NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1904806543|ref|YP_009919792|]
View 

Cox1 (mitochondrion) [Metschnikowia agaves]

Protein Classification

cytochrome c oxidase subunit 1( domain architecture ID 10108859)

cytochrome c oxidase subunit 1 is the catalytic subunit of cytochrome c oxidase, which is the component of the respiratory chain that catalyzes the reduction of oxygen to water

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 11-453 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: 651.09  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543  11 TSHKDMAMLYLGYGLMSSMVATWMSVMMRMELSGPNPQYlyGNNQVYNVLVTGHAMAMMFLFVMPVLMGAFGNYFLPMLM 90
Cdd:cd01663     1 TNHKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQL--GNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543  91 GAVDMAFARLNNMSFWCLPPALVCMMASVLMEQGAGTG-NCYPPLSSINAHSGPSVDLAMFALHLTSMSSLLGAMNFMVT 169
Cdd:cd01663    79 GAPDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGwTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITT 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 170 FINMRTMGLHMVNAPLFVWAMFMTAMLLLLSLPVLTAGVTLLLMDRNFNTGFYEVAAGGDPVTYEHLFWFFGHPEVYMMI 249
Cdd:cd01663   159 IFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILI 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 250 MPGFGMMSHIVSTYS-KKPMFGEMGMLYAMGSMGLLGFLVWSHHMYVVGLDIDSRAYFTSATMVMAVPTGMKMFSWMATM 328
Cdd:cd01663   239 LPGFGIISHIISTFSgKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATM 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 329 YGGEVRLAVPMLFALGFLFLFTMGGLTGVMLSNASMDVAFHDTYYVVGHFHYVLSMGALFSLVGGYYYWGPSMFGLNYNK 408
Cdd:cd01663   319 WGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNE 398

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*
gi 1904806543 409 VWAEIHFWLLFMSVNLIFLPMHFLGTNGMPRRIPQYPDAFIGWNY 453
Cdd:cd01663   399 TLGKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNM 443
 
Name Accession Description Interval E-value
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 11-453 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: 651.09  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543  11 TSHKDMAMLYLGYGLMSSMVATWMSVMMRMELSGPNPQYlyGNNQVYNVLVTGHAMAMMFLFVMPVLMGAFGNYFLPMLM 90
Cdd:cd01663     1 TNHKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQL--GNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543  91 GAVDMAFARLNNMSFWCLPPALVCMMASVLMEQGAGTG-NCYPPLSSINAHSGPSVDLAMFALHLTSMSSLLGAMNFMVT 169
Cdd:cd01663    79 GAPDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGwTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITT 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 170 FINMRTMGLHMVNAPLFVWAMFMTAMLLLLSLPVLTAGVTLLLMDRNFNTGFYEVAAGGDPVTYEHLFWFFGHPEVYMMI 249
Cdd:cd01663   159 IFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILI 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 250 MPGFGMMSHIVSTYS-KKPMFGEMGMLYAMGSMGLLGFLVWSHHMYVVGLDIDSRAYFTSATMVMAVPTGMKMFSWMATM 328
Cdd:cd01663   239 LPGFGIISHIISTFSgKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATM 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 329 YGGEVRLAVPMLFALGFLFLFTMGGLTGVMLSNASMDVAFHDTYYVVGHFHYVLSMGALFSLVGGYYYWGPSMFGLNYNK 408
Cdd:cd01663   319 WGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNE 398

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*
gi 1904806543 409 VWAEIHFWLLFMSVNLIFLPMHFLGTNGMPRRIPQYPDAFIGWNY 453
Cdd:cd01663   399 TLGKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNM 443
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 4-452 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 587.99  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543   4 MTRWLYSTSHKDMAMLYLGYGLMSSMVATWMSVMMRMELSgpNPQYLYGNNQVYNVLVTGHAMAMMFLFVMPVLMGAFGN 83
Cdd:MTH00153    1 MNKWLFSTNHKDIGTLYFIFGAWSGMVGTSLSLLIRAELG--QPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGN 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543  84 YFLPMLMGAVDMAFARLNNMSFWCLPPALVCMMASVLMEQGAGTG-NCYPPLSSINAHSGPSVDLAMFALHLTSMSSLLG 162
Cdd:MTH00153   79 WLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGwTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILG 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 163 AMNFMVTFINMRTMGLHMVNAPLFVWAMFMTAMLLLLSLPVLTAGVTLLLMDRNFNTGFYEVAAGGDPVTYEHLFWFFGH 242
Cdd:MTH00153  159 AINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGH 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 243 PEVYMMIMPGFGMMSHIVSTYS-KKPMFGEMGMLYAMGSMGLLGFLVWSHHMYVVGLDIDSRAYFTSATMVMAVPTGMKM 321
Cdd:MTH00153  239 PEVYILILPGFGMISHIISQESgKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKI 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 322 FSWMATMYGGEVRLAVPMLFALGFLFLFTMGGLTGVMLSNASMDVAFHDTYYVVGHFHYVLSMGALFSLVGGYYYWGPSM 401
Cdd:MTH00153  319 FSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLF 398

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1904806543 402 FGLNYNKVWAEIHFWLLFMSVNLIFLPMHFLGTNGMPRRIPQYPDAFIGWN 452
Cdd:MTH00153  399 TGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWN 449
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 8-453 6.81e-161

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: 466.70  E-value: 6.81e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543   8 LYSTSHKDMAMLYLGYGLMSSMVATWMSVMMRMELSGPNPQYLygNNQVYNVLVTGHAMAMMFLFVMPvLMGAFGNYFLP 87
Cdd:TIGR02891   1 LTTVDHKRIGILYLVTAFAFFLVGGVLALLMRAQLATPGNTFM--DAETYNQLFTMHGTIMIFLFAIP-ILAGFGNYLLP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543  88 MLMGAVDMAFARLNNMSFWCLPPALVCMMASVLMEQGAGTG-NCYPPLSSINAHSGPSVDLAMFALHLTSMSSLLGAMNF 166
Cdd:TIGR02891  78 LMIGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGwTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNF 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 167 MVTFINMRTMGLHMVNAPLFVWAMFMTAMLLLLSLPVLTAGVTLLLMDRNFNTGFYEVAAGGDPVTYEHLFWFFGHPEVY 246
Cdd:TIGR02891 158 IVTILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVY 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 247 MMIMPGFGMMSHIVSTYSKKPMFGEMGMLYAMGSMGLLGFLVWSHHMYVVGLDIDSRAYFTSATMVMAVPTGMKMFSWMA 326
Cdd:TIGR02891 238 IIFLPAFGIISEILPTFARKPIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIA 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 327 TMYGGEVRLAVPMLFALGFLFLFTMGGLTGVMLSNASMDVAFHDTYYVVGHFHYVLSMGALFSLVGGYYYWGPSMFGLNY 406
Cdd:TIGR02891 318 TLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMY 397

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*....
gi 1904806543 407 NKVWAEIHFWLLFMSVNLIFLPMHFLGTNGMPRRIPQYPDA--FIGWNY 453
Cdd:TIGR02891 398 NERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNL 446
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
2-452 8.86e-157

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 457.67  E-value: 8.86e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543   2 SYMTRWLYSTSHKDMAMLYLGYGLMSSMVATWMSVMMRMELSGPNPQYLygNNQVYNVLVTGHAMAMMFLFVMPvLMGAF 81
Cdd:COG0843     4 SGWRRWLTTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLL--SPETYNQLFTMHGTIMIFFFATP-FLAGF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543  82 GNYFLPMLMGAVDMAFARLNNMSFWCLPPALVCMMASVLMEQGAGTG-NCYPPLSSINAHSGPSVDLAMFALHLTSMSSL 160
Cdd:COG0843    81 GNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGwTFYPPLSGLEASPGVGVDLWLLGLALFGVGSI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 161 LGAMNFMVTFINMRTMGLHMVNAPLFVWAMFMTAMLLLLSLPVLTAGVTLLLMDRNFNTGFYEVAAGGDPVTYEHLFWFF 240
Cdd:COG0843   161 LGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFF 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 241 GHPEVYMMIMPGFGMMSHIVSTYSKKPMFGEMGMLYAMGSMGLLGFLVWSHHMYVVGLDIDSRAYFTSATMVMAVPTGMK 320
Cdd:COG0843   241 GHPEVYILILPAFGIVSEIIPTFSRKPLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVK 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 321 MFSWMATMYGGEVRLAVPMLFALGFLFLFTMGGLTGVMLSNASMDVAFHDTYYVVGHFHYVLSMGALFSLVGGYYYWGPS 400
Cdd:COG0843   321 VFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPK 400

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1904806543 401 MFGLNYNKVWAEIHFWLLFMSVNLIFLPMHFLGTNGMPRRIPQYP--DAFIGWN 452
Cdd:COG0843   401 MTGRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLN 454
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 15-452 1.11e-113

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: 343.79  E-value: 1.11e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543  15 DMAMLYLGYGLMSSMVATWMSVMMRMELSGPNPQYLygNNQVYNVLVTGHAMAMMFLFVMPVLMGaFGNYFLPMLMGAVD 94
Cdd:pfam00115   1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFL--SPLTYNQLRTLHGNLMIFWFATPFLFG-FGNYLVPLMIGARD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543  95 MAFARLNNMSFWCLPPALVCMMASVLMEQGAGTGncYPPLssinahsgPSVDLAMFALHLTSMSSLLGAMNFMVTFINMR 174
Cdd:pfam00115  78 MAFPRLNALSFWLVVLGAVLLLASFGGATTGWTE--YPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRR 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 175 TMGLHMvNAPLFVWAMFMTAMLLLLSLPVLTAGVTLLLMDRNFNTGfyevaaGGDPVTYEHLFWFFGHPEVYMMIMPGFG 254
Cdd:pfam00115 148 APGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLGAG------GGDPLLDQHLFWWFGHPEVYILILPAFG 220

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 255 MMSHIVSTYSKKPMFGEMGMLYAMGSMGLLGFLVWSHHMYVVGLDIDSRAYFTSATMVMAVPTGMKMFSWMATMYGGEVR 334
Cdd:pfam00115 221 IIYYILPKFAGRPLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIR 300

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 335 LA-VPMLFALGFLFLFTMGGLTGVMLSNASMDVAFHDTYYVVGHFHYVLSMGALFSLVGGYYYWGPSMFGLNYNKVWAEI 413
Cdd:pfam00115 301 FRtTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKL 380

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 1904806543 414 HFWLLFMSVNLIFLPMHFLGTNGMPRRIP----QYPDAFIGWN 452
Cdd:pfam00115 381 HFWLLFIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPLN 423
 
Name Accession Description Interval E-value
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 11-453 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: 651.09  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543  11 TSHKDMAMLYLGYGLMSSMVATWMSVMMRMELSGPNPQYlyGNNQVYNVLVTGHAMAMMFLFVMPVLMGAFGNYFLPMLM 90
Cdd:cd01663     1 TNHKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQL--GNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543  91 GAVDMAFARLNNMSFWCLPPALVCMMASVLMEQGAGTG-NCYPPLSSINAHSGPSVDLAMFALHLTSMSSLLGAMNFMVT 169
Cdd:cd01663    79 GAPDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGwTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITT 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 170 FINMRTMGLHMVNAPLFVWAMFMTAMLLLLSLPVLTAGVTLLLMDRNFNTGFYEVAAGGDPVTYEHLFWFFGHPEVYMMI 249
Cdd:cd01663   159 IFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILI 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 250 MPGFGMMSHIVSTYS-KKPMFGEMGMLYAMGSMGLLGFLVWSHHMYVVGLDIDSRAYFTSATMVMAVPTGMKMFSWMATM 328
Cdd:cd01663   239 LPGFGIISHIISTFSgKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATM 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 329 YGGEVRLAVPMLFALGFLFLFTMGGLTGVMLSNASMDVAFHDTYYVVGHFHYVLSMGALFSLVGGYYYWGPSMFGLNYNK 408
Cdd:cd01663   319 WGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNE 398

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*
gi 1904806543 409 VWAEIHFWLLFMSVNLIFLPMHFLGTNGMPRRIPQYPDAFIGWNY 453
Cdd:cd01663   399 TLGKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNM 443
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 4-452 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 587.99  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543   4 MTRWLYSTSHKDMAMLYLGYGLMSSMVATWMSVMMRMELSgpNPQYLYGNNQVYNVLVTGHAMAMMFLFVMPVLMGAFGN 83
Cdd:MTH00153    1 MNKWLFSTNHKDIGTLYFIFGAWSGMVGTSLSLLIRAELG--QPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGN 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543  84 YFLPMLMGAVDMAFARLNNMSFWCLPPALVCMMASVLMEQGAGTG-NCYPPLSSINAHSGPSVDLAMFALHLTSMSSLLG 162
Cdd:MTH00153   79 WLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGwTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILG 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 163 AMNFMVTFINMRTMGLHMVNAPLFVWAMFMTAMLLLLSLPVLTAGVTLLLMDRNFNTGFYEVAAGGDPVTYEHLFWFFGH 242
Cdd:MTH00153  159 AINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGH 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 243 PEVYMMIMPGFGMMSHIVSTYS-KKPMFGEMGMLYAMGSMGLLGFLVWSHHMYVVGLDIDSRAYFTSATMVMAVPTGMKM 321
Cdd:MTH00153  239 PEVYILILPGFGMISHIISQESgKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKI 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 322 FSWMATMYGGEVRLAVPMLFALGFLFLFTMGGLTGVMLSNASMDVAFHDTYYVVGHFHYVLSMGALFSLVGGYYYWGPSM 401
Cdd:MTH00153  319 FSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLF 398

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1904806543 402 FGLNYNKVWAEIHFWLLFMSVNLIFLPMHFLGTNGMPRRIPQYPDAFIGWN 452
Cdd:MTH00153  399 TGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWN 449
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 3-452 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 572.78  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543   3 YMTRWLYSTSHKDMAMLYLGYGLMSSMVATWMSVMMRMELSGPNPqyLYGNNQVYNVLVTGHAMAMMFLFVMPVLMGAFG 82
Cdd:MTH00167    2 WINRWLFSTNHKDIGTLYFIFGAWAGMVGTALSLLIRAELSQPGS--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543  83 NYFLPMLMGAVDMAFARLNNMSFWCLPPALVCMMASVLMEQGAGTG-NCYPPLSSINAHSGPSVDLAMFALHLTSMSSLL 161
Cdd:MTH00167   80 NWLVPLMIGAPDMAFPRMNNMSFWLLPPSLLLLLASSGVEAGAGTGwTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSIL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 162 GAMNFMVTFINMRTMGLHMVNAPLFVWAMFMTAMLLLLSLPVLTAGVTLLLMDRNFNTGFYEVAAGGDPVTYEHLFWFFG 241
Cdd:MTH00167  160 GSINFITTIINMKPPGITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFG 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 242 HPEVYMMIMPGFGMMSHIVSTYS-KKPMFGEMGMLYAMGSMGLLGFLVWSHHMYVVGLDIDSRAYFTSATMVMAVPTGMK 320
Cdd:MTH00167  240 HPEVYILILPGFGMISHIVVYYSgKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIK 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 321 MFSWMATMYGGEVRLAVPMLFALGFLFLFTMGGLTGVMLSNASMDVAFHDTYYVVGHFHYVLSMGALFSLVGGYYYWGPS 400
Cdd:MTH00167  320 VFSWLATLHGGKIKWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPL 399

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1904806543 401 MFGLNYNKVWAEIHFWLLFMSVNLIFLPMHFLGTNGMPRRIPQYPDAFIGWN 452
Cdd:MTH00167  400 FTGLTLNETWTKIHFFVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWN 451
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 6-452 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 566.53  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543   6 RWLYSTSHKDMAMLYLGYGLMSSMVATWMSVMMRMELSgpNPQYLYGNNQVYNVLVTGHAMAMMFLFVMPVLMGAFGNYF 85
Cdd:MTH00223    2 RWLFSTNHKDIGTLYLIFGMWSGLVGTSLSLLIRAELG--QPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543  86 LPMLMGAVDMAFARLNNMSFWCLPPALVCMMASVLMEQGAGTG-NCYPPLSSINAHSGPSVDLAMFALHLTSMSSLLGAM 164
Cdd:MTH00223   80 VPLMLGAPDMAFPRLNNMSFWLLPPSLYLLLSSSAVESGVGTGwTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAI 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 165 NFMVTFINMRTMGLHMVNAPLFVWAMFMTAMLLLLSLPVLTAGVTLLLMDRNFNTGFYEVAAGGDPVTYEHLFWFFGHPE 244
Cdd:MTH00223  160 NFITTIINMRSPGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPE 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 245 VYMMIMPGFGMMSHIVSTYS-KKPMFGEMGMLYAMGSMGLLGFLVWSHHMYVVGLDIDSRAYFTSATMVMAVPTGMKMFS 323
Cdd:MTH00223  240 VYILILPGFGMISHIVSHYSsKKEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFS 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 324 WMATMYGGEVRLAVPMLFALGFLFLFTMGGLTGVMLSNASMDVAFHDTYYVVGHFHYVLSMGALFSLVGGYYYWGPSMFG 403
Cdd:MTH00223  320 WLATIYGSKIKYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLFTG 399

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*....
gi 1904806543 404 LNYNKVWAEIHFWLLFMSVNLIFLPMHFLGTNGMPRRIPQYPDAFIGWN 452
Cdd:MTH00223  400 VTLHRRWAKAHFFLMFLGVNLTFFPQHFLGLAGMPRRYSDYPDCYTKWN 448
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 2-452 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 558.17  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543   2 SYMTRWLYSTSHKDMAMLYLGYGLMSSMVATWMSVMMRMELSGPNPqyLYGNNQVYNVLVTGHAMAMMFLFVMPVLMGAF 81
Cdd:MTH00116    1 MFITRWLFSTNHKDIGTLYLIFGAWAGMVGTALSLLIRAELGQPGT--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543  82 GNYFLPMLMGAVDMAFARLNNMSFWCLPPALVCMMASVLMEQGAGTG-NCYPPLSSINAHSGPSVDLAMFALHLTSMSSL 160
Cdd:MTH00116   79 GNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGwTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSI 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 161 LGAMNFMVTFINMRTMGLHMVNAPLFVWAMFMTAMLLLLSLPVLTAGVTLLLMDRNFNTGFYEVAAGGDPVTYEHLFWFF 240
Cdd:MTH00116  159 LGAINFITTCINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFF 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 241 GHPEVYMMIMPGFGMMSHIVSTYS-KKPMFGEMGMLYAMGSMGLLGFLVWSHHMYVVGLDIDSRAYFTSATMVMAVPTGM 319
Cdd:MTH00116  239 GHPEVYILILPGFGIISHIVTYYAgKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGI 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 320 KMFSWMATMYGGEVRLAVPMLFALGFLFLFTMGGLTGVMLSNASMDVAFHDTYYVVGHFHYVLSMGALFSLVGGYYYWGP 399
Cdd:MTH00116  319 KVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFP 398

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1904806543 400 SMFGLNYNKVWAEIHFWLLFMSVNLIFLPMHFLGTNGMPRRIPQYPDAFIGWN 452
Cdd:MTH00116  399 LFTGYTLHQTWTKAQFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWN 451
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 4-452 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 548.17  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543   4 MTRWLYSTSHKDMAMLYLGYGLMSSMVATWMSVMMRMELSGPNPqyLYGNNQVYNVLVTGHAMAMMFLFVMPVLMGAFGN 83
Cdd:MTH00142    1 MMRWLFSTNHKDIGTLYFLFGAWAGMVGTGLSLLIRAELGQPGS--LLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGN 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543  84 YFLPMLMGAVDMAFARLNNMSFWCLPPALVCMMASVLMEQGAGTG-NCYPPLSSINAHSGPSVDLAMFALHLTSMSSLLG 162
Cdd:MTH00142   79 WLVPLMLGAPDMAFPRMNNMSFWLLPPALLLLLSSAAVESGAGTGwTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILG 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 163 AMNFMVTFINMRTMGLHMVNAPLFVWAMFMTAMLLLLSLPVLTAGVTLLLMDRNFNTGFYEVAAGGDPVTYEHLFWFFGH 242
Cdd:MTH00142  159 AINFITTVINMRAGGMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGH 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 243 PEVYMMIMPGFGMMSHIVSTYS-KKPMFGEMGMLYAMGSMGLLGFLVWSHHMYVVGLDIDSRAYFTSATMVMAVPTGMKM 321
Cdd:MTH00142  239 PEVYILILPGFGMISHIINHYSgKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKV 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 322 FSWMATMYGGEVRLAVPMLFALGFLFLFTMGGLTGVMLSNASMDVAFHDTYYVVGHFHYVLSMGALFSLVGGYYYWGPSM 401
Cdd:MTH00142  319 FSWLATLHGSKVKYEPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLF 398

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1904806543 402 FGLNYNKVWAEIHFWLLFMSVNLIFLPMHFLGTNGMPRRIPQYPDAFIGWN 452
Cdd:MTH00142  399 TGLTLNPRWLKAHFYTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWN 449
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-452 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 524.01  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543   1 MSYMTRWLYSTSHKDMAMLYLGYGLMSSMVATWMSVMMRMELSGPNPqyLYGNNQVYNVLVTGHAMAMMFLFVMPVLMGA 80
Cdd:MTH00184    2 SLYLSRWLFSTNHKDIGTLYLLFGAFAGMIGTAFSMLIRLELSAPGS--MLGDDHLYNVIVTAHAFVMIFFLVMPVMIGG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543  81 FGNYFLPMLMGAVDMAFARLNNMSFWCLPPALVCMMASVLMEQGAGTG-NCYPPLSSINAHSGPSVDLAMFALHLTSMSS 159
Cdd:MTH00184   80 FGNWFVPLYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGAGTGwTVYPPLSSIQAHSGGSVDMAIFSLHLAGISS 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 160 LLGAMNFMVTFINMRTMGLHMVNAPLFVWAMFMTAMLLLLSLPVLTAGVTLLLMDRNFNTGFYEVAAGGDPVTYEHLFWF 239
Cdd:MTH00184  160 ILGAMNFITTIFNMRAPGITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWF 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 240 FGHPEVYMMIMPGFGMMSHIVSTYS-KKPMFGEMGMLYAMGSMGLLGFLVWSHHMYVVGLDIDSRAYFTSATMVMAVPTG 318
Cdd:MTH00184  240 FGHPEVYILILPGFGIISQIIPTFAaKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTG 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 319 MKMFSWMATMYGGEVRLAVPMLFALGFLFLFTMGGLTGVMLSNASMDVAFHDTYYVVGHFHYVLSMGALFSLVGGYYYWG 398
Cdd:MTH00184  320 IKIFSWIATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWF 399

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1904806543 399 PSMFGLNYNKVWAEIHFWLLFMSVNLIFLPMHFLGTNGMPRRIPQYPDAFIGWN 452
Cdd:MTH00184  400 GKITGYCYNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDSFAGWN 453
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 2-452 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 520.15  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543   2 SYMTRWLYSTSHKDMAMLYLGYGLMSSMVATWMSVMMRMELSGPNPqyLYGNNQVYNVLVTGHAMAMMFLFVMPVLMGAF 81
Cdd:MTH00182    3 LYLTRWVFSTNHKDIGTLYLVFGAGAGMIGTAFSMLIRLELSAPGA--MLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543  82 GNYFLPMLMGAVDMAFARLNNMSFWCLPPALVCMMASVLMEQGAGTG-NCYPPLSSINAHSGPSVDLAMFALHLTSMSSL 160
Cdd:MTH00182   81 GNWLVPLYIGAPDMAFPRLNNISFWLLPPALILLLGSAFVEQGAGTGwTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 161 LGAMNFMVTFINMRTMGLHMVNAPLFVWAMFMTAMLLLLSLPVLTAGVTLLLMDRNFNTGFYEVAAGGDPVTYEHLFWFF 240
Cdd:MTH00182  161 LGAINFITTIFNMRAPGVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFF 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 241 GHPEVYMMIMPGFGMMSHIVSTYS-KKPMFGEMGMLYAMGSMGLLGFLVWSHHMYVVGLDIDSRAYFTSATMVMAVPTGM 319
Cdd:MTH00182  241 GHPEVYILILPGFGMISQIIPTFVaKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGI 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 320 KMFSWMATMYGGEVRLAVPMLFALGFLFLFTMGGLTGVMLSNASMDVAFHDTYYVVGHFHYVLSMGALFSLVGGYYYWGP 399
Cdd:MTH00182  321 KVFSWLATIYGGTLRLDTPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFG 400

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1904806543 400 SMFGLNYNKVWAEIHFWLLFMSVNLIFLPMHFLGTNGMPRRIPQYPDAFIGWN 452
Cdd:MTH00182  401 KITGYCYNELYGKIHFWLMFIGVNLTFFPQHFLGLAGFPRRYSDFADAFAGWN 453
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 6-452 1.14e-177

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 510.21  E-value: 1.14e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543   6 RWLYSTSHKDMAMLYLGYGLMSSMVATWMSVMMRMELSGPNPqyLYGNNQVYNVLVTGHAMAMMFLFVMPVLMGAFGNYF 85
Cdd:MTH00007    2 RWLYSTNHKDIGTLYFILGVWGGLLGTSMSLLIRIELGQPGA--FLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543  86 LPMLMGAVDMAFARLNNMSFWCLPPALVCMMASVLMEQGAGTG-NCYPPLSSINAHSGPSVDLAMFALHLTSMSSLLGAM 164
Cdd:MTH00007   80 VPLMLGAPDMAFPRLNNMSFWLLPPALILLVSSAAVEKGVGTGwTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAI 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 165 NFMVTFINMRTMGLHMVNAPLFVWAMFMTAMLLLLSLPVLTAGVTLLLMDRNFNTGFYEVAAGGDPVTYEHLFWFFGHPE 244
Cdd:MTH00007  160 NFITTVINMRWKGLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPE 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 245 VYMMIMPGFGMMSHIVSTYSKKPM-FGEMGMLYAMGSMGLLGFLVWSHHMYVVGLDIDSRAYFTSATMVMAVPTGMKMFS 323
Cdd:MTH00007  240 VYILILPGFGAISHIVTHYAGKLEpFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFS 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 324 WMATMYGGEVRLAVPMLFALGFLFLFTMGGLTGVMLSNASMDVAFHDTYYVVGHFHYVLSMGALFSLVGGYYYWGPSMFG 403
Cdd:MTH00007  320 WLATIHGSPIKYETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTG 399

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*....
gi 1904806543 404 LNYNKVWAEIHFWLLFMSVNLIFLPMHFLGTNGMPRRIPQYPDAFIGWN 452
Cdd:MTH00007  400 LTLHDRWAKAHFFLMFLGVNLTFFPQHFLGLSGMPRRYSDYPDAYTKWN 448
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 4-452 2.46e-177

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 509.46  E-value: 2.46e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543   4 MTRWLYSTSHKDMAMLYLGYGLMSSMVATWMSVMMRMELSGPNPqyLYGNNQVYNVLVTGHAMAMMFLFVMPVLMGAFGN 83
Cdd:MTH00183    3 ITRWFFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGA--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543  84 YFLPMLMGAVDMAFARLNNMSFWCLPPALVCMMASVLMEQGAGTG-NCYPPLSSINAHSGPSVDLAMFALHLTSMSSLLG 162
Cdd:MTH00183   81 WLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGwTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 163 AMNFMVTFINMRTMGLHMVNAPLFVWAMFMTAMLLLLSLPVLTAGVTLLLMDRNFNTGFYEVAAGGDPVTYEHLFWFFGH 242
Cdd:MTH00183  161 AINFITTIINMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGH 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 243 PEVYMMIMPGFGMMSHIVSTYS-KKPMFGEMGMLYAMGSMGLLGFLVWSHHMYVVGLDIDSRAYFTSATMVMAVPTGMKM 321
Cdd:MTH00183  241 PEVYILILPGFGMISHIVAYYSgKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKV 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 322 FSWMATMYGGEVRLAVPMLFALGFLFLFTMGGLTGVMLSNASMDVAFHDTYYVVGHFHYVLSMGALFSLVGGYYYWGPSM 401
Cdd:MTH00183  321 FSWLATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLF 400

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1904806543 402 FGLNYNKVWAEIHFWLLFMSVNLIFLPMHFLGTNGMPRRIPQYPDAFIGWN 452
Cdd:MTH00183  401 SGYTLHSTWTKIHFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWN 451
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 4-522 3.01e-177

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 509.10  E-value: 3.01e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543   4 MTRWLYSTSHKDMAMLYLGYGLMSSMVATWMSVMMRMELSGPNPqyLYGNNQVYNVLVTGHAMAMMFLFVMPVLMGAFGN 83
Cdd:MTH00077    3 ITRWLFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGT--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543  84 YFLPMLMGAVDMAFARLNNMSFWCLPPALVCMMASVLMEQGAGTG-NCYPPLSSINAHSGPSVDLAMFALHLTSMSSLLG 162
Cdd:MTH00077   81 WLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGwTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 163 AMNFMVTFINMRTMGLHMVNAPLFVWAMFMTAMLLLLSLPVLTAGVTLLLMDRNFNTGFYEVAAGGDPVTYEHLFWFFGH 242
Cdd:MTH00077  161 AINFITTSINMKPPSMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGH 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 243 PEVYMMIMPGFGMMSHIVSTYS-KKPMFGEMGMLYAMGSMGLLGFLVWSHHMYVVGLDIDSRAYFTSATMVMAVPTGMKM 321
Cdd:MTH00077  241 PEVYILILPGFGMISHIVTYYSaKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKV 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 322 FSWMATMYGGEVRLAVPMLFALGFLFLFTMGGLTGVMLSNASMDVAFHDTYYVVGHFHYVLSMGALFSLVGGYYYWGPSM 401
Cdd:MTH00077  321 FSWLATMHGGAIKWDAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLF 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 402 FGLNYNKVWAEIHFWLLFMSVNLIFLPMHFLGTNGMPRRIPQYPDAFIGWNYISSIGSTISIISVLVGLKSV-EIQLNNG 480
Cdd:MTH00077  401 SGYTLHSTWSKIHFGVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMMMFIIwEAFSSKR 480

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|..
gi 1904806543 481 LNHNTELQMTpdylesnltrltrdsDIELILSRPAEYHTFSE 522
Cdd:MTH00077  481 EVLTTELTST---------------NIEWLHGCPPPYHTFEE 507
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 3-452 4.79e-175

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 503.65  E-value: 4.79e-175
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543   3 YMTRWLYSTSHKDMAMLYLGYGLMSSMVATWMSVMMRMELSGPNPqyLYGNNQVYNVLVTGHAMAMMFLFVMPVLMGAFG 82
Cdd:MTH00103    2 FINRWLFSTNHKDIGTLYLLFGAWAGMVGTALSLLIRAELGQPGT--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543  83 NYFLPMLMGAVDMAFARLNNMSFWCLPPALVCMMASVLMEQGAGTG-NCYPPLSSINAHSGPSVDLAMFALHLTSMSSLL 161
Cdd:MTH00103   80 NWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGwTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSIL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 162 GAMNFMVTFINMRTMGLHMVNAPLFVWAMFMTAMLLLLSLPVLTAGVTLLLMDRNFNTGFYEVAAGGDPVTYEHLFWFFG 241
Cdd:MTH00103  160 GAINFITTIINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFG 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 242 HPEVYMMIMPGFGMMSHIVSTYS-KKPMFGEMGMLYAMGSMGLLGFLVWSHHMYVVGLDIDSRAYFTSATMVMAVPTGMK 320
Cdd:MTH00103  240 HPEVYILILPGFGMISHIVTYYSgKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVK 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 321 MFSWMATMYGGEVRLAVPMLFALGFLFLFTMGGLTGVMLSNASMDVAFHDTYYVVGHFHYVLSMGALFSLVGGYYYWGPS 400
Cdd:MTH00103  320 VFSWLATLHGGNIKWSPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPL 399

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1904806543 401 MFGLNYNKVWAEIHFWLLFMSVNLIFLPMHFLGTNGMPRRIPQYPDAFIGWN 452
Cdd:MTH00103  400 FSGYTLNDTWAKIHFTIMFVGVNMTFFPQHFLGLSGMPRRYSDYPDAYTTWN 451
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 3-531 2.55e-172

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 496.66  E-value: 2.55e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543   3 YMTRWLYSTSHKDMAMLYLGYGLMSSMVATWMSVMMRMELSGPNPqyLYGNNQVYNVLVTGHAMAMMFLFVMPVLMGAFG 82
Cdd:MTH00037    2 QLSRWLFSTNHKDIGTLYLIFGAWAGMVGTAMSVIIRTELAQPGS--LLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543  83 NYFLPMLMGAVDMAFARLNNMSFWCLPPALVCMMASVLMEQGAGTG-NCYPPLSSINAHSGPSVDLAMFALHLTSMSSLL 161
Cdd:MTH00037   80 NWLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLLASAGVESGAGTGwTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSIL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 162 GAMNFMVTFINMRTMGLHMVNAPLFVWAMFMTAMLLLLSLPVLTAGVTLLLMDRNFNTGFYEVAAGGDPVTYEHLFWFFG 241
Cdd:MTH00037  160 ASINFITTIINMRTPGMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFG 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 242 HPEVYMMIMPGFGMMSHIVSTYS-KKPMFGEMGMLYAMGSMGLLGFLVWSHHMYVVGLDIDSRAYFTSATMVMAVPTGMK 320
Cdd:MTH00037  240 HPEVYILILPGFGMISHVIAHYSgKQEPFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIK 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 321 MFSWMATMYGGEVRLAVPMLFALGFLFLFTMGGLTGVMLSNASMDVAFHDTYYVVGHFHYVLSMGALFSLVGGYYYWGPS 400
Cdd:MTH00037  320 VFSWMATLQGSNLRWETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPL 399

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 401 MFGLNYNKVWAEIHFWLLFMSVNLIFLPMHFLGTNGMPRRIPQYPDAFIGWNYISSIGSTISIISVLVGLKSVEIQLNng 480
Cdd:MTH00037  400 FSGVSLHPLWSKVHFFLMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSTISLVATLFFLFLIWEAFA-- 477

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1904806543 481 lnhNTELQMTPDYLESNLTRLTRdsdielilSRPAEYHTFSELPVLVSPNK 531
Cdd:MTH00037  478 ---SQREVISPEFSSSSLEWQYS--------SFPPSHHTFDETPSTVILIK 517
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 13-452 2.88e-166

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: 479.33  E-value: 2.88e-166
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543  13 HKDMAMLYLGYGLMSSMVATWMSVMMRMELSGPNPQYLygNNQVYNVLVTGHAMAMMFLFVMPVLMGAFGNYFLPMLmGA 92
Cdd:cd00919     1 HKDIGLLYLIFAFVALLLGGLLALLIRLELATPGSLFL--DPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPPLI-GA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543  93 VDMAFARLNNMSFWCLPPALVCMMASVLMEQGAGTG-NCYPPLSSINAHSGPSVDLAMFALHLTSMSSLLGAMNFMVTFI 171
Cdd:cd00919    78 RDLAFPRLNNLSFWLFPPGLLLLLSSVLVGGGAGTGwTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTIL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 172 NMRTMGLHMVNAPLFVWAMFMTAMLLLLSLPVLTAGVTLLLMDRNFNTGFYEVAAGGDPVTYEHLFWFFGHPEVYMMIMP 251
Cdd:cd00919   158 NMRAPGMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILP 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 252 GFGMMSHIVSTYSKKPMFGEMGMLYAMGSMGLLGFLVWSHHMYVVGLDIDSRAYFTSATMVMAVPTGMKMFSWMATMYGG 331
Cdd:cd00919   238 AFGAISEIIPTFSGKPLFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGG 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 332 EVRLAVPMLFALGFLFLFTMGGLTGVMLSNASMDVAFHDTYYVVGHFHYVLSMGALFSLVGGYYYWGPSMFGLNYNKVWA 411
Cdd:cd00919   318 RIRFDPPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKLG 397

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|.
gi 1904806543 412 EIHFWLLFMSVNLIFLPMHFLGTNGMPRRIPQYPDAFIGWN 452
Cdd:cd00919   398 KIHFWLWFIGFNLTFFPMHFLGLLGMPRRYADYPDGFAPWN 438
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-531 4.93e-161

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 468.72  E-value: 4.93e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543   1 MSYMTRWLYSTSHKDMAMLYLGYGLMSSMVATWMSVMMRMELSGPNPqyLYGNNQVYNVLVTGHAMAMMFLFVMPVLMGA 80
Cdd:MTH00026    1 MTSFVRWFFSCNHKDIGSLYLVFGALSGAIGTAFSMLIRLELSSPGS--MLGDDHLYNVIVTAHAFVMIFFLVMPTMIGG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543  81 FGNYFLPMLMGAVDMAFARLNNMSFWCLPPALVCMMASVLMEQGAGTG-NCYPPLSSINAHSGPSVDLAMFALHLTSMSS 159
Cdd:MTH00026   79 FGNWFVPLMIGAPDMAFPRLNNISFWLLPPALFLLLGSSLVEQGAGTGwTVYPPLASIQAHSGGSVDMAIFSLHLAGLSS 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 160 LLGAMNFMVTFINMRTMGLHMVNAPLFVWAMFMTAMLLLLSLPVLTAGVTLLLMDRNFNTGFYEVAAGGDPVTYEHLFWF 239
Cdd:MTH00026  159 ILGAMNFITTVMNMRTPGMTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWF 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 240 FGHPEVYMMIMPGFGMMSHIVSTYS-KKPMFGEMGMLYAMGSMGLLGFLVWSHHMYVVGLDIDSRAYFTSATMVMAVPTG 318
Cdd:MTH00026  239 FGHPEVYILILPGFGIISQILSLFSyKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTG 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 319 MKMFSWMATMYGGEVRL--AVPMLFALGFLFLFTMGGLTGVMLSNASMDVAFHDTYYVVGHFHYVLSMGALFSLVGGYYY 396
Cdd:MTH00026  319 IKIFSWLATVSGSGRNLifTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYL 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 397 WGPSMFGLNYNKVWAEIHFWLLFMSVNLIFLPMHFLGTNGMPRRIPQYPDAFIGWNYISSIGSTISIISVLVGLKSVEIQ 476
Cdd:MTH00026  399 WFGKITGYAYKDIYGLIHFWLMFIGVNITFFPQHFLGLAGLPRRYADYPDNFEDFNQISSFGSIISIIAVIWFIVVIFDA 478

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1904806543 477 LNNGLNHNTELQMTPDYLESNLTRLTRDSdIELILSRPAEYHTFSELPVLVSPNK 531
Cdd:MTH00026  479 YYREEPFDINIMAKGPLIPFSCQPAHFDT-LEWSLTSPPEHHTYNELPYIVGGPK 532
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 8-453 6.81e-161

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: 466.70  E-value: 6.81e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543   8 LYSTSHKDMAMLYLGYGLMSSMVATWMSVMMRMELSGPNPQYLygNNQVYNVLVTGHAMAMMFLFVMPvLMGAFGNYFLP 87
Cdd:TIGR02891   1 LTTVDHKRIGILYLVTAFAFFLVGGVLALLMRAQLATPGNTFM--DAETYNQLFTMHGTIMIFLFAIP-ILAGFGNYLLP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543  88 MLMGAVDMAFARLNNMSFWCLPPALVCMMASVLMEQGAGTG-NCYPPLSSINAHSGPSVDLAMFALHLTSMSSLLGAMNF 166
Cdd:TIGR02891  78 LMIGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGwTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNF 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 167 MVTFINMRTMGLHMVNAPLFVWAMFMTAMLLLLSLPVLTAGVTLLLMDRNFNTGFYEVAAGGDPVTYEHLFWFFGHPEVY 246
Cdd:TIGR02891 158 IVTILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVY 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 247 MMIMPGFGMMSHIVSTYSKKPMFGEMGMLYAMGSMGLLGFLVWSHHMYVVGLDIDSRAYFTSATMVMAVPTGMKMFSWMA 326
Cdd:TIGR02891 238 IIFLPAFGIISEILPTFARKPIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIA 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 327 TMYGGEVRLAVPMLFALGFLFLFTMGGLTGVMLSNASMDVAFHDTYYVVGHFHYVLSMGALFSLVGGYYYWGPSMFGLNY 406
Cdd:TIGR02891 318 TLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMY 397

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*....
gi 1904806543 407 NKVWAEIHFWLLFMSVNLIFLPMHFLGTNGMPRRIPQYPDA--FIGWNY 453
Cdd:TIGR02891 398 NERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNL 446
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-452 1.88e-159

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 463.38  E-value: 1.88e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543   1 MSYMTRWLYSTSHKDMAMLYLGYGLMSSMVATWMSVMMRMELSGPNpqYLYGNNQVYNVLVTGHAMAMMFLFVMPVLMGA 80
Cdd:MTH00079    1 QGGLSVWLESSNHKDIGTLYFLFGLWSGMVGTSLSLIIRLELSKPG--LLLGNGQLYNSVITAHAILMIFFMVMPSMIGG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543  81 FGNYFLPMLMGAVDMAFARLNNMSFWCLPPALVCMMASVLMEQGAGTG-NCYPPLSSInAHSGPSVDLAMFALHLTSMSS 159
Cdd:MTH00079   79 FGNWMLPLMLGAPDMSFPRLNNLSFWLLPTSLFLILDSCFVDMGPGTSwTVYPPLSTL-GHPGSSVDLAIFSLHCAGISS 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 160 LLGAMNFMVTFINMRTMGLHMVNAPLFVWAMFMTAMLLLLSLPVLTAGVTLLLMDRNFNTGFYEVAAGGDPVTYEHLFWF 239
Cdd:MTH00079  158 ILGGINFMVTTKNLRSSSISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWF 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 240 FGHPEVYMMIMPGFGMMSHIVSTYS-KKPMFGEMGMLYAMGSMGLLGFLVWSHHMYVVGLDIDSRAYFTSATMVMAVPTG 318
Cdd:MTH00079  238 FGHPEVYILILPAFGIISQSTLYLTgKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTG 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 319 MKMFSWMATMYGGEVRLAVPMLFALGFLFLFTMGGLTGVMLSNASMDVAFHDTYYVVGHFHYVLSMGALFSLVGGYYYWG 398
Cdd:MTH00079  318 VKVFSWLATLFGMKMKFQPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWW 397

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1904806543 399 PSMFGLNYNKVWAEIHFWLLFMSVNLIFLPMHFLGTNGMPRRIPQYPDAFIGWN 452
Cdd:MTH00079  398 PFMTGIVYDKLMMSAVFFLMFVGVNLTFFPLHFAGLHGMPRKYLDYPDVYSVWN 451
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
2-452 8.86e-157

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 457.67  E-value: 8.86e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543   2 SYMTRWLYSTSHKDMAMLYLGYGLMSSMVATWMSVMMRMELSGPNPQYLygNNQVYNVLVTGHAMAMMFLFVMPvLMGAF 81
Cdd:COG0843     4 SGWRRWLTTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLL--SPETYNQLFTMHGTIMIFFFATP-FLAGF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543  82 GNYFLPMLMGAVDMAFARLNNMSFWCLPPALVCMMASVLMEQGAGTG-NCYPPLSSINAHSGPSVDLAMFALHLTSMSSL 160
Cdd:COG0843    81 GNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGwTFYPPLSGLEASPGVGVDLWLLGLALFGVGSI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 161 LGAMNFMVTFINMRTMGLHMVNAPLFVWAMFMTAMLLLLSLPVLTAGVTLLLMDRNFNTGFYEVAAGGDPVTYEHLFWFF 240
Cdd:COG0843   161 LGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFF 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 241 GHPEVYMMIMPGFGMMSHIVSTYSKKPMFGEMGMLYAMGSMGLLGFLVWSHHMYVVGLDIDSRAYFTSATMVMAVPTGMK 320
Cdd:COG0843   241 GHPEVYILILPAFGIVSEIIPTFSRKPLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVK 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 321 MFSWMATMYGGEVRLAVPMLFALGFLFLFTMGGLTGVMLSNASMDVAFHDTYYVVGHFHYVLSMGALFSLVGGYYYWGPS 400
Cdd:COG0843   321 VFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPK 400

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1904806543 401 MFGLNYNKVWAEIHFWLLFMSVNLIFLPMHFLGTNGMPRRIPQYP--DAFIGWN 452
Cdd:COG0843   401 MTGRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLN 454
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 7-452 4.89e-134

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: 398.49  E-value: 4.89e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543   7 WLYSTSHKDMAMLYLGYGLMSSMVATWMSVMMRMELSGPNPQYLygNNQVYNVLVTGHAMAMMFLFVMPVLMGaFGNYFL 86
Cdd:cd01662     1 WLTTVDHKRIGIMYIITAFVFFLRGGVDALLMRTQLALPGNDFL--SPEHYNQIFTMHGTIMIFLFAMPLVFG-LMNYLV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543  87 PMLMGAVDMAFARLNNMSFWCLPPALVCMMASVLMEQGAGTG-NCYPPLSSINAHSGPSVDLAMFALHLTSMSSLLGAMN 165
Cdd:cd01662    78 PLQIGARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGwFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAIN 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 166 FMVTFINMRTMGLHMVNAPLFVWAMFMTAMLLLLSLPVLTAGVTLLLMDRNFNTGFYEVAAGGDPVTYEHLFWFFGHPEV 245
Cdd:cd01662   158 FIVTILKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEV 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 246 YMMIMPGFGMMSHIVSTYSKKPMFGEMGMLYAMGSMGLLGFLVWSHHMYVVGLDIDSRAYFTSATMVMAVPTGMKMFSWM 325
Cdd:cd01662   238 YILILPAFGIFSEIVPTFSRKPLFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWL 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 326 ATMYGGEVRLAVPMLFALGFLFLFTMGGLTGVMLSNASMDVAFHDTYYVVGHFHYVLSMGALFSLVGGYYYWGPSMFGLN 405
Cdd:cd01662   318 FTMWRGRIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRM 397

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*..
gi 1904806543 406 YNKVWAEIHFWLLFMSVNLIFLPMHFLGTNGMPRRIPQYPDAfIGWN 452
Cdd:cd01662   398 LNERLGKWSFWLWFIGFNLTFFPMHILGLMGMPRRVYTYLPG-PGWD 443
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 1-448 2.84e-122

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 368.62  E-value: 2.84e-122
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543   1 MSYMTRWLYSTSHKDMAMLYLGYGLMSSMVATWMSVMMRMELSgpNPQYLYGNNQVYNVLVTGHAMAMMFLFVMPVLMGA 80
Cdd:MTH00048    1 MNSLLSWLFTLDHKRIGVIYTLLGVWSGFVGLSLSLLIRLNFL--DPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543  81 FGNYFLPMLMGAVDMAFARLNNMSFWCLPPALVCMMASvlMEQGAGTG-NCYPPLSSINAHSGPSVDLAMFALHLTSMSS 159
Cdd:MTH00048   79 FGNYLLPLLLGLSDLNLPRLNALSAWLLVPSIVFLLLS--MCLGAGVGwTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSS 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 160 LLGAMNFMVTfINMRTMGLHMVNAPLFVWAMFMTAMLLLLSLPVLTAGVTLLLMDRNFNTGFYEVAAGGDPVTYEHLFWF 239
Cdd:MTH00048  157 LFGSINFICT-IYSAFMTNVFSRTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWF 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 240 FGHPEVYMMIMPGFGMMSHIVSTYSKKP-MFGEMGMLYAMGSMGLLGFLVWSHHMYVVGLDIDSRAYFTSATMVMAVPTG 318
Cdd:MTH00048  236 FGHPEVYVLILPGFGIISHICLSLSNNDdPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTG 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 319 MKMFSWMATMYGGEVRLAVP-MLFALGFLFLFTMGGLTGVMLSNASMDVAFHDTYYVVGHFHYVLSMGALFSLVGGYYYW 397
Cdd:MTH00048  316 IKVFSWLYMLLNSRVRKSDPvVWWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWW 395

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1904806543 398 GPSMFGLNYNKVWAEIHFWLLFMSVNLIFLPMHFLGTNGMPRRIPQYPDAF 448
Cdd:MTH00048  396 WPLITGLSLNKYLLQCHCIISMIGFNLCFFPMHYFGLCGLPRRVCVYEPSY 446
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 15-452 1.11e-113

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: 343.79  E-value: 1.11e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543  15 DMAMLYLGYGLMSSMVATWMSVMMRMELSGPNPQYLygNNQVYNVLVTGHAMAMMFLFVMPVLMGaFGNYFLPMLMGAVD 94
Cdd:pfam00115   1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFL--SPLTYNQLRTLHGNLMIFWFATPFLFG-FGNYLVPLMIGARD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543  95 MAFARLNNMSFWCLPPALVCMMASVLMEQGAGTGncYPPLssinahsgPSVDLAMFALHLTSMSSLLGAMNFMVTFINMR 174
Cdd:pfam00115  78 MAFPRLNALSFWLVVLGAVLLLASFGGATTGWTE--YPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRR 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 175 TMGLHMvNAPLFVWAMFMTAMLLLLSLPVLTAGVTLLLMDRNFNTGfyevaaGGDPVTYEHLFWFFGHPEVYMMIMPGFG 254
Cdd:pfam00115 148 APGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLGAG------GGDPLLDQHLFWWFGHPEVYILILPAFG 220

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 255 MMSHIVSTYSKKPMFGEMGMLYAMGSMGLLGFLVWSHHMYVVGLDIDSRAYFTSATMVMAVPTGMKMFSWMATMYGGEVR 334
Cdd:pfam00115 221 IIYYILPKFAGRPLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIR 300

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 335 LA-VPMLFALGFLFLFTMGGLTGVMLSNASMDVAFHDTYYVVGHFHYVLSMGALFSLVGGYYYWGPSMFGLNYNKVWAEI 413
Cdd:pfam00115 301 FRtTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKL 380

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 1904806543 414 HFWLLFMSVNLIFLPMHFLGTNGMPRRIP----QYPDAFIGWN 452
Cdd:pfam00115 381 HFWLLFIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPLN 423
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 5-446 3.04e-82

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 269.11  E-value: 3.04e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543   5 TRWLYSTSHKDMAMLYLGYGLMSSMVATWMSVMMRME---LSGPNPQYLYGNNqvYNVLVTGHAMAMMFLFVMPVLMGAF 81
Cdd:PRK15017   46 KEWLTSVDHKRLGIMYIIVAIVMLLRGFADAIMMRSQqalASAGEAGFLPPHH--YDQIFTAHGVIMIFFVAMPFVIGLM 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543  82 gNYFLPMLMGAVDMAFARLNNMSFWCLPPALVCMMASVLMEQGAGTG-NCYPPLSSINAHSGPSVDLAMFALHLTSMSSL 160
Cdd:PRK15017  124 -NLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGwLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTT 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 161 LGAMNFMVTFINMRTMGLHMVNAPLFVWAMFMTAMLLLLSLPVLTAGVTLLLMDRNFNTGFYEVAAGGDPVTYEHLFWFF 240
Cdd:PRK15017  203 LTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAW 282

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 241 GHPEVYMMIMPGFGMMSHIVSTYSKKPMFGEMGMLYAMGSMGLLGFLVWSHHMYVVGLDIDSRAYFTSATMVMAVPTGMK 320
Cdd:PRK15017  283 GHPEVYILILPVFGVFSEIAATFSRKRLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVK 362

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 321 MFSWMATMYGGEVRLAVPMLFALGFLFLFTMGGLTGVMLSNASMDVAFHDTYYVVGHFHYVLSMGALFSLVGGYYYWGPS 400
Cdd:PRK15017  363 IFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYWWPK 442

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 1904806543 401 MFGLNYNKVWAEIHFWLLFMSVNLIFLPMHFLGTNGMPRRIPQYPD 446
Cdd:PRK15017  443 AFGFKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMTRRLSQQID 488
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
 236-446 7.94e-11

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: 64.23  E-value: 7.94e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 236 LFWFFGHPEVYMMIMPGFGMMSHIVSTYSKKPMFGEmgmlyAMGSMGLLGFLVWS-----HHMYV-VGLDIDSRAYFTSA 309
Cdd:cd01660   207 LFWWFGHPLVYFWLLPAYIAWYTILPKIAGGKLFSD-----PLARLAFILFLLFStpvgfHHQFAdPGIGPGWKFIHMVL 281

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 310 TMVMAVPT-------------------GMKMFSWMATMYGGEVRLAVPMLFALGFLFlftmGGLTGVMLSNASMDVAFHD 370
Cdd:cd01660   282 TFMVALPSlltaftvfasleiagrlrgGKGLFGWIRALPWGDPMFLALFLAMLMFIP----GGAGGIINASYQLNYVVHN 357

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 371 TYYVVGHFHyvLSMGALFSLV--GGYYYWGPSMFGLNYNKVW-AEIHFWLLFMSVNLIFLPMHFLGTNGMPRR--IPQYP 445
Cdd:cd01660   358 TAWVPGHFH--LTVGGAVALTfmAVAYWLVPHLTGRELAAKRlALAQPWLWFVGMTIMSTAMHVAGLLGAPRRtaEAQYG 435


                  .
gi 1904806543 446 D 446
Cdd:cd01660   436 G 436
PRK14485 PRK14485
putative bifunctional cbb3-type cytochrome c oxidase subunit I/II; Provisional
 351-433 8.26e-03

putative bifunctional cbb3-type cytochrome c oxidase subunit I/II; Provisional


Pssm-ID: 184703 [Multi-domain]  Cd Length: 712  Bit Score: 38.91  E-value: 8.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1904806543 351 MGGLTGVMLSNASMDVAFHDTYYVVGHFHyvlsMGAL----FSLVGGYYYWGPSMFGLN-YNKVWAEIHFWLLFMSVNLI 425
Cdd:PRK14485  318 MATFEGPMLSLKNVNAIAHYTDWIIAHVH----VGALgwngFLTFGMLYWLLPRLFKTKlYSTKLANFHFWIGTLGIILY 393


                  ....*...
gi 1904806543 426 FLPMHFLG 433
Cdd:PRK14485  394 ALPMYVAG 401
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH