NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2513212473|gb|WIF29578|]
View 

cytochrome c oxidase subunit I (mitochondrion) [Paraechinus hypomelas]

Protein Classification

cytochrome-c oxidase subunit 1( domain architecture ID 10009591)

cytochrome-c oxidase subunit 1 is the catalytic subunit of cytochrome c oxidase, which is the component of the respiratory chain that catalyzes the reduction of oxygen to water

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
5-512 0e+00

cytochrome c oxidase subunit I; Provisional


:

Pssm-ID: 177210  Cd Length: 511  Bit Score: 952.77  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473   5 RWLFSTNHKDIGTLYLLFGAWAGMVGTSLSLLIRAELGQPGALMGDDQIYNVVVTAHAFVMIFFMVMPIMLGGFGNWLVP 84
Cdd:MTH00153    3 KWLFSTNHKDIGTLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVP 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473  85 LMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGVGTGWTVYPPLAGNLAHAGCSVDLAIFSLHLAGVSSILGAINF 164
Cdd:MTH00153   83 LMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINF 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 165 ITTIINMKPPAMSQYQTPLFVWSILITAVLLLLALPVLAAGITMLLTDRNINTTFFDPAGGGDPILYQHLFWFFGHPEVY 244
Cdd:MTH00153  163 ITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 245 ILILPGFGIISHIVAYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGLDVDTRAYFTSATMIIAIPTGVKVFSWL 324
Cdd:MTH00153  243 ILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 325 ATLHGGHINWAPALMWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLLTGYT 404
Cdd:MTH00153  323 ATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLT 402
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 405 LNDTWAKIHFIIMFMGVNITFFPQHFLGLAGMPRRYSDYPDAYTTWNTVSSMGSFISLTAVMLMVFLIWEAFAAKREVLK 484
Cdd:MTH00153  403 MNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPVLF 482
                         490       500
                  ....*....|....*....|....*...
gi 2513212473 485 IEFTNTNIEWLHGCPPPYHTFEEPTYIM 512
Cdd:MTH00153  483 SLNLSSSIEWLQNLPPAEHSYSELPLLT 510
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
5-512 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 952.77  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473   5 RWLFSTNHKDIGTLYLLFGAWAGMVGTSLSLLIRAELGQPGALMGDDQIYNVVVTAHAFVMIFFMVMPIMLGGFGNWLVP 84
Cdd:MTH00153    3 KWLFSTNHKDIGTLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVP 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473  85 LMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGVGTGWTVYPPLAGNLAHAGCSVDLAIFSLHLAGVSSILGAINF 164
Cdd:MTH00153   83 LMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINF 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 165 ITTIINMKPPAMSQYQTPLFVWSILITAVLLLLALPVLAAGITMLLTDRNINTTFFDPAGGGDPILYQHLFWFFGHPEVY 244
Cdd:MTH00153  163 ITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 245 ILILPGFGIISHIVAYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGLDVDTRAYFTSATMIIAIPTGVKVFSWL 324
Cdd:MTH00153  243 ILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 325 ATLHGGHINWAPALMWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLLTGYT 404
Cdd:MTH00153  323 ATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLT 402
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 405 LNDTWAKIHFIIMFMGVNITFFPQHFLGLAGMPRRYSDYPDAYTTWNTVSSMGSFISLTAVMLMVFLIWEAFAAKREVLK 484
Cdd:MTH00153  403 MNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPVLF 482
                         490       500
                  ....*....|....*....|....*...
gi 2513212473 485 IEFTNTNIEWLHGCPPPYHTFEEPTYIM 512
Cdd:MTH00153  483 SLNLSSSIEWLQNLPPAEHSYSELPLLT 510
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
10-496 0e+00

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: 877.20  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473  10 TNHKDIGTLYLLFGAWAGMVGTSLSLLIRAELGQPGALMGDDQIYNVVVTAHAFVMIFFMVMPIMLGGFGNWLVPLMIGA 89
Cdd:cd01663     1 TNHKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473  90 PDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGVGTGWTVYPPLAGNLAHAGCSVDLAIFSLHLAGVSSILGAINFITTII 169
Cdd:cd01663    81 PDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 170 NMKPPAMSQYQTPLFVWSILITAVLLLLALPVLAAGITMLLTDRNINTTFFDPAGGGDPILYQHLFWFFGHPEVYILILP 249
Cdd:cd01663   161 NMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILP 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 250 GFGIISHIVAYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGLDVDTRAYFTSATMIIAIPTGVKVFSWLATLHG 329
Cdd:cd01663   241 GFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWG 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 330 GHINWAPALMWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLLTGYTLNDTW 409
Cdd:cd01663   321 GSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETL 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 410 AKIHFIIMFMGVNITFFPQHFLGLAGMPRRYSDYPDAYTTWNTVSSMGSFISLTAVMLMVFLIWEAFAAKREVL-KIEFT 488
Cdd:cd01663   401 GKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIfNVGEG 480

                  ....*...
gi 2513212473 489 NTNIEWLH 496
Cdd:cd01663   481 STSLEWTL 488
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
2-511 0e+00

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 568.60  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473   2 LISRWLFSTNHKDIGTLYLLFGAWAGMVGTSLSLLIRAELGQPGALMGDDQIYNVVVTAHAFVMIFFMVMPiMLGGFGNW 81
Cdd:COG0843     5 GWRRWLTTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNY 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473  82 LVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGVGTGWTVYPPLAGNLAHAGCSVDLAIFSLHLAGVSSILGA 161
Cdd:COG0843    84 LVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGG 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 162 INFITTIINMKPPAMSQYQTPLFVWSILITAVLLLLALPVLAAGITMLLTDRNINTTFFDPAGGGDPILYQHLFWFFGHP 241
Cdd:COG0843   164 VNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHP 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 242 EVYILILPGFGIISHIVAYYSGKKePFGYMGMVWAMMSIGFLGFIVWAHHMFTVGLDVDTRAYFTSATMIIAIPTGVKVF 321
Cdd:COG0843   244 EVYILILPAFGIVSEIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVF 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 322 SWLATLHGGHINWAPALMWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLLT 401
Cdd:COG0843   323 NWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMT 402
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 402 GYTLNDTWAKIHFIIMFMGVNITFFPQHFLGLAGMPRRYSDYP--DAYTTWNTVSSMGSFISLTAVMLMVFLIWEAFAAK 479
Cdd:COG0843   403 GRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAFILAVGFLLFLINLVVSLRKG 482
                         490       500       510
                  ....*....|....*....|....*....|..
gi 2513212473 480 REVLKIEFTNTNIEWLHGCPPPYHTFEEPTYI 511
Cdd:COG0843   483 PKAGGNPWGARTLEWATPSPPPLYNFASIPVV 514
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
7-505 0e+00

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: 564.54  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473   7 LFSTNHKDIGTLYLLFGAWAGMVGTSLSLLIRAELGQPGALMGDDQIYNVVVTAHAFVMIFFMVMPiMLGGFGNWLVPLM 86
Cdd:TIGR02891   1 LTTVDHKRIGILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIP-ILAGFGNYLLPLM 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473  87 IGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGVGTGWTVYPPLAGNLAHAGCSVDLAIFSLHLAGVSSILGAINFIT 166
Cdd:TIGR02891  80 IGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 167 TIINMKPPAMSQYQTPLFVWSILITAVLLLLALPVLAAGITMLLTDRNINTTFFDPAGGGDPILYQHLFWFFGHPEVYIL 246
Cdd:TIGR02891 160 TILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYII 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 247 ILPGFGIISHIVAYYSGKKePFGYMGMVWAMMSIGFLGFIVWAHHMFTVGLDVDTRAYFTSATMIIAIPTGVKVFSWLAT 326
Cdd:TIGR02891 240 FLPAFGIISEILPTFARKP-IFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIAT 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 327 LHGGHINWAPALMWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLLTGYTLN 406
Cdd:TIGR02891 319 LWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYN 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 407 DTWAKIHFIIMFMGVNITFFPQHFLGLAGMPRRYSDYPDA--YTTWNTVSSMGSFISLTAVMLMVFLIWEAFAAKREVLK 484
Cdd:TIGR02891 399 ERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGPKAGA 478
                         490       500
                  ....*....|....*....|.
gi 2513212473 485 IEFTNTNIEWLHGCPPPYHTF 505
Cdd:TIGR02891 479 NPWGATTLEWTTSSPPPAHNF 499
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
14-460 1.58e-131

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: 388.85  E-value: 1.58e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473  14 DIGTLYLLFGAWAGMVGTSLSLLIRAELGQPGALMGDDQIYNVVVTAHAFVMIFFMVMPIMlGGFGNWLVPLMIGAPDMA 93
Cdd:pfam00115   1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATPFL-FGFGNYLVPLMIGARDMA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473  94 FPRMNNMSFWLLPPSFLLLLASSMveaGVGTGWTVYPPLAGnlahagcsVDLAIFSLHLAGVSSILGAINFITTIINMKP 173
Cdd:pfam00115  80 FPRLNALSFWLVVLGAVLLLASFG---GATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRA 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 174 PAMSQyQTPLFVWSILITAVLLLLALPVLAAGITMLLTDRNINttffdpAGGGDPILYQHLFWFFGHPEVYILILPGFGI 253
Cdd:pfam00115 149 PGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGI 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 254 ISHIVAYYSGKKePFGYMGMVWAMMSIGFLGFIVWAHHMFTVGLDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGHIN 333
Cdd:pfam00115 222 IYYILPKFAGRP-LFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIR 300
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 334 WA-PALMWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLLTGYTLNDTWAKI 412
Cdd:pfam00115 301 FRtTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKL 380
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2513212473 413 HFIIMFMGVNITFFPQHFLGLAGMPRRYS----DYPDAYTTWNTVSSMGSFI 460
Cdd:pfam00115 381 HFWLLFIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPLNWIRTIGGVL 432
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
5-512 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 952.77  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473   5 RWLFSTNHKDIGTLYLLFGAWAGMVGTSLSLLIRAELGQPGALMGDDQIYNVVVTAHAFVMIFFMVMPIMLGGFGNWLVP 84
Cdd:MTH00153    3 KWLFSTNHKDIGTLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVP 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473  85 LMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGVGTGWTVYPPLAGNLAHAGCSVDLAIFSLHLAGVSSILGAINF 164
Cdd:MTH00153   83 LMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINF 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 165 ITTIINMKPPAMSQYQTPLFVWSILITAVLLLLALPVLAAGITMLLTDRNINTTFFDPAGGGDPILYQHLFWFFGHPEVY 244
Cdd:MTH00153  163 ITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 245 ILILPGFGIISHIVAYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGLDVDTRAYFTSATMIIAIPTGVKVFSWL 324
Cdd:MTH00153  243 ILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWL 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 325 ATLHGGHINWAPALMWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLLTGYT 404
Cdd:MTH00153  323 ATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLT 402
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 405 LNDTWAKIHFIIMFMGVNITFFPQHFLGLAGMPRRYSDYPDAYTTWNTVSSMGSFISLTAVMLMVFLIWEAFAAKREVLK 484
Cdd:MTH00153  403 MNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPVLF 482
                         490       500
                  ....*....|....*....|....*...
gi 2513212473 485 IEFTNTNIEWLHGCPPPYHTFEEPTYIM 512
Cdd:MTH00153  483 SLNLSSSIEWLQNLPPAEHSYSELPLLT 510
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
1-515 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 952.23  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473   1 MLISRWLFSTNHKDIGTLYLLFGAWAGMVGTSLSLLIRAELGQPGALMGDDQIYNVVVTAHAFVMIFFMVMPIMLGGFGN 80
Cdd:MTH00116    1 MFITRWLFSTNHKDIGTLYLIFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473  81 WLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGVGTGWTVYPPLAGNLAHAGCSVDLAIFSLHLAGVSSILG 160
Cdd:MTH00116   81 WLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 161 AINFITTIINMKPPAMSQYQTPLFVWSILITAVLLLLALPVLAAGITMLLTDRNINTTFFDPAGGGDPILYQHLFWFFGH 240
Cdd:MTH00116  161 AINFITTCINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGH 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 241 PEVYILILPGFGIISHIVAYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGLDVDTRAYFTSATMIIAIPTGVKV 320
Cdd:MTH00116  241 PEVYILILPGFGIISHIVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKV 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 321 FSWLATLHGGHINWAPALMWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLL 400
Cdd:MTH00116  321 FSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLF 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 401 TGYTLNDTWAKIHFIIMFMGVNITFFPQHFLGLAGMPRRYSDYPDAYTTWNTVSSMGSFISLTAVMLMVFLIWEAFAAKR 480
Cdd:MTH00116  401 TGYTLHQTWTKAQFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTISSIGSLISMTAVIMLMFIIWEAFSSKR 480
                         490       500       510
                  ....*....|....*....|....*....|....*
gi 2513212473 481 EVLKIEFTNTNIEWLHGCPPPYHTFEEPTYIMTKQ 515
Cdd:MTH00116  481 KVLQPELTTTNIEWIHGCPPPYHTFEEPAFVQVQE 515
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
1-513 0e+00

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 915.04  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473   1 MLISRWLFSTNHKDIGTLYLLFGAWAGMVGTSLSLLIRAELGQPGALMGDDQIYNVVVTAHAFVMIFFMVMPIMLGGFGN 80
Cdd:MTH00103    1 MFINRWLFSTNHKDIGTLYLLFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473  81 WLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGVGTGWTVYPPLAGNLAHAGCSVDLAIFSLHLAGVSSILG 160
Cdd:MTH00103   81 WLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 161 AINFITTIINMKPPAMSQYQTPLFVWSILITAVLLLLALPVLAAGITMLLTDRNINTTFFDPAGGGDPILYQHLFWFFGH 240
Cdd:MTH00103  161 AINFITTIINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGH 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 241 PEVYILILPGFGIISHIVAYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGLDVDTRAYFTSATMIIAIPTGVKV 320
Cdd:MTH00103  241 PEVYILILPGFGMISHIVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKV 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 321 FSWLATLHGGHINWAPALMWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLL 400
Cdd:MTH00103  321 FSWLATLHGGNIKWSPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLF 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 401 TGYTLNDTWAKIHFIIMFMGVNITFFPQHFLGLAGMPRRYSDYPDAYTTWNTVSSMGSFISLTAVMLMVFLIWEAFAAKR 480
Cdd:MTH00103  401 SGYTLNDTWAKIHFTIMFVGVNMTFFPQHFLGLSGMPRRYSDYPDAYTTWNTVSSMGSFISLTAVMLMIFMIWEAFASKR 480
                         490       500       510
                  ....*....|....*....|....*....|...
gi 2513212473 481 EVLKIEFTNTNIEWLHGCPPPYHTFEEPTYIMT 513
Cdd:MTH00103  481 EVLTVELTTTNLEWLHGCPPPYHTFEEPTYVKL 513
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
1-512 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 914.83  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473   1 MLISRWLFSTNHKDIGTLYLLFGAWAGMVGTSLSLLIRAELGQPGALMGDDQIYNVVVTAHAFVMIFFMVMPIMLGGFGN 80
Cdd:MTH00167    1 MWINRWLFSTNHKDIGTLYFIFGAWAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473  81 WLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGVGTGWTVYPPLAGNLAHAGCSVDLAIFSLHLAGVSSILG 160
Cdd:MTH00167   81 WLVPLMIGAPDMAFPRMNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 161 AINFITTIINMKPPAMSQYQTPLFVWSILITAVLLLLALPVLAAGITMLLTDRNINTTFFDPAGGGDPILYQHLFWFFGH 240
Cdd:MTH00167  161 SINFITTIINMKPPGITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGH 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 241 PEVYILILPGFGIISHIVAYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGLDVDTRAYFTSATMIIAIPTGVKV 320
Cdd:MTH00167  241 PEVYILILPGFGMISHIVVYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKV 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 321 FSWLATLHGGHINWAPALMWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLL 400
Cdd:MTH00167  321 FSWLATLHGGKIKWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLF 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 401 TGYTLNDTWAKIHFIIMFMGVNITFFPQHFLGLAGMPRRYSDYPDAYTTWNTVSSMGSFISLTAVMLMVFLIWEAFAAKR 480
Cdd:MTH00167  401 TGLTLNETWTKIHFFVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNVVSSIGSLISLVAVILFLFIIWEAFSSKR 480
                         490       500       510
                  ....*....|....*....|....*....|..
gi 2513212473 481 EVLKIEFTNTNIEWLHGCPPPYHTFEEPTYIM 512
Cdd:MTH00167  481 KLLPVELTSTNVEWLHGCPPPHHTWEEPPFVQ 512
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
1-515 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 877.72  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473   1 MLISRWLFSTNHKDIGTLYLLFGAWAGMVGTSLSLLIRAELGQPGALMGDDQIYNVVVTAHAFVMIFFMVMPIMLGGFGN 80
Cdd:MTH00183    1 MAITRWFFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473  81 WLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGVGTGWTVYPPLAGNLAHAGCSVDLAIFSLHLAGVSSILG 160
Cdd:MTH00183   81 WLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 161 AINFITTIINMKPPAMSQYQTPLFVWSILITAVLLLLALPVLAAGITMLLTDRNINTTFFDPAGGGDPILYQHLFWFFGH 240
Cdd:MTH00183  161 AINFITTIINMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGH 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 241 PEVYILILPGFGIISHIVAYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGLDVDTRAYFTSATMIIAIPTGVKV 320
Cdd:MTH00183  241 PEVYILILPGFGMISHIVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKV 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 321 FSWLATLHGGHINWAPALMWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLL 400
Cdd:MTH00183  321 FSWLATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLF 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 401 TGYTLNDTWAKIHFIIMFMGVNITFFPQHFLGLAGMPRRYSDYPDAYTTWNTVSSMGSFISLTAVMLMVFLIWEAFAAKR 480
Cdd:MTH00183  401 SGYTLHSTWTKIHFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMFLFILWEAFAAKR 480
                         490       500       510
                  ....*....|....*....|....*....|....*
gi 2513212473 481 EVLKIEFTNTNIEWLHGCPPPYHTFEEPTYIMTKQ 515
Cdd:MTH00183  481 EVLSVELTSTNVEWLHGCPPPYHTFEEPAFVQVQS 515
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
10-496 0e+00

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: 877.20  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473  10 TNHKDIGTLYLLFGAWAGMVGTSLSLLIRAELGQPGALMGDDQIYNVVVTAHAFVMIFFMVMPIMLGGFGNWLVPLMIGA 89
Cdd:cd01663     1 TNHKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473  90 PDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGVGTGWTVYPPLAGNLAHAGCSVDLAIFSLHLAGVSSILGAINFITTII 169
Cdd:cd01663    81 PDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 170 NMKPPAMSQYQTPLFVWSILITAVLLLLALPVLAAGITMLLTDRNINTTFFDPAGGGDPILYQHLFWFFGHPEVYILILP 249
Cdd:cd01663   161 NMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILP 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 250 GFGIISHIVAYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGLDVDTRAYFTSATMIIAIPTGVKVFSWLATLHG 329
Cdd:cd01663   241 GFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWG 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 330 GHINWAPALMWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLLTGYTLNDTW 409
Cdd:cd01663   321 GSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETL 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 410 AKIHFIIMFMGVNITFFPQHFLGLAGMPRRYSDYPDAYTTWNTVSSMGSFISLTAVMLMVFLIWEAFAAKREVL-KIEFT 488
Cdd:cd01663   401 GKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIfNVGEG 480

                  ....*...
gi 2513212473 489 NTNIEWLH 496
Cdd:cd01663   481 STSLEWTL 488
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
1-514 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 866.18  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473   1 MLISRWLFSTNHKDIGTLYLLFGAWAGMVGTSLSLLIRAELGQPGALMGDDQIYNVVVTAHAFVMIFFMVMPIMLGGFGN 80
Cdd:MTH00077    1 MMITRWLFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473  81 WLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGVGTGWTVYPPLAGNLAHAGCSVDLAIFSLHLAGVSSILG 160
Cdd:MTH00077   81 WLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 161 AINFITTIINMKPPAMSQYQTPLFVWSILITAVLLLLALPVLAAGITMLLTDRNINTTFFDPAGGGDPILYQHLFWFFGH 240
Cdd:MTH00077  161 AINFITTSINMKPPSMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGH 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 241 PEVYILILPGFGIISHIVAYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGLDVDTRAYFTSATMIIAIPTGVKV 320
Cdd:MTH00077  241 PEVYILILPGFGMISHIVTYYSAKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKV 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 321 FSWLATLHGGHINWAPALMWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLL 400
Cdd:MTH00077  321 FSWLATMHGGAIKWDAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLF 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 401 TGYTLNDTWAKIHFIIMFMGVNITFFPQHFLGLAGMPRRYSDYPDAYTTWNTVSSMGSFISLTAVMLMVFLIWEAFAAKR 480
Cdd:MTH00077  401 SGYTLHSTWSKIHFGVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMMMFIIWEAFSSKR 480
                         490       500       510
                  ....*....|....*....|....*....|....
gi 2513212473 481 EVLKIEFTNTNIEWLHGCPPPYHTFEEPTYIMTK 514
Cdd:MTH00077  481 EVLTTELTSTNIEWLHGCPPPYHTFEEPSFVQTR 514
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
4-514 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 833.47  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473   4 SRWLFSTNHKDIGTLYLLFGAWAGMVGTSLSLLIRAELGQPGALMGDDQIYNVVVTAHAFVMIFFMVMPIMLGGFGNWLV 83
Cdd:MTH00223    1 MRWLFSTNHKDIGTLYLIFGMWSGLVGTSLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473  84 PLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGVGTGWTVYPPLAGNLAHAGCSVDLAIFSLHLAGVSSILGAIN 163
Cdd:MTH00223   81 PLMLGAPDMAFPRLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAIN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 164 FITTIINMKPPAMSQYQTPLFVWSILITAVLLLLALPVLAAGITMLLTDRNINTTFFDPAGGGDPILYQHLFWFFGHPEV 243
Cdd:MTH00223  161 FITTIINMRSPGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEV 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 244 YILILPGFGIISHIVAYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGLDVDTRAYFTSATMIIAIPTGVKVFSW 323
Cdd:MTH00223  241 YILILPGFGMISHIVSHYSSKKEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSW 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 324 LATLHGGHINWAPALMWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLLTGY 403
Cdd:MTH00223  321 LATIYGSKIKYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLFTGV 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 404 TLNDTWAKIHFIIMFMGVNITFFPQHFLGLAGMPRRYSDYPDAYTTWNTVSSMGSFISLTAVMLMVFLIWEAFAAKREVL 483
Cdd:MTH00223  401 TLHRRWAKAHFFLMFLGVNLTFFPQHFLGLAGMPRRYSDYPDCYTKWNQVSSFGSMISFVSVLFFMFIVWEAFVSQRSVV 480
                         490       500       510
                  ....*....|....*....|....*....|.
gi 2513212473 484 KIEFTNTNIEWLHGCPPPYHTFEEPTYIMTK 514
Cdd:MTH00223  481 WSGHLSTSLEWDNLLPADFHNNSETGALVIN 511
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
3-508 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 827.44  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473   3 ISRWLFSTNHKDIGTLYLLFGAWAGMVGTSLSLLIRAELGQPGALMGDDQIYNVVVTAHAFVMIFFMVMPIMLGGFGNWL 82
Cdd:MTH00142    1 MMRWLFSTNHKDIGTLYFLFGAWAGMVGTGLSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473  83 VPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGVGTGWTVYPPLAGNLAHAGCSVDLAIFSLHLAGVSSILGAI 162
Cdd:MTH00142   81 VPLMLGAPDMAFPRMNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 163 NFITTIINMKPPAMSQYQTPLFVWSILITAVLLLLALPVLAAGITMLLTDRNINTTFFDPAGGGDPILYQHLFWFFGHPE 242
Cdd:MTH00142  161 NFITTVINMRAGGMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 243 VYILILPGFGIISHIVAYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGLDVDTRAYFTSATMIIAIPTGVKVFS 322
Cdd:MTH00142  241 VYILILPGFGMISHIINHYSGKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFS 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 323 WLATLHGGHINWAPALMWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLLTG 402
Cdd:MTH00142  321 WLATLHGSKVKYEPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLFTG 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 403 YTLNDTWAKIHFIIMFMGVNITFFPQHFLGLAGMPRRYSDYPDAYTTWNTVSSMGSFISLTAVMLMVFLIWEAFAAKREV 482
Cdd:MTH00142  401 LTLNPRWLKAHFYTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSSLGSMISFIAVLMFVFIVWESFVSQRLV 480
                         490       500
                  ....*....|....*....|....*.
gi 2513212473 483 LKIEFTNTNIEWLHGCPPPYHTFEEP 508
Cdd:MTH00142  481 MWSSHLSTSLEWSHRLPPDFHTYDEL 506
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
1-507 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 772.85  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473   1 MLISRWLFSTNHKDIGTLYLLFGAWAGMVGTSLSLLIRAELGQPGALMGDDQIYNVVVTAHAFVMIFFMVMPIMLGGFGN 80
Cdd:MTH00037    1 MQLSRWLFSTNHKDIGTLYLIFGAWAGMVGTAMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473  81 WLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGVGTGWTVYPPLAGNLAHAGCSVDLAIFSLHLAGVSSILG 160
Cdd:MTH00037   81 WLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 161 AINFITTIINMKPPAMSQYQTPLFVWSILITAVLLLLALPVLAAGITMLLTDRNINTTFFDPAGGGDPILYQHLFWFFGH 240
Cdd:MTH00037  161 SINFITTIINMRTPGMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGH 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 241 PEVYILILPGFGIISHIVAYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGLDVDTRAYFTSATMIIAIPTGVKV 320
Cdd:MTH00037  241 PEVYILILPGFGMISHVIAHYSGKQEPFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKV 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 321 FSWLATLHGGHINWAPALMWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLL 400
Cdd:MTH00037  321 FSWMATLQGSNLRWETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLF 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 401 TGYTLNDTWAKIHFIIMFMGVNITFFPQHFLGLAGMPRRYSDYPDAYTTWNTVSSMGSFISLTAVMLMVFLIWEAFAAKR 480
Cdd:MTH00037  401 SGVSLHPLWSKVHFFLMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSTISLVATLFFLFLIWEAFASQR 480
                         490       500
                  ....*....|....*....|....*...
gi 2513212473 481 EVLKIEFTNTNIEWLHGC-PPPYHTFEE 507
Cdd:MTH00037  481 EVISPEFSSSSLEWQYSSfPPSHHTFDE 508
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
5-513 0e+00

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 735.94  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473   5 RWLFSTNHKDIGTLYLLFGAWAGMVGTSLSLLIRAELGQPGALMGDDQIYNVVVTAHAFVMIFFMVMPIMLGGFGNWLVP 84
Cdd:MTH00007    2 RWLYSTNHKDIGTLYFILGVWGGLLGTSMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473  85 LMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGVGTGWTVYPPLAGNLAHAGCSVDLAIFSLHLAGVSSILGAINF 164
Cdd:MTH00007   82 LMLGAPDMAFPRLNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINF 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 165 ITTIINMKPPAMSQYQTPLFVWSILITAVLLLLALPVLAAGITMLLTDRNINTTFFDPAGGGDPILYQHLFWFFGHPEVY 244
Cdd:MTH00007  162 ITTVINMRWKGLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 245 ILILPGFGIISHIVAYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGLDVDTRAYFTSATMIIAIPTGVKVFSWL 324
Cdd:MTH00007  242 ILILPGFGAISHIVTHYAGKLEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWL 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 325 ATLHGGHINWAPALMWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLLTGYT 404
Cdd:MTH00007  322 ATIHGSPIKYETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTGLT 401
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 405 LNDTWAKIHFIIMFMGVNITFFPQHFLGLAGMPRRYSDYPDAYTTWNTVSSMGSFISLTAVMLMVFLIWEAFAAKREVLK 484
Cdd:MTH00007  402 LHDRWAKAHFFLMFLGVNLTFFPQHFLGLSGMPRRYSDYPDAYTKWNVVSSFGSMLSFVALLLFIFILWEAFSAQRGVIA 481
                         490       500
                  ....*....|....*....|....*....
gi 2513212473 485 IEFTNTNIEWLHGCPPPYHTFEEPTYIMT 513
Cdd:MTH00007  482 SPHMSSSLEWQDTLPLDFHNLPETGIITT 510
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
3-511 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 688.48  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473   3 ISRWLFSTNHKDIGTLYLLFGAWAGMVGTSLSLLIRAELGQPGALMGDDQIYNVVVTAHAFVMIFFMVMPIMLGGFGNWL 82
Cdd:MTH00182    5 LTRWVFSTNHKDIGTLYLVFGAGAGMIGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473  83 VPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGVGTGWTVYPPLAGNLAHAGCSVDLAIFSLHLAGVSSILGAI 162
Cdd:MTH00182   85 VPLYIGAPDMAFPRLNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAI 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 163 NFITTIINMKPPAMSQYQTPLFVWSILITAVLLLLALPVLAAGITMLLTDRNINTTFFDPAGGGDPILYQHLFWFFGHPE 242
Cdd:MTH00182  165 NFITTIFNMRAPGVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPE 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 243 VYILILPGFGIISHIVAYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGLDVDTRAYFTSATMIIAIPTGVKVFS 322
Cdd:MTH00182  245 VYILILPGFGMISQIIPTFVAKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFS 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 323 WLATLHGGHINWAPALMWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLLTG 402
Cdd:MTH00182  325 WLATIYGGTLRLDTPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITG 404
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 403 YTLNDTWAKIHFIIMFMGVNITFFPQHFLGLAGMPRRYSDYPDAYTTWNTVSSMGSFISLTAVMLMVFLIWEAFAAKREV 482
Cdd:MTH00182  405 YCYNELYGKIHFWLMFIGVNLTFFPQHFLGLAGFPRRYSDFADAFAGWNLVSSLGSIISIVGVVWFIYIIYDAYVREEKF 484
                         490       500       510
                  ....*....|....*....|....*....|...
gi 2513212473 483 L----KIEFTNTNIEWLHGCPPPYHTFEEPTYI 511
Cdd:MTH00182  485 IgwkeGTGESWASLEWVHSSPPLFHTYNELPFV 517
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
3-512 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 681.94  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473   3 ISRWLFSTNHKDIGTLYLLFGAWAGMVGTSLSLLIRAELGQPGALMGDDQIYNVVVTAHAFVMIFFMVMPIMLGGFGNWL 82
Cdd:MTH00184    5 LSRWLFSTNHKDIGTLYLLFGAFAGMIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWF 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473  83 VPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGVGTGWTVYPPLAGNLAHAGCSVDLAIFSLHLAGVSSILGAI 162
Cdd:MTH00184   85 VPLYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAM 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 163 NFITTIINMKPPAMSQYQTPLFVWSILITAVLLLLALPVLAAGITMLLTDRNINTTFFDPAGGGDPILYQHLFWFFGHPE 242
Cdd:MTH00184  165 NFITTIFNMRAPGITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPE 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 243 VYILILPGFGIISHIVAYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGLDVDTRAYFTSATMIIAIPTGVKVFS 322
Cdd:MTH00184  245 VYILILPGFGIISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFS 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 323 WLATLHGGHINWAPALMWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLLTG 402
Cdd:MTH00184  325 WIATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITG 404
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 403 YTLNDTWAKIHFIIMFMGVNITFFPQHFLGLAGMPRRYSDYPDAYTTWNTVSSMGSFISLTAVMLMVFLIWEAFAakREV 482
Cdd:MTH00184  405 YCYNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDSFAGWNQISSLGSVISIVGVVWFIYIVYDAYV--REI 482
                         490       500       510
                  ....*....|....*....|....*....|....*
gi 2513212473 483 LKIEFTN-----TNIEWLHGCPPPYHTFEEPTYIM 512
Cdd:MTH00184  483 KFVGWVEdsghyPSLEWAQTSPPAHHTYNELPYVY 517
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
3-507 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 662.92  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473   3 ISRWLFSTNHKDIGTLYLLFGAWAGMVGTSLSLLIRAELGQPGALMGDDQIYNVVVTAHAFVMIFFMVMPIMLGGFGNWL 82
Cdd:MTH00079    4 LSVWLESSNHKDIGTLYFLFGLWSGMVGTSLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWM 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473  83 VPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGVGTGWTVYPPLAgNLAHAGCSVDLAIFSLHLAGVSSILGAI 162
Cdd:MTH00079   84 LPLMLGAPDMSFPRLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLS-TLGHPGSSVDLAIFSLHCAGISSILGGI 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 163 NFITTIINMKPPAMSQYQTPLFVWSILITAVLLLLALPVLAAGITMLLTDRNINTTFFDPAGGGDPILYQHLFWFFGHPE 242
Cdd:MTH00079  163 NFMVTTKNLRSSSISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPE 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 243 VYILILPGFGIISHIVAYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGLDVDTRAYFTSATMIIAIPTGVKVFS 322
Cdd:MTH00079  243 VYILILPAFGIISQSTLYLTGKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFS 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 323 WLATLHGGHINWAPALMWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLLTG 402
Cdd:MTH00079  323 WLATLFGMKMKFQPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFMTG 402
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 403 YTLNDTWAKIHFIIMFMGVNITFFPQHFLGLAGMPRRYSDYPDAYTTWNTVSSMGSFISLTAVMLMVFLIWEAFAAKREV 482
Cdd:MTH00079  403 IVYDKLMMSAVFFLMFVGVNLTFFPLHFAGLHGMPRKYLDYPDVYSVWNVISSYGSMISVFALFLFIYVLLESFFSYRLV 482
                         490       500
                  ....*....|....*....|....*
gi 2513212473 483 LKIEFTNTNIEWLHGCPPPYHTFEE 507
Cdd:MTH00079  483 LHDNYINSSPEYSLSSYVFGHSYQS 507
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
5-512 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 599.69  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473   5 RWLFSTNHKDIGTLYLLFGAWAGMVGTSLSLLIRAELGQPGALMGDDQIYNVVVTAHAFVMIFFMVMPIMLGGFGNWLVP 84
Cdd:MTH00026    6 RWFFSCNHKDIGSLYLVFGALSGAIGTAFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFVP 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473  85 LMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGVGTGWTVYPPLAGNLAHAGCSVDLAIFSLHLAGVSSILGAINF 164
Cdd:MTH00026   86 LMIGAPDMAFPRLNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMNF 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 165 ITTIINMKPPAMSQYQTPLFVWSILITAVLLLLALPVLAAGITMLLTDRNINTTFFDPAGGGDPILYQHLFWFFGHPEVY 244
Cdd:MTH00026  166 ITTVMNMRTPGMTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVY 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 245 ILILPGFGIISHIVAYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGLDVDTRAYFTSATMIIAIPTGVKVFSWL 324
Cdd:MTH00026  246 ILILPGFGIISQILSLFSYKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSWL 325
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 325 ATLHGGHIN--WAPALMWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLLTG 402
Cdd:MTH00026  326 ATVSGSGRNliFTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWFGKITG 405
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 403 YTLNDTWAKIHFIIMFMGVNITFFPQHFLGLAGMPRRYSDYPDAYTTWNTVSSMGSFISLTAVMLMVFLIWEAFaAKREV 482
Cdd:MTH00026  406 YAYKDIYGLIHFWLMFIGVNITFFPQHFLGLAGLPRRYADYPDNFEDFNQISSFGSIISIIAVIWFIVVIFDAY-YREEP 484
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....
gi 2513212473 483 LKIEFTNT--------------NIEWLHGCPPPYHTFEEPTYIM 512
Cdd:MTH00026  485 FDINIMAKgplipfscqpahfdTLEWSLTSPPEHHTYNELPYIV 528
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
12-476 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.


Pssm-ID: 238461  Cd Length: 463  Bit Score: 587.58  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473  12 HKDIGTLYLLFGAWAGMVGTSLSLLIRAELGQPGALMGDDQIYNVVVTAHAFVMIFFMVMPIMLGGFGNWLVPlMIGAPD 91
Cdd:cd00919     1 HKDIGLLYLIFAFVALLLGGLLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473  92 MAFPRMNNMSFWLLPPSFLLLLASSMVEAGVGTGWTVYPPLAGNLAHAGCSVDLAIFSLHLAGVSSILGAINFITTIINM 171
Cdd:cd00919    80 LAFPRLNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNM 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 172 KPPAMSQYQTPLFVWSILITAVLLLLALPVLAAGITMLLTDRNINTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGF 251
Cdd:cd00919   160 RAPGMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAF 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 252 GIISHIVAYYSGKKePFGYMGMVWAMMSIGFLGFIVWAHHMFTVGLDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGH 331
Cdd:cd00919   240 GAISEIIPTFSGKP-LFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGR 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 332 INWAPALMWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLLTGYTLNDTWAK 411
Cdd:cd00919   319 IRFDPPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKLGK 398
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2513212473 412 IHFIIMFMGVNITFFPQHFLGLAGMPRRYSDYPDAYTTWNTVSSMGSFISLTAVMLMVFLIWEAF 476
Cdd:cd00919   399 IHFWLWFIGFNLTFFPMHFLGLLGMPRRYADYPDGFAPWNFISSVGAFILGLGLLLFLGNLFLSL 463
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
2-511 0e+00

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 568.60  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473   2 LISRWLFSTNHKDIGTLYLLFGAWAGMVGTSLSLLIRAELGQPGALMGDDQIYNVVVTAHAFVMIFFMVMPiMLGGFGNW 81
Cdd:COG0843     5 GWRRWLTTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNY 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473  82 LVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGVGTGWTVYPPLAGNLAHAGCSVDLAIFSLHLAGVSSILGA 161
Cdd:COG0843    84 LVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGG 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 162 INFITTIINMKPPAMSQYQTPLFVWSILITAVLLLLALPVLAAGITMLLTDRNINTTFFDPAGGGDPILYQHLFWFFGHP 241
Cdd:COG0843   164 VNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHP 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 242 EVYILILPGFGIISHIVAYYSGKKePFGYMGMVWAMMSIGFLGFIVWAHHMFTVGLDVDTRAYFTSATMIIAIPTGVKVF 321
Cdd:COG0843   244 EVYILILPAFGIVSEIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVF 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 322 SWLATLHGGHINWAPALMWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLLT 401
Cdd:COG0843   323 NWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMT 402
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 402 GYTLNDTWAKIHFIIMFMGVNITFFPQHFLGLAGMPRRYSDYP--DAYTTWNTVSSMGSFISLTAVMLMVFLIWEAFAAK 479
Cdd:COG0843   403 GRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAFILAVGFLLFLINLVVSLRKG 482
                         490       500       510
                  ....*....|....*....|....*....|..
gi 2513212473 480 REVLKIEFTNTNIEWLHGCPPPYHTFEEPTYI 511
Cdd:COG0843   483 PKAGGNPWGARTLEWATPSPPPLYNFASIPVV 514
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
7-505 0e+00

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: 564.54  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473   7 LFSTNHKDIGTLYLLFGAWAGMVGTSLSLLIRAELGQPGALMGDDQIYNVVVTAHAFVMIFFMVMPiMLGGFGNWLVPLM 86
Cdd:TIGR02891   1 LTTVDHKRIGILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIP-ILAGFGNYLLPLM 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473  87 IGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGVGTGWTVYPPLAGNLAHAGCSVDLAIFSLHLAGVSSILGAINFIT 166
Cdd:TIGR02891  80 IGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 167 TIINMKPPAMSQYQTPLFVWSILITAVLLLLALPVLAAGITMLLTDRNINTTFFDPAGGGDPILYQHLFWFFGHPEVYIL 246
Cdd:TIGR02891 160 TILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYII 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 247 ILPGFGIISHIVAYYSGKKePFGYMGMVWAMMSIGFLGFIVWAHHMFTVGLDVDTRAYFTSATMIIAIPTGVKVFSWLAT 326
Cdd:TIGR02891 240 FLPAFGIISEILPTFARKP-IFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIAT 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 327 LHGGHINWAPALMWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLLTGYTLN 406
Cdd:TIGR02891 319 LWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYN 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 407 DTWAKIHFIIMFMGVNITFFPQHFLGLAGMPRRYSDYPDA--YTTWNTVSSMGSFISLTAVMLMVFLIWEAFAAKREVLK 484
Cdd:TIGR02891 399 ERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGPKAGA 478
                         490       500
                  ....*....|....*....|.
gi 2513212473 485 IEFTNTNIEWLHGCPPPYHTF 505
Cdd:TIGR02891 479 NPWGATTLEWTTSSPPPAHNF 499
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
6-504 1.10e-176

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 506.91  E-value: 1.10e-176
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473   6 WLFSTNHKDIGTLYLLFGAWAGMVGTSLSLLIRAELGQPGALMGDDQIYNVVVTAHAFVMIFFMVMPIMLGGFGNWLVPL 85
Cdd:MTH00048    7 WLFTLDHKRIGVIYTLLGVWSGFVGLSLSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473  86 MIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVeaGVGTGWTVYPPLAGNLAHAGCSVDLAIFSLHLAGVSSILGAINFI 165
Cdd:MTH00048   87 LLGLSDLNLPRLNALSAWLLVPSIVFLLLSMCL--GAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFI 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 166 TTIINMKPPAMSqYQTPLFVWSILITAVLLLLALPVLAAGITMLLTDRNINTTFFDPAGGGDPILYQHLFWFFGHPEVYI 245
Cdd:MTH00048  165 CTIYSAFMTNVF-SRTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPEVYV 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 246 LILPGFGIISHIVAYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGLDVDTRAYFTSATMIIAIPTGVKVFSWLA 325
Cdd:MTH00048  244 LILPGFGIISHICLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFSWLY 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 326 TLHGGHIN-WAPALMWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLLTGYT 404
Cdd:MTH00048  324 MLLNSRVRkSDPVVWWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWPLITGLS 403
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 405 LNDTWAKIHFIIMFMGVNITFFPQHFLGLAGMPRRYSDYPDAYTTWNTVSSMGSFISLTAVMLMVFLIWEAFAAKREVLK 484
Cdd:MTH00048  404 LNKYLLQCHCIISMIGFNLCFFPMHYFGLCGLPRRVCVYEPSYYWINVVCTVGSFISAFSGCFFVFILWESLVVKNEVLG 483
                         490       500
                  ....*....|....*....|
gi 2513212473 485 IEFTNTNIEWLHGCPPPYHT 504
Cdd:MTH00048  484 LWGSSSCVVNVLMSPVPYHN 503
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
6-505 2.34e-173

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: 497.87  E-value: 2.34e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473   6 WLFSTNHKDIGTLYLLFGAWAGMVGTSLSLLIRAELGQPGALMGDDQIYNVVVTAHAFVMIFFMVMPIMLGgFGNWLVPL 85
Cdd:cd01662     1 WLTTVDHKRIGIMYIITAFVFFLRGGVDALLMRTQLALPGNDFLSPEHYNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473  86 MIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGVGTGWTVYPPLAGNLAHAGCSVDLAIFSLHLAGVSSILGAINFI 165
Cdd:cd01662    80 QIGARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFI 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 166 TTIINMKPPAMSQYQTPLFVWSILITAVLLLLALPVLAAGITMLLTDRNINTTFFDPAGGGDPILYQHLFWFFGHPEVYI 245
Cdd:cd01662   160 VTILKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYI 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 246 LILPGFGIISHIVAYYSGKKePFGYMGMVWAMMSIGFLGFIVWAHHMFTVGLDVDTRAYFTSATMIIAIPTGVKVFSWLA 325
Cdd:cd01662   240 LILPAFGIFSEIVPTFSRKP-LFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLF 318
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 326 TLHGGHINWAPALMWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLLTGYTL 405
Cdd:cd01662   319 TMWRGRIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRML 398
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 406 NDTWAKIHFIIMFMGVNITFFPQHFLGLAGMPRRYSDYP--DAYTTWNTVSSMGSFISLTAVMLMVF-LIWEAFAAKREV 482
Cdd:cd01662   399 NERLGKWSFWLWFIGFNLTFFPMHILGLMGMPRRVYTYLpgPGWDPLNLISTIGAFLIAAGVLLFLInVIVSIRKGKRDA 478
                         490       500
                  ....*....|....*....|...
gi 2513212473 483 LKIEFTNTNIEWLHGCPPPYHTF 505
Cdd:cd01662   479 TGDPWGARTLEWATSSPPPAYNF 501
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
14-460 1.58e-131

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: 388.85  E-value: 1.58e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473  14 DIGTLYLLFGAWAGMVGTSLSLLIRAELGQPGALMGDDQIYNVVVTAHAFVMIFFMVMPIMlGGFGNWLVPLMIGAPDMA 93
Cdd:pfam00115   1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATPFL-FGFGNYLVPLMIGARDMA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473  94 FPRMNNMSFWLLPPSFLLLLASSMveaGVGTGWTVYPPLAGnlahagcsVDLAIFSLHLAGVSSILGAINFITTIINMKP 173
Cdd:pfam00115  80 FPRLNALSFWLVVLGAVLLLASFG---GATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRA 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 174 PAMSQyQTPLFVWSILITAVLLLLALPVLAAGITMLLTDRNINttffdpAGGGDPILYQHLFWFFGHPEVYILILPGFGI 253
Cdd:pfam00115 149 PGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGI 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 254 ISHIVAYYSGKKePFGYMGMVWAMMSIGFLGFIVWAHHMFTVGLDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGHIN 333
Cdd:pfam00115 222 IYYILPKFAGRP-LFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIR 300
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 334 WA-PALMWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLLTGYTLNDTWAKI 412
Cdd:pfam00115 301 FRtTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKL 380
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2513212473 413 HFIIMFMGVNITFFPQHFLGLAGMPRRYS----DYPDAYTTWNTVSSMGSFI 460
Cdd:pfam00115 381 HFWLLFIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPLNWIRTIGGVL 432
CyoB TIGR02843
cytochrome o ubiquinol oxidase, subunit I; Cytochrome o terminal oxidase complex is the ...
2-507 1.29e-121

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: 370.54  E-value: 1.29e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473   2 LISRWLFSTNHKDIGTLYLLFGAWAGMVGTSLSLLIRAEL-----GQPGALMGD--DQIYnvvvTAHAFVMIFFMVMPIM 74
Cdd:TIGR02843  43 LWNEWLTTVDHKKIGIMYIIVALVMLLRGFADAIMMRTQQalasgGSAGYLPPHhyDQIF----TAHGVIMIFFVAMPFV 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473  75 LGGFgNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGVGTGWTVYPPLAGNLAHAGCSVDLAIFSLHLAG 154
Cdd:TIGR02843 119 FGLM-NLVVPLQIGARDVAFPFLNSLSFWLTVVGAILVNVSLGVGEFAQTGWLAYPPLSELQYSPGVGVDYYIWALQISG 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 155 VSSILGAINFITTIINMKPPAMSQYQTPLFVWSILITAVLLLLALPVLAAGITMLLTDRNINTTFFDPAGGGDPILYQHL 234
Cdd:TIGR02843 198 IGTLLTGINFFVTIIKMRAPGMTLMKMPVFTWTSLCSNVLIIASFPILTVTLALLTLDRYLGMHFFTNEAGGNPMMYVNL 277
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 235 FWFFGHPEVYILILPGFGIISHIVAYYSGKKEpFGYMGMVWAMMSIGFLGFIVWAHHMFTVGLDVDTRAYFTSATMIIAI 314
Cdd:TIGR02843 278 IWAWGHPEVYILILPAFGIFSEVVATFSRKRL-FGYTSMVWATIAITVLSFIVWLHHFFTMGAGANVNAFFGIATMIIAI 356
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 315 PTGVKVFSWLATLHGGHINWAPALMWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFI 394
Cdd:TIGR02843 357 PTGVKIFNWLFTMYKGRIRFETPMLWTIGFMVTFSIGGMTGVLLAVPPADFVLHNSLFLIAHFHNVIIGGVVFGCFAGLT 436
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 395 HWFPLLTGYTLNDTWAKIHFIIMFMGVNITFFPQHFLGLAGMPRRYSDYPD-AYTTWNTVSSMGSFISLTAVMLMVFLIW 473
Cdd:TIGR02843 437 YWFPKAFGFKLNEKLGKRSFWCWFIGFYLAFMPLYILGFMGMTRRLNHYDNpEWHPMLIIAAFGAFLIACGILCQIIQIF 516
                         490       500       510
                  ....*....|....*....|....*....|....*..
gi 2513212473 474 EAFAAK---REVLKIEFTNTNIEWLHGCPPPYHTFEE 507
Cdd:TIGR02843 517 VSIRDRdqnRDTTGDPWGGRTLEWSTSSPPPFYNFAV 553
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
2-505 1.16e-116

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


Pssm-ID: 131928  Cd Length: 643  Bit Score: 358.01  E-value: 1.16e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473   2 LISRWLFSTNHKDIGTLYLLFGAWAGMVGTSLSLLIRAELGQPGALMGDDQIYNVVVTAHAFVMIFFMVMPIMLGgFGNW 81
Cdd:TIGR02882  40 LWNEWLTTVDHKKIGVMYIICAVLMLFRGGIDALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNI 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473  82 LVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGVGTGWTVYPPLAGNLAHAGCSVDLAIFSLHLAGVSSILGA 161
Cdd:TIGR02882 119 VVPLQIGARDVAFPVLNALSFWLFFAGAMLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTG 198
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 162 INFITTIINMKPPAMSQYQTPLFVWSILITAVLLLLALPVLAAGITMLLTDRNINTTFFDPAGGGDPILYQHLFWFFGHP 241
Cdd:TIGR02882 199 INFFVTILKMRAPGMKLMQMPMFTWTTLITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLFWIWGHP 278
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 242 EVYILILPGFGIISHIVAYYSgKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGLDVDTRAYFTSATMIIAIPTGVKVF 321
Cdd:TIGR02882 279 EVYIVILPAFGIYSEIISTFA-QKRLFGYKSMVWSTVGIAFLSFLVWVHHFFTMGNGALINSFFSITTMAIAIPTGVKIF 357
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 322 SWLATLHGGHINWAPALMWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLLT 401
Cdd:TIGR02882 358 NWLLTLYKGKIRFTTPMLFSLAFIPNFLIGGVTGVMLAMASADYQYHNTYFLVAHFHYVLITGVVFACLAGLIYWYPKMF 437
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 402 GYTLNDTWAKIHFIIMFMGVNITFFPQHFLGLAGMPRRYSDY--PDAYTTWNTVSSMGS-FISLTAVMLMVFLIWEAFAA 478
Cdd:TIGR02882 438 GYKLNERLGKWCFWFFMIGFNVCFFPMYILGLDGMPRRMYTYspSDGWFPLNLISTIGAlLMAIGFIFLVYNIYYSHRKS 517
                         490       500
                  ....*....|....*....|....*..
gi 2513212473 479 KREVLKIEFTNTNIEWLHGCPPPYHTF 505
Cdd:TIGR02882 518 PREATGDPWNGRTLEWATASPPPKYNF 544
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
2-505 2.00e-109

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 339.60  E-value: 2.00e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473   2 LISRWLFSTNHKDIGTLYLLFGAWAGMVGTSLSLLIR-----AELGQPGALmgDDQIYNVVVTAHAFVMIFFMVMPIMLG 76
Cdd:PRK15017   44 LWKEWLTSVDHKRLGIMYIIVAIVMLLRGFADAIMMRsqqalASAGEAGFL--PPHHYDQIFTAHGVIMIFFVAMPFVIG 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473  77 gFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGVGTGWTVYPPLAGNLAHAGCSVDLAIFSLHLAGVS 156
Cdd:PRK15017  122 -LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIG 200
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 157 SILGAINFITTIINMKPPAMSQYQTPLFVWSILITAVLLLLALPVLAAGITMLLTDRNINTTFFDPAGGGDPILYQHLFW 236
Cdd:PRK15017  201 TTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIW 280
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 237 FFGHPEVYILILPGFGIISHIVAYYSgKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGLDVDTRAYFTSATMIIAIPT 316
Cdd:PRK15017  281 AWGHPEVYILILPVFGVFSEIAATFS-RKRLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPT 359
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 317 GVKVFSWLATLHGGHINWAPALMWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFIHW 396
Cdd:PRK15017  360 GVKIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYW 439
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 397 FPLLTGYTLNDTWAKIHFIIMFMGVNITFFPQHFLGLAGMPRRYSDYPD-AYTTWNTVSSMGSFISLTAVMLMVFLIWEA 475
Cdd:PRK15017  440 WPKAFGFKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMTRRLSQQIDpQFHTMLMIAASGAALIALGILCQVIQMYVS 519
                         490       500       510
                  ....*....|....*....|....*....|...
gi 2513212473 476 FAAK---REVLKIEFTNTNIEWLHGCPPPYHTF 505
Cdd:PRK15017  520 IRDRdqnRDLTGDPWGGRTLEWATSSPPPFYNF 552
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
227-472 6.90e-19

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: 89.27  E-value: 6.90e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 227 DPILYQHLFWFFGHPEVYILILPGFGIISHIVAYYSGKKEPFGYMGMVwAMMSIGFLGFIVWAHHMFT-VGLDVDTRAYF 305
Cdd:cd01660   200 DVLLSRTLFWWFGHPLVYFWLLPAYIAWYTILPKIAGGKLFSDPLARL-AFILFLLFSTPVGFHHQFAdPGIGPGWKFIH 278
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 306 TSATMIIAIPTGVKVFSWLATL--------HGGHINWAPALMW--------ALGFIFlFTVGGLTGIVLANSSLDIVLHD 369
Cdd:cd01660   279 MVLTFMVALPSLLTAFTVFASLeiagrlrgGKGLFGWIRALPWgdpmflalFLAMLM-FIPGGAGGIINASYQLNYVVHN 357
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2513212473 370 TYYVVAHFHyvLSMGAVFAIMG-GFIHWF-PLLTGYTLNDTW-AKIHFIIMFMGVNITFFPQHFLGLAGMPRR--YSDYP 444
Cdd:cd01660   358 TAWVPGHFH--LTVGGAVALTFmAVAYWLvPHLTGRELAAKRlALAQPWLWFVGMTIMSTAMHVAGLLGAPRRtaEAQYG 435
                         250       260       270
                  ....*....|....*....|....*....|...
gi 2513212473 445 DAY-----TTWNTVSSMGSFISLTAVMLMVFLI 472
Cdd:cd01660   436 GLPaagewAPYQQLMAIGGTILFVSGALFLYIL 468
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH