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Conserved domains on  [gi|1011708245|gb|AMR97179|]
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cytochrome oxidase subunit I, partial (mitochondrion) [Ceuthophilus sp. Ceu_183_TX_Com_CampBCv1]

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 ...
 1-283 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: 570.66  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011708245   1 LMLGAPDMAFPRMNNMSFWLLPPSLSLLLASSLVENGAGTGWTVYPPLSAGIAHAGASVDLAIFSLHLAGISSILGAVNF 80
Cdd:MTH00153   83 LMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINF 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011708245  81 ITTTINMRSPGMNFDQMPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 160
Cdd:MTH00153  163 ITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 242

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011708245 161 ILILPGFGMISHIISQESGKKEAFGTLGMVYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 240
Cdd:MTH00153  243 ILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 322

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1011708245 241 ATLHGTQFNYSPALLWALGFVFLFTIGGLTGVILANSSIDIIL 283
Cdd:MTH00153  323 ATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIIL 365
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-283 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 570.66  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011708245   1 LMLGAPDMAFPRMNNMSFWLLPPSLSLLLASSLVENGAGTGWTVYPPLSAGIAHAGASVDLAIFSLHLAGISSILGAVNF 80
Cdd:MTH00153   83 LMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINF 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011708245  81 ITTTINMRSPGMNFDQMPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 160
Cdd:MTH00153  163 ITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 242

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011708245 161 ILILPGFGMISHIISQESGKKEAFGTLGMVYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 240
Cdd:MTH00153  243 ILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 322

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1011708245 241 ATLHGTQFNYSPALLWALGFVFLFTIGGLTGVILANSSIDIIL 283
Cdd:MTH00153  323 ATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIIL 365
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-283 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: 509.72  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011708245   1 LMLGAPDMAFPRMNNMSFWLLPPSLSLLLASSLVENGAGTGWTVYPPLSAGIAHAGASVDLAIFSLHLAGISSILGAVNF 80
Cdd:cd01663    76 LMIGAPDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINF 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011708245  81 ITTTINMRSPGMNFDQMPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 160
Cdd:cd01663   156 ITTIFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVY 235

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011708245 161 ILILPGFGMISHIISQESGKKEAFGTLGMVYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 240
Cdd:cd01663   236 ILILPGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWL 315

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1011708245 241 ATLHGTQFNYSPALLWALGFVFLFTIGGLTGVILANSSIDIIL 283
Cdd:cd01663   316 ATMWGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIAL 358
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-283 3.02e-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: 338.04  E-value: 3.02e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011708245   1 LMLGAPDMAFPRMNNMSFWLLPPSLSLLLASSLVENGAGTGWTVYPPLSAGIAHAGASVDLAIFSLHLAGISSILGAVNF 80
Cdd:TIGR02891  78 LMIGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNF 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011708245  81 ITTTINMRSPGMNFDQMPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 160
Cdd:TIGR02891 158 IVTILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVY 237

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011708245 161 ILILPGFGMISHIISQESGKKeAFGTLGMVYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 240
Cdd:TIGR02891 238 IIFLPAFGIISEILPTFARKP-IFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWI 316

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1011708245 241 ATLHGTQFNYSPALLWALGFVFLFTIGGLTGVILANSSIDIIL 283
Cdd:TIGR02891 317 ATLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQL 359
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-283 4.83e-114

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 338.64  E-value: 4.83e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011708245   1 LMLGAPDMAFPRMNNMSFWLLPPSLSLLLASSLVENGAGTGWTVYPPLSAGIAHAGASVDLAIFSLHLAGISSILGAVNF 80
Cdd:COG0843    87 LQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNF 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011708245  81 ITTTINMRSPGMNFDQMPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 160
Cdd:COG0843   167 IVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVY 246

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011708245 161 ILILPGFGMISHIISQESGKKeAFGTLGMVYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 240
Cdd:COG0843   247 ILILPAFGIVSEIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWI 325

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1011708245 241 ATLHGTQFNYSPALLWALGFVFLFTIGGLTGVILANSSIDIIL 283
Cdd:COG0843   326 ATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQV 368
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-283 5.73e-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: 230.15  E-value: 5.73e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011708245   1 LMLGAPDMAFPRMNNMSFWLLPPSLSLLLASSlveNGAGTGWTVYPPLSAgiahagasVDLAIFSLHLAGISSILGAVNF 80
Cdd:pfam00115  71 LMIGARDMAFPRLNALSFWLVVLGAVLLLASF---GGATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINF 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011708245  81 ITTTINMRSPGMNFdQMPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNtsffdpAGGGDPILYQHLFWFFGHPEVY 160
Cdd:pfam00115 140 IVTILKRRAPGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVY 212

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011708245 161 ILILPGFGMISHIISQESGKKeAFGTLGMVYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 240
Cdd:pfam00115 213 ILILPAFGIIYYILPKFAGRP-LFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWL 291

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1011708245 241 ATLHGT--QFNYSPaLLWALGFVFLFTIGGLTGVILANSSIDIIL 283
Cdd:pfam00115 292 ATLWGGwiRFRTTP-MLFFLGFAFLFIIGGLTGVMLALPPVNYYV 335
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-283 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 570.66  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011708245   1 LMLGAPDMAFPRMNNMSFWLLPPSLSLLLASSLVENGAGTGWTVYPPLSAGIAHAGASVDLAIFSLHLAGISSILGAVNF 80
Cdd:MTH00153   83 LMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINF 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011708245  81 ITTTINMRSPGMNFDQMPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 160
Cdd:MTH00153  163 ITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 242

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011708245 161 ILILPGFGMISHIISQESGKKEAFGTLGMVYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 240
Cdd:MTH00153  243 ILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 322

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1011708245 241 ATLHGTQFNYSPALLWALGFVFLFTIGGLTGVILANSSIDIIL 283
Cdd:MTH00153  323 ATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIIL 365
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-283 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: 509.72  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011708245   1 LMLGAPDMAFPRMNNMSFWLLPPSLSLLLASSLVENGAGTGWTVYPPLSAGIAHAGASVDLAIFSLHLAGISSILGAVNF 80
Cdd:cd01663    76 LMIGAPDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINF 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011708245  81 ITTTINMRSPGMNFDQMPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 160
Cdd:cd01663   156 ITTIFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVY 235

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011708245 161 ILILPGFGMISHIISQESGKKEAFGTLGMVYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 240
Cdd:cd01663   236 ILILPGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWL 315

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1011708245 241 ATLHGTQFNYSPALLWALGFVFLFTIGGLTGVILANSSIDIIL 283
Cdd:cd01663   316 ATMWGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIAL 358
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-283 1.27e-167

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 474.17  E-value: 1.27e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011708245   1 LMLGAPDMAFPRMNNMSFWLLPPSLSLLLASSLVENGAGTGWTVYPPLSAGIAHAGASVDLAIFSLHLAGISSILGAVNF 80
Cdd:MTH00167   85 LMIGAPDMAFPRMNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINF 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011708245  81 ITTTINMRSPGMNFDQMPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 160
Cdd:MTH00167  165 ITTIINMKPPGITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVY 244

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011708245 161 ILILPGFGMISHIISQESGKKEAFGTLGMVYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 240
Cdd:MTH00167  245 ILILPGFGMISHIVVYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWL 324

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1011708245 241 ATLHGTQFNYSPALLWALGFVFLFTIGGLTGVILANSSIDIIL 283
Cdd:MTH00167  325 ATLHGGKIKWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVL 367
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-283 5.05e-167

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 472.54  E-value: 5.05e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011708245   1 LMLGAPDMAFPRMNNMSFWLLPPSLSLLLASSLVENGAGTGWTVYPPLSAGIAHAGASVDLAIFSLHLAGISSILGAVNF 80
Cdd:MTH00223   82 LMLGAPDMAFPRLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINF 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011708245  81 ITTTINMRSPGMNFDQMPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 160
Cdd:MTH00223  162 ITTIINMRSPGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVY 241

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011708245 161 ILILPGFGMISHIISQESGKKEAFGTLGMVYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 240
Cdd:MTH00223  242 ILILPGFGMISHIVSHYSSKKEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWL 321

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1011708245 241 ATLHGTQFNYSPALLWALGFVFLFTIGGLTGVILANSSIDIIL 283
Cdd:MTH00223  322 ATIYGSKIKYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIML 364
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-283 8.58e-167

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 471.90  E-value: 8.58e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011708245   1 LMLGAPDMAFPRMNNMSFWLLPPSLSLLLASSLVENGAGTGWTVYPPLSAGIAHAGASVDLAIFSLHLAGISSILGAVNF 80
Cdd:MTH00142   83 LMLGAPDMAFPRMNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINF 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011708245  81 ITTTINMRSPGMNFDQMPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 160
Cdd:MTH00142  163 ITTVINMRAGGMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVY 242

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011708245 161 ILILPGFGMISHIISQESGKKEAFGTLGMVYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 240
Cdd:MTH00142  243 ILILPGFGMISHIINHYSGKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFSWL 322

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1011708245 241 ATLHGTQFNYSPALLWALGFVFLFTIGGLTGVILANSSIDIIL 283
Cdd:MTH00142  323 ATLHGSKVKYEPPMLWALGFIFLFTVGGLTGIVLANSSLDVVL 365
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-283 1.61e-165

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 469.19  E-value: 1.61e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011708245   1 LMLGAPDMAFPRMNNMSFWLLPPSLSLLLASSLVENGAGTGWTVYPPLSAGIAHAGASVDLAIFSLHLAGISSILGAVNF 80
Cdd:MTH00116   85 LMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINF 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011708245  81 ITTTINMRSPGMNFDQMPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 160
Cdd:MTH00116  165 ITTCINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVY 244

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011708245 161 ILILPGFGMISHIISQESGKKEAFGTLGMVYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 240
Cdd:MTH00116  245 ILILPGFGIISHIVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSWL 324

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1011708245 241 ATLHGTQFNYSPALLWALGFVFLFTIGGLTGVILANSSIDIIL 283
Cdd:MTH00116  325 ATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVL 367
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-283 9.89e-150

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 428.86  E-value: 9.89e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011708245   1 LMLGAPDMAFPRMNNMSFWLLPPSLSLLLASSLVENGAGTGWTVYPPLSAGIAHAGASVDLAIFSLHLAGISSILGAVNF 80
Cdd:MTH00037   85 LMIGAPDMAFPRMNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINF 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011708245  81 ITTTINMRSPGMNFDQMPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 160
Cdd:MTH00037  165 ITTIINMRTPGMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPEVY 244

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011708245 161 ILILPGFGMISHIISQESGKKEAFGTLGMVYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 240
Cdd:MTH00037  245 ILILPGFGMISHVIAHYSGKQEPFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWM 324

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1011708245 241 ATLHGTQFNYSPALLWALGFVFLFTIGGLTGVILANSSIDIIL 283
Cdd:MTH00037  325 ATLQGSNLRWETPLLWALGFVFLFTIGGLTGIVLANSSIDVVL 367
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-283 8.62e-149

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 426.24  E-value: 8.62e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011708245   1 LMLGAPDMAFPRMNNMSFWLLPPSLSLLLASSLVENGAGTGWTVYPPLSAGIAHAGASVDLAIFSLHLAGISSILGAVNF 80
Cdd:MTH00007   82 LMLGAPDMAFPRLNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINF 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011708245  81 ITTTINMRSPGMNFDQMPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 160
Cdd:MTH00007  162 ITTVINMRWKGLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 241

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011708245 161 ILILPGFGMISHIISQESGKKEAFGTLGMVYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 240
Cdd:MTH00007  242 ILILPGFGAISHIVTHYAGKLEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWL 321

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1011708245 241 ATLHGTQFNYSPALLWALGFVFLFTIGGLTGVILANSSIDIIL 283
Cdd:MTH00007  322 ATIHGSPIKYETPMLWALGFIFLFTTGGLTGIVLSNSSLDIIL 364
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-283 4.39e-148

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 424.68  E-value: 4.39e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011708245   1 LMLGAPDMAFPRMNNMSFWLLPPSLSLLLASSLVENGAGTGWTVYPPLSAGIAHAGASVDLAIFSLHLAGISSILGAVNF 80
Cdd:MTH00103   85 LMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINF 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011708245  81 ITTTINMRSPGMNFDQMPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 160
Cdd:MTH00103  165 ITTIINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVY 244

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011708245 161 ILILPGFGMISHIISQESGKKEAFGTLGMVYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 240
Cdd:MTH00103  245 ILILPGFGMISHIVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWL 324

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1011708245 241 ATLHGTQFNYSPALLWALGFVFLFTIGGLTGVILANSSIDIIL 283
Cdd:MTH00103  325 ATLHGGNIKWSPAMLWALGFIFLFTVGGLTGIVLANSSLDIVL 367
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-283 2.43e-146

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 420.48  E-value: 2.43e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011708245   1 LMLGAPDMAFPRMNNMSFWLLPPSLSLLLASSLVENGAGTGWTVYPPLSAGIAHAGASVDLAIFSLHLAGISSILGAVNF 80
Cdd:MTH00183   85 LMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINF 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011708245  81 ITTTINMRSPGMNFDQMPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 160
Cdd:MTH00183  165 ITTIINMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVY 244

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011708245 161 ILILPGFGMISHIISQESGKKEAFGTLGMVYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 240
Cdd:MTH00183  245 ILILPGFGMISHIVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWL 324

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1011708245 241 ATLHGTQFNYSPALLWALGFVFLFTIGGLTGVILANSSIDIIL 283
Cdd:MTH00183  325 ATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLANSSLDIVL 367
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-283 1.00e-143

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 413.31  E-value: 1.00e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011708245   1 LMLGAPDMAFPRMNNMSFWLLPPSLSLLLASSLVENGAGTGWTVYPPLSAgIAHAGASVDLAIFSLHLAGISSILGAVNF 80
Cdd:MTH00079   86 LMLGAPDMSFPRLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLST-LGHPGSSVDLAIFSLHCAGISSILGGINF 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011708245  81 ITTTINMRSPGMNFDQMPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 160
Cdd:MTH00079  165 MVTTKNLRSSSISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPEVY 244

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011708245 161 ILILPGFGMISHIISQESGKKEAFGTLGMVYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 240
Cdd:MTH00079  245 ILILPAFGIISQSTLYLTGKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWL 324

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1011708245 241 ATLHGTQFNYSPALLWALGFVFLFTIGGLTGVILANSSIDIIL 283
Cdd:MTH00079  325 ATLFGMKMKFQPLLLWVLGFIFLFTIGGLTGVILSNSSLDIIL 367
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-283 6.01e-143

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 411.64  E-value: 6.01e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011708245   1 LMLGAPDMAFPRMNNMSFWLLPPSLSLLLASSLVENGAGTGWTVYPPLSAGIAHAGASVDLAIFSLHLAGISSILGAVNF 80
Cdd:MTH00077   85 LMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINF 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011708245  81 ITTTINMRSPGMNFDQMPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 160
Cdd:MTH00077  165 ITTSINMKPPSMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVY 244

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011708245 161 ILILPGFGMISHIISQESGKKEAFGTLGMVYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 240
Cdd:MTH00077  245 ILILPGFGMISHIVTYYSAKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVFSWL 324

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1011708245 241 ATLHGTQFNYSPALLWALGFVFLFTIGGLTGVILANSSIDIIL 283
Cdd:MTH00077  325 ATMHGGAIKWDAAMLWALGFIFLFTVGGLTGIVLANSSLDIVL 367
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-283 3.87e-140

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 404.97  E-value: 3.87e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011708245   1 LMLGAPDMAFPRMNNMSFWLLPPSLSLLLASSLVENGAGTGWTVYPPLSAGIAHAGASVDLAIFSLHLAGISSILGAVNF 80
Cdd:MTH00182   87 LYIGAPDMAFPRLNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINF 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011708245  81 ITTTINMRSPGMNFDQMPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 160
Cdd:MTH00182  167 ITTIFNMRAPGVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVY 246

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011708245 161 ILILPGFGMISHIISQESGKKEAFGTLGMVYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 240
Cdd:MTH00182  247 ILILPGFGMISQIIPTFVAKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWL 326

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1011708245 241 ATLHGTQFNYSPALLWALGFVFLFTIGGLTGVILANSSIDIIL 283
Cdd:MTH00182  327 ATIYGGTLRLDTPMLWAMGFVFLFTLGGLTGVVLANSSLDIVL 369
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-283 1.44e-136

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 395.73  E-value: 1.44e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011708245   1 LMLGAPDMAFPRMNNMSFWLLPPSLSLLLASSLVENGAGTGWTVYPPLSAGIAHAGASVDLAIFSLHLAGISSILGAVNF 80
Cdd:MTH00184   87 LYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNF 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011708245  81 ITTTINMRSPGMNFDQMPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 160
Cdd:MTH00184  167 ITTIFNMRAPGITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVY 246

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011708245 161 ILILPGFGMISHIISQESGKKEAFGTLGMVYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 240
Cdd:MTH00184  247 ILILPGFGIISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWI 326

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1011708245 241 ATLHGTQFNYSPALLWALGFVFLFTIGGLTGVILANSSIDIIL 283
Cdd:MTH00184  327 ATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVL 369
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-283 3.04e-123

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 362.02  E-value: 3.04e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011708245   1 LMLGAPDMAFPRMNNMSFWLLPPSLSLLLASSLVENGAGTGWTVYPPLSAGIAHAGASVDLAIFSLHLAGISSILGAVNF 80
Cdd:MTH00026   86 LMIGAPDMAFPRLNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNF 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011708245  81 ITTTINMRSPGMNFDQMPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 160
Cdd:MTH00026  166 ITTVMNMRTPGMTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVY 245

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011708245 161 ILILPGFGMISHIISQESGKKEAFGTLGMVYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 240
Cdd:MTH00026  246 ILILPGFGIISQILSLFSYKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSWL 325

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1011708245 241 ATLHGTQFN--YSPALLWALGFVFLFTIGGLTGVILANSSIDIIL 283
Cdd:MTH00026  326 ATVSGSGRNliFTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILL 370
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-283 1.44e-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: 350.29  E-value: 1.44e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011708245   1 LMLGAPDMAFPRMNNMSFWLLPPSLSLLLASSLVENGAGTGWTVYPPLSAGIAHAGASVDLAIFSLHLAGISSILGAVNF 80
Cdd:cd00919    73 PLIGARDLAFPRLNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINF 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011708245  81 ITTTINMRSPGMNFDQMPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 160
Cdd:cd00919   153 ITTILNMRAPGMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVY 232

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011708245 161 ILILPGFGMISHIISQESGKKeAFGTLGMVYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 240
Cdd:cd00919   233 ILILPAFGAISEIIPTFSGKP-LFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWL 311

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1011708245 241 ATLHGTQFNYSPALLWALGFVFLFTIGGLTGVILANSSIDIIL 283
Cdd:cd00919   312 ATLWGGRIRFDPPMLFALGFLFLFTIGGLTGVVLANVPLDIVL 354
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-283 3.02e-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: 338.04  E-value: 3.02e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011708245   1 LMLGAPDMAFPRMNNMSFWLLPPSLSLLLASSLVENGAGTGWTVYPPLSAGIAHAGASVDLAIFSLHLAGISSILGAVNF 80
Cdd:TIGR02891  78 LMIGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNF 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011708245  81 ITTTINMRSPGMNFDQMPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 160
Cdd:TIGR02891 158 IVTILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVY 237

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011708245 161 ILILPGFGMISHIISQESGKKeAFGTLGMVYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 240
Cdd:TIGR02891 238 IIFLPAFGIISEILPTFARKP-IFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWI 316

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1011708245 241 ATLHGTQFNYSPALLWALGFVFLFTIGGLTGVILANSSIDIIL 283
Cdd:TIGR02891 317 ATLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQL 359
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-283 4.83e-114

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 338.64  E-value: 4.83e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011708245   1 LMLGAPDMAFPRMNNMSFWLLPPSLSLLLASSLVENGAGTGWTVYPPLSAGIAHAGASVDLAIFSLHLAGISSILGAVNF 80
Cdd:COG0843    87 LQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNF 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011708245  81 ITTTINMRSPGMNFDQMPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 160
Cdd:COG0843   167 IVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVY 246

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011708245 161 ILILPGFGMISHIISQESGKKeAFGTLGMVYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 240
Cdd:COG0843   247 ILILPAFGIVSEIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWI 325

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1011708245 241 ATLHGTQFNYSPALLWALGFVFLFTIGGLTGVILANSSIDIIL 283
Cdd:COG0843   326 ATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQV 368
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 1-283 1.10e-101

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 306.22  E-value: 1.10e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011708245   1 LMLGAPDMAFPRMNNMSFWLLPPSLSLLLASSLVenGAGTGWTVYPPLSAGIAHAGASVDLAIFSLHLAGISSILGAVNF 80
Cdd:MTH00048   86 LLLGLSDLNLPRLNALSAWLLVPSIVFLLLSMCL--GAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINF 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011708245  81 ITTTINMRSPGMNFdQMPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 160
Cdd:MTH00048  164 ICTIYSAFMTNVFS-RTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPEVY 242

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011708245 161 ILILPGFGMISHIISQESGKKEAFGTLGMVYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 240
Cdd:MTH00048  243 VLILPGFGIISHICLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFSWL 322

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1011708245 241 ATLHGTQFNYS-PALLWALGFVFLFTIGGLTGVILANSSIDIIL 283
Cdd:MTH00048  323 YMLLNSRVRKSdPVVWWVVSFIVLFTIGGVTGIVLSASVLDNVL 366
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 1-280 5.17e-101

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: 304.12  E-value: 5.17e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011708245   1 LMLGAPDMAFPRMNNMSFWLLPPSLSLLLASSLVENGAGTGWTVYPPLSAGIAHAGASVDLAIFSLHLAGISSILGAVNF 80
Cdd:cd01662    79 LQIGARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINF 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011708245  81 ITTTINMRSPGMNFDQMPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 160
Cdd:cd01662   159 IVTILKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVY 238

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011708245 161 ILILPGFGMISHIISQESGKKeAFGTLGMVYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 240
Cdd:cd01662   239 ILILPAFGIFSEIVPTFSRKP-LFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWL 317

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1011708245 241 ATLHGTQFNYSPALLWALGFVFLFTIGGLTGVILANSSID 280
Cdd:cd01662   318 FTMWRGRIRFETPMLWAIGFLVTFVIGGLTGVMLASPPAD 357
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-283 5.73e-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: 230.15  E-value: 5.73e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011708245   1 LMLGAPDMAFPRMNNMSFWLLPPSLSLLLASSlveNGAGTGWTVYPPLSAgiahagasVDLAIFSLHLAGISSILGAVNF 80
Cdd:pfam00115  71 LMIGARDMAFPRLNALSFWLVVLGAVLLLASF---GGATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINF 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011708245  81 ITTTINMRSPGMNFdQMPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNtsffdpAGGGDPILYQHLFWFFGHPEVY 160
Cdd:pfam00115 140 IVTILKRRAPGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVY 212

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011708245 161 ILILPGFGMISHIISQESGKKeAFGTLGMVYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 240
Cdd:pfam00115 213 ILILPAFGIIYYILPKFAGRP-LFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWL 291

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1011708245 241 ATLHGT--QFNYSPaLLWALGFVFLFTIGGLTGVILANSSIDIIL 283
Cdd:pfam00115 292 ATLWGGwiRFRTTP-MLFFLGFAFLFIIGGLTGVMLALPPVNYYV 335
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 1-283 5.84e-69

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 225.59  E-value: 5.84e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011708245   1 LMLGAPDMAFPRMNNMSFWLLPPSLSLLLASSLVENGAGTGWTVYPPLSAGIAHAGASVDLAIFSLHLAGISSILGAVNF 80
Cdd:PRK15017  129 LQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTTLTGINF 208

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011708245  81 ITTTINMRSPGMNFDQMPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 160
Cdd:PRK15017  209 FVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWGHPEVY 288

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011708245 161 ILILPGFGMISHIISQESgKKEAFGTLGMVYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 240
Cdd:PRK15017  289 ILILPVFGVFSEIAATFS-RKRLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVKIFNWL 367

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1011708245 241 ATLHGTQFNYSPALLWALGFVFLFTIGGLTGVILANSSIDIIL 283
Cdd:PRK15017  368 FTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVL 410
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 1-280 9.30e-65

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: 213.95  E-value: 9.30e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011708245   1 LMLGAPDMAFPRMNNMSFWLLPPSLSLLLASSLVENGAGTGWTVYPPLSAGIAHAGASVDLAIFSLHLAGISSILGAVNF 80
Cdd:TIGR02882 122 LQIGARDVAFPVLNALSFWLFFAGAMLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINF 201

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011708245  81 ITTTINMRSPGMNFDQMPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 160
Cdd:TIGR02882 202 FVTILKMRAPGMKLMQMPMFTWTTLITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLFWIWGHPEVY 281

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011708245 161 ILILPGFGMISHIISQESgKKEAFGTLGMVYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 240
Cdd:TIGR02882 282 IVILPAFGIYSEIISTFA-QKRLFGYKSMVWSTVGIAFLSFLVWVHHFFTMGNGALINSFFSITTMAIAIPTGVKIFNWL 360

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1011708245 241 ATLHGTQFNYSPALLWALGFVFLFTIGGLTGVILANSSID 280
Cdd:TIGR02882 361 LTLYKGKIRFTTPMLFSLAFIPNFLIGGVTGVMLAMASAD 400
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
 143-282 2.72e-04

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: 41.89  E-value: 2.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1011708245 143 DPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKEAFGTLGMVyAMLAIGLLGFVVWAHHMFT-VGMDVDTRAYF 221
Cdd:cd01660   200 DVLLSRTLFWWFGHPLVYFWLLPAYIAWYTILPKIAGGKLFSDPLARL-AFILFLLFSTPVGFHHQFAdPGIGPGWKFIH 278

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1011708245 222 TSATMIIAVPTGIKIFSWLATL--------HGTQFNYSPALLW--------ALGFVFlFTIGGLTGVILANSSIDII 282
Cdd:cd01660   279 MVLTFMVALPSLLTAFTVFASLeiagrlrgGKGLFGWIRALPWgdpmflalFLAMLM-FIPGGAGGIINASYQLNYV 354
 
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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