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Conserved domains on  [gi|58272111|gb|AAW69705|]
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cytochrome oxidase subunit I, partial (mitochondrion) [Gymnopternus angustifrons]

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 ...
 1-268 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: 558.33  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58272111    1 LILPGFGMISHIISQECGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLA 80
Cdd:MTH00153 244 LILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLA 323

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58272111   81 TLHGSQLSYSPALMWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYSLFTGLTL 160
Cdd:MTH00153 324 TLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTM 403

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58272111  161 NSTWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTAWNVVSTIGSTISLLGILFFLFIIWESMITQRQVIFP 240
Cdd:MTH00153 404 NPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPVLFS 483

                        250       260
                 ....*....|....*....|....*...
gi 58272111  241 IQLNSSIEWYQNIPPAEHSYSELPLLTN 268
Cdd:MTH00153 484 LNLSSSIEWLQNLPPAEHSYSELPLLTN 511
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-268 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 558.33  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58272111    1 LILPGFGMISHIISQECGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLA 80
Cdd:MTH00153 244 LILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLA 323

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58272111   81 TLHGSQLSYSPALMWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYSLFTGLTL 160
Cdd:MTH00153 324 TLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTM 403

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58272111  161 NSTWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTAWNVVSTIGSTISLLGILFFLFIIWESMITQRQVIFP 240
Cdd:MTH00153 404 NPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPVLFS 483

                        250       260
                 ....*....|....*....|....*...
gi 58272111  241 IQLNSSIEWYQNIPPAEHSYSELPLLTN 268
Cdd:MTH00153 484 LNLSSSIEWLQNLPPAEHSYSELPLLTN 511
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-249 8.29e-160

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: 452.71  E-value: 8.29e-160
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58272111   1 LILPGFGMISHIISQECGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLA 80
Cdd:cd01663 237 LILPGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLA 316

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58272111  81 TLHGSQLSYSPALMWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYSLFTGLTL 160
Cdd:cd01663 317 TMWGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSY 396

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58272111 161 NSTWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTAWNVVSTIGSTISLLGILFFLFIIWESMITQRQVIFP 240
Cdd:cd01663 397 NETLGKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFN 476

                       250
                ....*....|
gi 58272111 241 I-QLNSSIEW 249
Cdd:cd01663 477 VgEGSTSLEW 486
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-267 1.96e-95

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 290.11  E-value: 1.96e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58272111   1 LILPGFGMISHIISQECGKKeTFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLA 80
Cdd:COG0843 248 LILPAFGIVSEIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIA 326

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58272111  81 TLHGSQLSYSPALMWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYSLFTGLTL 160
Cdd:COG0843 327 TMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRML 406

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58272111 161 NSTWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYP--DAYTAWNVVSTIGSTISLLGILFFLFIIWESMITQRQV- 237
Cdd:COG0843 407 NERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAFILAVGFLLFLINLVVSLRKGPKAg 486

                       250       260       270
                ....*....|....*....|....*....|
gi 58272111 238 IFPIQLNsSIEWYQNIPPAEHSYSELPLLT 267
Cdd:COG0843 487 GNPWGAR-TLEWATPSPPPLYNFASIPVVR 515
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-260 1.74e-91

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: 279.11  E-value: 1.74e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58272111     1 LILPGFGMISHIISQECGKKeTFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLA 80
Cdd:TIGR02891 239 IFLPAFGIISEILPTFARKP-IFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIA 317

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58272111    81 TLHGSQLSYSPALMWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYSLFTGLTL 160
Cdd:TIGR02891 318 TLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMY 397

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58272111   161 NSTWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDA--YTAWNVVSTIGSTISLLGILFFLFIIWESMITQRQVI 238
Cdd:TIGR02891 398 NERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGPKAG 477

                         250       260
                  ....*....|....*....|..
gi 58272111   239 FPIQLNSSIEWYQNIPPAEHSY 260
Cdd:TIGR02891 478 ANPWGATTLEWTTSSPPPAHNF 499
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-215 5.12e-65

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: 208.97  E-value: 5.12e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58272111     1 LILPGFGMISHIISQECGKKeTFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLA 80
Cdd:pfam00115 214 LILPAFGIIYYILPKFAGRP-LFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLA 292

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58272111    81 TLHGSQLS-YSPALMWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYSLFTGLT 159
Cdd:pfam00115 293 TLWGGWIRfRTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRM 372

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 58272111   160 LNSTWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYS----DYPDAYTAWNVVSTIGSTI 215
Cdd:pfam00115 373 YSEKLGKLHFWLLFIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPLNWIRTIGGVL 432
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-268 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 558.33  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58272111    1 LILPGFGMISHIISQECGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLA 80
Cdd:MTH00153 244 LILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLA 323

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58272111   81 TLHGSQLSYSPALMWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYSLFTGLTL 160
Cdd:MTH00153 324 TLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLTM 403

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58272111  161 NSTWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTAWNVVSTIGSTISLLGILFFLFIIWESMITQRQVIFP 240
Cdd:MTH00153 404 NPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPVLFS 483

                        250       260
                 ....*....|....*....|....*...
gi 58272111  241 IQLNSSIEWYQNIPPAEHSYSELPLLTN 268
Cdd:MTH00153 484 LNLSSSIEWLQNLPPAEHSYSELPLLTN 511
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-249 8.29e-160

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: 452.71  E-value: 8.29e-160
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58272111   1 LILPGFGMISHIISQECGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLA 80
Cdd:cd01663 237 LILPGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLA 316

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58272111  81 TLHGSQLSYSPALMWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYSLFTGLTL 160
Cdd:cd01663 317 TMWGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSY 396

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58272111 161 NSTWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTAWNVVSTIGSTISLLGILFFLFIIWESMITQRQVIFP 240
Cdd:cd01663 397 NETLGKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFN 476

                       250
                ....*....|
gi 58272111 241 I-QLNSSIEW 249
Cdd:cd01663 477 VgEGSTSLEW 486
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-268 2.75e-156

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 444.94  E-value: 2.75e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58272111    1 LILPGFGMISHIISQECGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLA 80
Cdd:MTH00142 244 LILPGFGMISHIINHYSGKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFSWLA 323

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58272111   81 TLHGSQLSYSPALMWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYSLFTGLTL 160
Cdd:MTH00142 324 TLHGSKVKYEPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLFTGLTL 403

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58272111  161 NSTWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTAWNVVSTIGSTISLLGILFFLFIIWESMITQRQVIFP 240
Cdd:MTH00142 404 NPRWLKAHFYTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSSLGSMISFIAVLMFVFIVWESFVSQRLVMWS 483

                        250       260
                 ....*....|....*....|....*...
gi 58272111  241 IQLNSSIEWYQNIPPAEHSYSELPLLTN 268
Cdd:MTH00142 484 SHLSTSLEWSHRLPPDFHTYDELPILVV 511
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 1-264 8.97e-156

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 443.65  E-value: 8.97e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58272111    1 LILPGFGMISHIISQECGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLA 80
Cdd:MTH00223 243 LILPGFGMISHIVSHYSSKKEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLA 322

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58272111   81 TLHGSQLSYSPALMWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYSLFTGLTL 160
Cdd:MTH00223 323 TIYGSKIKYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLFTGVTL 402

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58272111  161 NSTWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTAWNVVSTIGSTISLLGILFFLFIIWESMITQRQVIFP 240
Cdd:MTH00223 403 HRRWAKAHFFLMFLGVNLTFFPQHFLGLAGMPRRYSDYPDCYTKWNQVSSFGSMISFVSVLFFMFIVWEAFVSQRSVVWS 482

                        250       260
                 ....*....|....*....|....
gi 58272111  241 IQLNSSIEWYQNIPPAEHSYSELP 264
Cdd:MTH00223 483 GHLSTSLEWDNLLPADFHNNSETG 506
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-266 2.66e-155

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 442.19  E-value: 2.66e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58272111    1 LILPGFGMISHIISQECGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLA 80
Cdd:MTH00167 246 LILPGFGMISHIVVYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSWLA 325

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58272111   81 TLHGSQLSYSPALMWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYSLFTGLTL 160
Cdd:MTH00167 326 TLHGGKIKWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGLTL 405

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58272111  161 NSTWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTAWNVVSTIGSTISLLGILFFLFIIWESMITQRQVIFP 240
Cdd:MTH00167 406 NETWTKIHFFVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNVVSSIGSLISLVAVILFLFIIWEAFSSKRKLLPV 485

                        250       260
                 ....*....|....*....|....*.
gi 58272111  241 IQLNSSIEWYQNIPPAEHSYSELPLL 266
Cdd:MTH00167 486 ELTSTNVEWLHGCPPPHHTWEEPPFV 511
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-268 1.58e-153

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 437.99  E-value: 1.58e-153
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58272111    1 LILPGFGMISHIISQECGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLA 80
Cdd:MTH00116 246 LILPGFGIISHIVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSWLA 325

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58272111   81 TLHGSQLSYSPALMWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYSLFTGLTL 160
Cdd:MTH00116 326 TLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGYTL 405

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58272111  161 NSTWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTAWNVVSTIGSTISLLGILFFLFIIWESMITQRQVIFP 240
Cdd:MTH00116 406 HQTWTKAQFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTISSIGSLISMTAVIMLMFIIWEAFSSKRKVLQP 485

                        250       260
                 ....*....|....*....|....*...
gi 58272111  241 IQLNSSIEWYQNIPPAEHSYSELPLLTN 268
Cdd:MTH00116 486 ELTTTNIEWIHGCPPPYHTFEEPAFVQV 513
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-265 7.05e-138

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 398.05  E-value: 7.05e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58272111    1 LILPGFGMISHIISQECGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLA 80
Cdd:MTH00037 246 LILPGFGMISHVIAHYSGKQEPFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWMA 325

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58272111   81 TLHGSQLSYSPALMWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYSLFTGLTL 160
Cdd:MTH00037 326 TLQGSNLRWETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLFSGVSL 405

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58272111  161 NSTWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTAWNVVSTIGSTISLLGILFFLFIIWESMITQRQVIFP 240
Cdd:MTH00037 406 HPLWSKVHFFLMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSTISLVATLFFLFLIWEAFASQREVISP 485

                        250       260
                 ....*....|....*....|....*.
gi 58272111  241 IQLNSSIEW-YQNIPPAEHSYSELPL 265
Cdd:MTH00037 486 EFSSSSLEWqYSSFPPSHHTFDETPS 511
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-262 8.22e-136

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 392.71  E-value: 8.22e-136
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58272111    1 LILPGFGMISHIISQECGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLA 80
Cdd:MTH00103 246 LILPGFGMISHIVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLA 325

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58272111   81 TLHGSQLSYSPALMWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYSLFTGLTL 160
Cdd:MTH00103 326 TLHGGNIKWSPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTL 405

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58272111  161 NSTWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTAWNVVSTIGSTISLLGILFFLFIIWESMITQRQVIFP 240
Cdd:MTH00103 406 NDTWAKIHFTIMFVGVNMTFFPQHFLGLSGMPRRYSDYPDAYTTWNTVSSMGSFISLTAVMLMIFMIWEAFASKREVLTV 485

                        250       260
                 ....*....|....*....|..
gi 58272111  241 IQLNSSIEWYQNIPPAEHSYSE 262
Cdd:MTH00103 486 ELTTTNLEWLHGCPPPYHTFEE 507
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-262 6.69e-134

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 388.13  E-value: 6.69e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58272111    1 LILPGFGMISHIISQECGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLA 80
Cdd:MTH00183 246 LILPGFGMISHIVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWLA 325

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58272111   81 TLHGSQLSYSPALMWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYSLFTGLTL 160
Cdd:MTH00183 326 TLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLFSGYTL 405

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58272111  161 NSTWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTAWNVVSTIGSTISLLGILFFLFIIWESMITQRQVIFP 240
Cdd:MTH00183 406 HSTWTKIHFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMFLFILWEAFAAKREVLSV 485

                        250       260
                 ....*....|....*....|..
gi 58272111  241 IQLNSSIEWYQNIPPAEHSYSE 262
Cdd:MTH00183 486 ELTSTNVEWLHGCPPPYHTFEE 507
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-267 5.80e-132

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 383.10  E-value: 5.80e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58272111    1 LILPGFGMISHIISQECGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLA 80
Cdd:MTH00007 243 LILPGFGAISHIVTHYAGKLEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLA 322

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58272111   81 TLHGSQLSYSPALMWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYSLFTGLTL 160
Cdd:MTH00007 323 TIHGSPIKYETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTGLTL 402

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58272111  161 NSTWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTAWNVVSTIGSTISLLGILFFLFIIWESMITQRQVIFP 240
Cdd:MTH00007 403 HDRWAKAHFFLMFLGVNLTFFPQHFLGLSGMPRRYSDYPDAYTKWNVVSSFGSMLSFVALLLFIFILWEAFSAQRGVIAS 482

                        250       260
                 ....*....|....*....|....*..
gi 58272111  241 IQLNSSIEWYQNIPPAEHSYSELPLLT 267
Cdd:MTH00007 483 PHMSSSLEWQDTLPLDFHNLPETGIIT 509
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-268 1.39e-130

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 379.67  E-value: 1.39e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58272111    1 LILPGFGMISHIISQECGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLA 80
Cdd:MTH00077 246 LILPGFGMISHIVTYYSAKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVFSWLA 325

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58272111   81 TLHGSQLSYSPALMWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYSLFTGLTL 160
Cdd:MTH00077 326 TMHGGAIKWDAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTL 405

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58272111  161 NSTWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTAWNVVSTIGSTISLLGILFFLFIIWESMITQRQVIFP 240
Cdd:MTH00077 406 HSTWSKIHFGVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMMMFIIWEAFSSKREVLTT 485

                        250       260
                 ....*....|....*....|....*...
gi 58272111  241 IQLNSSIEWYQNIPPAEHSYSELPLLTN 268
Cdd:MTH00077 486 ELTSTNIEWLHGCPPPYHTFEEPSFVQT 513
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-266 2.16e-117

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 346.42  E-value: 2.16e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58272111    1 LILPGFGMISHIISQECGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLA 80
Cdd:MTH00182 248 LILPGFGMISQIIPTFVAKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLA 327

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58272111   81 TLHGSQLSYSPALMWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYSLFTGLTL 160
Cdd:MTH00182 328 TIYGGTLRLDTPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCY 407

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58272111  161 NSTWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTAWNVVSTIGSTISLLGILFFLFIIWESMITQRQVIFP 240
Cdd:MTH00182 408 NELYGKIHFWLMFIGVNLTFFPQHFLGLAGFPRRYSDFADAFAGWNLVSSLGSIISIVGVVWFIYIIYDAYVREEKFIGW 487

                        250       260       270
                 ....*....|....*....|....*....|
gi 58272111  241 IQLN----SSIEWYQNIPPAEHSYSELPLL 266
Cdd:MTH00182 488 KEGTgeswASLEWVHSSPPLFHTYNELPFV 517
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-262 7.70e-116

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 341.66  E-value: 7.70e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58272111    1 LILPGFGMISHIISQECGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLA 80
Cdd:MTH00079 246 LILPAFGIISQSTLYLTGKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSWLA 325

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58272111   81 TLHGSQLSYSPALMWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYSLFTGLTL 160
Cdd:MTH00079 326 TLFGMKMKFQPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFMTGIVY 405

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58272111  161 NSTWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTAWNVVSTIGSTISLLGILFFLFIIWESMITQRQVIFP 240
Cdd:MTH00079 406 DKLMMSAVFFLMFVGVNLTFFPLHFAGLHGMPRKYLDYPDVYSVWNVISSYGSMISVFALFLFIYVLLESFFSYRLVLHD 485

                        250       260
                 ....*....|....*....|..
gi 58272111  241 IQLNSSIEWYQNIPPAEHSYSE 262
Cdd:MTH00079 486 NYINSSPEYSLSSYVFGHSYQS 507
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-266 7.61e-112

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 331.79  E-value: 7.61e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58272111    1 LILPGFGMISHIISQECGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLA 80
Cdd:MTH00184 248 LILPGFGIISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIA 327

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58272111   81 TLHGSQLSYSPALMWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYSLFTGLTL 160
Cdd:MTH00184 328 TIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYCY 407

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58272111  161 NSTWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTAWNVVSTIGSTISLLGILFFLFIIWESMITQRQVIFP 240
Cdd:MTH00184 408 NEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDSFAGWNQISSLGSVISIVGVVWFIYIVYDAYVREIKFVGW 487

                        250       260
                 ....*....|....*....|....*....
gi 58272111  241 IQ---LNSSIEWYQNIPPAEHSYSELPLL 266
Cdd:MTH00184 488 VEdsgHYPSLEWAQTSPPAHHTYNELPYV 516
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-231 2.69e-103

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: 308.31  E-value: 2.69e-103
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58272111   1 LILPGFGMISHIISQECGKKeTFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLA 80
Cdd:cd00919 234 LILPAFGAISEIIPTFSGKP-LFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLA 312

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58272111  81 TLHGSQLSYSPALMWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYSLFTGLTL 160
Cdd:cd00919 313 TLWGGRIRFDPPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRML 392

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 58272111 161 NSTWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTAWNVVSTIGSTISLLGILFFLFIIWESM 231
Cdd:cd00919 393 SEKLGKIHFWLWFIGFNLTFFPMHFLGLLGMPRRYADYPDGFAPWNFISSVGAFILGLGLLLFLGNLFLSL 463
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-267 1.96e-95

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 290.11  E-value: 1.96e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58272111   1 LILPGFGMISHIISQECGKKeTFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLA 80
Cdd:COG0843 248 LILPAFGIVSEIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNWIA 326

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58272111  81 TLHGSQLSYSPALMWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYSLFTGLTL 160
Cdd:COG0843 327 TMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGRML 406

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58272111 161 NSTWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYP--DAYTAWNVVSTIGSTISLLGILFFLFIIWESMITQRQV- 237
Cdd:COG0843 407 NERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAFILAVGFLLFLINLVVSLRKGPKAg 486

                       250       260       270
                ....*....|....*....|....*....|
gi 58272111 238 IFPIQLNsSIEWYQNIPPAEHSYSELPLLT 267
Cdd:COG0843 487 GNPWGAR-TLEWATPSPPPLYNFASIPVVR 515
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-266 1.03e-91

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 280.75  E-value: 1.03e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58272111    1 LILPGFGMISHIISQECGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLA 80
Cdd:MTH00026 247 LILPGFGIISQILSLFSYKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSWLA 326

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58272111   81 TLHGS--QLSYSPALMWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYSLFTGL 158
Cdd:MTH00026 327 TVSGSgrNLIFTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWFGKITGY 406

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58272111  159 TLNSTWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTAWNVVSTIGSTISLLGILFFLFIIWESM------- 231
Cdd:MTH00026 407 AYKDIYGLIHFWLMFIGVNITFFPQHFLGLAGLPRRYADYPDNFEDFNQISSFGSIISIIAVIWFIVVIFDAYyreepfd 486

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 58272111  232 --ITQRQVIFPIQLN----SSIEWYQNIPPAEHSYSELPLL 266
Cdd:MTH00026 487 inIMAKGPLIPFSCQpahfDTLEWSLTSPPEHHTYNELPYI 527
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-260 1.74e-91

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: 279.11  E-value: 1.74e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58272111     1 LILPGFGMISHIISQECGKKeTFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLA 80
Cdd:TIGR02891 239 IFLPAFGIISEILPTFARKP-IFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIA 317

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58272111    81 TLHGSQLSYSPALMWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYSLFTGLTL 160
Cdd:TIGR02891 318 TLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMY 397

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58272111   161 NSTWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDA--YTAWNVVSTIGSTISLLGILFFLFIIWESMITQRQVI 238
Cdd:TIGR02891 398 NERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGPKAG 477

                         250       260
                  ....*....|....*....|..
gi 58272111   239 FPIQLNSSIEWYQNIPPAEHSY 260
Cdd:TIGR02891 478 ANPWGATTLEWTTSSPPPAHNF 499
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 1-238 7.10e-86

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 265.00  E-value: 7.10e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58272111    1 LILPGFGMISHIISQECGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLA 80
Cdd:MTH00048 244 LILPGFGIISHICLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFSWLY 323

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58272111   81 TLHGSQLSYS-PALMWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYSLFTGLT 159
Cdd:MTH00048 324 MLLNSRVRKSdPVVWWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWPLITGLS 403

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 58272111  160 LNSTWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTAWNVVSTIGSTISLLGILFFLFIIWESMITQRQVI 238
Cdd:MTH00048 404 LNKYLLQCHCIISMIGFNLCFFPMHYFGLCGLPRRVCVYEPSYYWINVVCTVGSFISAFSGCFFVFILWESLVVKNEVL 482
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 1-231 2.51e-83

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: 258.28  E-value: 2.51e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58272111   1 LILPGFGMISHIISQECGKKeTFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLA 80
Cdd:cd01662 240 LILPAFGIFSEIVPTFSRKP-LFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLF 318

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58272111  81 TLHGSQLSYSPALMWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYSLFTGLTL 160
Cdd:cd01662 319 TMWRGRIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRML 398

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 58272111 161 NSTWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYP--DAYTAWNVVSTIGSTISLLGILFFLFIIWESM 231
Cdd:cd01662 399 NERLGKWSFWLWFIGFNLTFFPMHILGLMGMPRRVYTYLpgPGWDPLNLISTIGAFLIAAGVLLFLINVIVSI 471
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 1-215 5.12e-65

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: 208.97  E-value: 5.12e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58272111     1 LILPGFGMISHIISQECGKKeTFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLA 80
Cdd:pfam00115 214 LILPAFGIIYYILPKFAGRP-LFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLA 292

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58272111    81 TLHGSQLS-YSPALMWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYSLFTGLT 159
Cdd:pfam00115 293 TLWGGWIRfRTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRM 372

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 58272111   160 LNSTWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYS----DYPDAYTAWNVVSTIGSTI 215
Cdd:pfam00115 373 YSEKLGKLHFWLLFIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPLNWIRTIGGVL 432
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 1-264 1.47e-50

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 175.51  E-value: 1.47e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58272111    1 LILPGFGMISHIISQeCGKKETFGSLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLA 80
Cdd:PRK15017 290 LILPVFGVFSEIAAT-FSRKRLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVKIFNWLF 368

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58272111   81 TLHGSQLSYSPALMWALGFVFLFTVGGLTGVVLANSSVDIILHDTYYVVAHFHYVLSMGAVFAIMAGFIHWYSLFTGLTL 160
Cdd:PRK15017 369 TMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYWWPKAFGFKL 448

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58272111  161 NSTWLKSQFIIMFIGVNLTFFPQHFLGLAGMPRRYSDYPD-AYTAWNVVSTIGSTISLLGILFFLFIIWESMITQ---RQ 236
Cdd:PRK15017 449 NETWGKRAFWFWIIGFFVAFMPLYALGFMGMTRRLSQQIDpQFHTMLMIAASGAALIALGILCQVIQMYVSIRDRdqnRD 528

                        250       260
                 ....*....|....*....|....*...
gi 58272111  237 VIFPIQLNSSIEWYQNIPPAEHSYSELP 264
Cdd:PRK15017 529 LTGDPWGGRTLEWATSSPPPFYNFAVVP 556
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
 64-231 3.99e-14

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: 71.55  E-value: 3.99e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58272111  64 TMIIAVPTGIKIFSWLATL-------HGSQL-SYSPALMW--------ALGFVFlFTVGGLTGVVLANSSVDIILHDTYY 127
Cdd:cd01660 282 TFMVALPSLLTAFTVFASLeiagrlrGGKGLfGWIRALPWgdpmflalFLAMLM-FIPGGAGGIINASYQLNYVVHNTAW 360

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58272111 128 VVAHFHyvLSMGAVFAIMA-GFIHWY-SLFTGLTLNSTWLKS-QFIIMFIGVNLTFFPQHFLGLAGMPRR--YSDYPDAY 202
Cdd:cd01660 361 VPGHFH--LTVGGAVALTFmAVAYWLvPHLTGRELAAKRLALaQPWLWFVGMTIMSTAMHVAGLLGAPRRtaEAQYGGLP 438

                       170       180       190
                ....*....|....*....|....*....|....
gi 58272111 203 -----TAWNVVSTIGSTISLLGILFFLFIIWESM 231
Cdd:cd01660 439 aagewAPYQQLMAIGGTILFVSGALFLYILFRTL 472
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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