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Conserved domains on  [gi|90102136|gb|ABD85230|]
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cytochrome oxidase subunit I, partial (mitochondrion) [Chalcosyrphus piger]

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 ...
 11-376 0e+00

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 MTH00153:

Pssm-ID: 469701  Cd Length: 511  Bit Score: 754.78  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136   11 VSSMVENGAGTGWTEYPPLSASIAHGGASVDLAIFSLHLAGMSSILGAVNFITTVINMRSTGITYDRMPLFVWSVVITAL 90
Cdd:MTH00153 112 SSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAI 191

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136   91 LLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQECGKKETFGSLGM 170
Cdd:MTH00153 192 LLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGM 271

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136  171 IYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIFSWLATLHGTQLIYSPAIMWALGFVFLFTVGGL 250
Cdd:MTH00153 272 IYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGL 351

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136  251 TGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTGLTLNIKWLKSQFIIMFIGVNLTFFPQHFLGL 330
Cdd:MTH00153 352 TGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGL 431

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 90102136  331 AGMPRRYSDYPDAYTTWNVISTIGSTISLVGIIFFMIIIWKSMIKQ 376
Cdd:MTH00153 432 AGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISK 477
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 11-376 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 754.78  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136   11 VSSMVENGAGTGWTEYPPLSASIAHGGASVDLAIFSLHLAGMSSILGAVNFITTVINMRSTGITYDRMPLFVWSVVITAL 90
Cdd:MTH00153 112 SSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAI 191

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136   91 LLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQECGKKETFGSLGM 170
Cdd:MTH00153 192 LLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGM 271

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136  171 IYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIFSWLATLHGTQLIYSPAIMWALGFVFLFTVGGL 250
Cdd:MTH00153 272 IYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGL 351

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136  251 TGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTGLTLNIKWLKSQFIIMFIGVNLTFFPQHFLGL 330
Cdd:MTH00153 352 TGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGL 431

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 90102136  331 AGMPRRYSDYPDAYTTWNVISTIGSTISLVGIIFFMIIIWKSMIKQ 376
Cdd:MTH00153 432 AGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISK 477
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 12-376 0e+00

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: 666.88  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136  12 SSMVENGAGTGWTEYPPLSASIAHGGASVDLAIFSLHLAGMSSILGAVNFITTVINMRSTGITYDRMPLFVWSVVITALL 91
Cdd:cd01663 106 SALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFL 185

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136  92 LLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQECGKKETFGSLGMI 171
Cdd:cd01663 186 LLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSGKKPVFGYLGMV 265

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136 172 YAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIFSWLATLHGTQLIYSPAIMWALGFVFLFTVGGLT 251
Cdd:cd01663 266 YAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPMLWALGFIFLFTIGGLT 345

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136 252 GVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTGLTLNIKWLKSQFIIMFIGVNLTFFPQHFLGLA 331
Cdd:cd01663 346 GVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHFWLMFIGVNLTFFPQHFLGLA 425

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*
gi 90102136 332 GMPRRYSDYPDAYTTWNVISTIGSTISLVGIIFFMIIIWKSMIKQ 376
Cdd:cd01663 426 GMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSG 470
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
18-375 1.47e-154

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 445.73  E-value: 1.47e-154
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136  18 GAGTGWTEYPPLSASIAHGGASVDLAIFSLHLAGMSSILGAVNFITTVINMRSTGITYDRMPLFVWSVVITALLLLLSLP 97
Cdd:COG0843 123 AADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFP 202

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136  98 VLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQECGKKeTFGSLGMIYAMLAI 177
Cdd:COG0843 203 VLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFSRKP-LFGYKAMVLATVAI 281

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136 178 GLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIFSWLATLHGTQLIYSPAIMWALGFVFLFTVGGLTGVVLAN 257
Cdd:COG0843 282 AFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLAS 361

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136 258 SSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTGLTLNIKWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRY 337
Cdd:COG0843 362 VPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRY 441

                       330       340       350       360
                ....*....|....*....|....*....|....*....|
gi 90102136 338 SDYP--DAYTTWNVISTIGSTISLVGIIFFMIIIWKSMIK 375
Cdd:COG0843 442 ATYPpePGWQPLNLISTIGAFILAVGFLLFLINLVVSLRK 481
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 18-376 1.08e-150

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: 434.73  E-value: 1.08e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136    18 GAGTGWTEYPPLSASIAHGGASVDLAIFSLHLAGMSSILGAVNFITTVINMRSTGITYDRMPLFVWSVVITALLLLLSLP 97
Cdd:TIGR02891 114 APDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLFVWGILVTSILILLAFP 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136    98 VLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQECGKKeTFGSLGMIYAMLAI 177
Cdd:TIGR02891 194 VLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFARKP-IFGYRAMVYATVAI 272

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136   178 GLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIFSWLATLHGTQLIYSPAIMWALGFVFLFTVGGLTGVVLAN 257
Cdd:TIGR02891 273 GFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLAS 352

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136   258 SSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTGLTLNIKWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRY 337
Cdd:TIGR02891 353 VPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRY 432

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 90102136   338 SDYPDA--YTTWNVISTIGSTISLVGIIFFMIIIWKSMIKQ 376
Cdd:TIGR02891 433 YTYPPQmgFATLNLISTIGAFILAAGFLVFLWNLIWSLRKG 473
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 17-357 4.24e-101

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: 305.65  E-value: 4.24e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136    17 NGAGTGWTEYPPLSAsiahggasVDLAIFSLHLAGMSSILGAVNFITTVINMRSTGITYdRMPLFVWSVVITALLLLLSL 96
Cdd:pfam00115 103 GGATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATAILILLAF 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136    97 PVLAGAITMLLTDRNLNtsffdpAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQECGKKeTFGSLGMIYAMLA 176
Cdd:pfam00115 174 PVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGRP-LFGYKLSVLAFWL 246

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136   177 IGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIFSWLATLHGTQL-IYSPAIMWALGFVFLFTVGGLTGVVL 255
Cdd:pfam00115 247 IAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIrFRTTPMLFFLGFAFLFIIGGLTGVML 326

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136   256 ANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTGLTLNIKWLKSQFIIMFIGVNLTFFPQHFLGLAGMPR 335
Cdd:pfam00115 327 ALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFWLLFIGFNLTFFPMHILGLLGMPR 406

                         330       340
                  ....*....|....*....|....*.
gi 90102136   336 RYS----DYPDAYTTWNVISTIGSTI 357
Cdd:pfam00115 407 RYAppfiETVPAFQPLNWIRTIGGVL 432
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 11-376 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 754.78  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136   11 VSSMVENGAGTGWTEYPPLSASIAHGGASVDLAIFSLHLAGMSSILGAVNFITTVINMRSTGITYDRMPLFVWSVVITAL 90
Cdd:MTH00153 112 SSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAI 191

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136   91 LLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQECGKKETFGSLGM 170
Cdd:MTH00153 192 LLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGM 271

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136  171 IYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIFSWLATLHGTQLIYSPAIMWALGFVFLFTVGGL 250
Cdd:MTH00153 272 IYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGL 351

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136  251 TGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTGLTLNIKWLKSQFIIMFIGVNLTFFPQHFLGL 330
Cdd:MTH00153 352 TGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGL 431

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 90102136  331 AGMPRRYSDYPDAYTTWNVISTIGSTISLVGIIFFMIIIWKSMIKQ 376
Cdd:MTH00153 432 AGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISK 477
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 12-376 0e+00

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: 666.88  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136  12 SSMVENGAGTGWTEYPPLSASIAHGGASVDLAIFSLHLAGMSSILGAVNFITTVINMRSTGITYDRMPLFVWSVVITALL 91
Cdd:cd01663 106 SALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFL 185

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136  92 LLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQECGKKETFGSLGMI 171
Cdd:cd01663 186 LLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSGKKPVFGYLGMV 265

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136 172 YAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIFSWLATLHGTQLIYSPAIMWALGFVFLFTVGGLT 251
Cdd:cd01663 266 YAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPMLWALGFIFLFTIGGLT 345

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136 252 GVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTGLTLNIKWLKSQFIIMFIGVNLTFFPQHFLGLA 331
Cdd:cd01663 346 GVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHFWLMFIGVNLTFFPQHFLGLA 425

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*
gi 90102136 332 GMPRRYSDYPDAYTTWNVISTIGSTISLVGIIFFMIIIWKSMIKQ 376
Cdd:cd01663 426 GMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSG 470
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 11-376 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 633.64  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136   11 VSSMVENGAGTGWTEYPPLSASIAHGGASVDLAIFSLHLAGMSSILGAVNFITTVINMRSTGITYDRMPLFVWSVVITAL 90
Cdd:MTH00167 114 ASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQTPLFVWSILVTTI 193

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136   91 LLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQECGKKETFGSLGM 170
Cdd:MTH00167 194 LLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVVYYSGKKEPFGYMGM 273

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136  171 IYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIFSWLATLHGTQLIYSPAIMWALGFVFLFTVGGL 250
Cdd:MTH00167 274 VWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLHGGKIKWETPMLWALGFIFLFTVGGL 353

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136  251 TGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTGLTLNIKWLKSQFIIMFIGVNLTFFPQHFLGL 330
Cdd:MTH00167 354 TGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGLTLNETWTKIHFFVMFIGVNLTFFPQHFLGL 433

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 90102136  331 AGMPRRYSDYPDAYTTWNVISTIGSTISLVGIIFFMIIIWKSMIKQ 376
Cdd:MTH00167 434 AGMPRRYSDYPDAYTLWNVVSSIGSLISLVAVILFLFIIWEAFSSK 479
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 11-376 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 628.93  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136   11 VSSMVENGAGTGWTEYPPLSASIAHGGASVDLAIFSLHLAGMSSILGAVNFITTVINMRSTGITYDRMPLFVWSVVITAL 90
Cdd:MTH00223 111 SSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERLPLFVWSVKVTAF 190

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136   91 LLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQECGKKETFGSLGM 170
Cdd:MTH00223 191 LLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSSKKEVFGTLGM 270

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136  171 IYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIFSWLATLHGTQLIYSPAIMWALGFVFLFTVGGL 250
Cdd:MTH00223 271 IYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGSKIKYEAPMLWALGFIFLFTVGGL 350

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136  251 TGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTGLTLNIKWLKSQFIIMFIGVNLTFFPQHFLGL 330
Cdd:MTH00223 351 TGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLFTGVTLHRRWAKAHFFLMFLGVNLTFFPQHFLGL 430

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 90102136  331 AGMPRRYSDYPDAYTTWNVISTIGSTISLVGIIFFMIIIWKSMIKQ 376
Cdd:MTH00223 431 AGMPRRYSDYPDCYTKWNQVSSFGSMISFVSVLFFMFIVWEAFVSQ 476
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 12-376 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 621.73  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136   12 SSMVENGAGTGWTEYPPLSASIAHGGASVDLAIFSLHLAGMSSILGAVNFITTVINMRSTGITYDRMPLFVWSVVITALL 91
Cdd:MTH00116 115 SSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTPLFVWSVLITAVL 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136   92 LLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQECGKKETFGSLGMI 171
Cdd:MTH00116 195 LLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVTYYAGKKEPFGYMGMV 274

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136  172 YAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIFSWLATLHGTQLIYSPAIMWALGFVFLFTVGGLT 251
Cdd:MTH00116 275 WAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLT 354

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136  252 GVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTGLTLNIKWLKSQFIIMFIGVNLTFFPQHFLGLA 331
Cdd:MTH00116 355 GIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGYTLHQTWTKAQFGVMFTGVNLTFFPQHFLGLA 434

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 90102136  332 GMPRRYSDYPDAYTTWNVISTIGSTISLVGIIFFMIIIWKSMIKQ 376
Cdd:MTH00116 435 GMPRRYSDYPDAYTLWNTISSIGSLISMTAVIMLMFIIWEAFSSK 479
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 12-376 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 621.36  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136   12 SSMVENGAGTGWTEYPPLSASIAHGGASVDLAIFSLHLAGMSSILGAVNFITTVINMRSTGITYDRMPLFVWSVVITALL 91
Cdd:MTH00142 113 SAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERVPLFVWSVKITAIL 192

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136   92 LLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQECGKKETFGSLGMI 171
Cdd:MTH00142 193 LLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIINHYSGKKEVFGTLGMI 272

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136  172 YAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIFSWLATLHGTQLIYSPAIMWALGFVFLFTVGGLT 251
Cdd:MTH00142 273 YAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFSWLATLHGSKVKYEPPMLWALGFIFLFTVGGLT 352

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136  252 GVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTGLTLNIKWLKSQFIIMFIGVNLTFFPQHFLGLA 331
Cdd:MTH00142 353 GIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLFTGLTLNPRWLKAHFYTMFIGVNLTFFPQHFLGLA 432

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 90102136  332 GMPRRYSDYPDAYTTWNVISTIGSTISLVGIIFFMIIIWKSMIKQ 376
Cdd:MTH00142 433 GMPRRYSDYPDAYTTWNVVSSLGSMISFIAVLMFVFIVWESFVSQ 477
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 12-376 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 560.60  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136   12 SSMVENGAGTGWTEYPPLSASIAHGGASVDLAIFSLHLAGMSSILGAVNFITTVINMRSTGITYDRMPLFVWSVVITALL 91
Cdd:MTH00037 115 SAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRLPLFVWSVFITAFL 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136   92 LLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQECGKKETFGSLGMI 171
Cdd:MTH00037 195 LLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKQEPFGYLGMV 274

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136  172 YAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIFSWLATLHGTQLIYSPAIMWALGFVFLFTVGGLT 251
Cdd:MTH00037 275 YAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWMATLQGSNLRWETPLLWALGFVFLFTIGGLT 354

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136  252 GVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTGLTLNIKWLKSQFIIMFIGVNLTFFPQHFLGLA 331
Cdd:MTH00037 355 GIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLFSGVSLHPLWSKVHFFLMFIGVNLTFFPQHFLGLA 434

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 90102136  332 GMPRRYSDYPDAYTTWNVISTIGSTISLVGIIFFMIIIWKSMIKQ 376
Cdd:MTH00037 435 GMPRRYSDYPDAYTLWNTVSSIGSTISLVATLFFLFLIWEAFASQ 479
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 12-376 0e+00

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 559.52  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136   12 SSMVENGAGTGWTEYPPLSASIAHGGASVDLAIFSLHLAGMSSILGAVNFITTVINMRSTGITYDRMPLFVWSVVITALL 91
Cdd:MTH00007 112 SAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERIPLFVWAVVITVVL 191

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136   92 LLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQECGKKETFGSLGMI 171
Cdd:MTH00007 192 LLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGAISHIVTHYAGKLEPFGTLGMI 271

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136  172 YAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIFSWLATLHGTQLIYSPAIMWALGFVFLFTVGGLT 251
Cdd:MTH00007 272 YAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGSPIKYETPMLWALGFIFLFTTGGLT 351

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136  252 GVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTGLTLNIKWLKSQFIIMFIGVNLTFFPQHFLGLA 331
Cdd:MTH00007 352 GIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTGLTLHDRWAKAHFFLMFLGVNLTFFPQHFLGLS 431

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 90102136  332 GMPRRYSDYPDAYTTWNVISTIGSTISLVGIIFFMIIIWKSMIKQ 376
Cdd:MTH00007 432 GMPRRYSDYPDAYTKWNVVSSFGSMLSFVALLLFIFILWEAFSAQ 476
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 11-372 0e+00

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 559.11  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136   11 VSSMVENGAGTGWTEYPPLSASIAHGGASVDLAIFSLHLAGMSSILGAVNFITTVINMRSTGITYDRMPLFVWSVVITAL 90
Cdd:MTH00103 114 ASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPLFVWSVLITAV 193

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136   91 LLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQECGKKETFGSLGM 170
Cdd:MTH00103 194 LLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVTYYSGKKEPFGYMGM 273

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136  171 IYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIFSWLATLHGTQLIYSPAIMWALGFVFLFTVGGL 250
Cdd:MTH00103 274 VWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGNIKWSPAMLWALGFIFLFTVGGL 353

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136  251 TGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTGLTLNIKWLKSQFIIMFIGVNLTFFPQHFLGL 330
Cdd:MTH00103 354 TGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLNDTWAKIHFTIMFVGVNMTFFPQHFLGL 433

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 90102136  331 AGMPRRYSDYPDAYTTWNVISTIGSTISLVGIIFFMIIIWKS 372
Cdd:MTH00103 434 SGMPRRYSDYPDAYTTWNTVSSMGSFISLTAVMLMIFMIWEA 475
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 12-372 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 552.22  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136   12 SSMVENGAGTGWTEYPPLSASIAHGGASVDLAIFSLHLAGMSSILGAVNFITTVINMRSTGITYDRMPLFVWSVVITALL 91
Cdd:MTH00183 115 SSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPLFVWAVLITAVL 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136   92 LLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQECGKKETFGSLGMI 171
Cdd:MTH00183 195 LLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVAYYSGKKEPFGYMGMV 274

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136  172 YAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIFSWLATLHGTQLIYSPAIMWALGFVFLFTVGGLT 251
Cdd:MTH00183 275 WAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGSIKWETPLLWALGFIFLFTVGGLT 354

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136  252 GVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTGLTLNIKWLKSQFIIMFIGVNLTFFPQHFLGLA 331
Cdd:MTH00183 355 GIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLFSGYTLHSTWTKIHFGVMFVGVNLTFFPQHFLGLA 434

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 90102136  332 GMPRRYSDYPDAYTTWNVISTIGSTISLVGIIFFMIIIWKS 372
Cdd:MTH00183 435 GMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMFLFILWEA 475
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 12-372 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 548.39  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136   12 SSMVENGAGTGWTEYPPLSASIAHGGASVDLAIFSLHLAGMSSILGAVNFITTVINMRSTGITYDRMPLFVWSVVITALL 91
Cdd:MTH00077 115 SSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQTPLFVWSVLITAVL 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136   92 LLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQECGKKETFGSLGMI 171
Cdd:MTH00077 195 LLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISHIVTYYSAKKEPFGYMGMV 274

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136  172 YAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIFSWLATLHGTQLIYSPAIMWALGFVFLFTVGGLT 251
Cdd:MTH00077 275 WAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGAIKWDAAMLWALGFIFLFTVGGLT 354

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136  252 GVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTGLTLNIKWLKSQFIIMFIGVNLTFFPQHFLGLA 331
Cdd:MTH00077 355 GIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLHSTWSKIHFGVMFIGVNLTFFPQHFLGLA 434

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 90102136  332 GMPRRYSDYPDAYTTWNVISTIGSTISLVGIIFFMIIIWKS 372
Cdd:MTH00077 435 GMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMMMFIIWEA 475
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 12-376 1.67e-180

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 511.29  E-value: 1.67e-180
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136   12 SSMVENGAGTGWTEYPPLSASIAHGGASVDLAIFSLHLAGMSSILGAVNFITTVINMRSTGITYDRMPLFVWSVVITALL 91
Cdd:MTH00182 117 SAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRLPLFVWSILITAFL 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136   92 LLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQECGKKETFGSLGMI 171
Cdd:MTH00182 197 LLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISQIIPTFVAKKQIFGYLGMV 276

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136  172 YAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIFSWLATLHGTQLIYSPAIMWALGFVFLFTVGGLT 251
Cdd:MTH00182 277 YAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGGTLRLDTPMLWAMGFVFLFTLGGLT 356

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136  252 GVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTGLTLNIKWLKSQFIIMFIGVNLTFFPQHFLGLA 331
Cdd:MTH00182 357 GVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNELYGKIHFWLMFIGVNLTFFPQHFLGLA 436

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 90102136  332 GMPRRYSDYPDAYTTWNVISTIGSTISLVGIIFFMIIIWKSMIKQ 376
Cdd:MTH00182 437 GFPRRYSDFADAFAGWNLVSSLGSIISIVGVVWFIYIIYDAYVRE 481
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 12-374 1.90e-180

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 510.76  E-value: 1.90e-180
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136   12 SSMVENGAGTGWTEYPPLSaSIAHGGASVDLAIFSLHLAGMSSILGAVNFITTVINMRSTGITYDRMPLFVWSVVITALL 91
Cdd:MTH00079 116 SCFVDMGPGTSWTVYPPLS-TLGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHMSLFVWTVFVTVFL 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136   92 LLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQECGKKETFGSLGMI 171
Cdd:MTH00079 195 LVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPEVYILILPAFGIISQSTLYLTGKKEVFGSLGMV 274

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136  172 YAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIFSWLATLHGTQLIYSPAIMWALGFVFLFTVGGLT 251
Cdd:MTH00079 275 YAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMKFQPLLLWVLGFIFLFTIGGLT 354

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136  252 GVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTGLTLNIKWLKSQFIIMFIGVNLTFFPQHFLGLA 331
Cdd:MTH00079 355 GVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFMTGIVYDKLMMSAVFFLMFVGVNLTFFPLHFAGLH 434

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 90102136  332 GMPRRYSDYPDAYTTWNVISTIGSTISLVGIIFFMIIIWKSMI 374
Cdd:MTH00079 435 GMPRKYLDYPDVYSVWNVISSYGSMISVFALFLFIYVLLESFF 477
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 12-376 7.79e-176

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 499.35  E-value: 7.79e-176
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136   12 SSMVENGAGTGWTEYPPLSASIAHGGASVDLAIFSLHLAGMSSILGAVNFITTVINMRSTGITYDRMPLFVWSVVITALL 91
Cdd:MTH00184 117 SAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRMPLFVWSILVTTFL 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136   92 LLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQECGKKETFGSLGMI 171
Cdd:MTH00184 197 LLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQIIPTFAAKKQIFGYLGMV 276

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136  172 YAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIFSWLATLHGTQLIYSPAIMWALGFVFLFTVGGLT 251
Cdd:MTH00184 277 YAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATIFGGSLRLDTPMLWAIGFVFLFTMGGLT 356

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136  252 GVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTGLTLNIKWLKSQFIIMFIGVNLTFFPQHFLGLA 331
Cdd:MTH00184 357 GIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNEVYGKIHFWLMFIGVNLTFFPQHFLGLA 436

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 90102136  332 GMPRRYSDYPDAYTTWNVISTIGSTISLVGIIFFMIIIWKSMIKQ 376
Cdd:MTH00184 437 GLPRRYSDFHDSFAGWNQISSLGSVISIVGVVWFIYIVYDAYVRE 481
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 11-373 1.58e-163

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: 465.85  E-value: 1.58e-163
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136  11 VSSMVENGAGTGWTEYPPLSASIAHGGASVDLAIFSLHLAGMSSILGAVNFITTVINMRSTGITYDRMPLFVWSVVITAL 90
Cdd:cd00919 102 SSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDKMPLFVWSVLVTAI 181

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136  91 LLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQECGKKeTFGSLGM 170
Cdd:cd00919 182 LLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAFGAISEIIPTFSGKP-LFGYKLM 260

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136 171 IYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIFSWLATLHGTQLIYSPAIMWALGFVFLFTVGGL 250
Cdd:cd00919 261 VYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGRIRFDPPMLFALGFLFLFTIGGL 340

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136 251 TGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTGLTLNIKWLKSQFIIMFIGVNLTFFPQHFLGL 330
Cdd:cd00919 341 TGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKLGKIHFWLWFIGFNLTFFPMHFLGL 420

                       330       340       350       360
                ....*....|....*....|....*....|....*....|...
gi 90102136 331 AGMPRRYSDYPDAYTTWNVISTIGSTISLVGIIFFMIIIWKSM 373
Cdd:cd00919 421 LGMPRRYADYPDGFAPWNFISSVGAFILGLGLLLFLGNLFLSL 463
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 12-376 6.13e-156

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 449.46  E-value: 6.13e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136   12 SSMVENGAGTGWTEYPPLSASIAHGGASVDLAIFSLHLAGMSSILGAVNFITTVINMRSTGITYDRMPLFVWSVVITALL 91
Cdd:MTH00026 116 SSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRIPLFVWSVFITAIL 195

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136   92 LLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQECGKKETFGSLGMI 171
Cdd:MTH00026 196 LLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQILSLFSYKKQIFGYLGMV 275

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136  172 YAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIFSWLATLHGT--QLIYSPAIMWALGFVFLFTVGG 249
Cdd:MTH00026 276 YAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSWLATVSGSgrNLIFTTPMAWALGFIFLFTIGG 355

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136  250 LTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTGLTLNIKWLKSQFIIMFIGVNLTFFPQHFLG 329
Cdd:MTH00026 356 LTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWFGKITGYAYKDIYGLIHFWLMFIGVNITFFPQHFLG 435

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 90102136  330 LAGMPRRYSDYPDAYTTWNVISTIGSTISLVGIIFFMIIIWKSMIKQ 376
Cdd:MTH00026 436 LAGLPRRYADYPDNFEDFNQISSFGSIISIIAVIWFIVVIFDAYYRE 482
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
18-375 1.47e-154

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 445.73  E-value: 1.47e-154
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136  18 GAGTGWTEYPPLSASIAHGGASVDLAIFSLHLAGMSSILGAVNFITTVINMRSTGITYDRMPLFVWSVVITALLLLLSLP 97
Cdd:COG0843 123 AADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFP 202

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136  98 VLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQECGKKeTFGSLGMIYAMLAI 177
Cdd:COG0843 203 VLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFSRKP-LFGYKAMVLATVAI 281

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136 178 GLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIFSWLATLHGTQLIYSPAIMWALGFVFLFTVGGLTGVVLAN 257
Cdd:COG0843 282 AFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLAS 361

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136 258 SSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTGLTLNIKWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRY 337
Cdd:COG0843 362 VPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRY 441

                       330       340       350       360
                ....*....|....*....|....*....|....*....|
gi 90102136 338 SDYP--DAYTTWNVISTIGSTISLVGIIFFMIIIWKSMIK 375
Cdd:COG0843 442 ATYPpePGWQPLNLISTIGAFILAVGFLLFLINLVVSLRK 481
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 18-376 1.08e-150

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: 434.73  E-value: 1.08e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136    18 GAGTGWTEYPPLSASIAHGGASVDLAIFSLHLAGMSSILGAVNFITTVINMRSTGITYDRMPLFVWSVVITALLLLLSLP 97
Cdd:TIGR02891 114 APDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLFVWGILVTSILILLAFP 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136    98 VLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQECGKKeTFGSLGMIYAMLAI 177
Cdd:TIGR02891 194 VLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFARKP-IFGYRAMVYATVAI 272

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136   178 GLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIFSWLATLHGTQLIYSPAIMWALGFVFLFTVGGLTGVVLAN 257
Cdd:TIGR02891 273 GFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLAS 352

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136   258 SSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTGLTLNIKWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRY 337
Cdd:TIGR02891 353 VPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRY 432

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 90102136   338 SDYPDA--YTTWNVISTIGSTISLVGIIFFMIIIWKSMIKQ 376
Cdd:TIGR02891 433 YTYPPQmgFATLNLISTIGAFILAAGFLVFLWNLIWSLRKG 473
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 18-374 1.65e-137

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 401.36  E-value: 1.65e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136   18 GAGTGWTEYPPLSASIAHGGASVDLAIFSLHLAGMSSILGAVNFITTVINMRSTGITYdRMPLFVWSVVITALLLLLSLP 97
Cdd:MTH00048 120 GAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNVFS-RTSIILWSYLFTSILLLLSLP 198

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136   98 VLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQECGKKETFGSLGMIYAMLAI 177
Cdd:MTH00048 199 VLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPEVYVLILPGFGIISHICLSLSNNDDPFGYYGLVFAMFSI 278

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136  178 GLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIFSWLATLHGTQL-IYSPAIMWALGFVFLFTVGGLTGVVLA 256
Cdd:MTH00048 279 VCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFSWLYMLLNSRVrKSDPVVWWVVSFIVLFTIGGVTGIVLS 358

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136  257 NSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTGLTLNIKWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRR 336
Cdd:MTH00048 359 ASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWPLITGLSLNKYLLQCHCIISMIGFNLCFFPMHYFGLCGLPRR 438

                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 90102136  337 YSDYPDAYTTWNVISTIGSTISLVGIIFFMIIIWKSMI 374
Cdd:MTH00048 439 VCVYEPSYYWINVVCTVGSFISAFSGCFFVFILWESLV 476
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 11-373 2.13e-134

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: 393.10  E-value: 2.13e-134
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136  11 VSSMVENGAGTGWTEYPPLSASIAHGGASVDLAIFSLHLAGMSSILGAVNFITTVINMRSTGITYDRMPLFVWSVVITAL 90
Cdd:cd01662 108 ASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWTTLVTSI 187

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136  91 LLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQECGKKeTFGSLGM 170
Cdd:cd01662 188 LILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYILILPAFGIFSEIVPTFSRKP-LFGYRSM 266

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136 171 IYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIFSWLATLHGTQLIYSPAIMWALGFVFLFTVGGL 250
Cdd:cd01662 267 VYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLFTMWRGRIRFETPMLWAIGFLVTFVIGGL 346

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136 251 TGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTGLTLNIKWLKSQFIIMFIGVNLTFFPQHFLGL 330
Cdd:cd01662 347 TGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRMLNERLGKWSFWLWFIGFNLTFFPMHILGL 426

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*
gi 90102136 331 AGMPRRYSDYP--DAYTTWNVISTIGSTISLVGIIFFMIIIWKSM 373
Cdd:cd01662 427 MGMPRRVYTYLpgPGWDPLNLISTIGAFLIAAGVLLFLINVIVSI 471
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 17-357 4.24e-101

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: 305.65  E-value: 4.24e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136    17 NGAGTGWTEYPPLSAsiahggasVDLAIFSLHLAGMSSILGAVNFITTVINMRSTGITYdRMPLFVWSVVITALLLLLSL 96
Cdd:pfam00115 103 GGATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATAILILLAF 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136    97 PVLAGAITMLLTDRNLNtsffdpAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQECGKKeTFGSLGMIYAMLA 176
Cdd:pfam00115 174 PVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGRP-LFGYKLSVLAFWL 246

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136   177 IGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIFSWLATLHGTQL-IYSPAIMWALGFVFLFTVGGLTGVVL 255
Cdd:pfam00115 247 IAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIrFRTTPMLFFLGFAFLFIIGGLTGVML 326

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136   256 ANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTGLTLNIKWLKSQFIIMFIGVNLTFFPQHFLGLAGMPR 335
Cdd:pfam00115 327 ALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFWLLFIGFNLTFFPMHILGLLGMPR 406

                         330       340
                  ....*....|....*....|....*.
gi 90102136   336 RYS----DYPDAYTTWNVISTIGSTI 357
Cdd:pfam00115 407 RYAppfiETVPAFQPLNWIRTIGGVL 432
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 11-372 1.15e-83

cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type quinone oxidase, one of several bacterial terminal oxidases. This complex couples oxidation of reduced quinones with the reduction of molecular oxygen to water and the pumping of protons to form a proton gradient utilized for ATP production. aa3-type oxidases contain two heme a cofactors as well as copper atoms in the active site. [Energy metabolism, Electron transport]


Pssm-ID: 131928  Cd Length: 643  Bit Score: 267.10  E-value: 1.15e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136    11 VSSMVENGAGTGWTEYPPLSASIAHGGASVDLAIFSLHLAGMSSILGAVNFITTVINMRSTGITYDRMPLFVWSVVITAL 90
Cdd:TIGR02882 151 ISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTL 230

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136    91 LLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQeCGKKETFGSLGM 170
Cdd:TIGR02882 231 IIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLFWIWGHPEVYIVILPAFGIYSEIIST-FAQKRLFGYKSM 309

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136   171 IYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIFSWLATLHGTQLIYSPAIMWALGFVFLFTVGGL 250
Cdd:TIGR02882 310 VWSTVGIAFLSFLVWVHHFFTMGNGALINSFFSITTMAIAIPTGVKIFNWLLTLYKGKIRFTTPMLFSLAFIPNFLIGGV 389

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136   251 TGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTGLTLNIKWLKSQFIIMFIGVNLTFFPQHFLGL 330
Cdd:TIGR02882 390 TGVMLAMASADYQYHNTYFLVAHFHYVLITGVVFACLAGLIYWYPKMFGYKLNERLGKWCFWFFMIGFNVCFFPMYILGL 469

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 90102136   331 AGMPRRYSDY--PDAYTTWNVISTIGSTISLVGIIFFMIIIWKS 372
Cdd:TIGR02882 470 DGMPRRMYTYspSDGWFPLNLISTIGALLMAIGFIFLVYNIYYS 513
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 19-373 1.40e-81

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 262.18  E-value: 1.40e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136   19 AGTGWTEYPPLSASIAHGGASVDLAIFSLHLAGMSSILGAVNFITTVINMRSTGITYDRMPLFVWSVVITALLLLLSLPV 98
Cdd:PRK15017 166 AQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPI 245

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136   99 LAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQeCGKKETFGSLGMIYAMLAIG 178
Cdd:PRK15017 246 LTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWGHPEVYILILPVFGVFSEIAAT-FSRKRLFGYTSLVWATVCIT 324

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136  179 LLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKIFSWLATLHGTQLIYSPAIMWALGFVFLFTVGGLTGVVLANS 258
Cdd:PRK15017 325 VLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVKIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVP 404

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136  259 SIDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYPLFTGLTLNIKWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYS 338
Cdd:PRK15017 405 GADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYWWPKAFGFKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMTRRLS 484

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 90102136  339 DYPD-AYTTWNVISTIGSTISLVGIIFFMIIIWKSM 373
Cdd:PRK15017 485 QQIDpQFHTMLMIAASGAALIALGILCQVIQMYVSI 520
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
 124-373 4.02e-21

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: 94.28  E-value: 4.02e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136 124 DPILYQHLFWFFGHPEVYILILPGFGMISHIISQECGKKETFGSLGMIyAMLAIGLLGFIVWAHHMFT-VGMDVDTRAYF 202
Cdd:cd01660 200 DVLLSRTLFWWFGHPLVYFWLLPAYIAWYTILPKIAGGKLFSDPLARL-AFILFLLFSTPVGFHHQFAdPGIGPGWKFIH 278

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136 203 TSATMIIAIPTGIKIFSWLATL-------HG-------TQLIYSPAIMWALGFVFL-FTVGGLTGVVLANSSIDIILHDT 267
Cdd:cd01660 279 MVLTFMVALPSLLTAFTVFASLeiagrlrGGkglfgwiRALPWGDPMFLALFLAMLmFIPGGAGGIINASYQLNYVVHNT 358

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90102136 268 YYVVAHFHyvLSMGAVFAIMA-GFIHWY-PLFTGLTLNIKWLKS-QFIIMFIGVNLTFFPQHFLGLAGMPRR--YSDYPD 342
Cdd:cd01660 359 AWVPGHFH--LTVGGAVALTFmAVAYWLvPHLTGRELAAKRLALaQPWLWFVGMTIMSTAMHVAGLLGAPRRtaEAQYGG 436

                       250       260       270
                ....*....|....*....|....*....|....*.
gi 90102136 343 AY-----TTWNVISTIGSTISLVGIIFFMIIIWKSM 373
Cdd:cd01660 437 LPaagewAPYQQLMAIGGTILFVSGALFLYILFRTL 472
 
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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