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Conserved domains on  [gi|1833819252|gb|QJD07184|]
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cytochrome c oxidase subunit I [Apicomplexa sp. corallicolid ex Leiopathes glaberrima]

Protein Classification

heme-copper oxidase family protein( domain architecture ID 14)

heme-copper oxidase family protein may catalyze the transfer of electrons from an electron donor onto molecular oxygen

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Heme_Cu_Oxidase_I super family cl00275
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 24-487 4.40e-171

Heme-copper oxidase subunit I. 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 three to five in bacteria and up to 13 in mammalian mitochondria. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria. Membership in the superfamily is defined by subunit I, which contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme and a copper ion. It also contains a low-spin heme, believed to participate in the transfer of electrons to the binuclear center. Only subunit I is common to the entire superfamily. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from the electron donor on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I of cytochrome c oxidase (CcO) and ubiquinol oxidase. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electron transfer occurs in two segments: from the electron donor to the low-spin heme, and from the low-spin heme to the binuclear center. The first segment can be a multi-step process and varies among the different families, while the second segment, a direct transfer, is consistent throughout the superfamily.


The actual alignment was detected with superfamily member cd01663:

Pssm-ID: 469701  Cd Length: 488  Bit Score: 490.84  E-value: 4.40e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252  24 CNHKVLGLYYIWLAFIFGISGSLASMVLRLELYTSGLRLITPEnqnFYNLTFTLHGLIMIFFTIMPGLYGGFGNYLIPIY 103
Cdd:cd01663     1 TNHKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQ---LYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLM 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 104 NGAPEVAFPRINSVSLLLLPISFGCVLLSTTAEFGGGSGWTLYPPLStSLMSLSPVSMDVIVLGLLLAGISTFLSSLNFI 183
Cdd:cd01663    78 IGAPDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLS-SILAHSGPSVDLAIFSLHLAGISSILGAINFI 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 184 TTIFHIRAKGFALGSLVFNTWGIVFTAAMLILTLPVLTAGLLMLITDLHLNTQFYDPVFSGDPVLYQHLFWFFGHPEVYV 263
Cdd:cd01663   157 TTIFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYI 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 264 LIIPGFGLISQVISTnFS--KIIFGNVTMILALGCISTLGSVVWAHHMITVGLEVDTRAYFTAVTILISLPTGTKIFNWL 341
Cdd:cd01663   237 LILPGFGIISHIIST-FSgkKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWL 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 342 STYMGSnnKITMSSTLLALS-FLLLFTLGGTTGVVLGNAAVDVSLHDTYYVVAHFHFVLSLGAIIALFTGFIFFQETFFG 420
Cdd:cd01663   316 ATMWGG--SIKFETPMLWALgFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITG 393

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1833819252 421 TQLALNSVLILWGLIFVaGIMISFVPLHILGFNVMPRRIPDYPDSLNYLNSISSIGSLVTFLSLLIL 487
Cdd:cd01663   394 LSYNETLGKIHFWLMFI-GVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLF 459
 
Name Accession Description Interval E-value
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 24-487 4.40e-171

Cytochrome C oxidase subunit I. 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, but subunit III, which is also conserved, may play a role in assembly or oxygen delivery to the active site. 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 I contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme (heme a3) and a copper ion (CuB). It also contains a low-spin heme (heme a), believed to participate in the transfer of electrons to the binuclear center. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from cytochrome c on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electrons are transferred from cytochrome c (the electron donor) to heme a via the CuA binuclear site in subunit II, and directly from heme a to the binuclear center.


Pssm-ID: 238833  Cd Length: 488  Bit Score: 490.84  E-value: 4.40e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252  24 CNHKVLGLYYIWLAFIFGISGSLASMVLRLELYTSGLRLITPEnqnFYNLTFTLHGLIMIFFTIMPGLYGGFGNYLIPIY 103
Cdd:cd01663     1 TNHKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQ---LYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLM 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 104 NGAPEVAFPRINSVSLLLLPISFGCVLLSTTAEFGGGSGWTLYPPLStSLMSLSPVSMDVIVLGLLLAGISTFLSSLNFI 183
Cdd:cd01663    78 IGAPDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLS-SILAHSGPSVDLAIFSLHLAGISSILGAINFI 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 184 TTIFHIRAKGFALGSLVFNTWGIVFTAAMLILTLPVLTAGLLMLITDLHLNTQFYDPVFSGDPVLYQHLFWFFGHPEVYV 263
Cdd:cd01663   157 TTIFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYI 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 264 LIIPGFGLISQVISTnFS--KIIFGNVTMILALGCISTLGSVVWAHHMITVGLEVDTRAYFTAVTILISLPTGTKIFNWL 341
Cdd:cd01663   237 LILPGFGIISHIIST-FSgkKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWL 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 342 STYMGSnnKITMSSTLLALS-FLLLFTLGGTTGVVLGNAAVDVSLHDTYYVVAHFHFVLSLGAIIALFTGFIFFQETFFG 420
Cdd:cd01663   316 ATMWGG--SIKFETPMLWALgFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITG 393

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1833819252 421 TQLALNSVLILWGLIFVaGIMISFVPLHILGFNVMPRRIPDYPDSLNYLNSISSIGSLVTFLSLLIL 487
Cdd:cd01663   394 LSYNETLGKIHFWLMFI-GVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLF 459
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 23-486 1.49e-152

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 444.42  E-value: 1.49e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252  23 SCNHKVLGLYYIWLAFIFGISGSLASMVLRLELYTSGLRLITPEnqnFYNLTFTLHGLIMIFFTIMPGLYGGFGNYLIPI 102
Cdd:MTH00223    6 STNHKDIGTLYLIFGMWSGLVGTSLSLLIRAELGQPGALLGDDQ---LYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 103 YNGAPEVAFPRINSVSLLLLPISFGCVLLSTTAEFGGGSGWTLYPPLStSLMSLSPVSMDVIVLGLLLAGISTFLSSLNF 182
Cdd:MTH00223   83 MLGAPDMAFPRLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLS-SNLAHAGPSVDLAIFSLHLAGVSSILGAINF 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 183 ITTIFHIRAKGFALGSLVFNTWGIVFTAAMLILTLPVLTAGLLMLITDLHLNTQFYDPVFSGDPVLYQHLFWFFGHPEVY 262
Cdd:MTH00223  162 ITTIINMRSPGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVY 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 263 VLIIPGFGLISQVISTNFSKI-IFGNVTMILALGCISTLGSVVWAHHMITVGLEVDTRAYFTAVTILISLPTGTKIFNWL 341
Cdd:MTH00223  242 ILILPGFGMISHIVSHYSSKKeVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWL 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 342 STYMGSNNKITmSSTLLALSFLLLFTLGGTTGVVLGNAAVDVSLHDTYYVVAHFHFVLSLGAIIALFTGFIFFQETFfgT 421
Cdd:MTH00223  322 ATIYGSKIKYE-APMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLF--T 398

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1833819252 422 QLALNSVlilWG----LIFVAGIMISFVPLHILGFNVMPRRIPDYPDSLNYLNSISSIGSLVTFLSLLI 486
Cdd:MTH00223  399 GVTLHRR---WAkahfFLMFLGVNLTFFPQHFLGLAGMPRRYSDYPDCYTKWNQVSSFGSMISFVSVLF 464
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 22-487 1.57e-127

cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) of cytochrome c oxidases of bacterial origin. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits I-III form the functional core of the enzyme complex. Subunit I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit II and heme a of subunit I to the bimetallic center formed by heme a3 and copper B. This cytochrome c oxidase shows proton pump activity across the membrane in addition to the electron transfer. In the bacilli an apparent split (paralogism) has created a sister clade (TIGR02882) encoding subunits (QoxA) of the aa3-type quinone oxidase complex which reacts directly with quinones, bypassing the interaction with soluble cytochrome c. This model attempts to exclude these sequences, placing them between the trusted and noise cutoffs. These families, as well as archaeal and eukaryotic cytochrome c subunit I's are included within the superfamily model, pfam00115. [Energy metabolism, Electron transport]


Pssm-ID: 213748  Cd Length: 499  Bit Score: 380.03  E-value: 1.57e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252  22 SSCNHKVLGLYYIWLAFIFGISGSLASMVLRLELYTSGLRLITPEnqnFYNLTFTLHGLIMIFFTIMPgLYGGFGNYLIP 101
Cdd:TIGR02891   2 TTVDHKRIGILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDAE---TYNQLFTMHGTIMIFLFAIP-ILAGFGNYLLP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 102 IYNGAPEVAFPRINSVSLLLLPisFGCVLLSTTAEFGGG--SGWTLYPPLSTSLMSlSPVSMDVIVLGLLLAGISTFLSS 179
Cdd:TIGR02891  78 LMIGARDMAFPRLNAFSYWLYL--FGGLLLLASFFTGGApdTGWTMYPPLSSTSGS-PGVGVDLWLLGLHLLGISSILGA 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 180 LNFITTIFHIRAKGFALGSLVFNTWGIVFTAAMLILTLPVLTAGLLMLITDLHLNTQFYDPVFSGDPVLYQHLFWFFGHP 259
Cdd:TIGR02891 155 VNFIVTILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHP 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 260 EVYVLIIPGFGLISQVISTNFSKIIFGNVTMILALGCISTLGSVVWAHHMITVGLEVDTRAYFTAVTILISLPTGTKIFN 339
Cdd:TIGR02891 235 EVYIIFLPAFGIISEILPTFARKPIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFN 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 340 WLSTYMGSNNKITmSSTLLALSFLLLFTLGGTTGVVLGNAAVDVSLHDTYYVVAHFHFVLSLGAIIALFTGFIFFQETFF 419
Cdd:TIGR02891 315 WIATLWGGSIRFT-TPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVT 393

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 420 GTQLALNSVLILWGLIFVaGIMISFVPLHILGFNVMPRRIPDYPDSLNY--LNSISSIGSLVTFLSLLIL 487
Cdd:TIGR02891 394 GRMYNERLGRWHFWLTFV-GFNLTFFPMHLLGLLGMPRRYYTYPPQMGFatLNLISTIGAFILAAGFLVF 462
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
21-487 5.86e-127

Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];


Pssm-ID: 440605  Cd Length: 535  Bit Score: 379.86  E-value: 5.86e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252  21 ISSCNHKVLGLYYIWLAFIFGISGSLASMVLRLELYTSGLRLITPEnqnFYNLTFTLHGLIMIFFTIMPGLyGGFGNYLI 100
Cdd:COG0843    10 LTTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPE---TYNQLFTMHGTIMIFFFATPFL-AGFGNYLV 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 101 PIYNGAPEVAFPRINSVSLLLLPISFGCVLLSTTAEFGGGSGWTLYPPLSTSLMSlSPVSMDVIVLGLLLAGISTFLSSL 180
Cdd:COG0843    86 PLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEAS-PGVGVDLWLLGLALFGVGSILGGV 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 181 NFITTIFHIRAKGFALGSLVFNTWGIVFTAAMLILTLPVLTAGLLMLITDLHLNTQFYDPVFSGDPVLYQHLFWFFGHPE 260
Cdd:COG0843   165 NFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPE 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 261 VYVLIIPGFGLISQVISTNFSKIIFGNVTMILALGCISTLGSVVWAHHMITVGLEVDTRAYFTAVTILISLPTGTKIFNW 340
Cdd:COG0843   245 VYILILPAFGIVSEIIPTFSRKPLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNW 324

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 341 LST-YMGsnnKITMSS-TLLALSFLLLFTLGGTTGVVLGNAAVDVSLHDTYYVVAHFHFVLSLGAIIALFTGFIFFQETF 418
Cdd:COG0843   325 IATmWRG---RIRFTTpMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKM 401

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1833819252 419 FGTQLALNSVLILWGLIFVaGIMISFVPLHILGFNVMPRRIPDYPDSLNY--LNSISSIGSLVTFLSLLIL 487
Cdd:COG0843   402 TGRMLNERLGKIHFWLWFI-GFNLTFFPMHILGLLGMPRRYATYPPEPGWqpLNLISTIGAFILAVGFLLF 471
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 28-479 8.27e-93

Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key enzyme in aerobic metabolism. Proton pumping haem-copper oxidases represent the terminal, energy-transfer enzymes of respiratory chains in prokaryotes and eukaryotes. The CuB-haem a3 (or haem o) binuclear centre, associated with the largest subunit I of cytochrome c and ubiquinol oxidases (E.C:1.10.3.11), is directly involved in the coupling between dioxygen reduction and proton pumping. Some terminal oxidases generate a transmembrane proton gradient across the plasma membrane (prokaryotes) or the mitochondrial inner membrane (eukaryotes). The enzyme complex consists of 3-4 subunits (prokaryotes) up to 13 polypeptides (mammals) of which only the catalytic subunit (equivalent to mammalian subunit I (COXI) is found in all haem-copper respiratory oxidases. The presence of a bimetallic centre (formed by a high-spin haem and copper B) as well as a low-spin haem, both ligated to six conserved histidine residues near the outer side of four transmembrane spans within CO I is common to all family members.


Pssm-ID: 459678  Cd Length: 432  Bit Score: 288.70  E-value: 8.27e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252  28 VLGLYYIWLAFIFGISGSLASMVLRLELYTSGLRLITPEnqnFYNLTFTLHGLIMIFFTIMPGLyGGFGNYLIPIYNGAP 107
Cdd:pfam00115   1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPL---TYNQLRTLHGNLMIFWFATPFL-FGFGNYLVPLMIGAR 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 108 EVAFPRINSVSLLLLPISFGCVLLSTTaefGGGSGWTLYPPLstslmslspVSMDVIVLGLLLAGISTFLSSLNFITTIF 187
Cdd:pfam00115  77 DMAFPRLNALSFWLVVLGAVLLLASFG---GATTGWTEYPPL---------VGVDLWYIGLLLAGVSSLLGAINFIVTIL 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 188 HIRAKGFALGSLVFnTWGIVFTAAMLILTLPVLTAGLLMLITDLHLNTqfydpvFSGDPVLYQHLFWFFGHPEVYVLIIP 267
Cdd:pfam00115 145 KRRAPGMTLRMPLF-VWAILATAILILLAFPVLAAALLLLLLDRSLGA------GGGDPLLDQHLFWWFGHPEVYILILP 217

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 268 GFGLISQVISTNFSKIIFGNVTMILALGCISTLGSVVWAHHMITVGLEVDTRAYFTAVTILISLPTGTKIFNWLSTYMGS 347
Cdd:pfam00115 218 AFGIIYYILPKFAGRPLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGG 297

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 348 NNKITMSSTLLALSFLLLFTLGGTTGVVLGNAAVDVSLHDTYYVVAHFHFVLSLGAIIALFTGFIFFQETFFGTQLALNS 427
Cdd:pfam00115 298 WIRFRTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKL 377

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1833819252 428 VLILWGLIFVaGIMISFVPLHILGFNVMPRRIP----DYPDSLNYLNSISSIGSLV 479
Cdd:pfam00115 378 GKLHFWLLFI-GFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPLNWIRTIGGVL 432
 
Name Accession Description Interval E-value
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 24-487 4.40e-171

Cytochrome C oxidase subunit I. 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, but subunit III, which is also conserved, may play a role in assembly or oxygen delivery to the active site. 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 I contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme (heme a3) and a copper ion (CuB). It also contains a low-spin heme (heme a), believed to participate in the transfer of electrons to the binuclear center. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from cytochrome c on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electrons are transferred from cytochrome c (the electron donor) to heme a via the CuA binuclear site in subunit II, and directly from heme a to the binuclear center.


Pssm-ID: 238833  Cd Length: 488  Bit Score: 490.84  E-value: 4.40e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252  24 CNHKVLGLYYIWLAFIFGISGSLASMVLRLELYTSGLRLITPEnqnFYNLTFTLHGLIMIFFTIMPGLYGGFGNYLIPIY 103
Cdd:cd01663     1 TNHKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQ---LYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLM 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 104 NGAPEVAFPRINSVSLLLLPISFGCVLLSTTAEFGGGSGWTLYPPLStSLMSLSPVSMDVIVLGLLLAGISTFLSSLNFI 183
Cdd:cd01663    78 IGAPDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLS-SILAHSGPSVDLAIFSLHLAGISSILGAINFI 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 184 TTIFHIRAKGFALGSLVFNTWGIVFTAAMLILTLPVLTAGLLMLITDLHLNTQFYDPVFSGDPVLYQHLFWFFGHPEVYV 263
Cdd:cd01663   157 TTIFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYI 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 264 LIIPGFGLISQVISTnFS--KIIFGNVTMILALGCISTLGSVVWAHHMITVGLEVDTRAYFTAVTILISLPTGTKIFNWL 341
Cdd:cd01663   237 LILPGFGIISHIIST-FSgkKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWL 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 342 STYMGSnnKITMSSTLLALS-FLLLFTLGGTTGVVLGNAAVDVSLHDTYYVVAHFHFVLSLGAIIALFTGFIFFQETFFG 420
Cdd:cd01663   316 ATMWGG--SIKFETPMLWALgFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITG 393

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1833819252 421 TQLALNSVLILWGLIFVaGIMISFVPLHILGFNVMPRRIPDYPDSLNYLNSISSIGSLVTFLSLLIL 487
Cdd:cd01663   394 LSYNETLGKIHFWLMFI-GVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLF 459
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 23-486 1.49e-152

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 444.42  E-value: 1.49e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252  23 SCNHKVLGLYYIWLAFIFGISGSLASMVLRLELYTSGLRLITPEnqnFYNLTFTLHGLIMIFFTIMPGLYGGFGNYLIPI 102
Cdd:MTH00223    6 STNHKDIGTLYLIFGMWSGLVGTSLSLLIRAELGQPGALLGDDQ---LYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 103 YNGAPEVAFPRINSVSLLLLPISFGCVLLSTTAEFGGGSGWTLYPPLStSLMSLSPVSMDVIVLGLLLAGISTFLSSLNF 182
Cdd:MTH00223   83 MLGAPDMAFPRLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLS-SNLAHAGPSVDLAIFSLHLAGVSSILGAINF 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 183 ITTIFHIRAKGFALGSLVFNTWGIVFTAAMLILTLPVLTAGLLMLITDLHLNTQFYDPVFSGDPVLYQHLFWFFGHPEVY 262
Cdd:MTH00223  162 ITTIINMRSPGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVY 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 263 VLIIPGFGLISQVISTNFSKI-IFGNVTMILALGCISTLGSVVWAHHMITVGLEVDTRAYFTAVTILISLPTGTKIFNWL 341
Cdd:MTH00223  242 ILILPGFGMISHIVSHYSSKKeVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWL 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 342 STYMGSNNKITmSSTLLALSFLLLFTLGGTTGVVLGNAAVDVSLHDTYYVVAHFHFVLSLGAIIALFTGFIFFQETFfgT 421
Cdd:MTH00223  322 ATIYGSKIKYE-APMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLF--T 398

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1833819252 422 QLALNSVlilWG----LIFVAGIMISFVPLHILGFNVMPRRIPDYPDSLNYLNSISSIGSLVTFLSLLI 486
Cdd:MTH00223  399 GVTLHRR---WAkahfFLMFLGVNLTFFPQHFLGLAGMPRRYSDYPDCYTKWNQVSSFGSMISFVSVLF 464
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 23-487 4.13e-152

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 443.16  E-value: 4.13e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252  23 SCNHKVLGLYYiwlaFIFGI----SGSLASMVLRLELYTSGLrLITpeNQNFYNLTFTLHGLIMIFFTIMPGLYGGFGNY 98
Cdd:MTH00153    7 STNHKDIGTLY----FIFGAwsgmVGTSLSLLIRAELGQPGS-LIG--DDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNW 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252  99 LIPIYNGAPEVAFPRINSVSLLLLPISFGCVLLSTTAEFGGGSGWTLYPPLStSLMSLSPVSMDVIVLGLLLAGISTFLS 178
Cdd:MTH00153   80 LVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLS-SNIAHSGASVDLAIFSLHLAGISSILG 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 179 SLNFITTIFHIRAKGFALGSLVFNTWGIVFTAAMLILTLPVLTAGLLMLITDLHLNTQFYDPVFSGDPVLYQHLFWFFGH 258
Cdd:MTH00153  159 AINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGH 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 259 PEVYVLIIPGFGLISQVISTNFSKI-IFGNVTMILALGCISTLGSVVWAHHMITVGLEVDTRAYFTAVTILISLPTGTKI 337
Cdd:MTH00153  239 PEVYILILPGFGMISHIISQESGKKeTFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKI 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 338 FNWLSTYMGSNNKITmSSTLLALSFLLLFTLGGTTGVVLGNAAVDVSLHDTYYVVAHFHFVLSLGAIIALFTGFIFFQET 417
Cdd:MTH00153  319 FSWLATLHGSQINYS-PSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPL 397

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 418 FFGTQLALNSVLILWGLIFVaGIMISFVPLHILGFNVMPRRIPDYPDSLNYLNSISSIGSLVTFLSLLIL 487
Cdd:MTH00153  398 FTGLTMNPKWLKIQFFIMFI-GVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFF 466
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 23-487 2.00e-145

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 426.40  E-value: 2.00e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252  23 SCNHKVLGLYYiwlaFIFGI----SGSLASMVLRLELYTSGLRLitpENQNFYNLTFTLHGLIMIFFTIMPGLYGGFGNY 98
Cdd:MTH00167    9 STNHKDIGTLY----FIFGAwagmVGTALSLLIRAELSQPGSLL---GDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNW 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252  99 LIPIYNGAPEVAFPRINSVSLLLLPISFGCVLLSTTAEFGGGSGWTLYPPLSTSLMSLSPvSMDVIVLGLLLAGISTFLS 178
Cdd:MTH00167   82 LVPLMIGAPDMAFPRMNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGA-SVDLAIFSLHLAGVSSILG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 179 SLNFITTIFHIRAKGFALGSLVFNTWGIVFTAAMLILTLPVLTAGLLMLITDLHLNTQFYDPVFSGDPVLYQHLFWFFGH 258
Cdd:MTH00167  161 SINFITTIINMKPPGITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGH 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 259 PEVYVLIIPGFGLISQVISTNFSK-IIFGNVTMILALGCISTLGSVVWAHHMITVGLEVDTRAYFTAVTILISLPTGTKI 337
Cdd:MTH00167  241 PEVYILILPGFGMISHIVVYYSGKkEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKV 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 338 FNWLSTYMGSNNKItMSSTLLALSFLLLFTLGGTTGVVLGNAAVDVSLHDTYYVVAHFHFVLSLGAIIALFTGFIFFQET 417
Cdd:MTH00167  321 FSWLATLHGGKIKW-ETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPL 399

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 418 FFGTQLALNSVLILWGLIFVaGIMISFVPLHILGFNVMPRRIPDYPDSLNYLNSISSIGSLVTFLSLLIL 487
Cdd:MTH00167  400 FTGLTLNETWTKIHFFVMFI-GVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNVVSSIGSLISLVAVILF 468
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 23-487 9.36e-141

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 414.49  E-value: 9.36e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252  23 SCNHKVLGLYYIWLAFIFGISGSLASMVLRLELYTSGLRLitpENQNFYNLTFTLHGLIMIFFTIMPGLYGGFGNYLIPI 102
Cdd:MTH00116    9 STNHKDIGTLYLIFGAWAGMVGTALSLLIRAELGQPGTLL---GDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 103 YNGAPEVAFPRINSVSLLLLPISFGCVLLSTTAEFGGGSGWTLYPPLSTSLMSLSPvSMDVIVLGLLLAGISTFLSSLNF 182
Cdd:MTH00116   86 MIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGA-SVDLAIFSLHLAGVSSILGAINF 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 183 ITTIFHIRAKGFALGSLVFNTWGIVFTAAMLILTLPVLTAGLLMLITDLHLNTQFYDPVFSGDPVLYQHLFWFFGHPEVY 262
Cdd:MTH00116  165 ITTCINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVY 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 263 VLIIPGFGLISQVIsTNFS--KIIFGNVTMILALGCISTLGSVVWAHHMITVGLEVDTRAYFTAVTILISLPTGTKIFNW 340
Cdd:MTH00116  245 ILILPGFGIISHIV-TYYAgkKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSW 323

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 341 LSTYMGSNNKITmSSTLLALSFLLLFTLGGTTGVVLGNAAVDVSLHDTYYVVAHFHFVLSLGAIIALFTGFIFFQETFFG 420
Cdd:MTH00116  324 LATLHGGTIKWD-PPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTG 402

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1833819252 421 TQLALNSVLILWGLIFVaGIMISFVPLHILGFNVMPRRIPDYPDSLNYLNSISSIGSLVTFLSLLIL 487
Cdd:MTH00116  403 YTLHQTWTKAQFGVMFT-GVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTISSIGSLISMTAVIML 468
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 21-487 2.16e-136

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 402.91  E-value: 2.16e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252  21 ISSCNHKVLGLYYIWLAFIFGISGSLASMVLRLELYTSGLRLItpeNQNFYNLTFTLHGLIMIFFTIMPGLYGGFGNYLI 100
Cdd:MTH00079    8 LESSNHKDIGTLYFLFGLWSGMVGTSLSLIIRLELSKPGLLLG---NGQLYNSVITAHAILMIFFMVMPSMIGGFGNWML 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 101 PIYNGAPEVAFPRINSVSLLLLPISFGCVLLSTTAEFGGGSGWTLYPPLSTslMSLSPVSMDVIVLGLLLAGISTFLSSL 180
Cdd:MTH00079   85 PLMLGAPDMSFPRLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLST--LGHPGSSVDLAIFSLHCAGISSILGGI 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 181 NFITTIFHIRAKGFALGSLVFNTWGIVFTAAMLILTLPVLTAGLLMLITDLHLNTQFYDPVFSGDPVLYQHLFWFFGHPE 260
Cdd:MTH00079  163 NFMVTTKNLRSSSISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPE 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 261 VYVLIIPGFGLISQVIST-NFSKIIFGNVTMILALGCISTLGSVVWAHHMITVGLEVDTRAYFTAVTILISLPTGTKIFN 339
Cdd:MTH00079  243 VYILILPAFGIISQSTLYlTGKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFS 322

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 340 WLSTYMGSNNKITmSSTLLALSFLLLFTLGGTTGVVLGNAAVDVSLHDTYYVVAHFHFVLSLGAIIALFTGFIFFQETFF 419
Cdd:MTH00079  323 WLATLFGMKMKFQ-PLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFMT 401

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1833819252 420 GTQLALNSVLILWGLIFVaGIMISFVPLHILGFNVMPRRIPDYPDSLNYLNSISSIGSLVTFLSLLIL 487
Cdd:MTH00079  402 GIVYDKLMMSAVFFLMFV-GVNLTFFPLHFAGLHGMPRKYLDYPDVYSVWNVISSYGSMISVFALFLF 468
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 26-487 3.47e-136

Heme-copper oxidase subunit I. 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 three to five in bacteria and up to 13 in mammalian mitochondria. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria. Membership in the superfamily is defined by subunit I, which contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme and a copper ion. It also contains a low-spin heme, believed to participate in the transfer of electrons to the binuclear center. Only subunit I is common to the entire superfamily. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from the electron donor on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I of cytochrome c oxidase (CcO) and ubiquinol oxidase. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electron transfer occurs in two segments: from the electron donor to the low-spin heme, and from the low-spin heme to the binuclear center. The first segment can be a multi-step process and varies among the different families, while the second segment, a direct transfer, is consistent throughout the superfamily.


Pssm-ID: 238461  Cd Length: 463  Bit Score: 400.75  E-value: 3.47e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252  26 HKVLGLYYIWLAFIFGISGSLASMVLRLELYTSGLRLITPEnqnFYNLTFTLHGLIMIFFTIMPGLYGGFGNYLIPIyNG 105
Cdd:cd00919     1 HKDIGLLYLIFAFVALLLGGLLALLIRLELATPGSLFLDPQ---LYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPPL-IG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 106 APEVAFPRINSVSLLLLPISFGCVLLSTTAEFGGGSGWTLYPPLSTSLMSlSPVSMDVIVLGLLLAGISTFLSSLNFITT 185
Cdd:cd00919    77 ARDLAFPRLNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYS-SGVGVDLAILGLHLAGVSSILGAINFITT 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 186 IFHIRAKGFALGSLVFNTWGIVFTAAMLILTLPVLTAGLLMLITDLHLNTQFYDPVFSGDPVLYQHLFWFFGHPEVYVLI 265
Cdd:cd00919   156 ILNMRAPGMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILI 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 266 IPGFGLISQVISTNFSKIIFGNVTMILALGCISTLGSVVWAHHMITVGLEVDTRAYFTAVTILISLPTGTKIFNWLSTYM 345
Cdd:cd00919   236 LPAFGAISEIIPTFSGKPLFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLW 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 346 GSNNKITMsSTLLALSFLLLFTLGGTTGVVLGNAAVDVSLHDTYYVVAHFHFVLSLGAIIALFTGFIFFQETFFGTQLAL 425
Cdd:cd00919   316 GGRIRFDP-PMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSE 394

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1833819252 426 NSVLILWGLIFVaGIMISFVPLHILGFNVMPRRIPDYPDSLNYLNSISSIGSLVTFLSLLIL 487
Cdd:cd00919   395 KLGKIHFWLWFI-GFNLTFFPMHFLGLLGMPRRYADYPDGFAPWNFISSVGAFILGLGLLLF 455
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 23-486 3.58e-135

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 399.87  E-value: 3.58e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252  23 SCNHKVLGLYYIWLAFIFGISGSLASMVLRLELYTSGLRLitpENQNFYNLTFTLHGLIMIFFTIMPGLYGGFGNYLIPI 102
Cdd:MTH00142    7 STNHKDIGTLYFLFGAWAGMVGTGLSLLIRAELGQPGSLL---GDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 103 YNGAPEVAFPRINSVSLLLLPISFGCVLLSTTAEFGGGSGWTLYPPLStSLMSLSPVSMDVIVLGLLLAGISTFLSSLNF 182
Cdd:MTH00142   84 MLGAPDMAFPRMNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLS-SNLAHSGGSVDLAIFSLHLAGVSSILGAINF 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 183 ITTIFHIRAKGFALGSLVFNTWGIVFTAAMLILTLPVLTAGLLMLITDLHLNTQFYDPVFSGDPVLYQHLFWFFGHPEVY 262
Cdd:MTH00142  163 ITTVINMRAGGMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVY 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 263 VLIIPGFGLISQVIsTNFS--KIIFGNVTMILALGCISTLGSVVWAHHMITVGLEVDTRAYFTAVTILISLPTGTKIFNW 340
Cdd:MTH00142  243 ILILPGFGMISHII-NHYSgkKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFSW 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 341 LSTYMGSNNKITmSSTLLALSFLLLFTLGGTTGVVLGNAAVDVSLHDTYYVVAHFHFVLSLGAIIALFTGFIFFQETFFG 420
Cdd:MTH00142  322 LATLHGSKVKYE-PPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLFTG 400

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1833819252 421 TQLALNSVLILWGLIFVaGIMISFVPLHILGFNVMPRRIPDYPDSLNYLNSISSIGSLVTFLSLLI 486
Cdd:MTH00142  401 LTLNPRWLKAHFYTMFI-GVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSSLGSMISFIAVLM 465
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 23-487 9.61e-130

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 386.20  E-value: 9.61e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252  23 SCNHKVLGLYYIWLAFIFGISGSLASMVLRLELYTSGLRLitpENQNFYNLTFTLHGLIMIFFTIMPGLYGGFGNYLIPI 102
Cdd:MTH00183    9 STNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGALL---GDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 103 YNGAPEVAFPRINSVSLLLLPISFGCVLLSTTAEFGGGSGWTLYPPLSTSLMSLSPvSMDVIVLGLLLAGISTFLSSLNF 182
Cdd:MTH00183   86 MIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGA-SVDLTIFSLHLAGVSSILGAINF 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 183 ITTIFHIRAKGFALGSLVFNTWGIVFTAAMLILTLPVLTAGLLMLITDLHLNTQFYDPVFSGDPVLYQHLFWFFGHPEVY 262
Cdd:MTH00183  165 ITTIINMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVY 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 263 VLIIPGFGLISQVIS-TNFSKIIFGNVTMILALGCISTLGSVVWAHHMITVGLEVDTRAYFTAVTILISLPTGTKIFNWL 341
Cdd:MTH00183  245 ILILPGFGMISHIVAyYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWL 324

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 342 STYMGSNNKITmSSTLLALSFLLLFTLGGTTGVVLGNAAVDVSLHDTYYVVAHFHFVLSLGAIIALFTGFIFFQETFFGT 421
Cdd:MTH00183  325 ATLHGGSIKWE-TPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLFSGY 403

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1833819252 422 QLALNSVLILWGLIFvAGIMISFVPLHILGFNVMPRRIPDYPDSLNYLNSISSIGSLVTFLSLLIL 487
Cdd:MTH00183  404 TLHSTWTKIHFGVMF-VGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMF 468
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 23-487 1.80e-129

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 385.41  E-value: 1.80e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252  23 SCNHKVLGLYYIWLAFIFGISGSLASMVLRLELYTSGLRLitpENQNFYNLTFTLHGLIMIFFTIMPGLYGGFGNYLIPI 102
Cdd:MTH00007    6 STNHKDIGTLYFILGVWGGLLGTSMSLLIRIELGQPGAFL---GSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 103 YNGAPEVAFPRINSVSLLLLPISFGCVLLSTTAEFGGGSGWTLYPPLSTSLMSLSPvSMDVIVLGLLLAGISTFLSSLNF 182
Cdd:MTH00007   83 MLGAPDMAFPRLNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGP-SVDLAIFSLHLAGVSSILGAINF 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 183 ITTIFHIRAKGFALGSLVFNTWGIVFTAAMLILTLPVLTAGLLMLITDLHLNTQFYDPVFSGDPVLYQHLFWFFGHPEVY 262
Cdd:MTH00007  162 ITTVINMRWKGLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 263 VLIIPGFGLISQVISTNFSKI-IFGNVTMILALGCISTLGSVVWAHHMITVGLEVDTRAYFTAVTILISLPTGTKIFNWL 341
Cdd:MTH00007  242 ILILPGFGAISHIVTHYAGKLePFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWL 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 342 STYMGSNNKiTMSSTLLALSFLLLFTLGGTTGVVLGNAAVDVSLHDTYYVVAHFHFVLSLGAIIALFTGFIFFQETFFGT 421
Cdd:MTH00007  322 ATIHGSPIK-YETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTGL 400

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1833819252 422 QLALNSVLILWGLIFVaGIMISFVPLHILGFNVMPRRIPDYPDSLNYLNSISSIGSLVTFLSLLIL 487
Cdd:MTH00007  401 TLHDRWAKAHFFLMFL-GVNLTFFPQHFLGLSGMPRRYSDYPDAYTKWNVVSSFGSMLSFVALLLF 465
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 23-487 4.02e-129

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 384.68  E-value: 4.02e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252  23 SCNHKVLGLYYIWLAFIFGISGSLASMVLRLELYTSGLRLitpENQNFYNLTFTLHGLIMIFFTIMPGLYGGFGNYLIPI 102
Cdd:MTH00077    9 STNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGTLL---GDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 103 YNGAPEVAFPRINSVSLLLLPISFGCVLLSTTAEFGGGSGWTLYPPLSTSLMSLSPvSMDVIVLGLLLAGISTFLSSLNF 182
Cdd:MTH00077   86 MIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGA-SVDLTIFSLHLAGVSSILGAINF 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 183 ITTIFHIRAKGFALGSLVFNTWGIVFTAAMLILTLPVLTAGLLMLITDLHLNTQFYDPVFSGDPVLYQHLFWFFGHPEVY 262
Cdd:MTH00077  165 ITTSINMKPPSMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVY 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 263 VLIIPGFGLISQVIS-TNFSKIIFGNVTMILALGCISTLGSVVWAHHMITVGLEVDTRAYFTAVTILISLPTGTKIFNWL 341
Cdd:MTH00077  245 ILILPGFGMISHIVTyYSAKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVFSWL 324

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 342 STYMGSNNKITmSSTLLALSFLLLFTLGGTTGVVLGNAAVDVSLHDTYYVVAHFHFVLSLGAIIALFTGFIFFQETFFGT 421
Cdd:MTH00077  325 ATMHGGAIKWD-AAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGY 403

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1833819252 422 QLALNSVLILWGLIFVaGIMISFVPLHILGFNVMPRRIPDYPDSLNYLNSISSIGSLVTFLSLLIL 487
Cdd:MTH00077  404 TLHSTWSKIHFGVMFI-GVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMM 468
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 23-487 4.33e-129

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 384.62  E-value: 4.33e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252  23 SCNHKVLGLYYIWLAFIFGISGSLASMVLRLELYTSGLRLitpENQNFYNLTFTLHGLIMIFFTIMPGLYGGFGNYLIPI 102
Cdd:MTH00103    9 STNHKDIGTLYLLFGAWAGMVGTALSLLIRAELGQPGTLL---GDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 103 YNGAPEVAFPRINSVSLLLLPISFGCVLLSTTAEFGGGSGWTLYPPLSTSLmSLSPVSMDVIVLGLLLAGISTFLSSLNF 182
Cdd:MTH00103   86 MIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNL-AHAGASVDLTIFSLHLAGVSSILGAINF 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 183 ITTIFHIRAKGFALGSLVFNTWGIVFTAAMLILTLPVLTAGLLMLITDLHLNTQFYDPVFSGDPVLYQHLFWFFGHPEVY 262
Cdd:MTH00103  165 ITTIINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVY 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 263 VLIIPGFGLISQVIS-TNFSKIIFGNVTMILALGCISTLGSVVWAHHMITVGLEVDTRAYFTAVTILISLPTGTKIFNWL 341
Cdd:MTH00103  245 ILILPGFGMISHIVTyYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWL 324

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 342 STYMGSNNKITmSSTLLALSFLLLFTLGGTTGVVLGNAAVDVSLHDTYYVVAHFHFVLSLGAIIALFTGFIFFQETFFGT 421
Cdd:MTH00103  325 ATLHGGNIKWS-PAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGY 403

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1833819252 422 QLALNSVLILWGLIFVaGIMISFVPLHILGFNVMPRRIPDYPDSLNYLNSISSIGSLVTFLSLLIL 487
Cdd:MTH00103  404 TLNDTWAKIHFTIMFV-GVNMTFFPQHFLGLSGMPRRYSDYPDAYTTWNTVSSMGSFISLTAVMLM 468
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 23-485 1.18e-128

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 383.79  E-value: 1.18e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252  23 SCNHKVLGLYYIWLAFIFGISGSLASMVLRLELYTSGLRLitpENQNFYNLTFTLHGLIMIFFTIMPGLYGGFGNYLIPI 102
Cdd:MTH00184   11 STNHKDIGTLYLLFGAFAGMIGTAFSMLIRLELSAPGSML---GDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 103 YNGAPEVAFPRINSVSLLLLPISFGCVLLSTTAEFGGGSGWTLYPPLStSLMSLSPVSMDVIVLGLLLAGISTFLSSLNF 182
Cdd:MTH00184   88 YIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLS-SIQAHSGGSVDMAIFSLHLAGISSILGAMNF 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 183 ITTIFHIRAKGFALGSLVFNTWGIVFTAAMLILTLPVLTAGLLMLITDLHLNTQFYDPVFSGDPVLYQHLFWFFGHPEVY 262
Cdd:MTH00184  167 ITTIFNMRAPGITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVY 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 263 VLIIPGFGLISQVIST-NFSKIIFGNVTMILALGCISTLGSVVWAHHMITVGLEVDTRAYFTAVTILISLPTGTKIFNWL 341
Cdd:MTH00184  247 ILILPGFGIISQIIPTfAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWI 326

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 342 STYMGSNNKITmSSTLLALSFLLLFTLGGTTGVVLGNAAVDVSLHDTYYVVAHFHFVLSLGAIIALFTGFIFFQETFFGT 421
Cdd:MTH00184  327 ATIFGGSLRLD-TPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGY 405

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1833819252 422 QLALNSVLILWGLIFVaGIMISFVPLHILGFNVMPRRIPDYPDSLNYLNSISSIGSLVTFLSLL 485
Cdd:MTH00184  406 CYNEVYGKIHFWLMFI-GVNLTFFPQHFLGLAGLPRRYSDFHDSFAGWNQISSLGSVISIVGVV 468
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 22-487 1.57e-127

cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) of cytochrome c oxidases of bacterial origin. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits I-III form the functional core of the enzyme complex. Subunit I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit II and heme a of subunit I to the bimetallic center formed by heme a3 and copper B. This cytochrome c oxidase shows proton pump activity across the membrane in addition to the electron transfer. In the bacilli an apparent split (paralogism) has created a sister clade (TIGR02882) encoding subunits (QoxA) of the aa3-type quinone oxidase complex which reacts directly with quinones, bypassing the interaction with soluble cytochrome c. This model attempts to exclude these sequences, placing them between the trusted and noise cutoffs. These families, as well as archaeal and eukaryotic cytochrome c subunit I's are included within the superfamily model, pfam00115. [Energy metabolism, Electron transport]


Pssm-ID: 213748  Cd Length: 499  Bit Score: 380.03  E-value: 1.57e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252  22 SSCNHKVLGLYYIWLAFIFGISGSLASMVLRLELYTSGLRLITPEnqnFYNLTFTLHGLIMIFFTIMPgLYGGFGNYLIP 101
Cdd:TIGR02891   2 TTVDHKRIGILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDAE---TYNQLFTMHGTIMIFLFAIP-ILAGFGNYLLP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 102 IYNGAPEVAFPRINSVSLLLLPisFGCVLLSTTAEFGGG--SGWTLYPPLSTSLMSlSPVSMDVIVLGLLLAGISTFLSS 179
Cdd:TIGR02891  78 LMIGARDMAFPRLNAFSYWLYL--FGGLLLLASFFTGGApdTGWTMYPPLSSTSGS-PGVGVDLWLLGLHLLGISSILGA 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 180 LNFITTIFHIRAKGFALGSLVFNTWGIVFTAAMLILTLPVLTAGLLMLITDLHLNTQFYDPVFSGDPVLYQHLFWFFGHP 259
Cdd:TIGR02891 155 VNFIVTILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHP 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 260 EVYVLIIPGFGLISQVISTNFSKIIFGNVTMILALGCISTLGSVVWAHHMITVGLEVDTRAYFTAVTILISLPTGTKIFN 339
Cdd:TIGR02891 235 EVYIIFLPAFGIISEILPTFARKPIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFN 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 340 WLSTYMGSNNKITmSSTLLALSFLLLFTLGGTTGVVLGNAAVDVSLHDTYYVVAHFHFVLSLGAIIALFTGFIFFQETFF 419
Cdd:TIGR02891 315 WIATLWGGSIRFT-TPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVT 393

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 420 GTQLALNSVLILWGLIFVaGIMISFVPLHILGFNVMPRRIPDYPDSLNY--LNSISSIGSLVTFLSLLIL 487
Cdd:TIGR02891 394 GRMYNERLGRWHFWLTFV-GFNLTFFPMHLLGLLGMPRRYYTYPPQMGFatLNLISTIGAFILAAGFLVF 462
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
21-487 5.86e-127

Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];


Pssm-ID: 440605  Cd Length: 535  Bit Score: 379.86  E-value: 5.86e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252  21 ISSCNHKVLGLYYIWLAFIFGISGSLASMVLRLELYTSGLRLITPEnqnFYNLTFTLHGLIMIFFTIMPGLyGGFGNYLI 100
Cdd:COG0843    10 LTTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPE---TYNQLFTMHGTIMIFFFATPFL-AGFGNYLV 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 101 PIYNGAPEVAFPRINSVSLLLLPISFGCVLLSTTAEFGGGSGWTLYPPLSTSLMSlSPVSMDVIVLGLLLAGISTFLSSL 180
Cdd:COG0843    86 PLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEAS-PGVGVDLWLLGLALFGVGSILGGV 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 181 NFITTIFHIRAKGFALGSLVFNTWGIVFTAAMLILTLPVLTAGLLMLITDLHLNTQFYDPVFSGDPVLYQHLFWFFGHPE 260
Cdd:COG0843   165 NFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPE 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 261 VYVLIIPGFGLISQVISTNFSKIIFGNVTMILALGCISTLGSVVWAHHMITVGLEVDTRAYFTAVTILISLPTGTKIFNW 340
Cdd:COG0843   245 VYILILPAFGIVSEIIPTFSRKPLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNW 324

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 341 LST-YMGsnnKITMSS-TLLALSFLLLFTLGGTTGVVLGNAAVDVSLHDTYYVVAHFHFVLSLGAIIALFTGFIFFQETF 418
Cdd:COG0843   325 IATmWRG---RIRFTTpMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKM 401

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1833819252 419 FGTQLALNSVLILWGLIFVaGIMISFVPLHILGFNVMPRRIPDYPDSLNY--LNSISSIGSLVTFLSLLIL 487
Cdd:COG0843   402 TGRMLNERLGKIHFWLWFI-GFNLTFFPMHILGLLGMPRRYATYPPEPGWqpLNLISTIGAFILAVGFLLF 471
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 23-486 3.51e-125

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 374.55  E-value: 3.51e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252  23 SCNHKVLGLYYIWLAFIFGISGSLASMVLRLELYTSGLRLitpENQNFYNLTFTLHGLIMIFFTIMPGLYGGFGNYLIPI 102
Cdd:MTH00037    9 STNHKDIGTLYLIFGAWAGMVGTAMSVIIRTELAQPGSLL---QDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 103 YNGAPEVAFPRINSVSLLLLPISFGCVLLSTTAEFGGGSGWTLYPPLSTSLmSLSPVSMDVIVLGLLLAGISTFLSSLNF 182
Cdd:MTH00037   86 MIGAPDMAFPRMNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNI-AHAGGSVDLAIFSLHLAGASSILASINF 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 183 ITTIFHIRAKGFALGSLVFNTWGIVFTAAMLILTLPVLTAGLLMLITDLHLNTQFYDPVFSGDPVLYQHLFWFFGHPEVY 262
Cdd:MTH00037  165 ITTIINMRTPGMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPEVY 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 263 VLIIPGFGLISQVISTNFSKI-IFGNVTMILALGCISTLGSVVWAHHMITVGLEVDTRAYFTAVTILISLPTGTKIFNWL 341
Cdd:MTH00037  245 ILILPGFGMISHVIAHYSGKQePFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWM 324

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 342 STYMGSNNKITmSSTLLALSFLLLFTLGGTTGVVLGNAAVDVSLHDTYYVVAHFHFVLSLGAIIALFTGFIFFQETFFGT 421
Cdd:MTH00037  325 ATLQGSNLRWE-TPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLFSGV 403

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1833819252 422 QLALNSVLILWGLIFVaGIMISFVPLHILGFNVMPRRIPDYPDSLNYLNSISSIGSLVTFLSLLI 486
Cdd:MTH00037  404 SLHPLWSKVHFFLMFI-GVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSTISLVATLF 467
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 17-485 2.47e-123

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 370.31  E-value: 2.47e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252  17 NYLT--ISSCNHKVLGLYYIWLAFIFGISGSLASMVLRLELYTSGLRLitpENQNFYNLTFTLHGLIMIFFTIMPGLYGG 94
Cdd:MTH00182    3 LYLTrwVFSTNHKDIGTLYLVFGAGAGMIGTAFSMLIRLELSAPGAML---GDDHLYNVIVTAHAFIMIFFLVMPVMIGG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252  95 FGNYLIPIYNGAPEVAFPRINSVSLLLLPISFGCVLLSTTAEFGGGSGWTLYPPLStSLMSLSPVSMDVIVLGLLLAGIS 174
Cdd:MTH00182   80 FGNWLVPLYIGAPDMAFPRLNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLS-SIQAHSGGAVDMAIFSLHLAGVS 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 175 TFLSSLNFITTIFHIRAKGFALGSLVFNTWGIVFTAAMLILTLPVLTAGLLMLITDLHLNTQFYDPVFSGDPVLYQHLFW 254
Cdd:MTH00182  159 SILGAINFITTIFNMRAPGVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFW 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 255 FFGHPEVYVLIIPGFGLISQVISTNFSK-IIFGNVTMILALGCISTLGSVVWAHHMITVGLEVDTRAYFTAVTILISLPT 333
Cdd:MTH00182  239 FFGHPEVYILILPGFGMISQIIPTFVAKkQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPT 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 334 GTKIFNWLSTYMGSNNKITmSSTLLALSFLLLFTLGGTTGVVLGNAAVDVSLHDTYYVVAHFHFVLSLGAIIALFTGFIF 413
Cdd:MTH00182  319 GIKVFSWLATIYGGTLRLD-TPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYY 397

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1833819252 414 FQETFFGTQLALNSVLILWGLIFVaGIMISFVPLHILGFNVMPRRIPDYPDSLNYLNSISSIGSLVTFLSLL 485
Cdd:MTH00182  398 WFGKITGYCYNELYGKIHFWLMFI-GVNLTFFPQHFLGLAGFPRRYSDFADAFAGWNLVSSLGSIISIVGVV 468
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 23-485 1.39e-118

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 358.56  E-value: 1.39e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252  23 SCNHKVLGLYYIWLAFIFGISGSLASMVLRLELYTSGLRLitpENQNFYNLTFTLHGLIMIFFTIMPGLYGGFGNYLIPI 102
Cdd:MTH00026   10 SCNHKDIGSLYLVFGALSGAIGTAFSMLIRLELSSPGSML---GDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 103 YNGAPEVAFPRINSVSLLLLPISFGCVLLSTTAEFGGGSGWTLYPPLStSLMSLSPVSMDVIVLGLLLAGISTFLSSLNF 182
Cdd:MTH00026   87 MIGAPDMAFPRLNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLA-SIQAHSGGSVDMAIFSLHLAGLSSILGAMNF 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 183 ITTIFHIRAKGFALGSLVFNTWGIVFTAAMLILTLPVLTAGLLMLITDLHLNTQFYDPVFSGDPVLYQHLFWFFGHPEVY 262
Cdd:MTH00026  166 ITTVMNMRTPGMTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVY 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 263 VLIIPGFGLISQVIST-NFSKIIFGNVTMILALGCISTLGSVVWAHHMITVGLEVDTRAYFTAVTILISLPTGTKIFNWL 341
Cdd:MTH00026  246 ILILPGFGIISQILSLfSYKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSWL 325

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 342 STYMGS-NNKITMSSTLLALSFLLLFTLGGTTGVVLGNAAVDVSLHDTYYVVAHFHFVLSLGAIIALFTGFIFFQETFFG 420
Cdd:MTH00026  326 ATVSGSgRNLIFTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWFGKITG 405

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1833819252 421 TQLALNSVLILWGLIFVaGIMISFVPLHILGFNVMPRRIPDYPDSLNYLNSISSIGSLVTFLSLL 485
Cdd:MTH00026  406 YAYKDIYGLIHFWLMFI-GVNITFFPQHFLGLAGLPRRYADYPDNFEDFNQISSFGSIISIIAVI 469
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 21-487 7.17e-115

Ubiquinol oxidase subunit I. 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. Subunit I contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme and a copper ion. It also contains a low-spin heme, believed to participate in the transfer of electrons from ubiquinol to the binuclear center. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from ubiquinol on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I. It is generally believed that the channels contain water molecules that act as 'proton wires' to transfer the protons. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electrons are believed to be transferred directly from ubiquinol (the electron donor) to the low-spin heme, and directly from the low-spin heme to the binuclear center.


Pssm-ID: 238832  Cd Length: 501  Bit Score: 347.65  E-value: 7.17e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252  21 ISSCNHKVLGLYYIWLAFIFGISGSLASMVLRLELYTSGLRLITPENqnfYNLTFTLHGLIMIFFTIMPgLYGGFGNYLI 100
Cdd:cd01662     2 LTTVDHKRIGIMYIITAFVFFLRGGVDALLMRTQLALPGNDFLSPEH---YNQIFTMHGTIMIFLFAMP-LVFGLMNYLV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 101 PIYNGAPEVAFPRINSVSLLLLpiSFGCVLLSTTAEFGGG--SGWTLYPPLSTSLMSlSPVSMDVIVLGLLLAGISTFLS 178
Cdd:cd01662    78 PLQIGARDVAFPRLNALSFWLF--LFGGLLLNASLLIGGFpdAGWFAYPPLSGLEYS-PGVGVDYWILGLQFSGIGTLLG 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 179 SLNFITTIFHIRAKGFALGSLVFNTWGIVFTAAMLILTLPVLTAGLLMLITDLHLNTQFYDPVFSGDPVLYQHLFWFFGH 258
Cdd:cd01662   155 AINFIVTILKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGH 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 259 PEVYVLIIPGFGLISQVISTNFSKIIFGNVTMILALGCISTLGSVVWAHHMITVGLEVDTRAYFTAVTILISLPTGTKIF 338
Cdd:cd01662   235 PEVYILILPAFGIFSEIVPTFSRKPLFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIF 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 339 NWLSTYMGSnnKITMSS-TLLALSFLLLFTLGGTTGVVLGNAAVDVSLHDTYYVVAHFHFVLSLGAIIALFTGFIFFQET 417
Cdd:cd01662   315 NWLFTMWRG--RIRFETpMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPK 392

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1833819252 418 FFGTQlaLNSVLILWGL-IFVAGIMISFVPLHILGFNVMPRRIPDYPDSLNY--LNSISSIGSLVTFLSLLIL 487
Cdd:cd01662   393 MFGRM--LNERLGKWSFwLWFIGFNLTFFPMHILGLMGMPRRVYTYLPGPGWdpLNLISTIGAFLIAAGVLLF 463
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 23-487 6.33e-109

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 332.80  E-value: 6.33e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252  23 SCNHKVLGLYYIWLAFIFGISGSLASMVLRLELYTSGLRLITPEnqnFYNLTFTLHGLIMIFFTIMPGLYGGFGNYLIPI 102
Cdd:MTH00048   10 TLDHKRIGVIYTLLGVWSGFVGLSLSLLIRLNFLDPYYNVISLD---VYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 103 YNGAPEVAFPRINSVSLLLLPISFGCVLLSTTaeFGGGSGWTLYPPLSTSLMSLSpVSMDVIVLGLLLAGISTFLSSLNF 182
Cdd:MTH00048   87 LLGLSDLNLPRLNALSAWLLVPSIVFLLLSMC--LGAGVGWTFYPPLSSSLFSSS-WGVDFLMFSLHLAGVSSLFGSINF 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 183 ITTIFHIRAKGFALGSLVFnTWGIVFTAAMLILTLPVLTAGLLMLITDLHLNTQFYDPVFSGDPVLYQHLFWFFGHPEVY 262
Cdd:MTH00048  164 ICTIYSAFMTNVFSRTSII-LWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPEVY 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 263 VLIIPGFGLISQV---ISTNFSkiIFGNVTMILALGCISTLGSVVWAHHMITVGLEVDTRAYFTAVTILISLPTGTKIFN 339
Cdd:MTH00048  243 VLILPGFGIISHIclsLSNNDD--PFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFS 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 340 WLSTYMGSNNKITMSSTLLALSFLLLFTLGGTTGVVLGNAAVDVSLHDTYYVVAHFHFVLSLGAIIALFTGFIFFQETFF 419
Cdd:MTH00048  321 WLYMLLNSRVRKSDPVVWWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWPLIT 400

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 420 GtqLALNSVLIL--WGLIFVaGIMISFVPLHILGFNVMPRRIPDYPDSLNYLNSISSIGSLVTFLSLLIL 487
Cdd:MTH00048  401 G--LSLNKYLLQchCIISMI-GFNLCFFPMHYFGLCGLPRRVCVYEPSYYWINVVCTVGSFISAFSGCFF 467
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 28-479 8.27e-93

Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key enzyme in aerobic metabolism. Proton pumping haem-copper oxidases represent the terminal, energy-transfer enzymes of respiratory chains in prokaryotes and eukaryotes. The CuB-haem a3 (or haem o) binuclear centre, associated with the largest subunit I of cytochrome c and ubiquinol oxidases (E.C:1.10.3.11), is directly involved in the coupling between dioxygen reduction and proton pumping. Some terminal oxidases generate a transmembrane proton gradient across the plasma membrane (prokaryotes) or the mitochondrial inner membrane (eukaryotes). The enzyme complex consists of 3-4 subunits (prokaryotes) up to 13 polypeptides (mammals) of which only the catalytic subunit (equivalent to mammalian subunit I (COXI) is found in all haem-copper respiratory oxidases. The presence of a bimetallic centre (formed by a high-spin haem and copper B) as well as a low-spin haem, both ligated to six conserved histidine residues near the outer side of four transmembrane spans within CO I is common to all family members.


Pssm-ID: 459678  Cd Length: 432  Bit Score: 288.70  E-value: 8.27e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252  28 VLGLYYIWLAFIFGISGSLASMVLRLELYTSGLRLITPEnqnFYNLTFTLHGLIMIFFTIMPGLyGGFGNYLIPIYNGAP 107
Cdd:pfam00115   1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPL---TYNQLRTLHGNLMIFWFATPFL-FGFGNYLVPLMIGAR 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 108 EVAFPRINSVSLLLLPISFGCVLLSTTaefGGGSGWTLYPPLstslmslspVSMDVIVLGLLLAGISTFLSSLNFITTIF 187
Cdd:pfam00115  77 DMAFPRLNALSFWLVVLGAVLLLASFG---GATTGWTEYPPL---------VGVDLWYIGLLLAGVSSLLGAINFIVTIL 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 188 HIRAKGFALGSLVFnTWGIVFTAAMLILTLPVLTAGLLMLITDLHLNTqfydpvFSGDPVLYQHLFWFFGHPEVYVLIIP 267
Cdd:pfam00115 145 KRRAPGMTLRMPLF-VWAILATAILILLAFPVLAAALLLLLLDRSLGA------GGGDPLLDQHLFWWFGHPEVYILILP 217

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 268 GFGLISQVISTNFSKIIFGNVTMILALGCISTLGSVVWAHHMITVGLEVDTRAYFTAVTILISLPTGTKIFNWLSTYMGS 347
Cdd:pfam00115 218 AFGIIYYILPKFAGRPLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGG 297

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 348 NNKITMSSTLLALSFLLLFTLGGTTGVVLGNAAVDVSLHDTYYVVAHFHFVLSLGAIIALFTGFIFFQETFFGTQLALNS 427
Cdd:pfam00115 298 WIRFRTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKL 377

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1833819252 428 VLILWGLIFVaGIMISFVPLHILGFNVMPRRIP----DYPDSLNYLNSISSIGSLV 479
Cdd:pfam00115 378 GKLHFWLLFI-GFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPLNWIRTIGGVL 432
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 21-459 3.26e-71

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 238.68  E-value: 3.26e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252  21 ISSCNHKVLGLYYIWLAFIFGISGSLASMVLRLE--LYTSGLRLITPENQnfYNLTFTLHGLIMIFFTIMPGLYGgFGNY 98
Cdd:PRK15017   49 LTSVDHKRLGIMYIIVAIVMLLRGFADAIMMRSQqaLASAGEAGFLPPHH--YDQIFTAHGVIMIFFVAMPFVIG-LMNL 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252  99 LIPIYNGAPEVAFPRINSVSLLLLPISFGCVLLSTTAEFGGGSGWTLYPPLSTslMSLSP-VSMDVIVLGLLLAGISTFL 177
Cdd:PRK15017  126 VVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLSG--IEYSPgVGVDYWIWSLQLSGIGTTL 203

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 178 SSLNFITTIFHIRAKGFALGSLVFNTWGIVFTAAMLILTLPVLTAGLLMLITDLHLNTQFYDPVFSGDPVLYQHLFWFFG 257
Cdd:PRK15017  204 TGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWG 283

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 258 HPEVYVLIIPGFGLISQVISTNFSKIIFGNVTMILALGCISTLGSVVWAHHMITVGLEVDTRAYFTAVTILISLPTGTKI 337
Cdd:PRK15017  284 HPEVYILILPVFGVFSEIAATFSRKRLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVKI 363

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 338 FNWLST-YMGsnnKITMSSTLL-ALSFLLLFTLGGTTGVVLGNAAVDVSLHDTYYVVAHFHFVLSLGAIIALFTGFIFFQ 415
Cdd:PRK15017  364 FNWLFTmYQG---RIVFHSAMLwTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYWW 440

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 1833819252 416 ETFFGtqLALNSVlilWGL----IFVAGIMISFVPLHILGFNVMPRRI 459
Cdd:PRK15017  441 PKAFG--FKLNET---WGKrafwFWIIGFFVAFMPLYALGFMGMTRRL 483
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
 203-487 4.19e-05

ba3-like heme-copper oxidase subunit I. 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. For general information on the heme-copper oxidase superfamily, please see cd00919.


Pssm-ID: 238830  Cd Length: 473  Bit Score: 45.74  E-value: 4.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 203 TWGIVFTAAM-LILTLPVLTAGLLMLITdlhLNTQFYDPVfsgDPVLYQHLFWFFGHPEVYVLIIPGFGLISQVIStnfs 281
Cdd:cd01660   163 TFMVVTTMILwLVASLGVALEVLFQLLP---WSLGLVDTV---DVLLSRTLFWWFGHPLVYFWLLPAYIAWYTILP---- 232

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 282 KIIFGN--------VTMILALgcisTLGSVVWAHHMIT-VGLEVDTRAYFTAVTILISLPT------------------- 333
Cdd:cd01660   233 KIAGGKlfsdplarLAFILFL----LFSTPVGFHHQFAdPGIGPGWKFIHMVLTFMVALPSlltaftvfasleiagrlrg 308

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 334 GTKIFNWLSTYMGSNnkitmSSTLLALSFLLLFTLGGTTGVVLGNAAVDVSLHDTYYVVAHFHFVLSLGAIIALFTGFIF 413
Cdd:cd01660   309 GKGLFGWIRALPWGD-----PMFLALFLAMLMFIPGGAGGIINASYQLNYVVHNTAWVPGHFHLTVGGAVALTFMAVAYW 383

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1833819252 414 FQETFFGTQLALNSVLILWGLIFVAGIMISFVPLHILGFNVMPRR--IPDYPDSLNYLNSI-----SSIGSLVTFLSLLI 486
Cdd:cd01660   384 LVPHLTGRELAAKRLALAQPWLWFVGMTIMSTAMHVAGLLGAPRRtaEAQYGGLPAAGEWApyqqlMAIGGTILFVSGAL 463


                  .
gi 1833819252 487 L 487
Cdd:cd01660   464 F 464
 
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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