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Conserved domains on  [gi|195984759|gb|ACG63939|]
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cytochrome c oxidase subunit 1, partial (mitochondrion) [Halidrys siliquosa]

Protein Classification

cytochrome c oxidase subunit 1( domain architecture ID 10108859)

cytochrome c oxidase subunit 1 is the catalytic subunit of cytochrome c oxidase, which is the component of the respiratory chain that catalyzes the reduction of oxygen to water

Graphical summary

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List of domain hits

 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 ...
 1-391 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: 657.63  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759   1 LYLIFGAFAGVLGTSMSVIIRLQLASPGNMFlgGNYQLYNVIVTAHAFLMIFFMVMPVLIGGFGNWFVPLMIGAPDMAFP 80
Cdd:cd01663    9 LYLIFGLWSGLVGTSLSLLIRLELSQPGSQL--GNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFP 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759  81 RMNNISFWLLPPSLILLLASSLVEAGAGTGWTVYPPLSSIQAHSGPSVDLAIFSLHLSGAASILGAINFITTIFNMRAPG 160
Cdd:cd01663   87 RLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPG 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759 161 MGMHRLPLFVWSVLITAFLLLLSLPVLAGGITMLLTDRNFNTTFFDPAG*************FGHPEVYILILPGFGIVS 240
Cdd:cd01663  167 MTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIIS 246

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759 241 HILATFS-RKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDIDTRAYFTAATMIIAVPTGIKIFSWIATMWGGSIRLK 319
Cdd:cd01663  247 HIISTFSgKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFE 326

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 195984759 320 TPMLFSIGFLFLFTIGGLTGVVLANSGVDIALHDTYYVVAHFHYVLSMGAAFTMFGAFYFWVGKMTGLGYPE 391
Cdd:cd01663  327 TPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNE 398
 
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 ...
 1-391 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: 657.63  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759   1 LYLIFGAFAGVLGTSMSVIIRLQLASPGNMFlgGNYQLYNVIVTAHAFLMIFFMVMPVLIGGFGNWFVPLMIGAPDMAFP 80
Cdd:cd01663    9 LYLIFGLWSGLVGTSLSLLIRLELSQPGSQL--GNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFP 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759  81 RMNNISFWLLPPSLILLLASSLVEAGAGTGWTVYPPLSSIQAHSGPSVDLAIFSLHLSGAASILGAINFITTIFNMRAPG 160
Cdd:cd01663   87 RLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPG 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759 161 MGMHRLPLFVWSVLITAFLLLLSLPVLAGGITMLLTDRNFNTTFFDPAG*************FGHPEVYILILPGFGIVS 240
Cdd:cd01663  167 MTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIIS 246

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759 241 HILATFS-RKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDIDTRAYFTAATMIIAVPTGIKIFSWIATMWGGSIRLK 319
Cdd:cd01663  247 HIISTFSgKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFE 326

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 195984759 320 TPMLFSIGFLFLFTIGGLTGVVLANSGVDIALHDTYYVVAHFHYVLSMGAAFTMFGAFYFWVGKMTGLGYPE 391
Cdd:cd01663  327 TPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNE 398
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-387 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 609.56  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759   1 LYLIFGAFAGVLGTSMSVIIRLQLASPGNMFlgGNYQLYNVIVTAHAFLMIFFMVMPVLIGGFGNWFVPLMIGAPDMAFP 80
Cdd:MTH00153  16 LYFIFGAWSGMVGTSLSLLIRAELGQPGSLI--GDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFP 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759  81 RMNNISFWLLPPSLILLLASSLVEAGAGTGWTVYPPLSSIQAHSGPSVDLAIFSLHLSGAASILGAINFITTIFNMRAPG 160
Cdd:MTH00153  94 RMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKG 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759 161 MGMHRLPLFVWSVLITAFLLLLSLPVLAGGITMLLTDRNFNTTFFDPAG*************FGHPEVYILILPGFGIVS 240
Cdd:MTH00153 174 MTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMIS 253

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759 241 HILATFS-RKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDIDTRAYFTAATMIIAVPTGIKIFSWIATMWGGSIRLK 319
Cdd:MTH00153 254 HIISQESgKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYS 333

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 195984759 320 TPMLFSIGFLFLFTIGGLTGVVLANSGVDIALHDTYYVVAHFHYVLSMGAAFTMFGAFYFWVGKMTGL 387
Cdd:MTH00153 334 PSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGL 401
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-391 2.38e-157

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: 452.06  E-value: 2.38e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759    1 LYLIFGAFAGVLGTSMSVIIRLQLASPGNMFLGgnYQLYNVIVTAHAFLMIFFMVMPVLiGGFGNWFVPLMIGAPDMAFP 80
Cdd:TIGR02891  12 LYLVTAFAFFLVGGVLALLMRAQLATPGNTFMD--AETYNQLFTMHGTIMIFLFAIPIL-AGFGNYLLPLMIGARDMAFP 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759   81 RMNNISFWLLPPSLILLLASSLVEAGAGTGWTVYPPLSSIQAHSGPSVDLAIFSLHLSGAASILGAINFITTIFNMRAPG 160
Cdd:TIGR02891  89 RLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPG 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759  161 MGMHRLPLFVWSVLITAFLLLLSLPVLAGGITMLLTDRNFNTTFFDPAG*************FGHPEVYILILPGFGIVS 240
Cdd:TIGR02891 169 MTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIIS 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759  241 HILATFSRKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDIDTRAYFTAATMIIAVPTGIKIFSWIATMWGGSIRLKT 320
Cdd:TIGR02891 249 EILPTFARKPIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTT 328

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 195984759  321 PMLFSIGFLFLFTIGGLTGVVLANSGVDIALHDTYYVVAHFHYVLSMGAAFTMFGAFYFWVGKMTGLGYPE 391
Cdd:TIGR02891 329 PMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNE 399
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-391 5.20e-157

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 452.66  E-value: 5.20e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759   1 LYLIFGAFAGVLGTSMSVIIRLQLASPGNMFLGGnyQLYNVIVTAHAFLMIFFMVMPvLIGGFGNWFVPLMIGAPDMAFP 80
Cdd:COG0843   21 MYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSP--ETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFP 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759  81 RMNNISFWLLPPSLILLLASSLVEAGAGTGWTVYPPLSSIQAHSGPSVDLAIFSLHLSGAASILGAINFITTIFNMRAPG 160
Cdd:COG0843   98 RLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPG 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759 161 MGMHRLPLFVWSVLITAFLLLLSLPVLAGGITMLLTDRNFNTTFFDPAG*************FGHPEVYILILPGFGIVS 240
Cdd:COG0843  178 MTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVS 257

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759 241 HILATFSRKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDIDTRAYFTAATMIIAVPTGIKIFSWIATMWGGSIRLKT 320
Cdd:COG0843  258 EIIPTFSRKPLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTT 337

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 195984759 321 PMLFSIGFLFLFTIGGLTGVVLANSGVDIALHDTYYVVAHFHYVLSMGAAFTMFGAFYFWVGKMTGLGYPE 391
Cdd:COG0843  338 PMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNE 408
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-391 1.23e-105

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: 317.98  E-value: 1.23e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759    1 LYLIFGAFAGVLGTSMSVIIRLQLASPGNMFLGgnYQLYNVIVTAHAFLMIFFMVMPVlIGGFGNWFVPLMIGAPDMAFP 80
Cdd:pfam00115   5 LYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLS--PLTYNQLRTLHGNLMIFWFATPF-LFGFGNYLVPLMIGARDMAFP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759   81 RMNNISFWLLPPSLILLLASSlveAGAGTGWTVYPPLssiqahsgPSVDLAIFSLHLSGAASILGAINFITTIFNMRAPG 160
Cdd:pfam00115  82 RLNALSFWLVVLGAVLLLASF---GGATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPG 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759  161 MGMhRLPLFVWSVLITAFLLLLSLPVLAGGITMLLTDRNFNTTFFDPAg*************FGHPEVYILILPGFGIVS 240
Cdd:pfam00115 151 MTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLGAGGGDPL------LDQHLFWWFGHPEVYILILPAFGIIY 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759  241 HILATFSRKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDIDTRAYFTAATMIIAVPTGIKIFSWIATMWGGSIRL-K 319
Cdd:pfam00115 224 YILPKFAGRPLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFrT 303

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 195984759  320 TPMLFSIGFLFLFTIGGLTGVVLANSGVDIALHDTYYVVAHFHYVLSMGAAFTMFGAFYFWVGKMTGLGYPE 391
Cdd:pfam00115 304 TPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSE 375
 
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 ...
 1-391 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: 657.63  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759   1 LYLIFGAFAGVLGTSMSVIIRLQLASPGNMFlgGNYQLYNVIVTAHAFLMIFFMVMPVLIGGFGNWFVPLMIGAPDMAFP 80
Cdd:cd01663    9 LYLIFGLWSGLVGTSLSLLIRLELSQPGSQL--GNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFP 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759  81 RMNNISFWLLPPSLILLLASSLVEAGAGTGWTVYPPLSSIQAHSGPSVDLAIFSLHLSGAASILGAINFITTIFNMRAPG 160
Cdd:cd01663   87 RLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPG 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759 161 MGMHRLPLFVWSVLITAFLLLLSLPVLAGGITMLLTDRNFNTTFFDPAG*************FGHPEVYILILPGFGIVS 240
Cdd:cd01663  167 MTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIIS 246

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759 241 HILATFS-RKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDIDTRAYFTAATMIIAVPTGIKIFSWIATMWGGSIRLK 319
Cdd:cd01663  247 HIISTFSgKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFE 326

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 195984759 320 TPMLFSIGFLFLFTIGGLTGVVLANSGVDIALHDTYYVVAHFHYVLSMGAAFTMFGAFYFWVGKMTGLGYPE 391
Cdd:cd01663  327 TPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNE 398
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-387 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 609.56  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759   1 LYLIFGAFAGVLGTSMSVIIRLQLASPGNMFlgGNYQLYNVIVTAHAFLMIFFMVMPVLIGGFGNWFVPLMIGAPDMAFP 80
Cdd:MTH00153  16 LYFIFGAWSGMVGTSLSLLIRAELGQPGSLI--GDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFP 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759  81 RMNNISFWLLPPSLILLLASSLVEAGAGTGWTVYPPLSSIQAHSGPSVDLAIFSLHLSGAASILGAINFITTIFNMRAPG 160
Cdd:MTH00153  94 RMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKG 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759 161 MGMHRLPLFVWSVLITAFLLLLSLPVLAGGITMLLTDRNFNTTFFDPAG*************FGHPEVYILILPGFGIVS 240
Cdd:MTH00153 174 MTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMIS 253

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759 241 HILATFS-RKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDIDTRAYFTAATMIIAVPTGIKIFSWIATMWGGSIRLK 319
Cdd:MTH00153 254 HIISQESgKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYS 333

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 195984759 320 TPMLFSIGFLFLFTIGGLTGVVLANSGVDIALHDTYYVVAHFHYVLSMGAAFTMFGAFYFWVGKMTGL 387
Cdd:MTH00153 334 PSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGL 401
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-388 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 569.23  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759   1 LYLIFGAFAGVLGTSMSVIIRLQLASPGnMFLGGNyQLYNVIVTAHAFLMIFFMVMPVLIGGFGNWFVPLMIGAPDMAFP 80
Cdd:MTH00223  15 LYLIFGMWSGLVGTSLSLLIRAELGQPG-ALLGDD-QLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFP 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759  81 RMNNISFWLLPPSLILLLASSLVEAGAGTGWTVYPPLSSIQAHSGPSVDLAIFSLHLSGAASILGAINFITTIFNMRAPG 160
Cdd:MTH00223  93 RLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPG 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759 161 MGMHRLPLFVWSVLITAFLLLLSLPVLAGGITMLLTDRNFNTTFFDPAG*************FGHPEVYILILPGFGIVS 240
Cdd:MTH00223 173 MQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMIS 252

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759 241 HILATFSRK-PVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDIDTRAYFTAATMIIAVPTGIKIFSWIATMWGGSIRLK 319
Cdd:MTH00223 253 HIVSHYSSKkEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGSKIKYE 332

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 195984759 320 TPMLFSIGFLFLFTIGGLTGVVLANSGVDIALHDTYYVVAHFHYVLSMGAAFTMFGAFYFWVGKMTGLG 388
Cdd:MTH00223 333 APMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLFTGVT 401
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-391 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 561.22  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759   1 LYLIFGAFAGVLGTSMSVIIRLQLASPGNMFlgGNYQLYNVIVTAHAFLMIFFMVMPVLIGGFGNWFVPLMIGAPDMAFP 80
Cdd:MTH00167  18 LYFIFGAWAGMVGTALSLLIRAELSQPGSLL--GDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFP 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759  81 RMNNISFWLLPPSLILLLASSLVEAGAGTGWTVYPPLSSIQAHSGPSVDLAIFSLHLSGAASILGAINFITTIFNMRAPG 160
Cdd:MTH00167  96 RMNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPG 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759 161 MGMHRLPLFVWSVLITAFLLLLSLPVLAGGITMLLTDRNFNTTFFDPAG*************FGHPEVYILILPGFGIVS 240
Cdd:MTH00167 176 ITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMIS 255

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759 241 HILATFS-RKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDIDTRAYFTAATMIIAVPTGIKIFSWIATMWGGSIRLK 319
Cdd:MTH00167 256 HIVVYYSgKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLHGGKIKWE 335

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 195984759 320 TPMLFSIGFLFLFTIGGLTGVVLANSGVDIALHDTYYVVAHFHYVLSMGAAFTMFGAFYFWVGKMTGLGYPE 391
Cdd:MTH00167 336 TPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGLTLNE 407
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-386 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 550.85  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759   1 LYLIFGAFAGVLGTSMSVIIRLQLASPGNMFlgGNYQLYNVIVTAHAFLMIFFMVMPVLIGGFGNWFVPLMIGAPDMAFP 80
Cdd:MTH00116  18 LYLIFGAWAGMVGTALSLLIRAELGQPGTLL--GDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFP 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759  81 RMNNISFWLLPPSLILLLASSLVEAGAGTGWTVYPPLSSIQAHSGPSVDLAIFSLHLSGAASILGAINFITTIFNMRAPG 160
Cdd:MTH00116  96 RMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPA 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759 161 MGMHRLPLFVWSVLITAFLLLLSLPVLAGGITMLLTDRNFNTTFFDPAG*************FGHPEVYILILPGFGIVS 240
Cdd:MTH00116 176 MSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIIS 255

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759 241 HILATFS-RKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDIDTRAYFTAATMIIAVPTGIKIFSWIATMWGGSIRLK 319
Cdd:MTH00116 256 HIVTYYAgKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSWLATLHGGTIKWD 335

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 195984759 320 TPMLFSIGFLFLFTIGGLTGVVLANSGVDIALHDTYYVVAHFHYVLSMGAAFTMFGAFYFWVGKMTG 386
Cdd:MTH00116 336 PPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTG 402
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-388 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 538.54  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759   1 LYLIFGAFAGVLGTSMSVIIRLQLASPGNMFlgGNYQLYNVIVTAHAFLMIFFMVMPVLIGGFGNWFVPLMIGAPDMAFP 80
Cdd:MTH00142  16 LYFLFGAWAGMVGTGLSLLIRAELGQPGSLL--GDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFP 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759  81 RMNNISFWLLPPSLILLLASSLVEAGAGTGWTVYPPLSSIQAHSGPSVDLAIFSLHLSGAASILGAINFITTIFNMRAPG 160
Cdd:MTH00142  94 RMNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGG 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759 161 MGMHRLPLFVWSVLITAFLLLLSLPVLAGGITMLLTDRNFNTTFFDPAG*************FGHPEVYILILPGFGIVS 240
Cdd:MTH00142 174 MKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMIS 253

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759 241 HILATFS-RKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDIDTRAYFTAATMIIAVPTGIKIFSWIATMWGGSIRLK 319
Cdd:MTH00142 254 HIINHYSgKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFSWLATLHGSKVKYE 333

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 195984759 320 TPMLFSIGFLFLFTIGGLTGVVLANSGVDIALHDTYYVVAHFHYVLSMGAAFTMFGAFYFWVGKMTGLG 388
Cdd:MTH00142 334 PPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLFTGLT 402
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-391 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 536.71  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759   1 LYLIFGAFAGVLGTSMSVIIRLQLASPGNMFlgGNYQLYNVIVTAHAFLMIFFMVMPVLIGGFGNWFVPLMIGAPDMAFP 80
Cdd:MTH00182  20 LYLVFGAGAGMIGTAFSMLIRLELSAPGAML--GDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFP 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759  81 RMNNISFWLLPPSLILLLASSLVEAGAGTGWTVYPPLSSIQAHSGPSVDLAIFSLHLSGAASILGAINFITTIFNMRAPG 160
Cdd:MTH00182  98 RLNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPG 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759 161 MGMHRLPLFVWSVLITAFLLLLSLPVLAGGITMLLTDRNFNTTFFDPAG*************FGHPEVYILILPGFGIVS 240
Cdd:MTH00182 178 VTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMIS 257

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759 241 HILATFS-RKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDIDTRAYFTAATMIIAVPTGIKIFSWIATMWGGSIRLK 319
Cdd:MTH00182 258 QIIPTFVaKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGGTLRLD 337

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 195984759 320 TPMLFSIGFLFLFTIGGLTGVVLANSGVDIALHDTYYVVAHFHYVLSMGAAFTMFGAFYFWVGKMTGLGYPE 391
Cdd:MTH00182 338 TPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNE 409
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-391 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 529.78  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759   1 LYLIFGAFAGVLGTSMSVIIRLQLASPGNMFlgGNYQLYNVIVTAHAFLMIFFMVMPVLIGGFGNWFVPLMIGAPDMAFP 80
Cdd:MTH00184  20 LYLLFGAFAGMIGTAFSMLIRLELSAPGSML--GDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFP 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759  81 RMNNISFWLLPPSLILLLASSLVEAGAGTGWTVYPPLSSIQAHSGPSVDLAIFSLHLSGAASILGAINFITTIFNMRAPG 160
Cdd:MTH00184  98 RLNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPG 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759 161 MGMHRLPLFVWSVLITAFLLLLSLPVLAGGITMLLTDRNFNTTFFDPAG*************FGHPEVYILILPGFGIVS 240
Cdd:MTH00184 178 ITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIIS 257

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759 241 HILATFS-RKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDIDTRAYFTAATMIIAVPTGIKIFSWIATMWGGSIRLK 319
Cdd:MTH00184 258 QIIPTFAaKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATIFGGSLRLD 337

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 195984759 320 TPMLFSIGFLFLFTIGGLTGVVLANSGVDIALHDTYYVVAHFHYVLSMGAAFTMFGAFYFWVGKMTGLGYPE 391
Cdd:MTH00184 338 TPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNE 409
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-389 3.02e-175

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 498.59  E-value: 3.02e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759   1 LYLIFGAFAGVLGTSMSVIIRLQLASPGNMFlgGNYQLYNVIVTAHAFLMIFFMVMPVLIGGFGNWFVPLMIGAPDMAFP 80
Cdd:MTH00037  18 LYLIFGAWAGMVGTAMSVIIRTELAQPGSLL--QDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFP 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759  81 RMNNISFWLLPPSLILLLASSLVEAGAGTGWTVYPPLSSIQAHSGPSVDLAIFSLHLSGAASILGAINFITTIFNMRAPG 160
Cdd:MTH00037  96 RMNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPG 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759 161 MGMHRLPLFVWSVLITAFLLLLSLPVLAGGITMLLTDRNFNTTFFDPAG*************FGHPEVYILILPGFGIVS 240
Cdd:MTH00037 176 MTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMIS 255

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759 241 HILATFS-RKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDIDTRAYFTAATMIIAVPTGIKIFSWIATMWGGSIRLK 319
Cdd:MTH00037 256 HVIAHYSgKQEPFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWMATLQGSNLRWE 335

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759 320 TPMLFSIGFLFLFTIGGLTGVVLANSGVDIALHDTYYVVAHFHYVLSMGAAFTMFGAFYFWVGKMTGLGY 389
Cdd:MTH00037 336 TPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLFSGVSL 405
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-386 4.41e-174

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 495.23  E-value: 4.41e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759   1 LYLIFGAFAGVLGTSMSVIIRLQLASPGNMFlgGNYQLYNVIVTAHAFLMIFFMVMPVLIGGFGNWFVPLMIGAPDMAFP 80
Cdd:MTH00077  18 LYLVFGAWAGMVGTALSLLIRAELSQPGTLL--GDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFP 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759  81 RMNNISFWLLPPSLILLLASSLVEAGAGTGWTVYPPLSSIQAHSGPSVDLAIFSLHLSGAASILGAINFITTIFNMRAPG 160
Cdd:MTH00077  96 RMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPS 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759 161 MGMHRLPLFVWSVLITAFLLLLSLPVLAGGITMLLTDRNFNTTFFDPAG*************FGHPEVYILILPGFGIVS 240
Cdd:MTH00077 176 MSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMIS 255

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759 241 HILATFS-RKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDIDTRAYFTAATMIIAVPTGIKIFSWIATMWGGSIRLK 319
Cdd:MTH00077 256 HIVTYYSaKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGAIKWD 335

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 195984759 320 TPMLFSIGFLFLFTIGGLTGVVLANSGVDIALHDTYYVVAHFHYVLSMGAAFTMFGAFYFWVGKMTG 386
Cdd:MTH00077 336 AAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSG 402
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-386 6.06e-173

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 492.52  E-value: 6.06e-173
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759   1 LYLIFGAFAGVLGTSMSVIIRLQLASPGNMFlgGNYQLYNVIVTAHAFLMIFFMVMPVLIGGFGNWFVPLMIGAPDMAFP 80
Cdd:MTH00183  18 LYLVFGAWAGMVGTALSLLIRAELSQPGALL--GDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFP 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759  81 RMNNISFWLLPPSLILLLASSLVEAGAGTGWTVYPPLSSIQAHSGPSVDLAIFSLHLSGAASILGAINFITTIFNMRAPG 160
Cdd:MTH00183  96 RMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPA 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759 161 MGMHRLPLFVWSVLITAFLLLLSLPVLAGGITMLLTDRNFNTTFFDPAG*************FGHPEVYILILPGFGIVS 240
Cdd:MTH00183 176 ISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMIS 255

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759 241 HILATFS-RKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDIDTRAYFTAATMIIAVPTGIKIFSWIATMWGGSIRLK 319
Cdd:MTH00183 256 HIVAYYSgKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGSIKWE 335

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 195984759 320 TPMLFSIGFLFLFTIGGLTGVVLANSGVDIALHDTYYVVAHFHYVLSMGAAFTMFGAFYFWVGKMTG 386
Cdd:MTH00183 336 TPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLFSG 402
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-387 1.22e-171

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 489.03  E-value: 1.22e-171
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759   1 LYLIFGAFAGVLGTSMSVIIRLQLASPGNmFLGGNyQLYNVIVTAHAFLMIFFMVMPVLIGGFGNWFVPLMIGAPDMAFP 80
Cdd:MTH00007  15 LYFILGVWGGLLGTSMSLLIRIELGQPGA-FLGSD-QLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFP 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759  81 RMNNISFWLLPPSLILLLASSLVEAGAGTGWTVYPPLSSIQAHSGPSVDLAIFSLHLSGAASILGAINFITTIFNMRAPG 160
Cdd:MTH00007  93 RLNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKG 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759 161 MGMHRLPLFVWSVLITAFLLLLSLPVLAGGITMLLTDRNFNTTFFDPAG*************FGHPEVYILILPGFGIVS 240
Cdd:MTH00007 173 LRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGAIS 252

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759 241 HILATFSRKP-VFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDIDTRAYFTAATMIIAVPTGIKIFSWIATMWGGSIRLK 319
Cdd:MTH00007 253 HIVTHYAGKLePFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGSPIKYE 332

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 195984759 320 TPMLFSIGFLFLFTIGGLTGVVLANSGVDIALHDTYYVVAHFHYVLSMGAAFTMFGAFYFWVGKMTGL 387
Cdd:MTH00007 333 TPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTGL 400
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-386 1.32e-171

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 489.01  E-value: 1.32e-171
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759   1 LYLIFGAFAGVLGTSMSVIIRLQLASPGNMFlgGNYQLYNVIVTAHAFLMIFFMVMPVLIGGFGNWFVPLMIGAPDMAFP 80
Cdd:MTH00103  18 LYLLFGAWAGMVGTALSLLIRAELGQPGTLL--GDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFP 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759  81 RMNNISFWLLPPSLILLLASSLVEAGAGTGWTVYPPLSSIQAHSGPSVDLAIFSLHLSGAASILGAINFITTIFNMRAPG 160
Cdd:MTH00103  96 RMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPA 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759 161 MGMHRLPLFVWSVLITAFLLLLSLPVLAGGITMLLTDRNFNTTFFDPAG*************FGHPEVYILILPGFGIVS 240
Cdd:MTH00103 176 MSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMIS 255

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759 241 HILATFS-RKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDIDTRAYFTAATMIIAVPTGIKIFSWIATMWGGSIRLK 319
Cdd:MTH00103 256 HIVTYYSgKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGNIKWS 335

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 195984759 320 TPMLFSIGFLFLFTIGGLTGVVLANSGVDIALHDTYYVVAHFHYVLSMGAAFTMFGAFYFWVGKMTG 386
Cdd:MTH00103 336 PAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSG 402
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-389 3.31e-163

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 467.62  E-value: 3.31e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759   1 LYLIFGAFAGVLGTSMSVIIRLQLASPGnmFLGGNYQLYNVIVTAHAFLMIFFMVMPVLIGGFGNWFVPLMIGAPDMAFP 80
Cdd:MTH00079  19 LYFLFGLWSGMVGTSLSLIIRLELSKPG--LLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFP 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759  81 RMNNISFWLLPPSLILLLASSLVEAGAGTGWTVYPPLSSiQAHSGPSVDLAIFSLHLSGAASILGAINFITTIFNMRAPG 160
Cdd:MTH00079  97 RLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLST-LGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSS 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759 161 MGMHRLPLFVWSVLITAFLLLLSLPVLAGGITMLLTDRNFNTTFFDPAG*************FGHPEVYILILPGFGIVS 240
Cdd:MTH00079 176 ISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPEVYILILPAFGIIS 255

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759 241 HILATFS-RKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDIDTRAYFTAATMIIAVPTGIKIFSWIATMWGGSIRLK 319
Cdd:MTH00079 256 QSTLYLTgKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMKFQ 335

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759 320 TPMLFSIGFLFLFTIGGLTGVVLANSGVDIALHDTYYVVAHFHYVLSMGAAFTMFGAFYFWVGKMTGLGY 389
Cdd:MTH00079 336 PLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFMTGIVY 405
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-391 1.25e-161

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 464.49  E-value: 1.25e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759   1 LYLIFGAFAGVLGTSMSVIIRLQLASPGNMFlgGNYQLYNVIVTAHAFLMIFFMVMPVLIGGFGNWFVPLMIGAPDMAFP 80
Cdd:MTH00026  19 LYLVFGALSGAIGTAFSMLIRLELSSPGSML--GDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFP 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759  81 RMNNISFWLLPPSLILLLASSLVEAGAGTGWTVYPPLSSIQAHSGPSVDLAIFSLHLSGAASILGAINFITTIFNMRAPG 160
Cdd:MTH00026  97 RLNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPG 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759 161 MGMHRLPLFVWSVLITAFLLLLSLPVLAGGITMLLTDRNFNTTFFDPAG*************FGHPEVYILILPGFGIVS 240
Cdd:MTH00026 177 MTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIIS 256

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759 241 HILATFS-RKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDIDTRAYFTAATMIIAVPTGIKIFSWIATMWGGSIRL- 318
Cdd:MTH00026 257 QILSLFSyKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSWLATVSGSGRNLi 336

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 195984759 319 -KTPMLFSIGFLFLFTIGGLTGVVLANSGVDIALHDTYYVVAHFHYVLSMGAAFTMFGAFYFWVGKMTGLGYPE 391
Cdd:MTH00026 337 fTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWFGKITGYAYKD 410
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-391 1.18e-158

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: 454.30  E-value: 1.18e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759   1 LYLIFGAFAGVLGTSMSVIIRLQLASPGNMFLggNYQLYNVIVTAHAFLMIFFMVMPVLIGGFGNWFVPlMIGAPDMAFP 80
Cdd:cd00919    7 LYLIFAFVALLLGGLLALLIRLELATPGSLFL--DPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARDLAFP 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759  81 RMNNISFWLLPPSLILLLASSLVEAGAGTGWTVYPPLSSIQAHSGPSVDLAIFSLHLSGAASILGAINFITTIFNMRAPG 160
Cdd:cd00919   84 RLNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPG 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759 161 MGMHRLPLFVWSVLITAFLLLLSLPVLAGGITMLLTDRNFNTTFFDPAG*************FGHPEVYILILPGFGIVS 240
Cdd:cd00919  164 MTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAFGAIS 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759 241 HILATFSRKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDIDTRAYFTAATMIIAVPTGIKIFSWIATMWGGSIRLKT 320
Cdd:cd00919  244 EIIPTFSGKPLFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGRIRFDP 323

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 195984759 321 PMLFSIGFLFLFTIGGLTGVVLANSGVDIALHDTYYVVAHFHYVLSMGAAFTMFGAFYFWVGKMTGLGYPE 391
Cdd:cd00919  324 PMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSE 394
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-391 2.38e-157

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: 452.06  E-value: 2.38e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759    1 LYLIFGAFAGVLGTSMSVIIRLQLASPGNMFLGgnYQLYNVIVTAHAFLMIFFMVMPVLiGGFGNWFVPLMIGAPDMAFP 80
Cdd:TIGR02891  12 LYLVTAFAFFLVGGVLALLMRAQLATPGNTFMD--AETYNQLFTMHGTIMIFLFAIPIL-AGFGNYLLPLMIGARDMAFP 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759   81 RMNNISFWLLPPSLILLLASSLVEAGAGTGWTVYPPLSSIQAHSGPSVDLAIFSLHLSGAASILGAINFITTIFNMRAPG 160
Cdd:TIGR02891  89 RLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPG 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759  161 MGMHRLPLFVWSVLITAFLLLLSLPVLAGGITMLLTDRNFNTTFFDPAG*************FGHPEVYILILPGFGIVS 240
Cdd:TIGR02891 169 MTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIIS 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759  241 HILATFSRKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDIDTRAYFTAATMIIAVPTGIKIFSWIATMWGGSIRLKT 320
Cdd:TIGR02891 249 EILPTFARKPIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTT 328

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 195984759  321 PMLFSIGFLFLFTIGGLTGVVLANSGVDIALHDTYYVVAHFHYVLSMGAAFTMFGAFYFWVGKMTGLGYPE 391
Cdd:TIGR02891 329 PMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNE 399
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-391 5.20e-157

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 452.66  E-value: 5.20e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759   1 LYLIFGAFAGVLGTSMSVIIRLQLASPGNMFLGGnyQLYNVIVTAHAFLMIFFMVMPvLIGGFGNWFVPLMIGAPDMAFP 80
Cdd:COG0843   21 MYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSP--ETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFP 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759  81 RMNNISFWLLPPSLILLLASSLVEAGAGTGWTVYPPLSSIQAHSGPSVDLAIFSLHLSGAASILGAINFITTIFNMRAPG 160
Cdd:COG0843   98 RLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPG 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759 161 MGMHRLPLFVWSVLITAFLLLLSLPVLAGGITMLLTDRNFNTTFFDPAG*************FGHPEVYILILPGFGIVS 240
Cdd:COG0843  178 MTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVS 257

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759 241 HILATFSRKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDIDTRAYFTAATMIIAVPTGIKIFSWIATMWGGSIRLKT 320
Cdd:COG0843  258 EIIPTFSRKPLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTT 337

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 195984759 321 PMLFSIGFLFLFTIGGLTGVVLANSGVDIALHDTYYVVAHFHYVLSMGAAFTMFGAFYFWVGKMTGLGYPE 391
Cdd:COG0843  338 PMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNE 408
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 1-386 2.28e-139

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: 406.58  E-value: 2.28e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759   1 LYLIFGAFAGVLGTSMSVIIRLQLASPGNMFLGGnyQLYNVIVTAHAFLMIFFMVMPVLIGgFGNWFVPLMIGAPDMAFP 80
Cdd:cd01662   13 MYIITAFVFFLRGGVDALLMRTQLALPGNDFLSP--EHYNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFP 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759  81 RMNNISFWLLPPSLILLLASSLVEAGAGTGWTVYPPLSSIQAHSGPSVDLAIFSLHLSGAASILGAINFITTIFNMRAPG 160
Cdd:cd01662   90 RLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPG 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759 161 MGMHRLPLFVWSVLITAFLLLLSLPVLAGGITMLLTDRNFNTTFFDPAG*************FGHPEVYILILPGFGIVS 240
Cdd:cd01662  170 MTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYILILPAFGIFS 249

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759 241 HILATFSRKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDIDTRAYFTAATMIIAVPTGIKIFSWIATMWGGSIRLKT 320
Cdd:cd01662  250 EIVPTFSRKPLFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLFTMWRGRIRFET 329

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 195984759 321 PMLFSIGFLFLFTIGGLTGVVLANSGVDIALHDTYYVVAHFHYVLSMGAAFTMFGAFYFWVGKMTG 386
Cdd:cd01662  330 PMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFG 395
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 1-387 1.83e-114

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 343.20  E-value: 1.83e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759   1 LYLIFGAFAGVLGTSMSVIIRLQLASPGNMFLggNYQLYNVIVTAHAFLMIFFMVMPVLIGGFGNWFVPLMIGAPDMAFP 80
Cdd:MTH00048  19 IYTLLGVWSGFVGLSLSLLIRLNFLDPYYNVI--SLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLP 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759  81 RMNNISFWLLPPSLILLLASSLVeaGAGTGWTVYPPLSSIQAHSGPSVDLAIFSLHLSGAASILGAINFITTIFNMRAPG 160
Cdd:MTH00048  97 RLNALSAWLLVPSIVFLLLSMCL--GAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTN 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759 161 MgMHRLPLFVWSVLITAFLLLLSLPVLAGGITMLLTDRNFNTTFFDPAG*************FGHPEVYILILPGFGIVS 240
Cdd:MTH00048 175 V-FSRTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPEVYVLILPGFGIIS 253

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759 241 HILATFSRKP-VFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDIDTRAYFTAATMIIAVPTGIKIFSWIATMWGGSIRLK 319
Cdd:MTH00048 254 HICLSLSNNDdPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFSWLYMLLNSRVRKS 333

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 195984759 320 TPML-FSIGFLFLFTIGGLTGVVLANSGVDIALHDTYYVVAHFHYVLSMGAAFTMFGAFYFWVGKMTGL 387
Cdd:MTH00048 334 DPVVwWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWPLITGL 402
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-391 1.23e-105

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: 317.98  E-value: 1.23e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759    1 LYLIFGAFAGVLGTSMSVIIRLQLASPGNMFLGgnYQLYNVIVTAHAFLMIFFMVMPVlIGGFGNWFVPLMIGAPDMAFP 80
Cdd:pfam00115   5 LYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLS--PLTYNQLRTLHGNLMIFWFATPF-LFGFGNYLVPLMIGARDMAFP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759   81 RMNNISFWLLPPSLILLLASSlveAGAGTGWTVYPPLssiqahsgPSVDLAIFSLHLSGAASILGAINFITTIFNMRAPG 160
Cdd:pfam00115  82 RLNALSFWLVVLGAVLLLASF---GGATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPG 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759  161 MGMhRLPLFVWSVLITAFLLLLSLPVLAGGITMLLTDRNFNTTFFDPAg*************FGHPEVYILILPGFGIVS 240
Cdd:pfam00115 151 MTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLGAGGGDPL------LDQHLFWWFGHPEVYILILPAFGIIY 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759  241 HILATFSRKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDIDTRAYFTAATMIIAVPTGIKIFSWIATMWGGSIRL-K 319
Cdd:pfam00115 224 YILPKFAGRPLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFrT 303

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 195984759  320 TPMLFSIGFLFLFTIGGLTGVVLANSGVDIALHDTYYVVAHFHYVLSMGAAFTMFGAFYFWVGKMTGLGYPE 391
Cdd:pfam00115 304 TPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSE 375
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 1-386 7.08e-93

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: 291.76  E-value: 7.08e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759    1 LYLIFGAFAGVLGTSMSVIIRLQLASPGNMFLGGNYqlYNVIVTAHAFLMIFFMVMPVLIGgFGNWFVPLMIGAPDMAFP 80
Cdd:TIGR02882  56 MYIICAVLMLFRGGIDALLMRAQLTVPDNKFLDAQH--YNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFP 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759   81 RMNNISFWLLPPSLILLLASSLVEAGAGTGWTVYPPLSSIQAHSGPSVDLAIFSLHLSGAASILGAINFITTIFNMRAPG 160
Cdd:TIGR02882 133 VLNALSFWLFFAGAMLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPG 212

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759  161 MGMHRLPLFVWSVLITAFLLLLSLPVLAGGITMLLTDRNFNTTFFDPAG*************FGHPEVYILILPGFGIVS 240
Cdd:TIGR02882 213 MKLMQMPMFTWTTLITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLFWIWGHPEVYIVILPAFGIYS 292

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759  241 HILATFSRKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDIDTRAYFTAATMIIAVPTGIKIFSWIATMWGGSIRLKT 320
Cdd:TIGR02882 293 EIISTFAQKRLFGYKSMVWSTVGIAFLSFLVWVHHFFTMGNGALINSFFSITTMAIAIPTGVKIFNWLLTLYKGKIRFTT 372

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 195984759  321 PMLFSIGFLFLFTIGGLTGVVLANSGVDIALHDTYYVVAHFHYVLSMGAAFTMFGAFYFWVGKMTG 386
Cdd:TIGR02882 373 PMLFSLAFIPNFLIGGVTGVMLAMASADYQYHNTYFLVAHFHYVLITGVVFACLAGLIYWYPKMFG 438
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 1-391 1.23e-88

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 281.05  E-value: 1.23e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759   1 LYLIFGAFAGVLGTSMSVIIRLQ--LASPGNM-FLGGNYqlYNVIVTAHAFLMIFFMVMPVLIGgFGNWFVPLMIGAPDM 77
Cdd:PRK15017  60 MYIIVAIVMLLRGFADAIMMRSQqaLASAGEAgFLPPHH--YDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDV 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759  78 AFPRMNNISFWLLPPSLILLLASSLVEAGAGTGWTVYPPLSSIQAHSGPSVDLAIFSLHLSGAASILGAINFITTIFNMR 157
Cdd:PRK15017 137 AFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMR 216

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759 158 APGMGMHRLPLFVWSVLITAFLLLLSLPVLAGGITMLLTDRNFNTTFFDPAG*************FGHPEVYILILPGFG 237
Cdd:PRK15017 217 APGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWGHPEVYILILPVFG 296

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759 238 IVSHILATFSRKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDIDTRAYFTAATMIIAVPTGIKIFSWIATMWGGSIR 317
Cdd:PRK15017 297 VFSEIAATFSRKRLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVKIFNWLFTMYQGRIV 376

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 195984759 318 LKTPMLFSIGFLFLFTIGGLTGVVLANSGVDIALHDTYYVVAHFHYVLSMGAAFTMFGAFYFWVGKMTGLGYPE 391
Cdd:PRK15017 377 FHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYWWPKAFGFKLNE 450
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
 223-386 1.46e-06

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: 49.98  E-value: 1.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759 223 FGHPEVYILILPGFGIVSHILATFSRKPVFGYLGMVYAMLSIGILGFIVWAHHMFT-VGLDIDTRAYFTAATMIIAVPTG 301
Cdd:cd01660  211 FGHPLVYFWLLPAYIAWYTILPKIAGGKLFSDPLARLAFILFLLFSTPVGFHHQFAdPGIGPGWKFIHMVLTFMVALPSL 290

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 195984759 302 IKIFSWIATM--------------WGGSIRLKTPMLFSIGF-LFLFTIGGLTGVVLANSGVDIALHDTYYVVAHFHYVLS 366
Cdd:cd01660  291 LTAFTVFASLeiagrlrggkglfgWIRALPWGDPMFLALFLaMLMFIPGGAGGIINASYQLNYVVHNTAWVPGHFHLTVG 370

                        170       180
                 ....*....|....*....|
gi 195984759 367 MGAAFTMFGAFYFWVGKMTG 386
Cdd:cd01660  371 GAVALTFMAVAYWLVPHLTG 390
 
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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