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Conserved domains on  [gi|55826777|gb|AAV66510|]
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cytochrome oxidase subunit I, partial (mitochondrion) [Cataglyphis bicolor]

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 ...
 1-255 2.49e-154

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: 439.30  E-value: 2.49e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55826777    1 IIMNESGKKETFGALGMIYALMAIGFLGFVVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWITTLHGTKINNNS 80
Cdd:MTH00153 255 IISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSP 334

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55826777   81 SLWWAMGFIFLFTMGGLTGIMLSNSSIDIVLHDTYYVVAHFHYVLSMGAVFAIIASFIHWFPLITGYSLNNFLLNIQFLS 160
Cdd:MTH00153 335 SLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFI 414

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55826777  161 MFIGVNLTFFPQHFLGLSGMPRRYSDYPDTFLAWNMISSIGSILSILSLIFLMFLIWEALSSKRMIMNLFFLNSSLEWLS 240
Cdd:MTH00153 415 MFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPVLFSLNLSSSIEWLQ 494

                        250
                 ....*....|....*
gi 55826777  241 SYPPINHSYNEIPAI 255
Cdd:MTH00153 495 NLPPAEHSYSELPLL 509
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-255 2.49e-154

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 439.30  E-value: 2.49e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55826777    1 IIMNESGKKETFGALGMIYALMAIGFLGFVVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWITTLHGTKINNNS 80
Cdd:MTH00153 255 IISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSP 334

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55826777   81 SLWWAMGFIFLFTMGGLTGIMLSNSSIDIVLHDTYYVVAHFHYVLSMGAVFAIIASFIHWFPLITGYSLNNFLLNIQFLS 160
Cdd:MTH00153 335 SLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFI 414

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55826777  161 MFIGVNLTFFPQHFLGLSGMPRRYSDYPDTFLAWNMISSIGSILSILSLIFLMFLIWEALSSKRMIMNLFFLNSSLEWLS 240
Cdd:MTH00153 415 MFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPVLFSLNLSSSIEWLQ 494

                        250
                 ....*....|....*
gi 55826777  241 SYPPINHSYNEIPAI 255
Cdd:MTH00153 495 NLPPAEHSYSELPLL 509
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-239 3.08e-132

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: 382.22  E-value: 3.08e-132
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55826777   1 IIMNESGKKETFGALGMIYALMAIGFLGFVVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWITTLHGTKINNNS 80
Cdd:cd01663 248 IISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFET 327

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55826777  81 SLWWAMGFIFLFTMGGLTGIMLSNSSIDIVLHDTYYVVAHFHYVLSMGAVFAIIASFIHWFPLITGYSLNNFLLNIQFLS 160
Cdd:cd01663 328 PMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHFWL 407

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55826777 161 MFIGVNLTFFPQHFLGLSGMPRRYSDYPDTFLAWNMISSIGSILSILSLIFLMFLIWEALSSKRM-IMNLFFLNSSLEWL 239
Cdd:cd01663 408 MFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKvIFNVGEGSTSLEWT 487
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
8-255 3.44e-74

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 235.02  E-value: 3.44e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55826777   8 KKETFGALGMIYALMAIGFLGFVVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWITTLHGTKINNNSSLWWAMG 87
Cdd:COG0843 265 RKPLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLFALG 344

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55826777  88 FIFLFTMGGLTGIMLSNSSIDIVLHDTYYVVAHFHYVLSMGAVFAIIASFIHWFPLITGYSLNNFLLNIQFLSMFIGVNL 167
Cdd:COG0843 345 FIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKIHFWLWFIGFNL 424

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55826777 168 TFFPQHFLGLSGMPRRYSDYPDTFLAWNMISSIGSILSILSLIFLMFL---IWEALSSKRMIMNLFFLNsSLEWLSSYPP 244
Cdd:COG0843 425 TFFPMHILGLLGMPRRYATYPPEPGWQPLNLISTIGAFILAVGFLLFLinlVVSLRKGPKAGGNPWGAR-TLEWATPSPP 503

                       250
                ....*....|.
gi 55826777 245 INHSYNEIPAI 255
Cdd:COG0843 504 PLYNFASIPVV 514
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 8-249 6.68e-74

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: 233.27  E-value: 6.68e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55826777     8 KKETFGALGMIYALMAIGFLGFVVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWITTLHGTKINNNSSLWWAMG 87
Cdd:TIGR02891 256 RKPIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLFALG 335

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55826777    88 FIFLFTMGGLTGIMLSNSSIDIVLHDTYYVVAHFHYVLSMGAVFAIIASFIHWFPLITGYSLNNFLLNIQFLSMFIGVNL 167
Cdd:TIGR02891 336 FIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLGRWHFWLTFVGFNL 415

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55826777   168 TFFPQHFLGLSGMPRRYSDYPD--TFLAWNMISSIGSILSILSLIFLMFLIWEALSSKRMIMNLFFLNSSLEWLSSYPPI 245
Cdd:TIGR02891 416 TFFPMHLLGLLGMPRRYYTYPPqmGFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGPKAGANPWGATTLEWTTSSPPP 495


                  ....
gi 55826777   246 NHSY 249
Cdd:TIGR02891 496 AHNF 499
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 8-186 2.97e-55

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: 183.16  E-value: 2.97e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55826777     8 KKETFGALGMIYALMAIGFLGFVVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWITTLHGTKIN-NNSSLWWAM 86
Cdd:pfam00115 231 GRPLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRfRTTPMLFFL 310

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55826777    87 GFIFLFTMGGLTGIMLSNSSIDIVLHDTYYVVAHFHYVLSMGAVFAIIASFIHWFPLITGYSLNNFLLNIQFLSMFIGVN 166
Cdd:pfam00115 311 GFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFWLLFIGFN 390

                         170       180
                  ....*....|....*....|
gi 55826777   167 LTFFPQHFLGLSGMPRRYSD 186
Cdd:pfam00115 391 LTFFPMHILGLLGMPRRYAP 410
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-255 2.49e-154

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 439.30  E-value: 2.49e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55826777    1 IIMNESGKKETFGALGMIYALMAIGFLGFVVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWITTLHGTKINNNS 80
Cdd:MTH00153 255 IISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSP 334

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55826777   81 SLWWAMGFIFLFTMGGLTGIMLSNSSIDIVLHDTYYVVAHFHYVLSMGAVFAIIASFIHWFPLITGYSLNNFLLNIQFLS 160
Cdd:MTH00153 335 SLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFI 414

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55826777  161 MFIGVNLTFFPQHFLGLSGMPRRYSDYPDTFLAWNMISSIGSILSILSLIFLMFLIWEALSSKRMIMNLFFLNSSLEWLS 240
Cdd:MTH00153 415 MFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPVLFSLNLSSSIEWLQ 494

                        250
                 ....*....|....*
gi 55826777  241 SYPPINHSYNEIPAI 255
Cdd:MTH00153 495 NLPPAEHSYSELPLL 509
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-239 3.08e-132

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: 382.22  E-value: 3.08e-132
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55826777   1 IIMNESGKKETFGALGMIYALMAIGFLGFVVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWITTLHGTKINNNS 80
Cdd:cd01663 248 IISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFET 327

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55826777  81 SLWWAMGFIFLFTMGGLTGIMLSNSSIDIVLHDTYYVVAHFHYVLSMGAVFAIIASFIHWFPLITGYSLNNFLLNIQFLS 160
Cdd:cd01663 328 PMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHFWL 407

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55826777 161 MFIGVNLTFFPQHFLGLSGMPRRYSDYPDTFLAWNMISSIGSILSILSLIFLMFLIWEALSSKRM-IMNLFFLNSSLEWL 239
Cdd:cd01663 408 MFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKvIFNVGEGSTSLEWT 487
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-255 9.22e-128

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 371.70  E-value: 9.22e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55826777    1 IIMNESGKKETFGALGMIYALMAIGFLGFVVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWITTLHGTKINNNS 80
Cdd:MTH00167 257 IVVYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLHGGKIKWET 336

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55826777   81 SLWWAMGFIFLFTMGGLTGIMLSNSSIDIVLHDTYYVVAHFHYVLSMGAVFAIIASFIHWFPLITGYSLNNFLLNIQFLS 160
Cdd:MTH00167 337 PMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGLTLNETWTKIHFFV 416

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55826777  161 MFIGVNLTFFPQHFLGLSGMPRRYSDYPDTFLAWNMISSIGSILSILSLIFLMFLIWEALSSKRMIMNLFFLNSSLEWLS 240
Cdd:MTH00167 417 MFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNVVSSIGSLISLVAVILFLFIIWEAFSSKRKLLPVELTSTNVEWLH 496

                        250
                 ....*....|....*
gi 55826777  241 SYPPINHSYNEIPAI 255
Cdd:MTH00167 497 GCPPPHHTWEEPPFV 511
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-255 4.03e-127

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 370.19  E-value: 4.03e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55826777    1 IIMNESGKKETFGALGMIYALMAIGFLGFVVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWITTLHGTKINNNS 80
Cdd:MTH00116 257 IVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSWLATLHGGTIKWDP 336

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55826777   81 SLWWAMGFIFLFTMGGLTGIMLSNSSIDIVLHDTYYVVAHFHYVLSMGAVFAIIASFIHWFPLITGYSLNNFLLNIQFLS 160
Cdd:MTH00116 337 PMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGYTLHQTWTKAQFGV 416

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55826777  161 MFIGVNLTFFPQHFLGLSGMPRRYSDYPDTFLAWNMISSIGSILSILSLIFLMFLIWEALSSKRMIMNLFFLNSSLEWLS 240
Cdd:MTH00116 417 MFTGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTISSIGSLISMTAVIMLMFIIWEAFSSKRKVLQPELTTTNIEWIH 496

                        250
                 ....*....|....*
gi 55826777  241 SYPPINHSYNEIPAI 255
Cdd:MTH00116 497 GCPPPYHTFEEPAFV 511
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-255 1.30e-123

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 361.22  E-value: 1.30e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55826777    1 IIMNESGKKETFGALGMIYALMAIGFLGFVVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWITTLHGTKINNNS 80
Cdd:MTH00223 254 IVSHYSSKKEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGSKIKYEA 333

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55826777   81 SLWWAMGFIFLFTMGGLTGIMLSNSSIDIVLHDTYYVVAHFHYVLSMGAVFAIIASFIHWFPLITGYSLNNFLLNIQFLS 160
Cdd:MTH00223 334 PMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLFTGVTLHRRWAKAHFFL 413

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55826777  161 MFIGVNLTFFPQHFLGLSGMPRRYSDYPDTFLAWNMISSIGSILSILSLIFLMFLIWEALSSKRMIMNLFFLNSSLEWLS 240
Cdd:MTH00223 414 MFLGVNLTFFPQHFLGLAGMPRRYSDYPDCYTKWNQVSSFGSMISFVSVLFFMFIVWEAFVSQRSVVWSGHLSTSLEWDN 493

                        250
                 ....*....|....*
gi 55826777  241 SYPPINHSYNEIPAI 255
Cdd:MTH00223 494 LLPADFHNNSETGAL 508
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-255 4.70e-121

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 354.41  E-value: 4.70e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55826777    1 IIMNESGKKETFGALGMIYALMAIGFLGFVVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWITTLHGTKINNNS 80
Cdd:MTH00142 255 IINHYSGKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFSWLATLHGSKVKYEP 334

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55826777   81 SLWWAMGFIFLFTMGGLTGIMLSNSSIDIVLHDTYYVVAHFHYVLSMGAVFAIIASFIHWFPLITGYSLNNFLLNIQFLS 160
Cdd:MTH00142 335 PMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLFTGLTLNPRWLKAHFYT 414

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55826777  161 MFIGVNLTFFPQHFLGLSGMPRRYSDYPDTFLAWNMISSIGSILSILSLIFLMFLIWEALSSKRMIMNLFFLNSSLEWLS 240
Cdd:MTH00142 415 MFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSSLGSMISFIAVLMFVFIVWESFVSQRLVMWSSHLSTSLEWSH 494

                        250
                 ....*....|....*
gi 55826777  241 SYPPINHSYNEIPAI 255
Cdd:MTH00142 495 RLPPDFHTYDELPIL 509
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-251 4.12e-111

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 329.15  E-value: 4.12e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55826777    1 IIMNESGKKETFGALGMIYALMAIGFLGFVVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWITTLHGTKINNNS 80
Cdd:MTH00103 257 IVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGNIKWSP 336

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55826777   81 SLWWAMGFIFLFTMGGLTGIMLSNSSIDIVLHDTYYVVAHFHYVLSMGAVFAIIASFIHWFPLITGYSLNNFLLNIQFLS 160
Cdd:MTH00103 337 AMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLNDTWAKIHFTI 416

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55826777  161 MFIGVNLTFFPQHFLGLSGMPRRYSDYPDTFLAWNMISSIGSILSILSLIFLMFLIWEALSSKRMIMNLFFLNSSLEWLS 240
Cdd:MTH00103 417 MFVGVNMTFFPQHFLGLSGMPRRYSDYPDAYTTWNTVSSMGSFISLTAVMLMIFMIWEAFASKREVLTVELTTTNLEWLH 496

                        250
                 ....*....|.
gi 55826777  241 SYPPINHSYNE 251
Cdd:MTH00103 497 GCPPPYHTFEE 507
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-253 3.09e-109

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 324.48  E-value: 3.09e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55826777    1 IIMNESGKKETFGALGMIYALMAIGFLGFVVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWITTLHGTKINNNS 80
Cdd:MTH00037 257 VIAHYSGKQEPFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWMATLQGSNLRWET 336

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55826777   81 SLWWAMGFIFLFTMGGLTGIMLSNSSIDIVLHDTYYVVAHFHYVLSMGAVFAIIASFIHWFPLITGYSLNNFLLNIQFLS 160
Cdd:MTH00037 337 PLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLFSGVSLHPLWSKVHFFL 416

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55826777  161 MFIGVNLTFFPQHFLGLSGMPRRYSDYPDTFLAWNMISSIGSILSILSLIFLMFLIWEALSSKRMIMNLFFLNSSLEW-L 239
Cdd:MTH00037 417 MFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSTISLVATLFFLFLIWEAFASQREVISPEFSSSSLEWqY 496

                        250
                 ....*....|....
gi 55826777  240 SSYPPINHSYNEIP 253
Cdd:MTH00037 497 SSFPPSHHTFDETP 510
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-251 5.89e-109

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 323.80  E-value: 5.89e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55826777    1 IIMNESGKKETFGALGMIYALMAIGFLGFVVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWITTLHGTKINNNS 80
Cdd:MTH00183 257 IVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGSIKWET 336

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55826777   81 SLWWAMGFIFLFTMGGLTGIMLSNSSIDIVLHDTYYVVAHFHYVLSMGAVFAIIASFIHWFPLITGYSLNNFLLNIQFLS 160
Cdd:MTH00183 337 PLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLFSGYTLHSTWTKIHFGV 416

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55826777  161 MFIGVNLTFFPQHFLGLSGMPRRYSDYPDTFLAWNMISSIGSILSILSLIFLMFLIWEALSSKRMIMNLFFLNSSLEWLS 240
Cdd:MTH00183 417 MFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMFLFILWEAFAAKREVLSVELTSTNVEWLH 496

                        250
                 ....*....|.
gi 55826777  241 SYPPINHSYNE 251
Cdd:MTH00183 497 GCPPPYHTFEE 507
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-251 6.02e-108

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 321.12  E-value: 6.02e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55826777    1 IIMNESGKKETFGALGMIYALMAIGFLGFVVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWITTLHGTKINNNS 80
Cdd:MTH00077 257 IVTYYSAKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGAIKWDA 336

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55826777   81 SLWWAMGFIFLFTMGGLTGIMLSNSSIDIVLHDTYYVVAHFHYVLSMGAVFAIIASFIHWFPLITGYSLNNFLLNIQFLS 160
Cdd:MTH00077 337 AMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLHSTWSKIHFGV 416

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55826777  161 MFIGVNLTFFPQHFLGLSGMPRRYSDYPDTFLAWNMISSIGSILSILSLIFLMFLIWEALSSKRMIMNLFFLNSSLEWLS 240
Cdd:MTH00077 417 MFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMMMFIIWEAFSSKREVLTTELTSTNIEWLH 496

                        250
                 ....*....|.
gi 55826777  241 SYPPINHSYNE 251
Cdd:MTH00077 497 GCPPPYHTFEE 507
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-251 6.26e-108

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 321.08  E-value: 6.26e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55826777    1 IIMNESGKKETFGALGMIYALMAIGFLGFVVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWITTLHGTKINNNS 80
Cdd:MTH00007 254 IVTHYAGKLEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGSPIKYET 333

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55826777   81 SLWWAMGFIFLFTMGGLTGIMLSNSSIDIVLHDTYYVVAHFHYVLSMGAVFAIIASFIHWFPLITGYSLNNFLLNIQFLS 160
Cdd:MTH00007 334 PMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTGLTLHDRWAKAHFFL 413

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55826777  161 MFIGVNLTFFPQHFLGLSGMPRRYSDYPDTFLAWNMISSIGSILSILSLIFLMFLIWEALSSKRMIMNLFFLNSSLEWLS 240
Cdd:MTH00007 414 MFLGVNLTFFPQHFLGLSGMPRRYSDYPDAYTKWNVVSSFGSMLSFVALLLFIFILWEAFSAQRGVIASPHMSSSLEWQD 493

                        250
                 ....*....|.
gi 55826777  241 SYPPINHSYNE 251
Cdd:MTH00007 494 TLPLDFHNLPE 504
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 3-251 8.12e-102

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 305.45  E-value: 8.12e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55826777    3 MNESGKKETFGALGMIYALMAIGFLGFVVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWITTLHGTKINNNSSL 82
Cdd:MTH00079 259 LYLTGKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMKFQPLL 338

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55826777   83 WWAMGFIFLFTMGGLTGIMLSNSSIDIVLHDTYYVVAHFHYVLSMGAVFAIIASFIHWFPLITGYSLNNFLLNIQFLSMF 162
Cdd:MTH00079 339 LWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFMTGIVYDKLMMSAVFFLMF 418

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55826777  163 IGVNLTFFPQHFLGLSGMPRRYSDYPDTFLAWNMISSIGSILSILSLIFLMFLIWEALSSKRMIMNLFFLNSSLEWLSSY 242
Cdd:MTH00079 419 VGVNLTFFPLHFAGLHGMPRKYLDYPDVYSVWNVISSYGSMISVFALFLFIYVLLESFFSYRLVLHDNYINSSPEYSLSS 498


                 ....*....
gi 55826777  243 PPINHSYNE 251
Cdd:MTH00079 499 YVFGHSYQS 507
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-255 4.68e-95

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 288.64  E-value: 4.68e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55826777    1 IIMNESGKKETFGALGMIYALMAIGFLGFVVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWITTLHGTKINNNS 80
Cdd:MTH00182 259 IIPTFVAKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGGTLRLDT 338

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55826777   81 SLWWAMGFIFLFTMGGLTGIMLSNSSIDIVLHDTYYVVAHFHYVLSMGAVFAIIASFIHWFPLITGYSLNNFLLNIQFLS 160
Cdd:MTH00182 339 PMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNELYGKIHFWL 418

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55826777  161 MFIGVNLTFFPQHFLGLSGMPRRYSDYPDTFLAWNMISSIGSILSILSLIFLMFLIWEALSSKRMIM----NLFFLNSSL 236
Cdd:MTH00182 419 MFIGVNLTFFPQHFLGLAGFPRRYSDFADAFAGWNLVSSLGSIISIVGVVWFIYIIYDAYVREEKFIgwkeGTGESWASL 498

                        250
                 ....*....|....*....
gi 55826777  237 EWLSSYPPINHSYNEIPAI 255
Cdd:MTH00182 499 EWVHSSPPLFHTYNELPFV 517
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-253 2.02e-94

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 286.72  E-value: 2.02e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55826777    1 IIMNESGKKETFGALGMIYALMAIGFLGFVVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWITTLHGTKINNNS 80
Cdd:MTH00184 259 IIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATIFGGSLRLDT 338

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55826777   81 SLWWAMGFIFLFTMGGLTGIMLSNSSIDIVLHDTYYVVAHFHYVLSMGAVFAIIASFIHWFPLITGYSLNNFLLNIQFLS 160
Cdd:MTH00184 339 PMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNEVYGKIHFWL 418

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55826777  161 MFIGVNLTFFPQHFLGLSGMPRRYSDYPDTFLAWNMISSIGSILSILSLIFLMFLIWEALSSKRMI---MNLFFLNSSLE 237
Cdd:MTH00184 419 MFIGVNLTFFPQHFLGLAGLPRRYSDFHDSFAGWNQISSLGSVISIVGVVWFIYIVYDAYVREIKFvgwVEDSGHYPSLE 498

                        250
                 ....*....|....*.
gi 55826777  238 WLSSYPPINHSYNEIP 253
Cdd:MTH00184 499 WAQTSPPAHHTYNELP 514
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 8-220 8.24e-83

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: 255.15  E-value: 8.24e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55826777   8 KKETFGALGMIYALMAIGFLGFVVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWITTLHGTKINNNSSLWWAMG 87
Cdd:cd00919 251 GKPLFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGRIRFDPPMLFALG 330

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55826777  88 FIFLFTMGGLTGIMLSNSSIDIVLHDTYYVVAHFHYVLSMGAVFAIIASFIHWFPLITGYSLNNFLLNIQFLSMFIGVNL 167
Cdd:cd00919 331 FLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKLGKIHFWLWFIGFNL 410

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 55826777 168 TFFPQHFLGLSGMPRRYSDYPDTFLAWNMISSIGSILSILSLIFLMFLIWEAL 220
Cdd:cd00919 411 TFFPMHFLGLLGMPRRYADYPDGFAPWNFISSVGAFILGLGLLLFLGNLFLSL 463
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 6-255 5.22e-76

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 239.53  E-value: 5.22e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55826777    6 SGKKETFGALGMIYALMAIGFLGFVVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWITTLHGTKIN--NNSSLW 83
Cdd:MTH00026 263 SYKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSWLATVSGSGRNliFTTPMA 342

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55826777   84 WAMGFIFLFTMGGLTGIMLSNSSIDIVLHDTYYVVAHFHYVLSMGAVFAIIASFIHWFPLITGYSLNNFLLNIQFLSMFI 163
Cdd:MTH00026 343 WALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWFGKITGYAYKDIYGLIHFWLMFI 422

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55826777  164 GVNLTFFPQHFLGLSGMPRRYSDYPDTFLAWNMISSIGSILSILSLIFLMFLIWEALSSKRMI-MNLFFLN--------- 233
Cdd:MTH00026 423 GVNITFFPQHFLGLAGLPRRYADYPDNFEDFNQISSFGSIISIIAVIWFIVVIFDAYYREEPFdINIMAKGplipfscqp 502

                        250       260
                 ....*....|....*....|....*
gi 55826777  234 ---SSLEWLSSYPPINHSYNEIPAI 255
Cdd:MTH00026 503 ahfDTLEWSLTSPPEHHTYNELPYI 527
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
8-255 3.44e-74

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 235.02  E-value: 3.44e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55826777   8 KKETFGALGMIYALMAIGFLGFVVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWITTLHGTKINNNSSLWWAMG 87
Cdd:COG0843 265 RKPLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLFALG 344

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55826777  88 FIFLFTMGGLTGIMLSNSSIDIVLHDTYYVVAHFHYVLSMGAVFAIIASFIHWFPLITGYSLNNFLLNIQFLSMFIGVNL 167
Cdd:COG0843 345 FIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKIHFWLWFIGFNL 424

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55826777 168 TFFPQHFLGLSGMPRRYSDYPDTFLAWNMISSIGSILSILSLIFLMFL---IWEALSSKRMIMNLFFLNsSLEWLSSYPP 244
Cdd:COG0843 425 TFFPMHILGLLGMPRRYATYPPEPGWQPLNLISTIGAFILAVGFLLFLinlVVSLRKGPKAGGNPWGAR-TLEWATPSPP 503

                       250
                ....*....|.
gi 55826777 245 INHSYNEIPAI 255
Cdd:COG0843 504 PLYNFASIPVV 514
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 8-249 6.68e-74

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: 233.27  E-value: 6.68e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55826777     8 KKETFGALGMIYALMAIGFLGFVVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWITTLHGTKINNNSSLWWAMG 87
Cdd:TIGR02891 256 RKPIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLFALG 335

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55826777    88 FIFLFTMGGLTGIMLSNSSIDIVLHDTYYVVAHFHYVLSMGAVFAIIASFIHWFPLITGYSLNNFLLNIQFLSMFIGVNL 167
Cdd:TIGR02891 336 FIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLGRWHFWLTFVGFNL 415

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55826777   168 TFFPQHFLGLSGMPRRYSDYPD--TFLAWNMISSIGSILSILSLIFLMFLIWEALSSKRMIMNLFFLNSSLEWLSSYPPI 245
Cdd:TIGR02891 416 TFFPMHLLGLLGMPRRYYTYPPqmGFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGPKAGANPWGATTLEWTTSSPPP 495


                  ....
gi 55826777   246 NHSY 249
Cdd:TIGR02891 496 AHNF 499
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 1-236 1.17e-73

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 233.03  E-value: 1.17e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55826777    1 IIMNESGKKETFGALGMIYALMAIGFLGFVVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWITTLHGTKIN-NN 79
Cdd:MTH00048 255 ICLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFSWLYMLLNSRVRkSD 334

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55826777   80 SSLWWAMGFIFLFTMGGLTGIMLSNSSIDIVLHDTYYVVAHFHYVLSMGAVFAIIASFIHWFPLITGYSLNNFLLNIQFL 159
Cdd:MTH00048 335 PVVWWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWPLITGLSLNKYLLQCHCI 414

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 55826777  160 SMFIGVNLTFFPQHFLGLSGMPRRYSDYPDTFLAWNMISSIGSILSILSLIFLMFLIWEALSSKRMIMNLFFLNSSL 236
Cdd:MTH00048 415 ISMIGFNLCFFPMHYFGLCGLPRRVCVYEPSYYWINVVCTVGSFISAFSGCFFVFILWESLVVKNEVLGLWGSSSCV 491
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 8-249 3.31e-69

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: 220.92  E-value: 3.31e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55826777   8 KKETFGALGMIYALMAIGFLGFVVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWITTLHGTKINNNSSLWWAMG 87
Cdd:cd01662 257 RKPLFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLFTMWRGRIRFETPMLWAIG 336

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55826777  88 FIFLFTMGGLTGIMLSNSSIDIVLHDTYYVVAHFHYVLSMGAVFAIIASFIHWFPLITGYSLNNFLLNIQFLSMFIGVNL 167
Cdd:cd01662 337 FLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRMLNERLGKWSFWLWFIGFNL 416

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55826777 168 TFFPQHFLGLSGMPRRYSDYP--DTFLAWNMISSI-GSILSILSLIFLMFLIWEALSSKRMIMNLFFLNSSLEWLSSYPP 244
Cdd:cd01662 417 TFFPMHILGLMGMPRRVYTYLpgPGWDPLNLISTIgAFLIAAGVLLFLINVIVSIRKGKRDATGDPWGARTLEWATSSPP 496


                ....*
gi 55826777 245 INHSY 249
Cdd:cd01662 497 PAYNF 501
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 8-186 2.97e-55

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: 183.16  E-value: 2.97e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55826777     8 KKETFGALGMIYALMAIGFLGFVVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWITTLHGTKIN-NNSSLWWAM 86
Cdd:pfam00115 231 GRPLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRfRTTPMLFFL 310

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55826777    87 GFIFLFTMGGLTGIMLSNSSIDIVLHDTYYVVAHFHYVLSMGAVFAIIASFIHWFPLITGYSLNNFLLNIQFLSMFIGVN 166
Cdd:pfam00115 311 GFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFWLLFIGFN 390

                         170       180
                  ....*....|....*....|
gi 55826777   167 LTFFPQHFLGLSGMPRRYSD 186
Cdd:pfam00115 391 LTFFPMHILGLLGMPRRYAP 410
CyoB TIGR02843
cytochrome o ubiquinol oxidase, subunit I; Cytochrome o terminal oxidase complex is the ...
 8-255 1.50e-48

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: 169.47  E-value: 1.50e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55826777     8 KKETFGALGMIYALMAIGFLGFVVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWITTLHGTKINNNSSLWWAMG 87
Cdd:TIGR02843 306 RKRLFGYTSMVWATIAITVLSFIVWLHHFFTMGAGANVNAFFGIATMIIAIPTGVKIFNWLFTMYKGRIRFETPMLWTIG 385

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55826777    88 FIFLFTMGGLTGIMLSNSSIDIVLHDTYYVVAHFHYVLSMGAVFAIIASFIHWFPLITGYSLNNFLLNIQFLSMFIGVNL 167
Cdd:TIGR02843 386 FMVTFSIGGMTGVLLAVPPADFVLHNSLFLIAHFHNVIIGGVVFGCFAGLTYWFPKAFGFKLNEKLGKRSFWCWFIGFYL 465

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55826777   168 TFFPQHFLGLSGMPRRYSDYPD-TFLAWNMISSIGSILSILSLIFLMFLIWEALSSKRMIMNLF---FLNSSLEWLSSYP 243
Cdd:TIGR02843 466 AFMPLYILGFMGMTRRLNHYDNpEWHPMLIIAAFGAFLIACGILCQIIQIFVSIRDRDQNRDTTgdpWGGRTLEWSTSSP 545

                         250
                  ....*....|..
gi 55826777   244 PINHSYNEIPAI 255
Cdd:TIGR02843 546 PPFYNFAVIPKV 557
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 8-255 1.74e-40

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 147.39  E-value: 1.74e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55826777    8 KKETFGALGMIYALMAIGFLGFVVWAHHMFTIGLDVDTRAYFTSATMIIAIPTGIKIFSWITTLHGTKINNNSSLWWAMG 87
Cdd:PRK15017 307 RKRLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVKIFNWLFTMYQGRIVFHSAMLWTIG 386

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55826777   88 FIFLFTMGGLTGIMLSNSSIDIVLHDTYYVVAHFHYVLSMGAVFAIIASFIHWFPLITGYSLNNFLLNIQFLSMFIGVNL 167
Cdd:PRK15017 387 FIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYWWPKAFGFKLNETWGKRAFWFWIIGFFV 466

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55826777  168 TFFPQHFLGLSGMPRRYSDYPD-TFLAWNMISSIGSILSILSLIFLMFLIWEALSSKRMIMNLF---FLNSSLEWLSSYP 243
Cdd:PRK15017 467 AFMPLYALGFMGMTRRLSQQIDpQFHTMLMIAASGAALIALGILCQVIQMYVSIRDRDQNRDLTgdpWGGRTLEWATSSP 546

                        250
                 ....*....|..
gi 55826777  244 PINHSYNEIPAI 255
Cdd:PRK15017 547 PPFYNFAVVPHV 558
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
 53-193 1.86e-08

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: 54.21  E-value: 1.86e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55826777  53 TMIIAIPTGIKIFSWITTL-HGTKINNNS-------SLWW--------AMGFIFlFTMGGLTGIMLSNSSIDIVLHDTYY 116
Cdd:cd01660 282 TFMVALPSLLTAFTVFASLeIAGRLRGGKglfgwirALPWgdpmflalFLAMLM-FIPGGAGGIINASYQLNYVVHNTAW 360

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55826777 117 VVAHFHYVLSMGAVFAIIASFIHWFPLITGYSL-NNFLLNIQFLSMFIGVNLTFFPQHFLGLSGMPRR--YSDYPDTFLA 193
Cdd:cd01660 361 VPGHFHLTVGGAVALTFMAVAYWLVPHLTGRELaAKRLALAQPWLWFVGMTIMSTAMHVAGLLGAPRRtaEAQYGGLPAA 440
 
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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