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Conserved domains on  [gi|1942342710|gb|QPP47632|]
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cytochrome c oxidase subunit I, partial (mitochondrion) [Pseudagrion microcephalum]

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 ...
 1-354 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: 708.56  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710   1 VVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLASSLVESGAGTGWTVYPPLAGAI 80
Cdd:MTH00153   55 IVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNI 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710  81 AHAGGSVDLTIFSLHLAGVSSILGAINFITTTINMKSPGMKMDQMPLFVWAVVITAVLLLLSLPVLAGAITMLLTDRNIN 160
Cdd:MTH00153  135 AHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLN 214

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710 161 TSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIIAQESGKKETFGVLGMIYAMIAIGILGFVVWAHHMFTVG 240
Cdd:MTH00153  215 TSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVG 294

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710 241 MDVDTRAYFTSATMVIAVPTGIKIFSWLATLHGSQLNYSPSLLWALGFVFLFTVGGLTGVVLANSSIDISMHDTYYVVAH 320
Cdd:MTH00153  295 MDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAH 374

                         330       340       350
                  ....*....|....*....|....*....|....
gi 1942342710 321 FHYVLSMGAVFAIMGGLIHWFPLFTGTTMNSQLL 354
Cdd:MTH00153  375 FHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWL 408
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-354 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 708.56  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710   1 VVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLASSLVESGAGTGWTVYPPLAGAI 80
Cdd:MTH00153   55 IVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNI 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710  81 AHAGGSVDLTIFSLHLAGVSSILGAINFITTTINMKSPGMKMDQMPLFVWAVVITAVLLLLSLPVLAGAITMLLTDRNIN 160
Cdd:MTH00153  135 AHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLN 214

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710 161 TSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIIAQESGKKETFGVLGMIYAMIAIGILGFVVWAHHMFTVG 240
Cdd:MTH00153  215 TSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVG 294

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710 241 MDVDTRAYFTSATMVIAVPTGIKIFSWLATLHGSQLNYSPSLLWALGFVFLFTVGGLTGVVLANSSIDISMHDTYYVVAH 320
Cdd:MTH00153  295 MDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAH 374

                         330       340       350
                  ....*....|....*....|....*....|....
gi 1942342710 321 FHYVLSMGAVFAIMGGLIHWFPLFTGTTMNSQLL 354
Cdd:MTH00153  375 FHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWL 408
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-354 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: 641.84  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710   1 VVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLASSLVESGAGTGWTVYPPLAGAI 80
Cdd:cd01663    48 IVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSIL 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710  81 AHAGGSVDLTIFSLHLAGVSSILGAINFITTTINMKSPGMKMDQMPLFVWAVVITAVLLLLSLPVLAGAITMLLTDRNIN 160
Cdd:cd01663   128 AHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFN 207

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710 161 TSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIIAQESGKKETFGVLGMIYAMIAIGILGFVVWAHHMFTVG 240
Cdd:cd01663   208 TSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVG 287

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710 241 MDVDTRAYFTSATMVIAVPTGIKIFSWLATLHGSQLNYSPSLLWALGFVFLFTVGGLTGVVLANSSIDISMHDTYYVVAH 320
Cdd:cd01663   288 LDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAH 367

                         330       340       350
                  ....*....|....*....|....*....|....
gi 1942342710 321 FHYVLSMGAVFAIMGGLIHWFPLFTGTTMNSQLL 354
Cdd:cd01663   368 FHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLG 401
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-353 5.59e-146

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 423.00  E-value: 5.59e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710   1 VVTAHAFVMIFFMVMPiMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLASSLVESGAGTGWTVYPPLAGAI 80
Cdd:COG0843    60 LFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLE 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710  81 AHAGGSVDLTIFSLHLAGVSSILGAINFITTTINMKSPGMKMDQMPLFVWAVVITAVLLLLSLPVLAGAITMLLTDRNIN 160
Cdd:COG0843   139 ASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLG 218

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710 161 TSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIIAQESGKKeTFGVLGMIYAMIAIGILGFVVWAHHMFTVG 240
Cdd:COG0843   219 THFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPG 297

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710 241 MDVDTRAYFTSATMVIAVPTGIKIFSWLATLHGSQLNYSPSLLWALGFVFLFTVGGLTGVVLANSSIDISMHDTYYVVAH 320
Cdd:COG0843   298 ISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAH 377

                         330       340       350
                  ....*....|....*....|....*....|...
gi 1942342710 321 FHYVLSMGAVFAIMGGLIHWFPLFTGTTMNSQL 353
Cdd:COG0843   378 FHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERL 410
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-353 1.04e-144

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: 418.55  E-value: 1.04e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710   1 VVTAHAFVMIFFMVMPIMiGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLASSLVESGAGTGWTVYPPLAGAI 80
Cdd:TIGR02891  51 LFTMHGTIMIFLFAIPIL-AGFGNYLLPLMIGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTS 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710  81 AHAGGSVDLTIFSLHLAGVSSILGAINFITTTINMKSPGMKMDQMPLFVWAVVITAVLLLLSLPVLAGAITMLLTDRNIN 160
Cdd:TIGR02891 130 GSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFG 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710 161 TSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIIAQESGKKeTFGVLGMIYAMIAIGILGFVVWAHHMFTVG 240
Cdd:TIGR02891 210 THFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFARKP-IFGYRAMVYATVAIGFLSFGVWAHHMFTTG 288

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710 241 MDVDTRAYFTSATMVIAVPTGIKIFSWLATLHGSQLNYSPSLLWALGFVFLFTVGGLTGVVLANSSIDISMHDTYYVVAH 320
Cdd:TIGR02891 289 MPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAH 368

                         330       340       350
                  ....*....|....*....|....*....|...
gi 1942342710 321 FHYVLSMGAVFAIMGGLIHWFPLFTGTTMNSQL 353
Cdd:TIGR02891 369 FHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERL 401
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-353 2.20e-95

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: 290.24  E-value: 2.20e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710   1 VVTAHAFVMIFFMVMPiMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLASSLvesGAGTGWTVYPPLAGai 80
Cdd:pfam00115  44 LRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALSFWLVVLGAVLLLASFG---GATTGWTEYPPLVG-- 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710  81 ahaggsVDLTIFSLHLAGVSSILGAINFITTTINMKSPGMKMdQMPLFVWAVVITAVLLLLSLPVLAGAITMLLTDRNIN 160
Cdd:pfam00115 118 ------VDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710 161 tsffdpAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIIAQESGKKeTFGVLGMIYAMIAIGILGFVVWAHHMFTVG 240
Cdd:pfam00115 191 ------AGGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGRP-LFGYKLSVLAFWLIAFLGFLVWAHHLFTTG 263

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710 241 MDVDTRAYFTSATMVIAVPTGIKIFSWLATLHGSQLN-YSPSLLWALGFVFLFTVGGLTGVVLANSSIDISMHDTYYVVA 319
Cdd:pfam00115 264 LPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRfRTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVA 343

                         330       340       350
                  ....*....|....*....|....*....|....
gi 1942342710 320 HFHYVLSMGAVFAIMGGLIHWFPLFTGTTMNSQL 353
Cdd:pfam00115 344 HFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKL 377
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-354 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 708.56  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710   1 VVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLASSLVESGAGTGWTVYPPLAGAI 80
Cdd:MTH00153   55 IVTAHAFIMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNI 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710  81 AHAGGSVDLTIFSLHLAGVSSILGAINFITTTINMKSPGMKMDQMPLFVWAVVITAVLLLLSLPVLAGAITMLLTDRNIN 160
Cdd:MTH00153  135 AHSGASVDLAIFSLHLAGISSILGAINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLN 214

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710 161 TSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIIAQESGKKETFGVLGMIYAMIAIGILGFVVWAHHMFTVG 240
Cdd:MTH00153  215 TSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVG 294

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710 241 MDVDTRAYFTSATMVIAVPTGIKIFSWLATLHGSQLNYSPSLLWALGFVFLFTVGGLTGVVLANSSIDISMHDTYYVVAH 320
Cdd:MTH00153  295 MDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAH 374

                         330       340       350
                  ....*....|....*....|....*....|....
gi 1942342710 321 FHYVLSMGAVFAIMGGLIHWFPLFTGTTMNSQLL 354
Cdd:MTH00153  375 FHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWL 408
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-354 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: 641.84  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710   1 VVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLASSLVESGAGTGWTVYPPLAGAI 80
Cdd:cd01663    48 IVTAHALIMIFFMVMPALIGGFGNWLVPLMIGAPDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSIL 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710  81 AHAGGSVDLTIFSLHLAGVSSILGAINFITTTINMKSPGMKMDQMPLFVWAVVITAVLLLLSLPVLAGAITMLLTDRNIN 160
Cdd:cd01663   128 AHSGPSVDLAIFSLHLAGISSILGAINFITTIFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFN 207

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710 161 TSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIIAQESGKKETFGVLGMIYAMIAIGILGFVVWAHHMFTVG 240
Cdd:cd01663   208 TSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVG 287

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710 241 MDVDTRAYFTSATMVIAVPTGIKIFSWLATLHGSQLNYSPSLLWALGFVFLFTVGGLTGVVLANSSIDISMHDTYYVVAH 320
Cdd:cd01663   288 LDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAH 367

                         330       340       350
                  ....*....|....*....|....*....|....
gi 1942342710 321 FHYVLSMGAVFAIMGGLIHWFPLFTGTTMNSQLL 354
Cdd:cd01663   368 FHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLG 401
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-353 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 604.75  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710   1 VVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLASSLVESGAGTGWTVYPPLAGAI 80
Cdd:MTH00167   57 IVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNL 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710  81 AHAGGSVDLTIFSLHLAGVSSILGAINFITTTINMKSPGMKMDQMPLFVWAVVITAVLLLLSLPVLAGAITMLLTDRNIN 160
Cdd:MTH00167  137 AHAGASVDLAIFSLHLAGVSSILGSINFITTIINMKPPGITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLN 216

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710 161 TSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIIAQESGKKETFGVLGMIYAMIAIGILGFVVWAHHMFTVG 240
Cdd:MTH00167  217 TTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVVYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVG 296

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710 241 MDVDTRAYFTSATMVIAVPTGIKIFSWLATLHGSQLNYSPSLLWALGFVFLFTVGGLTGVVLANSSIDISMHDTYYVVAH 320
Cdd:MTH00167  297 MDVDTRAYFTSATMIIAVPTGIKVFSWLATLHGGKIKWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAH 376

                         330       340       350
                  ....*....|....*....|....*....|...
gi 1942342710 321 FHYVLSMGAVFAIMGGLIHWFPLFTGTTMNSQL 353
Cdd:MTH00167  377 FHYVLSMGAVFAIMAGFTHWFPLFTGLTLNETW 409
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-353 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 604.39  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710   1 VVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLASSLVESGAGTGWTVYPPLAGAI 80
Cdd:MTH00116   57 IVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNL 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710  81 AHAGGSVDLTIFSLHLAGVSSILGAINFITTTINMKSPGMKMDQMPLFVWAVVITAVLLLLSLPVLAGAITMLLTDRNIN 160
Cdd:MTH00116  137 AHAGASVDLAIFSLHLAGVSSILGAINFITTCINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLN 216

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710 161 TSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIIAQESGKKETFGVLGMIYAMIAIGILGFVVWAHHMFTVG 240
Cdd:MTH00116  217 TTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVG 296

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710 241 MDVDTRAYFTSATMVIAVPTGIKIFSWLATLHGSQLNYSPSLLWALGFVFLFTVGGLTGVVLANSSIDISMHDTYYVVAH 320
Cdd:MTH00116  297 MDVDTRAYFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAH 376

                         330       340       350
                  ....*....|....*....|....*....|...
gi 1942342710 321 FHYVLSMGAVFAIMGGLIHWFPLFTGTTMNSQL 353
Cdd:MTH00116  377 FHYVLSMGAVFAIMAGFTHWFPLFTGYTLHQTW 409
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-354 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 597.86  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710   1 VVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLASSLVESGAGTGWTVYPPLAGAI 80
Cdd:MTH00142   55 IVTAHAFVMIFFMVMPVMIGGFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNL 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710  81 AHAGGSVDLTIFSLHLAGVSSILGAINFITTTINMKSPGMKMDQMPLFVWAVVITAVLLLLSLPVLAGAITMLLTDRNIN 160
Cdd:MTH00142  135 AHSGGSVDLAIFSLHLAGVSSILGAINFITTVINMRAGGMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFN 214

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710 161 TSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIIAQESGKKETFGVLGMIYAMIAIGILGFVVWAHHMFTVG 240
Cdd:MTH00142  215 TSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIINHYSGKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVG 294

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710 241 MDVDTRAYFTSATMVIAVPTGIKIFSWLATLHGSQLNYSPSLLWALGFVFLFTVGGLTGVVLANSSIDISMHDTYYVVAH 320
Cdd:MTH00142  295 MDVDTRAYFTAATMVIAVPTGIKVFSWLATLHGSKVKYEPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAH 374

                         330       340       350
                  ....*....|....*....|....*....|....
gi 1942342710 321 FHYVLSMGAVFAIMGGLIHWFPLFTGTTMNSQLL 354
Cdd:MTH00142  375 FHYVLSMGAVFALFAGFIHWFPLFTGLTLNPRWL 408
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-352 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 595.42  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710   1 VVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLASSLVESGAGTGWTVYPPLAGAI 80
Cdd:MTH00223   54 IVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNL 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710  81 AHAGGSVDLTIFSLHLAGVSSILGAINFITTTINMKSPGMKMDQMPLFVWAVVITAVLLLLSLPVLAGAITMLLTDRNIN 160
Cdd:MTH00223  134 AHAGPSVDLAIFSLHLAGVSSILGAINFITTIINMRSPGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFN 213

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710 161 TSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIIAQESGKKETFGVLGMIYAMIAIGILGFVVWAHHMFTVG 240
Cdd:MTH00223  214 TSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSSKKEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVG 293

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710 241 MDVDTRAYFTSATMVIAVPTGIKIFSWLATLHGSQLNYSPSLLWALGFVFLFTVGGLTGVVLANSSIDISMHDTYYVVAH 320
Cdd:MTH00223  294 MDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGSKIKYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAH 373

                         330       340       350
                  ....*....|....*....|....*....|..
gi 1942342710 321 FHYVLSMGAVFAIMGGLIHWFPLFTGTTMNSQ 352
Cdd:MTH00223  374 FHYVLSMGAVFALFAGFNHWFPLFTGVTLHRR 405
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-351 0e+00

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 544.86  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710   1 VVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLASSLVESGAGTGWTVYPPLAGAI 80
Cdd:MTH00103   57 IVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNL 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710  81 AHAGGSVDLTIFSLHLAGVSSILGAINFITTTINMKSPGMKMDQMPLFVWAVVITAVLLLLSLPVLAGAITMLLTDRNIN 160
Cdd:MTH00103  137 AHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLN 216

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710 161 TSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIIAQESGKKETFGVLGMIYAMIAIGILGFVVWAHHMFTVG 240
Cdd:MTH00103  217 TTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVG 296

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710 241 MDVDTRAYFTSATMVIAVPTGIKIFSWLATLHGSQLNYSPSLLWALGFVFLFTVGGLTGVVLANSSIDISMHDTYYVVAH 320
Cdd:MTH00103  297 MDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGNIKWSPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAH 376

                         330       340       350
                  ....*....|....*....|....*....|.
gi 1942342710 321 FHYVLSMGAVFAIMGGLIHWFPLFTGTTMNS 351
Cdd:MTH00103  377 FHYVLSMGAVFAIMGGFVHWFPLFSGYTLND 407
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-353 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 540.96  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710   1 VVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLASSLVESGAGTGWTVYPPLAGAI 80
Cdd:MTH00037   57 IVTAHALVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNI 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710  81 AHAGGSVDLTIFSLHLAGVSSILGAINFITTTINMKSPGMKMDQMPLFVWAVVITAVLLLLSLPVLAGAITMLLTDRNIN 160
Cdd:MTH00037  137 AHAGGSVDLAIFSLHLAGASSILASINFITTIINMRTPGMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNIN 216

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710 161 TSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIIAQESGKKETFGVLGMIYAMIAIGILGFVVWAHHMFTVG 240
Cdd:MTH00037  217 TTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKQEPFGYLGMVYAMIAIGILGFLVWAHHMFTVG 296

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710 241 MDVDTRAYFTSATMVIAVPTGIKIFSWLATLHGSQLNYSPSLLWALGFVFLFTVGGLTGVVLANSSIDISMHDTYYVVAH 320
Cdd:MTH00037  297 MDVDTRAYFTAATMIIAVPTGIKVFSWMATLQGSNLRWETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAH 376

                         330       340       350
                  ....*....|....*....|....*....|...
gi 1942342710 321 FHYVLSMGAVFAIMGGLIHWFPLFTGTTMNSQL 353
Cdd:MTH00037  377 FHYVLSMGAVFAIFAGFTHWFPLFSGVSLHPLW 409
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-351 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 539.90  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710   1 VVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLASSLVESGAGTGWTVYPPLAGAI 80
Cdd:MTH00183   57 IVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNL 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710  81 AHAGGSVDLTIFSLHLAGVSSILGAINFITTTINMKSPGMKMDQMPLFVWAVVITAVLLLLSLPVLAGAITMLLTDRNIN 160
Cdd:MTH00183  137 AHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLN 216

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710 161 TSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIIAQESGKKETFGVLGMIYAMIAIGILGFVVWAHHMFTVG 240
Cdd:MTH00183  217 TTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVG 296

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710 241 MDVDTRAYFTSATMVIAVPTGIKIFSWLATLHGSQLNYSPSLLWALGFVFLFTVGGLTGVVLANSSIDISMHDTYYVVAH 320
Cdd:MTH00183  297 MDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAH 376

                         330       340       350
                  ....*....|....*....|....*....|.
gi 1942342710 321 FHYVLSMGAVFAIMGGLIHWFPLFTGTTMNS 351
Cdd:MTH00183  377 FHYVLSMGAVFAIMAAFVHWFPLFSGYTLHS 407
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-352 0e+00

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 530.24  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710   1 VVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLASSLVESGAGTGWTVYPPLAGAI 80
Cdd:MTH00007   54 IVTAHAFLMIFFLVMPVFIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNL 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710  81 AHAGGSVDLTIFSLHLAGVSSILGAINFITTTINMKSPGMKMDQMPLFVWAVVITAVLLLLSLPVLAGAITMLLTDRNIN 160
Cdd:MTH00007  134 AHAGPSVDLAIFSLHLAGVSSILGAINFITTVINMRWKGLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLN 213

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710 161 TSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIIAQESGKKETFGVLGMIYAMIAIGILGFVVWAHHMFTVG 240
Cdd:MTH00007  214 TSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGAISHIVTHYAGKLEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVG 293

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710 241 MDVDTRAYFTSATMVIAVPTGIKIFSWLATLHGSQLNYSPSLLWALGFVFLFTVGGLTGVVLANSSIDISMHDTYYVVAH 320
Cdd:MTH00007  294 MDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGSPIKYETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAH 373

                         330       340       350
                  ....*....|....*....|....*....|..
gi 1942342710 321 FHYVLSMGAVFAIMGGLIHWFPLFTGTTMNSQ 352
Cdd:MTH00007  374 FHYVLSMGAVFAIFAAFNHWFPLFTGLTLHDR 405
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-351 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 528.36  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710   1 VVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLASSLVESGAGTGWTVYPPLAGAI 80
Cdd:MTH00077   57 IVTAHAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNL 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710  81 AHAGGSVDLTIFSLHLAGVSSILGAINFITTTINMKSPGMKMDQMPLFVWAVVITAVLLLLSLPVLAGAITMLLTDRNIN 160
Cdd:MTH00077  137 AHAGASVDLTIFSLHLAGVSSILGAINFITTSINMKPPSMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLN 216

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710 161 TSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIIAQESGKKETFGVLGMIYAMIAIGILGFVVWAHHMFTVG 240
Cdd:MTH00077  217 TTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISHIVTYYSAKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVD 296

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710 241 MDVDTRAYFTSATMVIAVPTGIKIFSWLATLHGSQLNYSPSLLWALGFVFLFTVGGLTGVVLANSSIDISMHDTYYVVAH 320
Cdd:MTH00077  297 LNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGAIKWDAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAH 376

                         330       340       350
                  ....*....|....*....|....*....|.
gi 1942342710 321 FHYVLSMGAVFAIMGGLIHWFPLFTGTTMNS 351
Cdd:MTH00077  377 FHYVLSMGAVFAIMGGFVHWFPLFSGYTLHS 407
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-354 8.77e-180

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 508.07  E-value: 8.77e-180
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710   1 VVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLASSLVESGAGTGWTVYPPLAgAI 80
Cdd:MTH00079   58 VITAHAILMIFFMVMPSMIGGFGNWMLPLMLGAPDMSFPRLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLS-TL 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710  81 AHAGGSVDLTIFSLHLAGVSSILGAINFITTTINMKSPGMKMDQMPLFVWAVVITAVLLLLSLPVLAGAITMLLTDRNIN 160
Cdd:MTH00079  137 GHPGSSVDLAIFSLHCAGISSILGGINFMVTTKNLRSSSISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLN 216

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710 161 TSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIIAQESGKKETFGVLGMIYAMIAIGILGFVVWAHHMFTVG 240
Cdd:MTH00079  217 TSFFDPSTGGNPLLYQHLFWFFGHPEVYILILPAFGIISQSTLYLTGKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVG 296

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710 241 MDVDTRAYFTSATMVIAVPTGIKIFSWLATLHGSQLNYSPSLLWALGFVFLFTVGGLTGVVLANSSIDISMHDTYYVVAH 320
Cdd:MTH00079  297 MDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMKFQPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSH 376

                         330       340       350
                  ....*....|....*....|....*....|....
gi 1942342710 321 FHYVLSMGAVFAIMGGLIHWFPLFTGTTMNSQLL 354
Cdd:MTH00079  377 FHYVLSLGAVFGIFTGISLWWPFMTGIVYDKLMM 410
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-350 6.34e-178

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 503.97  E-value: 6.34e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710   1 VVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLASSLVESGAGTGWTVYPPLAGAI 80
Cdd:MTH00182   59 IVTAHAFIMIFFLVMPVMIGGFGNWLVPLYIGAPDMAFPRLNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQ 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710  81 AHAGGSVDLTIFSLHLAGVSSILGAINFITTTINMKSPGMKMDQMPLFVWAVVITAVLLLLSLPVLAGAITMLLTDRNIN 160
Cdd:MTH00182  139 AHSGGAVDMAIFSLHLAGVSSILGAINFITTIFNMRAPGVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFN 218

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710 161 TSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIIAQESGKKETFGVLGMIYAMIAIGILGFVVWAHHMFTVG 240
Cdd:MTH00182  219 TTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISQIIPTFVAKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVG 298

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710 241 MDVDTRAYFTSATMVIAVPTGIKIFSWLATLHGSQLNYSPSLLWALGFVFLFTVGGLTGVVLANSSIDISMHDTYYVVAH 320
Cdd:MTH00182  299 MDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGGTLRLDTPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAH 378

                         330       340       350
                  ....*....|....*....|....*....|
gi 1942342710 321 FHYVLSMGAVFAIMGGLIHWFPLFTGTTMN 350
Cdd:MTH00182  379 FHYVLSMGAVFAIFGGFYYWFGKITGYCYN 408
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-350 1.16e-173

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 492.80  E-value: 1.16e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710   1 VVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLASSLVESGAGTGWTVYPPLAGAI 80
Cdd:MTH00184   59 IVTAHAFVMIFFLVMPVMIGGFGNWFVPLYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQ 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710  81 AHAGGSVDLTIFSLHLAGVSSILGAINFITTTINMKSPGMKMDQMPLFVWAVVITAVLLLLSLPVLAGAITMLLTDRNIN 160
Cdd:MTH00184  139 AHSGGSVDMAIFSLHLAGISSILGAMNFITTIFNMRAPGITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFN 218

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710 161 TSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIIAQESGKKETFGVLGMIYAMIAIGILGFVVWAHHMFTVG 240
Cdd:MTH00184  219 TTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVG 298

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710 241 MDVDTRAYFTSATMVIAVPTGIKIFSWLATLHGSQLNYSPSLLWALGFVFLFTVGGLTGVVLANSSIDISMHDTYYVVAH 320
Cdd:MTH00184  299 MDVDTRAYFTAATMIIAVPTGIKIFSWIATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAH 378

                         330       340       350
                  ....*....|....*....|....*....|
gi 1942342710 321 FHYVLSMGAVFAIMGGLIHWFPLFTGTTMN 350
Cdd:MTH00184  379 FHYVLSMGAVFAIFGGFYYWFGKITGYCYN 408
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-346 1.10e-156

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 450.23  E-value: 1.10e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710   1 VVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLASSLVESGAGTGWTVYPPLAGAI 80
Cdd:MTH00026   58 IVTAHAFVMIFFLVMPTMIGGFGNWFVPLMIGAPDMAFPRLNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQ 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710  81 AHAGGSVDLTIFSLHLAGVSSILGAINFITTTINMKSPGMKMDQMPLFVWAVVITAVLLLLSLPVLAGAITMLLTDRNIN 160
Cdd:MTH00026  138 AHSGGSVDMAIFSLHLAGLSSILGAMNFITTVMNMRTPGMTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFN 217

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710 161 TSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIIAQESGKKETFGVLGMIYAMIAIGILGFVVWAHHMFTVG 240
Cdd:MTH00026  218 TTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQILSLFSYKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVG 297

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710 241 MDVDTRAYFTSATMVIAVPTGIKIFSWLATLHGSQLN--YSPSLLWALGFVFLFTVGGLTGVVLANSSIDISMHDTYYVV 318
Cdd:MTH00026  298 MDVDTRAYFTAATMIIAVPTGIKIFSWLATVSGSGRNliFTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVV 377

                         330       340
                  ....*....|....*....|....*...
gi 1942342710 319 AHFHYVLSMGAVFAIMGGLIHWFPLFTG 346
Cdd:MTH00026  378 AHFHFVLSMGAVFAIFGGFYLWFGKITG 405
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-353 5.57e-151

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: 433.11  E-value: 5.57e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710   1 VVTAHAFVMIFFMVMPIMIGGFGNWLVPlMLGAPDMAFPRLNNMSFWLLPPSLTLLLASSLVESGAGTGWTVYPPLAGAI 80
Cdd:cd00919    46 LVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARDLAFPRLNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLS 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710  81 AHAGGSVDLTIFSLHLAGVSSILGAINFITTTINMKSPGMKMDQMPLFVWAVVITAVLLLLSLPVLAGAITMLLTDRNIN 160
Cdd:cd00919   125 YSSGVGVDLAILGLHLAGVSSILGAINFITTILNMRAPGMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFG 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710 161 TSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIIAQESGKKeTFGVLGMIYAMIAIGILGFVVWAHHMFTVG 240
Cdd:cd00919   205 TSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAFGAISEIIPTFSGKP-LFGYKLMVYAFLAIGFLSFLVWAHHMFTVG 283

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710 241 MDVDTRAYFTSATMVIAVPTGIKIFSWLATLHGSQLNYSPSLLWALGFVFLFTVGGLTGVVLANSSIDISMHDTYYVVAH 320
Cdd:cd00919   284 LPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGRIRFDPPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAH 363

                         330       340       350
                  ....*....|....*....|....*....|...
gi 1942342710 321 FHYVLSMGAVFAIMGGLIHWFPLFTGTTMNSQL 353
Cdd:cd00919   364 FHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKL 396
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-353 5.59e-146

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 423.00  E-value: 5.59e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710   1 VVTAHAFVMIFFMVMPiMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLASSLVESGAGTGWTVYPPLAGAI 80
Cdd:COG0843    60 LFTMHGTIMIFFFATP-FLAGFGNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLE 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710  81 AHAGGSVDLTIFSLHLAGVSSILGAINFITTTINMKSPGMKMDQMPLFVWAVVITAVLLLLSLPVLAGAITMLLTDRNIN 160
Cdd:COG0843   139 ASPGVGVDLWLLGLALFGVGSILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLG 218

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710 161 TSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIIAQESGKKeTFGVLGMIYAMIAIGILGFVVWAHHMFTVG 240
Cdd:COG0843   219 THFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPG 297

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710 241 MDVDTRAYFTSATMVIAVPTGIKIFSWLATLHGSQLNYSPSLLWALGFVFLFTVGGLTGVVLANSSIDISMHDTYYVVAH 320
Cdd:COG0843   298 ISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAH 377

                         330       340       350
                  ....*....|....*....|....*....|...
gi 1942342710 321 FHYVLSMGAVFAIMGGLIHWFPLFTGTTMNSQL 353
Cdd:COG0843   378 FHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERL 410
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-353 1.04e-144

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: 418.55  E-value: 1.04e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710   1 VVTAHAFVMIFFMVMPIMiGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLASSLVESGAGTGWTVYPPLAGAI 80
Cdd:TIGR02891  51 LFTMHGTIMIFLFAIPIL-AGFGNYLLPLMIGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTS 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710  81 AHAGGSVDLTIFSLHLAGVSSILGAINFITTTINMKSPGMKMDQMPLFVWAVVITAVLLLLSLPVLAGAITMLLTDRNIN 160
Cdd:TIGR02891 130 GSPGVGVDLWLLGLHLLGISSILGAVNFIVTILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFG 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710 161 TSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIIAQESGKKeTFGVLGMIYAMIAIGILGFVVWAHHMFTVG 240
Cdd:TIGR02891 210 THFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFARKP-IFGYRAMVYATVAIGFLSFGVWAHHMFTTG 288

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710 241 MDVDTRAYFTSATMVIAVPTGIKIFSWLATLHGSQLNYSPSLLWALGFVFLFTVGGLTGVVLANSSIDISMHDTYYVVAH 320
Cdd:TIGR02891 289 MPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAH 368

                         330       340       350
                  ....*....|....*....|....*....|...
gi 1942342710 321 FHYVLSMGAVFAIMGGLIHWFPLFTGTTMNSQL 353
Cdd:TIGR02891 369 FHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERL 401
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 1-354 6.42e-132

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 386.34  E-value: 6.42e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710   1 VVTAHAFVMIFFMVMPIMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLASSLVesGAGTGWTVYPPLAGAI 80
Cdd:MTH00048   58 LITNHGIIMIFFFLMPVLIGGFGNYLLPLLLGLSDLNLPRLNALSAWLLVPSIVFLLLSMCL--GAGVGWTFYPPLSSSL 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710  81 AHAGGSVDLTIFSLHLAGVSSILGAINFITTTINMKSPGMkMDQMPLFVWAVVITAVLLLLSLPVLAGAITMLLTDRNIN 160
Cdd:MTH00048  136 FSSSWGVDFLMFSLHLAGVSSLFGSINFICTIYSAFMTNV-FSRTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFG 214

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710 161 TSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIIAQESGKKETFGVLGMIYAMIAIGILGFVVWAHHMFTVG 240
Cdd:MTH00048  215 SAFFDPLGGGDPVLFQHMFWFFGHPEVYVLILPGFGIISHICLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVG 294

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710 241 MDVDTRAYFTSATMVIAVPTGIKIFSWLATLHGSQLNYS-PSLLWALGFVFLFTVGGLTGVVLANSSIDISMHDTYYVVA 319
Cdd:MTH00048  295 LDVKTAVFFSSVTMIIGVPTGIKVFSWLYMLLNSRVRKSdPVVWWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVA 374

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1942342710 320 HFHYVLSMGAVFAIMGGLIHWFPLFTGTTMNSQLL 354
Cdd:MTH00048  375 HFHYVLSLGSYSSVVIMFIWWWPLITGLSLNKYLL 409
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 3-353 9.05e-130

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: 9.05e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710   3 TAHAFVMIFFMVMPIMIGgFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLASSLVESGAGTGWTVYPPLAGAIAH 82
Cdd:cd01662    54 TMHGTIMIFLFAMPLVFG-LMNYLVPLQIGARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYS 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710  83 AGGSVDLTIFSLHLAGVSSILGAINFITTTINMKSPGMKMDQMPLFVWAVVITAVLLLLSLPVLAGAITMLLTDRNINTS 162
Cdd:cd01662   133 PGVGVDYWILGLQFSGIGTLLGAINFIVTILKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTH 212

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710 163 FFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIIAQESGKKeTFGVLGMIYAMIAIGILGFVVWAHHMFTVGMD 242
Cdd:cd01662   213 FFTNALGGNPMLWQHLFWIFGHPEVYILILPAFGIFSEIVPTFSRKP-LFGYRSMVYATVAIGFLSFGVWVHHMFTTGAG 291

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710 243 VDTRAYFTSATMVIAVPTGIKIFSWLATLHGSQLNYSPSLLWALGFVFLFTVGGLTGVVLANSSIDISMHDTYYVVAHFH 322
Cdd:cd01662   292 ALVNAFFSIATMIIAVPTGVKIFNWLFTMWRGRIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFH 371

                         330       340       350
                  ....*....|....*....|....*....|.
gi 1942342710 323 YVLSMGAVFAIMGGLIHWFPLFTGTTMNSQL 353
Cdd:cd01662   372 YVLIGGVVFPLFAGFYYWFPKMFGRMLNERL 402
CyoB TIGR02843
cytochrome o ubiquinol oxidase, subunit I; Cytochrome o terminal oxidase complex is the ...
 1-353 2.08e-101

cytochrome o ubiquinol oxidase, subunit I; Cytochrome o terminal oxidase complex is the component of the aerobic respiratory chain which reacts with oxygen, reducing it to water with the concomitant transport of 4 protons across the membrane. Also known as the cytochrome bo complex, cytochrome o ubiquinol oxidase contains four subunits, two heme b cofactors and a copper atom which is believed to be the oxygen active site. This complex is structurally related to the cytochrome caa3 oxidases which utilize cytochrome c as the reductant and contain heme a cofactors, as well as the intermediate form aa3 oxidases which also react directly with quinones as the reductant. [Energy metabolism, Electron transport]


Pssm-ID: 131890  Cd Length: 646  Bit Score: 312.38  E-value: 2.08e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710   1 VVTAHAFVMIFFMVMPIMIGGFgNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLASSLVESGAGTGWTVYPPLAGAI 80
Cdd:TIGR02843 101 IFTAHGVIMIFFVAMPFVFGLM-NLVVPLQIGARDVAFPFLNSLSFWLTVVGAILVNVSLGVGEFAQTGWLAYPPLSELQ 179

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710  81 AHAGGSVDLTIFSLHLAGVSSILGAINFITTTINMKSPGMKMDQMPLFVWAVVITAVLLLLSLPVLAGAITMLLTDRNIN 160
Cdd:TIGR02843 180 YSPGVGVDYYIWALQISGIGTLLTGINFFVTIIKMRAPGMTLMKMPVFTWTSLCSNVLIIASFPILTVTLALLTLDRYLG 259

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710 161 TSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIIAQESGKKeTFGVLGMIYAMIAIGILGFVVWAHHMFTVG 240
Cdd:TIGR02843 260 MHFFTNEAGGNPMMYVNLIWAWGHPEVYILILPAFGIFSEVVATFSRKR-LFGYTSMVWATIAITVLSFIVWLHHFFTMG 338

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710 241 MDVDTRAYFTSATMVIAVPTGIKIFSWLATLHGSQLNYSPSLLWALGFVFLFTVGGLTGVVLANSSIDISMHDTYYVVAH 320
Cdd:TIGR02843 339 AGANVNAFFGIATMIIAIPTGVKIFNWLFTMYKGRIRFETPMLWTIGFMVTFSIGGMTGVLLAVPPADFVLHNSLFLIAH 418

                         330       340       350
                  ....*....|....*....|....*....|...
gi 1942342710 321 FHYVLSMGAVFAIMGGLIHWFPLFTGTTMNSQL 353
Cdd:TIGR02843 419 FHNVIIGGVVFGCFAGLTYWFPKAFGFKLNEKL 451
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-353 2.20e-95

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: 290.24  E-value: 2.20e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710   1 VVTAHAFVMIFFMVMPiMIGGFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLASSLvesGAGTGWTVYPPLAGai 80
Cdd:pfam00115  44 LRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMAFPRLNALSFWLVVLGAVLLLASFG---GATTGWTEYPPLVG-- 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710  81 ahaggsVDLTIFSLHLAGVSSILGAINFITTTINMKSPGMKMdQMPLFVWAVVITAVLLLLSLPVLAGAITMLLTDRNIN 160
Cdd:pfam00115 118 ------VDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710 161 tsffdpAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIIAQESGKKeTFGVLGMIYAMIAIGILGFVVWAHHMFTVG 240
Cdd:pfam00115 191 ------AGGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGRP-LFGYKLSVLAFWLIAFLGFLVWAHHLFTTG 263

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710 241 MDVDTRAYFTSATMVIAVPTGIKIFSWLATLHGSQLN-YSPSLLWALGFVFLFTVGGLTGVVLANSSIDISMHDTYYVVA 319
Cdd:pfam00115 264 LPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRfRTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVA 343

                         330       340       350
                  ....*....|....*....|....*....|....
gi 1942342710 320 HFHYVLSMGAVFAIMGGLIHWFPLFTGTTMNSQL 353
Cdd:pfam00115 344 HFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKL 377
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 1-350 7.23e-90

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 282.98  E-value: 7.23e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710   1 VVTAHAFVMIFFMVMPIMIGgFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLASSLVESGAGTGWTVYPPLAGAI 80
Cdd:PRK15017  102 IFTAHGVIMIFFVAMPFVIG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLSGIE 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710  81 AHAGGSVDLTIFSLHLAGVSSILGAINFITTTINMKSPGMKMDQMPLFVWAVVITAVLLLLSLPVLAGAITMLLTDRNIN 160
Cdd:PRK15017  181 YSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDRYLG 260

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710 161 TSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIIAQESgKKETFGVLGMIYAMIAIGILGFVVWAHHMFTVG 240
Cdd:PRK15017  261 THFFTNDMGGNMMMYINLIWAWGHPEVYILILPVFGVFSEIAATFS-RKRLFGYTSLVWATVCITVLSFIVWLHHFFTMG 339

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710 241 MDVDTRAYFTSATMVIAVPTGIKIFSWLATLHGSQLNYSPSLLWALGFVFLFTVGGLTGVVLANSSIDISMHDTYYVVAH 320
Cdd:PRK15017  340 AGANVNAFFGITTMIIAIPTGVKIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAH 419

                         330       340       350
                  ....*....|....*....|....*....|
gi 1942342710 321 FHYVLSMGAVFAIMGGLIHWFPLFTGTTMN 350
Cdd:PRK15017  420 FHNVIIGGVVFGCFAGMTYWWPKAFGFKLN 449
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 1-353 1.67e-87

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: 276.35  E-value: 1.67e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710   1 VVTAHAFVMIFFMVMPIMIGgFGNWLVPLMLGAPDMAFPRLNNMSFWLLPPSLTLLLASSLVESGAGTGWTVYPPLAGAI 80
Cdd:TIGR02882  95 IFTTHGVIMIIFMAMPFIIG-LMNIVVPLQIGARDVAFPVLNALSFWLFFAGAMLFNISFVIGGSPDAGWTNYAPLAGPE 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710  81 AHAGGSVDLTIFSLHLAGVSSILGAINFITTTINMKSPGMKMDQMPLFVWAVVITAVLLLLSLPVLAGAITMLLTDRNIN 160
Cdd:TIGR02882 174 FSPGVGVNYYLIALQISGIGTLMTGINFFVTILKMRAPGMKLMQMPMFTWTTLITTLIIIFAFPVLTVALALMTTDRIFD 253

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710 161 TSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIIAQESgKKETFGVLGMIYAMIAIGILGFVVWAHHMFTVG 240
Cdd:TIGR02882 254 TAFFTVAHGGMPMLWANLFWIWGHPEVYIVILPAFGIYSEIISTFA-QKRLFGYKSMVWSTVGIAFLSFLVWVHHFFTMG 332

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710 241 MDVDTRAYFTSATMVIAVPTGIKIFSWLATLHGSQLNYSPSLLWALGFVFLFTVGGLTGVVLANSSIDISMHDTYYVVAH 320
Cdd:TIGR02882 333 NGALINSFFSITTMAIAIPTGVKIFNWLLTLYKGKIRFTTPMLFSLAFIPNFLIGGVTGVMLAMASADYQYHNTYFLVAH 412

                         330       340       350
                  ....*....|....*....|....*....|...
gi 1942342710 321 FHYVLSMGAVFAIMGGLIHWFPLFTGTTMNSQL 353
Cdd:TIGR02882 413 FHYVLITGVVFACLAGLIYWYPKMFGYKLNERL 445
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
 1-346 2.92e-09

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: 58.07  E-value: 2.92e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710   1 VVTAHAFVM-IFFMVMPIMigGFGNWLVPLMLGAPDMAfPRLNNMSFWLLPPSLTLLLASSlVESGAGTGWTVYPPLaga 79
Cdd:cd01660    47 GLTLHGVLLaIVFTTFFIM--GFFYAIVARALLRSLFN-RRLAWAGFWLMVIGTVMAAVPI-LLGQASVLYTFYPPL--- 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710  80 IAHAGGSVDLTIFSLHlagvSSILGAINFITTTINMKS-PGMKMdqmPLFVWAVVITAVLLLLSLPVLAGAITMLLtdrn 158
Cdd:cd01660   120 QAHPLFYIGAALVVVG----SWISGFAMFVTLWRWKKAnPGKKV---PLATFMVVTTMILWLVASLGVALEVLFQL---- 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710 159 INTSFFDpAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIIAQESGKKeTFGVLGMIYAMIAIGILGFVVWAHHMFT 238
Cdd:cd01660   189 LPWSLGL-VDTVDVLLSRTLFWWFGHPLVYFWLLPAYIAWYTILPKIAGGK-LFSDPLARLAFILFLLFSTPVGFHHQFA 266

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1942342710 239 -VGMDVDTRAYFTSATMVIAVPTGIKIFSWLATL-HGSQLNYSPSLLW---------------ALGFVFlFTVGGLTGVV 301
Cdd:cd01660   267 dPGIGPGWKFIHMVLTFMVALPSLLTAFTVFASLeIAGRLRGGKGLFGwiralpwgdpmflalFLAMLM-FIPGGAGGII 345

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 1942342710 302 LANSSIDISMHDTYYVVAHFHyvLSMGAVFAIMG-GLIHWF-PLFTG 346
Cdd:cd01660   346 NASYQLNYVVHNTAWVPGHFH--LTVGGAVALTFmAVAYWLvPHLTG 390
 
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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