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Conserved domains on  [gi|823078557|gb|AKI26690|]
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cytochrome oxidase subunit I, partial (mitochondrion) [Eumigus monticolus]

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 ...
 1-384 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: 763.64  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557   1 MVDMGAGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGISSILGAVNFITTAINMRSESMTLDQTPLFVWSVAITALLLL 80
Cdd:MTH00153 115 MVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLL 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557  81 LSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYA 160
Cdd:MTH00153 195 LSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMIYA 274

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557 161 MLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFKFNPPLLWALGFIFLFTIGGLTGL 240
Cdd:MTH00153 275 MLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGV 354

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557 241 ILANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLTMNNTWLKIQFTIMFIGVNLTFFPQHFLGLAGM 320
Cdd:MTH00153 355 VLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGM 434

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 823078557 321 PRRYSDYPDAYTSWNVISSIGSTISIVGIIMFIMIMWESMISNRTVMFSINMPSSTEWLQNNPP 384
Cdd:MTH00153 435 PRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPVLFSLNLSSSIEWLQNLPP 498
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-384 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 763.64  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557   1 MVDMGAGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGISSILGAVNFITTAINMRSESMTLDQTPLFVWSVAITALLLL 80
Cdd:MTH00153 115 MVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLL 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557  81 LSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYA 160
Cdd:MTH00153 195 LSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMIYA 274

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557 161 MLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFKFNPPLLWALGFIFLFTIGGLTGL 240
Cdd:MTH00153 275 MLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGV 354

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557 241 ILANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLTMNNTWLKIQFTIMFIGVNLTFFPQHFLGLAGM 320
Cdd:MTH00153 355 VLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGM 434

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 823078557 321 PRRYSDYPDAYTSWNVISSIGSTISIVGIIMFIMIMWESMISNRTVMFSINMPSSTEWLQNNPP 384
Cdd:MTH00153 435 PRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPVLFSLNLSSSIEWLQNLPP 498
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-380 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: 657.63  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557   1 MVDMGAGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGISSILGAVNFITTAINMRSESMTLDQTPLFVWSVAITALLLL 80
Cdd:cd01663  108 LVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLL 187

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557  81 LSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYA 160
Cdd:cd01663  188 LSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSGKKPVFGYLGMVYA 267

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557 161 MLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFKFNPPLLWALGFIFLFTIGGLTGL 240
Cdd:cd01663  268 MLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPMLWALGFIFLFTIGGLTGV 347

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557 241 ILANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLTMNNTWLKIQFTIMFIGVNLTFFPQHFLGLAGM 320
Cdd:cd01663  348 VLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHFWLMFIGVNLTFFPQHFLGLAGM 427

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 823078557 321 PRRYSDYPDAYTSWNVISSIGSTISIVGIIMFIMIMWESMISNRTVMFSINMPSST-EWLQ 380
Cdd:cd01663  428 PRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFNVGEGSTSlEWTL 488
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
2-364 3.44e-148

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 429.93  E-value: 3.44e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557   2 VDMGAGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGISSILGAVNFITTAINMRSESMTLDQTPLFVWSVAITALLLLL 81
Cdd:COG0843  120 VGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILL 199

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557  82 SLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKiESFGTLGMIYAM 161
Cdd:COG0843  200 AFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFSRK-PLFGYKAMVLAT 278

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557 162 LSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLI 241
Cdd:COG0843  279 VAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVM 358

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557 242 LANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLTMNNTWLKIQFTIMFIGVNLTFFPQHFLGLAGMP 321
Cdd:COG0843  359 LASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMP 438

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 823078557 322 RRYSDYP--DAYTSWNVISSIGSTISIVGIIMFIMIMWESMISNR 364
Cdd:COG0843  439 RRYATYPpePGWQPLNLISTIGAFILAVGFLLFLINLVVSLRKGP 483
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 2-384 6.39e-148

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: 427.80  E-value: 6.39e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557    2 VDMGAGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGISSILGAVNFITTAINMRSESMTLDQTPLFVWSVAITALLLLL 81
Cdd:TIGR02891 111 TGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLFVWGILVTSILILL 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557   82 SLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKiESFGTLGMIYAM 161
Cdd:TIGR02891 191 AFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFARK-PIFGYRAMVYAT 269

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557  162 LSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLI 241
Cdd:TIGR02891 270 VAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLFALGFIFLFVIGGLTGVM 349

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557  242 LANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLTMNNTWLKIQFTIMFIGVNLTFFPQHFLGLAGMP 321
Cdd:TIGR02891 350 LASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLGRWHFWLTFVGFNLTFFPMHLLGLLGMP 429

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 823078557  322 RRYSDYPDA--YTSWNVISSIGSTISIVGIIMFIMIMWESMISNRTVMFSINMPSSTEWLQNNPP 384
Cdd:TIGR02891 430 RRYYTYPPQmgFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGPKAGANPWGATTLEWTTSSPP 494
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 4-326 9.52e-99

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: 300.26  E-value: 9.52e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557    4 MGAGTGWTVYPPLAGaiahggasVDLAIFSLHLAGISSILGAVNFITTAINMRSESMTLdQTPLFVWSVAITALLLLLSL 83
Cdd:pfam00115 103 GGATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATAILILLAF 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557   84 PVLAGAITMLLTDRNLNtsffdpAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKiESFGTLGMIYAMLS 163
Cdd:pfam00115 174 PVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGR-PLFGYKLSVLAFWL 246

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557  164 IGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFKFN-PPLLWALGFIFLFTIGGLTGLIL 242
Cdd:pfam00115 247 IAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFRtTPMLFFLGFAFLFIIGGLTGVML 326

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557  243 ANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLTMNNTWLKIQFTIMFIGVNLTFFPQHFLGLAGMPR 322
Cdd:pfam00115 327 ALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFWLLFIGFNLTFFPMHILGLLGMPR 406


                  ....
gi 823078557  323 RYSD 326
Cdd:pfam00115 407 RYAP 410
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-384 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 763.64  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557   1 MVDMGAGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGISSILGAVNFITTAINMRSESMTLDQTPLFVWSVAITALLLL 80
Cdd:MTH00153 115 MVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLL 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557  81 LSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYA 160
Cdd:MTH00153 195 LSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMIYA 274

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557 161 MLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFKFNPPLLWALGFIFLFTIGGLTGL 240
Cdd:MTH00153 275 MLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGV 354

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557 241 ILANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLTMNNTWLKIQFTIMFIGVNLTFFPQHFLGLAGM 320
Cdd:MTH00153 355 VLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGM 434

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 823078557 321 PRRYSDYPDAYTSWNVISSIGSTISIVGIIMFIMIMWESMISNRTVMFSINMPSSTEWLQNNPP 384
Cdd:MTH00153 435 PRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPVLFSLNLSSSIEWLQNLPP 498
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-380 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: 657.63  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557   1 MVDMGAGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGISSILGAVNFITTAINMRSESMTLDQTPLFVWSVAITALLLL 80
Cdd:cd01663  108 LVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLL 187

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557  81 LSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYA 160
Cdd:cd01663  188 LSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSGKKPVFGYLGMVYA 267

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557 161 MLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFKFNPPLLWALGFIFLFTIGGLTGL 240
Cdd:cd01663  268 MLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPMLWALGFIFLFTIGGLTGV 347

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557 241 ILANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLTMNNTWLKIQFTIMFIGVNLTFFPQHFLGLAGM 320
Cdd:cd01663  348 VLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHFWLMFIGVNLTFFPQHFLGLAGM 427

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 823078557 321 PRRYSDYPDAYTSWNVISSIGSTISIVGIIMFIMIMWESMISNRTVMFSINMPSST-EWLQ 380
Cdd:cd01663  428 PRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFNVGEGSTSlEWTL 488
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-378 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 628.16  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557   1 MVDMGAGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGISSILGAVNFITTAINMRSESMTLDQTPLFVWSVAITALLLL 80
Cdd:MTH00223 114 AVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERLPLFVWSVKVTAFLLL 193

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557  81 LSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYA 160
Cdd:MTH00223 194 LSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSSKKEVFGTLGMIYA 273

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557 161 MLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFKFNPPLLWALGFIFLFTIGGLTGL 240
Cdd:MTH00223 274 MLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGSKIKYEAPMLWALGFIFLFTVGGLTGI 353

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557 241 ILANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLTMNNTWLKIQFTIMFIGVNLTFFPQHFLGLAGM 320
Cdd:MTH00223 354 ILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLFTGVTLHRRWAKAHFFLMFLGVNLTFFPQHFLGLAGM 433

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 823078557 321 PRRYSDYPDAYTSWNVISSIGSTISIVGIIMFIMIMWESMISNRTVMFSINMPSSTEW 378
Cdd:MTH00223 434 PRRYSDYPDCYTKWNQVSSFGSMISFVSVLFFMFIVWEAFVSQRSVVWSGHLSTSLEW 491
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-384 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 625.16  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557   1 MVDMGAGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGISSILGAVNFITTAINMRSESMTLDQTPLFVWSVAITALLLL 80
Cdd:MTH00167 117 GVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQTPLFVWSILVTTILLL 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557  81 LSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYA 160
Cdd:MTH00167 197 LSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVVYYSGKKEPFGYMGMVWA 276

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557 161 MLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFKFNPPLLWALGFIFLFTIGGLTGL 240
Cdd:MTH00167 277 MMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLHGGKIKWETPMLWALGFIFLFTVGGLTGI 356

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557 241 ILANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLTMNNTWLKIQFTIMFIGVNLTFFPQHFLGLAGM 320
Cdd:MTH00167 357 VLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGLTLNETWTKIHFFVMFIGVNLTFFPQHFLGLAGM 436

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 823078557 321 PRRYSDYPDAYTSWNVISSIGSTISIVGIIMFIMIMWESMISNRTVMFSINMPSSTEWLQNNPP 384
Cdd:MTH00167 437 PRRYSDYPDAYTLWNVVSSIGSLISLVAVILFLFIIWEAFSSKRKLLPVELTSTNVEWLHGCPP 500
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 2-384 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 624.42  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557   2 VDMGAGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGISSILGAVNFITTAINMRSESMTLDQTPLFVWSVAITALLLLL 81
Cdd:MTH00116 118 VEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTPLFVWSVLITAVLLLL 197

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557  82 SLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAM 161
Cdd:MTH00116 198 SLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVTYYAGKKEPFGYMGMVWAM 277

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557 162 LSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLI 241
Cdd:MTH00116 278 LSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIV 357

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557 242 LANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLTMNNTWLKIQFTIMFIGVNLTFFPQHFLGLAGMP 321
Cdd:MTH00116 358 LANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGYTLHQTWTKAQFGVMFTGVNLTFFPQHFLGLAGMP 437

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 823078557 322 RRYSDYPDAYTSWNVISSIGSTISIVGIIMFIMIMWESMISNRTVMFSINMPSSTEWLQNNPP 384
Cdd:MTH00116 438 RRYSDYPDAYTLWNTISSIGSLISMTAVIMLMFIIWEAFSSKRKVLQPELTTTNIEWIHGCPP 500
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-384 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 618.66  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557   1 MVDMGAGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGISSILGAVNFITTAINMRSESMTLDQTPLFVWSVAITALLLL 80
Cdd:MTH00142 115 AVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERVPLFVWSVKITAILLL 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557  81 LSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYA 160
Cdd:MTH00142 195 LSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIINHYSGKKEVFGTLGMIYA 274

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557 161 MLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFKFNPPLLWALGFIFLFTIGGLTGL 240
Cdd:MTH00142 275 MLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFSWLATLHGSKVKYEPPMLWALGFIFLFTVGGLTGI 354

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557 241 ILANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLTMNNTWLKIQFTIMFIGVNLTFFPQHFLGLAGM 320
Cdd:MTH00142 355 VLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLFTGLTLNPRWLKAHFYTMFIGVNLTFFPQHFLGLAGM 434

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 823078557 321 PRRYSDYPDAYTSWNVISSIGSTISIVGIIMFIMIMWESMISNRTVMFSINMPSSTEWLQNNPP 384
Cdd:MTH00142 435 PRRYSDYPDAYTTWNVVSSLGSMISFIAVLMFVFIVWESFVSQRLVMWSSHLSTSLEWSHRLPP 498
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-384 0e+00

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 559.50  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557   1 MVDMGAGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGISSILGAVNFITTAINMRSESMTLDQTPLFVWSVAITALLLL 80
Cdd:MTH00103 117 MVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPLFVWSVLITAVLLL 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557  81 LSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYA 160
Cdd:MTH00103 197 LSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVTYYSGKKEPFGYMGMVWA 276

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557 161 MLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFKFNPPLLWALGFIFLFTIGGLTGL 240
Cdd:MTH00103 277 MMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGNIKWSPAMLWALGFIFLFTVGGLTGI 356

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557 241 ILANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLTMNNTWLKIQFTIMFIGVNLTFFPQHFLGLAGM 320
Cdd:MTH00103 357 VLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLNDTWAKIHFTIMFVGVNMTFFPQHFLGLSGM 436

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 823078557 321 PRRYSDYPDAYTSWNVISSIGSTISIVGIIMFIMIMWESMISNRTVMFSINMPSSTEWLQNNPP 384
Cdd:MTH00103 437 PRRYSDYPDAYTTWNTVSSMGSFISLTAVMLMIFMIWEAFASKREVLTVELTTTNLEWLHGCPP 500
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 2-383 0e+00

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 558.75  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557   2 VDMGAGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGISSILGAVNFITTAINMRSESMTLDQTPLFVWSVAITALLLLL 81
Cdd:MTH00007 115 VEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERIPLFVWAVVITVVLLLL 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557  82 SLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAM 161
Cdd:MTH00007 195 SLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGAISHIVTHYAGKLEPFGTLGMIYAM 274

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557 162 LSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLI 241
Cdd:MTH00007 275 LGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGSPIKYETPMLWALGFIFLFTTGGLTGIV 354

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557 242 LANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLTMNNTWLKIQFTIMFIGVNLTFFPQHFLGLAGMP 321
Cdd:MTH00007 355 LSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTGLTLHDRWAKAHFFLMFLGVNLTFFPQHFLGLSGMP 434

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 823078557 322 RRYSDYPDAYTSWNVISSIGSTISIVGIIMFIMIMWESMISNRTVMFSINMPSSTEWLQNNP 383
Cdd:MTH00007 435 RRYSDYPDAYTKWNVVSSFGSMLSFVALLLFIFILWEAFSAQRGVIASPHMSSSLEWQDTLP 496
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 2-384 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 555.69  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557   2 VDMGAGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGISSILGAVNFITTAINMRSESMTLDQTPLFVWSVAITALLLLL 81
Cdd:MTH00183 118 VEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPLFVWAVLITAVLLLL 197

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557  82 SLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAM 161
Cdd:MTH00183 198 SLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVAYYSGKKEPFGYMGMVWAM 277

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557 162 LSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLI 241
Cdd:MTH00183 278 MAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGSIKWETPLLWALGFIFLFTVGGLTGIV 357

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557 242 LANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLTMNNTWLKIQFTIMFIGVNLTFFPQHFLGLAGMP 321
Cdd:MTH00183 358 LANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLFSGYTLHSTWTKIHFGVMFVGVNLTFFPQHFLGLAGMP 437

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 823078557 322 RRYSDYPDAYTSWNVISSIGSTISIVGIIMFIMIMWESMISNRTVMFSINMPSSTEWLQNNPP 384
Cdd:MTH00183 438 RRYSDYPDAYTLWNTVSSIGSLISLVAVIMFLFILWEAFAAKREVLSVELTSTNVEWLHGCPP 500
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-384 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 550.31  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557   1 MVDMGAGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGISSILGAVNFITTAINMRSESMTLDQTPLFVWSVAITALLLL 80
Cdd:MTH00077 117 GVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQTPLFVWSVLITAVLLL 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557  81 LSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYA 160
Cdd:MTH00077 197 LSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISHIVTYYSAKKEPFGYMGMVWA 276

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557 161 MLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFKFNPPLLWALGFIFLFTIGGLTGL 240
Cdd:MTH00077 277 MMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGAIKWDAAMLWALGFIFLFTVGGLTGI 356

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557 241 ILANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLTMNNTWLKIQFTIMFIGVNLTFFPQHFLGLAGM 320
Cdd:MTH00077 357 VLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLHSTWSKIHFGVMFIGVNLTFFPQHFLGLAGM 436

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 823078557 321 PRRYSDYPDAYTSWNVISSIGSTISIVGIIMFIMIMWESMISNRTVMFSINMPSSTEWLQNNPP 384
Cdd:MTH00077 437 PRRYSDYPDAYTLWNTVSSIGSLISLVAVIMMMFIIWEAFSSKREVLTTELTSTNIEWLHGCPP 500
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 2-384 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 543.27  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557   2 VDMGAGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGISSILGAVNFITTAINMRSESMTLDQTPLFVWSVAITALLLLL 81
Cdd:MTH00037 118 VESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRLPLFVWSVFITAFLLLL 197

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557  82 SLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAM 161
Cdd:MTH00037 198 SLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKQEPFGYLGMVYAM 277

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557 162 LSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLI 241
Cdd:MTH00037 278 IAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWMATLQGSNLRWETPLLWALGFVFLFTIGGLTGIV 357

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557 242 LANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLTMNNTWLKIQFTIMFIGVNLTFFPQHFLGLAGMP 321
Cdd:MTH00037 358 LANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLFSGVSLHPLWSKVHFFLMFIGVNLTFFPQHFLGLAGMP 437

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 823078557 322 RRYSDYPDAYTSWNVISSIGSTISIVGIIMFIMIMWESMISNRTVMFSINMPSSTEWLQNNPP 384
Cdd:MTH00037 438 RRYSDYPDAYTLWNTVSSIGSTISLVATLFFLFLIWEAFASQREVISPEFSSSSLEWQYSSFP 500
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-384 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 521.16  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557   1 MVDMGAGTGWTVYPPLAgAIAHGGASVDLAIFSLHLAGISSILGAVNFITTAINMRSESMTLDQTPLFVWSVAITALLLL 80
Cdd:MTH00079 118 FVDMGPGTSWTVYPPLS-TLGHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHMSLFVWTVFVTVFLLV 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557  81 LSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYA 160
Cdd:MTH00079 197 LSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPEVYILILPAFGIISQSTLYLTGKKEVFGSLGMVYA 276

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557 161 MLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFKFNPPLLWALGFIFLFTIGGLTGL 240
Cdd:MTH00079 277 ILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMKFQPLLLWVLGFIFLFTIGGLTGV 356

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557 241 ILANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLTMNNTWLKIQFTIMFIGVNLTFFPQHFLGLAGM 320
Cdd:MTH00079 357 ILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFMTGIVYDKLMMSAVFFLMFVGVNLTFFPLHFAGLHGM 436

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 823078557 321 PRRYSDYPDAYTSWNVISSIGSTISIVGIIMFIMIMWESMISNRTVMFSINMPSSTEWLQNNPP 384
Cdd:MTH00079 437 PRKYLDYPDVYSVWNVISSYGSMISVFALFLFIYVLLESFFSYRLVLHDNYINSSPEYSLSSYV 500
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 2-384 1.89e-176

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 501.66  E-value: 1.89e-176
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557   2 VDMGAGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGISSILGAVNFITTAINMRSESMTLDQTPLFVWSVAITALLLLL 81
Cdd:MTH00182 120 VEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRLPLFVWSILITAFLLLL 199

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557  82 SLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAM 161
Cdd:MTH00182 200 SLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISQIIPTFVAKKQIFGYLGMVYAM 279

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557 162 LSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLI 241
Cdd:MTH00182 280 LSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGGTLRLDTPMLWAMGFVFLFTLGGLTGVV 359

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557 242 LANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLTMNNTWLKIQFTIMFIGVNLTFFPQHFLGLAGMP 321
Cdd:MTH00182 360 LANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNELYGKIHFWLMFIGVNLTFFPQHFLGLAGFP 439

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 823078557 322 RRYSDYPDAYTSWNVISSIGSTISIVGIIMFIMIMWESMISNRTVMFSINMP----SSTEWLQNNPP 384
Cdd:MTH00182 440 RRYSDFADAFAGWNLVSSLGSIISIVGVVWFIYIIYDAYVREEKFIGWKEGTgeswASLEWVHSSPP 506
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 2-384 3.55e-172

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 490.49  E-value: 3.55e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557   2 VDMGAGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGISSILGAVNFITTAINMRSESMTLDQTPLFVWSVAITALLLLL 81
Cdd:MTH00184 120 VEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRMPLFVWSILVTTFLLLL 199

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557  82 SLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAM 161
Cdd:MTH00184 200 SLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQIIPTFAAKKQIFGYLGMVYAM 279

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557 162 LSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLI 241
Cdd:MTH00184 280 VSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIV 359

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557 242 LANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLTMNNTWLKIQFTIMFIGVNLTFFPQHFLGLAGMP 321
Cdd:MTH00184 360 LANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLP 439

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 823078557 322 RRYSDYPDAYTSWNVISSIGSTISIVGIIMFIMIMWESM---ISNRTVMFSINMPSSTEWLQNNPP 384
Cdd:MTH00184 440 RRYSDFHDSFAGWNQISSLGSVISIVGVVWFIYIVYDAYvreIKFVGWVEDSGHYPSLEWAQTSPP 505
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 2-360 4.81e-159

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: 455.07  E-value: 4.81e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557   2 VDMGAGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGISSILGAVNFITTAINMRSESMTLDQTPLFVWSVAITALLLLL 81
Cdd:cd00919  106 VGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDKMPLFVWSVLVTAILLLL 185

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557  82 SLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKiESFGTLGMIYAM 161
Cdd:cd00919  186 ALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAFGAISEIIPTFSGK-PLFGYKLMVYAF 264

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557 162 LSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLI 241
Cdd:cd00919  265 LAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGRIRFDPPMLFALGFLFLFTIGGLTGVV 344

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557 242 LANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLTMNNTWLKIQFTIMFIGVNLTFFPQHFLGLAGMP 321
Cdd:cd00919  345 LANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKLGKIHFWLWFIGFNLTFFPMHFLGLLGMP 424

                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 823078557 322 RRYSDYPDAYTSWNVISSIGSTISIVGIIMFIMIMWESM 360
Cdd:cd00919  425 RRYADYPDGFAPWNFISSVGAFILGLGLLLFLGNLFLSL 463
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-359 5.07e-150

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 434.83  E-value: 5.07e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557   1 MVDMGAGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGISSILGAVNFITTAINMRSESMTLDQTPLFVWSVAITALLLL 80
Cdd:MTH00026 118 LVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRIPLFVWSVFITAILLL 197

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557  81 LSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYA 160
Cdd:MTH00026 198 LSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQILSLFSYKKQIFGYLGMVYA 277

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557 161 MLSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGT--KFKFNPPLLWALGFIFLFTIGGLT 238
Cdd:MTH00026 278 MLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSWLATVSGSgrNLIFTTPMAWALGFIFLFTIGGLT 357

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557 239 GLILANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLTMNNTWLKIQFTIMFIGVNLTFFPQHFLGLA 318
Cdd:MTH00026 358 GIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWFGKITGYAYKDIYGLIHFWLMFIGVNITFFPQHFLGLA 437

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 823078557 319 GMPRRYSDYPDAYTSWNVISSIGSTISIVGIIMFIMIMWES 359
Cdd:MTH00026 438 GLPRRYADYPDNFEDFNQISSFGSIISIIAVIWFIVVIFDA 478
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
2-364 3.44e-148

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 429.93  E-value: 3.44e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557   2 VDMGAGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGISSILGAVNFITTAINMRSESMTLDQTPLFVWSVAITALLLLL 81
Cdd:COG0843  120 VGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILL 199

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557  82 SLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKiESFGTLGMIYAM 161
Cdd:COG0843  200 AFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFSRK-PLFGYKAMVLAT 278

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557 162 LSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLI 241
Cdd:COG0843  279 VAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVM 358

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557 242 LANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLTMNNTWLKIQFTIMFIGVNLTFFPQHFLGLAGMP 321
Cdd:COG0843  359 LASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMP 438

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 823078557 322 RRYSDYP--DAYTSWNVISSIGSTISIVGIIMFIMIMWESMISNR 364
Cdd:COG0843  439 RRYATYPpePGWQPLNLISTIGAFILAVGFLLFLINLVVSLRKGP 483
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 2-384 6.39e-148

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: 427.80  E-value: 6.39e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557    2 VDMGAGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGISSILGAVNFITTAINMRSESMTLDQTPLFVWSVAITALLLLL 81
Cdd:TIGR02891 111 TGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLFVWGILVTSILILL 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557   82 SLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKiESFGTLGMIYAM 161
Cdd:TIGR02891 191 AFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFARK-PIFGYRAMVYAT 269

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557  162 LSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLI 241
Cdd:TIGR02891 270 VAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLFALGFIFLFVIGGLTGVM 349

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557  242 LANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLTMNNTWLKIQFTIMFIGVNLTFFPQHFLGLAGMP 321
Cdd:TIGR02891 350 LASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLGRWHFWLTFVGFNLTFFPMHLLGLLGMP 429

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 823078557  322 RRYSDYPDA--YTSWNVISSIGSTISIVGIIMFIMIMWESMISNRTVMFSINMPSSTEWLQNNPP 384
Cdd:TIGR02891 430 RRYYTYPPQmgFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGPKAGANPWGATTLEWTTSSPP 494
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 4-367 5.30e-133

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 390.19  E-value: 5.30e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557   4 MGAGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGISSILGAVNFITTAINMRSESMTLdQTPLFVWSVAITALLLLLSL 83
Cdd:MTH00048 119 LGAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNVFS-RTSIILWSYLFTSILLLLSL 197

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557  84 PVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKIESFGTLGMIYAMLS 163
Cdd:MTH00048 198 PVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPEVYVLILPGFGIISHICLSLSNNDDPFGYYGLVFAMFS 277

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557 164 IGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFKFNPPLL-WALGFIFLFTIGGLTGLIL 242
Cdd:MTH00048 278 IVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFSWLYMLLNSRVRKSDPVVwWVVSFIVLFTIGGVTGIVL 357

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557 243 ANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLTMNNTWLKIQFTIMFIGVNLTFFPQHFLGLAGMPR 322
Cdd:MTH00048 358 SASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWPLITGLSLNKYLLQCHCIISMIGFNLCFFPMHYFGLCGLPR 437

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 823078557 323 RYSDYPDAYTSWNVISSIGSTISIVGIIMFIMIMWESMISNRTVM 367
Cdd:MTH00048 438 RVCVYEPSYYWINVVCTVGSFISAFSGCFFVFILWESLVVKNEVL 482
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 2-360 2.92e-129

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: 380.39  E-value: 2.92e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557   2 VDMGAGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGISSILGAVNFITTAINMRSESMTLDQTPLFVWSVAITALLLLL 81
Cdd:cd01662  112 IGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWTTLVTSILILF 191

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557  82 SLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKiESFGTLGMIYAM 161
Cdd:cd01662  192 AFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYILILPAFGIFSEIVPTFSRK-PLFGYRSMVYAT 270

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557 162 LSIGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLI 241
Cdd:cd01662  271 VAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLFTMWRGRIRFETPMLWAIGFLVTFVIGGLTGVM 350

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557 242 LANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLTMNNTWLKIQFTIMFIGVNLTFFPQHFLGLAGMP 321
Cdd:cd01662  351 LASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRMLNERLGKWSFWLWFIGFNLTFFPMHILGLMGMP 430

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 823078557 322 RRYSDYP--DAYTSWNVISSIGSTISIVGIIMFIMIMWESM 360
Cdd:cd01662  431 RRVYTYLpgPGWDPLNLISTIGAFLIAAGVLLFLINVIVSI 471
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 4-326 9.52e-99

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: 300.26  E-value: 9.52e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557    4 MGAGTGWTVYPPLAGaiahggasVDLAIFSLHLAGISSILGAVNFITTAINMRSESMTLdQTPLFVWSVAITALLLLLSL 83
Cdd:pfam00115 103 GGATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATAILILLAF 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557   84 PVLAGAITMLLTDRNLNtsffdpAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKiESFGTLGMIYAMLS 163
Cdd:pfam00115 174 PVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGR-PLFGYKLSVLAFWL 246

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557  164 IGLMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFKFN-PPLLWALGFIFLFTIGGLTGLIL 242
Cdd:pfam00115 247 IAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFRtTPMLFFLGFAFLFIIGGLTGVML 326

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557  243 ANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLTMNNTWLKIQFTIMFIGVNLTFFPQHFLGLAGMPR 322
Cdd:pfam00115 327 ALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFWLLFIGFNLTFFPMHILGLLGMPR 406


                  ....
gi 823078557  323 RYSD 326
Cdd:pfam00115 407 RYAP 410
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 9-384 2.29e-81

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: 261.33  E-value: 2.29e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557    9 GWTVYPPLAGAIAHGGASVDLAIFSLHLAGISSILGAVNFITTAINMRSESMTLDQTPLFVWSVAITALLLLLSLPVLAG 88
Cdd:TIGR02882 162 GWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTLIIIFAFPVLTV 241

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557   89 AITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKiESFGTLGMIYAMLSIGLMG 168
Cdd:TIGR02882 242 ALALMTTDRIFDTAFFTVAHGGMPMLWANLFWIWGHPEVYIVILPAFGIYSEIISTFAQK-RLFGYKSMVWSTVGIAFLS 320

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557  169 FIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLILANSSLD 248
Cdd:TIGR02882 321 FLVWVHHFFTMGNGALINSFFSITTMAIAIPTGVKIFNWLLTLYKGKIRFTTPMLFSLAFIPNFLIGGVTGVMLAMASAD 400

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557  249 IILHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLTMNNTWLKIQFTIMFIGVNLTFFPQHFLGLAGMPRRYSDY- 327
Cdd:TIGR02882 401 YQYHNTYFLVAHFHYVLITGVVFACLAGLIYWYPKMFGYKLNERLGKWCFWFFMIGFNVCFFPMYILGLDGMPRRMYTYs 480

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 823078557  328 -PDAYTSWNVISSIGSTISIVGIIMFIM-IMWESMISNRTVMFSINMPSSTEWLQNNPP 384
Cdd:TIGR02882 481 pSDGWFPLNLISTIGALLMAIGFIFLVYnIYYSHRKSPREATGDPWNGRTLEWATASPP 539
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 6-384 2.60e-79

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 256.40  E-value: 2.60e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557   6 AGTGWTVYPPLAGAIAHGGASVDLAIFSLHLAGISSILGAVNFITTAINMRSESMTLDQTPLFVWSVAITALLLLLSLPV 85
Cdd:PRK15017 166 AQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPI 245

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557  86 LAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGKiESFGTLGMIYAMLSIG 165
Cdd:PRK15017 246 LTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWGHPEVYILILPVFGVFSEIAATFSRK-RLFGYTSLVWATVCIT 324

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557 166 LMGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLYGTKFKFNPPLLWALGFIFLFTIGGLTGLILANS 245
Cdd:PRK15017 325 VLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVKIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVP 404

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557 246 SLDIILHDTYYVVAHFHYVLSMGAVFAIMGGIIQWYPLFTGLTMNNTWLKIQFTIMFIGVNLTFFPQHFLGLAGMPRRYS 325
Cdd:PRK15017 405 GADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYWWPKAFGFKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMTRRLS 484

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 823078557 326 DYPD-AYTSWNVISSIGSTISIVGIIMFIMIMWESMIS---NRTVMFSINMPSSTEWLQNNPP 384
Cdd:PRK15017 485 QQIDpQFHTMLMIAASGAALIALGILCQVIQMYVSIRDrdqNRDLTGDPWGGRTLEWATSSPP 547
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
 111-360 3.24e-16

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: 80.02  E-value: 3.24e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557 111 DPILYQHLFWFFGHPEVYILILPGFGIISHIVCQESGkIESFGTLGMIYAMLSIGLMGFIVWAHHMFT-VGMDVDTRAYF 189
Cdd:cd01660  200 DVLLSRTLFWWFGHPLVYFWLLPAYIAWYTILPKIAG-GKLFSDPLARLAFILFLLFSTPVGFHHQFAdPGIGPGWKFIH 278

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557 190 TSATMIIAVPTGIKVFSWLATL-YGTKFKFNPPLLW---------------ALGFIFlFTIGGLTGLILANSSLDIILHD 253
Cdd:cd01660  279 MVLTFMVALPSLLTAFTVFASLeIAGRLRGGKGLFGwiralpwgdpmflalFLAMLM-FIPGGAGGIINASYQLNYVVHN 357

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 823078557 254 TYYVVAHFHyvLSMGAVFAIMG-GIIQWY-PLFTGLTMNNTWL-KIQFTIMFIGVNLTFFPQHFLGLAGMPRR--YSDYP 328
Cdd:cd01660  358 TAWVPGHFH--LTVGGAVALTFmAVAYWLvPHLTGRELAAKRLaLAQPWLWFVGMTIMSTAMHVAGLLGAPRRtaEAQYG 435

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 823078557 329 DAY-----TSWNVISSIGSTISIVGIIMFIMIMWESM 360
Cdd:cd01660  436 GLPaagewAPYQQLMAIGGTILFVSGALFLYILFRTL 472
 
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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