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Conserved domains on  [gi|1148359081|gb|AQS17649|]
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cytchrome oxidase subunit I, partial (mitochondrion) [Kilyana sp. CG306]

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 ...
 1-358 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: 685.06  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081   1 TLYLLFGVWSAMVGTAMSVLIRMELGQVGSLYGDDHLYNVIVTAHAFVMIFFMVMPILIGGFGNWLIPLMLGAPDMAFPR 80
Cdd:MTH00153   15 TLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPR 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081  81 MNNLSFWLLPPSLILLFISSMAEMGVGAGWTVYPPLAANISHPGSAMDFAIFSLHLAGASSIMGAINFITTIINMRLLGM 160
Cdd:MTH00153   95 MNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGM 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081 161 TMEKVPLFVWSVFVTTILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGIVSH 240
Cdd:MTH00153  175 TLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISH 254

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081 241 IISAYVGKREPFGSLGMIYAMVGIGGMGFVVWAHHMFSVGMDMDTRAYFTAATMIIAVPTGIKVFSWMATFHGSLFKIDT 320
Cdd:MTH00153  255 IISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSP 334

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1148359081 321 SLMWCIGFVFLFTLGGITGVVLSNSSLDIVLHDTYYVV 358
Cdd:MTH00153  335 SLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVV 372
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-358 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 685.06  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081   1 TLYLLFGVWSAMVGTAMSVLIRMELGQVGSLYGDDHLYNVIVTAHAFVMIFFMVMPILIGGFGNWLIPLMLGAPDMAFPR 80
Cdd:MTH00153   15 TLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPR 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081  81 MNNLSFWLLPPSLILLFISSMAEMGVGAGWTVYPPLAANISHPGSAMDFAIFSLHLAGASSIMGAINFITTIINMRLLGM 160
Cdd:MTH00153   95 MNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGM 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081 161 TMEKVPLFVWSVFVTTILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGIVSH 240
Cdd:MTH00153  175 TLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISH 254

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081 241 IISAYVGKREPFGSLGMIYAMVGIGGMGFVVWAHHMFSVGMDMDTRAYFTAATMIIAVPTGIKVFSWMATFHGSLFKIDT 320
Cdd:MTH00153  255 IISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSP 334

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1148359081 321 SLMWCIGFVFLFTLGGITGVVLSNSSLDIVLHDTYYVV 358
Cdd:MTH00153  335 SLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVV 372
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-358 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: 637.99  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081   1 TLYLLFGVWSAMVGTAMSVLIRMELGQVGSLYGDDHLYNVIVTAHAFVMIFFMVMPILIGGFGNWLIPLMLGAPDMAFPR 80
Cdd:cd01663     8 TLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPR 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081  81 MNNLSFWLLPPSLILLFISSMAEMGVGAGWTVYPPLAANISHPGSAMDFAIFSLHLAGASSIMGAINFITTIINMRLLGM 160
Cdd:cd01663    88 LNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGM 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081 161 TMEKVPLFVWSVFVTTILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGIVSH 240
Cdd:cd01663   168 TLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISH 247

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081 241 IISAYVGKREPFGSLGMIYAMVGIGGMGFVVWAHHMFSVGMDMDTRAYFTAATMIIAVPTGIKVFSWMATFHGSLFKIDT 320
Cdd:cd01663   248 IISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFET 327

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1148359081 321 SLMWCIGFVFLFTLGGITGVVLSNSSLDIVLHDTYYVV 358
Cdd:cd01663   328 PMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVV 365
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-358 5.34e-139

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: 404.30  E-value: 5.34e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081   1 TLYLLFGVWSAMVGTAMSVLIRMELGQVGSLYGDDHLYNVIVTAHAFVMIFFMVMPILiGGFGNWLIPLMLGAPDMAFPR 80
Cdd:TIGR02891  11 ILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIPIL-AGFGNYLLPLMIGARDMAFPR 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081  81 MNNLSFWLLPPSLILLFISSMAEMGVGAGWTVYPPLAANISHPGSAMDFAIFSLHLAGASSIMGAINFITTIINMRLLGM 160
Cdd:TIGR02891  90 LNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGM 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081 161 TMEKVPLFVWSVFVTTILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGIVSH 240
Cdd:TIGR02891 170 TLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISE 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081 241 IISAYVGKRePFGSLGMIYAMVGIGGMGFVVWAHHMFSVGMDMDTRAYFTAATMIIAVPTGIKVFSWMATFHGSLFKIDT 320
Cdd:TIGR02891 250 ILPTFARKP-IFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTT 328

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1148359081 321 SLMWCIGFVFLFTLGGITGVVLSNSSLDIVLHDTYYVV 358
Cdd:TIGR02891 329 PMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVV 366
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
2-358 1.24e-137

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 401.81  E-value: 1.24e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081   2 LYLLFGVWSAMVGTAMSVLIRMELGQVGSLYGDDHLYNVIVTAHAFVMIFFMVMPIlIGGFGNWLIPLMLGAPDMAFPRM 81
Cdd:COG0843    21 MYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATPF-LAGFGNYLVPLQIGARDMAFPRL 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081  82 NNLSFWLLPPSLILLFISSMAEMGVGAGWTVYPPLAANISHPGSAMDFAIFSLHLAGASSIMGAINFITTIINMRLLGMT 161
Cdd:COG0843   100 NALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMT 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081 162 MEKVPLFVWSVFVTTILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGIVSHI 241
Cdd:COG0843   180 LMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEI 259

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081 242 ISAYVGKRePFGSLGMIYAMVGIGGMGFVVWAHHMFSVGMDMDTRAYFTAATMIIAVPTGIKVFSWMATFHGSLFKIDTS 321
Cdd:COG0843   260 IPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTP 338

                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1148359081 322 LMWCIGFVFLFTLGGITGVVLSNSSLDIVLHDTYYVV 358
Cdd:COG0843   339 MLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVV 375
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 2-358 5.28e-91

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


Pssm-ID: 459678  Cd Length: 432  Bit Score: 279.07  E-value: 5.28e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081   2 LYLLFGVWSAMVGTAMSVLIRMELGQVGSLYGDDHLYNVIVTAHAFVMIFFMVMPIlIGGFGNWLIPLMLGAPDMAFPRM 81
Cdd:pfam00115   5 LYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATPF-LFGFGNYLVPLMIGARDMAFPRL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081  82 NNLSFWLLPPSLILLFISSMaemGVGAGWTVYPPLAAnishpgsaMDFAIFSLHLAGASSIMGAINFITTIINMRLLGMT 161
Cdd:pfam00115  84 NALSFWLVVLGAVLLLASFG---GATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMT 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081 162 MeKVPLFVWSVFVTTILLLLSLPVLAGAITMLLTDRNFNtsffdpAGGGDPILFQHLFWFFGHPEVYILILPGFGIVSHI 241
Cdd:pfam00115 153 L-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYI 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081 242 ISAYVGKRePFGSLGMIYAMVGIGGMGFVVWAHHMFSVGMDMDTRAYFTAATMIIAVPTGIKVFSWMATFHGSLFKIDTS 321
Cdd:pfam00115 226 LPKFAGRP-LFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFRTT 304

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1148359081 322 -LMWCIGFVFLFTLGGITGVVLSNSSLDIVLHDTYYVV 358
Cdd:pfam00115 305 pMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVV 342
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-358 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 685.06  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081   1 TLYLLFGVWSAMVGTAMSVLIRMELGQVGSLYGDDHLYNVIVTAHAFVMIFFMVMPILIGGFGNWLIPLMLGAPDMAFPR 80
Cdd:MTH00153   15 TLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPR 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081  81 MNNLSFWLLPPSLILLFISSMAEMGVGAGWTVYPPLAANISHPGSAMDFAIFSLHLAGASSIMGAINFITTIINMRLLGM 160
Cdd:MTH00153   95 MNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGM 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081 161 TMEKVPLFVWSVFVTTILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGIVSH 240
Cdd:MTH00153  175 TLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISH 254

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081 241 IISAYVGKREPFGSLGMIYAMVGIGGMGFVVWAHHMFSVGMDMDTRAYFTAATMIIAVPTGIKVFSWMATFHGSLFKIDT 320
Cdd:MTH00153  255 IISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSP 334

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1148359081 321 SLMWCIGFVFLFTLGGITGVVLSNSSLDIVLHDTYYVV 358
Cdd:MTH00153  335 SLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVV 372
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-358 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: 637.99  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081   1 TLYLLFGVWSAMVGTAMSVLIRMELGQVGSLYGDDHLYNVIVTAHAFVMIFFMVMPILIGGFGNWLIPLMLGAPDMAFPR 80
Cdd:cd01663     8 TLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPR 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081  81 MNNLSFWLLPPSLILLFISSMAEMGVGAGWTVYPPLAANISHPGSAMDFAIFSLHLAGASSIMGAINFITTIINMRLLGM 160
Cdd:cd01663    88 LNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGM 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081 161 TMEKVPLFVWSVFVTTILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGIVSH 240
Cdd:cd01663   168 TLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISH 247

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081 241 IISAYVGKREPFGSLGMIYAMVGIGGMGFVVWAHHMFSVGMDMDTRAYFTAATMIIAVPTGIKVFSWMATFHGSLFKIDT 320
Cdd:cd01663   248 IISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFET 327

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1148359081 321 SLMWCIGFVFLFTLGGITGVVLSNSSLDIVLHDTYYVV 358
Cdd:cd01663   328 PMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVV 365
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-358 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 608.21  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081   1 TLYLLFGVWSAMVGTAMSVLIRMELGQVGSLYGDDHLYNVIVTAHAFVMIFFMVMPILIGGFGNWLIPLMLGAPDMAFPR 80
Cdd:MTH00167   17 TLYFIFGAWAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPR 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081  81 MNNLSFWLLPPSLILLFISSMAEMGVGAGWTVYPPLAANISHPGSAMDFAIFSLHLAGASSIMGAINFITTIINMRLLGM 160
Cdd:MTH00167   97 MNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGI 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081 161 TMEKVPLFVWSVFVTTILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGIVSH 240
Cdd:MTH00167  177 TQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISH 256

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081 241 IISAYVGKREPFGSLGMIYAMVGIGGMGFVVWAHHMFSVGMDMDTRAYFTAATMIIAVPTGIKVFSWMATFHGSLFKIDT 320
Cdd:MTH00167  257 IVVYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLHGGKIKWET 336

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1148359081 321 SLMWCIGFVFLFTLGGITGVVLSNSSLDIVLHDTYYVV 358
Cdd:MTH00167  337 PMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVV 374
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-358 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 596.96  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081   1 TLYLLFGVWSAMVGTAMSVLIRMELGQVGSLYGDDHLYNVIVTAHAFVMIFFMVMPILIGGFGNWLIPLMLGAPDMAFPR 80
Cdd:MTH00223   14 TLYLIFGMWSGLVGTSLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPR 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081  81 MNNLSFWLLPPSLILLFISSMAEMGVGAGWTVYPPLAANISHPGSAMDFAIFSLHLAGASSIMGAINFITTIINMRLLGM 160
Cdd:MTH00223   94 LNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGM 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081 161 TMEKVPLFVWSVFVTTILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGIVSH 240
Cdd:MTH00223  174 QLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISH 253

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081 241 IISAYVGKREPFGSLGMIYAMVGIGGMGFVVWAHHMFSVGMDMDTRAYFTAATMIIAVPTGIKVFSWMATFHGSLFKIDT 320
Cdd:MTH00223  254 IVSHYSSKKEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGSKIKYEA 333

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1148359081 321 SLMWCIGFVFLFTLGGITGVVLSNSSLDIVLHDTYYVV 358
Cdd:MTH00223  334 PMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVV 371
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-358 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 589.37  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081   1 TLYLLFGVWSAMVGTAMSVLIRMELGQVGSLYGDDHLYNVIVTAHAFVMIFFMVMPILIGGFGNWLIPLMLGAPDMAFPR 80
Cdd:MTH00116   17 TLYLIFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPR 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081  81 MNNLSFWLLPPSLILLFISSMAEMGVGAGWTVYPPLAANISHPGSAMDFAIFSLHLAGASSIMGAINFITTIINMRLLGM 160
Cdd:MTH00116   97 MNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAM 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081 161 TMEKVPLFVWSVFVTTILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGIVSH 240
Cdd:MTH00116  177 SQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISH 256

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081 241 IISAYVGKREPFGSLGMIYAMVGIGGMGFVVWAHHMFSVGMDMDTRAYFTAATMIIAVPTGIKVFSWMATFHGSLFKIDT 320
Cdd:MTH00116  257 IVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSWLATLHGGTIKWDP 336

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1148359081 321 SLMWCIGFVFLFTLGGITGVVLSNSSLDIVLHDTYYVV 358
Cdd:MTH00116  337 PMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVV 374
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-358 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 581.68  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081   1 TLYLLFGVWSAMVGTAMSVLIRMELGQVGSLYGDDHLYNVIVTAHAFVMIFFMVMPILIGGFGNWLIPLMLGAPDMAFPR 80
Cdd:MTH00142   15 TLYFLFGAWAGMVGTGLSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPR 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081  81 MNNLSFWLLPPSLILLFISSMAEMGVGAGWTVYPPLAANISHPGSAMDFAIFSLHLAGASSIMGAINFITTIINMRLLGM 160
Cdd:MTH00142   95 MNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGM 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081 161 TMEKVPLFVWSVFVTTILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGIVSH 240
Cdd:MTH00142  175 KFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISH 254

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081 241 IISAYVGKREPFGSLGMIYAMVGIGGMGFVVWAHHMFSVGMDMDTRAYFTAATMIIAVPTGIKVFSWMATFHGSLFKIDT 320
Cdd:MTH00142  255 IINHYSGKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFSWLATLHGSKVKYEP 334

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1148359081 321 SLMWCIGFVFLFTLGGITGVVLSNSSLDIVLHDTYYVV 358
Cdd:MTH00142  335 PMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVV 372
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-358 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 544.04  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081   1 TLYLLFGVWSAMVGTAMSVLIRMELGQVGSLYGDDHLYNVIVTAHAFVMIFFMVMPILIGGFGNWLIPLMLGAPDMAFPR 80
Cdd:MTH00037   17 TLYLIFGAWAGMVGTAMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPR 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081  81 MNNLSFWLLPPSLILLFISSMAEMGVGAGWTVYPPLAANISHPGSAMDFAIFSLHLAGASSIMGAINFITTIINMRLLGM 160
Cdd:MTH00037   97 MNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGM 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081 161 TMEKVPLFVWSVFVTTILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGIVSH 240
Cdd:MTH00037  177 TFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISH 256

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081 241 IISAYVGKREPFGSLGMIYAMVGIGGMGFVVWAHHMFSVGMDMDTRAYFTAATMIIAVPTGIKVFSWMATFHGSLFKIDT 320
Cdd:MTH00037  257 VIAHYSGKQEPFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWMATLQGSNLRWET 336

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1148359081 321 SLMWCIGFVFLFTLGGITGVVLSNSSLDIVLHDTYYVV 358
Cdd:MTH00037  337 PLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVV 374
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-358 0e+00

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 534.87  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081   1 TLYLLFGVWSAMVGTAMSVLIRMELGQVGSLYGDDHLYNVIVTAHAFVMIFFMVMPILIGGFGNWLIPLMLGAPDMAFPR 80
Cdd:MTH00007   14 TLYFILGVWGGLLGTSMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPR 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081  81 MNNLSFWLLPPSLILLFISSMAEMGVGAGWTVYPPLAANISHPGSAMDFAIFSLHLAGASSIMGAINFITTIINMRLLGM 160
Cdd:MTH00007   94 LNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGL 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081 161 TMEKVPLFVWSVFVTTILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGIVSH 240
Cdd:MTH00007  174 RLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGAISH 253

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081 241 IISAYVGKREPFGSLGMIYAMVGIGGMGFVVWAHHMFSVGMDMDTRAYFTAATMIIAVPTGIKVFSWMATFHGSLFKIDT 320
Cdd:MTH00007  254 IVTHYAGKLEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGSPIKYET 333

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1148359081 321 SLMWCIGFVFLFTLGGITGVVLSNSSLDIVLHDTYYVV 358
Cdd:MTH00007  334 PMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVV 371
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-358 0e+00

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 530.61  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081   1 TLYLLFGVWSAMVGTAMSVLIRMELGQVGSLYGDDHLYNVIVTAHAFVMIFFMVMPILIGGFGNWLIPLMLGAPDMAFPR 80
Cdd:MTH00103   17 TLYLLFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPR 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081  81 MNNLSFWLLPPSLILLFISSMAEMGVGAGWTVYPPLAANISHPGSAMDFAIFSLHLAGASSIMGAINFITTIINMRLLGM 160
Cdd:MTH00103   97 MNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAM 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081 161 TMEKVPLFVWSVFVTTILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGIVSH 240
Cdd:MTH00103  177 SQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISH 256

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081 241 IISAYVGKREPFGSLGMIYAMVGIGGMGFVVWAHHMFSVGMDMDTRAYFTAATMIIAVPTGIKVFSWMATFHGSLFKIDT 320
Cdd:MTH00103  257 IVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGNIKWSP 336

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1148359081 321 SLMWCIGFVFLFTLGGITGVVLSNSSLDIVLHDTYYVV 358
Cdd:MTH00103  337 AMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVV 374
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-358 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 523.33  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081   1 TLYLLFGVWSAMVGTAMSVLIRMELGQVGSLYGDDHLYNVIVTAHAFVMIFFMVMPILIGGFGNWLIPLMLGAPDMAFPR 80
Cdd:MTH00183   17 TLYLVFGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPR 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081  81 MNNLSFWLLPPSLILLFISSMAEMGVGAGWTVYPPLAANISHPGSAMDFAIFSLHLAGASSIMGAINFITTIINMRLLGM 160
Cdd:MTH00183   97 MNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAI 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081 161 TMEKVPLFVWSVFVTTILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGIVSH 240
Cdd:MTH00183  177 SQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISH 256

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081 241 IISAYVGKREPFGSLGMIYAMVGIGGMGFVVWAHHMFSVGMDMDTRAYFTAATMIIAVPTGIKVFSWMATFHGSLFKIDT 320
Cdd:MTH00183  257 IVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGSIKWET 336

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1148359081 321 SLMWCIGFVFLFTLGGITGVVLSNSSLDIVLHDTYYVV 358
Cdd:MTH00183  337 PLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVV 374
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-358 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 520.27  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081   1 TLYLLFGVWSAMVGTAMSVLIRMELGQVGSLYGDDHLYNVIVTAHAFVMIFFMVMPILIGGFGNWLIPLMLGAPDMAFPR 80
Cdd:MTH00077   17 TLYLVFGAWAGMVGTALSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPR 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081  81 MNNLSFWLLPPSLILLFISSMAEMGVGAGWTVYPPLAANISHPGSAMDFAIFSLHLAGASSIMGAINFITTIINMRLLGM 160
Cdd:MTH00077   97 MNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSM 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081 161 TMEKVPLFVWSVFVTTILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGIVSH 240
Cdd:MTH00077  177 SQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISH 256

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081 241 IISAYVGKREPFGSLGMIYAMVGIGGMGFVVWAHHMFSVGMDMDTRAYFTAATMIIAVPTGIKVFSWMATFHGSLFKIDT 320
Cdd:MTH00077  257 IVTYYSAKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGAIKWDA 336

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1148359081 321 SLMWCIGFVFLFTLGGITGVVLSNSSLDIVLHDTYYVV 358
Cdd:MTH00077  337 AMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVV 374
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-358 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 514.76  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081   1 TLYLLFGVWSAMVGTAMSVLIRMELGQVGSLYGDDHLYNVIVTAHAFVMIFFMVMPILIGGFGNWLIPLMLGAPDMAFPR 80
Cdd:MTH00182   19 TLYLVFGAGAGMIGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPR 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081  81 MNNLSFWLLPPSLILLFISSMAEMGVGAGWTVYPPLAANISHPGSAMDFAIFSLHLAGASSIMGAINFITTIINMRLLGM 160
Cdd:MTH00182   99 LNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGV 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081 161 TMEKVPLFVWSVFVTTILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGIVSH 240
Cdd:MTH00182  179 TFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISQ 258

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081 241 IISAYVGKREPFGSLGMIYAMVGIGGMGFVVWAHHMFSVGMDMDTRAYFTAATMIIAVPTGIKVFSWMATFHGSLFKIDT 320
Cdd:MTH00182  259 IIPTFVAKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGGTLRLDT 338

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1148359081 321 SLMWCIGFVFLFTLGGITGVVLSNSSLDIVLHDTYYVV 358
Cdd:MTH00182  339 PMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVV 376
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-358 1.22e-177

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 503.20  E-value: 1.22e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081   1 TLYLLFGVWSAMVGTAMSVLIRMELGQVGSLYGDDHLYNVIVTAHAFVMIFFMVMPILIGGFGNWLIPLMLGAPDMAFPR 80
Cdd:MTH00184   19 TLYLLFGAFAGMIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPR 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081  81 MNNLSFWLLPPSLILLFISSMAEMGVGAGWTVYPPLAANISHPGSAMDFAIFSLHLAGASSIMGAINFITTIINMRLLGM 160
Cdd:MTH00184   99 LNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGI 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081 161 TMEKVPLFVWSVFVTTILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGIVSH 240
Cdd:MTH00184  179 TMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQ 258

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081 241 IISAYVGKREPFGSLGMIYAMVGIGGMGFVVWAHHMFSVGMDMDTRAYFTAATMIIAVPTGIKVFSWMATFHGSLFKIDT 320
Cdd:MTH00184  259 IIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATIFGGSLRLDT 338

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1148359081 321 SLMWCIGFVFLFTLGGITGVVLSNSSLDIVLHDTYYVV 358
Cdd:MTH00184  339 PMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVV 376
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-358 1.14e-176

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 500.36  E-value: 1.14e-176
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081   1 TLYLLFGVWSAMVGTAMSVLIRMELGQVGSLYGDDHLYNVIVTAHAFVMIFFMVMPILIGGFGNWLIPLMLGAPDMAFPR 80
Cdd:MTH00079   18 TLYFLFGLWSGMVGTSLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPR 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081  81 MNNLSFWLLPPSLILLFISSMAEMGVGAGWTVYPPLAaNISHPGSAMDFAIFSLHLAGASSIMGAINFITTIINMRLLGM 160
Cdd:MTH00079   98 LNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLS-TLGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSI 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081 161 TMEKVPLFVWSVFVTTILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGIVSH 240
Cdd:MTH00079  177 SLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPEVYILILPAFGIISQ 256

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081 241 IISAYVGKREPFGSLGMIYAMVGIGGMGFVVWAHHMFSVGMDMDTRAYFTAATMIIAVPTGIKVFSWMATFHGSLFKIDT 320
Cdd:MTH00079  257 STLYLTGKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMKFQP 336

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1148359081 321 SLMWCIGFVFLFTLGGITGVVLSNSSLDIVLHDTYYVV 358
Cdd:MTH00079  337 LLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVV 374
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-358 5.39e-158

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 453.70  E-value: 5.39e-158
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081   1 TLYLLFGVWSAMVGTAMSVLIRMELGQVGSLYGDDHLYNVIVTAHAFVMIFFMVMPILIGGFGNWLIPLMLGAPDMAFPR 80
Cdd:MTH00026   18 SLYLVFGALSGAIGTAFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPR 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081  81 MNNLSFWLLPPSLILLFISSMAEMGVGAGWTVYPPLAANISHPGSAMDFAIFSLHLAGASSIMGAINFITTIINMRLLGM 160
Cdd:MTH00026   98 LNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGM 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081 161 TMEKVPLFVWSVFVTTILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGIVSH 240
Cdd:MTH00026  178 TMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQ 257

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081 241 IISAYVGKREPFGSLGMIYAMVGIGGMGFVVWAHHMFSVGMDMDTRAYFTAATMIIAVPTGIKVFSWMATFHGSLFKI-- 318
Cdd:MTH00026  258 ILSLFSYKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSWLATVSGSGRNLif 337

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1148359081 319 DTSLMWCIGFVFLFTLGGITGVVLSNSSLDIVLHDTYYVV 358
Cdd:MTH00026  338 TTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVV 377
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-358 3.24e-147

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: 423.87  E-value: 3.24e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081   1 TLYLLFGVWSAMVGTAMSVLIRMELGQVGSLYGDDHLYNVIVTAHAFVMIFFMVMPILIGGFGNWLIPlMLGAPDMAFPR 80
Cdd:cd00919     6 LLYLIFAFVALLLGGLLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARDLAFPR 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081  81 MNNLSFWLLPPSLILLFISSMAEMGVGAGWTVYPPLAANISHPGSAMDFAIFSLHLAGASSIMGAINFITTIINMRLLGM 160
Cdd:cd00919    85 LNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGM 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081 161 TMEKVPLFVWSVFVTTILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGIVSH 240
Cdd:cd00919   165 TLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAFGAISE 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081 241 IISAYVGKRePFGSLGMIYAMVGIGGMGFVVWAHHMFSVGMDMDTRAYFTAATMIIAVPTGIKVFSWMATFHGSLFKIDT 320
Cdd:cd00919   245 IIPTFSGKP-LFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGRIRFDP 323

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1148359081 321 SLMWCIGFVFLFTLGGITGVVLSNSSLDIVLHDTYYVV 358
Cdd:cd00919   324 PMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVV 361
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-358 5.34e-139

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: 404.30  E-value: 5.34e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081   1 TLYLLFGVWSAMVGTAMSVLIRMELGQVGSLYGDDHLYNVIVTAHAFVMIFFMVMPILiGGFGNWLIPLMLGAPDMAFPR 80
Cdd:TIGR02891  11 ILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIPIL-AGFGNYLLPLMIGARDMAFPR 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081  81 MNNLSFWLLPPSLILLFISSMAEMGVGAGWTVYPPLAANISHPGSAMDFAIFSLHLAGASSIMGAINFITTIINMRLLGM 160
Cdd:TIGR02891  90 LNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGM 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081 161 TMEKVPLFVWSVFVTTILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGIVSH 240
Cdd:TIGR02891 170 TLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISE 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081 241 IISAYVGKRePFGSLGMIYAMVGIGGMGFVVWAHHMFSVGMDMDTRAYFTAATMIIAVPTGIKVFSWMATFHGSLFKIDT 320
Cdd:TIGR02891 250 ILPTFARKP-IFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTT 328

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1148359081 321 SLMWCIGFVFLFTLGGITGVVLSNSSLDIVLHDTYYVV 358
Cdd:TIGR02891 329 PMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVV 366
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
2-358 1.24e-137

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 401.81  E-value: 1.24e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081   2 LYLLFGVWSAMVGTAMSVLIRMELGQVGSLYGDDHLYNVIVTAHAFVMIFFMVMPIlIGGFGNWLIPLMLGAPDMAFPRM 81
Cdd:COG0843    21 MYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATPF-LAGFGNYLVPLQIGARDMAFPRL 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081  82 NNLSFWLLPPSLILLFISSMAEMGVGAGWTVYPPLAANISHPGSAMDFAIFSLHLAGASSIMGAINFITTIINMRLLGMT 161
Cdd:COG0843   100 NALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMT 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081 162 MEKVPLFVWSVFVTTILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGIVSHI 241
Cdd:COG0843   180 LMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEI 259

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081 242 ISAYVGKRePFGSLGMIYAMVGIGGMGFVVWAHHMFSVGMDMDTRAYFTAATMIIAVPTGIKVFSWMATFHGSLFKIDTS 321
Cdd:COG0843   260 IPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTP 338

                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1148359081 322 LMWCIGFVFLFTLGGITGVVLSNSSLDIVLHDTYYVV 358
Cdd:COG0843   339 MLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVV 375
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 2-358 8.98e-130

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 380.95  E-value: 8.98e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081   2 LYLLFGVWSAMVGTAMSVLIRMELGQVGSLYGDDHLYNVIVTAHAFVMIFFMVMPILIGGFGNWLIPLMLGAPDMAFPRM 81
Cdd:MTH00048   19 IYTLLGVWSGFVGLSLSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRL 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081  82 NNLSFWLLPPSLILLFISSMaeMGVGAGWTVYPPLAANISHPGSAMDFAIFSLHLAGASSIMGAINFITTIINMRLLGMT 161
Cdd:MTH00048   99 NALSAWLLVPSIVFLLLSMC--LGAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNVF 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081 162 mEKVPLFVWSVFVTTILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGIVSHI 241
Cdd:MTH00048  177 -SRTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPEVYVLILPGFGIISHI 255

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081 242 ISAYVGKREPFGSLGMIYAMVGIGGMGFVVWAHHMFSVGMDMDTRAYFTAATMIIAVPTGIKVFSWMATFHGS-LFKIDT 320
Cdd:MTH00048  256 CLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFSWLYMLLNSrVRKSDP 335

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1148359081 321 SLMWCIGFVFLFTLGGITGVVLSNSSLDIVLHDTYYVV 358
Cdd:MTH00048  336 VVWWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVV 373
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 2-358 1.22e-114

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: 341.87  E-value: 1.22e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081   2 LYLLFGVWSAMVGTAMSVLIRMELGQVGSLYGDDHLYNVIVTAHAFVMIFFMVMPILIGgFGNWLIPLMLGAPDMAFPRM 81
Cdd:cd01662    13 MYIITAFVFFLRGGVDALLMRTQLALPGNDFLSPEHYNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFPRL 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081  82 NNLSFWLLPPSLILLFISSMAEMGVGAGWTVYPPLAANISHPGSAMDFAIFSLHLAGASSIMGAINFITTIINMRLLGMT 161
Cdd:cd01662    92 NALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMT 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081 162 MEKVPLFVWSVFVTTILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGIVSHI 241
Cdd:cd01662   172 LMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYILILPAFGIFSEI 251

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081 242 ISAYVGKRePFGSLGMIYAMVGIGGMGFVVWAHHMFSVGMDMDTRAYFTAATMIIAVPTGIKVFSWMATFHGSLFKIDTS 321
Cdd:cd01662   252 VPTFSRKP-LFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLFTMWRGRIRFETP 330

                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1148359081 322 LMWCIGFVFLFTLGGITGVVLSNSSLDIVLHDTYYVV 358
Cdd:cd01662   331 MLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVV 367
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 2-358 5.28e-91

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


Pssm-ID: 459678  Cd Length: 432  Bit Score: 279.07  E-value: 5.28e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081   2 LYLLFGVWSAMVGTAMSVLIRMELGQVGSLYGDDHLYNVIVTAHAFVMIFFMVMPIlIGGFGNWLIPLMLGAPDMAFPRM 81
Cdd:pfam00115   5 LYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATPF-LFGFGNYLVPLMIGARDMAFPRL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081  82 NNLSFWLLPPSLILLFISSMaemGVGAGWTVYPPLAAnishpgsaMDFAIFSLHLAGASSIMGAINFITTIINMRLLGMT 161
Cdd:pfam00115  84 NALSFWLVVLGAVLLLASFG---GATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMT 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081 162 MeKVPLFVWSVFVTTILLLLSLPVLAGAITMLLTDRNFNtsffdpAGGGDPILFQHLFWFFGHPEVYILILPGFGIVSHI 241
Cdd:pfam00115 153 L-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYI 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081 242 ISAYVGKRePFGSLGMIYAMVGIGGMGFVVWAHHMFSVGMDMDTRAYFTAATMIIAVPTGIKVFSWMATFHGSLFKIDTS 321
Cdd:pfam00115 226 LPKFAGRP-LFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFRTT 304

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1148359081 322 -LMWCIGFVFLFTLGGITGVVLSNSSLDIVLHDTYYVV 358
Cdd:pfam00115 305 pMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVV 342
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 2-358 1.47e-75

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 245.62  E-value: 1.47e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081   2 LYLLFGVWSAMVGTAMSVLIRME-----LGQVGSLygDDHLYNVIVTAHAFVMIFFMVMPILIGgFGNWLIPLMLGAPDM 76
Cdd:PRK15017   60 MYIIVAIVMLLRGFADAIMMRSQqalasAGEAGFL--PPHHYDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDV 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081  77 AFPRMNNLSFWLLPPSLILLFISsmaeMGVG----AGWTVYPPLAANISHPGSAMDFAIFSLHLAGASSIMGAINFITTI 152
Cdd:PRK15017  137 AFPFLNNLSFWFTVVGVILVNVS----LGVGefaqTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTI 212

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081 153 INMRLLGMTMEKVPLFVWSVFVTTILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILFQHLFWFFGHPEVYILIL 232
Cdd:PRK15017  213 LKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWGHPEVYILIL 292

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081 233 PGFGIVSHIISAYVGKRePFGSLGMIYAMVGIGGMGFVVWAHHMFSVGMDMDTRAYFTAATMIIAVPTGIKVFSWMATFH 312
Cdd:PRK15017  293 PVFGVFSEIAATFSRKR-LFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVKIFNWLFTMY 371

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1148359081 313 GSLFKIDTSLMWCIGFVFLFTLGGITGVVLSNSSLDIVLHDTYYVV 358
Cdd:PRK15017  372 QGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLI 417
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
 3-358 1.45e-05

ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and some archaea which catalyze the reduction of O2 and simultaneously pump protons across the membrane. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria. The ba3 family contains oxidases that lack the conserved residues that form the D- and K-pathways in CcO and ubiquinol oxidase. Instead they contain a potential alternative K-pathway. Additional proton channels have been proposed for this family of oxidases but none have been identified definitively. For general information on the heme-copper oxidase superfamily, please see cd00919.


Pssm-ID: 238830  Cd Length: 473  Bit Score: 46.51  E-value: 1.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081   3 YLLFGVWSAMVGTAMSVLIRMELGQVGSLYGDDHLYNVIVTAHAFVMIFfmVMPIL-IGGFGNWLIPLMLGAPDMAfPRM 81
Cdd:cd01660     9 HFVVAFLALLLGGLFGLLQVLVRTGVFPLPSSGILYYQGLTLHGVLLAI--VFTTFfIMGFFYAIVARALLRSLFN-RRL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081  82 NNLSFWLLppslilLFISSMAEMGVGAG-----WTVYPPLAAnisHPGsamdFAIFSLHLAGASSIMGAINFITTIINMR 156
Cdd:cd01660    86 AWAGFWLM------VIGTVMAAVPILLGqasvlYTFYPPLQA---HPL----FYIGAALVVVGSWISGFAMFVTLWRWKK 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081 157 LlgMTMEKVPLFVWSVFVTTILLLLSLPVLAGAITMLLTDRNFNTsffdpAGGGDPILFQHLFWFFGHPEVYILILPGFG 236
Cdd:cd01660   153 A--NPGKKVPLATFMVVTTMILWLVASLGVALEVLFQLLPWSLGL-----VDTVDVLLSRTLFWWFGHPLVYFWLLPAYI 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1148359081 237 IVSHIISAYVGKR---EPFGSLGMIYAMVGIGGMGFvvwaHHMFS-VGMDMDTRAYFTAATMIIAVPTGIKVFSWMATF- 311
Cdd:cd01660   226 AWYTILPKIAGGKlfsDPLARLAFILFLLFSTPVGF----HHQFAdPGIGPGWKFIHMVLTFMVALPSLLTAFTVFASLe 301

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1148359081 312 ------HGS-LFKIDTSLMW--------CIGFVFlFTLGGITGVVLSNSSLDIVLHDTYYVV 358
Cdd:cd01660   302 iagrlrGGKgLFGWIRALPWgdpmflalFLAMLM-FIPGGAGGIINASYQLNYVVHNTAWVP 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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