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Conserved domains on  [gi|672590014|gb|AIJ29311|]
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cytochrome c oxidase subunit I, partial (mitochondrion) [Ixodes scapularis]

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 ...
 1-251 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: 515.57  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672590014   1 LVESGAGTGWTVYPPLSSNISHSGASVDMAIFSLHLAGISSILGAINFITTIINMRSPGMSLERMPLFVWSVFITAILLL 80
Cdd:MTH00153 115 MVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLL 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672590014  81 LSLPVLAGAITMLLTDRNFNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGMVSHIICFHTGKKEPFGTLGMIYA 160
Cdd:MTH00153 195 LSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMIYA 274

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672590014 161 MLAIGFLGFIVWAHHMFTVGMDIDTRAYFTAATMIIAVPTGIKIFSWLATLHGSNINYNSSMLWVLGFVFLFTLGGLTGI 240
Cdd:MTH00153 275 MLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGV 354

                        250
                 ....*....|.
gi 672590014 241 ILANSSIDIIL 251
Cdd:MTH00153 355 VLANSSIDIIL 365
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-251 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 515.57  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672590014   1 LVESGAGTGWTVYPPLSSNISHSGASVDMAIFSLHLAGISSILGAINFITTIINMRSPGMSLERMPLFVWSVFITAILLL 80
Cdd:MTH00153 115 MVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLL 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672590014  81 LSLPVLAGAITMLLTDRNFNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGMVSHIICFHTGKKEPFGTLGMIYA 160
Cdd:MTH00153 195 LSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMIYA 274

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672590014 161 MLAIGFLGFIVWAHHMFTVGMDIDTRAYFTAATMIIAVPTGIKIFSWLATLHGSNINYNSSMLWVLGFVFLFTLGGLTGI 240
Cdd:MTH00153 275 MLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGV 354

                        250
                 ....*....|.
gi 672590014 241 ILANSSIDIIL 251
Cdd:MTH00153 355 VLANSSIDIIL 365
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-251 2.66e-171

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: 481.21  E-value: 2.66e-171
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672590014   1 LVESGAGTGWTVYPPLSSNISHSGASVDMAIFSLHLAGISSILGAINFITTIINMRSPGMSLERMPLFVWSVFITAILLL 80
Cdd:cd01663  108 LVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLL 187

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672590014  81 LSLPVLAGAITMLLTDRNFNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGMVSHIICFHTGKKEPFGTLGMIYA 160
Cdd:cd01663  188 LSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSGKKPVFGYLGMVYA 267

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672590014 161 MLAIGFLGFIVWAHHMFTVGMDIDTRAYFTAATMIIAVPTGIKIFSWLATLHGSNINYNSSMLWVLGFVFLFTLGGLTGI 240
Cdd:cd01663  268 MLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPMLWALGFIFLFTIGGLTGV 347

                        250
                 ....*....|.
gi 672590014 241 ILANSSIDIIL 251
Cdd:cd01663  348 VLANSSLDIAL 358
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-251 4.91e-110

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: 325.72  E-value: 4.91e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672590014    1 LVESGAGTGWTVYPPLSSNISHSGASVDMAIFSLHLAGISSILGAINFITTIINMRSPGMSLERMPLFVWSVFITAILLL 80
Cdd:TIGR02891 110 FTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLFVWGILVTSILIL 189

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672590014   81 LSLPVLAGAITMLLTDRNFNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGMVSHIICFHTGKKePFGTLGMIYA 160
Cdd:TIGR02891 190 LAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFARKP-IFGYRAMVYA 268

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672590014  161 MLAIGFLGFIVWAHHMFTVGMDIDTRAYFTAATMIIAVPTGIKIFSWLATLHGSNINYNSSMLWVLGFVFLFTLGGLTGI 240
Cdd:TIGR02891 269 TVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLFALGFIFLFVIGGLTGV 348

                         250
                  ....*....|.
gi 672590014  241 ILANSSIDIIL 251
Cdd:TIGR02891 349 MLASVPLDWQL 359
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-251 1.68e-109

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 325.54  E-value: 1.68e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672590014   1 LVESGAGTGWTVYPPLSSNISHSGASVDMAIFSLHLAGISSILGAINFITTIINMRSPGMSLERMPLFVWSVFITAILLL 80
Cdd:COG0843  119 FVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILIL 198

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672590014  81 LSLPVLAGAITMLLTDRNFNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGMVSHIICFHTGKKePFGTLGMIYA 160
Cdd:COG0843  199 LAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFSRKP-LFGYKAMVLA 277

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672590014 161 MLAIGFLGFIVWAHHMFTVGMDIDTRAYFTAATMIIAVPTGIKIFSWLATLHGSNINYNSSMLWVLGFVFLFTLGGLTGI 240
Cdd:COG0843  278 TVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGV 357

                        250
                 ....*....|.
gi 672590014 241 ILANSSIDIIL 251
Cdd:COG0843  358 MLASVPLDYQV 368
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 5-251 1.08e-69

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: 220.14  E-value: 1.08e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672590014    5 GAGTGWTVYPPLssnishsgASVDMAIFSLHLAGISSILGAINFITTIINMRSPGMSLeRMPLFVWSVFITAILLLLSLP 84
Cdd:pfam00115 104 GATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATAILILLAFP 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672590014   85 VLAGAITMLLTDRNFNTsffdpsGGGDPILYQHLFWFFGHPEVYILILPGFGMVSHIICFHTGKKePFGTLGMIYAMLAI 164
Cdd:pfam00115 175 VLAAALLLLLLDRSLGA------GGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGRP-LFGYKLSVLAFWLI 247

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672590014  165 GFLGFIVWAHHMFTVGMDIDTRAYFTAATMIIAVPTGIKIFSWLATLHGSNINYNSS-MLWVLGFVFLFTLGGLTGIILA 243
Cdd:pfam00115 248 AFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFRTTpMLFFLGFAFLFIIGGLTGVMLA 327


                  ....*...
gi 672590014  244 NSSIDIIL 251
Cdd:pfam00115 328 LPPVNYYV 335
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-251 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 515.57  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672590014   1 LVESGAGTGWTVYPPLSSNISHSGASVDMAIFSLHLAGISSILGAINFITTIINMRSPGMSLERMPLFVWSVFITAILLL 80
Cdd:MTH00153 115 MVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLL 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672590014  81 LSLPVLAGAITMLLTDRNFNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGMVSHIICFHTGKKEPFGTLGMIYA 160
Cdd:MTH00153 195 LSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMIYA 274

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672590014 161 MLAIGFLGFIVWAHHMFTVGMDIDTRAYFTAATMIIAVPTGIKIFSWLATLHGSNINYNSSMLWVLGFVFLFTLGGLTGI 240
Cdd:MTH00153 275 MLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGV 354

                        250
                 ....*....|.
gi 672590014 241 ILANSSIDIIL 251
Cdd:MTH00153 355 VLANSSIDIIL 365
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-251 2.66e-171

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: 481.21  E-value: 2.66e-171
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672590014   1 LVESGAGTGWTVYPPLSSNISHSGASVDMAIFSLHLAGISSILGAINFITTIINMRSPGMSLERMPLFVWSVFITAILLL 80
Cdd:cd01663  108 LVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLL 187

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672590014  81 LSLPVLAGAITMLLTDRNFNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGMVSHIICFHTGKKEPFGTLGMIYA 160
Cdd:cd01663  188 LSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSGKKPVFGYLGMVYA 267

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672590014 161 MLAIGFLGFIVWAHHMFTVGMDIDTRAYFTAATMIIAVPTGIKIFSWLATLHGSNINYNSSMLWVLGFVFLFTLGGLTGI 240
Cdd:cd01663  268 MLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPMLWALGFIFLFTIGGLTGV 347

                        250
                 ....*....|.
gi 672590014 241 ILANSSIDIIL 251
Cdd:cd01663  348 VLANSSLDIAL 358
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-251 5.54e-160

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 453.28  E-value: 5.54e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672590014   1 LVESGAGTGWTVYPPLSSNISHSGASVDMAIFSLHLAGISSILGAINFITTIINMRSPGMSLERMPLFVWSVFITAILLL 80
Cdd:MTH00223 114 AVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERLPLFVWSVKVTAFLLL 193

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672590014  81 LSLPVLAGAITMLLTDRNFNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGMVSHIICFHTGKKEPFGTLGMIYA 160
Cdd:MTH00223 194 LSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSSKKEVFGTLGMIYA 273

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672590014 161 MLAIGFLGFIVWAHHMFTVGMDIDTRAYFTAATMIIAVPTGIKIFSWLATLHGSNINYNSSMLWVLGFVFLFTLGGLTGI 240
Cdd:MTH00223 274 MLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGSKIKYEAPMLWALGFIFLFTVGGLTGI 353

                        250
                 ....*....|.
gi 672590014 241 ILANSSIDIIL 251
Cdd:MTH00223 354 ILSNSSLDIML 364
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-251 4.69e-158

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 448.36  E-value: 4.69e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672590014   1 LVESGAGTGWTVYPPLSSNISHSGASVDMAIFSLHLAGISSILGAINFITTIINMRSPGMSLERMPLFVWSVFITAILLL 80
Cdd:MTH00167 117 GVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQTPLFVWSILVTTILLL 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672590014  81 LSLPVLAGAITMLLTDRNFNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGMVSHIICFHTGKKEPFGTLGMIYA 160
Cdd:MTH00167 197 LSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVVYYSGKKEPFGYMGMVWA 276

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672590014 161 MLAIGFLGFIVWAHHMFTVGMDIDTRAYFTAATMIIAVPTGIKIFSWLATLHGSNINYNSSMLWVLGFVFLFTLGGLTGI 240
Cdd:MTH00167 277 MMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLHGGKIKWETPMLWALGFIFLFTVGGLTGI 356

                        250
                 ....*....|.
gi 672590014 241 ILANSSIDIIL 251
Cdd:MTH00167 357 VLANSSLDIVL 367
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 2-251 9.05e-154

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 437.60  E-value: 9.05e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672590014   2 VESGAGTGWTVYPPLSSNISHSGASVDMAIFSLHLAGISSILGAINFITTIINMRSPGMSLERMPLFVWSVFITAILLLL 81
Cdd:MTH00116 118 VEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTPLFVWSVLITAVLLLL 197

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672590014  82 SLPVLAGAITMLLTDRNFNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGMVSHIICFHTGKKEPFGTLGMIYAM 161
Cdd:MTH00116 198 SLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVTYYAGKKEPFGYMGMVWAM 277

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672590014 162 LAIGFLGFIVWAHHMFTVGMDIDTRAYFTAATMIIAVPTGIKIFSWLATLHGSNINYNSSMLWVLGFVFLFTLGGLTGII 241
Cdd:MTH00116 278 LSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIV 357

                        250
                 ....*....|
gi 672590014 242 LANSSIDIIL 251
Cdd:MTH00116 358 LANSSLDIVL 367
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-251 8.56e-153

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 435.31  E-value: 8.56e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672590014   1 LVESGAGTGWTVYPPLSSNISHSGASVDMAIFSLHLAGISSILGAINFITTIINMRSPGMSLERMPLFVWSVFITAILLL 80
Cdd:MTH00142 115 AVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERVPLFVWSVKITAILLL 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672590014  81 LSLPVLAGAITMLLTDRNFNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGMVSHIICFHTGKKEPFGTLGMIYA 160
Cdd:MTH00142 195 LSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIINHYSGKKEVFGTLGMIYA 274

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672590014 161 MLAIGFLGFIVWAHHMFTVGMDIDTRAYFTAATMIIAVPTGIKIFSWLATLHGSNINYNSSMLWVLGFVFLFTLGGLTGI 240
Cdd:MTH00142 275 MLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFSWLATLHGSKVKYEPPMLWALGFIFLFTVGGLTGI 354

                        250
                 ....*....|.
gi 672590014 241 ILANSSIDIIL 251
Cdd:MTH00142 355 VLANSSLDVVL 365
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-251 9.34e-138

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 396.97  E-value: 9.34e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672590014   1 LVESGAGTGWTVYPPLSSNISHSGASVDMAIFSLHLAGISSILGAINFITTIINMRSPGMSLERMPLFVWSVFITAILLL 80
Cdd:MTH00007 114 AVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERIPLFVWAVVITVVLLL 193

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672590014  81 LSLPVLAGAITMLLTDRNFNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGMVSHIICFHTGKKEPFGTLGMIYA 160
Cdd:MTH00007 194 LSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGAISHIVTHYAGKLEPFGTLGMIYA 273

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672590014 161 MLAIGFLGFIVWAHHMFTVGMDIDTRAYFTAATMIIAVPTGIKIFSWLATLHGSNINYNSSMLWVLGFVFLFTLGGLTGI 240
Cdd:MTH00007 274 MLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGSPIKYETPMLWALGFIFLFTTGGLTGI 353

                        250
                 ....*....|.
gi 672590014 241 ILANSSIDIIL 251
Cdd:MTH00007 354 VLSNSSLDIIL 364
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-251 2.51e-136

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 393.48  E-value: 2.51e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672590014   1 LVESGAGTGWTVYPPLSSNISHSGASVDMAIFSLHLAGISSILGAINFITTIINMRSPGMSLERMPLFVWSVFITAILLL 80
Cdd:MTH00103 117 MVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPLFVWSVLITAVLLL 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672590014  81 LSLPVLAGAITMLLTDRNFNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGMVSHIICFHTGKKEPFGTLGMIYA 160
Cdd:MTH00103 197 LSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVTYYSGKKEPFGYMGMVWA 276

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672590014 161 MLAIGFLGFIVWAHHMFTVGMDIDTRAYFTAATMIIAVPTGIKIFSWLATLHGSNINYNSSMLWVLGFVFLFTLGGLTGI 240
Cdd:MTH00103 277 MMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGNIKWSPAMLWALGFIFLFTVGGLTGI 356

                        250
                 ....*....|.
gi 672590014 241 ILANSSIDIIL 251
Cdd:MTH00103 357 VLANSSLDIVL 367
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 2-251 4.76e-136

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 392.66  E-value: 4.76e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672590014   2 VESGAGTGWTVYPPLSSNISHSGASVDMAIFSLHLAGISSILGAINFITTIINMRSPGMSLERMPLFVWSVFITAILLLL 81
Cdd:MTH00037 118 VESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRLPLFVWSVFITAFLLLL 197

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672590014  82 SLPVLAGAITMLLTDRNFNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGMVSHIICFHTGKKEPFGTLGMIYAM 161
Cdd:MTH00037 198 SLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKQEPFGYLGMVYAM 277

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672590014 162 LAIGFLGFIVWAHHMFTVGMDIDTRAYFTAATMIIAVPTGIKIFSWLATLHGSNINYNSSMLWVLGFVFLFTLGGLTGII 241
Cdd:MTH00037 278 IAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWMATLQGSNLRWETPLLWALGFVFLFTIGGLTGIV 357

                        250
                 ....*....|
gi 672590014 242 LANSSIDIIL 251
Cdd:MTH00037 358 LANSSIDVVL 367
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 2-251 6.23e-135

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 390.05  E-value: 6.23e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672590014   2 VESGAGTGWTVYPPLSSNISHSGASVDMAIFSLHLAGISSILGAINFITTIINMRSPGMSLERMPLFVWSVFITAILLLL 81
Cdd:MTH00183 118 VEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPLFVWAVLITAVLLLL 197

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672590014  82 SLPVLAGAITMLLTDRNFNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGMVSHIICFHTGKKEPFGTLGMIYAM 161
Cdd:MTH00183 198 SLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVAYYSGKKEPFGYMGMVWAM 277

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672590014 162 LAIGFLGFIVWAHHMFTVGMDIDTRAYFTAATMIIAVPTGIKIFSWLATLHGSNINYNSSMLWVLGFVFLFTLGGLTGII 241
Cdd:MTH00183 278 MAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGSIKWETPLLWALGFIFLFTVGGLTGIV 357

                        250
                 ....*....|
gi 672590014 242 LANSSIDIIL 251
Cdd:MTH00183 358 LANSSLDIVL 367
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-251 1.06e-130

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 379.02  E-value: 1.06e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672590014   1 LVESGAGTGWTVYPPLSSnISHSGASVDMAIFSLHLAGISSILGAINFITTIINMRSPGMSLERMPLFVWSVFITAILLL 80
Cdd:MTH00079 118 FVDMGPGTSWTVYPPLST-LGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHMSLFVWTVFVTVFLLV 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672590014  81 LSLPVLAGAITMLLTDRNFNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGMVSHIICFHTGKKEPFGTLGMIYA 160
Cdd:MTH00079 197 LSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPEVYILILPAFGIISQSTLYLTGKKEVFGSLGMVYA 276

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672590014 161 MLAIGFLGFIVWAHHMFTVGMDIDTRAYFTAATMIIAVPTGIKIFSWLATLHGSNINYNSSMLWVLGFVFLFTLGGLTGI 240
Cdd:MTH00079 277 ILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMKFQPLLLWVLGFIFLFTIGGLTGV 356

                        250
                 ....*....|.
gi 672590014 241 ILANSSIDIIL 251
Cdd:MTH00079 357 ILSNSSLDIIL 367
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-251 1.28e-130

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 379.17  E-value: 1.28e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672590014   1 LVESGAGTGWTVYPPLSSNISHSGASVDMAIFSLHLAGISSILGAINFITTIINMRSPGMSLERMPLFVWSVFITAILLL 80
Cdd:MTH00182 119 FVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRLPLFVWSILITAFLLL 198

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672590014  81 LSLPVLAGAITMLLTDRNFNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGMVSHIICFHTGKKEPFGTLGMIYA 160
Cdd:MTH00182 199 LSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISQIIPTFVAKKQIFGYLGMVYA 278

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672590014 161 MLAIGFLGFIVWAHHMFTVGMDIDTRAYFTAATMIIAVPTGIKIFSWLATLHGSNINYNSSMLWVLGFVFLFTLGGLTGI 240
Cdd:MTH00182 279 MLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGGTLRLDTPMLWAMGFVFLFTLGGLTGV 358

                        250
                 ....*....|.
gi 672590014 241 ILANSSIDIIL 251
Cdd:MTH00182 359 VLANSSLDIVL 369
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 2-251 2.66e-130

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 378.13  E-value: 2.66e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672590014   2 VESGAGTGWTVYPPLSSNISHSGASVDMAIFSLHLAGISSILGAINFITTIINMRSPGMSLERMPLFVWSVFITAILLLL 81
Cdd:MTH00077 118 VEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQTPLFVWSVLITAVLLLL 197

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672590014  82 SLPVLAGAITMLLTDRNFNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGMVSHIICFHTGKKEPFGTLGMIYAM 161
Cdd:MTH00077 198 SLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISHIVTYYSAKKEPFGYMGMVWAM 277

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672590014 162 LAIGFLGFIVWAHHMFTVGMDIDTRAYFTAATMIIAVPTGIKIFSWLATLHGSNINYNSSMLWVLGFVFLFTLGGLTGII 241
Cdd:MTH00077 278 MSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGAIKWDAAMLWALGFIFLFTVGGLTGIV 357

                        250
                 ....*....|
gi 672590014 242 LANSSIDIIL 251
Cdd:MTH00077 358 LANSSLDIVL 367
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-251 1.90e-128

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 373.39  E-value: 1.90e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672590014   1 LVESGAGTGWTVYPPLSSNISHSGASVDMAIFSLHLAGISSILGAINFITTIINMRSPGMSLERMPLFVWSVFITAILLL 80
Cdd:MTH00184 119 FVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRMPLFVWSILVTTFLLL 198

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672590014  81 LSLPVLAGAITMLLTDRNFNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGMVSHIICFHTGKKEPFGTLGMIYA 160
Cdd:MTH00184 199 LSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQIIPTFAAKKQIFGYLGMVYA 278

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672590014 161 MLAIGFLGFIVWAHHMFTVGMDIDTRAYFTAATMIIAVPTGIKIFSWLATLHGSNINYNSSMLWVLGFVFLFTLGGLTGI 240
Cdd:MTH00184 279 MVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGI 358

                        250
                 ....*....|.
gi 672590014 241 ILANSSIDIIL 251
Cdd:MTH00184 359 VLANSSLDVVL 369
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-251 5.02e-115

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 339.68  E-value: 5.02e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672590014   1 LVESGAGTGWTVYPPLSSNISHSGASVDMAIFSLHLAGISSILGAINFITTIINMRSPGMSLERMPLFVWSVFITAILLL 80
Cdd:MTH00026 118 LVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRIPLFVWSVFITAILLL 197

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672590014  81 LSLPVLAGAITMLLTDRNFNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGMVSHIICFHTGKKEPFGTLGMIYA 160
Cdd:MTH00026 198 LSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQILSLFSYKKQIFGYLGMVYA 277

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672590014 161 MLAIGFLGFIVWAHHMFTVGMDIDTRAYFTAATMIIAVPTGIKIFSWLATLHGS--NINYNSSMLWVLGFVFLFTLGGLT 238
Cdd:MTH00026 278 MLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSWLATVSGSgrNLIFTTPMAWALGFIFLFTIGGLT 357

                        250
                 ....*....|...
gi 672590014 239 GIILANSSIDIIL 251
Cdd:MTH00026 358 GIVLSNSSLDILL 370
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-251 6.30e-114

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: 334.50  E-value: 6.30e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672590014   1 LVESGAGTGWTVYPPLSSNISHSGASVDMAIFSLHLAGISSILGAINFITTIINMRSPGMSLERMPLFVWSVFITAILLL 80
Cdd:cd00919  105 LVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDKMPLFVWSVLVTAILLL 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672590014  81 LSLPVLAGAITMLLTDRNFNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGMVSHIICFHTGKKePFGTLGMIYA 160
Cdd:cd00919  185 LALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAFGAISEIIPTFSGKP-LFGYKLMVYA 263

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672590014 161 MLAIGFLGFIVWAHHMFTVGMDIDTRAYFTAATMIIAVPTGIKIFSWLATLHGSNINYNSSMLWVLGFVFLFTLGGLTGI 240
Cdd:cd00919  264 FLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGRIRFDPPMLFALGFLFLFTIGGLTGV 343

                        250
                 ....*....|.
gi 672590014 241 ILANSSIDIIL 251
Cdd:cd00919  344 VLANVPLDIVL 354
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-251 4.91e-110

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: 325.72  E-value: 4.91e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672590014    1 LVESGAGTGWTVYPPLSSNISHSGASVDMAIFSLHLAGISSILGAINFITTIINMRSPGMSLERMPLFVWSVFITAILLL 80
Cdd:TIGR02891 110 FTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLFVWGILVTSILIL 189

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672590014   81 LSLPVLAGAITMLLTDRNFNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGMVSHIICFHTGKKePFGTLGMIYA 160
Cdd:TIGR02891 190 LAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFARKP-IFGYRAMVYA 268

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672590014  161 MLAIGFLGFIVWAHHMFTVGMDIDTRAYFTAATMIIAVPTGIKIFSWLATLHGSNINYNSSMLWVLGFVFLFTLGGLTGI 240
Cdd:TIGR02891 269 TVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLFALGFIFLFVIGGLTGV 348

                         250
                  ....*....|.
gi 672590014  241 ILANSSIDIIL 251
Cdd:TIGR02891 349 MLASVPLDWQL 359
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-251 1.68e-109

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 325.54  E-value: 1.68e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672590014   1 LVESGAGTGWTVYPPLSSNISHSGASVDMAIFSLHLAGISSILGAINFITTIINMRSPGMSLERMPLFVWSVFITAILLL 80
Cdd:COG0843  119 FVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILIL 198

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672590014  81 LSLPVLAGAITMLLTDRNFNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGMVSHIICFHTGKKePFGTLGMIYA 160
Cdd:COG0843  199 LAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFSRKP-LFGYKAMVLA 277

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672590014 161 MLAIGFLGFIVWAHHMFTVGMDIDTRAYFTAATMIIAVPTGIKIFSWLATLHGSNINYNSSMLWVLGFVFLFTLGGLTGI 240
Cdd:COG0843  278 TVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGV 357

                        250
                 ....*....|.
gi 672590014 241 ILANSSIDIIL 251
Cdd:COG0843  358 MLASVPLDYQV 368
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 5-251 6.61e-97

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 292.74  E-value: 6.61e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672590014   5 GAGTGWTVYPPLSSNISHSGASVDMAIFSLHLAGISSILGAINFITTIINMRSPGMSlERMPLFVWSVFITAILLLLSLP 84
Cdd:MTH00048 120 GAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNVF-SRTSIILWSYLFTSILLLLSLP 198

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672590014  85 VLAGAITMLLTDRNFNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGMVSHIICFHTGKKEPFGTLGMIYAMLAI 164
Cdd:MTH00048 199 VLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPEVYVLILPGFGIISHICLSLSNNDDPFGYYGLVFAMFSI 278

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672590014 165 GFLGFIVWAHHMFTVGMDIDTRAYFTAATMIIAVPTGIKIFSWLATLHGSNINYNSSML-WVLGFVFLFTLGGLTGIILA 243
Cdd:MTH00048 279 VCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFSWLYMLLNSRVRKSDPVVwWVVSFIVLFTIGGVTGIVLS 358


                 ....*...
gi 672590014 244 NSSIDIIL 251
Cdd:MTH00048 359 ASVLDNVL 366
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 1-248 6.51e-96

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: 289.87  E-value: 6.51e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672590014   1 LVESGAGTGWTVYPPLSSNISHSGASVDMAIFSLHLAGISSILGAINFITTIINMRSPGMSLERMPLFVWSVFITAILLL 80
Cdd:cd01662  111 LIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWTTLVTSILIL 190

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672590014  81 LSLPVLAGAITMLLTDRNFNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGMVSHIICFHTGKKePFGTLGMIYA 160
Cdd:cd01662  191 FAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYILILPAFGIFSEIVPTFSRKP-LFGYRSMVYA 269

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672590014 161 MLAIGFLGFIVWAHHMFTVGMDIDTRAYFTAATMIIAVPTGIKIFSWLATLHGSNINYNSSMLWVLGFVFLFTLGGLTGI 240
Cdd:cd01662  270 TVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLFTMWRGRIRFETPMLWAIGFLVTFVIGGLTGV 349


                 ....*...
gi 672590014 241 ILANSSID 248
Cdd:cd01662  350 MLASPPAD 357
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 5-251 1.08e-69

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: 220.14  E-value: 1.08e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672590014    5 GAGTGWTVYPPLssnishsgASVDMAIFSLHLAGISSILGAINFITTIINMRSPGMSLeRMPLFVWSVFITAILLLLSLP 84
Cdd:pfam00115 104 GATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATAILILLAFP 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672590014   85 VLAGAITMLLTDRNFNTsffdpsGGGDPILYQHLFWFFGHPEVYILILPGFGMVSHIICFHTGKKePFGTLGMIYAMLAI 164
Cdd:pfam00115 175 VLAAALLLLLLDRSLGA------GGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGRP-LFGYKLSVLAFWLI 247

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672590014  165 GFLGFIVWAHHMFTVGMDIDTRAYFTAATMIIAVPTGIKIFSWLATLHGSNINYNSS-MLWVLGFVFLFTLGGLTGIILA 243
Cdd:pfam00115 248 AFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFRTTpMLFFLGFAFLFIIGGLTGVMLA 327


                  ....*...
gi 672590014  244 NSSIDIIL 251
Cdd:pfam00115 328 LPPVNYYV 335
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 6-251 1.53e-63

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 209.79  E-value: 1.53e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672590014   6 AGTGWTVYPPLSSNISHSGASVDMAIFSLHLAGISSILGAINFITTIINMRSPGMSLERMPLFVWSVFITAILLLLSLPV 85
Cdd:PRK15017 166 AQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPI 245

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672590014  86 LAGAITMLLTDRNFNTSFFDPSGGGDPILYQHLFWFFGHPEVYILILPGFGMVSHIICFHTgKKEPFGTLGMIYAMLAIG 165
Cdd:PRK15017 246 LTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWGHPEVYILILPVFGVFSEIAATFS-RKRLFGYTSLVWATVCIT 324

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672590014 166 FLGFIVWAHHMFTVGMDIDTRAYFTAATMIIAVPTGIKIFSWLATLHGSNINYNSSMLWVLGFVFLFTLGGLTGIILANS 245
Cdd:PRK15017 325 VLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVKIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVP 404


                 ....*.
gi 672590014 246 SIDIIL 251
Cdd:PRK15017 405 GADFVL 410
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
 111-250 8.81e-03

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


Pssm-ID: 238830  Cd Length: 473  Bit Score: 36.88  E-value: 8.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672590014 111 DPILYQHLFWFFGHPEVYILILPGFGMVSHIICFHTGKK---EPFGTLGMIYAMLAIGFLGFivwaHHMFT-VGMDIDTR 186
Cdd:cd01660  200 DVLLSRTLFWWFGHPLVYFWLLPAYIAWYTILPKIAGGKlfsDPLARLAFILFLLFSTPVGF----HHQFAdPGIGPGWK 275

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672590014 187 AYFTAATMIIAVPTGIKIFSWLATL-HGSNINYNSSMLW---------------VLGFVFlFTLGGLTGIILANSSIDII 250
Cdd:cd01660  276 FIHMVLTFMVALPSLLTAFTVFASLeIAGRLRGGKGLFGwiralpwgdpmflalFLAMLM-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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