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Conserved domains on  [gi|1822240077|gb|QIN89944|]
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cytochrome c oxidase subunit I, partial (mitochondrion) [Neopetrosia sp. UPDM SZN-HL100]

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 ...
 1-337 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 cd01663:

Pssm-ID: 469701  Cd Length: 488  Bit Score: 627.97  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077   1 IGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFWLLPPA 80
Cdd:cd01663    20 VGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPS 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077  81 LTLLLGSAFVEQGAGTGWTVYPPLSSIQTHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGMTMDRIPLFVWSV 160
Cdd:cd01663   100 LLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSV 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077 161 LVTAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISQIIPTFAAKKQIF 240
Cdd:cd01663   180 LITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSGKKPVF 259

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077 241 GYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWVATIFGGSLRLDTPMLWAVGFVFLF 320
Cdd:cd01663   260 GYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPMLWALGFIFLF 339

                         330
                  ....*....|....*..
gi 1822240077 321 TIGGLTGIVLANSSLDV 337
Cdd:cd01663   340 TIGGLTGVVLANSSLDI 356
 
Name Accession Description Interval E-value
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-337 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: 627.97  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077   1 IGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFWLLPPA 80
Cdd:cd01663    20 VGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPS 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077  81 LTLLLGSAFVEQGAGTGWTVYPPLSSIQTHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGMTMDRIPLFVWSV 160
Cdd:cd01663   100 LLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSV 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077 161 LVTAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISQIIPTFAAKKQIF 240
Cdd:cd01663   180 LITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSGKKPVF 259

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077 241 GYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWVATIFGGSLRLDTPMLWAVGFVFLF 320
Cdd:cd01663   260 GYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPMLWALGFIFLF 339

                         330
                  ....*....|....*..
gi 1822240077 321 TIGGLTGIVLANSSLDV 337
Cdd:cd01663   340 TIGGLTGVVLANSSLDI 356
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-337 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 614.95  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077   1 IGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFWLLPPA 80
Cdd:MTH00153   27 VGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPS 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077  81 LTLLLGSAFVEQGAGTGWTVYPPLSSIQTHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGMTMDRIPLFVWSV 160
Cdd:MTH00153  107 LTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSV 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077 161 LVTAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISQIIPTFAAKKQIF 240
Cdd:MTH00153  187 LITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETF 266

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077 241 GYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWVATIFGGSLRLDTPMLWAVGFVFLF 320
Cdd:MTH00153  267 GTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLF 346

                         330
                  ....*....|....*..
gi 1822240077 321 TIGGLTGIVLANSSLDV 337
Cdd:MTH00153  347 TIGGLTGVVLANSSIDI 363
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-337 3.96e-149

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: 428.95  E-value: 3.96e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077   1 IGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFVMIFFLVMPvMIGGFGNWLVPLYIGAPDMAFPRLNNISFWLLPPA 80
Cdd:TIGR02891  23 VGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIP-ILAGFGNYLLPLMIGARDMAFPRLNAFSYWLYLFG 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077  81 LTLLLGSAFVEQGAGTGWTVYPPLSSIQTHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGMTMDRIPLFVWSV 160
Cdd:TIGR02891 102 GLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLFVWGI 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077 161 LVTAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISQIIPTFaAKKQIF 240
Cdd:TIGR02891 182 LVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTF-ARKPIF 260

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077 241 GYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWVATIFGGSLRLDTPMLWAVGFVFLF 320
Cdd:TIGR02891 261 GYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLFALGFIFLF 340

                         330
                  ....*....|....*..
gi 1822240077 321 TIGGLTGIVLANSSLDV 337
Cdd:TIGR02891 341 VIGGLTGVMLASVPLDW 357
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-337 1.18e-145

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 421.46  E-value: 1.18e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077   1 IGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFVMIFFLVMPvMIGGFGNWLVPLYIGAPDMAFPRLNNISFWLLPPA 80
Cdd:COG0843    32 IGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFG 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077  81 LTLLLGSAFVEQGAGTGWTVYPPLSSIQTHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGMTMDRIPLFVWSV 160
Cdd:COG0843   111 GLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAA 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077 161 LVTAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISQIIPTFAAKKqIF 240
Cdd:COG0843   191 LVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFSRKP-LF 269

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077 241 GYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWVATIFGGSLRLDTPMLWAVGFVFLF 320
Cdd:COG0843   270 GYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLFALGFIILF 349

                         330
                  ....*....|....*..
gi 1822240077 321 TIGGLTGIVLANSSLDV 337
Cdd:COG0843   350 VIGGLTGVMLASVPLDY 366
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-337 9.37e-94

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: 285.62  E-value: 9.37e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077   1 IGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFVMIFFLVMPvMIGGFGNWLVPLYIGAPDMAFPRLNNISFWLLPPA 80
Cdd:pfam00115  16 VGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALSFWLVVLG 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077  81 LTLLLGSAfveQGAGTGWTVYPPLssiqthsgGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGMTMdRIPLFVWSV 160
Cdd:pfam00115  95 AVLLLASF---GGATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAI 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077 161 LVTAFLLLLSLPVLAGAITMLLTDRNFNttffdpAGGGDPILYQHLFWFFGHPEVYILILPGFGMISQIIPTFAaKKQIF 240
Cdd:pfam00115 163 LATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFA-GRPLF 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077 241 GYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWVATIFGGSLRL-DTPMLWAVGFVFL 319
Cdd:pfam00115 236 GYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFrTTPMLFFLGFAFL 315

                         330
                  ....*....|....*...
gi 1822240077 320 FTIGGLTGIVLANSSLDV 337
Cdd:pfam00115 316 FIIGGLTGVMLALPPVNY 333
 
Name Accession Description Interval E-value
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-337 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: 627.97  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077   1 IGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFWLLPPA 80
Cdd:cd01663    20 VGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPS 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077  81 LTLLLGSAFVEQGAGTGWTVYPPLSSIQTHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGMTMDRIPLFVWSV 160
Cdd:cd01663   100 LLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSV 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077 161 LVTAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISQIIPTFAAKKQIF 240
Cdd:cd01663   180 LITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSGKKPVF 259

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077 241 GYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWVATIFGGSLRLDTPMLWAVGFVFLF 320
Cdd:cd01663   260 GYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPMLWALGFIFLF 339

                         330
                  ....*....|....*..
gi 1822240077 321 TIGGLTGIVLANSSLDV 337
Cdd:cd01663   340 TIGGLTGVVLANSSLDI 356
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-337 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 614.95  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077   1 IGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFWLLPPA 80
Cdd:MTH00153   27 VGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPS 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077  81 LTLLLGSAFVEQGAGTGWTVYPPLSSIQTHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGMTMDRIPLFVWSV 160
Cdd:MTH00153  107 LTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSV 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077 161 LVTAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISQIIPTFAAKKQIF 240
Cdd:MTH00153  187 LITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETF 266

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077 241 GYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWVATIFGGSLRLDTPMLWAVGFVFLF 320
Cdd:MTH00153  267 GTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLF 346

                         330
                  ....*....|....*..
gi 1822240077 321 TIGGLTGIVLANSSLDV 337
Cdd:MTH00153  347 TIGGLTGVVLANSSIDI 363
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-337 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 611.83  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077   1 IGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFWLLPPA 80
Cdd:MTH00184   31 IGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPRLNNISFWLLPPA 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077  81 LTLLLGSAFVEQGAGTGWTVYPPLSSIQTHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGMTMDRIPLFVWSV 160
Cdd:MTH00184  111 LTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRMPLFVWSI 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077 161 LVTAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISQIIPTFAAKKQIF 240
Cdd:MTH00184  191 LVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQIIPTFAAKKQIF 270

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077 241 GYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWVATIFGGSLRLDTPMLWAVGFVFLF 320
Cdd:MTH00184  271 GYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATIFGGSLRLDTPMLWAIGFVFLF 350

                         330
                  ....*....|....*..
gi 1822240077 321 TIGGLTGIVLANSSLDV 337
Cdd:MTH00184  351 TMGGLTGIVLANSSLDV 367
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-337 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 576.39  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077   1 IGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFWLLPPA 80
Cdd:MTH00182   31 IGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFWLLPPA 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077  81 LTLLLGSAFVEQGAGTGWTVYPPLSSIQTHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGMTMDRIPLFVWSV 160
Cdd:MTH00182  111 LILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRLPLFVWSI 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077 161 LVTAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISQIIPTFAAKKQIF 240
Cdd:MTH00182  191 LITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISQIIPTFVAKKQIF 270

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077 241 GYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWVATIFGGSLRLDTPMLWAVGFVFLF 320
Cdd:MTH00182  271 GYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGGTLRLDTPMLWAMGFVFLF 350

                         330
                  ....*....|....*..
gi 1822240077 321 TIGGLTGIVLANSSLDV 337
Cdd:MTH00182  351 TLGGLTGVVLANSSLDI 367
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-337 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 573.08  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077   1 IGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFWLLPPA 80
Cdd:MTH00223   26 VGTSLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPS 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077  81 LTLLLGSAFVEQGAGTGWTVYPPLSSIQTHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGMTMDRIPLFVWSV 160
Cdd:MTH00223  106 LYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERLPLFVWSV 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077 161 LVTAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISQIIPTFAAKKQIF 240
Cdd:MTH00223  186 KVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSSKKEVF 265

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077 241 GYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWVATIFGGSLRLDTPMLWAVGFVFLF 320
Cdd:MTH00223  266 GTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGSKIKYEAPMLWALGFIFLF 345

                         330
                  ....*....|....*..
gi 1822240077 321 TIGGLTGIVLANSSLDV 337
Cdd:MTH00223  346 TVGGLTGIILSNSSLDI 362
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-337 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 567.77  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077   1 IGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFWLLPPA 80
Cdd:MTH00167   29 VGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPS 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077  81 LTLLLGSAFVEQGAGTGWTVYPPLSSIQTHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGMTMDRIPLFVWSV 160
Cdd:MTH00167  109 LLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQTPLFVWSI 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077 161 LVTAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISQIIPTFAAKKQIF 240
Cdd:MTH00167  189 LVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVVYYSGKKEPF 268

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077 241 GYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWVATIFGGSLRLDTPMLWAVGFVFLF 320
Cdd:MTH00167  269 GYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLHGGKIKWETPMLWALGFIFLF 348

                         330
                  ....*....|....*..
gi 1822240077 321 TIGGLTGIVLANSSLDV 337
Cdd:MTH00167  349 TVGGLTGIVLANSSLDI 365
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-337 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 550.08  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077   1 IGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFWLLPPA 80
Cdd:MTH00116   29 VGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPS 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077  81 LTLLLGSAFVEQGAGTGWTVYPPLSSIQTHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGMTMDRIPLFVWSV 160
Cdd:MTH00116  109 FLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTPLFVWSV 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077 161 LVTAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISQIIPTFAAKKQIF 240
Cdd:MTH00116  189 LITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVTYYAGKKEPF 268

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077 241 GYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWVATIFGGSLRLDTPMLWAVGFVFLF 320
Cdd:MTH00116  269 GYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPMLWALGFIFLF 348

                         330
                  ....*....|....*..
gi 1822240077 321 TIGGLTGIVLANSSLDV 337
Cdd:MTH00116  349 TIGGLTGIVLANSSLDI 365
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-337 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 547.79  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077   1 IGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFWLLPPA 80
Cdd:MTH00142   27 VGTGLSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPA 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077  81 LTLLLGSAFVEQGAGTGWTVYPPLSSIQTHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGMTMDRIPLFVWSV 160
Cdd:MTH00142  107 LLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERVPLFVWSV 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077 161 LVTAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISQIIPTFAAKKQIF 240
Cdd:MTH00142  187 KITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIINHYSGKKEVF 266

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077 241 GYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWVATIFGGSLRLDTPMLWAVGFVFLF 320
Cdd:MTH00142  267 GTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFSWLATLHGSKVKYEPPMLWALGFIFLF 346

                         330
                  ....*....|....*..
gi 1822240077 321 TIGGLTGIVLANSSLDV 337
Cdd:MTH00142  347 TVGGLTGIVLANSSLDV 363
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-337 8.89e-178

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 502.44  E-value: 8.89e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077   1 IGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFWLLPPA 80
Cdd:MTH00037   29 VGTAMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPS 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077  81 LTLLLGSAFVEQGAGTGWTVYPPLSSIQTHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGMTMDRIPLFVWSV 160
Cdd:MTH00037  109 FLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRLPLFVWSV 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077 161 LVTAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISQIIPTFAAKKQIF 240
Cdd:MTH00037  189 FITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKQEPF 268

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077 241 GYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWVATIFGGSLRLDTPMLWAVGFVFLF 320
Cdd:MTH00037  269 GYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWMATLQGSNLRWETPLLWALGFVFLF 348

                         330
                  ....*....|....*..
gi 1822240077 321 TIGGLTGIVLANSSLDV 337
Cdd:MTH00037  349 TIGGLTGIVLANSSIDV 365
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-337 2.16e-174

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 494.06  E-value: 2.16e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077   1 IGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFWLLPPA 80
Cdd:MTH00183   29 VGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPS 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077  81 LTLLLGSAFVEQGAGTGWTVYPPLSSIQTHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGMTMDRIPLFVWSV 160
Cdd:MTH00183  109 FLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPLFVWAV 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077 161 LVTAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISQIIPTFAAKKQIF 240
Cdd:MTH00183  189 LITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVAYYSGKKEPF 268

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077 241 GYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWVATIFGGSLRLDTPMLWAVGFVFLF 320
Cdd:MTH00183  269 GYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGSIKWETPLLWALGFIFLF 348

                         330
                  ....*....|....*..
gi 1822240077 321 TIGGLTGIVLANSSLDV 337
Cdd:MTH00183  349 TVGGLTGIVLANSSLDI 365
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-337 1.39e-172

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 489.39  E-value: 1.39e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077   1 IGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFWLLPPA 80
Cdd:MTH00103   29 VGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPS 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077  81 LTLLLGSAFVEQGAGTGWTVYPPLSSIQTHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGMTMDRIPLFVWSV 160
Cdd:MTH00103  109 FLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPLFVWSV 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077 161 LVTAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISQIIPTFAAKKQIF 240
Cdd:MTH00103  189 LITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVTYYSGKKEPF 268

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077 241 GYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWVATIFGGSLRLDTPMLWAVGFVFLF 320
Cdd:MTH00103  269 GYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGNIKWSPAMLWALGFIFLF 348

                         330
                  ....*....|....*..
gi 1822240077 321 TIGGLTGIVLANSSLDV 337
Cdd:MTH00103  349 TVGGLTGIVLANSSLDI 365
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-337 6.44e-171

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 485.21  E-value: 6.44e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077   1 IGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFWLLPPA 80
Cdd:MTH00077   29 VGTALSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPS 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077  81 LTLLLGSAFVEQGAGTGWTVYPPLSSIQTHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGMTMDRIPLFVWSV 160
Cdd:MTH00077  109 FLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQTPLFVWSV 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077 161 LVTAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISQIIPTFAAKKQIF 240
Cdd:MTH00077  189 LITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISHIVTYYSAKKEPF 268

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077 241 GYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWVATIFGGSLRLDTPMLWAVGFVFLF 320
Cdd:MTH00077  269 GYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGAIKWDAAMLWALGFIFLF 348

                         330
                  ....*....|....*..
gi 1822240077 321 TIGGLTGIVLANSSLDV 337
Cdd:MTH00077  349 TVGGLTGIVLANSSLDI 365
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-337 8.86e-171

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 484.41  E-value: 8.86e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077   1 IGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFWLLPPA 80
Cdd:MTH00007   26 LGTSMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPA 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077  81 LTLLLGSAFVEQGAGTGWTVYPPLSSIQTHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGMTMDRIPLFVWSV 160
Cdd:MTH00007  106 LILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERIPLFVWAV 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077 161 LVTAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISQIIPTFAAKKQIF 240
Cdd:MTH00007  186 VITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGAISHIVTHYAGKLEPF 265

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077 241 GYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWVATIFGGSLRLDTPMLWAVGFVFLF 320
Cdd:MTH00007  266 GTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGSPIKYETPMLWALGFIFLF 345

                         330
                  ....*....|....*..
gi 1822240077 321 TIGGLTGIVLANSSLDV 337
Cdd:MTH00007  346 TTGGLTGIVLSNSSLDI 362
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-337 1.60e-170

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 484.90  E-value: 1.60e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077   1 IGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFWLLPPA 80
Cdd:MTH00026   30 IGTAFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPRLNNISFWLLPPA 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077  81 LTLLLGSAFVEQGAGTGWTVYPPLSSIQTHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGMTMDRIPLFVWSV 160
Cdd:MTH00026  110 LFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRIPLFVWSV 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077 161 LVTAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISQIIPTFAAKKQIF 240
Cdd:MTH00026  190 FITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQILSLFSYKKQIF 269

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077 241 GYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWVATIFGG--SLRLDTPMLWAVGFVF 318
Cdd:MTH00026  270 GYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSWLATVSGSgrNLIFTTPMAWALGFIF 349

                         330
                  ....*....|....*....
gi 1822240077 319 LFTIGGLTGIVLANSSLDV 337
Cdd:MTH00026  350 LFTIGGLTGIVLSNSSLDI 368
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-337 7.04e-167

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 474.55  E-value: 7.04e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077   1 IGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFWLLPPA 80
Cdd:MTH00079   30 VGTSLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPRLNNLSFWLLPTS 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077  81 LTLLLGSAFVEQGAGTGWTVYPPLSSiQTHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGMTMDRIPLFVWSV 160
Cdd:MTH00079  110 LFLILDSCFVDMGPGTSWTVYPPLST-LGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHMSLFVWTV 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077 161 LVTAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISQIIPTFAAKKQIF 240
Cdd:MTH00079  189 FVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPEVYILILPAFGIISQSTLYLTGKKEVF 268

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077 241 GYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWVATIFGGSLRLDTPMLWAVGFVFLF 320
Cdd:MTH00079  269 GSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMKFQPLLLWVLGFIFLF 348

                         330
                  ....*....|....*..
gi 1822240077 321 TIGGLTGIVLANSSLDV 337
Cdd:MTH00079  349 TIGGLTGVILSNSSLDI 365
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-337 1.18e-149

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: 428.87  E-value: 1.18e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077   1 IGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWLVPLyIGAPDMAFPRLNNISFWLLPPA 80
Cdd:cd00919    18 LGGLLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPPL-IGARDLAFPRLNNLSFWLFPPG 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077  81 LTLLLGSAFVEQGAGTGWTVYPPLSSIQTHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGMTMDRIPLFVWSV 160
Cdd:cd00919    97 LLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDKMPLFVWSV 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077 161 LVTAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISQIIPTFAAKKqIF 240
Cdd:cd00919   177 LVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAFGAISEIIPTFSGKP-LF 255

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077 241 GYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWVATIFGGSLRLDTPMLWAVGFVFLF 320
Cdd:cd00919   256 GYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGRIRFDPPMLFALGFLFLF 335

                         330
                  ....*....|....*..
gi 1822240077 321 TIGGLTGIVLANSSLDV 337
Cdd:cd00919   336 TIGGLTGVVLANVPLDI 352
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-337 3.96e-149

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: 428.95  E-value: 3.96e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077   1 IGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFVMIFFLVMPvMIGGFGNWLVPLYIGAPDMAFPRLNNISFWLLPPA 80
Cdd:TIGR02891  23 VGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIP-ILAGFGNYLLPLMIGARDMAFPRLNAFSYWLYLFG 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077  81 LTLLLGSAFVEQGAGTGWTVYPPLSSIQTHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGMTMDRIPLFVWSV 160
Cdd:TIGR02891 102 GLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLFVWGI 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077 161 LVTAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISQIIPTFaAKKQIF 240
Cdd:TIGR02891 182 LVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTF-ARKPIF 260

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077 241 GYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWVATIFGGSLRLDTPMLWAVGFVFLF 320
Cdd:TIGR02891 261 GYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLFALGFIFLF 340

                         330
                  ....*....|....*..
gi 1822240077 321 TIGGLTGIVLANSSLDV 337
Cdd:TIGR02891 341 VIGGLTGVMLASVPLDW 357
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-337 1.18e-145

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 421.46  E-value: 1.18e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077   1 IGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFVMIFFLVMPvMIGGFGNWLVPLYIGAPDMAFPRLNNISFWLLPPA 80
Cdd:COG0843    32 IGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFG 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077  81 LTLLLGSAFVEQGAGTGWTVYPPLSSIQTHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGMTMDRIPLFVWSV 160
Cdd:COG0843   111 GLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAA 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077 161 LVTAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISQIIPTFAAKKqIF 240
Cdd:COG0843   191 LVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFSRKP-LF 269

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077 241 GYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWVATIFGGSLRLDTPMLWAVGFVFLF 320
Cdd:COG0843   270 GYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLFALGFIILF 349

                         330
                  ....*....|....*..
gi 1822240077 321 TIGGLTGIVLANSSLDV 337
Cdd:COG0843   350 VIGGLTGVMLASVPLDY 366
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 1-336 5.18e-131

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: 383.08  E-value: 5.18e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077   1 IGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGgFGNWLVPLYIGAPDMAFPRLNNISFWLLPPA 80
Cdd:cd01662    24 RGGVDALLMRTQLALPGNDFLSPEHYNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFPRLNALSFWLFLFG 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077  81 LTLLLGSAFVEQGAGTGWTVYPPLSSIQTHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGMTMDRIPLFVWSV 160
Cdd:cd01662   103 GLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWTT 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077 161 LVTAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISQIIPTFaAKKQIF 240
Cdd:cd01662   183 LVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYILILPAFGIFSEIVPTF-SRKPLF 261

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077 241 GYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWVATIFGGSLRLDTPMLWAVGFVFLF 320
Cdd:cd01662   262 GYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLFTMWRGRIRFETPMLWAIGFLVTF 341

                         330
                  ....*....|....*.
gi 1822240077 321 TIGGLTGIVLANSSLD 336
Cdd:cd01662   342 VIGGLTGVMLASPPAD 357
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 1-337 8.74e-123

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 362.46  E-value: 8.74e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077   1 IGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFWLLPPA 80
Cdd:MTH00048   30 VGLSLSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRLNALSAWLLVPS 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077  81 LTLLLGSAFVeqGAGTGWTVYPPLSSIQTHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGMTMdRIPLFVWSV 160
Cdd:MTH00048  110 IVFLLLSMCL--GAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNVFS-RTSIILWSY 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077 161 LVTAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISQIIPTFAAKKQIF 240
Cdd:MTH00048  187 LFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPEVYVLILPGFGIISHICLSLSNNDDPF 266

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077 241 GYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWVATIFGGSLRLDTPML-WAVGFVFL 319
Cdd:MTH00048  267 GYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFSWLYMLLNSRVRKSDPVVwWVVSFIVL 346

                         330
                  ....*....|....*...
gi 1822240077 320 FTIGGLTGIVLANSSLDV 337
Cdd:MTH00048  347 FTIGGVTGIVLSASVLDN 364
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-337 9.37e-94

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: 285.62  E-value: 9.37e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077   1 IGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFVMIFFLVMPvMIGGFGNWLVPLYIGAPDMAFPRLNNISFWLLPPA 80
Cdd:pfam00115  16 VGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALSFWLVVLG 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077  81 LTLLLGSAfveQGAGTGWTVYPPLssiqthsgGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGMTMdRIPLFVWSV 160
Cdd:pfam00115  95 AVLLLASF---GGATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAI 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077 161 LVTAFLLLLSLPVLAGAITMLLTDRNFNttffdpAGGGDPILYQHLFWFFGHPEVYILILPGFGMISQIIPTFAaKKQIF 240
Cdd:pfam00115 163 LATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFA-GRPLF 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077 241 GYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWVATIFGGSLRL-DTPMLWAVGFVFL 319
Cdd:pfam00115 236 GYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFrTTPMLFFLGFAFL 315

                         330
                  ....*....|....*...
gi 1822240077 320 FTIGGLTGIVLANSSLDV 337
Cdd:pfam00115 316 FIIGGLTGVMLALPPVNY 333
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 24-331 8.68e-85

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 269.11  E-value: 8.68e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077  24 HLYNVIVTAHAFVMIFFLVMPVMIGgFGNWLVPLYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPP 103
Cdd:PRK15017   97 HHYDQIFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPP 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077 104 LSSIQTHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGMTMDRIPLFVWSVLVTAFLLLLSLPVLAGAITMLLT 183
Cdd:PRK15017  176 LSGIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTL 255

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077 184 DRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISQIIPTFaAKKQIFGYLGMVYAMVSIGILGFIVWAHH 263
Cdd:PRK15017  256 DRYLGTHFFTNDMGGNMMMYINLIWAWGHPEVYILILPVFGVFSEIAATF-SRKRLFGYTSLVWATVCITVLSFIVWLHH 334

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1822240077 264 MFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWVATIFGGSLRLDTPMLWAVGFVFLFTIGGLTGIVLA 331
Cdd:PRK15017  335 FFTMGAGANVNAFFGITTMIIAIPTGVKIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLA 402
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
 1-336 4.17e-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: 44.97  E-value: 4.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077   1 IGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFVMIFFLVMpVMIGGFGNWLVPLYIGAPDMAfPRLNNISFWLLPPA 80
Cdd:cd01660    19 LGGLFGLLQVLVRTGVFPLPSSGILYYQGLTLHGVLLAIVFTT-FFIMGFFYAIVARALLRSLFN-RRLAWAGFWLMVIG 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077  81 LTLLLGSAFVEQgAGTGWTVYPPLssiQTHSGGSVDMAIFSLHlagiSSILGAMNFIT-TIFNMRAPGmtmDRIPLFVWS 159
Cdd:cd01660    97 TVMAAVPILLGQ-ASVLYTFYPPL---QAHPLFYIGAALVVVG----SWISGFAMFVTlWRWKKANPG---KKVPLATFM 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077 160 VLVTAFLLLLSLPVLAGAITMLLTDRNFNTTffdpaGGGDPILYQHLFWFFGHPEVYILILPGFGMISQIIPTFAAKKQI 239
Cdd:cd01660   166 VVTTMILWLVASLGVALEVLFQLLPWSLGLV-----DTVDVLLSRTLFWWFGHPLVYFWLLPAYIAWYTILPKIAGGKLF 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1822240077 240 FGYLGMVyAMVSIGILGFIVWAHHMFT-VGMDVDTRAYFTAATMIIAVPTGIKIFSWVATI-FGGSLR------------ 305
Cdd:cd01660   241 SDPLARL-AFILFLLFSTPVGFHHQFAdPGIGPGWKFIHMVLTFMVALPSLLTAFTVFASLeIAGRLRggkglfgwiral 319

                         330       340       350
                  ....*....|....*....|....*....|...
gi 1822240077 306 -LDTPMLWAVGFVFL-FTIGGLTGIVLANSSLD 336
Cdd:cd01660   320 pWGDPMFLALFLAMLmFIPGGAGGIINASYQLN 352
 
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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