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Conserved domains on  [gi|1194587600|gb|ARR97107|]
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cytochrome oxidase subunit I, partial (mitochondrion) [Arthroleptis xenodactyloides]

Protein Classification

heme-copper oxidase family protein( domain architecture ID 14)

heme-copper oxidase family protein may catalyze the transfer of electrons from an electron donor onto molecular oxygen

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Heme_Cu_Oxidase_I super family cl00275
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-255 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 MTH00116:

Pssm-ID: 469701  Cd Length: 515  Bit Score: 510.40  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587600   1 LNTTFFDP*GGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVTYYSGKKEPFGYMGMVWAMLSIGLLGFIVWAHHMFT 80
Cdd:MTH00116  215 LNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFT 294

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587600  81 TDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGMIKWETPMLWALGFIFLFTIGGLTGIVLSNSSIDIVLHDTYYVV 160
Cdd:MTH00116  295 VGMDVDTRAYFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVV 374

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587600 161 AHFHYVLSMGAVFAIMAGFVHWFPLFTGFTLHKTWTKIHFAVMFTGVNITFFPQHFLGLAGMPRRYSDYPDAYALWNTVS 240
Cdd:MTH00116  375 AHFHYVLSMGAVFAIMAGFTHWFPLFTGYTLHQTWTKAQFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTIS 454

                         250
                  ....*....|....*
gi 1194587600 241 SIGSLISLVAVVM*M 255
Cdd:MTH00116  455 SIGSLISMTAVIMLM 469
 
Name Accession Description Interval E-value
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-255 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 510.40  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587600   1 LNTTFFDP*GGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVTYYSGKKEPFGYMGMVWAMLSIGLLGFIVWAHHMFT 80
Cdd:MTH00116  215 LNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFT 294

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587600  81 TDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGMIKWETPMLWALGFIFLFTIGGLTGIVLSNSSIDIVLHDTYYVV 160
Cdd:MTH00116  295 VGMDVDTRAYFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVV 374

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587600 161 AHFHYVLSMGAVFAIMAGFVHWFPLFTGFTLHKTWTKIHFAVMFTGVNITFFPQHFLGLAGMPRRYSDYPDAYALWNTVS 240
Cdd:MTH00116  375 AHFHYVLSMGAVFAIMAGFTHWFPLFTGYTLHQTWTKAQFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTIS 454

                         250
                  ....*....|....*
gi 1194587600 241 SIGSLISLVAVVM*M 255
Cdd:MTH00116  455 SIGSLISMTAVIMLM 469
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-255 2.18e-178

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: 499.32  E-value: 2.18e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587600   1 LNTTFFDP*GGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVTYYSGKKEPFGYMGMVWAMLSIGLLGFIVWAHHMFT 80
Cdd:cd01663   206 FNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFT 285

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587600  81 TDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGMIKWETPMLWALGFIFLFTIGGLTGIVLSNSSIDIVLHDTYYVV 160
Cdd:cd01663   286 VGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVV 365

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587600 161 AHFHYVLSMGAVFAIMAGFVHWFPLFTGFTLHKTWTKIHFAVMFTGVNITFFPQHFLGLAGMPRRYSDYPDAYALWNTVS 240
Cdd:cd01663   366 AHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMIS 445

                         250
                  ....*....|....*
gi 1194587600 241 SIGSLISLVAVVM*M 255
Cdd:cd01663   446 SIGSLISFVSVLLFL 460
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-253 6.84e-118

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 347.11  E-value: 6.84e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587600   1 LNTTFFDP*GGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVTYYSGKKePFGYMGMVWAMLSIGLLGFIVWAHHMFT 80
Cdd:COG0843   217 LGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFT 295

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587600  81 TDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGMIKWETPMLWALGFIFLFTIGGLTGIVLSNSSIDIVLHDTYYVV 160
Cdd:COG0843   296 PGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVV 375

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587600 161 AHFHYVLSMGAVFAIMAGFVHWFPLFTGFTLHKTWTKIHFAVMFTGVNITFFPQHFLGLAGMPRRYSDYP--DAYALWNT 238
Cdd:COG0843   376 AHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNL 455

                         250
                  ....*....|....*
gi 1194587600 239 VSSIGSLISLVAVVM 253
Cdd:COG0843   456 ISTIGAFILAVGFLL 470
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-253 9.79e-114

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: 335.35  E-value: 9.79e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587600   1 LNTTFFDP*GGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVTYYSGKKePFGYMGMVWAMLSIGLLGFIVWAHHMFT 80
Cdd:TIGR02891 208 FGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFARKP-IFGYRAMVYATVAIGFLSFGVWAHHMFT 286

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587600  81 TDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGMIKWETPMLWALGFIFLFTIGGLTGIVLSNSSIDIVLHDTYYVV 160
Cdd:TIGR02891 287 TGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVV 366

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587600 161 AHFHYVLSMGAVFAIMAGFVHWFPLFTGFTLHKTWTKIHFAVMFTGVNITFFPQHFLGLAGMPRRYSDYPDA--YALWNT 238
Cdd:TIGR02891 367 AHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNL 446

                         250
                  ....*....|....*
gi 1194587600 239 VSSIGSLISLVAVVM 253
Cdd:TIGR02891 447 ISTIGAFILAAGFLV 461
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 8-246 1.69e-80

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: 248.26  E-value: 1.69e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587600   8 P*GGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVTYYSGKKePFGYMGMVWAMLSIGLLGFIVWAHHMFTTDLNVDT 87
Cdd:pfam00115 190 GAGGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGRP-LFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWL 268

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587600  88 RAYFTSATMIIAIPTGVKVFSWLATMHGGMIKW-ETPMLWALGFIFLFTIGGLTGIVLSNSSIDIVLHDTYYVVAHFHYV 166
Cdd:pfam00115 269 QALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFrTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYV 348

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587600 167 LSMGAVFAIMAGFVHWFPLFTGFTLHKTWTKIHFAVMFTGVNITFFPQHFLGLAGMPRRYS----DYPDAYALWNTVSSI 242
Cdd:pfam00115 349 LFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFWLLFIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPLNWIRTI 428


                  ....
gi 1194587600 243 GSLI 246
Cdd:pfam00115 429 GGVL 432
 
Name Accession Description Interval E-value
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 1-255 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 510.40  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587600   1 LNTTFFDP*GGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVTYYSGKKEPFGYMGMVWAMLSIGLLGFIVWAHHMFT 80
Cdd:MTH00116  215 LNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFT 294

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587600  81 TDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGMIKWETPMLWALGFIFLFTIGGLTGIVLSNSSIDIVLHDTYYVV 160
Cdd:MTH00116  295 VGMDVDTRAYFTSATMIIAIPTGIKVFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVV 374

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587600 161 AHFHYVLSMGAVFAIMAGFVHWFPLFTGFTLHKTWTKIHFAVMFTGVNITFFPQHFLGLAGMPRRYSDYPDAYALWNTVS 240
Cdd:MTH00116  375 AHFHYVLSMGAVFAIMAGFTHWFPLFTGYTLHQTWTKAQFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTIS 454

                         250
                  ....*....|....*
gi 1194587600 241 SIGSLISLVAVVM*M 255
Cdd:MTH00116  455 SIGSLISMTAVIMLM 469
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 1-255 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 506.71  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587600   1 LNTTFFDP*GGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVTYYSGKKEPFGYMGMVWAMLSIGLLGFIVWAHHMFT 80
Cdd:MTH00153  213 LNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFT 292

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587600  81 TDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGMIKWETPMLWALGFIFLFTIGGLTGIVLSNSSIDIVLHDTYYVV 160
Cdd:MTH00153  293 VGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVV 372

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587600 161 AHFHYVLSMGAVFAIMAGFVHWFPLFTGFTLHKTWTKIHFAVMFTGVNITFFPQHFLGLAGMPRRYSDYPDAYALWNTVS 240
Cdd:MTH00153  373 AHFHYVLSMGAVFAIMGGFIHWFPLFTGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVIS 452

                         250
                  ....*....|....*
gi 1194587600 241 SIGSLISLVAVVM*M 255
Cdd:MTH00153  453 SIGSTISLISILFFI 467
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 1-255 2.18e-178

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: 499.32  E-value: 2.18e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587600   1 LNTTFFDP*GGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVTYYSGKKEPFGYMGMVWAMLSIGLLGFIVWAHHMFT 80
Cdd:cd01663   206 FNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFT 285

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587600  81 TDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGMIKWETPMLWALGFIFLFTIGGLTGIVLSNSSIDIVLHDTYYVV 160
Cdd:cd01663   286 VGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVV 365

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587600 161 AHFHYVLSMGAVFAIMAGFVHWFPLFTGFTLHKTWTKIHFAVMFTGVNITFFPQHFLGLAGMPRRYSDYPDAYALWNTVS 240
Cdd:cd01663   366 AHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETLGKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMIS 445

                         250
                  ....*....|....*
gi 1194587600 241 SIGSLISLVAVVM*M 255
Cdd:cd01663   446 SIGSLISFVSVLLFL 460
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 1-255 2.90e-174

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 489.96  E-value: 2.90e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587600   1 LNTTFFDP*GGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVTYYSGKKEPFGYMGMVWAMLSIGLLGFIVWAHHMFT 80
Cdd:MTH00167  215 LNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVVYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFT 294

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587600  81 TDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGMIKWETPMLWALGFIFLFTIGGLTGIVLSNSSIDIVLHDTYYVV 160
Cdd:MTH00167  295 VGMDVDTRAYFTSATMIIAVPTGIKVFSWLATLHGGKIKWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVV 374

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587600 161 AHFHYVLSMGAVFAIMAGFVHWFPLFTGFTLHKTWTKIHFAVMFTGVNITFFPQHFLGLAGMPRRYSDYPDAYALWNTVS 240
Cdd:MTH00167  375 AHFHYVLSMGAVFAIMAGFTHWFPLFTGLTLNETWTKIHFFVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNVVS 454

                         250
                  ....*....|....*
gi 1194587600 241 SIGSLISLVAVVM*M 255
Cdd:MTH00167  455 SIGSLISLVAVILFL 469
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 1-255 2.53e-169

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 477.51  E-value: 2.53e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587600   1 LNTTFFDP*GGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVTYYSGKKEPFGYMGMVWAMLSIGLLGFIVWAHHMFT 80
Cdd:MTH00077  215 LNTTFFDPAGGGDPVLYQHLFWFFGHPEVYILILPGFGMISHIVTYYSAKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFT 294

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587600  81 TDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGMIKWETPMLWALGFIFLFTIGGLTGIVLSNSSIDIVLHDTYYVV 160
Cdd:MTH00077  295 VDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGAIKWDAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVV 374

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587600 161 AHFHYVLSMGAVFAIMAGFVHWFPLFTGFTLHKTWTKIHFAVMFTGVNITFFPQHFLGLAGMPRRYSDYPDAYALWNTVS 240
Cdd:MTH00077  375 AHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLHSTWSKIHFGVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVS 454

                         250
                  ....*....|....*
gi 1194587600 241 SIGSLISLVAVVM*M 255
Cdd:MTH00077  455 SIGSLISLVAVIMMM 469
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 1-255 3.03e-161

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 457.08  E-value: 3.03e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587600   1 LNTTFFDP*GGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVTYYSGKKEPFGYMGMVWAMLSIGLLGFIVWAHHMFT 80
Cdd:MTH00183  215 LNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFT 294

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587600  81 TDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGMIKWETPMLWALGFIFLFTIGGLTGIVLSNSSIDIVLHDTYYVV 160
Cdd:MTH00183  295 VGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVV 374

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587600 161 AHFHYVLSMGAVFAIMAGFVHWFPLFTGFTLHKTWTKIHFAVMFTGVNITFFPQHFLGLAGMPRRYSDYPDAYALWNTVS 240
Cdd:MTH00183  375 AHFHYVLSMGAVFAIMAAFVHWFPLFSGYTLHSTWTKIHFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVS 454

                         250
                  ....*....|....*
gi 1194587600 241 SIGSLISLVAVVM*M 255
Cdd:MTH00183  455 SIGSLISLVAVIMFL 469
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 2-255 9.95e-161

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 455.59  E-value: 9.95e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587600   2 NTTFFDP*GGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVTYYSGKKEPFGYMGMVWAMLSIGLLGFIVWAHHMFTT 81
Cdd:MTH00223  213 NTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVSHYSSKKEVFGTLGMIYAMLSIGVLGFIVWAHHMFTV 292

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587600  82 DLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGMIKWETPMLWALGFIFLFTIGGLTGIVLSNSSIDIVLHDTYYVVA 161
Cdd:MTH00223  293 GMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGSKIKYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVA 372

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587600 162 HFHYVLSMGAVFAIMAGFVHWFPLFTGFTLHKTWTKIHFAVMFTGVNITFFPQHFLGLAGMPRRYSDYPDAYALWNTVSS 241
Cdd:MTH00223  373 HFHYVLSMGAVFALFAGFNHWFPLFTGVTLHRRWAKAHFFLMFLGVNLTFFPQHFLGLAGMPRRYSDYPDCYTKWNQVSS 452

                         250
                  ....*....|....
gi 1194587600 242 IGSLISLVAVVM*M 255
Cdd:MTH00223  453 FGSMISFVSVLFFM 466
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 1-255 2.80e-157

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 446.86  E-value: 2.80e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587600   1 LNTTFFDP*GGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVTYYSGKKEPFGYMGMVWAMLSIGLLGFIVWAHHMFT 80
Cdd:MTH00142  213 FNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIINHYSGKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFT 292

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587600  81 TDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGMIKWETPMLWALGFIFLFTIGGLTGIVLSNSSIDIVLHDTYYVV 160
Cdd:MTH00142  293 VGMDVDTRAYFTAATMVIAVPTGIKVFSWLATLHGSKVKYEPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVV 372

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587600 161 AHFHYVLSMGAVFAIMAGFVHWFPLFTGFTLHKTWTKIHFAVMFTGVNITFFPQHFLGLAGMPRRYSDYPDAYALWNTVS 240
Cdd:MTH00142  373 AHFHYVLSMGAVFALFAGFIHWFPLFTGLTLNPRWLKAHFYTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVS 452

                         250
                  ....*....|....*
gi 1194587600 241 SIGSLISLVAVVM*M 255
Cdd:MTH00142  453 SLGSMISFIAVLMFV 467
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 1-255 4.24e-157

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 446.25  E-value: 4.24e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587600   1 LNTTFFDP*GGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVTYYSGKKEPFGYMGMVWAMLSIGLLGFIVWAHHMFT 80
Cdd:MTH00103  215 LNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFT 294

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587600  81 TDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGMIKWETPMLWALGFIFLFTIGGLTGIVLSNSSIDIVLHDTYYVV 160
Cdd:MTH00103  295 VGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGNIKWSPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVV 374

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587600 161 AHFHYVLSMGAVFAIMAGFVHWFPLFTGFTLHKTWTKIHFAVMFTGVNITFFPQHFLGLAGMPRRYSDYPDAYALWNTVS 240
Cdd:MTH00103  375 AHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLNDTWAKIHFTIMFVGVNMTFFPQHFLGLSGMPRRYSDYPDAYTTWNTVS 454

                         250
                  ....*....|....*
gi 1194587600 241 SIGSLISLVAVVM*M 255
Cdd:MTH00103  455 SMGSFISLTAVMLMI 469
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 1-255 1.92e-146

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 419.23  E-value: 1.92e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587600   1 LNTTFFDP*GGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVTYYSGKKEPFGYMGMVWAMLSIGLLGFIVWAHHMFT 80
Cdd:MTH00037  215 INTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISHVIAHYSGKQEPFGYLGMVYAMIAIGILGFLVWAHHMFT 294

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587600  81 TDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGMIKWETPMLWALGFIFLFTIGGLTGIVLSNSSIDIVLHDTYYVV 160
Cdd:MTH00037  295 VGMDVDTRAYFTAATMIIAVPTGIKVFSWMATLQGSNLRWETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVV 374

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587600 161 AHFHYVLSMGAVFAIMAGFVHWFPLFTGFTLHKTWTKIHFAVMFTGVNITFFPQHFLGLAGMPRRYSDYPDAYALWNTVS 240
Cdd:MTH00037  375 AHFHYVLSMGAVFAIFAGFTHWFPLFSGVSLHPLWSKVHFFLMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVS 454

                         250
                  ....*....|....*
gi 1194587600 241 SIGSLISLVAVVM*M 255
Cdd:MTH00037  455 SIGSTISLVATLFFL 469
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 1-255 5.85e-143

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 410.45  E-value: 5.85e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587600   1 LNTTFFDP*GGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVTYYSGKKEPFGYMGMVWAMLSIGLLGFIVWAHHMFT 80
Cdd:MTH00007  212 LNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGAISHIVTHYAGKLEPFGTLGMIYAMLGIGVLGFIVWAHHMFT 291

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587600  81 TDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGMIKWETPMLWALGFIFLFTIGGLTGIVLSNSSIDIVLHDTYYVV 160
Cdd:MTH00007  292 VGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGSPIKYETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVV 371

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587600 161 AHFHYVLSMGAVFAIMAGFVHWFPLFTGFTLHKTWTKIHFAVMFTGVNITFFPQHFLGLAGMPRRYSDYPDAYALWNTVS 240
Cdd:MTH00007  372 AHFHYVLSMGAVFAIFAAFNHWFPLFTGLTLHDRWAKAHFFLMFLGVNLTFFPQHFLGLSGMPRRYSDYPDAYTKWNVVS 451

                         250
                  ....*....|....*
gi 1194587600 241 SIGSLISLVAVVM*M 255
Cdd:MTH00007  452 SFGSMLSFVALLLFI 466
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 2-252 3.06e-128

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 373.39  E-value: 3.06e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587600   2 NTTFFDP*GGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVTYYSGKKEPFGYMGMVWAMLSIGLLGFIVWAHHMFTT 81
Cdd:MTH00182  218 NTTFFDPAGGGDPILFQHLFWFFGHPEVYILILPGFGMISQIIPTFVAKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTV 297

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587600  82 DLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGMIKWETPMLWALGFIFLFTIGGLTGIVLSNSSIDIVLHDTYYVVA 161
Cdd:MTH00182  298 GMDVDTRAYFTAATMIIAVPTGIKVFSWLATIYGGTLRLDTPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVA 377

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587600 162 HFHYVLSMGAVFAIMAGFVHWFPLFTGFTLHKTWTKIHFAVMFTGVNITFFPQHFLGLAGMPRRYSDYPDAYALWNTVSS 241
Cdd:MTH00182  378 HFHYVLSMGAVFAIFGGFYYWFGKITGYCYNELYGKIHFWLMFIGVNLTFFPQHFLGLAGFPRRYSDFADAFAGWNLVSS 457

                         250
                  ....*....|.
gi 1194587600 242 IGSLISLVAVV 252
Cdd:MTH00182  458 LGSIISIVGVV 468
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 1-253 5.20e-128

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 372.09  E-value: 5.20e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587600   1 LNTTFFDP*GGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVTYYSGKKEPFGYMGMVWAMLSIGLLGFIVWAHHMFT 80
Cdd:MTH00079  215 LNTSFFDPSTGGNPLLYQHLFWFFGHPEVYILILPAFGIISQSTLYLTGKKEVFGSLGMVYAILSIGLIGCVVWAHHMYT 294

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587600  81 TDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGMIKWETPMLWALGFIFLFTIGGLTGIVLSNSSIDIVLHDTYYVV 160
Cdd:MTH00079  295 VGMDLDSRAYFTAATMVIAVPTGVKVFSWLATLFGMKMKFQPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVV 374

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587600 161 AHFHYVLSMGAVFAIMAGFVHWFPLFTGFTLHKTWTKIHFAVMFTGVNITFFPQHFLGLAGMPRRYSDYPDAYALWNTVS 240
Cdd:MTH00079  375 SHFHYVLSLGAVFGIFTGISLWWPFMTGIVYDKLMMSAVFFLMFVGVNLTFFPLHFAGLHGMPRKYLDYPDVYSVWNVIS 454

                         250
                  ....*....|...
gi 1194587600 241 SIGSLISLVAVVM 253
Cdd:MTH00079  455 SYGSMISVFALFL 467
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 1-252 3.46e-126

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 368.00  E-value: 3.46e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587600   1 LNTTFFDP*GGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVTYYSGKKEPFGYMGMVWAMLSIGLLGFIVWAHHMFT 80
Cdd:MTH00184  217 FNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFT 296

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587600  81 TDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGMIKWETPMLWALGFIFLFTIGGLTGIVLSNSSIDIVLHDTYYVV 160
Cdd:MTH00184  297 VGMDVDTRAYFTAATMIIAVPTGIKIFSWIATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVV 376

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587600 161 AHFHYVLSMGAVFAIMAGFVHWFPLFTGFTLHKTWTKIHFAVMFTGVNITFFPQHFLGLAGMPRRYSDYPDAYALWNTVS 240
Cdd:MTH00184  377 AHFHYVLSMGAVFAIFGGFYYWFGKITGYCYNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDSFAGWNQIS 456

                         250
                  ....*....|..
gi 1194587600 241 SIGSLISLVAVV 252
Cdd:MTH00184  457 SLGSVISIVGVV 468
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 1-253 2.81e-120

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: 350.68  E-value: 2.81e-120
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587600   1 LNTTFFDP*GGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVTYYSGKKePFGYMGMVWAMLSIGLLGFIVWAHHMFT 80
Cdd:cd00919   203 FGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAFGAISEIIPTFSGKP-LFGYKLMVYAFLAIGFLSFLVWAHHMFT 281

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587600  81 TDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGMIKWETPMLWALGFIFLFTIGGLTGIVLSNSSIDIVLHDTYYVV 160
Cdd:cd00919   282 VGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGRIRFDPPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVV 361

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587600 161 AHFHYVLSMGAVFAIMAGFVHWFPLFTGFTLHKTWTKIHFAVMFTGVNITFFPQHFLGLAGMPRRYSDYPDAYALWNTVS 240
Cdd:cd00919   362 AHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKLGKIHFWLWFIGFNLTFFPMHFLGLLGMPRRYADYPDGFAPWNFIS 441

                         250
                  ....*....|...
gi 1194587600 241 SIGSLISLVAVVM 253
Cdd:cd00919   442 SVGAFILGLGLLL 454
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
1-253 6.84e-118

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 347.11  E-value: 6.84e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587600   1 LNTTFFDP*GGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVTYYSGKKePFGYMGMVWAMLSIGLLGFIVWAHHMFT 80
Cdd:COG0843   217 LGTHFFDPAGGGDPLLWQHLFWFFGHPEVYILILPAFGIVSEIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFT 295

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587600  81 TDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGMIKWETPMLWALGFIFLFTIGGLTGIVLSNSSIDIVLHDTYYVV 160
Cdd:COG0843   296 PGISPLVKAFFSIATMLIAVPTGVKVFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVV 375

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587600 161 AHFHYVLSMGAVFAIMAGFVHWFPLFTGFTLHKTWTKIHFAVMFTGVNITFFPQHFLGLAGMPRRYSDYP--DAYALWNT 238
Cdd:COG0843   376 AHFHYVLIGGVVFAFFAGLYYWFPKMTGRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNL 455

                         250
                  ....*....|....*
gi 1194587600 239 VSSIGSLISLVAVVM 253
Cdd:COG0843   456 ISTIGAFILAVGFLL 470
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 1-253 9.79e-114

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: 335.35  E-value: 9.79e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587600   1 LNTTFFDP*GGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVTYYSGKKePFGYMGMVWAMLSIGLLGFIVWAHHMFT 80
Cdd:TIGR02891 208 FGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFLPAFGIISEILPTFARKP-IFGYRAMVYATVAIGFLSFGVWAHHMFT 286

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587600  81 TDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGMIKWETPMLWALGFIFLFTIGGLTGIVLSNSSIDIVLHDTYYVV 160
Cdd:TIGR02891 287 TGMPPLALAFFSAATMLIAVPTGVKVFNWIATLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVV 366

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587600 161 AHFHYVLSMGAVFAIMAGFVHWFPLFTGFTLHKTWTKIHFAVMFTGVNITFFPQHFLGLAGMPRRYSDYPDA--YALWNT 238
Cdd:TIGR02891 367 AHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNL 446

                         250
                  ....*....|....*
gi 1194587600 239 VSSIGSLISLVAVVM 253
Cdd:TIGR02891 447 ISTIGAFILAAGFLV 461
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 1-252 4.08e-109

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 325.04  E-value: 4.08e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587600   1 LNTTFFDP*GGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVTYYSGKKEPFGYMGMVWAMLSIGLLGFIVWAHHMFT 80
Cdd:MTH00026  216 FNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISQILSLFSYKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYV 295

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587600  81 TDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGG--MIKWETPMLWALGFIFLFTIGGLTGIVLSNSSIDIVLHDTYY 158
Cdd:MTH00026  296 VGMDVDTRAYFTAATMIIAVPTGIKIFSWLATVSGSgrNLIFTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYY 375

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587600 159 VVAHFHYVLSMGAVFAIMAGFVHWFPLFTGFTLHKTWTKIHFAVMFTGVNITFFPQHFLGLAGMPRRYSDYPDAYALWNT 238
Cdd:MTH00026  376 VVAHFHFVLSMGAVFAIFGGFYLWFGKITGYAYKDIYGLIHFWLMFIGVNITFFPQHFLGLAGLPRRYADYPDNFEDFNQ 455

                         250
                  ....*....|....
gi 1194587600 239 VSSIGSLISLVAVV 252
Cdd:MTH00026  456 ISSFGSIISIIAVI 469
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 1-253 2.31e-106

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: 316.83  E-value: 2.31e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587600   1 LNTTFFDP*GGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVTYYSGKKePFGYMGMVWAMLSIGLLGFIVWAHHMFT 80
Cdd:cd01662   209 FGTHFFTNALGGNPMLWQHLFWIFGHPEVYILILPAFGIFSEIVPTFSRKP-LFGYRSMVYATVAIGFLSFGVWVHHMFT 287

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587600  81 TDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGMIKWETPMLWALGFIFLFTIGGLTGIVLSNSSIDIVLHDTYYVV 160
Cdd:cd01662   288 TGAGALVNAFFSIATMIIAVPTGVKIFNWLFTMWRGRIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVV 367

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587600 161 AHFHYVLSMGAVFAIMAGFVHWFPLFTGFTLHKTWTKIHFAVMFTGVNITFFPQHFLGLAGMPRRYSDYP--DAYALWNT 238
Cdd:cd01662   368 AHFHYVLIGGVVFPLFAGFYYWFPKMFGRMLNERLGKWSFWLWFIGFNLTFFPMHILGLMGMPRRVYTYLpgPGWDPLNL 447

                         250
                  ....*....|....*
gi 1194587600 239 VSSIGSLISLVAVVM 253
Cdd:cd01662   448 ISTIGAFLIAAGVLL 462
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 2-255 2.75e-99

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 298.90  E-value: 2.75e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587600   2 NTTFFDP*GGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVTYYSGKKEPFGYMGMVWAMLSIGLLGFIVWAHHMFTT 81
Cdd:MTH00048  214 GSAFFDPLGGGDPVLFQHMFWFFGHPEVYVLILPGFGIISHICLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWAHHMFTV 293

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587600  82 DLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHG-GMIKWETPMLWALGFIFLFTIGGLTGIVLSNSSIDIVLHDTYYVV 160
Cdd:MTH00048  294 GLDVKTAVFFSSVTMIIGVPTGIKVFSWLYMLLNsRVRKSDPVVWWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVV 373

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587600 161 AHFHYVLSMGAVFAIMAGFVHWFPLFTGFTLHKTWTKIHFAVMFTGVNITFFPQHFLGLAGMPRRYSDYPDAYALWNTVS 240
Cdd:MTH00048  374 AHFHYVLSLGSYSSVVIMFIWWWPLITGLSLNKYLLQCHCIISMIGFNLCFFPMHYFGLCGLPRRVCVYEPSYYWINVVC 453

                         250
                  ....*....|....*
gi 1194587600 241 SIGSLISLVAVVM*M 255
Cdd:MTH00048  454 TVGSFISAFSGCFFV 468
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 8-246 1.69e-80

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: 248.26  E-value: 1.69e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587600   8 P*GGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVTYYSGKKePFGYMGMVWAMLSIGLLGFIVWAHHMFTTDLNVDT 87
Cdd:pfam00115 190 GAGGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYILPKFAGRP-LFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWL 268

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587600  88 RAYFTSATMIIAIPTGVKVFSWLATMHGGMIKW-ETPMLWALGFIFLFTIGGLTGIVLSNSSIDIVLHDTYYVVAHFHYV 166
Cdd:pfam00115 269 QALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFrTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYV 348

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587600 167 LSMGAVFAIMAGFVHWFPLFTGFTLHKTWTKIHFAVMFTGVNITFFPQHFLGLAGMPRRYS----DYPDAYALWNTVSSI 242
Cdd:pfam00115 349 LFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFWLLFIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPLNWIRTI 428


                  ....
gi 1194587600 243 GSLI 246
Cdd:pfam00115 429 GGVL 432
CyoB TIGR02843
cytochrome o ubiquinol oxidase, subunit I; Cytochrome o terminal oxidase complex is the ...
 1-252 1.17e-74

cytochrome o ubiquinol oxidase, subunit I; Cytochrome o terminal oxidase complex is the component of the aerobic respiratory chain which reacts with oxygen, reducing it to water with the concomitant transport of 4 protons across the membrane. Also known as the cytochrome bo complex, cytochrome o ubiquinol oxidase contains four subunits, two heme b cofactors and a copper atom which is believed to be the oxygen active site. This complex is structurally related to the cytochrome caa3 oxidases which utilize cytochrome c as the reductant and contain heme a cofactors, as well as the intermediate form aa3 oxidases which also react directly with quinones as the reductant. [Energy metabolism, Electron transport]


Pssm-ID: 131890  Cd Length: 646  Bit Score: 238.80  E-value: 1.17e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587600   1 LNTTFFDP*GGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVTYYSGKKEpFGYMGMVWAMLSIGLLGFIVWAHHMFT 80
Cdd:TIGR02843 258 LGMHFFTNEAGGNPMMYVNLIWAWGHPEVYILILPAFGIFSEVVATFSRKRL-FGYTSMVWATIAITVLSFIVWLHHFFT 336

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587600  81 TDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGMIKWETPMLWALGFIFLFTIGGLTGIVLSNSSIDIVLHDTYYVV 160
Cdd:TIGR02843 337 MGAGANVNAFFGIATMIIAIPTGVKIFNWLFTMYKGRIRFETPMLWTIGFMVTFSIGGMTGVLLAVPPADFVLHNSLFLI 416

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587600 161 AHFHYVLSMGAVFAIMAGFVHWFPLFTGFTLHKTWTKIHFAVMFTGVNITFFPQHFLGLAGMPRRYSDYPD-AYALWNTV 239
Cdd:TIGR02843 417 AHFHNVIIGGVVFGCFAGLTYWFPKAFGFKLNEKLGKRSFWCWFIGFYLAFMPLYILGFMGMTRRLNHYDNpEWHPMLII 496

                         250
                  ....*....|...
gi 1194587600 240 SSIGSLISLVAVV 252
Cdd:TIGR02843 497 AAFGAFLIACGIL 509
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 1-231 3.06e-62

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 206.33  E-value: 3.06e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587600   1 LNTTFFDP*GGGDPVLYQHLFWFFGHPEVYILILPGFGIISHVVTYYSgKKEPFGYMGMVWAMLSIGLLGFIVWAHHMFT 80
Cdd:PRK15017  259 LGTHFFTNDMGGNMMMYINLIWAWGHPEVYILILPVFGVFSEIAATFS-RKRLFGYTSLVWATVCITVLSFIVWLHHFFT 337

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587600  81 TDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMHGGMIKWETPMLWALGFIFLFTIGGLTGIVLSNSSIDIVLHDTYYVV 160
Cdd:PRK15017  338 MGAGANVNAFFGITTMIIAIPTGVKIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLI 417

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1194587600 161 AHFHYVLSMGAVFAIMAGFVHWFPLFTGFTLHKTWTKIHFAVMFTGVNITFFPQHFLGLAGMPRRYSDYPD 231
Cdd:PRK15017  418 AHFHNVIIGGVVFGCFAGMTYWWPKAFGFKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMTRRLSQQID 488
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
 13-253 2.85e-16

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: 77.71  E-value: 2.85e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587600  13 DPVLYQHLFWFFGHPEVYILILPGFGIISHVVTYYSGKKEPFGYMGMVWAMLSIgLLGFIVWAHHMFTtDLNVDTRAYF- 91
Cdd:cd01660   200 DVLLSRTLFWWFGHPLVYFWLLPAYIAWYTILPKIAGGKLFSDPLARLAFILFL-LFSTPVGFHHQFA-DPGIGPGWKFi 277

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587600  92 -TSATMIIAIPTGVKVFSWLATM--------HGGMIKWETPMLW--------ALGFIFlFTIGGLTGIVLSNSSIDIVLH 154
Cdd:cd01660   278 hMVLTFMVALPSLLTAFTVFASLeiagrlrgGKGLFGWIRALPWgdpmflalFLAMLM-FIPGGAGGIINASYQLNYVVH 356

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194587600 155 DTYYVVAHFHyvLSMGAVFAIMA-GFVHWF-PLFTGFTL-HKTWTKIHFAVMFTGVNITFFPQHFLGLAGMPRR--YSDY 229
Cdd:cd01660   357 NTAWVPGHFH--LTVGGAVALTFmAVAYWLvPHLTGRELaAKRLALAQPWLWFVGMTIMSTAMHVAGLLGAPRRtaEAQY 434

                         250       260
                  ....*....|....*....|....*....
gi 1194587600 230 PDAY-----ALWNTVSSIGSLISLVAVVM 253
Cdd:cd01660   435 GGLPaagewAPYQQLMAIGGTILFVSGAL 463
 
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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