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Conserved domains on  [gi|1955005209|gb|QQN96126|]
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cytochrome c oxidase subunit I, partial (mitochondrion) [Hemiandrus jacinda]

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 ...
 1-260 0e+00

Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and mitochondria which catalyze the reduction of O2 and simultaneously pump protons across the membrane. The superfamily is diverse in terms of electron donors, subunit composition, and heme types. The number of subunits varies from three to five in bacteria and up to 13 in mammalian mitochondria. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria. Membership in the superfamily is defined by subunit I, which contains a heme-copper binuclear center (the active site where O2 is reduced to water) formed by a high-spin heme and a copper ion. It also contains a low-spin heme, believed to participate in the transfer of electrons to the binuclear center. Only subunit I is common to the entire superfamily. For every reduction of an O2 molecule, eight protons are taken from the inside aqueous compartment and four electrons are taken from the electron donor on the opposite side of the membrane. The four electrons and four of the protons are used in the reduction of O2; the four remaining protons are pumped across the membrane. This charge separation of four charges contributes to the electrochemical gradient used for ATP synthesis. Two proton channels, the D-pathway and K-pathway, leading to the binuclear center have been identified in subunit I of cytochrome c oxidase (CcO) and ubiquinol oxidase. A well-defined pathway for the transfer of pumped protons beyond the binuclear center has not been identified. Electron transfer occurs in two segments: from the electron donor to the low-spin heme, and from the low-spin heme to the binuclear center. The first segment can be a multi-step process and varies among the different families, while the second segment, a direct transfer, is consistent throughout the superfamily.


The actual alignment was detected with superfamily member MTH00153:

Pssm-ID: 469701  Cd Length: 511  Bit Score: 542.15  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955005209   1 PEVYILILPGFGMISHIISQESGKKEAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKI 80
Cdd:MTH00153  239 PEVYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKI 318

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955005209  81 FSWLATLHGTQINYSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLF 160
Cdd:MTH00153  319 FSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLF 398

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955005209 161 TGLTLNPKWLKIQFSVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAFTSWNVVSSLGSTISFIGILILIFIIWESMITNR 240
Cdd:MTH00153  399 TGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKR 478

                         250       260
                  ....*....|....*....|
gi 1955005209 241 TVMFPLSMVSSLEWYQNLPP 260
Cdd:MTH00153  479 PVLFSLNLSSSIEWLQNLPP 498
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-260 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 542.15  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955005209   1 PEVYILILPGFGMISHIISQESGKKEAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKI 80
Cdd:MTH00153  239 PEVYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKI 318

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955005209  81 FSWLATLHGTQINYSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLF 160
Cdd:MTH00153  319 FSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLF 398

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955005209 161 TGLTLNPKWLKIQFSVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAFTSWNVVSSLGSTISFIGILILIFIIWESMITNR 240
Cdd:MTH00153  399 TGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKR 478

                         250       260
                  ....*....|....*....|
gi 1955005209 241 TVMFPLSMVSSLEWYQNLPP 260
Cdd:MTH00153  479 PVLFSLNLSSSIEWLQNLPP 498
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-254 1.01e-159

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: 452.32  E-value: 1.01e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955005209   1 PEVYILILPGFGMISHIISQESGKKEAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKI 80
Cdd:cd01663   232 PEVYILILPGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKV 311

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955005209  81 FSWLATLHGTQINYSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLF 160
Cdd:cd01663   312 FSWLATMWGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKI 391

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955005209 161 TGLTLNPKWLKIQFSVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAFTSWNVVSSLGSTISFIGILILIFIIWESMITNR 240
Cdd:cd01663   392 TGLSYNETLGKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGR 471

                         250
                  ....*....|....*
gi 1955005209 241 TVMF-PLSMVSSLEW 254
Cdd:cd01663   472 KVIFnVGEGSTSLEW 486
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-220 3.99e-95

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 288.95  E-value: 3.99e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955005209   1 PEVYILILPGFGMISHIISQESGKKeAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKI 80
Cdd:COG0843   243 PEVYILILPAFGIVSEIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKV 321

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955005209  81 FSWLATLHGTQINYSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLF 160
Cdd:COG0843   322 FNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKM 401

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1955005209 161 TGLTLNPKWLKIQFSVMFIGVNLTFFPQHFLGLAGMPRRYSDYP--DAFTSWNVVSSLGSTI 220
Cdd:COG0843   402 TGRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAFI 463
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-260 6.67e-93

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: 282.19  E-value: 6.67e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955005209   1 PEVYILILPGFGMISHIISQESGKKeAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKI 80
Cdd:TIGR02891 234 PEVYIIFLPAFGIISEILPTFARKP-IFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKV 312

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955005209  81 FSWLATLHGTQINYSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLF 160
Cdd:TIGR02891 313 FNWIATLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKV 392

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955005209 161 TGLTLNPKWLKIQFSVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDA--FTSWNVVSSLGSTISFIGILILIFIIWESMIT 238
Cdd:TIGR02891 393 TGRMYNERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNLISTIGAFILAAGFLVFLWNLIWSLRK 472

                         250       260
                  ....*....|....*....|..
gi 1955005209 239 NRTVMFPLSMVSSLEWYQNLPP 260
Cdd:TIGR02891 473 GPKAGANPWGATTLEWTTSSPP 494
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-220 6.04e-70

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: 221.29  E-value: 6.04e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955005209   1 PEVYILILPGFGMISHIISQESGKKeAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKI 80
Cdd:pfam00115 209 PEVYILILPAFGIIYYILPKFAGRP-LFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKV 287

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955005209  81 FSWLATLHGTQIN-YSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPL 159
Cdd:pfam00115 288 FNWLATLWGGWIRfRTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPK 367

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1955005209 160 FTGLTLNPKWLKIQFSVMFIGVNLTFFPQHFLGLAGMPRRYS----DYPDAFTSWNVVSSLGSTI 220
Cdd:pfam00115 368 LTGRMYSEKLGKLHFWLLFIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPLNWIRTIGGVL 432
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-260 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 542.15  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955005209   1 PEVYILILPGFGMISHIISQESGKKEAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKI 80
Cdd:MTH00153  239 PEVYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKI 318

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955005209  81 FSWLATLHGTQINYSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLF 160
Cdd:MTH00153  319 FSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLF 398

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955005209 161 TGLTLNPKWLKIQFSVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAFTSWNVVSSLGSTISFIGILILIFIIWESMITNR 240
Cdd:MTH00153  399 TGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKR 478

                         250       260
                  ....*....|....*....|
gi 1955005209 241 TVMFPLSMVSSLEWYQNLPP 260
Cdd:MTH00153  479 PVLFSLNLSSSIEWLQNLPP 498
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-254 1.01e-159

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: 452.32  E-value: 1.01e-159
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955005209   1 PEVYILILPGFGMISHIISQESGKKEAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKI 80
Cdd:cd01663   232 PEVYILILPGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKV 311

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955005209  81 FSWLATLHGTQINYSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLF 160
Cdd:cd01663   312 FSWLATMWGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKI 391

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955005209 161 TGLTLNPKWLKIQFSVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAFTSWNVVSSLGSTISFIGILILIFIIWESMITNR 240
Cdd:cd01663   392 TGLSYNETLGKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGR 471

                         250
                  ....*....|....*
gi 1955005209 241 TVMF-PLSMVSSLEW 254
Cdd:cd01663   472 KVIFnVGEGSTSLEW 486
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-260 1.86e-153

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 437.23  E-value: 1.86e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955005209   1 PEVYILILPGFGMISHIISQESGKKEAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKI 80
Cdd:MTH00142  239 PEVYILILPGFGMISHIINHYSGKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKV 318

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955005209  81 FSWLATLHGTQINYSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLF 160
Cdd:MTH00142  319 FSWLATLHGSKVKYEPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLF 398

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955005209 161 TGLTLNPKWLKIQFSVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAFTSWNVVSSLGSTISFIGILILIFIIWESMITNR 240
Cdd:MTH00142  399 TGLTLNPRWLKAHFYTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSSLGSMISFIAVLMFVFIVWESFVSQR 478

                         250       260
                  ....*....|....*....|
gi 1955005209 241 TVMFPLSMVSSLEWYQNLPP 260
Cdd:MTH00142  479 LVMWSSHLSTSLEWSHRLPP 498
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-260 1.03e-152

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 435.29  E-value: 1.03e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955005209   1 PEVYILILPGFGMISHIISQESGKKEAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKI 80
Cdd:MTH00116  241 PEVYILILPGFGIISHIVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKV 320

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955005209  81 FSWLATLHGTQINYSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLF 160
Cdd:MTH00116  321 FSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLF 400

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955005209 161 TGLTLNPKWLKIQFSVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAFTSWNVVSSLGSTISFIGILILIFIIWESMITNR 240
Cdd:MTH00116  401 TGYTLHQTWTKAQFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTISSIGSLISMTAVIMLMFIIWEAFSSKR 480

                         250       260
                  ....*....|....*....|
gi 1955005209 241 TVMFPLSMVSSLEWYQNLPP 260
Cdd:MTH00116  481 KVLQPELTTTNIEWIHGCPP 500
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-260 6.50e-151

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 430.64  E-value: 6.50e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955005209   1 PEVYILILPGFGMISHIISQESGKKEAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKI 80
Cdd:MTH00167  241 PEVYILILPGFGMISHIVVYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKV 320

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955005209  81 FSWLATLHGTQINYSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLF 160
Cdd:MTH00167  321 FSWLATLHGGKIKWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLF 400

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955005209 161 TGLTLNPKWLKIQFSVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAFTSWNVVSSLGSTISFIGILILIFIIWESMITNR 240
Cdd:MTH00167  401 TGLTLNETWTKIHFFVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNVVSSIGSLISLVAVILFLFIIWEAFSSKR 480

                         250       260
                  ....*....|....*....|
gi 1955005209 241 TVMFPLSMVSSLEWYQNLPP 260
Cdd:MTH00167  481 KLLPVELTSTNVEWLHGCPP 500
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-260 7.36e-151

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 430.55  E-value: 7.36e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955005209   1 PEVYILILPGFGMISHIISQESGKKEAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKI 80
Cdd:MTH00223  238 PEVYILILPGFGMISHIVSHYSSKKEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKV 317

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955005209  81 FSWLATLHGTQINYSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLF 160
Cdd:MTH00223  318 FSWLATIYGSKIKYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLF 397

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955005209 161 TGLTLNPKWLKIQFSVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAFTSWNVVSSLGSTISFIGILILIFIIWESMITNR 240
Cdd:MTH00223  398 TGVTLHRRWAKAHFFLMFLGVNLTFFPQHFLGLAGMPRRYSDYPDCYTKWNQVSSFGSMISFVSVLFFMFIVWEAFVSQR 477

                         250       260
                  ....*....|....*....|
gi 1955005209 241 TVMFPLSMVSSLEWYQNLPP 260
Cdd:MTH00223  478 SVVWSGHLSTSLEWDNLLPA 497
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-260 4.68e-133

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 385.39  E-value: 4.68e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955005209   1 PEVYILILPGFGMISHIISQESGKKEAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKI 80
Cdd:MTH00103  241 PEVYILILPGFGMISHIVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKV 320

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955005209  81 FSWLATLHGTQINYSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLF 160
Cdd:MTH00103  321 FSWLATLHGGNIKWSPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLF 400

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955005209 161 TGLTLNPKWLKIQFSVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAFTSWNVVSSLGSTISFIGILILIFIIWESMITNR 240
Cdd:MTH00103  401 SGYTLNDTWAKIHFTIMFVGVNMTFFPQHFLGLSGMPRRYSDYPDAYTTWNTVSSMGSFISLTAVMLMIFMIWEAFASKR 480

                         250       260
                  ....*....|....*....|
gi 1955005209 241 TVMFPLSMVSSLEWYQNLPP 260
Cdd:MTH00103  481 EVLTVELTTTNLEWLHGCPP 500
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-260 8.97e-133

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 384.95  E-value: 8.97e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955005209   1 PEVYILILPGFGMISHIISQESGKKEAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKI 80
Cdd:MTH00037  241 PEVYILILPGFGMISHVIAHYSGKQEPFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKV 320

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955005209  81 FSWLATLHGTQINYSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLF 160
Cdd:MTH00037  321 FSWMATLQGSNLRWETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLF 400

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955005209 161 TGLTLNPKWLKIQFSVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAFTSWNVVSSLGSTISFIGILILIFIIWESMITNR 240
Cdd:MTH00037  401 SGVSLHPLWSKVHFFLMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSTISLVATLFFLFLIWEAFASQR 480

                         250       260
                  ....*....|....*....|.
gi 1955005209 241 TVMFPLSMVSSLEW-YQNLPP 260
Cdd:MTH00037  481 EVISPEFSSSSLEWqYSSFPP 501
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-259 5.29e-130

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 377.71  E-value: 5.29e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955005209   1 PEVYILILPGFGMISHIISQESGKKEAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKI 80
Cdd:MTH00007  238 PEVYILILPGFGAISHIVTHYAGKLEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKV 317

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955005209  81 FSWLATLHGTQINYSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLF 160
Cdd:MTH00007  318 FSWLATIHGSPIKYETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLF 397

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955005209 161 TGLTLNPKWLKIQFSVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAFTSWNVVSSLGSTISFIGILILIFIIWESMITNR 240
Cdd:MTH00007  398 TGLTLHDRWAKAHFFLMFLGVNLTFFPQHFLGLSGMPRRYSDYPDAYTKWNVVSSFGSMLSFVALLLFIFILWEAFSAQR 477

                         250
                  ....*....|....*....
gi 1955005209 241 TVMFPLSMVSSLEWYQNLP 259
Cdd:MTH00007  478 GVIASPHMSSSLEWQDTLP 496
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-260 6.03e-130

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 377.73  E-value: 6.03e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955005209   1 PEVYILILPGFGMISHIISQESGKKEAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKI 80
Cdd:MTH00183  241 PEVYILILPGFGMISHIVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKV 320

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955005209  81 FSWLATLHGTQINYSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLF 160
Cdd:MTH00183  321 FSWLATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLF 400

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955005209 161 TGLTLNPKWLKIQFSVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAFTSWNVVSSLGSTISFIGILILIFIIWESMITNR 240
Cdd:MTH00183  401 SGYTLHSTWTKIHFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMFLFILWEAFAAKR 480

                         250       260
                  ....*....|....*....|
gi 1955005209 241 TVMFPLSMVSSLEWYQNLPP 260
Cdd:MTH00183  481 EVLSVELTSTNVEWLHGCPP 500
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-260 4.03e-128

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 372.74  E-value: 4.03e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955005209   1 PEVYILILPGFGMISHIISQESGKKEAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKI 80
Cdd:MTH00077  241 PEVYILILPGFGMISHIVTYYSAKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKV 320

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955005209  81 FSWLATLHGTQINYSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLF 160
Cdd:MTH00077  321 FSWLATMHGGAIKWDAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLF 400

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955005209 161 TGLTLNPKWLKIQFSVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAFTSWNVVSSLGSTISFIGILILIFIIWESMITNR 240
Cdd:MTH00077  401 SGYTLHSTWSKIHFGVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMMMFIIWEAFSSKR 480

                         250       260
                  ....*....|....*....|
gi 1955005209 241 TVMFPLSMVSSLEWYQNLPP 260
Cdd:MTH00077  481 EVLTTELTSTNIEWLHGCPP 500
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-260 7.47e-117

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 343.97  E-value: 7.47e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955005209   1 PEVYILILPGFGMISHIISQESGKKEAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKI 80
Cdd:MTH00079  241 PEVYILILPAFGIISQSTLYLTGKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKV 320

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955005209  81 FSWLATLHGTQINYSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLF 160
Cdd:MTH00079  321 FSWLATLFGMKMKFQPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFM 400

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955005209 161 TGLTLNPKWLKIQFSVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAFTSWNVVSSLGSTISFIGILILIFIIWESMITNR 240
Cdd:MTH00079  401 TGIVYDKLMMSAVFFLMFVGVNLTFFPLHFAGLHGMPRKYLDYPDVYSVWNVISSYGSMISVFALFLFIYVLLESFFSYR 480

                         250       260
                  ....*....|....*....|
gi 1955005209 241 TVMFPLSMVSSLEWYQNLPP 260
Cdd:MTH00079  481 LVLHDNYINSSPEYSLSSYV 500
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-260 8.58e-113

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 334.10  E-value: 8.58e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955005209   1 PEVYILILPGFGMISHIISQESGKKEAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKI 80
Cdd:MTH00182  243 PEVYILILPGFGMISQIIPTFVAKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKV 322

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955005209  81 FSWLATLHGTQINYSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLF 160
Cdd:MTH00182  323 FSWLATIYGGTLRLDTPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKI 402

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955005209 161 TGLTLNPKWLKIQFSVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAFTSWNVVSSLGSTISFIGILILIFIIWESMITNR 240
Cdd:MTH00182  403 TGYCYNELYGKIHFWLMFIGVNLTFFPQHFLGLAGFPRRYSDFADAFAGWNLVSSLGSIISIVGVVWFIYIIYDAYVREE 482

                         250       260
                  ....*....|....*....|....
gi 1955005209 241 T----VMFPLSMVSSLEWYQNLPP 260
Cdd:MTH00182  483 KfigwKEGTGESWASLEWVHSSPP 506
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-260 5.60e-108

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 321.78  E-value: 5.60e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955005209   1 PEVYILILPGFGMISHIISQESGKKEAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKI 80
Cdd:MTH00184  243 PEVYILILPGFGIISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKI 322

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955005209  81 FSWLATLHGTQINYSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLF 160
Cdd:MTH00184  323 FSWIATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKI 402

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955005209 161 TGLTLNPKWLKIQFSVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAFTSWNVVSSLGSTISFIGILILIFIIWESM---I 237
Cdd:MTH00184  403 TGYCYNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDSFAGWNQISSLGSVISIVGVVWFIYIVYDAYvreI 482

                         250       260
                  ....*....|....*....|...
gi 1955005209 238 TNRTVMFPLSMVSSLEWYQNLPP 260
Cdd:MTH00184  483 KFVGWVEDSGHYPSLEWAQTSPP 505
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-236 5.22e-104

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: 309.46  E-value: 5.22e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955005209   1 PEVYILILPGFGMISHIISQESGKKeAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKI 80
Cdd:cd00919   229 PEVYILILPAFGAISEIIPTFSGKP-LFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKV 307

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955005209  81 FSWLATLHGTQINYSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLF 160
Cdd:cd00919   308 FNWLATLWGGRIRFDPPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKM 387

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1955005209 161 TGLTLNPKWLKIQFSVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAFTSWNVVSSLGSTISFIGILILIFIIWESM 236
Cdd:cd00919   388 TGRMLSEKLGKIHFWLWFIGFNLTFFPMHFLGLLGMPRRYADYPDGFAPWNFISSVGAFILGLGLLLFLGNLFLSL 463
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-220 3.99e-95

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 288.95  E-value: 3.99e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955005209   1 PEVYILILPGFGMISHIISQESGKKeAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKI 80
Cdd:COG0843   243 PEVYILILPAFGIVSEIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKV 321

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955005209  81 FSWLATLHGTQINYSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLF 160
Cdd:COG0843   322 FNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKM 401

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1955005209 161 TGLTLNPKWLKIQFSVMFIGVNLTFFPQHFLGLAGMPRRYSDYP--DAFTSWNVVSSLGSTI 220
Cdd:COG0843   402 TGRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAFI 463
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-260 6.67e-93

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: 282.19  E-value: 6.67e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955005209   1 PEVYILILPGFGMISHIISQESGKKeAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKI 80
Cdd:TIGR02891 234 PEVYIIFLPAFGIISEILPTFARKP-IFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKV 312

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955005209  81 FSWLATLHGTQINYSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLF 160
Cdd:TIGR02891 313 FNWIATLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKV 392

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955005209 161 TGLTLNPKWLKIQFSVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDA--FTSWNVVSSLGSTISFIGILILIFIIWESMIT 238
Cdd:TIGR02891 393 TGRMYNERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNLISTIGAFILAAGFLVFLWNLIWSLRK 472

                         250       260
                  ....*....|....*....|..
gi 1955005209 239 NRTVMFPLSMVSSLEWYQNLPP 260
Cdd:TIGR02891 473 GPKAGANPWGATTLEWTTSSPP 494
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-221 1.02e-90

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 278.05  E-value: 1.02e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955005209   1 PEVYILILPGFGMISHIISQESGKKEAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKI 80
Cdd:MTH00026  242 PEVYILILPGFGIISQILSLFSYKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKI 321

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955005209  81 FSWLATLHGTQIN--YSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYP 158
Cdd:MTH00026  322 FSWLATVSGSGRNliFTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWFG 401

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1955005209 159 LFTGLTLNPKWLKIQFSVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAFTSWNVVSSLGSTIS 221
Cdd:MTH00026  402 KITGYAYKDIYGLIHFWLMFIGVNITFFPQHFLGLAGLPRRYADYPDNFEDFNQISSFGSIIS 464
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 1-220 4.09e-87

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: 267.52  E-value: 4.09e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955005209   1 PEVYILILPGFGMISHIISQESGKKeAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKI 80
Cdd:cd01662   235 PEVYILILPAFGIFSEIVPTFSRKP-LFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKI 313

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955005209  81 FSWLATLHGTQINYSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLF 160
Cdd:cd01662   314 FNWLFTMWRGRIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKM 393

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1955005209 161 TGLTLNPKWLKIQFSVMFIGVNLTFFPQHFLGLAGMPRRYSDYP--DAFTSWNVVSSLGSTI 220
Cdd:cd01662   394 FGRMLNERLGKWSFWLWFIGFNLTFFPMHILGLMGMPRRVYTYLpgPGWDPLNLISTIGAFL 455
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 1-243 5.21e-87

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 267.70  E-value: 5.21e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955005209   1 PEVYILILPGFGMISHIISQESGKKEAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKI 80
Cdd:MTH00048  239 PEVYVLILPGFGIISHICLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKV 318

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955005209  81 FSWLATLHGTQINYS-PALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPL 159
Cdd:MTH00048  319 FSWLYMLLNSRVRKSdPVVWWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWPL 398

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955005209 160 FTGLTLNPKWLKIQFSVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAFTSWNVVSSLGSTISFIGILILIFIIWESMITN 239
Cdd:MTH00048  399 ITGLSLNKYLLQCHCIISMIGFNLCFFPMHYFGLCGLPRRVCVYEPSYYWINVVCTVGSFISAFSGCFFVFILWESLVVK 478


                  ....
gi 1955005209 240 RTVM 243
Cdd:MTH00048  479 NEVL 482
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-220 6.04e-70

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: 221.29  E-value: 6.04e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955005209   1 PEVYILILPGFGMISHIISQESGKKeAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKI 80
Cdd:pfam00115 209 PEVYILILPAFGIIYYILPKFAGRP-LFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKV 287

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955005209  81 FSWLATLHGTQIN-YSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPL 159
Cdd:pfam00115 288 FNWLATLWGGWIRfRTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPK 367

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1955005209 160 FTGLTLNPKWLKIQFSVMFIGVNLTFFPQHFLGLAGMPRRYS----DYPDAFTSWNVVSSLGSTI 220
Cdd:pfam00115 368 LTGRMYSEKLGKLHFWLLFIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPLNWIRTIGGVL 432
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 1-220 8.66e-57

cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type quinone oxidase, one of several bacterial terminal oxidases. This complex couples oxidation of reduced quinones with the reduction of molecular oxygen to water and the pumping of protons to form a proton gradient utilized for ATP production. aa3-type oxidases contain two heme a cofactors as well as copper atoms in the active site. [Energy metabolism, Electron transport]


Pssm-ID: 131928  Cd Length: 643  Bit Score: 191.61  E-value: 8.66e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955005209   1 PEVYILILPGFGMISHIISQESgKKEAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKI 80
Cdd:TIGR02882 278 PEVYIVILPAFGIYSEIISTFA-QKRLFGYKSMVWSTVGIAFLSFLVWVHHFFTMGNGALINSFFSITTMAIAIPTGVKI 356

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955005209  81 FSWLATLHGTQINYSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLF 160
Cdd:TIGR02882 357 FNWLLTLYKGKIRFTTPMLFSLAFIPNFLIGGVTGVMLAMASADYQYHNTYFLVAHFHYVLITGVVFACLAGLIYWYPKM 436

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1955005209 161 TGLTLNPKWLKIQFSVMFIGVNLTFFPQHFLGLAGMPRRYSDY--PDAFTSWNVVSSLGSTI 220
Cdd:TIGR02882 437 FGYKLNERLGKWCFWFFMIGFNVCFFPMYILGLDGMPRRMYTYspSDGWFPLNLISTIGALL 498
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 1-220 3.86e-52

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 179.75  E-value: 3.86e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955005209   1 PEVYILILPGFGMISHIISQESgKKEAFGTLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKI 80
Cdd:PRK15017  285 PEVYILILPVFGVFSEIAATFS-RKRLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVKI 363

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955005209  81 FSWLATLHGTQINYSPALLWALGFVFLFTIGGLTGVVLANSSLDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIQWYPLF 160
Cdd:PRK15017  364 FNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYWWPKA 443

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1955005209 161 TGLTLNPKWLKIQFSVMFIGVNLTFFPQHFLGLAGMPRRYSDYPD-AFTSWNVVSSLGSTI 220
Cdd:PRK15017  444 FGFKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMTRRLSQQIDpQFHTMLMIAASGAAL 504
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
 1-220 1.90e-11

ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and some archaea which catalyze the reduction of O2 and simultaneously pump protons across the membrane. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria. The ba3 family contains oxidases that lack the conserved residues that form the D- and K-pathways in CcO and ubiquinol oxidase. Instead they contain a potential alternative K-pathway. Additional proton channels have been proposed for this family of oxidases but none have been identified definitively. For general information on the heme-copper oxidase superfamily, please see cd00919.


Pssm-ID: 238830  Cd Length: 473  Bit Score: 63.46  E-value: 1.90e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955005209   1 PEVYILILPGFGMISHIISQESGKKEAFGTLGMIyAMLAIGLLGFVVWAHHMFT-VGMDVDTRAYFTSATMIIAVPTGIK 79
Cdd:cd01660   214 PLVYFWLLPAYIAWYTILPKIAGGKLFSDPLARL-AFILFLLFSTPVGFHHQFAdPGIGPGWKFIHMVLTFMVALPSLLT 292

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955005209  80 IFSWLATL-HGTQINYSPALLW---------------ALGFVFlFTIGGLTGVVLANSSLDIILHDTYYVVAHFHyvLSM 143
Cdd:cd01660   293 AFTVFASLeIAGRLRGGKGLFGwiralpwgdpmflalFLAMLM-FIPGGAGGIINASYQLNYVVHNTAWVPGHFH--LTV 369

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1955005209 144 GAVFAIMAGFIQWY--PLFTGLTLNPKWL-KIQFSVMFIGVNLTFFPQHFLGLAGMPRR-------YSDYPDAFTSWNVV 213
Cdd:cd01660   370 GGAVALTFMAVAYWlvPHLTGRELAAKRLaLAQPWLWFVGMTIMSTAMHVAGLLGAPRRtaeaqygGLPAAGEWAPYQQL 449


                  ....*..
gi 1955005209 214 SSLGSTI 220
Cdd:cd01660   450 MAIGGTI 456
 
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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