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Conserved domains on  [gi|674659114|gb|AIL27082|]
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cytochrome oxidase subunit I, partial (mitochondrion) [Neurotoma nemoralis]

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 ...
 1-359 0e+00

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


The actual alignment was detected with superfamily member MTH00153:

Pssm-ID: 469701  Cd Length: 511  Bit Score: 663.49  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114   1 TLYFIFGMWSGMLGTSMSMLIRLELGTPGSLIGDDQIYNVIVTAHAFLMIFFMVMPMMIGGFGNWLVPL*LGAPDMAFPR 80
Cdd:MTH00153  15 TLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPR 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114  81 MNNMSFWLLPPSLILLLTSSIMNKGAGTGWTVYPPLSSNLSHSGSSVDFAIFSLHMAGISSIMGAINFISTIMNMKIYGL 160
Cdd:MTH00153  95 MNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGM 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114 161 SLDQLSLFTWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISH 240
Cdd:MTH00153 175 TLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISH 254

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114 241 MIFHESGKKETFGTLGMIYAMISIGILGFVVWAHHMFTIGMDVDTRAYFTSATMIIAVPTGIKVFSWMATMHGMKFKINP 320
Cdd:MTH00153 255 IISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSP 334

                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 674659114 321 TILWASGFVFLFTIGGLTGVVLSNSSVDIILHDTYYVVA 359
Cdd:MTH00153 335 SLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVA 373
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-359 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 663.49  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114   1 TLYFIFGMWSGMLGTSMSMLIRLELGTPGSLIGDDQIYNVIVTAHAFLMIFFMVMPMMIGGFGNWLVPL*LGAPDMAFPR 80
Cdd:MTH00153  15 TLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPR 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114  81 MNNMSFWLLPPSLILLLTSSIMNKGAGTGWTVYPPLSSNLSHSGSSVDFAIFSLHMAGISSIMGAINFISTIMNMKIYGL 160
Cdd:MTH00153  95 MNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGM 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114 161 SLDQLSLFTWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISH 240
Cdd:MTH00153 175 TLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISH 254

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114 241 MIFHESGKKETFGTLGMIYAMISIGILGFVVWAHHMFTIGMDVDTRAYFTSATMIIAVPTGIKVFSWMATMHGMKFKINP 320
Cdd:MTH00153 255 IISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSP 334

                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 674659114 321 TILWASGFVFLFTIGGLTGVVLSNSSVDIILHDTYYVVA 359
Cdd:MTH00153 335 SLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVA 373
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-359 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: 611.80  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114   1 TLYFIFGMWSGMLGTSMSMLIRLELGTPGSLIGDDQIYNVIVTAHAFLMIFFMVMPMMIGGFGNWLVPL*LGAPDMAFPR 80
Cdd:cd01663    8 TLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPR 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114  81 MNNMSFWLLPPSLILLLTSSIMNKGAGTGWTVYPPLSSNLSHSGSSVDFAIFSLHMAGISSIMGAINFISTIMNMKIYGL 160
Cdd:cd01663   88 LNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGM 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114 161 SLDQLSLFTWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISH 240
Cdd:cd01663  168 TLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISH 247

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114 241 MIFHESGKKETFGTLGMIYAMISIGILGFVVWAHHMFTIGMDVDTRAYFTSATMIIAVPTGIKVFSWMATMHGMKFKINP 320
Cdd:cd01663  248 IISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFET 327

                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 674659114 321 TILWASGFVFLFTIGGLTGVVLSNSSVDIILHDTYYVVA 359
Cdd:cd01663  328 PMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVA 366
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-359 7.09e-129

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: 378.49  E-value: 7.09e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114    1 TLYFIFGMWSGMLGTSMSMLIRLELGTPGSLIGDDQIYNVIVTAHAFLMIFFMVMPMMiGGFGNWLVPL*LGAPDMAFPR 80
Cdd:TIGR02891  11 ILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIPIL-AGFGNYLLPLMIGARDMAFPR 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114   81 MNNMSFWLLPPSLILLLTSSIMNKGAGTGWTVYPPLSSNLSHSGSSVDFAIFSLHMAGISSIMGAINFISTIMNMKIYGL 160
Cdd:TIGR02891  90 LNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGM 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114  161 SLDQLSLFTWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISH 240
Cdd:TIGR02891 170 TLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISE 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114  241 MIFHESGKKeTFGTLGMIYAMISIGILGFVVWAHHMFTIGMDVDTRAYFTSATMIIAVPTGIKVFSWMATMHGMKFKINP 320
Cdd:TIGR02891 250 ILPTFARKP-IFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTT 328

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 674659114  321 TILWASGFVFLFTIGGLTGVVLSNSSVDIILHDTYYVVA 359
Cdd:TIGR02891 329 PMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVA 367
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
2-359 3.24e-128

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 377.93  E-value: 3.24e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114   2 LYFIFGMWSGMLGTSMSMLIRLELGTPGSLIGDDQIYNVIVTAHAFLMIFFMVMPMmIGGFGNWLVPL*LGAPDMAFPRM 81
Cdd:COG0843   21 MYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATPF-LAGFGNYLVPLQIGARDMAFPRL 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114  82 NNMSFWLLPPSLILLLTSSIMNKGAGTGWTVYPPLSSNLSHSGSSVDFAIFSLHMAGISSIMGAINFISTIMNMKIYGLS 161
Cdd:COG0843  100 NALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMT 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114 162 LDQLSLFTWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISHM 241
Cdd:COG0843  180 LMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEI 259

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114 242 IFHESGKKeTFGTLGMIYAMISIGILGFVVWAHHMFTIGMDVDTRAYFTSATMIIAVPTGIKVFSWMATMHGMKFKINPT 321
Cdd:COG0843  260 IPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTP 338

                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 674659114 322 ILWASGFVFLFTIGGLTGVVLSNSSVDIILHDTYYVVA 359
Cdd:COG0843  339 MLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVA 376
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 2-359 4.55e-88

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: 271.75  E-value: 4.55e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114    2 LYFIFGMWSGMLGTSMSMLIRLELGTPGSLIGDDQIYNVIVTAHAFLMIFFMVMPMmIGGFGNWLVPL*LGAPDMAFPRM 81
Cdd:pfam00115   5 LYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATPF-LFGFGNYLVPLMIGARDMAFPRL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114   82 NNMSFWLLPPSLILLLTSSimnKGAGTGWTVYPPLSSnlshsgssVDFAIFSLHMAGISSIMGAINFISTIMNMKIYGLS 161
Cdd:pfam00115  84 NALSFWLVVLGAVLLLASF---GGATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMT 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114  162 LdQLSLFTWSVLITAILLLLSLPVLAGAITMLLTDRNLNtsffdpAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISHM 241
Cdd:pfam00115 153 L-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYI 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114  242 IFHESGKKeTFGTLGMIYAMISIGILGFVVWAHHMFTIGMDVDTRAYFTSATMIIAVPTGIKVFSWMATMHGMKFKIN-P 320
Cdd:pfam00115 226 LPKFAGRP-LFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFRtT 304

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 674659114  321 TILWASGFVFLFTIGGLTGVVLSNSSVDIILHDTYYVVA 359
Cdd:pfam00115 305 PMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVA 343
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-359 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 663.49  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114   1 TLYFIFGMWSGMLGTSMSMLIRLELGTPGSLIGDDQIYNVIVTAHAFLMIFFMVMPMMIGGFGNWLVPL*LGAPDMAFPR 80
Cdd:MTH00153  15 TLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPR 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114  81 MNNMSFWLLPPSLILLLTSSIMNKGAGTGWTVYPPLSSNLSHSGSSVDFAIFSLHMAGISSIMGAINFISTIMNMKIYGL 160
Cdd:MTH00153  95 MNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGM 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114 161 SLDQLSLFTWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISH 240
Cdd:MTH00153 175 TLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISH 254

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114 241 MIFHESGKKETFGTLGMIYAMISIGILGFVVWAHHMFTIGMDVDTRAYFTSATMIIAVPTGIKVFSWMATMHGMKFKINP 320
Cdd:MTH00153 255 IISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSP 334

                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 674659114 321 TILWASGFVFLFTIGGLTGVVLSNSSVDIILHDTYYVVA 359
Cdd:MTH00153 335 SLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVA 373
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-359 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: 611.80  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114   1 TLYFIFGMWSGMLGTSMSMLIRLELGTPGSLIGDDQIYNVIVTAHAFLMIFFMVMPMMIGGFGNWLVPL*LGAPDMAFPR 80
Cdd:cd01663    8 TLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPR 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114  81 MNNMSFWLLPPSLILLLTSSIMNKGAGTGWTVYPPLSSNLSHSGSSVDFAIFSLHMAGISSIMGAINFISTIMNMKIYGL 160
Cdd:cd01663   88 LNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGM 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114 161 SLDQLSLFTWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISH 240
Cdd:cd01663  168 TLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISH 247

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114 241 MIFHESGKKETFGTLGMIYAMISIGILGFVVWAHHMFTIGMDVDTRAYFTSATMIIAVPTGIKVFSWMATMHGMKFKINP 320
Cdd:cd01663  248 IISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFET 327

                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 674659114 321 TILWASGFVFLFTIGGLTGVVLSNSSVDIILHDTYYVVA 359
Cdd:cd01663  328 PMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVA 366
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-359 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 573.55  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114   1 TLYFIFGMWSGMLGTSMSMLIRLELGTPGSLIGDDQIYNVIVTAHAFLMIFFMVMPMMIGGFGNWLVPL*LGAPDMAFPR 80
Cdd:MTH00167  17 TLYFIFGAWAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPR 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114  81 MNNMSFWLLPPSLILLLTSSIMNKGAGTGWTVYPPLSSNLSHSGSSVDFAIFSLHMAGISSIMGAINFISTIMNMKIYGL 160
Cdd:MTH00167  97 MNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGI 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114 161 SLDQLSLFTWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISH 240
Cdd:MTH00167 177 TQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISH 256

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114 241 MIFHESGKKETFGTLGMIYAMISIGILGFVVWAHHMFTIGMDVDTRAYFTSATMIIAVPTGIKVFSWMATMHGMKFKINP 320
Cdd:MTH00167 257 IVVYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLHGGKIKWET 336

                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 674659114 321 TILWASGFVFLFTIGGLTGVVLSNSSVDIILHDTYYVVA 359
Cdd:MTH00167 337 PMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVA 375
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-359 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 674659114   1 TLYFIFGMWSGMLGTSMSMLIRLELGTPGSLIGDDQIYNVIVTAHAFLMIFFMVMPMMIGGFGNWLVPL*LGAPDMAFPR 80
Cdd:MTH00223  14 TLYLIFGMWSGLVGTSLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPR 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114  81 MNNMSFWLLPPSLILLLTSSIMNKGAGTGWTVYPPLSSNLSHSGSSVDFAIFSLHMAGISSIMGAINFISTIMNMKIYGL 160
Cdd:MTH00223  94 LNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGM 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114 161 SLDQLSLFTWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISH 240
Cdd:MTH00223 174 QLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISH 253

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114 241 MIFHESGKKETFGTLGMIYAMISIGILGFVVWAHHMFTIGMDVDTRAYFTSATMIIAVPTGIKVFSWMATMHGMKFKINP 320
Cdd:MTH00223 254 IVSHYSSKKEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGSKIKYEA 333

                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 674659114 321 TILWASGFVFLFTIGGLTGVVLSNSSVDIILHDTYYVVA 359
Cdd:MTH00223 334 PMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVA 372
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-359 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 559.71  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114   1 TLYFIFGMWSGMLGTSMSMLIRLELGTPGSLIGDDQIYNVIVTAHAFLMIFFMVMPMMIGGFGNWLVPL*LGAPDMAFPR 80
Cdd:MTH00116  17 TLYLIFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPR 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114  81 MNNMSFWLLPPSLILLLTSSIMNKGAGTGWTVYPPLSSNLSHSGSSVDFAIFSLHMAGISSIMGAINFISTIMNMKIYGL 160
Cdd:MTH00116  97 MNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAM 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114 161 SLDQLSLFTWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISH 240
Cdd:MTH00116 177 SQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISH 256

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114 241 MIFHESGKKETFGTLGMIYAMISIGILGFVVWAHHMFTIGMDVDTRAYFTSATMIIAVPTGIKVFSWMATMHGMKFKINP 320
Cdd:MTH00116 257 IVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSWLATLHGGTIKWDP 336

                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 674659114 321 TILWASGFVFLFTIGGLTGVVLSNSSVDIILHDTYYVVA 359
Cdd:MTH00116 337 PMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVA 375
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-359 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 558.96  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114   1 TLYFIFGMWSGMLGTSMSMLIRLELGTPGSLIGDDQIYNVIVTAHAFLMIFFMVMPMMIGGFGNWLVPL*LGAPDMAFPR 80
Cdd:MTH00142  15 TLYFLFGAWAGMVGTGLSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPR 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114  81 MNNMSFWLLPPSLILLLTSSIMNKGAGTGWTVYPPLSSNLSHSGSSVDFAIFSLHMAGISSIMGAINFISTIMNMKIYGL 160
Cdd:MTH00142  95 MNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGM 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114 161 SLDQLSLFTWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISH 240
Cdd:MTH00142 175 KFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISH 254

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114 241 MIFHESGKKETFGTLGMIYAMISIGILGFVVWAHHMFTIGMDVDTRAYFTSATMIIAVPTGIKVFSWMATMHGMKFKINP 320
Cdd:MTH00142 255 IINHYSGKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFSWLATLHGSKVKYEP 334

                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 674659114 321 TILWASGFVFLFTIGGLTGVVLSNSSVDIILHDTYYVVA 359
Cdd:MTH00142 335 PMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVA 373
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-359 0e+00

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 512.91  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114   1 TLYFIFGMWSGMLGTSMSMLIRLELGTPGSLIGDDQIYNVIVTAHAFLMIFFMVMPMMIGGFGNWLVPL*LGAPDMAFPR 80
Cdd:MTH00007  14 TLYFILGVWGGLLGTSMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPR 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114  81 MNNMSFWLLPPSLILLLTSSIMNKGAGTGWTVYPPLSSNLSHSGSSVDFAIFSLHMAGISSIMGAINFISTIMNMKIYGL 160
Cdd:MTH00007  94 LNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGL 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114 161 SLDQLSLFTWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISH 240
Cdd:MTH00007 174 RLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGAISH 253

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114 241 MIFHESGKKETFGTLGMIYAMISIGILGFVVWAHHMFTIGMDVDTRAYFTSATMIIAVPTGIKVFSWMATMHGMKFKINP 320
Cdd:MTH00007 254 IVTHYAGKLEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGSPIKYET 333

                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 674659114 321 TILWASGFVFLFTIGGLTGVVLSNSSVDIILHDTYYVVA 359
Cdd:MTH00007 334 PMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVA 372
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-359 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 512.07  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114   1 TLYFIFGMWSGMLGTSMSMLIRLELGTPGSLIGDDQIYNVIVTAHAFLMIFFMVMPMMIGGFGNWLVPL*LGAPDMAFPR 80
Cdd:MTH00037  17 TLYLIFGAWAGMVGTAMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPR 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114  81 MNNMSFWLLPPSLILLLTSSIMNKGAGTGWTVYPPLSSNLSHSGSSVDFAIFSLHMAGISSIMGAINFISTIMNMKIYGL 160
Cdd:MTH00037  97 MNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGM 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114 161 SLDQLSLFTWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISH 240
Cdd:MTH00037 177 TFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISH 256

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114 241 MIFHESGKKETFGTLGMIYAMISIGILGFVVWAHHMFTIGMDVDTRAYFTSATMIIAVPTGIKVFSWMATMHGMKFKINP 320
Cdd:MTH00037 257 VIAHYSGKQEPFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWMATLQGSNLRWET 336

                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 674659114 321 TILWASGFVFLFTIGGLTGVVLSNSSVDIILHDTYYVVA 359
Cdd:MTH00037 337 PLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVA 375
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-359 1.76e-179

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 507.88  E-value: 1.76e-179
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114   1 TLYFIFGMWSGMLGTSMSMLIRLELGTPGSLIGDDQIYNVIVTAHAFLMIFFMVMPMMIGGFGNWLVPL*LGAPDMAFPR 80
Cdd:MTH00103  17 TLYLLFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPR 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114  81 MNNMSFWLLPPSLILLLTSSIMNKGAGTGWTVYPPLSSNLSHSGSSVDFAIFSLHMAGISSIMGAINFISTIMNMKIYGL 160
Cdd:MTH00103  97 MNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAM 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114 161 SLDQLSLFTWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISH 240
Cdd:MTH00103 177 SQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISH 256

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114 241 MIFHESGKKETFGTLGMIYAMISIGILGFVVWAHHMFTIGMDVDTRAYFTSATMIIAVPTGIKVFSWMATMHGMKFKINP 320
Cdd:MTH00103 257 IVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGNIKWSP 336

                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 674659114 321 TILWASGFVFLFTIGGLTGVVLSNSSVDIILHDTYYVVA 359
Cdd:MTH00103 337 AMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVA 375
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-359 8.18e-178

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 503.69  E-value: 8.18e-178
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114   1 TLYFIFGMWSGMLGTSMSMLIRLELGTPGSLIGDDQIYNVIVTAHAFLMIFFMVMPMMIGGFGNWLVPL*LGAPDMAFPR 80
Cdd:MTH00183  17 TLYLVFGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPR 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114  81 MNNMSFWLLPPSLILLLTSSIMNKGAGTGWTVYPPLSSNLSHSGSSVDFAIFSLHMAGISSIMGAINFISTIMNMKIYGL 160
Cdd:MTH00183  97 MNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAI 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114 161 SLDQLSLFTWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISH 240
Cdd:MTH00183 177 SQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISH 256

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114 241 MIFHESGKKETFGTLGMIYAMISIGILGFVVWAHHMFTIGMDVDTRAYFTSATMIIAVPTGIKVFSWMATMHGMKFKINP 320
Cdd:MTH00183 257 IVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGSIKWET 336

                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 674659114 321 TILWASGFVFLFTIGGLTGVVLSNSSVDIILHDTYYVVA 359
Cdd:MTH00183 337 PLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVA 375
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-359 4.84e-176

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 499.08  E-value: 4.84e-176
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114   1 TLYFIFGMWSGMLGTSMSMLIRLELGTPGSLIGDDQIYNVIVTAHAFLMIFFMVMPMMIGGFGNWLVPL*LGAPDMAFPR 80
Cdd:MTH00077  17 TLYLVFGAWAGMVGTALSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPR 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114  81 MNNMSFWLLPPSLILLLTSSIMNKGAGTGWTVYPPLSSNLSHSGSSVDFAIFSLHMAGISSIMGAINFISTIMNMKIYGL 160
Cdd:MTH00077  97 MNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSM 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114 161 SLDQLSLFTWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISH 240
Cdd:MTH00077 177 SQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISH 256

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114 241 MIFHESGKKETFGTLGMIYAMISIGILGFVVWAHHMFTIGMDVDTRAYFTSATMIIAVPTGIKVFSWMATMHGMKFKINP 320
Cdd:MTH00077 257 IVTYYSAKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGAIKWDA 336

                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 674659114 321 TILWASGFVFLFTIGGLTGVVLSNSSVDIILHDTYYVVA 359
Cdd:MTH00077 337 AMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVA 375
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-359 1.97e-175

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 497.28  E-value: 1.97e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114   1 TLYFIFGMWSGMLGTSMSMLIRLELGTPGSLIGDDQIYNVIVTAHAFLMIFFMVMPMMIGGFGNWLVPL*LGAPDMAFPR 80
Cdd:MTH00079  18 TLYFLFGLWSGMVGTSLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPR 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114  81 MNNMSFWLLPPSLILLLTSSIMNKGAGTGWTVYPPLSSNLSHSGSsVDFAIFSLHMAGISSIMGAINFISTIMNMKIYGL 160
Cdd:MTH00079  98 LNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLSTLGHPGSS-VDLAIFSLHCAGISSILGGINFMVTTKNLRSSSI 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114 161 SLDQLSLFTWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISH 240
Cdd:MTH00079 177 SLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPEVYILILPAFGIISQ 256

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114 241 MIFHESGKKETFGTLGMIYAMISIGILGFVVWAHHMFTIGMDVDTRAYFTSATMIIAVPTGIKVFSWMATMHGMKFKINP 320
Cdd:MTH00079 257 STLYLTGKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMKFQP 336

                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 674659114 321 TILWASGFVFLFTIGGLTGVVLSNSSVDIILHDTYYVVA 359
Cdd:MTH00079 337 LLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVS 375
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-359 1.31e-171

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 488.18  E-value: 1.31e-171
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114   1 TLYFIFGMWSGMLGTSMSMLIRLELGTPGSLIGDDQIYNVIVTAHAFLMIFFMVMPMMIGGFGNWLVPL*LGAPDMAFPR 80
Cdd:MTH00182  19 TLYLVFGAGAGMIGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPR 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114  81 MNNMSFWLLPPSLILLLTSSIMNKGAGTGWTVYPPLSSNLSHSGSSVDFAIFSLHMAGISSIMGAINFISTIMNMKIYGL 160
Cdd:MTH00182  99 LNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGV 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114 161 SLDQLSLFTWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISH 240
Cdd:MTH00182 179 TFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISQ 258

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114 241 MIFHESGKKETFGTLGMIYAMISIGILGFVVWAHHMFTIGMDVDTRAYFTSATMIIAVPTGIKVFSWMATMHGMKFKINP 320
Cdd:MTH00182 259 IIPTFVAKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGGTLRLDT 338

                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 674659114 321 TILWASGFVFLFTIGGLTGVVLSNSSVDIILHDTYYVVA 359
Cdd:MTH00182 339 PMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVA 377
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-359 9.91e-168

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 478.17  E-value: 9.91e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114   1 TLYFIFGMWSGMLGTSMSMLIRLELGTPGSLIGDDQIYNVIVTAHAFLMIFFMVMPMMIGGFGNWLVPL*LGAPDMAFPR 80
Cdd:MTH00184  19 TLYLLFGAFAGMIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPR 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114  81 MNNMSFWLLPPSLILLLTSSIMNKGAGTGWTVYPPLSSNLSHSGSSVDFAIFSLHMAGISSIMGAINFISTIMNMKIYGL 160
Cdd:MTH00184  99 LNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGI 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114 161 SLDQLSLFTWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISH 240
Cdd:MTH00184 179 TMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQ 258

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114 241 MIFHESGKKETFGTLGMIYAMISIGILGFVVWAHHMFTIGMDVDTRAYFTSATMIIAVPTGIKVFSWMATMHGMKFKINP 320
Cdd:MTH00184 259 IIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATIFGGSLRLDT 338

                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 674659114 321 TILWASGFVFLFTIGGLTGVVLSNSSVDIILHDTYYVVA 359
Cdd:MTH00184 339 PMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVA 377
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-359 1.29e-149

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 432.51  E-value: 1.29e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114   1 TLYFIFGMWSGMLGTSMSMLIRLELGTPGSLIGDDQIYNVIVTAHAFLMIFFMVMPMMIGGFGNWLVPL*LGAPDMAFPR 80
Cdd:MTH00026  18 SLYLVFGALSGAIGTAFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPR 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114  81 MNNMSFWLLPPSLILLLTSSIMNKGAGTGWTVYPPLSSNLSHSGSSVDFAIFSLHMAGISSIMGAINFISTIMNMKIYGL 160
Cdd:MTH00026  98 LNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGM 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114 161 SLDQLSLFTWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISH 240
Cdd:MTH00026 178 TMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQ 257

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114 241 MIFHESGKKETFGTLGMIYAMISIGILGFVVWAHHMFTIGMDVDTRAYFTSATMIIAVPTGIKVFSWMATM--HGMKFKI 318
Cdd:MTH00026 258 ILSLFSYKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSWLATVsgSGRNLIF 337

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 674659114 319 NPTILWASGFVFLFTIGGLTGVVLSNSSVDIILHDTYYVVA 359
Cdd:MTH00026 338 TTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVA 378
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-359 4.16e-141

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: 408.07  E-value: 4.16e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114   1 TLYFIFGMWSGMLGTSMSMLIRLELGTPGSLIGDDQIYNVIVTAHAFLMIFFMVMPMMIGGFGNWLVPL*LGAPDMAFPR 80
Cdd:cd00919    6 LLYLIFAFVALLLGGLLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPPL-IGARDLAFPR 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114  81 MNNMSFWLLPPSLILLLTSSIMNKGAGTGWTVYPPLSSNLSHSGSSVDFAIFSLHMAGISSIMGAINFISTIMNMKIYGL 160
Cdd:cd00919   85 LNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGM 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114 161 SLDQLSLFTWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISH 240
Cdd:cd00919  165 TLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAFGAISE 244

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114 241 MIFHESGKKeTFGTLGMIYAMISIGILGFVVWAHHMFTIGMDVDTRAYFTSATMIIAVPTGIKVFSWMATMHGMKFKINP 320
Cdd:cd00919  245 IIPTFSGKP-LFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGRIRFDP 323

                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 674659114 321 TILWASGFVFLFTIGGLTGVVLSNSSVDIILHDTYYVVA 359
Cdd:cd00919  324 PMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVA 362
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-359 7.09e-129

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: 378.49  E-value: 7.09e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114    1 TLYFIFGMWSGMLGTSMSMLIRLELGTPGSLIGDDQIYNVIVTAHAFLMIFFMVMPMMiGGFGNWLVPL*LGAPDMAFPR 80
Cdd:TIGR02891  11 ILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIPIL-AGFGNYLLPLMIGARDMAFPR 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114   81 MNNMSFWLLPPSLILLLTSSIMNKGAGTGWTVYPPLSSNLSHSGSSVDFAIFSLHMAGISSIMGAINFISTIMNMKIYGL 160
Cdd:TIGR02891  90 LNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGM 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114  161 SLDQLSLFTWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISH 240
Cdd:TIGR02891 170 TLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISE 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114  241 MIFHESGKKeTFGTLGMIYAMISIGILGFVVWAHHMFTIGMDVDTRAYFTSATMIIAVPTGIKVFSWMATMHGMKFKINP 320
Cdd:TIGR02891 250 ILPTFARKP-IFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTT 328

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 674659114  321 TILWASGFVFLFTIGGLTGVVLSNSSVDIILHDTYYVVA 359
Cdd:TIGR02891 329 PMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVA 367
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
2-359 3.24e-128

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 377.93  E-value: 3.24e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114   2 LYFIFGMWSGMLGTSMSMLIRLELGTPGSLIGDDQIYNVIVTAHAFLMIFFMVMPMmIGGFGNWLVPL*LGAPDMAFPRM 81
Cdd:COG0843   21 MYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATPF-LAGFGNYLVPLQIGARDMAFPRL 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114  82 NNMSFWLLPPSLILLLTSSIMNKGAGTGWTVYPPLSSNLSHSGSSVDFAIFSLHMAGISSIMGAINFISTIMNMKIYGLS 161
Cdd:COG0843  100 NALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMT 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114 162 LDQLSLFTWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISHM 241
Cdd:COG0843  180 LMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEI 259

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114 242 IFHESGKKeTFGTLGMIYAMISIGILGFVVWAHHMFTIGMDVDTRAYFTSATMIIAVPTGIKVFSWMATMHGMKFKINPT 321
Cdd:COG0843  260 IPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTP 338

                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 674659114 322 ILWASGFVFLFTIGGLTGVVLSNSSVDIILHDTYYVVA 359
Cdd:COG0843  339 MLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVA 376
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 2-359 6.80e-128

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 376.33  E-value: 6.80e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114   2 LYFIFGMWSGMLGTSMSMLIRLELGTPGSLIGDDQIYNVIVTAHAFLMIFFMVMPMMIGGFGNWLVPL*LGAPDMAFPRM 81
Cdd:MTH00048  19 IYTLLGVWSGFVGLSLSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRL 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114  82 NNMSFWLLPPSLILLLTSsiMNKGAGTGWTVYPPLSSNLSHSGSSVDFAIFSLHMAGISSIMGAINFISTIMNMKIYGLS 161
Cdd:MTH00048  99 NALSAWLLVPSIVFLLLS--MCLGAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNVF 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114 162 LdQLSLFTWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISHM 241
Cdd:MTH00048 177 S-RTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPEVYVLILPGFGIISHI 255

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114 242 IFHESGKKETFGTLGMIYAMISIGILGFVVWAHHMFTIGMDVDTRAYFTSATMIIAVPTGIKVFSWMATMHGMKF-KINP 320
Cdd:MTH00048 256 CLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFSWLYMLLNSRVrKSDP 335

                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 674659114 321 TILWASGFVFLFTIGGLTGVVLSNSSVDIILHDTYYVVA 359
Cdd:MTH00048 336 VVWWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVA 374
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 13-359 1.36e-109

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: 329.16  E-value: 1.36e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114  13 LGTSMSMLIRLELGTPGSLIGDDQIYNVIVTAHAFLMIFFMVMPMMIGgFGNWLVPL*LGAPDMAFPRMNNMSFWLLPPS 92
Cdd:cd01662   24 RGGVDALLMRTQLALPGNDFLSPEHYNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFPRLNALSFWLFLFG 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114  93 LILLLTSSIMNKGAGTGWTVYPPLSSNLSHSGSSVDFAIFSLHMAGISSIMGAINFISTIMNMKIYGLSLDQLSLFTWSV 172
Cdd:cd01662  103 GLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWTT 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114 173 LITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMIShMIFHESGKKETF 252
Cdd:cd01662  183 LVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYILILPAFGIFS-EIVPTFSRKPLF 261

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114 253 GTLGMIYAMISIGILGFVVWAHHMFTIGMDVDTRAYFTSATMIIAVPTGIKVFSWMATMHGMKFKINPTILWASGFVFLF 332
Cdd:cd01662  262 GYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLFTMWRGRIRFETPMLWAIGFLVTF 341

                        330       340
                 ....*....|....*....|....*..
gi 674659114 333 TIGGLTGVVLSNSSVDIILHDTYYVVA 359
Cdd:cd01662  342 VIGGLTGVMLASPPADFQVHDTYFVVA 368
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 2-359 4.55e-88

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: 271.75  E-value: 4.55e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114    2 LYFIFGMWSGMLGTSMSMLIRLELGTPGSLIGDDQIYNVIVTAHAFLMIFFMVMPMmIGGFGNWLVPL*LGAPDMAFPRM 81
Cdd:pfam00115   5 LYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATPF-LFGFGNYLVPLMIGARDMAFPRL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114   82 NNMSFWLLPPSLILLLTSSimnKGAGTGWTVYPPLSSnlshsgssVDFAIFSLHMAGISSIMGAINFISTIMNMKIYGLS 161
Cdd:pfam00115  84 NALSFWLVVLGAVLLLASF---GGATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMT 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114  162 LdQLSLFTWSVLITAILLLLSLPVLAGAITMLLTDRNLNtsffdpAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISHM 241
Cdd:pfam00115 153 L-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYI 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114  242 IFHESGKKeTFGTLGMIYAMISIGILGFVVWAHHMFTIGMDVDTRAYFTSATMIIAVPTGIKVFSWMATMHGMKFKIN-P 320
Cdd:pfam00115 226 LPKFAGRP-LFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFRtT 304

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 674659114  321 TILWASGFVFLFTIGGLTGVVLSNSSVDIILHDTYYVVA 359
Cdd:pfam00115 305 PMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVA 343
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 38-359 1.41e-73

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 240.61  E-value: 1.41e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114  38 YNVIVTAHAFLMIFFMVMPMMIGgFGNWLVPL*LGAPDMAFPRMNNMSFWLLPPSLILLLTSSIMNKGAGTGWTVYPPLS 117
Cdd:PRK15017  99 YDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLS 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114 118 SNLSHSGSSVDFAIFSLHMAGISSIMGAINFISTIMNMKIYGLSLDQLSLFTWSVLITAILLLLSLPVLAGAITMLLTDR 197
Cdd:PRK15017 178 GIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDR 257

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114 198 NLNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISHMIFHESgKKETFGTLGMIYAMISIGILGFVVWAHHMF 277
Cdd:PRK15017 258 YLGTHFFTNDMGGNMMMYINLIWAWGHPEVYILILPVFGVFSEIAATFS-RKRLFGYTSLVWATVCITVLSFIVWLHHFF 336

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114 278 TIGMDVDTRAYFTSATMIIAVPTGIKVFSWMATMHGMKFKINPTILWASGFVFLFTIGGLTGVVLSNSSVDIILHDTYYV 357
Cdd:PRK15017 337 TMGAGANVNAFFGITTMIIAIPTGVKIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFL 416


                 ..
gi 674659114 358 VA 359
Cdd:PRK15017 417 IA 418
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 2-359 1.59e-73

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: 239.76  E-value: 1.59e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114    2 LYFIFGMWSGMLGTSMSMLIRLELGTPGSLIGDDQIYNVIVTAHAFLMIFFMVMPMMIGgFGNWLVPL*LGAPDMAFPRM 81
Cdd:TIGR02882  56 MYIICAVLMLFRGGIDALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVL 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114   82 NNMSFWLLPPSLILLLTSSIMNKGAGTGWTVYPPLSSNLSHSGSSVDFAIFSLHMAGISSIMGAINFISTIMNMKIYGLS 161
Cdd:TIGR02882 135 NALSFWLFFAGAMLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMK 214

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114  162 LDQLSLFTWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISHM 241
Cdd:TIGR02882 215 LMQMPMFTWTTLITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLFWIWGHPEVYIVILPAFGIYSEI 294

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114  242 IfHESGKKETFGTLGMIYAMISIGILGFVVWAHHMFTIGMDVDTRAYFTSATMIIAVPTGIKVFSWMATMHGMKFKINPT 321
Cdd:TIGR02882 295 I-STFAQKRLFGYKSMVWSTVGIAFLSFLVWVHHFFTMGNGALINSFFSITTMAIAIPTGVKIFNWLLTLYKGKIRFTTP 373

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 674659114  322 ILWASGFVFLFTIGGLTGVVLSNSSVDIILHDTYYVVA 359
Cdd:TIGR02882 374 MLFSLAFIPNFLIGGVTGVMLAMASADYQYHNTYFLVA 411
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
 211-358 1.89e-03

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: 39.96  E-value: 1.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114 211 DPVLYQHLFWFFGHPEVYILILPGFGMISHMIFHESGKKETFGTLGMIyAMISIGILGFVVWAHHMFT-IGMDVDTRAYF 289
Cdd:cd01660  200 DVLLSRTLFWWFGHPLVYFWLLPAYIAWYTILPKIAGGKLFSDPLARL-AFILFLLFSTPVGFHHQFAdPGIGPGWKFIH 278

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 674659114 290 TSATMIIAVPTGIKVFSWMATM-HGMKFKINPTILW-----------ASGFVF---LFTIGGLTGVVLSNSSVDIILHDT 354
Cdd:cd01660  279 MVLTFMVALPSLLTAFTVFASLeIAGRLRGGKGLFGwiralpwgdpmFLALFLamlMFIPGGAGGIINASYQLNYVVHNT 358


                 ....
gi 674659114 355 YYVV 358
Cdd:cd01660  359 AWVP 362
 
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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