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Conserved domains on  [gi|407361533|gb|AFU10339|]
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cytochrome oxidase subunit I, partial (mitochondrion) [Sarcophaga hirtipes]

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 ...
 1-150 3.24e-88

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: 265.96  E-value: 3.24e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407361533   1 LFLFTVGWLTGDVFAYSSLDIIFHYTYFVVAYFHYVLSIGAVFAIIAVFVHWYPLFTGFTFNNKMLKSQFTIMFIGVNLT 80
Cdd:MTH00153 343 VFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIMFIGVNLT 422

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407361533  81 FFPQHFLGLAGMPRRYSDYPDAYTAWNVISTIGSTISLLGILFFFFIIWESLASQRQVMFPVQLNSSIEW 150
Cdd:MTH00153 423 FFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPVLFSLNLSSSIEW 492
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-150 3.24e-88

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 265.96  E-value: 3.24e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407361533   1 LFLFTVGWLTGDVFAYSSLDIIFHYTYFVVAYFHYVLSIGAVFAIIAVFVHWYPLFTGFTFNNKMLKSQFTIMFIGVNLT 80
Cdd:MTH00153 343 VFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIMFIGVNLT 422

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407361533  81 FFPQHFLGLAGMPRRYSDYPDAYTAWNVISTIGSTISLLGILFFFFIIWESLASQRQVMFPVQLNSSIEW 150
Cdd:MTH00153 423 FFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPVLFSLNLSSSIEW 492
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-150 1.24e-73

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: 227.75  E-value: 1.24e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407361533   1 LFLFTVGWLTGDVFAYSSLDIIFHYTYFVVAYFHYVLSIGAVFAIIAVFVHWYPLFTGFTFNNKMLKSQFTIMFIGVNLT 80
Cdd:cd01663  336 IFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHFWLMFIGVNLT 415

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 407361533  81 FFPQHFLGLAGMPRRYSDYPDAYTAWNVISTIGSTISLLGILFFFFIIWESLASQRQVMFPV-QLNSSIEW 150
Cdd:cd01663  416 FFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFNVgEGSTSLEW 486
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-132 5.17e-40

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 140.65  E-value: 5.17e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407361533   1 LFLFTVGWLTGDVFAYSSLDIIFHYTYFVVAYFHYVLSIGAVFAIIAVFVHWYPLFTGFTFNNKMLKSQFTIMFIGVNLT 80
Cdd:COG0843  346 IILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKIHFWLWFIGFNLT 425

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 407361533  81 FFPQHFLGLAGMPRRYSDYP--DAYTAWNVISTIGSTISLLGILFFFFIIWESL 132
Cdd:COG0843  426 FFPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAFILAVGFLLFLINLVVSL 479
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-138 7.93e-39

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: 136.97  E-value: 7.93e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407361533    1 LFLFTVGWLTGDVFAYSSLDIIFHYTYFVVAYFHYVLSIGAVFAIIAVFVHWYPLFTGFTFNNKMLKSQFTIMFIGVNLT 80
Cdd:TIGR02891 337 IFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLGRWHFWLTFVGFNLT 416

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 407361533   81 FFPQHFLGLAGMPRRYSDYPDA--YTAWNVISTIGSTISLLGILFFFFIIWESLASQRQV 138
Cdd:TIGR02891 417 FFPMHLLGLLGMPRRYYTYPPQmgFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGPKA 476
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-116 2.24e-25

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: 99.57  E-value: 2.24e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407361533    1 LFLFTVGWLTGDVFAYSSLDIIFHYTYFVVAYFHYVLSIGAVFAIIAVFVHWYPLFTGFTFNNKMLKSQFTIMFIGVNLT 80
Cdd:pfam00115 313 AFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFWLLFIGFNLT 392

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 407361533   81 FFPQHFLGLAGMPRRYS----DYPDAYTAWNVISTIGSTI 116
Cdd:pfam00115 393 FFPMHILGLLGMPRRYAppfiETVPAFQPLNWIRTIGGVL 432
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-150 3.24e-88

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 265.96  E-value: 3.24e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407361533   1 LFLFTVGWLTGDVFAYSSLDIIFHYTYFVVAYFHYVLSIGAVFAIIAVFVHWYPLFTGFTFNNKMLKSQFTIMFIGVNLT 80
Cdd:MTH00153 343 VFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIMFIGVNLT 422

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407361533  81 FFPQHFLGLAGMPRRYSDYPDAYTAWNVISTIGSTISLLGILFFFFIIWESLASQRQVMFPVQLNSSIEW 150
Cdd:MTH00153 423 FFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPVLFSLNLSSSIEW 492
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-150 1.24e-73

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: 227.75  E-value: 1.24e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407361533   1 LFLFTVGWLTGDVFAYSSLDIIFHYTYFVVAYFHYVLSIGAVFAIIAVFVHWYPLFTGFTFNNKMLKSQFTIMFIGVNLT 80
Cdd:cd01663  336 IFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHFWLMFIGVNLT 415

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 407361533  81 FFPQHFLGLAGMPRRYSDYPDAYTAWNVISTIGSTISLLGILFFFFIIWESLASQRQVMFPV-QLNSSIEW 150
Cdd:cd01663  416 FFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFNVgEGSTSLEW 486
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-150 1.14e-71

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 223.43  E-value: 1.14e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407361533   1 LFLFTVGWLTGDVFAYSSLDIIFHYTYFVVAYFHYVLSIGAVFAIIAVFVHWYPLFTGFTFNNKMLKSQFTIMFIGVNLT 80
Cdd:MTH00116 345 IFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGYTLHQTWTKAQFGVMFTGVNLT 424

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407361533  81 FFPQHFLGLAGMPRRYSDYPDAYTAWNVISTIGSTISLLGILFFFFIIWESLASQRQVMFPVQLNSSIEW 150
Cdd:MTH00116 425 FFPQHFLGLAGMPRRYSDYPDAYTLWNTISSIGSLISMTAVIMLMFIIWEAFSSKRKVLQPELTTTNIEW 494
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-150 3.06e-71

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 222.24  E-value: 3.06e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407361533   1 LFLFTVGWLTGDVFAYSSLDIIFHYTYFVVAYFHYVLSIGAVFAIIAVFVHWYPLFTGFTFNNKMLKSQFTIMFIGVNLT 80
Cdd:MTH00167 345 IFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGLTLNETWTKIHFFVMFIGVNLT 424

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407361533  81 FFPQHFLGLAGMPRRYSDYPDAYTAWNVISTIGSTISLLGILFFFFIIWESLASQRQVMFPVQLNSSIEW 150
Cdd:MTH00167 425 FFPQHFLGLAGMPRRYSDYPDAYTLWNVVSSIGSLISLVAVILFLFIIWEAFSSKRKLLPVELTSTNVEW 494
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-150 1.88e-69

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 217.54  E-value: 1.88e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407361533   1 LFLFTVGWLTGDVFAYSSLDIIFHYTYFVVAYFHYVLSIGAVFAIIAVFVHWYPLFTGFTFNNKMLKSQFTIMFIGVNLT 80
Cdd:MTH00223 342 IFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLFTGVTLHRRWAKAHFFLMFLGVNLT 421

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407361533  81 FFPQHFLGLAGMPRRYSDYPDAYTAWNVISTIGSTISLLGILFFFFIIWESLASQRQVMFPVQLNSSIEW 150
Cdd:MTH00223 422 FFPQHFLGLAGMPRRYSDYPDCYTKWNQVSSFGSMISFVSVLFFMFIVWEAFVSQRSVVWSGHLSTSLEW 491
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-150 2.12e-68

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 214.97  E-value: 2.12e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407361533   1 LFLFTVGWLTGDVFAYSSLDIIFHYTYFVVAYFHYVLSIGAVFAIIAVFVHWYPLFTGFTFNNKMLKSQFTIMFIGVNLT 80
Cdd:MTH00142 343 IFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLFTGLTLNPRWLKAHFYTMFIGVNLT 422

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407361533  81 FFPQHFLGLAGMPRRYSDYPDAYTAWNVISTIGSTISLLGILFFFFIIWESLASQRQVMFPVQLNSSIEW 150
Cdd:MTH00142 423 FFPQHFLGLAGMPRRYSDYPDAYTTWNVVSSLGSMISFIAVLMFVFIVWESFVSQRLVMWSSHLSTSLEW 492
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-150 6.96e-62

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 198.18  E-value: 6.96e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407361533   1 LFLFTVGWLTGDVFAYSSLDIIFHYTYFVVAYFHYVLSIGAVFAIIAVFVHWYPLFTGFTFNNKMLKSQFTIMFIGVNLT 80
Cdd:MTH00103 345 IFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLNDTWAKIHFTIMFVGVNMT 424

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407361533  81 FFPQHFLGLAGMPRRYSDYPDAYTAWNVISTIGSTISLLGILFFFFIIWESLASQRQVMFPVQLNSSIEW 150
Cdd:MTH00103 425 FFPQHFLGLSGMPRRYSDYPDAYTTWNTVSSMGSFISLTAVMLMIFMIWEAFASKREVLTVELTTTNLEW 494
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-150 1.22e-61

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 197.45  E-value: 1.22e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407361533   1 LFLFTVGWLTGDVFAYSSLDIIFHYTYFVVAYFHYVLSIGAVFAIIAVFVHWYPLFTGFTFNNKMLKSQFTIMFIGVNLT 80
Cdd:MTH00183 345 IFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLFSGYTLHSTWTKIHFGVMFVGVNLT 424

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407361533  81 FFPQHFLGLAGMPRRYSDYPDAYTAWNVISTIGSTISLLGILFFFFIIWESLASQRQVMFPVQLNSSIEW 150
Cdd:MTH00183 425 FFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMFLFILWEAFAAKREVLSVELTSTNVEW 494
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-150 2.75e-61

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 196.70  E-value: 2.75e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407361533   1 LFLFTVGWLTGDVFAYSSLDIIFHYTYFVVAYFHYVLSIGAVFAIIAVFVHWYPLFTGFTFNNKMLKSQFTIMFIGVNLT 80
Cdd:MTH00077 345 IFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLHSTWSKIHFGVMFIGVNLT 424

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407361533  81 FFPQHFLGLAGMPRRYSDYPDAYTAWNVISTIGSTISLLGILFFFFIIWESLASQRQVMFPVQLNSSIEW 150
Cdd:MTH00077 425 FFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMMMFIIWEAFSSKREVLTTELTSTNIEW 494
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-150 8.84e-61

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 195.12  E-value: 8.84e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407361533   1 LFLFTVGWLTGDVFAYSSLDIIFHYTYFVVAYFHYVLSIGAVFAIIAVFVHWYPLFTGFTFNNKMLKSQFTIMFIGVNLT 80
Cdd:MTH00007 342 IFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTGLTLHDRWAKAHFFLMFLGVNLT 421

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407361533  81 FFPQHFLGLAGMPRRYSDYPDAYTAWNVISTIGSTISLLGILFFFFIIWESLASQRQVMFPVQLNSSIEW 150
Cdd:MTH00007 422 FFPQHFLGLSGMPRRYSDYPDAYTKWNVVSSFGSMLSFVALLLFIFILWEAFSAQRGVIASPHMSSSLEW 491
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-150 1.04e-60

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 195.05  E-value: 1.04e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407361533   1 LFLFTVGWLTGDVFAYSSLDIIFHYTYFVVAYFHYVLSIGAVFAIIAVFVHWYPLFTGFTFNNKMLKSQFTIMFIGVNLT 80
Cdd:MTH00037 345 VFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLFSGVSLHPLWSKVHFFLMFIGVNLT 424

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407361533  81 FFPQHFLGLAGMPRRYSDYPDAYTAWNVISTIGSTISLLGILFFFFIIWESLASQRQVMFPVQLNSSIEW 150
Cdd:MTH00037 425 FFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSTISLVATLFFLFLIWEAFASQREVISPEFSSSSLEW 494
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-150 1.14e-48

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 163.31  E-value: 1.14e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407361533   1 LFLFTVGWLTGDVFAYSSLDIIFHYTYFVVAYFHYVLSIGAVFAIIAVFVHWYPLFTGFTFNNKMLKSQFTIMFIGVNLT 80
Cdd:MTH00079 345 IFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFMTGIVYDKLMMSAVFFLMFVGVNLT 424

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407361533  81 FFPQHFLGLAGMPRRYSDYPDAYTAWNVISTIGSTISLLGILFFFFIIWESLASQRQVMFPVQLNSSIEW 150
Cdd:MTH00079 425 FFPLHFAGLHGMPRKYLDYPDVYSVWNVISSYGSMISVFALFLFIYVLLESFFSYRLVLHDNYINSSPEY 494
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-150 4.52e-46

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 156.52  E-value: 4.52e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407361533   1 LFLFTVGWLTGDVFAYSSLDIIFHYTYFVVAYFHYVLSIGAVFAIIAVFVHWYPLFTGFTFNNKMLKSQFTIMFIGVNLT 80
Cdd:MTH00182 347 VFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNELYGKIHFWLMFIGVNLT 426

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 407361533  81 FFPQHFLGLAGMPRRYSDYPDAYTAWNVISTIGSTISLLGILFFFFIIWESLASQRQVMFPVQLN----SSIEW 150
Cdd:MTH00182 427 FFPQHFLGLAGFPRRYSDFADAFAGWNLVSSLGSIISIVGVVWFIYIIYDAYVREEKFIGWKEGTgeswASLEW 500
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-132 1.71e-45

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: 153.84  E-value: 1.71e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407361533   1 LFLFTVGWLTGDVFAYSSLDIIFHYTYFVVAYFHYVLSIGAVFAIIAVFVHWYPLFTGFTFNNKMLKSQFTIMFIGVNLT 80
Cdd:cd00919  332 LFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKLGKIHFWLWFIGFNLT 411

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 407361533  81 FFPQHFLGLAGMPRRYSDYPDAYTAWNVISTIGSTISLLGILFFFFIIWESL 132
Cdd:cd00919  412 FFPMHFLGLLGMPRRYADYPDGFAPWNFISSVGAFILGLGLLLFLGNLFLSL 463
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-135 7.65e-45

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 153.44  E-value: 7.65e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407361533   1 LFLFTVGWLTGDVFAYSSLDIIFHYTYFVVAYFHYVLSIGAVFAIIAVFVHWYPLFTGFTFNNKMLKSQFTIMFIGVNLT 80
Cdd:MTH00184 347 VFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNEVYGKIHFWLMFIGVNLT 426

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 407361533  81 FFPQHFLGLAGMPRRYSDYPDAYTAWNVISTIGSTISLLGILFFFFIIWESLASQ 135
Cdd:MTH00184 427 FFPQHFLGLAGLPRRYSDFHDSFAGWNQISSLGSVISIVGVVWFIYIVYDAYVRE 481
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-132 5.17e-40

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 140.65  E-value: 5.17e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407361533   1 LFLFTVGWLTGDVFAYSSLDIIFHYTYFVVAYFHYVLSIGAVFAIIAVFVHWYPLFTGFTFNNKMLKSQFTIMFIGVNLT 80
Cdd:COG0843  346 IILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKIHFWLWFIGFNLT 425

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 407361533  81 FFPQHFLGLAGMPRRYSDYP--DAYTAWNVISTIGSTISLLGILFFFFIIWESL 132
Cdd:COG0843  426 FFPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAFILAVGFLLFLINLVVSL 479
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-138 7.93e-39

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: 136.97  E-value: 7.93e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407361533    1 LFLFTVGWLTGDVFAYSSLDIIFHYTYFVVAYFHYVLSIGAVFAIIAVFVHWYPLFTGFTFNNKMLKSQFTIMFIGVNLT 80
Cdd:TIGR02891 337 IFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLGRWHFWLTFVGFNLT 416

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 407361533   81 FFPQHFLGLAGMPRRYSDYPDA--YTAWNVISTIGSTISLLGILFFFFIIWESLASQRQV 138
Cdd:TIGR02891 417 FFPMHLLGLLGMPRRYYTYPPQmgFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGPKA 476
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 1-139 3.67e-38

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 135.19  E-value: 3.67e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407361533   1 LFLFTVGWLTGDVFAYSSLDIIFHYTYFVVAYFHYVLSIGAVFAIIAVFVHWYPLFTGFTFNNKMLKSQFTIMFIGVNLT 80
Cdd:MTH00048 344 IVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWPLITGLSLNKYLLQCHCIISMIGFNLC 423

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 407361533  81 FFPQHFLGLAGMPRRYSDYPDAYTAWNVISTIGSTISLLGILFFFFIIWESLASQRQVM 139
Cdd:MTH00048 424 FFPMHYFGLCGLPRRVCVYEPSYYWINVVCTVGSFISAFSGCFFVFILWESLVVKNEVL 482
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-131 6.40e-35

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 126.67  E-value: 6.40e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407361533   1 LFLFTVGWLTGDVFAYSSLDIIFHYTYFVVAYFHYVLSIGAVFAIIAVFVHWYPLFTGFTFNNKMLKSQFTIMFIGVNLT 80
Cdd:MTH00026 348 IFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWFGKITGYAYKDIYGLIHFWLMFIGVNIT 427

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 407361533  81 FFPQHFLGLAGMPRRYSDYPDAYTAWNVISTIGSTISLLGILFFFFIIWES 131
Cdd:MTH00026 428 FFPQHFLGLAGLPRRYADYPDNFEDFNQISSFGSIISIIAVIWFIVVIFDA 478
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 1-132 2.31e-34

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: 125.00  E-value: 2.31e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407361533   1 LFLFTVGWLTGDVFAYSSLDIIFHYTYFVVAYFHYVLSIGAVFAIIAVFVHWYPLFTGFTFNNKMLKSQFTIMFIGVNLT 80
Cdd:cd01662  338 LVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRMLNERLGKWSFWLWFIGFNLT 417

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 407361533  81 FFPQHFLGLAGMPRRYSDYP--DAYTAWNVISTIGSTISLLGILFFFFIIWESL 132
Cdd:cd01662  418 FFPMHILGLMGMPRRVYTYLpgPGWDPLNLISTIGAFLIAAGVLLFLINVIVSI 471
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-116 2.24e-25

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: 99.57  E-value: 2.24e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407361533    1 LFLFTVGWLTGDVFAYSSLDIIFHYTYFVVAYFHYVLSIGAVFAIIAVFVHWYPLFTGFTFNNKMLKSQFTIMFIGVNLT 80
Cdd:pfam00115 313 AFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFWLLFIGFNLT 392

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 407361533   81 FFPQHFLGLAGMPRRYS----DYPDAYTAWNVISTIGSTI 116
Cdd:pfam00115 393 FFPMHILGLLGMPRRYAppfiETVPAFQPLNWIRTIGGVL 432
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
 1-132 3.83e-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: 51.13  E-value: 3.83e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407361533   1 LFLFTVGWLTGDVFAYSSLDIIFHYTYFVVAYFHyvLSIGAVFAIIAVFVHWY--PLFTGFTF-NNKMLKSQFTIMFIGV 77
Cdd:cd01660  333 MLMFIPGGAGGIINASYQLNYVVHNTAWVPGHFH--LTVGGAVALTFMAVAYWlvPHLTGRELaAKRLALAQPWLWFVGM 410

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 407361533  78 NLTFFPQHFLGLAGMPRR--YSDYPDAY-----TAWNVISTIGSTISLLGILFFFFIIWESL 132
Cdd:cd01660  411 TIMSTAMHVAGLLGAPRRtaEAQYGGLPaagewAPYQQLMAIGGTILFVSGALFLYILFRTL 472
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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