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Conserved domains on  [gi|14549805|gb|AAK66991|]
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cytochrome oxidase subunit I, partial (mitochondrion) [Conostigmus sp. M85]

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 ...
 1-139 2.03e-91

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: 273.67  E-value: 2.03e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14549805    1 YILILPGFGLISHMICNESMKKEVFGTMGMIYAMISIGLLGFIVWAHHMFTIGMDVDTRAYFTSATMIIAVPTGIKIFSW 80
Cdd:MTH00153 242 YILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSW 321

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 14549805   81 LASMNGMKIYMNVTNLWLLGFIFLFTLGGLTGIMLSNSSIDIVLHDTYYVVAHFHYVLS 139
Cdd:MTH00153 322 LATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLS 380
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-139 2.03e-91

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 273.67  E-value: 2.03e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14549805    1 YILILPGFGLISHMICNESMKKEVFGTMGMIYAMISIGLLGFIVWAHHMFTIGMDVDTRAYFTSATMIIAVPTGIKIFSW 80
Cdd:MTH00153 242 YILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSW 321

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 14549805   81 LASMNGMKIYMNVTNLWLLGFIFLFTLGGLTGIMLSNSSIDIVLHDTYYVVAHFHYVLS 139
Cdd:MTH00153 322 LATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLS 380
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-139 1.16e-88

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: 265.89  E-value: 1.16e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14549805   1 YILILPGFGLISHMICNESMKKEVFGTMGMIYAMISIGLLGFIVWAHHMFTIGMDVDTRAYFTSATMIIAVPTGIKIFSW 80
Cdd:cd01663 235 YILILPGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSW 314

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 14549805  81 LASMNGMKIYMNVTNLWLLGFIFLFTLGGLTGIMLSNSSIDIVLHDTYYVVAHFHYVLS 139
Cdd:cd01663 315 LATMWGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLS 373
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-138 5.96e-53

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 174.55  E-value: 5.96e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14549805   1 YILILPGFGLISHMICNESmKKEVFGTMGMIYAMISIGLLGFIVWAHHMFTIGMDVDTRAYFTSATMIIAVPTGIKIFSW 80
Cdd:COG0843 246 YILILPAFGIVSEIIPTFS-RKPLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNW 324

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 14549805  81 LASMNGMKIYMNVTNLWLLGFIFLFTLGGLTGIMLSNSSIDIVLHDTYYVVAHFHYVL 138
Cdd:COG0843 325 IATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVL 382
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-138 9.93e-53

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: 173.18  E-value: 9.93e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14549805     1 YILILPGFGLISHMICNESmKKEVFGTMGMIYAMISIGLLGFIVWAHHMFTIGMDVDTRAYFTSATMIIAVPTGIKIFSW 80
Cdd:TIGR02891 237 YIIFLPAFGIISEILPTFA-RKPIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNW 315

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 14549805    81 LASMNGMKIYMNVTNLWLLGFIFLFTLGGLTGIMLSNSSIDIVLHDTYYVVAHFHYVL 138
Cdd:TIGR02891 316 IATLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVL 373
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-138 5.14e-38

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: 133.08  E-value: 5.14e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14549805     1 YILILPGFGLISHMICNESmKKEVFGTMGMIYAMISIGLLGFIVWAHHMFTIGMDVDTRAYFTSATMIIAVPTGIKIFSW 80
Cdd:pfam00115 212 YILILPAFGIIYYILPKFA-GRPLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNW 290

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 14549805    81 LASMNGMKIYMNVT-NLWLLGFIFLFTLGGLTGIMLSNSSIDIVLHDTYYVVAHFHYVL 138
Cdd:pfam00115 291 LATLWGGWIRFRTTpMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVL 349
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-139 2.03e-91

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 273.67  E-value: 2.03e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14549805    1 YILILPGFGLISHMICNESMKKEVFGTMGMIYAMISIGLLGFIVWAHHMFTIGMDVDTRAYFTSATMIIAVPTGIKIFSW 80
Cdd:MTH00153 242 YILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSW 321

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 14549805   81 LASMNGMKIYMNVTNLWLLGFIFLFTLGGLTGIMLSNSSIDIVLHDTYYVVAHFHYVLS 139
Cdd:MTH00153 322 LATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLS 380
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-139 1.16e-88

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: 265.89  E-value: 1.16e-88
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14549805   1 YILILPGFGLISHMICNESMKKEVFGTMGMIYAMISIGLLGFIVWAHHMFTIGMDVDTRAYFTSATMIIAVPTGIKIFSW 80
Cdd:cd01663 235 YILILPGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSW 314

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 14549805  81 LASMNGMKIYMNVTNLWLLGFIFLFTLGGLTGIMLSNSSIDIVLHDTYYVVAHFHYVLS 139
Cdd:cd01663 315 LATMWGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLS 373
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-139 6.79e-81

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 246.81  E-value: 6.79e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14549805    1 YILILPGFGLISHMICNESMKKEVFGTMGMIYAMISIGLLGFIVWAHHMFTIGMDVDTRAYFTSATMIIAVPTGIKIFSW 80
Cdd:MTH00223 241 YILILPGFGMISHIVSHYSSKKEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSW 320

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 14549805   81 LASMNGMKIYMNVTNLWLLGFIFLFTLGGLTGIMLSNSSIDIVLHDTYYVVAHFHYVLS 139
Cdd:MTH00223 321 LATIYGSKIKYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLS 379
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-139 7.71e-78

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 238.81  E-value: 7.71e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14549805    1 YILILPGFGLISHMICNESMKKEVFGTMGMIYAMISIGLLGFIVWAHHMFTIGMDVDTRAYFTSATMIIAVPTGIKIFSW 80
Cdd:MTH00167 244 YILILPGFGMISHIVVYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSW 323

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 14549805   81 LASMNGMKIYMNVTNLWLLGFIFLFTLGGLTGIMLSNSSIDIVLHDTYYVVAHFHYVLS 139
Cdd:MTH00167 324 LATLHGGKIKWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLS 382
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-139 1.42e-76

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 235.76  E-value: 1.42e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14549805    1 YILILPGFGLISHMICNESMKKEVFGTMGMIYAMISIGLLGFIVWAHHMFTIGMDVDTRAYFTSATMIIAVPTGIKIFSW 80
Cdd:MTH00116 244 YILILPGFGIISHIVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSW 323

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 14549805   81 LASMNGMKIYMNVTNLWLLGFIFLFTLGGLTGIMLSNSSIDIVLHDTYYVVAHFHYVLS 139
Cdd:MTH00116 324 LATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLS 382
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-139 3.15e-74

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 229.61  E-value: 3.15e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14549805    1 YILILPGFGLISHMICNESMKKEVFGTMGMIYAMISIGLLGFIVWAHHMFTIGMDVDTRAYFTSATMIIAVPTGIKIFSW 80
Cdd:MTH00142 242 YILILPGFGMISHIINHYSGKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFSW 321

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 14549805   81 LASMNGMKIYMNVTNLWLLGFIFLFTLGGLTGIMLSNSSIDIVLHDTYYVVAHFHYVLS 139
Cdd:MTH00142 322 LATLHGSKVKYEPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLS 380
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-139 1.21e-67

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 212.77  E-value: 1.21e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14549805    1 YILILPGFGLISHMICNESMKKEVFGTMGMIYAMISIGLLGFIVWAHHMFTIGMDVDTRAYFTSATMIIAVPTGIKIFSW 80
Cdd:MTH00037 244 YILILPGFGMISHVIAHYSGKQEPFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSW 323

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 14549805   81 LASMNGMKIYMNVTNLWLLGFIFLFTLGGLTGIMLSNSSIDIVLHDTYYVVAHFHYVLS 139
Cdd:MTH00037 324 MATLQGSNLRWETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLS 382
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-139 8.84e-67

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 209.92  E-value: 8.84e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14549805    1 YILILPGFGLISHMICNESMKKEVFGTMGMIYAMISIGLLGFIVWAHHMFTIGMDVDTRAYFTSATMIIAVPTGIKIFSW 80
Cdd:MTH00079 244 YILILPAFGIISQSTLYLTGKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSW 323

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 14549805   81 LASMNGMKIYMNVTNLWLLGFIFLFTLGGLTGIMLSNSSIDIVLHDTYYVVAHFHYVLS 139
Cdd:MTH00079 324 LATLFGMKMKFQPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLS 382
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-139 5.19e-66

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 208.22  E-value: 5.19e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14549805    1 YILILPGFGLISHMICNESMKKEVFGTMGMIYAMISIGLLGFIVWAHHMFTIGMDVDTRAYFTSATMIIAVPTGIKIFSW 80
Cdd:MTH00007 241 YILILPGFGAISHIVTHYAGKLEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSW 320

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 14549805   81 LASMNGMKIYMNVTNLWLLGFIFLFTLGGLTGIMLSNSSIDIVLHDTYYVVAHFHYVLS 139
Cdd:MTH00007 321 LATIHGSPIKYETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLS 379
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-139 6.91e-66

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 207.85  E-value: 6.91e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14549805    1 YILILPGFGLISHMICNESMKKEVFGTMGMIYAMISIGLLGFIVWAHHMFTIGMDVDTRAYFTSATMIIAVPTGIKIFSW 80
Cdd:MTH00183 244 YILILPGFGMISHIVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSW 323

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 14549805   81 LASMNGMKIYMNVTNLWLLGFIFLFTLGGLTGIMLSNSSIDIVLHDTYYVVAHFHYVLS 139
Cdd:MTH00183 324 LATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLS 382
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-139 6.95e-66

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 207.81  E-value: 6.95e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14549805    1 YILILPGFGLISHMICNESMKKEVFGTMGMIYAMISIGLLGFIVWAHHMFTIGMDVDTRAYFTSATMIIAVPTGIKIFSW 80
Cdd:MTH00103 244 YILILPGFGMISHIVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSW 323

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 14549805   81 LASMNGMKIYMNVTNLWLLGFIFLFTLGGLTGIMLSNSSIDIVLHDTYYVVAHFHYVLS 139
Cdd:MTH00103 324 LATLHGGNIKWSPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLS 382
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-139 1.10e-65

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 207.49  E-value: 1.10e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14549805    1 YILILPGFGLISHMICNESMKKEVFGTMGMIYAMISIGLLGFIVWAHHMFTIGMDVDTRAYFTSATMIIAVPTGIKIFSW 80
Cdd:MTH00077 244 YILILPGFGMISHIVTYYSAKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVFSW 323

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 14549805   81 LASMNGMKIYMNVTNLWLLGFIFLFTLGGLTGIMLSNSSIDIVLHDTYYVVAHFHYVLS 139
Cdd:MTH00077 324 LATMHGGAIKWDAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLS 382
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-139 4.39e-64

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 203.51  E-value: 4.39e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14549805    1 YILILPGFGLISHMICNESMKKEVFGTMGMIYAMISIGLLGFIVWAHHMFTIGMDVDTRAYFTSATMIIAVPTGIKIFSW 80
Cdd:MTH00182 246 YILILPGFGMISQIIPTFVAKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSW 325

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 14549805   81 LASMNGMKIYMNVTNLWLLGFIFLFTLGGLTGIMLSNSSIDIVLHDTYYVVAHFHYVLS 139
Cdd:MTH00182 326 LATIYGGTLRLDTPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLS 384
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-139 1.04e-62

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 199.67  E-value: 1.04e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14549805    1 YILILPGFGLISHMICNESMKKEVFGTMGMIYAMISIGLLGFIVWAHHMFTIGMDVDTRAYFTSATMIIAVPTGIKIFSW 80
Cdd:MTH00184 246 YILILPGFGIISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSW 325

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 14549805   81 LASMNGMKIYMNVTNLWLLGFIFLFTLGGLTGIMLSNSSIDIVLHDTYYVVAHFHYVLS 139
Cdd:MTH00184 326 IATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLS 384
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-139 4.48e-56

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: 181.19  E-value: 4.48e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14549805   1 YILILPGFGLISHMICNESmKKEVFGTMGMIYAMISIGLLGFIVWAHHMFTIGMDVDTRAYFTSATMIIAVPTGIKIFSW 80
Cdd:cd00919 232 YILILPAFGAISEIIPTFS-GKPLFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNW 310

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 14549805  81 LASMNGMKIYMNVTNLWLLGFIFLFTLGGLTGIMLSNSSIDIVLHDTYYVVAHFHYVLS 139
Cdd:cd00919 311 LATLWGGRIRFDPPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLS 369
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-139 9.28e-54

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 176.74  E-value: 9.28e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14549805    1 YILILPGFGLISHMICNESMKKEVFGTMGMIYAMISIGLLGFIVWAHHMFTIGMDVDTRAYFTSATMIIAVPTGIKIFSW 80
Cdd:MTH00026 245 YILILPGFGIISQILSLFSYKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSW 324

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14549805   81 LASM--NGMKIYMNVTNLWLLGFIFLFTLGGLTGIMLSNSSIDIVLHDTYYVVAHFHYVLS 139
Cdd:MTH00026 325 LATVsgSGRNLIFTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLS 385
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-138 5.96e-53

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 174.55  E-value: 5.96e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14549805   1 YILILPGFGLISHMICNESmKKEVFGTMGMIYAMISIGLLGFIVWAHHMFTIGMDVDTRAYFTSATMIIAVPTGIKIFSW 80
Cdd:COG0843 246 YILILPAFGIVSEIIPTFS-RKPLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNW 324

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 14549805  81 LASMNGMKIYMNVTNLWLLGFIFLFTLGGLTGIMLSNSSIDIVLHDTYYVVAHFHYVL 138
Cdd:COG0843 325 IATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVL 382
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-138 9.93e-53

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: 173.18  E-value: 9.93e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14549805     1 YILILPGFGLISHMICNESmKKEVFGTMGMIYAMISIGLLGFIVWAHHMFTIGMDVDTRAYFTSATMIIAVPTGIKIFSW 80
Cdd:TIGR02891 237 YIIFLPAFGIISEILPTFA-RKPIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNW 315

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 14549805    81 LASMNGMKIYMNVTNLWLLGFIFLFTLGGLTGIMLSNSSIDIVLHDTYYVVAHFHYVL 138
Cdd:TIGR02891 316 IATLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVL 373
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 1-139 4.81e-52

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 171.78  E-value: 4.81e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14549805    1 YILILPGFGLISHMICNESMKKEVFGTMGMIYAMISIGLLGFIVWAHHMFTIGMDVDTRAYFTSATMIIAVPTGIKIFSW 80
Cdd:MTH00048 242 YVLILPGFGIISHICLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFSW 321

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 14549805   81 LASMNGMKIYMNVTNL-WLLGFIFLFTLGGLTGIMLSNSSIDIVLHDTYYVVAHFHYVLS 139
Cdd:MTH00048 322 LYMLLNSRVRKSDPVVwWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLS 381
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 1-138 4.53e-49

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: 163.52  E-value: 4.53e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14549805   1 YILILPGFGLISHMICNESmKKEVFGTMGMIYAMISIGLLGFIVWAHHMFTIGMDVDTRAYFTSATMIIAVPTGIKIFSW 80
Cdd:cd01662 238 YILILPAFGIFSEIVPTFS-RKPLFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNW 316

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 14549805  81 LASMNGMKIYMNVTNLWLLGFIFLFTLGGLTGIMLSNSSIDIVLHDTYYVVAHFHYVL 138
Cdd:cd01662 317 LFTMWRGRIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVL 374
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-138 5.14e-38

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: 133.08  E-value: 5.14e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14549805     1 YILILPGFGLISHMICNESmKKEVFGTMGMIYAMISIGLLGFIVWAHHMFTIGMDVDTRAYFTSATMIIAVPTGIKIFSW 80
Cdd:pfam00115 212 YILILPAFGIIYYILPKFA-GRPLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNW 290

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 14549805    81 LASMNGMKIYMNVT-NLWLLGFIFLFTLGGLTGIMLSNSSIDIVLHDTYYVVAHFHYVL 138
Cdd:pfam00115 291 LATLWGGWIRFRTTpMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVL 349
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 1-138 1.27e-34

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 126.20  E-value: 1.27e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14549805    1 YILILPGFGLISHMICNESmKKEVFGTMGMIYAMISIGLLGFIVWAHHMFTIGMDVDTRAYFTSATMIIAVPTGIKIFSW 80
Cdd:PRK15017 288 YILILPVFGVFSEIAATFS-RKRLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVKIFNW 366

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 14549805   81 LASMNGMKIYMNVTNLWLLGFIFLFTLGGLTGIMLSNSSIDIVLHDTYYVVAHFHYVL 138
Cdd:PRK15017 367 LFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHFHNVI 424
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
 66-135 4.19e-03

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: 36.11  E-value: 4.19e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14549805  66 TMIIAVPTGIKIFSWLASMN-------GMKIYMNVTNLW-----LLGFIF---LFTLGGLTGIMLSNSSIDIVLHDTYYV 130
Cdd:cd01660 282 TFMVALPSLLTAFTVFASLEiagrlrgGKGLFGWIRALPwgdpmFLALFLamlMFIPGGAGGIINASYQLNYVVHNTAWV 361


                ....*
gi 14549805 131 VAHFH 135
Cdd:cd01660 362 PGHFH 366
 
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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