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Conserved domains on  [gi|1435072317|gb|AXG50296|]
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cytochrome oxidase subunit I, partial (mitochondrion) [Thoracoplites bifurcatus]

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 ...
 2-367 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: 580.29  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317   2 LYFLLGMWAGMIGLSMSLIIRLELGMPGSLLMNDQIYNSIVTGHAFVMIFFMVMPVMIGGFGNWLIPLMLGSPDMAFPRM 81
Cdd:MTH00153   16 LYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRM 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317  82 NNMSFWLLIPSLFLLLFSGVVNVGVGTGWTVYPPLSSLMGQMGISIDLAIFSLHLAGMSSIMGAINFITTVFNMRLIGSK 161
Cdd:MTH00153   96 NNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMT 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317 162 MDQINLFIWSILITAFLLLLSLPVLAGAITMLLTDRNLNTTFFDFSGGGDPILYQHLF*****************IISHI 241
Cdd:MTH00153  176 LDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHI 255

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317 242 IFNESGKKETFGSLGMIYAMLTIGFLGFIVWAHHMFTIGMDVDTRAYFTSATMIIAVPTGIKVFSWLATFSGMKFnNLNL 321
Cdd:MTH00153  256 ISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQI-NYSP 334

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1435072317 322 GILWSMGFVFLFTLGGLTGIILANSSVDIVLHDTYYVVAHFHYVLS 367
Cdd:MTH00153  335 SLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLS 380
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 2-367 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 580.29  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317   2 LYFLLGMWAGMIGLSMSLIIRLELGMPGSLLMNDQIYNSIVTGHAFVMIFFMVMPVMIGGFGNWLIPLMLGSPDMAFPRM 81
Cdd:MTH00153   16 LYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRM 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317  82 NNMSFWLLIPSLFLLLFSGVVNVGVGTGWTVYPPLSSLMGQMGISIDLAIFSLHLAGMSSIMGAINFITTVFNMRLIGSK 161
Cdd:MTH00153   96 NNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMT 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317 162 MDQINLFIWSILITAFLLLLSLPVLAGAITMLLTDRNLNTTFFDFSGGGDPILYQHLF*****************IISHI 241
Cdd:MTH00153  176 LDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHI 255

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317 242 IFNESGKKETFGSLGMIYAMLTIGFLGFIVWAHHMFTIGMDVDTRAYFTSATMIIAVPTGIKVFSWLATFSGMKFnNLNL 321
Cdd:MTH00153  256 ISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQI-NYSP 334

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1435072317 322 GILWSMGFVFLFTLGGLTGIILANSSVDIVLHDTYYVVAHFHYVLS 367
Cdd:MTH00153  335 SLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLS 380
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-367 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: 538.22  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317   1 VLYFLLGMWAGMIGLSMSLIIRLELGMPGSLLMNDQIYNSIVTGHAFVMIFFMVMPVMIGGFGNWLIPLMLGSPDMAFPR 80
Cdd:cd01663     8 TLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPR 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317  81 MNNMSFWLLIPSLFLLLFSGVVNVGVGTGWTVYPPLSSLMGQMGISIDLAIFSLHLAGMSSIMGAINFITTVFNMRLIGS 160
Cdd:cd01663    88 LNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGM 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317 161 KMDQINLFIWSILITAFLLLLSLPVLAGAITMLLTDRNLNTTFFDFSGGGDPILYQHLF*****************IISH 240
Cdd:cd01663   168 TLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISH 247

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317 241 IIFNESGKKETFGSLGMIYAMLTIGFLGFIVWAHHMFTIGMDVDTRAYFTSATMIIAVPTGIKVFSWLATFSGMKFnNLN 320
Cdd:cd01663   248 IISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSI-KFE 326

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 1435072317 321 LGILWSMGFVFLFTLGGLTGIILANSSVDIVLHDTYYVVAHFHYVLS 367
Cdd:cd01663   327 TPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLS 373
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-366 1.79e-114

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: 341.90  E-value: 1.79e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317   1 VLYFLLGMWAGMIGLSMSLIIRLELGMPGSLLMNDQIYNSIVTGHAFVMIFFMVMPvMIGGFGNWLIPLMLGSPDMAFPR 80
Cdd:TIGR02891  11 ILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIP-ILAGFGNYLLPLMIGARDMAFPR 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317  81 MNNMSFWLLIPSLFLLLFSGVVNVGVGTGWTVYPPLSSLMGQMGISIDLAIFSLHLAGMSSIMGAINFITTVFNMRLIGS 160
Cdd:TIGR02891  90 LNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGM 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317 161 KMDQINLFIWSILITAFLLLLSLPVLAGAITMLLTDRNLNTTFFDFSGGGDPILYQHLF*****************IISH 240
Cdd:TIGR02891 170 TLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISE 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317 241 IIFNESGKKeTFGSLGMIYAMLTIGFLGFIVWAHHMFTIGMDVDTRAYFTSATMIIAVPTGIKVFSWLATFSGMKFnNLN 320
Cdd:TIGR02891 250 ILPTFARKP-IFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSI-RFT 327

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1435072317 321 LGILWSMGFVFLFTLGGLTGIILANSSVDIVLHDTYYVVAHFHYVL 366
Cdd:TIGR02891 328 TPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVL 373
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-366 4.31e-109

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 329.40  E-value: 4.31e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317   1 VLYFLLGMWAGMIGLSMSLIIRLELGMPGSLLMNDQIYNSIVTGHAFVMIFFMVMPvMIGGFGNWLIPLMLGSPDMAFPR 80
Cdd:COG0843    20 IMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPR 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317  81 MNNMSFWLLIPSLFLLLFSGVVNVGVGTGWTVYPPLSSLMGQMGISIDLAIFSLHLAGMSSIMGAINFITTVFNMRLIGS 160
Cdd:COG0843    99 LNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGM 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317 161 KMDQINLFIWSILITAFLLLLSLPVLAGAITMLLTDRNLNTTFFDFSGGGDPILYQHLF*****************IISH 240
Cdd:COG0843   179 TLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSE 258

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317 241 IIFNESGKKeTFGSLGMIYAMLTIGFLGFIVWAHHMFTIGMDVDTRAYFTSATMIIAVPTGIKVFSWLATFSGMKFnNLN 320
Cdd:COG0843   259 IIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRI-RFT 336

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1435072317 321 LGILWSMGFVFLFTLGGLTGIILANSSVDIVLHDTYYVVAHFHYVL 366
Cdd:COG0843   337 TPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVL 382
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-366 2.75e-73

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: 234.00  E-value: 2.75e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317   1 VLYFLLGMWAGMIGLSMSLIIRLELGMPGSLLMNDQIYNSIVTGHAFVMIFFMVMPvMIGGFGNWLIPLMLGSPDMAFPR 80
Cdd:pfam00115   4 LLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317  81 MNNMSFWLLIPSLFLLLFSGVVNVGVgtgWTVYPPLsslmgqmgISIDLAIFSLHLAGMSSIMGAINFITTVFNMRLIGS 160
Cdd:pfam00115  83 LNALSFWLVVLGAVLLLASFGGATTG---WTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGM 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317 161 KMdQINLFIWSILITAFLLLLSLPVLAGAITMLLTDRNLNTtffdfsGGGDPILYQHLF*****************IISH 240
Cdd:pfam00115 152 TL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLGA------GGGDPLLDQHLFWWFGHPEVYILILPAFGIIYY 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317 241 IIFNESGKKeTFGSLGMIYAMLTIGFLGFIVWAHHMFTIGMDVDTRAYFTSATMIIAVPTGIKVFSWLATFSGMKFNNLN 320
Cdd:pfam00115 225 ILPKFAGRP-LFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFRT 303

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1435072317 321 LGILWSMGFVFLFTLGGLTGIILANSSVDIVLHDTYYVVAHFHYVL 366
Cdd:pfam00115 304 TPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVL 349
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 2-367 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 580.29  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317   2 LYFLLGMWAGMIGLSMSLIIRLELGMPGSLLMNDQIYNSIVTGHAFVMIFFMVMPVMIGGFGNWLIPLMLGSPDMAFPRM 81
Cdd:MTH00153   16 LYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRM 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317  82 NNMSFWLLIPSLFLLLFSGVVNVGVGTGWTVYPPLSSLMGQMGISIDLAIFSLHLAGMSSIMGAINFITTVFNMRLIGSK 161
Cdd:MTH00153   96 NNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMT 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317 162 MDQINLFIWSILITAFLLLLSLPVLAGAITMLLTDRNLNTTFFDFSGGGDPILYQHLF*****************IISHI 241
Cdd:MTH00153  176 LDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHI 255

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317 242 IFNESGKKETFGSLGMIYAMLTIGFLGFIVWAHHMFTIGMDVDTRAYFTSATMIIAVPTGIKVFSWLATFSGMKFnNLNL 321
Cdd:MTH00153  256 ISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQI-NYSP 334

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1435072317 322 GILWSMGFVFLFTLGGLTGIILANSSVDIVLHDTYYVVAHFHYVLS 367
Cdd:MTH00153  335 SLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLS 380
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-367 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: 538.22  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317   1 VLYFLLGMWAGMIGLSMSLIIRLELGMPGSLLMNDQIYNSIVTGHAFVMIFFMVMPVMIGGFGNWLIPLMLGSPDMAFPR 80
Cdd:cd01663     8 TLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPR 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317  81 MNNMSFWLLIPSLFLLLFSGVVNVGVGTGWTVYPPLSSLMGQMGISIDLAIFSLHLAGMSSIMGAINFITTVFNMRLIGS 160
Cdd:cd01663    88 LNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGM 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317 161 KMDQINLFIWSILITAFLLLLSLPVLAGAITMLLTDRNLNTTFFDFSGGGDPILYQHLF*****************IISH 240
Cdd:cd01663   168 TLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISH 247

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317 241 IIFNESGKKETFGSLGMIYAMLTIGFLGFIVWAHHMFTIGMDVDTRAYFTSATMIIAVPTGIKVFSWLATFSGMKFnNLN 320
Cdd:cd01663   248 IISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSI-KFE 326

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 1435072317 321 LGILWSMGFVFLFTLGGLTGIILANSSVDIVLHDTYYVVAHFHYVLS 367
Cdd:cd01663   327 TPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLS 373
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 2-367 4.51e-178

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 504.21  E-value: 4.51e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317   2 LYFLLGMWAGMIGLSMSLIIRLELGMPGSLLMNDQIYNSIVTGHAFVMIFFMVMPVMIGGFGNWLIPLMLGSPDMAFPRM 81
Cdd:MTH00167   18 LYFIFGAWAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRM 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317  82 NNMSFWLLIPSLFLLLFSGVVNVGVGTGWTVYPPLSSLMGQMGISIDLAIFSLHLAGMSSIMGAINFITTVFNMRLIGSK 161
Cdd:MTH00167   98 NNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGIT 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317 162 MDQINLFIWSILITAFLLLLSLPVLAGAITMLLTDRNLNTTFFDFSGGGDPILYQHLF*****************IISHI 241
Cdd:MTH00167  178 QYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHI 257

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317 242 IFNESGKKETFGSLGMIYAMLTIGFLGFIVWAHHMFTIGMDVDTRAYFTSATMIIAVPTGIKVFSWLATFSGMKFnNLNL 321
Cdd:MTH00167  258 VVYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLHGGKI-KWET 336

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1435072317 322 GILWSMGFVFLFTLGGLTGIILANSSVDIVLHDTYYVVAHFHYVLS 367
Cdd:MTH00167  337 PMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLS 382
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 2-367 4.58e-178

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 504.51  E-value: 4.58e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317   2 LYFLLGMWAGMIGLSMSLIIRLELGMPGSLLMNDQIYNSIVTGHAFVMIFFMVMPVMIGGFGNWLIPLMLGSPDMAFPRM 81
Cdd:MTH00223   15 LYLIFGMWSGLVGTSLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRL 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317  82 NNMSFWLLIPSLFLLLFSGVVNVGVGTGWTVYPPLSSLMGQMGISIDLAIFSLHLAGMSSIMGAINFITTVFNMRLIGSK 161
Cdd:MTH00223   95 NNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQ 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317 162 MDQINLFIWSILITAFLLLLSLPVLAGAITMLLTDRNLNTTFFDFSGGGDPILYQHLF*****************IISHI 241
Cdd:MTH00223  175 LERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHI 254

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317 242 IFNESGKKETFGSLGMIYAMLTIGFLGFIVWAHHMFTIGMDVDTRAYFTSATMIIAVPTGIKVFSWLATFSGMKFNNlNL 321
Cdd:MTH00223  255 VSHYSSKKEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGSKIKY-EA 333

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1435072317 322 GILWSMGFVFLFTLGGLTGIILANSSVDIVLHDTYYVVAHFHYVLS 367
Cdd:MTH00223  334 PMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLS 379
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 2-367 4.80e-174

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 494.23  E-value: 4.80e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317   2 LYFLLGMWAGMIGLSMSLIIRLELGMPGSLLMNDQIYNSIVTGHAFVMIFFMVMPVMIGGFGNWLIPLMLGSPDMAFPRM 81
Cdd:MTH00116   18 LYLIFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRM 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317  82 NNMSFWLLIPSLFLLLFSGVVNVGVGTGWTVYPPLSSLMGQMGISIDLAIFSLHLAGMSSIMGAINFITTVFNMRLIGSK 161
Cdd:MTH00116   98 NNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMS 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317 162 MDQINLFIWSILITAFLLLLSLPVLAGAITMLLTDRNLNTTFFDFSGGGDPILYQHLF*****************IISHI 241
Cdd:MTH00116  178 QYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHI 257

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317 242 IFNESGKKETFGSLGMIYAMLTIGFLGFIVWAHHMFTIGMDVDTRAYFTSATMIIAVPTGIKVFSWLATFSGMKFnNLNL 321
Cdd:MTH00116  258 VTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSWLATLHGGTI-KWDP 336

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1435072317 322 GILWSMGFVFLFTLGGLTGIILANSSVDIVLHDTYYVVAHFHYVLS 367
Cdd:MTH00116  337 PMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLS 382
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 2-367 1.83e-171

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 487.69  E-value: 1.83e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317   2 LYFLLGMWAGMIGLSMSLIIRLELGMPGSLLMNDQIYNSIVTGHAFVMIFFMVMPVMIGGFGNWLIPLMLGSPDMAFPRM 81
Cdd:MTH00142   16 LYFLFGAWAGMVGTGLSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPRM 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317  82 NNMSFWLLIPSLFLLLFSGVVNVGVGTGWTVYPPLSSLMGQMGISIDLAIFSLHLAGMSSIMGAINFITTVFNMRLIGSK 161
Cdd:MTH00142   96 NNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMK 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317 162 MDQINLFIWSILITAFLLLLSLPVLAGAITMLLTDRNLNTTFFDFSGGGDPILYQHLF*****************IISHI 241
Cdd:MTH00142  176 FERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHI 255

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317 242 IFNESGKKETFGSLGMIYAMLTIGFLGFIVWAHHMFTIGMDVDTRAYFTSATMIIAVPTGIKVFSWLATFSGMKFnNLNL 321
Cdd:MTH00142  256 INHYSGKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFSWLATLHGSKV-KYEP 334

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1435072317 322 GILWSMGFVFLFTLGGLTGIILANSSVDIVLHDTYYVVAHFHYVLS 367
Cdd:MTH00142  335 PMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLS 380
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 2-367 1.89e-157

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 452.36  E-value: 1.89e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317   2 LYFLLGMWAGMIGLSMSLIIRLELGMPGSLLMNDQIYNSIVTGHAFVMIFFMVMPVMIGGFGNWLIPLMLGSPDMAFPRM 81
Cdd:MTH00037   18 LYLIFGAWAGMVGTAMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRM 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317  82 NNMSFWLLIPSLFLLLFSGVVNVGVGTGWTVYPPLSSLMGQMGISIDLAIFSLHLAGMSSIMGAINFITTVFNMRLIGSK 161
Cdd:MTH00037   98 NNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMT 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317 162 MDQINLFIWSILITAFLLLLSLPVLAGAITMLLTDRNLNTTFFDFSGGGDPILYQHLF*****************IISHI 241
Cdd:MTH00037  178 FDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHV 257

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317 242 IFNESGKKETFGSLGMIYAMLTIGFLGFIVWAHHMFTIGMDVDTRAYFTSATMIIAVPTGIKVFSWLATFSGMKFnNLNL 321
Cdd:MTH00037  258 IAHYSGKQEPFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWMATLQGSNL-RWET 336

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1435072317 322 GILWSMGFVFLFTLGGLTGIILANSSVDIVLHDTYYVVAHFHYVLS 367
Cdd:MTH00037  337 PLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLS 382
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 2-367 3.12e-157

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 451.28  E-value: 3.12e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317   2 LYFLLGMWAGMIGLSMSLIIRLELGMPGSLLMNDQIYNSIVTGHAFVMIFFMVMPVMIGGFGNWLIPLMLGSPDMAFPRM 81
Cdd:MTH00007   15 LYFILGVWGGLLGTSMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPRL 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317  82 NNMSFWLLIPSLFLLLFSGVVNVGVGTGWTVYPPLSSLMGQMGISIDLAIFSLHLAGMSSIMGAINFITTVFNMRLIGSK 161
Cdd:MTH00007   95 NNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLR 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317 162 MDQINLFIWSILITAFLLLLSLPVLAGAITMLLTDRNLNTTFFDFSGGGDPILYQHLF*****************IISHI 241
Cdd:MTH00007  175 LERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGAISHI 254

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317 242 IFNESGKKETFGSLGMIYAMLTIGFLGFIVWAHHMFTIGMDVDTRAYFTSATMIIAVPTGIKVFSWLATFSGMKFnNLNL 321
Cdd:MTH00007  255 VTHYAGKLEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGSPI-KYET 333

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1435072317 322 GILWSMGFVFLFTLGGLTGIILANSSVDIVLHDTYYVVAHFHYVLS 367
Cdd:MTH00007  334 PMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLS 379
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 2-367 1.42e-154

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 444.75  E-value: 1.42e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317   2 LYFLLGMWAGMIGLSMSLIIRLELGMPGSLLMNDQIYNSIVTGHAFVMIFFMVMPVMIGGFGNWLIPLMLGSPDMAFPRM 81
Cdd:MTH00183   18 LYLVFGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRM 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317  82 NNMSFWLLIPSLFLLLFSGVVNVGVGTGWTVYPPLSSLMGQMGISIDLAIFSLHLAGMSSIMGAINFITTVFNMRLIGSK 161
Cdd:MTH00183   98 NNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAIS 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317 162 MDQINLFIWSILITAFLLLLSLPVLAGAITMLLTDRNLNTTFFDFSGGGDPILYQHLF*****************IISHI 241
Cdd:MTH00183  178 QYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHI 257

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317 242 IFNESGKKETFGSLGMIYAMLTIGFLGFIVWAHHMFTIGMDVDTRAYFTSATMIIAVPTGIKVFSWLATFSGMKFnNLNL 321
Cdd:MTH00183  258 VAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGSI-KWET 336

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1435072317 322 GILWSMGFVFLFTLGGLTGIILANSSVDIVLHDTYYVVAHFHYVLS 367
Cdd:MTH00183  337 PLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLS 382
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 2-367 3.14e-154

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 443.94  E-value: 3.14e-154
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317   2 LYFLLGMWAGMIGLSMSLIIRLELGMPGSLLMNDQIYNSIVTGHAFVMIFFMVMPVMIGGFGNWLIPLMLGSPDMAFPRM 81
Cdd:MTH00103   18 LYLLFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRM 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317  82 NNMSFWLLIPSLFLLLFSGVVNVGVGTGWTVYPPLSSLMGQMGISIDLAIFSLHLAGMSSIMGAINFITTVFNMRLIGSK 161
Cdd:MTH00103   98 NNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMS 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317 162 MDQINLFIWSILITAFLLLLSLPVLAGAITMLLTDRNLNTTFFDFSGGGDPILYQHLF*****************IISHI 241
Cdd:MTH00103  178 QYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHI 257

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317 242 IFNESGKKETFGSLGMIYAMLTIGFLGFIVWAHHMFTIGMDVDTRAYFTSATMIIAVPTGIKVFSWLATFSGMKFnNLNL 321
Cdd:MTH00103  258 VTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGNI-KWSP 336

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1435072317 322 GILWSMGFVFLFTLGGLTGIILANSSVDIVLHDTYYVVAHFHYVLS 367
Cdd:MTH00103  337 AMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLS 382
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 2-367 7.11e-151

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 435.52  E-value: 7.11e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317   2 LYFLLGMWAGMIGLSMSLIIRLELGMPGSLLMNDQIYNSIVTGHAFVMIFFMVMPVMIGGFGNWLIPLMLGSPDMAFPRM 81
Cdd:MTH00077   18 LYLVFGAWAGMVGTALSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRM 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317  82 NNMSFWLLIPSLFLLLFSGVVNVGVGTGWTVYPPLSSLMGQMGISIDLAIFSLHLAGMSSIMGAINFITTVFNMRLIGSK 161
Cdd:MTH00077   98 NNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMS 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317 162 MDQINLFIWSILITAFLLLLSLPVLAGAITMLLTDRNLNTTFFDFSGGGDPILYQHLF*****************IISHI 241
Cdd:MTH00077  178 QYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISHI 257

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317 242 IFNESGKKETFGSLGMIYAMLTIGFLGFIVWAHHMFTIGMDVDTRAYFTSATMIIAVPTGIKVFSWLATFSGMKFnNLNL 321
Cdd:MTH00077  258 VTYYSAKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGAI-KWDA 336

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1435072317 322 GILWSMGFVFLFTLGGLTGIILANSSVDIVLHDTYYVVAHFHYVLS 367
Cdd:MTH00077  337 AMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLS 382
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 2-367 7.21e-150

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 432.57  E-value: 7.21e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317   2 LYFLLGMWAGMIGLSMSLIIRLELGMPGSLLMNDQIYNSIVTGHAFVMIFFMVMPVMIGGFGNWLIPLMLGSPDMAFPRM 81
Cdd:MTH00079   19 LYFLFGLWSGMVGTSLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPRL 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317  82 NNMSFWLLIPSLFLLLFSGVVNVGVGTGWTVYPPLSSlMGQMGISIDLAIFSLHLAGMSSIMGAINFITTVFNMRLIGSK 161
Cdd:MTH00079   99 NNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLST-LGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSIS 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317 162 MDQINLFIWSILITAFLLLLSLPVLAGAITMLLTDRNLNTTFFDFSGGGDPILYQHLF*****************IISHI 241
Cdd:MTH00079  178 LEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPEVYILILPAFGIISQS 257

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317 242 IFNESGKKETFGSLGMIYAMLTIGFLGFIVWAHHMFTIGMDVDTRAYFTSATMIIAVPTGIKVFSWLATFSGMKFNNLNL 321
Cdd:MTH00079  258 TLYLTGKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMKFQPL 337

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1435072317 322 gILWSMGFVFLFTLGGLTGIILANSSVDIVLHDTYYVVAHFHYVLS 367
Cdd:MTH00079  338 -LLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLS 382
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 2-367 7.63e-149

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 430.40  E-value: 7.63e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317   2 LYFLLGMWAGMIGLSMSLIIRLELGMPGSLLMNDQIYNSIVTGHAFVMIFFMVMPVMIGGFGNWLIPLMLGSPDMAFPRM 81
Cdd:MTH00182   20 LYLVFGAGAGMIGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRL 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317  82 NNMSFWLLIPSLFLLLFSGVVNVGVGTGWTVYPPLSSLMGQMGISIDLAIFSLHLAGMSSIMGAINFITTVFNMRLIGSK 161
Cdd:MTH00182  100 NNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVT 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317 162 MDQINLFIWSILITAFLLLLSLPVLAGAITMLLTDRNLNTTFFDFSGGGDPILYQHLF*****************IISHI 241
Cdd:MTH00182  180 FNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISQI 259

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317 242 IFNESGKKETFGSLGMIYAMLTIGFLGFIVWAHHMFTIGMDVDTRAYFTSATMIIAVPTGIKVFSWLATFSGMKFnNLNL 321
Cdd:MTH00182  260 IPTFVAKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGGTL-RLDT 338

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1435072317 322 GILWSMGFVFLFTLGGLTGIILANSSVDIVLHDTYYVVAHFHYVLS 367
Cdd:MTH00182  339 PMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLS 384
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 2-367 8.09e-148

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 427.71  E-value: 8.09e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317   2 LYFLLGMWAGMIGLSMSLIIRLELGMPGSLLMNDQIYNSIVTGHAFVMIFFMVMPVMIGGFGNWLIPLMLGSPDMAFPRM 81
Cdd:MTH00184   20 LYLLFGAFAGMIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPRL 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317  82 NNMSFWLLIPSLFLLLFSGVVNVGVGTGWTVYPPLSSLMGQMGISIDLAIFSLHLAGMSSIMGAINFITTVFNMRLIGSK 161
Cdd:MTH00184  100 NNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGIT 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317 162 MDQINLFIWSILITAFLLLLSLPVLAGAITMLLTDRNLNTTFFDFSGGGDPILYQHLF*****************IISHI 241
Cdd:MTH00184  180 MDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQI 259

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317 242 IFNESGKKETFGSLGMIYAMLTIGFLGFIVWAHHMFTIGMDVDTRAYFTSATMIIAVPTGIKVFSWLATFSGMKFnNLNL 321
Cdd:MTH00184  260 IPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATIFGGSL-RLDT 338

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1435072317 322 GILWSMGFVFLFTLGGLTGIILANSSVDIVLHDTYYVVAHFHYVLS 367
Cdd:MTH00184  339 PMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLS 384
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 2-367 8.75e-130

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 382.44  E-value: 8.75e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317   2 LYFLLGMWAGMIGLSMSLIIRLELGMPGSLLMNDQIYNSIVTGHAFVMIFFMVMPVMIGGFGNWLIPLMLGSPDMAFPRM 81
Cdd:MTH00026   19 LYLVFGALSGAIGTAFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPRL 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317  82 NNMSFWLLIPSLFLLLFSGVVNVGVGTGWTVYPPLSSLMGQMGISIDLAIFSLHLAGMSSIMGAINFITTVFNMRLIGSK 161
Cdd:MTH00026   99 NNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMT 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317 162 MDQINLFIWSILITAFLLLLSLPVLAGAITMLLTDRNLNTTFFDFSGGGDPILYQHLF*****************IISHI 241
Cdd:MTH00026  179 MSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQI 258

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317 242 IFNESGKKETFGSLGMIYAMLTIGFLGFIVWAHHMFTIGMDVDTRAYFTSATMIIAVPTGIKVFSWLATFSGMKFNNL-N 320
Cdd:MTH00026  259 LSLFSYKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSWLATVSGSGRNLIfT 338

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 1435072317 321 LGILWSMGFVFLFTLGGLTGIILANSSVDIVLHDTYYVVAHFHYVLS 367
Cdd:MTH00026  339 TPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLS 385
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-367 4.09e-119

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: 352.60  E-value: 4.09e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317   1 VLYFLLGMWAGMIGLSMSLIIRLELGMPGSLLMNDQIYNSIVTGHAFVMIFFMVMPVMIGGFGNWLIPlMLGSPDMAFPR 80
Cdd:cd00919     6 LLYLIFAFVALLLGGLLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARDLAFPR 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317  81 MNNMSFWLLIPSLFLLLFSGVVNVGVGTGWTVYPPLSSLMGQMGISIDLAIFSLHLAGMSSIMGAINFITTVFNMRLIGS 160
Cdd:cd00919    85 LNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGM 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317 161 KMDQINLFIWSILITAFLLLLSLPVLAGAITMLLTDRNLNTTFFDFSGGGDPILYQHLF*****************IISH 240
Cdd:cd00919   165 TLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAFGAISE 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317 241 IIFNESGKKeTFGSLGMIYAMLTIGFLGFIVWAHHMFTIGMDVDTRAYFTSATMIIAVPTGIKVFSWLATFSGMKFnNLN 320
Cdd:cd00919   245 IIPTFSGKP-LFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGRI-RFD 322

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 1435072317 321 LGILWSMGFVFLFTLGGLTGIILANSSVDIVLHDTYYVVAHFHYVLS 367
Cdd:cd00919   323 PPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLS 369
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-366 1.79e-114

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: 341.90  E-value: 1.79e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317   1 VLYFLLGMWAGMIGLSMSLIIRLELGMPGSLLMNDQIYNSIVTGHAFVMIFFMVMPvMIGGFGNWLIPLMLGSPDMAFPR 80
Cdd:TIGR02891  11 ILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIP-ILAGFGNYLLPLMIGARDMAFPR 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317  81 MNNMSFWLLIPSLFLLLFSGVVNVGVGTGWTVYPPLSSLMGQMGISIDLAIFSLHLAGMSSIMGAINFITTVFNMRLIGS 160
Cdd:TIGR02891  90 LNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGM 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317 161 KMDQINLFIWSILITAFLLLLSLPVLAGAITMLLTDRNLNTTFFDFSGGGDPILYQHLF*****************IISH 240
Cdd:TIGR02891 170 TLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISE 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317 241 IIFNESGKKeTFGSLGMIYAMLTIGFLGFIVWAHHMFTIGMDVDTRAYFTSATMIIAVPTGIKVFSWLATFSGMKFnNLN 320
Cdd:TIGR02891 250 ILPTFARKP-IFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSI-RFT 327

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1435072317 321 LGILWSMGFVFLFTLGGLTGIILANSSVDIVLHDTYYVVAHFHYVL 366
Cdd:TIGR02891 328 TPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVL 373
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-366 4.31e-109

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 329.40  E-value: 4.31e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317   1 VLYFLLGMWAGMIGLSMSLIIRLELGMPGSLLMNDQIYNSIVTGHAFVMIFFMVMPvMIGGFGNWLIPLMLGSPDMAFPR 80
Cdd:COG0843    20 IMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPR 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317  81 MNNMSFWLLIPSLFLLLFSGVVNVGVGTGWTVYPPLSSLMGQMGISIDLAIFSLHLAGMSSIMGAINFITTVFNMRLIGS 160
Cdd:COG0843    99 LNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGM 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317 161 KMDQINLFIWSILITAFLLLLSLPVLAGAITMLLTDRNLNTTFFDFSGGGDPILYQHLF*****************IISH 240
Cdd:COG0843   179 TLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSE 258

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317 241 IIFNESGKKeTFGSLGMIYAMLTIGFLGFIVWAHHMFTIGMDVDTRAYFTSATMIIAVPTGIKVFSWLATFSGMKFnNLN 320
Cdd:COG0843   259 IIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRI-RFT 336

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1435072317 321 LGILWSMGFVFLFTLGGLTGIILANSSVDIVLHDTYYVVAHFHYVL 366
Cdd:COG0843   337 TPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVL 382
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 1-367 1.76e-108

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 327.02  E-value: 1.76e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317   1 VLYFLLGMWAGMIGLSMSLIIRLELGMPGSLLMNDQIYNSIVTGHAFVMIFFMVMPVMIGGFGNWLIPLMLGSPDMAFPR 80
Cdd:MTH00048   18 VIYTLLGVWSGFVGLSLSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPR 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317  81 MNNMSFWLLIPSLFLLLFSGVVNVGVGtgWTVYPPLSSLMGQMGISIDLAIFSLHLAGMSSIMGAINFITTVFNMrLIGS 160
Cdd:MTH00048   98 LNALSAWLLVPSIVFLLLSMCLGAGVG--WTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSA-FMTN 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317 161 KMDQINLFIWSILITAFLLLLSLPVLAGAITMLLTDRNLNTTFFDFSGGGDPILYQHLF*****************IISH 240
Cdd:MTH00048  175 VFSRTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPEVYVLILPGFGIISH 254

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317 241 IIFNESGKKETFGSLGMIYAMLTIGFLGFIVWAHHMFTIGMDVDTRAYFTSATMIIAVPTGIKVFSWLATFSGMKFNNLN 320
Cdd:MTH00048  255 ICLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFSWLYMLLNSRVRKSD 334

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 1435072317 321 LGILWSMGFVFLFTLGGLTGIILANSSVDIVLHDTYYVVAHFHYVLS 367
Cdd:MTH00048  335 PVVWWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLS 381
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 1-366 3.21e-92

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: 284.86  E-value: 3.21e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317   1 VLYFLLGMWAGMIGLSMSLIIRLELGMPGSLLMNDQIYNSIVTGHAFVMIFFMVMPVMIGgFGNWLIPLMLGSPDMAFPR 80
Cdd:cd01662    12 IMYIITAFVFFLRGGVDALLMRTQLALPGNDFLSPEHYNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFPR 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317  81 MNNMSFWLLIPSLFLLLFSGVVNVGVGTGWTVYPPLSSLMGQMGISIDLAIFSLHLAGMSSIMGAINFITTVFNMRLIGS 160
Cdd:cd01662    91 LNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGM 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317 161 KMDQINLFIWSILITAFLLLLSLPVLAGAITMLLTDRNLNTTFFDFSGGGDPILYQHLF*****************IISH 240
Cdd:cd01662   171 TLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYILILPAFGIFSE 250

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317 241 IIFNESGKKeTFGSLGMIYAMLTIGFLGFIVWAHHMFTIGMDVDTRAYFTSATMIIAVPTGIKVFSWLATFSGMKFnNLN 320
Cdd:cd01662   251 IVPTFSRKP-LFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLFTMWRGRI-RFE 328

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1435072317 321 LGILWSMGFVFLFTLGGLTGIILANSSVDIVLHDTYYVVAHFHYVL 366
Cdd:cd01662   329 TPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVL 374
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-366 2.75e-73

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: 234.00  E-value: 2.75e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317   1 VLYFLLGMWAGMIGLSMSLIIRLELGMPGSLLMNDQIYNSIVTGHAFVMIFFMVMPvMIGGFGNWLIPLMLGSPDMAFPR 80
Cdd:pfam00115   4 LLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317  81 MNNMSFWLLIPSLFLLLFSGVVNVGVgtgWTVYPPLsslmgqmgISIDLAIFSLHLAGMSSIMGAINFITTVFNMRLIGS 160
Cdd:pfam00115  83 LNALSFWLVVLGAVLLLASFGGATTG---WTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGM 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317 161 KMdQINLFIWSILITAFLLLLSLPVLAGAITMLLTDRNLNTtffdfsGGGDPILYQHLF*****************IISH 240
Cdd:pfam00115 152 TL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLGA------GGGDPLLDQHLFWWFGHPEVYILILPAFGIIYY 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317 241 IIFNESGKKeTFGSLGMIYAMLTIGFLGFIVWAHHMFTIGMDVDTRAYFTSATMIIAVPTGIKVFSWLATFSGMKFNNLN 320
Cdd:pfam00115 225 ILPKFAGRP-LFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFRT 303

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1435072317 321 LGILWSMGFVFLFTLGGLTGIILANSSVDIVLHDTYYVVAHFHYVL 366
Cdd:pfam00115 304 TPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVL 349
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 18-366 1.17e-59

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: 203.55  E-value: 1.17e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317  18 SLIIRLELGMPGSLLMNDQIYNSIVTGHAFVMIFFMVMPVMIGgFGNWLIPLMLGSPDMAFPRMNNMSFWLLIPSLFLLL 97
Cdd:TIGR02882  72 ALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFN 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317  98 FSGVVNVGVGTGWTVYPPLSSLMGQMGISIDLAIFSLHLAGMSSIMGAINFITTVFNMRLIGSKMDQINLFIWSILITAF 177
Cdd:TIGR02882 151 ISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTL 230

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317 178 LLLLSLPVLAGAITMLLTDRNLNTTFFDFSGGGDPILYQHLF*****************IISHIIFNESgKKETFGSLGM 257
Cdd:TIGR02882 231 IIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLFWIWGHPEVYIVILPAFGIYSEIISTFA-QKRLFGYKSM 309

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317 258 IYAMLTIGFLGFIVWAHHMFTIGMDVDTRAYFTSATMIIAVPTGIKVFSWLATFSGMKFnNLNLGILWSMGFVFLFTLGG 337
Cdd:TIGR02882 310 VWSTVGIAFLSFLVWVHHFFTMGNGALINSFFSITTMAIAIPTGVKIFNWLLTLYKGKI-RFTTPMLFSLAFIPNFLIGG 388

                         330       340
                  ....*....|....*....|....*....
gi 1435072317 338 LTGIILANSSVDIVLHDTYYVVAHFHYVL 366
Cdd:TIGR02882 389 VTGVMLAMASADYQYHNTYFLVAHFHYVL 417
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 38-366 8.57e-58

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 198.62  E-value: 8.57e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317  38 YNSIVTGHAFVMIFFMVMPVMIGgFGNWLIPLMLGSPDMAFPRMNNMSFWLLIPSLFLLLFSGVVNVGVGTGWTVYPPLS 117
Cdd:PRK15017   99 YDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLS 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317 118 SLMGQMGISIDLAIFSLHLAGMSSIMGAINFITTVFNMRLIGSKMDQINLFIWSILITAFLLLLSLPVLAGAITMLLTDR 197
Cdd:PRK15017  178 GIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDR 257

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317 198 NLNTTFFDFSGGGDPILYQHLF*****************IISHIIFNESgKKETFGSLGMIYAMLTIGFLGFIVWAHHMF 277
Cdd:PRK15017  258 YLGTHFFTNDMGGNMMMYINLIWAWGHPEVYILILPVFGVFSEIAATFS-RKRLFGYTSLVWATVCITVLSFIVWLHHFF 336

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1435072317 278 TIGMDVDTRAYFTSATMIIAVPTGIKVFSWLATFSGMKFnNLNLGILWSMGFVFLFTLGGLTGIILANSSVDIVLHDTYY 357
Cdd:PRK15017  337 TMGAGANVNAFFGITTMIIAIPTGVKIFNWLFTMYQGRI-VFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLF 415


                  ....*....
gi 1435072317 358 VVAHFHYVL 366
Cdd:PRK15017  416 LIAHFHNVI 424
 
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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