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Conserved domains on  [gi|1931720863|ref|XP_037490992|]
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cytochrome c oxidase subunit I (mitochondrion) [Plasmodium vinckei vinckei]

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 ...
 1-415 4.11e-172

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: 490.46  E-value: 4.11e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863   1 MIFTVHGIIMIFFNIMPGLFGGFGNYFLPILCGSSELAYPRINSISLLLQPIAFILVILSTAAEFGGGTGWTLYPPLStS 80
Cdd:cd01663    47 VIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLS-S 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863  81 LMSLSPVAVDVIVIGLLVSGIASIMSSLNFLTTVMHLRAKGLTLGILSVSTWSLIITSVMLLLTLPVLTGGVLMLLSDLH 160
Cdd:cd01663   126 ILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRN 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863 161 FNTLFFDPTFAGDPILYQHLFWFFGHPEVYILILPAFGIISHVISTNYCR-SLFGNQSMILAMGCIAVLGSVVWVHHMYT 239
Cdd:cd01663   206 FNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSGKkPVFGYLGMVYAMLSIGILGFIVWAHHMFT 285

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863 240 TGLEVDTRAFFTSTTILISIPTGTKVFNWLCTYMSTNFGIThSSSLLSLLFICTFTFGGTTGVILGNGAIDVALHDTYYV 319
Cdd:cd01663   286 VGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFE-TPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYV 364

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863 320 IAHFHFVLSIGAIIALFTSVSFFQESFFGKTLRENTIIVLWsILFFVGVVLTFLPMHFLGFNVMPRRIPDYPDALNGWNM 399
Cdd:cd01663   365 VAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHF-WLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNM 443

                         410
                  ....*....|....*.
gi 1931720863 400 ICSIGSTMTLFGLLIF 415
Cdd:cd01663   444 ISSIGSLISFVSVLLF 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 ...
 1-415 4.11e-172

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: 490.46  E-value: 4.11e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863   1 MIFTVHGIIMIFFNIMPGLFGGFGNYFLPILCGSSELAYPRINSISLLLQPIAFILVILSTAAEFGGGTGWTLYPPLStS 80
Cdd:cd01663    47 VIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLS-S 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863  81 LMSLSPVAVDVIVIGLLVSGIASIMSSLNFLTTVMHLRAKGLTLGILSVSTWSLIITSVMLLLTLPVLTGGVLMLLSDLH 160
Cdd:cd01663   126 ILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRN 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863 161 FNTLFFDPTFAGDPILYQHLFWFFGHPEVYILILPAFGIISHVISTNYCR-SLFGNQSMILAMGCIAVLGSVVWVHHMYT 239
Cdd:cd01663   206 FNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSGKkPVFGYLGMVYAMLSIGILGFIVWAHHMFT 285

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863 240 TGLEVDTRAFFTSTTILISIPTGTKVFNWLCTYMSTNFGIThSSSLLSLLFICTFTFGGTTGVILGNGAIDVALHDTYYV 319
Cdd:cd01663   286 VGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFE-TPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYV 364

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863 320 IAHFHFVLSIGAIIALFTSVSFFQESFFGKTLRENTIIVLWsILFFVGVVLTFLPMHFLGFNVMPRRIPDYPDALNGWNM 399
Cdd:cd01663   365 VAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHF-WLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNM 443

                         410
                  ....*....|....*.
gi 1931720863 400 ICSIGSTMTLFGLLIF 415
Cdd:cd01663   444 ISSIGSLISFVSVLLF 459
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 2-415 4.33e-153

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 442.77  E-value: 4.33e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863   2 IFTVHGIIMIFFNIMPGLFGGFGNYFLPILCGSSELAYPRINSISLLLQPIAFILVILSTAAEFGGGTGWTLYPPLStSL 81
Cdd:MTH00153   55 IVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLS-SN 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863  82 MSLSPVAVDVIVIGLLVSGIASIMSSLNFLTTVMHLRAKGLTLGILSVSTWSLIITSVMLLLTLPVLTGGVLMLLSDLHF 161
Cdd:MTH00153  134 IAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNL 213

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863 162 NTLFFDPTFAGDPILYQHLFWFFGHPEVYILILPAFGIISHVISTNYC-RSLFGNQSMILAMGCIAVLGSVVWVHHMYTT 240
Cdd:MTH00153  214 NTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGkKETFGTLGMIYAMLAIGLLGFIVWAHHMFTV 293

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863 241 GLEVDTRAFFTSTTILISIPTGTKVFNWLCTYMSTNFGIThSSSLLSLLFICTFTFGGTTGVILGNGAIDVALHDTYYVI 320
Cdd:MTH00153  294 GMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYS-PSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVV 372

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863 321 AHFHFVLSIGAIIALFTSVSFFQESFFGKTLRENTIIVLWSILfFVGVVLTFLPMHFLGFNVMPRRIPDYPDALNGWNMI 400
Cdd:MTH00153  373 AHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIM-FIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVI 451

                         410
                  ....*....|....*
gi 1931720863 401 CSIGSTMTLFGLLIF 415
Cdd:MTH00153  452 SSIGSTISLISILFF 466
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
2-415 8.01e-128

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 379.09  E-value: 8.01e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863   2 IFTVHGIIMIFFNIMPgLFGGFGNYFLPILCGSSELAYPRINSISLLLQPIAFILVILSTAAEFGGGTGWTLYPPLSTSL 81
Cdd:COG0843    60 LFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLE 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863  82 MSlSPVAVDVIVIGLLVSGIASIMSSLNFLTTVMHLRAKGLTLGILSVSTWSLIITSVMLLLTLPVLTGGVLMLLSDLHF 161
Cdd:COG0843   139 AS-PGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSL 217

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863 162 NTLFFDPTFAGDPILYQHLFWFFGHPEVYILILPAFGIISHVISTNYCRSLFGNQSMILAMGCIAVLGSVVWVHHMYTTG 241
Cdd:COG0843   218 GTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFSRKPLFGYKAMVLATVAIAFLSFLVWAHHMFTPG 297

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863 242 LEVDTRAFFTSTTILISIPTGTKVFNWLCTYMSTNFGIThSSSLLSLLFICTFTFGGTTGVILGNGAIDVALHDTYYVIA 321
Cdd:COG0843   298 ISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFT-TPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVA 376

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863 322 HFHFVLSIGAIIALFTSVSFFQESFFGKTLRENT-IIVLWsiLFFVGVVLTFLPMHFLGFNVMPRRIPDYP--DALNGWN 398
Cdd:COG0843   377 HFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLgKIHFW--LWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLN 454

                         410
                  ....*....|....*..
gi 1931720863 399 MICSIGSTMTLFGLLIF 415
Cdd:COG0843   455 LISTIGAFILAVGFLLF 471
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 2-415 3.08e-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: 376.56  E-value: 3.08e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863   2 IFTVHGIIMIFFNIMPgLFGGFGNYFLPILCGSSELAYPRINSISLLLQPIAFILVILSTAAEFGGGTGWTLYPPLSTSL 81
Cdd:TIGR02891  51 LFTMHGTIMIFLFAIP-ILAGFGNYLLPLMIGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTS 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863  82 MSlSPVAVDVIVIGLLVSGIASIMSSLNFLTTVMHLRAKGLTLGILSVSTWSLIITSVMLLLTLPVLTGGVLMLLSDLHF 161
Cdd:TIGR02891 130 GS-PGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLF 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863 162 NTLFFDPTFAGDPILYQHLFWFFGHPEVYILILPAFGIISHVISTNYCRSLFGNQSMILAMGCIAVLGSVVWVHHMYTTG 241
Cdd:TIGR02891 209 GTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFARKPIFGYRAMVYATVAIGFLSFGVWAHHMFTTG 288

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863 242 LEVDTRAFFTSTTILISIPTGTKVFNWLCTYMSTNFGIThSSSLLSLLFICTFTFGGTTGVILGNGAIDVALHDTYYVIA 321
Cdd:TIGR02891 289 MPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFT-TPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVA 367

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863 322 HFHFVLSIGAIIALFTSVSFFQESFFGKTLRENT-IIVLWsiLFFVGVVLTFLPMHFLGFNVMPRRIPDYPDALN--GWN 398
Cdd:TIGR02891 368 HFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLgRWHFW--LTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQMGfaTLN 445

                         410
                  ....*....|....*..
gi 1931720863 399 MICSIGSTMTLFGLLIF 415
Cdd:TIGR02891 446 LISTIGAFILAAGFLVF 462
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 2-407 1.24e-91

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: 282.92  E-value: 1.24e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863   2 IFTVHGIIMIFFNIMPGLFGgFGNYFLPILCGSSELAYPRINSISLLLQPIAFILVILSTAaefGGGTGWTLYPPLstsl 81
Cdd:pfam00115  44 LRTLHGNLMIFWFATPFLFG-FGNYLVPLMIGARDMAFPRLNALSFWLVVLGAVLLLASFG---GATTGWTEYPPL---- 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863  82 mslspVAVDVIVIGLLVSGIASIMSSLNFLTTVMHLRAKGLTLgILSVSTWSLIITSVMLLLTLPVLTGGVLMLLSDLHF 161
Cdd:pfam00115 116 -----VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSL 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863 162 NTLffdptfAGDPILYQHLFWFFGHPEVYILILPAFGIISHVISTNYCRSLFGNQSMILAMGCIAVLGSVVWVHHMYTTG 241
Cdd:pfam00115 190 GAG------GGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGRPLFGYKLSVLAFWLIAFLGFLVWAHHLFTTG 263

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863 242 LEVDTRAFFTSTTILISIPTGTKVFNWLCTYMSTNFGITHSSSLLSLLFICTFTFGGTTGVILGNGAIDVALHDTYYVIA 321
Cdd:pfam00115 264 LPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFRTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVA 343

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863 322 HFHFVLSIGAIIALFTSVSFFQESFFGKTLRENTIIVLWsILFFVGVVLTFLPMHFLGFNVMPRRIP----DYPDALNGW 397
Cdd:pfam00115 344 HFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHF-WLLFIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPL 422

                         410
                  ....*....|
gi 1931720863 398 NMICSIGSTM 407
Cdd:pfam00115 423 NWIRTIGGVL 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 ...
 1-415 4.11e-172

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: 490.46  E-value: 4.11e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863   1 MIFTVHGIIMIFFNIMPGLFGGFGNYFLPILCGSSELAYPRINSISLLLQPIAFILVILSTAAEFGGGTGWTLYPPLStS 80
Cdd:cd01663    47 VIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLS-S 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863  81 LMSLSPVAVDVIVIGLLVSGIASIMSSLNFLTTVMHLRAKGLTLGILSVSTWSLIITSVMLLLTLPVLTGGVLMLLSDLH 160
Cdd:cd01663   126 ILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRN 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863 161 FNTLFFDPTFAGDPILYQHLFWFFGHPEVYILILPAFGIISHVISTNYCR-SLFGNQSMILAMGCIAVLGSVVWVHHMYT 239
Cdd:cd01663   206 FNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSGKkPVFGYLGMVYAMLSIGILGFIVWAHHMFT 285

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863 240 TGLEVDTRAFFTSTTILISIPTGTKVFNWLCTYMSTNFGIThSSSLLSLLFICTFTFGGTTGVILGNGAIDVALHDTYYV 319
Cdd:cd01663   286 VGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFE-TPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYV 364

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863 320 IAHFHFVLSIGAIIALFTSVSFFQESFFGKTLRENTIIVLWsILFFVGVVLTFLPMHFLGFNVMPRRIPDYPDALNGWNM 399
Cdd:cd01663   365 VAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHF-WLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNM 443

                         410
                  ....*....|....*.
gi 1931720863 400 ICSIGSTMTLFGLLIF 415
Cdd:cd01663   444 ISSIGSLISFVSVLLF 459
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 2-415 4.33e-153

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 442.77  E-value: 4.33e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863   2 IFTVHGIIMIFFNIMPGLFGGFGNYFLPILCGSSELAYPRINSISLLLQPIAFILVILSTAAEFGGGTGWTLYPPLStSL 81
Cdd:MTH00153   55 IVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLS-SN 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863  82 MSLSPVAVDVIVIGLLVSGIASIMSSLNFLTTVMHLRAKGLTLGILSVSTWSLIITSVMLLLTLPVLTGGVLMLLSDLHF 161
Cdd:MTH00153  134 IAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNL 213

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863 162 NTLFFDPTFAGDPILYQHLFWFFGHPEVYILILPAFGIISHVISTNYC-RSLFGNQSMILAMGCIAVLGSVVWVHHMYTT 240
Cdd:MTH00153  214 NTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGkKETFGTLGMIYAMLAIGLLGFIVWAHHMFTV 293

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863 241 GLEVDTRAFFTSTTILISIPTGTKVFNWLCTYMSTNFGIThSSSLLSLLFICTFTFGGTTGVILGNGAIDVALHDTYYVI 320
Cdd:MTH00153  294 GMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYS-PSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVV 372

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863 321 AHFHFVLSIGAIIALFTSVSFFQESFFGKTLRENTIIVLWSILfFVGVVLTFLPMHFLGFNVMPRRIPDYPDALNGWNMI 400
Cdd:MTH00153  373 AHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIM-FIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVI 451

                         410
                  ....*....|....*
gi 1931720863 401 CSIGSTMTLFGLLIF 415
Cdd:MTH00153  452 SSIGSTISLISILFF 466
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-415 3.61e-150

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 435.56  E-value: 3.61e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863   1 MIFTVHGIIMIFFNIMPGLFGGFGNYFLPILCGSSELAYPRINSISLLLQPIAFILVILSTAAEFGGGTGWTLYPPLStS 80
Cdd:MTH00223   53 VIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLS-S 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863  81 LMSLSPVAVDVIVIGLLVSGIASIMSSLNFLTTVMHLRAKGLTLGILSVSTWSLIITSVMLLLTLPVLTGGVLMLLSDLH 160
Cdd:MTH00223  132 NLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRN 211

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863 161 FNTLFFDPTFAGDPILYQHLFWFFGHPEVYILILPAFGIISHVIStNYC--RSLFGNQSMILAMGCIAVLGSVVWVHHMY 238
Cdd:MTH00223  212 FNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVS-HYSskKEVFGTLGMIYAMLSIGVLGFIVWAHHMF 290

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863 239 TTGLEVDTRAFFTSTTILISIPTGTKVFNWLCTyMSTNFGITHSSSLLSLLFICTFTFGGTTGVILGNGAIDVALHDTYY 318
Cdd:MTH00223  291 TVGMDVDTRAYFTAATMIIAVPTGIKVFSWLAT-IYGSKIKYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYY 369

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863 319 VIAHFHFVLSIGAIIALFTSVSFFQESFFGKTLREntiivLWS----ILFFVGVVLTFLPMHFLGFNVMPRRIPDYPDAL 394
Cdd:MTH00223  370 VVAHFHYVLSMGAVFALFAGFNHWFPLFTGVTLHR-----RWAkahfFLMFLGVNLTFFPQHFLGLAGMPRRYSDYPDCY 444

                         410       420
                  ....*....|....*....|.
gi 1931720863 395 NGWNMICSIGSTMTLFGLLIF 415
Cdd:MTH00223  445 TKWNQVSSFGSMISFVSVLFF 465
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 2-415 5.06e-146

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 424.86  E-value: 5.06e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863   2 IFTVHGIIMIFFNIMPGLFGGFGNYFLPILCGSSELAYPRINSISLLLQPIAFILVILSTAAEFGGGTGWTLYPPLSTSL 81
Cdd:MTH00167   57 IVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNL 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863  82 MSLSPvAVDVIVIGLLVSGIASIMSSLNFLTTVMHLRAKGLTLGILSVSTWSLIITSVMLLLTLPVLTGGVLMLLSDLHF 161
Cdd:MTH00167  137 AHAGA-SVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNL 215

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863 162 NTLFFDPTFAGDPILYQHLFWFFGHPEVYILILPAFGIISHVISTNYCR-SLFGNQSMILAMGCIAVLGSVVWVHHMYTT 240
Cdd:MTH00167  216 NTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVVYYSGKkEPFGYMGMVWAMMAIGLLGFIVWAHHMFTV 295

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863 241 GLEVDTRAFFTSTTILISIPTGTKVFNWLCTYMSTNFgITHSSSLLSLLFICTFTFGGTTGVILGNGAIDVALHDTYYVI 320
Cdd:MTH00167  296 GMDVDTRAYFTSATMIIAVPTGIKVFSWLATLHGGKI-KWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVV 374

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863 321 AHFHFVLSIGAIIALFTSVSFFQESFFGKTLRE-NTIIVLWsiLFFVGVVLTFLPMHFLGFNVMPRRIPDYPDALNGWNM 399
Cdd:MTH00167  375 AHFHYVLSMGAVFAIMAGFTHWFPLFTGLTLNEtWTKIHFF--VMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNV 452

                         410
                  ....*....|....*.
gi 1931720863 400 ICSIGSTMTLFGLLIF 415
Cdd:MTH00167  453 VSSIGSLISLVAVILF 468
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 2-415 1.66e-136

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 400.64  E-value: 1.66e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863   2 IFTVHGIIMIFFNIMPGLFGGFGNYFLPILCGSSELAYPRINSISLLLQPIAFILVILSTAAEFGGGTGWTLYPPLStSL 81
Cdd:MTH00142   55 IVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLS-SN 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863  82 MSLSPVAVDVIVIGLLVSGIASIMSSLNFLTTVMHLRAKGLTLGILSVSTWSLIITSVMLLLTLPVLTGGVLMLLSDLHF 161
Cdd:MTH00142  134 LAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNF 213

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863 162 NTLFFDPTFAGDPILYQHLFWFFGHPEVYILILPAFGIISHVIsTNYC--RSLFGNQSMILAMGCIAVLGSVVWVHHMYT 239
Cdd:MTH00142  214 NTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHII-NHYSgkKEVFGTLGMIYAMLSIGLLGFIVWAHHMFT 292

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863 240 TGLEVDTRAFFTSTTILISIPTGTKVFNWLCTYMSTNFGItHSSSLLSLLFICTFTFGGTTGVILGNGAIDVALHDTYYV 319
Cdd:MTH00142  293 VGMDVDTRAYFTAATMVIAVPTGIKVFSWLATLHGSKVKY-EPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYV 371

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863 320 IAHFHFVLSIGAIIALFTSVSFFQESFFGKTLRENTIIVLWSILfFVGVVLTFLPMHFLGFNVMPRRIPDYPDALNGWNM 399
Cdd:MTH00142  372 VAHFHYVLSMGAVFALFAGFIHWFPLFTGLTLNPRWLKAHFYTM-FIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNV 450

                         410
                  ....*....|....*.
gi 1931720863 400 ICSIGSTMTLFGLLIF 415
Cdd:MTH00142  451 VSSLGSMISFIAVLMF 466
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-415 3.91e-136

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 399.85  E-value: 3.91e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863   1 MIFTVHGIIMIFFNIMPGLFGGFGNYFLPILCGSSELAYPRINSISLLLQPIAFILVILSTAAEFGGGTGWTLYPPLSTS 80
Cdd:MTH00116   56 VIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGN 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863  81 LMSLSPvAVDVIVIGLLVSGIASIMSSLNFLTTVMHLRAKGLTLGILSVSTWSLIITSVMLLLTLPVLTGGVLMLLSDLH 160
Cdd:MTH00116  136 LAHAGA-SVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRN 214

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863 161 FNTLFFDPTFAGDPILYQHLFWFFGHPEVYILILPAFGIISHVISTNYC-RSLFGNQSMILAMGCIAVLGSVVWVHHMYT 239
Cdd:MTH00116  215 LNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVTYYAGkKEPFGYMGMVWAMLSIGFLGFIVWAHHMFT 294

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863 240 TGLEVDTRAFFTSTTILISIPTGTKVFNWLCTYMStnfGITH--SSSLLSLLFICTFTFGGTTGVILGNGAIDVALHDTY 317
Cdd:MTH00116  295 VGMDVDTRAYFTSATMIIAIPTGIKVFSWLATLHG---GTIKwdPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTY 371

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863 318 YVIAHFHFVLSIGAIIALFTSVSFFQESFFGKTLREN-TIIVLWsiLFFVGVVLTFLPMHFLGFNVMPRRIPDYPDALNG 396
Cdd:MTH00116  372 YVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGYTLHQTwTKAQFG--VMFTGVNLTFFPQHFLGLAGMPRRYSDYPDAYTL 449

                         410
                  ....*....|....*....
gi 1931720863 397 WNMICSIGSTMTLFGLLIF 415
Cdd:MTH00116  450 WNTISSIGSLISMTAVIML 468
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 2-415 9.06e-135

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 395.97  E-value: 9.06e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863   2 IFTVHGIIMIFFNIMPGLFGGFGNYFLPILCGSSELAYPRINSISLLLQPIAFILVILSTAAEFGGGTGWTLYPPLSTsl 81
Cdd:MTH00079   58 VITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPRLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLST-- 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863  82 MSLSPVAVDVIVIGLLVSGIASIMSSLNFLTTVMHLRAKGLTLGILSVSTWSLIITSVMLLLTLPVLTGGVLMLLSDLHF 161
Cdd:MTH00079  136 LGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNL 215

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863 162 NTLFFDPTFAGDPILYQHLFWFFGHPEVYILILPAFGIISHVIST-NYCRSLFGNQSMILAMGCIAVLGSVVWVHHMYTT 240
Cdd:MTH00079  216 NTSFFDPSTGGNPLLYQHLFWFFGHPEVYILILPAFGIISQSTLYlTGKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTV 295

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863 241 GLEVDTRAFFTSTTILISIPTGTKVFNWLCTYMSTNFgITHSSSLLSLLFICTFTFGGTTGVILGNGAIDVALHDTYYVI 320
Cdd:MTH00079  296 GMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKM-KFQPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVV 374

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863 321 AHFHFVLSIGAIIALFTSVSFFQESFFGKTLRENTIIVLWsILFFVGVVLTFLPMHFLGFNVMPRRIPDYPDALNGWNMI 400
Cdd:MTH00079  375 SHFHYVLSLGAVFGIFTGISLWWPFMTGIVYDKLMMSAVF-FLMFVGVNLTFFPLHFAGLHGMPRKYLDYPDVYSVWNVI 453

                         410
                  ....*....|....*
gi 1931720863 401 CSIGSTMTLFGLLIF 415
Cdd:MTH00079  454 SSYGSMISVFALFLF 468
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 2-415 5.48e-134

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: 392.28  E-value: 5.48e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863   2 IFTVHGIIMIFFNIMPGLFGGFGNYFLPILcGSSELAYPRINSISLLLQPIAFILVILSTAAEFGGGTGWTLYPPLSTSL 81
Cdd:cd00919    46 LVTAHGVIMIFFFVMPAIFGGFGNLLPPLI-GARDLAFPRLNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLS 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863  82 MSlSPVAVDVIVIGLLVSGIASIMSSLNFLTTVMHLRAKGLTLGILSVSTWSLIITSVMLLLTLPVLTGGVLMLLSDLHF 161
Cdd:cd00919   125 YS-SGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNF 203

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863 162 NTLFFDPTFAGDPILYQHLFWFFGHPEVYILILPAFGIISHVISTNYCRSLFGNQSMILAMGCIAVLGSVVWVHHMYTTG 241
Cdd:cd00919   204 GTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAFGAISEIIPTFSGKPLFGYKLMVYAFLAIGFLSFLVWAHHMFTVG 283

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863 242 LEVDTRAFFTSTTILISIPTGTKVFNWLCTyMSTNFGITHSSSLLSLLFICTFTFGGTTGVILGNGAIDVALHDTYYVIA 321
Cdd:cd00919   284 LPVDTRAYFTAATMIIAVPTGIKVFNWLAT-LWGGRIRFDPPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVA 362

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863 322 HFHFVLSIGAIIALFTSVSFFQESFFGKTLRENTIIVLWsILFFVGVVLTFLPMHFLGFNVMPRRIPDYPDALNGWNMIC 401
Cdd:cd00919   363 HFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKLGKIHF-WLWFIGFNLTFFPMHFLGLLGMPRRYADYPDGFAPWNFIS 441

                         410
                  ....*....|....
gi 1931720863 402 SIGSTMTLFGLLIF 415
Cdd:cd00919   442 SVGAFILGLGLLLF 455
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 2-415 9.69e-131

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 385.79  E-value: 9.69e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863   2 IFTVHGIIMIFFNIMPGLFGGFGNYFLPILCGSSELAYPRINSISLLLQPIAFILVILSTAAEFGGGTGWTLYPPLSTSL 81
Cdd:MTH00007   54 IVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNL 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863  82 MSLSPvAVDVIVIGLLVSGIASIMSSLNFLTTVMHLRAKGLTLGILSVSTWSLIITSVMLLLTLPVLTGGVLMLLSDLHF 161
Cdd:MTH00007  134 AHAGP-SVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNL 212

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863 162 NTLFFDPTFAGDPILYQHLFWFFGHPEVYILILPAFGIISHVIsTNYCRSL--FGNQSMILAMGCIAVLGSVVWVHHMYT 239
Cdd:MTH00007  213 NTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGAISHIV-THYAGKLepFGTLGMIYAMLGIGVLGFIVWAHHMFT 291

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863 240 TGLEVDTRAFFTSTTILISIPTGTKVFNWLCTYMSTNFGiTHSSSLLSLLFICTFTFGGTTGVILGNGAIDVALHDTYYV 319
Cdd:MTH00007  292 VGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGSPIK-YETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYV 370

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863 320 IAHFHFVLSIGAIIALFTSVSFFQESFFGKTLRENTIIVLWsILFFVGVVLTFLPMHFLGFNVMPRRIPDYPDALNGWNM 399
Cdd:MTH00007  371 VAHFHYVLSMGAVFAIFAAFNHWFPLFTGLTLHDRWAKAHF-FLMFLGVNLTFFPQHFLGLSGMPRRYSDYPDAYTKWNV 449

                         410
                  ....*....|....*.
gi 1931720863 400 ICSIGSTMTLFGLLIF 415
Cdd:MTH00007  450 VSSFGSMLSFVALLLF 465
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
2-415 8.01e-128

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 379.09  E-value: 8.01e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863   2 IFTVHGIIMIFFNIMPgLFGGFGNYFLPILCGSSELAYPRINSISLLLQPIAFILVILSTAAEFGGGTGWTLYPPLSTSL 81
Cdd:COG0843    60 LFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLE 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863  82 MSlSPVAVDVIVIGLLVSGIASIMSSLNFLTTVMHLRAKGLTLGILSVSTWSLIITSVMLLLTLPVLTGGVLMLLSDLHF 161
Cdd:COG0843   139 AS-PGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSL 217

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863 162 NTLFFDPTFAGDPILYQHLFWFFGHPEVYILILPAFGIISHVISTNYCRSLFGNQSMILAMGCIAVLGSVVWVHHMYTTG 241
Cdd:COG0843   218 GTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFSRKPLFGYKAMVLATVAIAFLSFLVWAHHMFTPG 297

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863 242 LEVDTRAFFTSTTILISIPTGTKVFNWLCTYMSTNFGIThSSSLLSLLFICTFTFGGTTGVILGNGAIDVALHDTYYVIA 321
Cdd:COG0843   298 ISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFT-TPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVA 376

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863 322 HFHFVLSIGAIIALFTSVSFFQESFFGKTLRENT-IIVLWsiLFFVGVVLTFLPMHFLGFNVMPRRIPDYP--DALNGWN 398
Cdd:COG0843   377 HFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLgKIHFW--LWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLN 454

                         410
                  ....*....|....*..
gi 1931720863 399 MICSIGSTMTLFGLLIF 415
Cdd:COG0843   455 LISTIGAFILAVGFLLF 471
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-415 9.70e-128

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 378.40  E-value: 9.70e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863   1 MIFTVHGIIMIFFNIMPGLFGGFGNYFLPILCGSSELAYPRINSISLLLQPIAFILVILSTAAEFGGGTGWTLYPPLSTS 80
Cdd:MTH00037   56 VIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSN 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863  81 LmSLSPVAVDVIVIGLLVSGIASIMSSLNFLTTVMHLRAKGLTLGILSVSTWSLIITSVMLLLTLPVLTGGVLMLLSDLH 160
Cdd:MTH00037  136 I-AHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRN 214

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863 161 FNTLFFDPTFAGDPILYQHLFWFFGHPEVYILILPAFGIISHVISTNYCRSL-FGNQSMILAMGCIAVLGSVVWVHHMYT 239
Cdd:MTH00037  215 INTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKQEpFGYLGMVYAMIAIGILGFLVWAHHMFT 294

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863 240 TGLEVDTRAFFTSTTILISIPTGTKVFNWLCTYMSTNFGIThSSSLLSLLFICTFTFGGTTGVILGNGAIDVALHDTYYV 319
Cdd:MTH00037  295 VGMDVDTRAYFTAATMIIAVPTGIKVFSWMATLQGSNLRWE-TPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYV 373

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863 320 IAHFHFVLSIGAIIALFTSVSFFQESFFGKTLRENTIIVLWsILFFVGVVLTFLPMHFLGFNVMPRRIPDYPDALNGWNM 399
Cdd:MTH00037  374 VAHFHYVLSMGAVFAIFAGFTHWFPLFSGVSLHPLWSKVHF-FLMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNT 452

                         410
                  ....*....|....*.
gi 1931720863 400 ICSIGSTMTLFGLLIF 415
Cdd:MTH00037  453 VSSIGSTISLVATLFF 468
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 2-415 3.08e-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: 376.56  E-value: 3.08e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863   2 IFTVHGIIMIFFNIMPgLFGGFGNYFLPILCGSSELAYPRINSISLLLQPIAFILVILSTAAEFGGGTGWTLYPPLSTSL 81
Cdd:TIGR02891  51 LFTMHGTIMIFLFAIP-ILAGFGNYLLPLMIGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTS 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863  82 MSlSPVAVDVIVIGLLVSGIASIMSSLNFLTTVMHLRAKGLTLGILSVSTWSLIITSVMLLLTLPVLTGGVLMLLSDLHF 161
Cdd:TIGR02891 130 GS-PGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLF 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863 162 NTLFFDPTFAGDPILYQHLFWFFGHPEVYILILPAFGIISHVISTNYCRSLFGNQSMILAMGCIAVLGSVVWVHHMYTTG 241
Cdd:TIGR02891 209 GTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFARKPIFGYRAMVYATVAIGFLSFGVWAHHMFTTG 288

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863 242 LEVDTRAFFTSTTILISIPTGTKVFNWLCTYMSTNFGIThSSSLLSLLFICTFTFGGTTGVILGNGAIDVALHDTYYVIA 321
Cdd:TIGR02891 289 MPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFT-TPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVA 367

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863 322 HFHFVLSIGAIIALFTSVSFFQESFFGKTLRENT-IIVLWsiLFFVGVVLTFLPMHFLGFNVMPRRIPDYPDALN--GWN 398
Cdd:TIGR02891 368 HFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLgRWHFW--LTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQMGfaTLN 445

                         410
                  ....*....|....*..
gi 1931720863 399 MICSIGSTMTLFGLLIF 415
Cdd:TIGR02891 446 LISTIGAFILAAGFLVF 462
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-415 1.53e-126

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 375.42  E-value: 1.53e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863   1 MIFTVHGIIMIFFNIMPGLFGGFGNYFLPILCGSSELAYPRINSISLLLQPIAFILVILSTAAEFGGGTGWTLYPPLSTS 80
Cdd:MTH00183   56 VIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGN 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863  81 LMSLSPvAVDVIVIGLLVSGIASIMSSLNFLTTVMHLRAKGLTLGILSVSTWSLIITSVMLLLTLPVLTGGVLMLLSDLH 160
Cdd:MTH00183  136 LAHAGA-SVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRN 214

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863 161 FNTLFFDPTFAGDPILYQHLFWFFGHPEVYILILPAFGIISHVISTNYCRS-LFGNQSMILAMGCIAVLGSVVWVHHMYT 239
Cdd:MTH00183  215 LNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVAYYSGKKePFGYMGMVWAMMAIGLLGFIVWAHHMFT 294

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863 240 TGLEVDTRAFFTSTTILISIPTGTKVFNWLCTYMSTNFGiTHSSSLLSLLFICTFTFGGTTGVILGNGAIDVALHDTYYV 319
Cdd:MTH00183  295 VGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGSIK-WETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYV 373

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863 320 IAHFHFVLSIGAIIALFTSVSFFQESFFGKTLRENTIIVLWSILfFVGVVLTFLPMHFLGFNVMPRRIPDYPDALNGWNM 399
Cdd:MTH00183  374 VAHFHYVLSMGAVFAIMAAFVHWFPLFSGYTLHSTWTKIHFGVM-FVGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNT 452

                         410
                  ....*....|....*.
gi 1931720863 400 ICSIGSTMTLFGLLIF 415
Cdd:MTH00183  453 VSSIGSLISLVAVIMF 468
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-414 3.72e-126

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 374.28  E-value: 3.72e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863   1 MIFTVHGIIMIFFNIMPGLFGGFGNYFLPILCGSSELAYPRINSISLLLQPIAFILVILSTAAEFGGGTGWTLYPPLSTS 80
Cdd:MTH00077   56 VIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGN 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863  81 LMSLSPvAVDVIVIGLLVSGIASIMSSLNFLTTVMHLRAKGLTLGILSVSTWSLIITSVMLLLTLPVLTGGVLMLLSDLH 160
Cdd:MTH00077  136 LAHAGA-SVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRN 214

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863 161 FNTLFFDPTFAGDPILYQHLFWFFGHPEVYILILPAFGIISHVIS-TNYCRSLFGNQSMILAMGCIAVLGSVVWVHHMYT 239
Cdd:MTH00077  215 LNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISHIVTyYSAKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFT 294

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863 240 TGLEVDTRAFFTSTTILISIPTGTKVFNWLCTyMSTNFGITHSSSLLSLLFICTFTFGGTTGVILGNGAIDVALHDTYYV 319
Cdd:MTH00077  295 VDLNVDTRAYFTSATMIIAIPTGVKVFSWLAT-MHGGAIKWDAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYV 373

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863 320 IAHFHFVLSIGAIIALFTSVSFFQESFFGKTLRENTIIVLWSILfFVGVVLTFLPMHFLGFNVMPRRIPDYPDALNGWNM 399
Cdd:MTH00077  374 VAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLHSTWSKIHFGVM-FIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNT 452

                         410
                  ....*....|....*
gi 1931720863 400 ICSIGSTMTLFGLLI 414
Cdd:MTH00077  453 VSSIGSLISLVAVIM 467
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-414 1.58e-124

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 369.98  E-value: 1.58e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863   1 MIFTVHGIIMIFFNIMPGLFGGFGNYFLPILCGSSELAYPRINSISLLLQPIAFILVILSTAAEFGGGTGWTLYPPLSTS 80
Cdd:MTH00103   56 VIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGN 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863  81 LmSLSPVAVDVIVIGLLVSGIASIMSSLNFLTTVMHLRAKGLTLGILSVSTWSLIITSVMLLLTLPVLTGGVLMLLSDLH 160
Cdd:MTH00103  136 L-AHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRN 214

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863 161 FNTLFFDPTFAGDPILYQHLFWFFGHPEVYILILPAFGIISHVIsTNYC--RSLFGNQSMILAMGCIAVLGSVVWVHHMY 238
Cdd:MTH00103  215 LNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIV-TYYSgkKEPFGYMGMVWAMMSIGFLGFIVWAHHMF 293

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863 239 TTGLEVDTRAFFTSTTILISIPTGTKVFNWLCTYMSTNFGIThSSSLLSLLFICTFTFGGTTGVILGNGAIDVALHDTYY 318
Cdd:MTH00103  294 TVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGNIKWS-PAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYY 372

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863 319 VIAHFHFVLSIGAIIALFTSVSFFQESFFGKTLRENTIIVLWSILfFVGVVLTFLPMHFLGFNVMPRRIPDYPDALNGWN 398
Cdd:MTH00103  373 VVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLNDTWAKIHFTIM-FVGVNMTFFPQHFLGLSGMPRRYSDYPDAYTTWN 451

                         410
                  ....*....|....*.
gi 1931720863 399 MICSIGSTMTLFGLLI 414
Cdd:MTH00103  452 TVSSMGSFISLTAVML 467
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-415 7.33e-124

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 368.77  E-value: 7.33e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863   1 MIFTVHGIIMIFFNIMPGLFGGFGNYFLPILCGSSELAYPRINSISLLLQPIAFILVILSTAAEFGGGTGWTLYPPLStS 80
Cdd:MTH00184   58 VIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLS-S 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863  81 LMSLSPVAVDVIVIGLLVSGIASIMSSLNFLTTVMHLRAKGLTLGILSVSTWSLIITSVMLLLTLPVLTGGVLMLLSDLH 160
Cdd:MTH00184  137 IQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRN 216

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863 161 FNTLFFDPTFAGDPILYQHLFWFFGHPEVYILILPAFGIISHVIST-NYCRSLFGNQSMILAMGCIAVLGSVVWVHHMYT 239
Cdd:MTH00184  217 FNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQIIPTfAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFT 296

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863 240 TGLEVDTRAFFTSTTILISIPTGTKVFNWLCTYMSTNFgITHSSSLLSLLFICTFTFGGTTGVILGNGAIDVALHDTYYV 319
Cdd:MTH00184  297 VGMDVDTRAYFTAATMIIAVPTGIKIFSWIATIFGGSL-RLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYV 375

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863 320 IAHFHFVLSIGAIIALFTSVSFFQESFFGKTLRE-NTIIVLWsiLFFVGVVLTFLPMHFLGFNVMPRRIPDYPDALNGWN 398
Cdd:MTH00184  376 VAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNEvYGKIHFW--LMFIGVNLTFFPQHFLGLAGLPRRYSDFHDSFAGWN 453

                         410
                  ....*....|....*..
gi 1931720863 399 MICSIGSTMTLFGLLIF 415
Cdd:MTH00184  454 QISSLGSVISIVGVVWF 470
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-415 1.75e-123

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 367.99  E-value: 1.75e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863   1 MIFTVHGIIMIFFNIMPGLFGGFGNYFLPILCGSSELAYPRINSISLLLQPIAFILVILSTAAEFGGGTGWTLYPPLStS 80
Cdd:MTH00182   58 VIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLS-S 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863  81 LMSLSPVAVDVIVIGLLVSGIASIMSSLNFLTTVMHLRAKGLTLGILSVSTWSLIITSVMLLLTLPVLTGGVLMLLSDLH 160
Cdd:MTH00182  137 IQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRN 216

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863 161 FNTLFFDPTFAGDPILYQHLFWFFGHPEVYILILPAFGIISHVISTNYC-RSLFGNQSMILAMGCIAVLGSVVWVHHMYT 239
Cdd:MTH00182  217 FNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISQIIPTFVAkKQIFGYLGMVYAMLSIGILGFIVWAHHMFT 296

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863 240 TGLEVDTRAFFTSTTILISIPTGTKVFNWLCTYMSTNFGIThSSSLLSLLFICTFTFGGTTGVILGNGAIDVALHDTYYV 319
Cdd:MTH00182  297 VGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGGTLRLD-TPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYV 375

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863 320 IAHFHFVLSIGAIIALFTSVSFFQESFFGKTLRE-NTIIVLWsiLFFVGVVLTFLPMHFLGFNVMPRRIPDYPDALNGWN 398
Cdd:MTH00182  376 VAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNElYGKIHFW--LMFIGVNLTFFPQHFLGLAGFPRRYSDFADAFAGWN 453

                         410
                  ....*....|....*..
gi 1931720863 399 MICSIGSTMTLFGLLIF 415
Cdd:MTH00182  454 LVSSLGSIISIVGVVWF 470
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 2-415 2.15e-117

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: 351.50  E-value: 2.15e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863   2 IFTVHGIIMIFFNIMPgLFGGFGNYFLPILCGSSELAYPRINSISLLLQPIAFILVILSTAAEFGGGTGWTLYPPLSTSL 81
Cdd:cd01662    52 IFTMHGTIMIFLFAMP-LVFGLMNYLVPLQIGARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLE 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863  82 MSlSPVAVDVIVIGLLVSGIASIMSSLNFLTTVMHLRAKGLTLGILSVSTWSLIITSVMLLLTLPVLTGGVLMLLSDLHF 161
Cdd:cd01662   131 YS-PGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYF 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863 162 NTLFFDPTFAGDPILYQHLFWFFGHPEVYILILPAFGIISHVISTNYCRSLFGNQSMILAMGCIAVLGSVVWVHHMYTTG 241
Cdd:cd01662   210 GTHFFTNALGGNPMLWQHLFWIFGHPEVYILILPAFGIFSEIVPTFSRKPLFGYRSMVYATVAIGFLSFGVWVHHMFTTG 289

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863 242 LEVDTRAFFTSTTILISIPTGTKVFNWLCTyMSTNFGITHSSSLLSLLFICTFTFGGTTGVILGNGAIDVALHDTYYVIA 321
Cdd:cd01662   290 AGALVNAFFSIATMIIAVPTGVKIFNWLFT-MWRGRIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVA 368

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863 322 HFHFVLSIGAIIALFTSVSFFQESFFGKTLRENT-IIVLWsiLFFVGVVLTFLPMHFLGFNVMPRRIPDYP--DALNGWN 398
Cdd:cd01662   369 HFHYVLIGGVVFPLFAGFYYWFPKMFGRMLNERLgKWSFW--LWFIGFNLTFFPMHILGLMGMPRRVYTYLpgPGWDPLN 446

                         410
                  ....*....|....*..
gi 1931720863 399 MICSIGSTMTLFGLLIF 415
Cdd:cd01662   447 LISTIGAFLIAAGVLLF 463
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 4-415 1.78e-114

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 344.35  E-value: 1.78e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863   4 TVHGIIMIFFNIMPGLFGGFGNYFLPILCGSSELAYPRINSISLLLQPIAFILVILSTAaeFGGGTGWTLYPPLSTSLMS 83
Cdd:MTH00048   60 TNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRLNALSAWLLVPSIVFLLLSMC--LGAGVGWTFYPPLSSSLFS 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863  84 LSpVAVDVIVIGLLVSGIASIMSSLNFLTTVMHLRAKGLTLGIlSVSTWSLIITSVMLLLTLPVLTGGVLMLLSDLHFNT 163
Cdd:MTH00048  138 SS-WGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNVFSRT-SIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGS 215

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863 164 LFFDPTFAGDPILYQHLFWFFGHPEVYILILPAFGIISHV-ISTNYCRSLFGNQSMILAMGCIAVLGSVVWVHHMYTTGL 242
Cdd:MTH00048  216 AFFDPLGGGDPVLFQHMFWFFGHPEVYVLILPGFGIISHIcLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGL 295

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863 243 EVDTRAFFTSTTILISIPTGTKVFNWLCTYMSTNFGITHSSSLLSLLFICTFTFGGTTGVILGNGAIDVALHDTYYVIAH 322
Cdd:MTH00048  296 DVKTAVFFSSVTMIIGVPTGIKVFSWLYMLLNSRVRKSDPVVWWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAH 375

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863 323 FHFVLSIGAIIALFTSVSFFQESFFGKTLRENTIIVLWsILFFVGVVLTFLPMHFLGFNVMPRRIPDYPDALNGWNMICS 402
Cdd:MTH00048  376 FHYVLSLGSYSSVVIMFIWWWPLITGLSLNKYLLQCHC-IISMIGFNLCFFPMHYFGLCGLPRRVCVYEPSYYWINVVCT 454

                         410
                  ....*....|...
gi 1931720863 403 IGSTMTLFGLLIF 415
Cdd:MTH00048  455 VGSFISAFSGCFF 467
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-415 2.15e-114

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 345.07  E-value: 2.15e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863   1 MIFTVHGIIMIFFNIMPGLFGGFGNYFLPILCGSSELAYPRINSISLLLQPIAFILVILSTAAEFGGGTGWTLYPPLStS 80
Cdd:MTH00026   57 VIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPRLNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLA-S 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863  81 LMSLSPVAVDVIVIGLLVSGIASIMSSLNFLTTVMHLRAKGLTLGILSVSTWSLIITSVMLLLTLPVLTGGVLMLLSDLH 160
Cdd:MTH00026  136 IQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRN 215

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863 161 FNTLFFDPTFAGDPILYQHLFWFFGHPEVYILILPAFGIISHVIST-NYCRSLFGNQSMILAMGCIAVLGSVVWVHHMYT 239
Cdd:MTH00026  216 FNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQILSLfSYKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYV 295

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863 240 TGLEVDTRAFFTSTTILISIPTGTKVFNWLCTYMSTNFGITHSS-SLLSLLFICTFTFGGTTGVILGNGAIDVALHDTYY 318
Cdd:MTH00026  296 VGMDVDTRAYFTAATMIIAVPTGIKIFSWLATVSGSGRNLIFTTpMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYY 375

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863 319 VIAHFHFVLSIGAIIALFTSVSFFQESFFGKTLRE-NTIIVLWsiLFFVGVVLTFLPMHFLGFNVMPRRIPDYPDALNGW 397
Cdd:MTH00026  376 VVAHFHFVLSMGAVFAIFGGFYLWFGKITGYAYKDiYGLIHFW--LMFIGVNITFFPQHFLGLAGLPRRYADYPDNFEDF 453

                         410
                  ....*....|....*...
gi 1931720863 398 NMICSIGSTMTLFGLLIF 415
Cdd:MTH00026  454 NQISSFGSIISIIAVIWF 471
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 2-407 1.24e-91

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: 282.92  E-value: 1.24e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863   2 IFTVHGIIMIFFNIMPGLFGgFGNYFLPILCGSSELAYPRINSISLLLQPIAFILVILSTAaefGGGTGWTLYPPLstsl 81
Cdd:pfam00115  44 LRTLHGNLMIFWFATPFLFG-FGNYLVPLMIGARDMAFPRLNALSFWLVVLGAVLLLASFG---GATTGWTEYPPL---- 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863  82 mslspVAVDVIVIGLLVSGIASIMSSLNFLTTVMHLRAKGLTLgILSVSTWSLIITSVMLLLTLPVLTGGVLMLLSDLHF 161
Cdd:pfam00115 116 -----VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSL 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863 162 NTLffdptfAGDPILYQHLFWFFGHPEVYILILPAFGIISHVISTNYCRSLFGNQSMILAMGCIAVLGSVVWVHHMYTTG 241
Cdd:pfam00115 190 GAG------GGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGRPLFGYKLSVLAFWLIAFLGFLVWAHHLFTTG 263

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863 242 LEVDTRAFFTSTTILISIPTGTKVFNWLCTYMSTNFGITHSSSLLSLLFICTFTFGGTTGVILGNGAIDVALHDTYYVIA 321
Cdd:pfam00115 264 LPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFRTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVA 343

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863 322 HFHFVLSIGAIIALFTSVSFFQESFFGKTLRENTIIVLWsILFFVGVVLTFLPMHFLGFNVMPRRIP----DYPDALNGW 397
Cdd:pfam00115 344 HFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHF-WLLFIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPL 422

                         410
                  ....*....|
gi 1931720863 398 NMICSIGSTM 407
Cdd:pfam00115 423 NWIRTIGGVL 432
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 2-415 9.54e-81

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: 260.94  E-value: 9.54e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863   2 IFTVHGIIMIFFNIMPGLFGgFGNYFLPILCGSSELAYPRINSISLLLQPIAFILVILSTAAEFGGGTGWTLYPPLSTSL 81
Cdd:TIGR02882  95 IFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFNISFVIGGSPDAGWTNYAPLAGPE 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863  82 MSLSPvAVDVIVIGLLVSGIASIMSSLNFLTTVMHLRAKGLTLGILSVSTWSLIITSVMLLLTLPVLTGGVLMLLSDLHF 161
Cdd:TIGR02882 174 FSPGV-GVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTLIIIFAFPVLTVALALMTTDRIF 252

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863 162 NTLFFDPTFAGDPILYQHLFWFFGHPEVYILILPAFGIISHVISTNYCRSLFGNQSMILAMGCIAVLGSVVWVHHMYTTG 241
Cdd:TIGR02882 253 DTAFFTVAHGGMPMLWANLFWIWGHPEVYIVILPAFGIYSEIISTFAQKRLFGYKSMVWSTVGIAFLSFLVWVHHFFTMG 332

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863 242 LEVDTRAFFTSTTILISIPTGTKVFNWLCTYMSTNFGIThSSSLLSLLFICTFTFGGTTGVILGNGAIDVALHDTYYVIA 321
Cdd:TIGR02882 333 NGALINSFFSITTMAIAIPTGVKIFNWLLTLYKGKIRFT-TPMLFSLAFIPNFLIGGVTGVMLAMASADYQYHNTYFLVA 411

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863 322 HFHFVLSIGAIIALFTSVSFFQESFFGKTLRENtiIVLWSILFFV-GVVLTFLPMHFLGFNVMPRRIPDYPDALnGW--- 397
Cdd:TIGR02882 412 HFHYVLITGVVFACLAGLIYWYPKMFGYKLNER--LGKWCFWFFMiGFNVCFFPMYILGLDGMPRRMYTYSPSD-GWfpl 488

                         410
                  ....*....|....*...
gi 1931720863 398 NMICSIGSTMTLFGLLIF 415
Cdd:TIGR02882 489 NLISTIGALLMAIGFIFL 506
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 2-413 1.05e-78

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 256.02  E-value: 1.05e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863   2 IFTVHGIIMIFFNIMPGLFGgFGNYFLPILCGSSELAYPRINSISLLLQPIAFILVILSTAAEFGGGTGWTLYPPLSTsl 81
Cdd:PRK15017  102 IFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLSG-- 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863  82 MSLSP-VAVDVIVIGLLVSGIASIMSSLNFLTTVMHLRAKGLTLGILSVSTWSLIITSVMLLLTLPVLTGGVLMLLSDLH 160
Cdd:PRK15017  179 IEYSPgVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDRY 258

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863 161 FNTLFFDPTFAGDPILYQHLFWFFGHPEVYILILPAFGIISHVISTNYCRSLFGNQSMILAMGCIAVLGSVVWVHHMYTT 240
Cdd:PRK15017  259 LGTHFFTNDMGGNMMMYINLIWAWGHPEVYILILPVFGVFSEIAATFSRKRLFGYTSLVWATVCITVLSFIVWLHHFFTM 338

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863 241 GLEVDTRAFFTSTTILISIPTGTKVFNWLCTyMSTNFGITHSSSLLSLLFICTFTFGGTTGVILGNGAIDVALHDTYYVI 320
Cdd:PRK15017  339 GAGANVNAFFGITTMIIAIPTGVKIFNWLFT-MYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLI 417

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863 321 AHFHFVLSIGAIIALFTSVSFFQESFFGKTLREN---TIIVLWSILFFVgvvlTFLPMHFLGFNVMPRRIPDYPD-ALNG 396
Cdd:PRK15017  418 AHFHNVIIGGVVFGCFAGMTYWWPKAFGFKLNETwgkRAFWFWIIGFFV----AFMPLYALGFMGMTRRLSQQIDpQFHT 493

                         410
                  ....*....|....*..
gi 1931720863 397 WNMICSIGSTMTLFGLL 413
Cdd:PRK15017  494 MLMIAASGAALIALGIL 510
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
 173-415 8.47e-10

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: 60.38  E-value: 8.47e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863 173 DPILYQHLFWFFGHPEVYILILPAFGIISHVISTNYCRSLFGNQSMILAMGCIAVLGSVVWVHHMYTTGLEVDTRAFFTS 252
Cdd:cd01660   200 DVLLSRTLFWWFGHPLVYFWLLPAYIAWYTILPKIAGGKLFSDPLARLAFILFLLFSTPVGFHHQFADPGIGPGWKFIHM 279

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863 253 T-TILISIPTGTKVFNWLCTYMSTN--------FGITHSSSLLSLLF------ICTFTFGGTTGVILGNGAIDVALHDTY 317
Cdd:cd01660   280 VlTFMVALPSLLTAFTVFASLEIAGrlrggkglFGWIRALPWGDPMFlalflaMLMFIPGGAGGIINASYQLNYVVHNTA 359

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1931720863 318 YVIAHFHfvLSIGAIIAL-FTSVSF-FQESFFGKTLRENTIIVLWSILFFVGVVLTFLPMHFLGFNVMPRRI-------P 388
Cdd:cd01660   360 WVPGHFH--LTVGGAVALtFMAVAYwLVPHLTGRELAAKRLALAQPWLWFVGMTIMSTAMHVAGLLGAPRRTaeaqyggL 437

                         250       260
                  ....*....|....*....|....*..
gi 1931720863 389 DYPDALNGWNMICSIGSTMTLFGLLIF 415
Cdd:cd01660   438 PAAGEWAPYQQLMAIGGTILFVSGALF 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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