHALMRFKVIAL 103
CuRO_HCO_II_like_5 cd13919
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 127-253 4.02e-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: 259986 [Multi-domain]  Cd Length: 107  Bit Score: 108.88  E-value: 4.02e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428508 127 DLTVKVTGYQWKWGYEYLDGsaaGVKFlstlstpraqienrepkgQFYLMEVDNHMVVPVDKKVRVVLTAADVIHSWMIP 206
Cdd:cd13919     1 ALVVEVTAQQWAWTFRYPGG---DGKL------------------GTDDDVTSPELHLPVGRPVLFNLRSKDVIHSFWVP 59

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1337428508 207 DFGVKQDAIPGFLRDAWFRAEQPGIYRGQCAELCGKDHAFMPIVVEV 253
Cdd:cd13919    60 EFRVKQDAVPGRTTRLWFTPTREGEYEVRCAELCGLGHYRMRATVKV 106
CuRO_HCO_II_like cd13842
Cupredoxin domain of Heme-copper oxidase subunit II; Heme-copper oxidases are transmembrane ...
 128-252 1.68e-27

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


Pssm-ID: 259911 [Multi-domain]  Cd Length: 95  Bit Score: 104.30  E-value: 1.68e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428508 128 LTVKVTGYQWKWGYEYLDGsaagvkflstlstpraqienrepkgqfylmEVDNHMVVPVDKKVRVVLTAADVIHSWMIPD 207
Cdd:cd13842     1 LTVYVTGVQWSWTFIYPNV------------------------------RTPNEIVVPAGTPVRFRVTSPDVIHGFYIPN 50

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1337428508 208 FGVKQDAIPGFLRDAWFRAEQPGIYRGQCAELCGKDHAFMPIVVE 252
Cdd:cd13842    51 LGVKVDAVPGYTSELWFVADKPGTYTIICAEYCGLGHSYMLGKVE 95
CuRO_HCO_II_like_6 cd13918
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 127-263 4.92e-27

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: 104.46  E-value: 4.92e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428508 127 DLTVKVTGYQWKWGYEYLDGSAAGvkflstlstpraqienrepkgqfylmevdNHMVVPVDKKVRVVLTAADVIHSWMIP 206
Cdd:cd13918    32 ALEVEVEGFQFGWQFEYPNGVTTG-----------------------------NTLRVPADTPIALRVTSTDVFHTFGIP 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1337428508 207 DFGVKQDAIPGFLRDAWFRAEQPGIYRGQCAELCGKDHAFMPIVVEVLAQADYDKWV 263
Cdd:cd13918    83 ELRVKADAIPGEYTSTWFEADEPGTYEAKCYELCGSGHSLMTGDVIVMDEEEFEAWY 139
CccA COG2010
Cytochrome c, mono- and diheme variants [Energy production and conversion];
270-367 3.48e-26

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


Pssm-ID: 441613 [Multi-domain]  Cd Length: 169  Bit Score: 103.11  E-value: 3.48e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428508 270 MAASADDPNKEWTEAELVARGEKVFAANCVACHQANGKGIPGSFPALDGDKVVLGPKAAQINTVLKGKPGTAMAAFGGQL 349
Cdd:COG2010    72 LLLAAAAADAPAADAEALARGKALYEQNCAACHGADGKGGLGAAPNLTDDALYGGDPEALVETILNGRPGGAMPAFGGQL 151

                          90
                  ....*....|....*...
gi 1337428508 350 NDVEIAAVISYTRHAWSN 367
Cdd:COG2010   152 SDEEIAALAAYLRSLSGN 169
PTZ00047 PTZ00047
cytochrome c oxidase subunit II; Provisional
 171-265 8.13e-25

cytochrome c oxidase subunit II; Provisional


Pssm-ID: 240243 [Multi-domain]  Cd Length: 162  Bit Score: 99.12  E-value: 8.13e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428508 171 GQFYLMEVDNHMVVPVDKKVRVVLTAADVIHSWMIPDFGVKQDAIPGFLRDAWFRAEQPGIYRGQCAELCGKDHAFMPIV 250
Cdd:PTZ00047   64 GMLRQLEVDKRLTLPTRTHIRFLITATDVIHSWSVPSLGIKADAIPGRLHKINTFILREGVFYGQCSEMCGTLHGFMPIV 143

                          90
                  ....*....|....*....
gi 1337428508 251 VEVLAQADY----DKWVED 265
Cdd:PTZ00047  144 VEAVSPEAYaahaKKYYKD 162
CuRO_HCO_II_like_3 cd13914
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 129-263 2.20e-22

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


Pssm-ID: 259981 [Multi-domain]  Cd Length: 108  Bit Score: 90.93  E-value: 2.20e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428508 129 TVKVTGYQWKWGYEYldgsaagvkflstlstPRAQIENREPkgqfylmevdnhMVVPVDKKVRVVLTAADVIHSWMIPDF 208
Cdd:cd13914     2 EIEVEAYQWGWEFSY----------------PEANVTTSEQ------------LVIPADRPVYFRITSRDVIHAFHVPEL 53

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1337428508 209 GVKQDAIPGFLRDAWFRAEQPGIYRGQCAELCGKDHAFMPIVVEVLAQADYDKWV 263
Cdd:cd13914    54 GLKQDAFPGQYNTIKTEATEEGEYQLYCAEYCGAGHSQMLSTVTVVSQDEYQQWL 108
Cytochrom_C pfam00034
Cytochrome c; The Pfam entry does not include all Prosite members. The cytochrome 556 and ...
 288-365 3.72e-14

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: 67.56  E-value: 3.72e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428508 288 ARGEKVFAANCVACHQANGKGIPGSFPALDG----------DKVVLGPKAAQINTVLK--GKPGTAMAAFGGqLNDVEIA 355
Cdd:pfam00034   1 ARGKKLFAANCAACHGVNGEGAGAGGPDLAGlaarypgdalGAIRENKHAIGGGGVDRagGPPGTGMPAFDG-LTDEEIA 79

                          90
                  ....*....|
gi 1337428508 356 AVISYTRHAW 365
Cdd:pfam00034  80 DLVAYLLSLS 89
TsdA COG3258
Thiosulfate dehydrogenase TsdA, contains C-terminal cytochrome c domain [Inorganic ion ...
 287-363 4.00e-11

Thiosulfate dehydrogenase TsdA, contains C-terminal cytochrome c domain [Inorganic ion transport and metabolism];


Pssm-ID: 442489 [Multi-domain]  Cd Length: 216  Bit Score: 62.18  E-value: 4.00e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428508 287 VARGEKVFAANCVACHQANGKGIPG-----SFPALDGDKVV-LGPKAAQINTVLKGKPGTAMAAF-GGQLNDVEIAAVIS 359
Cdd:COG3258   117 VERGKALYAERCASCHGADGEGQGRadgqyGFPPLWGGDSYnDGAGMARLGTLADFIKGRNMPLGkPGSLSDDEAWDVAA 196


                  ....
gi 1337428508 360 YTRH 363
Cdd:COG3258   197 YVRS 200
Cytochrome_CBB3 pfam13442
Cytochrome C oxidase, cbb3-type, subunit III;
285-360 4.87e-11

Cytochrome C oxidase, cbb3-type, subunit III;


Pssm-ID: 463879 [Multi-domain]  Cd Length: 67  Bit Score: 57.80  E-value: 4.87e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1337428508 285 ELVARGEKVFAANCVACHQANGKGipgsfPALDGDKVvlgPKAAQINTVLKGKpgTAMAAFGGQLNDVEIAAVISY 360
Cdd:pfam13442   1 AAAAAGEALYAANCASCHGTGGAG-----PSLAGRAL---PPEALVDIIRNGK--GAMPAFGGDLSDEELEALAAY 66
COX2_TM pfam02790
Cytochrome C oxidase subunit II, transmembrane domain; The N-terminal domain of cytochrome C ...
 34-112 8.99e-11

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: 57.73  E-value: 8.99e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428508  34 QLNLHEGVTQIARDVMWLHWMLLTICIVIFIGVFGVMFYSIWAHRKSRGHKAATFHEHlG--VEVAWTVIPFIIVIAMAL 111
Cdd:pfam02790   6 GLGFQDAASPLMEGLLELHDYIMFILTLILILVLYILVTCLIRFNRRKNPITARYTTH-GqtIEIIWTIIPAVILILIAL 84


                  .
gi 1337428508 112 P 112
Cdd:pfam02790  85 P 85
CytC553 COG2863
Cytochrome c553 [Energy production and conversion];
284-360 2.95e-10

Cytochrome c553 [Energy production and conversion];


Pssm-ID: 442110 [Multi-domain]  Cd Length: 98  Bit Score: 56.66  E-value: 2.95e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428508 284 AELVARGEKvFAANCVACHQANGKG-IPGSFPALDGdkvvLGPK--AAQINTVLKGK-PGTAMAAFGGQLNDVEIAAVIS 359
Cdd:COG2863    12 AGDAARGKA-YAAACAACHGADGEGnPGGGAPRLAG----QHAEylVAQLKAFRSGArKNGVMPAIAKGLSDEDIKALAA 86


                  .
gi 1337428508 360 Y 360
Cdd:COG2863    87 Y 87
ccoP TIGR00782
cytochrome c oxidase, cbb3-type, subunit III; This model describes a di-heme subunit of ...
 247-370 7.15e-10

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: 59.52  E-value: 7.15e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428508 247 MPIVVEVLAQADYDKWVEDQKKRMAASADDPnkewteaELVARGEKVFAANCVACHQANGKGIPG-SFPALDGDKVVLGP 325
Cdd:TIGR00782 170 MPAFGPLLEEADIKDVASYVMSLSSGKPKDE-------ALAAKGQELFADNCTTCHGEDGKGLQElGAPNLTDDVWLYGG 242

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1337428508 326 KAAQINTVLKGKPGTAMAAFGGQLNDVEIAAVISYTrhaWSNAGK 370
Cdd:TIGR00782 243 DLKTITTTITNGRGGVMPAWGPRLSEAQIKALAAYV---HSLGGG 284
ba3_CcO_II_C cd13913
C-terminal cupredoxin domain of Ba3-like heme-copper oxidase subunit II; The ba3 family of ...
 180-252 1.40e-09

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: 54.88  E-value: 1.40e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1337428508 180 NHMVVPVDKKVRVVLTAADVIHSWMIPDFGVKQDAIPGFLRDAWFRAEQPGIYRGQCAELCGKDHAFM--PIVVE 252
Cdd:cd13913    25 NEIEVPAGATVTFYVTSKDVIHGFEIAGTNVNVMVIPGQVSSVTYTFDKPGEYLIICNEYCGAGHHNMygKIIVE 99
thiosulf_SoxX TIGR04485
sulfur oxidation c-type cytochrome SoxX; Members of this family are SoxX, a c-type cytochrome ...
 297-360 7.78e-09

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


Pssm-ID: 275278 [Multi-domain]  Cd Length: 78  Bit Score: 52.20  E-value: 7.78e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1337428508 297 NCVACHQANGKGI-PGSF-PALDGDKVVLGPKA---AQINTVLKGKPGTAMAAFG--GQLNDVEIAAVISY 360
Cdd:TIGR04485   4 NCLACHQIPGSEVfPGNIgPSLTGYGARYPDEAylrAKIADAKAVNPCTVMPRFGknGILTEQEIEDVVAY 74
CuRO_UO_II cd04212
The cupredoxin domain of Ubiquinol oxidase subunit II; Ubiquinol oxidase, the terminal oxidase ...
 128-254 2.43e-08

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: 51.39  E-value: 2.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428508 128 LTVKVTGYQWKWGYEYLDGSAAGVkflstlstpraqienrepkgqfylmevdNHMVVPVDKKVRVVLTAADVIHSWMIPD 207
Cdd:cd04212     1 LEIQVVSLDWKWLFIYPEQGIATV----------------------------NELVIPVGRPVNFRLTSDSVMNSFFIPQ 52

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1337428508 208 FGVKQDAIPGFLRDAWFRAEQPGIYRGQCAELCGKDHAFMPIVVEVL 254
Cdd:cd04212    53 LGGQIYAMAGMQTQLHLIADKPGTYQGLSANYSGEGFSDMKFKVLAV 99
petJ CHL00183
cytochrome c553; Provisional
 282-360 3.58e-08

cytochrome c553; Provisional


Pssm-ID: 177085  Cd Length: 108  Bit Score: 50.93  E-value: 3.58e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428508 282 TEAELVARGEKVFAANCVACHqANGKGipgsfpALDGDKvVLGPKA----------AQINTVLKGKpgTAMAAFGGQLND 351
Cdd:CHL00183   21 AFAADLDNGEQIFSANCAACH-AGGNN------VIMPEK-TLKKDAleansmnsieAITYQVTNGK--NAMPAFGGRLSD 90


                  ....*....
gi 1337428508 352 VEIAAVISY 360
Cdd:CHL00183   91 EDIEDVANY 99
PetJ COG5677
Cytochrome c6 [Energy production and conversion];
284-360 5.47e-08

Cytochrome c6 [Energy production and conversion];


Pssm-ID: 444391 [Multi-domain]  Cd Length: 112  Bit Score: 50.65  E-value: 5.47e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428508 284 AELVARGEKVFAANCVACHqANGKGI--PG---SFPALdgDKVVLGPKAAQINTVLKGKPgtAMAAFGGQLNDVEIAAVI 358
Cdd:COG5677    25 AADLANGAKIFSANCAGCH-IGGGNIirRGktlKKEAL--EKYGMDSLEAIATQVTNGKN--AMPAFKDRLSEEQIEDVA 99


                  ..
gi 1337428508 359 SY 360
Cdd:COG5677   100 AY 101
Cyc7 COG3474
Cytochrome c2 [Energy production and conversion];
287-360 1.90e-07

Cytochrome c2 [Energy production and conversion];


Pssm-ID: 442697 [Multi-domain]  Cd Length: 101  Bit Score: 48.73  E-value: 1.90e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428508 287 VARGEKVFAANCVACHQANGKGIPGSFPALDGdkvVLGPKAAQI-----NTVLKGK--------------------PGTA 341
Cdd:COG3474     3 AAAGEKLFNRKCAACHSVDGGAGNRVGPNLNG---VVGRKAGSVegfaySDALKASglvwdeetldawladpkafvPGTK 79

                          90
                  ....*....|....*....
gi 1337428508 342 MaAFGGQLNDVEIAAVISY 360
Cdd:COG3474    80 M-PFAGLKDPEDRADLIAY 97
PRK13697 PRK13697
cytochrome c6; Provisional
 284-360 3.56e-07

cytochrome c6; Provisional


Pssm-ID: 184253 [Multi-domain]  Cd Length: 111  Bit Score: 48.24  E-value: 3.56e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428508 284 AELVARGEKVFAANCVACHqANGKGIPGSFPAL---DGDKVVLGPKAAQINTVLKGKpgTAMAAFGGQLNDVEIAAVISY 360
Cdd:PRK13697   25 AADAANGEQVFSANCASCH-AGGKNLVNAGKTLkkaDLEKYGMYSLEAITAQVTNGK--NAMPAFKDRLSPDQIEDVAAY 101
PRK14486 PRK14486
putative bifunctional cbb3-type cytochrome c oxidase subunit II/cytochrome c; Provisional
 267-362 4.90e-07

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


Pssm-ID: 184704 [Multi-domain]  Cd Length: 294  Bit Score: 50.97  E-value: 4.90e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428508 267 KKRMAASADDPNKEWTEAELVARGEKVFAANCVACHQANGKGIPGsfPALDGDKVVLGPKAAQINTVLKGKPGTAMAAFG 346
Cdd:PRK14486  195 AGGAEVDLELPNPFATDVAAIAKGKALYDANCAACHGDEAQGQEG--VALNDIDDGDLPDAAYFGMIKGGSDAKGMPGFG 272

                          90
                  ....*....|....*.
gi 1337428508 347 GQLNDVEIAAVISYTR 362
Cdd:PRK14486  273 GDLSDDDIWAIVAYIR 288
PRK10525 PRK10525
cytochrome o ubiquinol oxidase subunit II; Provisional
 54-268 6.05e-07

cytochrome o ubiquinol oxidase subunit II; Provisional


Pssm-ID: 182518 [Multi-domain]  Cd Length: 315  Bit Score: 50.57  E-value: 6.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428508  54 MLLTICIVIFIGVFGVMFYSI---WAHRKSrgHKAATF-----HEHLGVEVAWTViPFIIVIAMALPATKTVVAMK---- 121
Cdd:PRK10525   43 LILTAFGLMLIVVIPAILMAVgfaWKYRAS--NKDAKYspnwsHSNKVEAVVWTV-PILIIIFLAVLTWKTTHALEpskp 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428508 122 -DTSSADLTVKVTGYQWKWGYEYLDGSAAGVkflstlstpraqienrepkgqfylmevdNHMVVPVDKKVRVVLTAADVI 200
Cdd:PRK10525  120 lAHDEKPITIEVVSMDWKWFFIYPEQGIATV----------------------------NEIAFPANVPVYFKVTSNSVM 171

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1337428508 201 HSWMIPDFGVKQDAIPGFLRDAWFRAEQPGIYRGQCAELCGKDHAFMPI-VVEVLAQADYDKWVEDQKK 268
Cdd:PRK10525  172 NSFFIPRLGSQIYAMAGMQTRLHLIANEPGTYDGISASYSGPGFSGMKFkAIATPDRAEFDQWVAKAKQ 240
CuRO_HCO_II_like_1 cd13916
Uncharacterized subfamily with similarity to Heme-copper oxidase subunit II cupredoxin domain; ...
 129-247 5.40e-06

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: 44.29  E-value: 5.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428508 129 TVKVTGYQWKWgyeyldgsaagvkflsTLSTPraqienrepkgqfylmevdnhmVVPVDKKVRVVLTAADVIHSWMI--P 206
Cdd:cd13916     2 VVAVTGHQWYW----------------ELSRT----------------------EIPAGKPVEFRVTSADVNHGFGIydP 43

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1337428508 207 DFG-VKQ-DAIPGFLRDAWFRAEQPGIYRGQCAELCGKDHAFM 247
Cdd:cd13916    44 DMRlLAQtQAMPGYTNVLRYTFDKPGTYTILCLEYCGLAHHVM 86
ccoP TIGR00782
cytochrome c oxidase, cbb3-type, subunit III; This model describes a di-heme subunit of ...
 257-362 1.98e-05

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: 46.04  E-value: 1.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428508 257 ADYDKWVED-QKKRMAASADDPNKEWTE----AELV----ARGEKVFAANCVACHQANGKGIPGsFPALDGDKVVLGPKA 327
Cdd:TIGR00782  68 SQVEEEIKKfNEKNAAKWAKLAQTPLEDiakdPELKqyarNAGAAIFRTWCAQCHGSGAGGAKG-FPNLLDNDWLWGGTL 146

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1337428508 328 AQINTVLK------GKPGTA---MAAFGGQLNDVEIAAVISYTR 362
Cdd:TIGR00782 147 EGIHTTIKhgirdpDDGDTYvgeMPAFGPLLEEADIKDVASYVM 190
N2OR_C cd04223
The C-terminal cupredoxin domain of Nitrous-oxide reductase; Nitrous-oxide reductase ...
 180-247 2.02e-03

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: 37.21  E-value: 2.02e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1337428508 180 NHMVVPVDKKVRVVLT----AADVIHSWMIPDFGVKQDAIPGFLRDAWFRAEQPGIYRGQCAELCGKDHAFM 247
Cdd:cd04223    16 DIIEVKEGDEVTVHLTnleqDEDITHGFAIPGYNVNLSLEPGETATVTFVADKPGVYPYYCTEFCSALHLEM 87
CxxCH_TIGR02603 TIGR02603
putative heme-binding domain, Pirellula/Verrucomicrobium type; This model represents a domain ...
 287-310 7.17e-03

putative heme-binding domain, Pirellula/Verrucomicrobium type; This model represents a domain limited to very few species but expanded into large paralogous families in some species that conain it. We find it in over 20 copies each in Pirellula sp. strain 1 (phylum Planctomycetes) and Verrucomicrobium spinosum DSM 4136 (phylum Verrucomicrobia), and no matches above trusted cutoff an any other species so far. This domain, about 140 amino acids long, contains an absolutely conserved motif CxxCH, the cytochrome c family heme-binding site signature (PS00190).


Pssm-ID: 274224  Cd Length: 133  Bit Score: 36.57  E-value: 7.17e-03
                          10        20
                  ....*....|....*....|....
gi 1337428508 287 VARGEKVFAANCVACHQANGKGIP 310
Cdd:TIGR02603   3 AARGKAVFAKVCYLCHRIGGQGVD 26
Cupredoxin_1 pfam13473
Cupredoxin-like domain; The cupredoxin-like fold consists of a beta-sandwich with 7 strands in ...
 153-233 9.97e-03

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: 35.25  E-value: 9.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1337428508 153 FLSTLSTPRAQIENREPK-----GQFYLMEVdnhmVVPVDKKVRVVLTAAD-VIHSWMIPDFGVKQDAIPGFLRDAWFRA 226
Cdd:pfam13473   7 VLFWLSKPAAAADDPTVEitvkdGGFSPSRI----TVPAGTPVKLEFKNKDkTPAEFESPDLGIEKVLAPGKTSTITIPP 82


                  ....*..
gi 1337428508 227 EQPGIYR 233
Cdd:pfam13473  83 LKPGEYD 89
 
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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