NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2172617464|ref|YP_010238770|]
View 

cytochrome c oxidase subunit I (mitochondrion) [Telenomus remus]

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
 6-510 0e+00

cytochrome c oxidase subunit I; Provisional


:

Pssm-ID: 177210  Cd Length: 511  Bit Score: 827.20  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464   6 MKWMLSTNHKDIGTLYFYFGVWAGMLGSAMSALIRMELSVPGMLIGNDQIYNSIVTSHAFIMIFFMVMPIMLGGFGNWLV 85
Cdd:MTH00153    2 NKWLFSTNHKDIGTLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464  86 PLMINAPDMAFPRLNNMSFWLLIPSLILLIYSNIFGSGTGTGWTVYPPLSSQL---NPSIDLTIFSLHIAGISSILSSIN 162
Cdd:MTH00153   82 PLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIahsGASVDLAIFSLHLAGISSILGAIN 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 163 FLCTIINMSNTSMN--NWTLFTWSVLITTILLLLSLPVLAGAITMILTDRNLNTAFFNPAGGGDPILYQHLFWFFGHPEV 240
Cdd:MTH00153  162 FITTIINMRSKGMTldRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEV 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 241 YILILPGFGLISHMICLESGKKETFGMLGMIYAMISIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMVIAIPTGIKVFSW 320
Cdd:MTH00153  242 YILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSW 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 321 MATINGMKIKLTPSMLWILGFIFLFTIGGLTGIILSNSSIDIILHDTYYVVAHFHYVLSMGAVFSIIGAFITWFPLLTGC 400
Cdd:MTH00153  322 LATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGL 401

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 401 TMNNFSLKIQFLTMFVGVNMTFFPQHFLGLSGMPRRYSDYPDFYLMWNKISSLGSMISIISIIHLMTIIVSSMKNKNLMI 480
Cdd:MTH00153  402 TMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPVL 481

                         490       500       510
                  ....*....|....*....|....*....|
gi 2172617464 481 NFYYKNSASEWTHSFPPMNHAFNESSILTK 510
Cdd:MTH00153  482 FSLNLSSSIEWLQNLPPAEHSYSELPLLTN 511
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 6-510 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 827.20  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464   6 MKWMLSTNHKDIGTLYFYFGVWAGMLGSAMSALIRMELSVPGMLIGNDQIYNSIVTSHAFIMIFFMVMPIMLGGFGNWLV 85
Cdd:MTH00153    2 NKWLFSTNHKDIGTLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464  86 PLMINAPDMAFPRLNNMSFWLLIPSLILLIYSNIFGSGTGTGWTVYPPLSSQL---NPSIDLTIFSLHIAGISSILSSIN 162
Cdd:MTH00153   82 PLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIahsGASVDLAIFSLHLAGISSILGAIN 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 163 FLCTIINMSNTSMN--NWTLFTWSVLITTILLLLSLPVLAGAITMILTDRNLNTAFFNPAGGGDPILYQHLFWFFGHPEV 240
Cdd:MTH00153  162 FITTIINMRSKGMTldRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEV 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 241 YILILPGFGLISHMICLESGKKETFGMLGMIYAMISIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMVIAIPTGIKVFSW 320
Cdd:MTH00153  242 YILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSW 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 321 MATINGMKIKLTPSMLWILGFIFLFTIGGLTGIILSNSSIDIILHDTYYVVAHFHYVLSMGAVFSIIGAFITWFPLLTGC 400
Cdd:MTH00153  322 LATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGL 401

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 401 TMNNFSLKIQFLTMFVGVNMTFFPQHFLGLSGMPRRYSDYPDFYLMWNKISSLGSMISIISIIHLMTIIVSSMKNKNLMI 480
Cdd:MTH00153  402 TMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPVL 481

                         490       500       510
                  ....*....|....*....|....*....|
gi 2172617464 481 NFYYKNSASEWTHSFPPMNHAFNESSILTK 510
Cdd:MTH00153  482 FSLNLSSSIEWLQNLPPAEHSYSELPLLTN 511
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 12-493 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: 747.77  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464  12 TNHKDIGTLYFYFGVWAGMLGSAMSALIRMELSVPGMLIGNDQIYNSIVTSHAFIMIFFMVMPIMLGGFGNWLVPLMINA 91
Cdd:cd01663     1 TNHKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464  92 PDMAFPRLNNMSFWLLIPSLILLIYSNIFGSGTGTGWTVYPPLSSQL---NPSIDLTIFSLHIAGISSILSSINFLCTII 168
Cdd:cd01663    81 PDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILahsGPSVDLAIFSLHLAGISSILGAINFITTIF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 169 NMSNTSMN--NWTLFTWSVLITTILLLLSLPVLAGAITMILTDRNLNTAFFNPAGGGDPILYQHLFWFFGHPEVYILILP 246
Cdd:cd01663   161 NMRAPGMTleKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILP 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 247 GFGLISHMICLESGKKETFGMLGMIYAMISIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMVIAIPTGIKVFSWMATING 326
Cdd:cd01663   241 GFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWG 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 327 MKIKLTPSMLWILGFIFLFTIGGLTGIILSNSSIDIILHDTYYVVAHFHYVLSMGAVFSIIGAFITWFPLLTGCTMNNFS 406
Cdd:cd01663   321 GSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETL 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 407 LKIQFLTMFVGVNMTFFPQHFLGLSGMPRRYSDYPDFYLMWNKISSLGSMISIISIIHLMTIIVSSMKNKNLMINFYYKN 486
Cdd:cd01663   401 GKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFNVGEG 480


                  ....*...
gi 2172617464 487 SAS-EWTH 493
Cdd:cd01663   481 STSlEWTL 488
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 11-442 1.55e-166

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: 480.57  E-value: 1.55e-166
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464  11 STNHKDIGTLYFYFGVWAGMLGSAMSALIRMELSVPGMLIGNDQIYNSIVTSHAFIMIFFMVMPiMLGGFGNWLVPLMIN 90
Cdd:TIGR02891   3 TVDHKRIGILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIP-ILAGFGNYLLPLMIG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464  91 APDMAFPRLNNMSFWLLIPSLILLIYSNIFGSGTGTGWTVYPPLSSQL---NPSIDLTIFSLHIAGISSILSSINFLCTI 167
Cdd:TIGR02891  82 ARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSgspGVGVDLWLLGLHLLGISSILGAVNFIVTI 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 168 INM--SNTSMNNWTLFTWSVLITTILLLLSLPVLAGAITMILTDRNLNTAFFNPAGGGDPILYQHLFWFFGHPEVYILIL 245
Cdd:TIGR02891 162 LNMraPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFL 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 246 PGFGLISHMICLESGKKeTFGMLGMIYAMISIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMVIAIPTGIKVFSWMATIN 325
Cdd:TIGR02891 242 PAFGIISEILPTFARKP-IFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLW 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 326 GMKIKLTPSMLWILGFIFLFTIGGLTGIILSNSSIDIILHDTYYVVAHFHYVLSMGAVFSIIGAFITWFPLLTGCTMNNF 405
Cdd:TIGR02891 321 GGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNER 400

                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 2172617464 406 SLKIQFLTMFVGVNMTFFPQHFLGLSGMPRRYSDYPD 442
Cdd:TIGR02891 401 LGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPP 437
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
5-442 7.85e-166

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 480.01  E-value: 7.85e-166
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464   5 FMKWMLSTNHKDIGTLYFYFGVWAGMLGSAMSALIRMELSVPGMLIGNDQIYNSIVTSHAFIMIFFMVMPiMLGGFGNWL 84
Cdd:COG0843     6 WRRWLTTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464  85 VPLMINAPDMAFPRLNNMSFWLLIPSLILLIYSNIFGSGTGTGWTVYPPLSSQL---NPSIDLTIFSLHIAGISSILSSI 161
Cdd:COG0843    85 VPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEaspGVGVDLWLLGLALFGVGSILGGV 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 162 NFLCTIINM--SNTSMNNWTLFTWSVLITTILLLLSLPVLAGAITMILTDRNLNTAFFNPAGGGDPILYQHLFWFFGHPE 239
Cdd:COG0843   165 NFIVTILKMraPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPE 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 240 VYILILPGFGLISHMICLESGKKeTFGMLGMIYAMISIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMVIAIPTGIKVFS 319
Cdd:COG0843   245 VYILILPAFGIVSEIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFN 323

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 320 WMATINGMKIKLTPSMLWILGFIFLFTIGGLTGIILSNSSIDIILHDTYYVVAHFHYVLSMGAVFSIIGAFITWFPLLTG 399
Cdd:COG0843   324 WIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTG 403

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 2172617464 400 CTMNNFSLKIQFLTMFVGVNMTFFPQHFLGLSGMPRRYSDYPD 442
Cdd:COG0843   404 RMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPP 446
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 16-439 6.29e-116

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: 348.79  E-value: 6.29e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464  16 DIGTLYFYFGVWAGMLGSAMSALIRMELSVPGMLIGNDQIYNSIVTSHAFIMIFFMVMPIMlGGFGNWLVPLMINAPDMA 95
Cdd:pfam00115   1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATPFL-FGFGNYLVPLMIGARDMA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464  96 FPRLNNMSFWLLIPSLILLIYSniFGSGTgTGWTVYPPLssqlnPSIDLTIFSLHIAGISSILSSINFLCTIINMSNTSM 175
Cdd:pfam00115  80 FPRLNALSFWLVVLGAVLLLAS--FGGAT-TGWTEYPPL-----VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGM 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 176 N-NWTLFTWSVLITTILLLLSLPVLAGAITMILTDRNLNtaffnpAGGGDPILYQHLFWFFGHPEVYILILPGFGLISHM 254
Cdd:pfam00115 152 TlRMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYI 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 255 ICLESGKKeTFGMLGMIYAMISIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMVIAIPTGIKVFSWMATINGMKIKL-TP 333
Cdd:pfam00115 226 LPKFAGRP-LFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFrTT 304

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 334 SMLWILGFIFLFTIGGLTGIILSNSSIDIILHDTYYVVAHFHYVLSMGAVFSIIGAFITWFPLLTGCTMNNFSLKIQFLT 413
Cdd:pfam00115 305 PMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFWL 384

                         410       420
                  ....*....|....*....|....*.
gi 2172617464 414 MFVGVNMTFFPQHFLGLSGMPRRYSD 439
Cdd:pfam00115 385 LFIGFNLTFFPMHILGLLGMPRRYAP 410
 
Name Accession Description Interval E-value
COX1 MTH00153
cytochrome c oxidase subunit I; Provisional
 6-510 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177210  Cd Length: 511  Bit Score: 827.20  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464   6 MKWMLSTNHKDIGTLYFYFGVWAGMLGSAMSALIRMELSVPGMLIGNDQIYNSIVTSHAFIMIFFMVMPIMLGGFGNWLV 85
Cdd:MTH00153    2 NKWLFSTNHKDIGTLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464  86 PLMINAPDMAFPRLNNMSFWLLIPSLILLIYSNIFGSGTGTGWTVYPPLSSQL---NPSIDLTIFSLHIAGISSILSSIN 162
Cdd:MTH00153   82 PLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIahsGASVDLAIFSLHLAGISSILGAIN 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 163 FLCTIINMSNTSMN--NWTLFTWSVLITTILLLLSLPVLAGAITMILTDRNLNTAFFNPAGGGDPILYQHLFWFFGHPEV 240
Cdd:MTH00153  162 FITTIINMRSKGMTldRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEV 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 241 YILILPGFGLISHMICLESGKKETFGMLGMIYAMISIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMVIAIPTGIKVFSW 320
Cdd:MTH00153  242 YILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSW 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 321 MATINGMKIKLTPSMLWILGFIFLFTIGGLTGIILSNSSIDIILHDTYYVVAHFHYVLSMGAVFSIIGAFITWFPLLTGC 400
Cdd:MTH00153  322 LATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGL 401

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 401 TMNNFSLKIQFLTMFVGVNMTFFPQHFLGLSGMPRRYSDYPDFYLMWNKISSLGSMISIISIIHLMTIIVSSMKNKNLMI 480
Cdd:MTH00153  402 TMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPVL 481

                         490       500       510
                  ....*....|....*....|....*....|
gi 2172617464 481 NFYYKNSASEWTHSFPPMNHAFNESSILTK 510
Cdd:MTH00153  482 FSLNLSSSIEWLQNLPPAEHSYSELPLLTN 511
Cyt_c_Oxidase_I cd01663
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ...
 12-493 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: 747.77  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464  12 TNHKDIGTLYFYFGVWAGMLGSAMSALIRMELSVPGMLIGNDQIYNSIVTSHAFIMIFFMVMPIMLGGFGNWLVPLMINA 91
Cdd:cd01663     1 TNHKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464  92 PDMAFPRLNNMSFWLLIPSLILLIYSNIFGSGTGTGWTVYPPLSSQL---NPSIDLTIFSLHIAGISSILSSINFLCTII 168
Cdd:cd01663    81 PDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILahsGPSVDLAIFSLHLAGISSILGAINFITTIF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 169 NMSNTSMN--NWTLFTWSVLITTILLLLSLPVLAGAITMILTDRNLNTAFFNPAGGGDPILYQHLFWFFGHPEVYILILP 246
Cdd:cd01663   161 NMRAPGMTleKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILP 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 247 GFGLISHMICLESGKKETFGMLGMIYAMISIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMVIAIPTGIKVFSWMATING 326
Cdd:cd01663   241 GFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWG 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 327 MKIKLTPSMLWILGFIFLFTIGGLTGIILSNSSIDIILHDTYYVVAHFHYVLSMGAVFSIIGAFITWFPLLTGCTMNNFS 406
Cdd:cd01663   321 GSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETL 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 407 LKIQFLTMFVGVNMTFFPQHFLGLSGMPRRYSDYPDFYLMWNKISSLGSMISIISIIHLMTIIVSSMKNKNLMINFYYKN 486
Cdd:cd01663   401 GKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFNVGEG 480


                  ....*...
gi 2172617464 487 SAS-EWTH 493
Cdd:cd01663   481 STSlEWTL 488
COX1 MTH00167
cytochrome c oxidase subunit I; Provisional
 5-508 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177222  Cd Length: 512  Bit Score: 736.87  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464   5 FMKWMLSTNHKDIGTLYFYFGVWAGMLGSAMSALIRMELSVPGMLIGNDQIYNSIVTSHAFIMIFFMVMPIMLGGFGNWL 84
Cdd:MTH00167    3 INRWLFSTNHKDIGTLYFIFGAWAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464  85 VPLMINAPDMAFPRLNNMSFWLLIPSLILLIYSNIFGSGTGTGWTVYPPLSSQL---NPSIDLTIFSLHIAGISSILSSI 161
Cdd:MTH00167   83 VPLMIGAPDMAFPRMNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLahaGASVDLAIFSLHLAGVSSILGSI 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 162 NFLCTIINMSNT--SMNNWTLFTWSVLITTILLLLSLPVLAGAITMILTDRNLNTAFFNPAGGGDPILYQHLFWFFGHPE 239
Cdd:MTH00167  163 NFITTIINMKPPgiTQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPE 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 240 VYILILPGFGLISHMICLESGKKETFGMLGMIYAMISIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMVIAIPTGIKVFS 319
Cdd:MTH00167  243 VYILILPGFGMISHIVVYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFS 322

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 320 WMATINGMKIKLTPSMLWILGFIFLFTIGGLTGIILSNSSIDIILHDTYYVVAHFHYVLSMGAVFSIIGAFITWFPLLTG 399
Cdd:MTH00167  323 WLATLHGGKIKWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTG 402

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 400 CTMNNFSLKIQFLTMFVGVNMTFFPQHFLGLSGMPRRYSDYPDFYLMWNKISSLGSMISIISIIHLMTIIVSSMKNKNLM 479
Cdd:MTH00167  403 LTLNETWTKIHFFVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNVVSSIGSLISLVAVILFLFIIWEAFSSKRKL 482

                         490       500
                  ....*....|....*....|....*....
gi 2172617464 480 INFYYKNSASEWTHSFPPMNHAFNESSIL 508
Cdd:MTH00167  483 LPVELTSTNVEWLHGCPPPHHTWEEPPFV 511
COX1 MTH00116
cytochrome c oxidase subunit I; Provisional
 4-504 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177177  Cd Length: 515  Bit Score: 720.72  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464   4 NFMKWMLSTNHKDIGTLYFYFGVWAGMLGSAMSALIRMELSVPGMLIGNDQIYNSIVTSHAFIMIFFMVMPIMLGGFGNW 83
Cdd:MTH00116    2 FITRWLFSTNHKDIGTLYLIFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNW 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464  84 LVPLMINAPDMAFPRLNNMSFWLLIPSLILLIYSNIFGSGTGTGWTVYPPLSSQL---NPSIDLTIFSLHIAGISSILSS 160
Cdd:MTH00116   82 LVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLahaGASVDLAIFSLHLAGVSSILGA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 161 INFLCTIINMSNTSMN--NWTLFTWSVLITTILLLLSLPVLAGAITMILTDRNLNTAFFNPAGGGDPILYQHLFWFFGHP 238
Cdd:MTH00116  162 INFITTCINMKPPAMSqyQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHP 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 239 EVYILILPGFGLISHMICLESGKKETFGMLGMIYAMISIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMVIAIPTGIKVF 318
Cdd:MTH00116  242 EVYILILPGFGIISHIVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVF 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 319 SWMATINGMKIKLTPSMLWILGFIFLFTIGGLTGIILSNSSIDIILHDTYYVVAHFHYVLSMGAVFSIIGAFITWFPLLT 398
Cdd:MTH00116  322 SWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFT 401

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 399 GCTMNNFSLKIQFLTMFVGVNMTFFPQHFLGLSGMPRRYSDYPDFYLMWNKISSLGSMISIISIIHLMTIIVSSMKNKNL 478
Cdd:MTH00116  402 GYTLHQTWTKAQFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTISSIGSLISMTAVIMLMFIIWEAFSSKRK 481

                         490       500
                  ....*....|....*....|....*.
gi 2172617464 479 MINFYYKNSASEWTHSFPPMNHAFNE 504
Cdd:MTH00116  482 VLQPELTTTNIEWIHGCPPPYHTFEE 507
COX1 MTH00223
cytochrome c oxidase subunit I; Provisional
 6-510 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177260  Cd Length: 512  Bit Score: 706.36  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464   6 MKWMLSTNHKDIGTLYFYFGVWAGMLGSAMSALIRMELSVPGMLIGNDQIYNSIVTSHAFIMIFFMVMPIMLGGFGNWLV 85
Cdd:MTH00223    1 MRWLFSTNHKDIGTLYLIFGMWSGLVGTSLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464  86 PLMINAPDMAFPRLNNMSFWLLIPSLILLIYSNIFGSGTGTGWTVYPPLSSQL---NPSIDLTIFSLHIAGISSILSSIN 162
Cdd:MTH00223   81 PLMLGAPDMAFPRLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLahaGPSVDLAIFSLHLAGVSSILGAIN 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 163 FLCTIINMSNTSMN--NWTLFTWSVLITTILLLLSLPVLAGAITMILTDRNLNTAFFNPAGGGDPILYQHLFWFFGHPEV 240
Cdd:MTH00223  161 FITTIINMRSPGMQleRLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEV 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 241 YILILPGFGLISHMICLESGKKETFGMLGMIYAMISIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMVIAIPTGIKVFSW 320
Cdd:MTH00223  241 YILILPGFGMISHIVSHYSSKKEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSW 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 321 MATINGMKIKLTPSMLWILGFIFLFTIGGLTGIILSNSSIDIILHDTYYVVAHFHYVLSMGAVFSIIGAFITWFPLLTGC 400
Cdd:MTH00223  321 LATIYGSKIKYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLFTGV 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 401 TMNNFSLKIQFLTMFVGVNMTFFPQHFLGLSGMPRRYSDYPDFYLMWNKISSLGSMISIISIIHLMTIIVSSMKNKNLMI 480
Cdd:MTH00223  401 TLHRRWAKAHFFLMFLGVNLTFFPQHFLGLAGMPRRYSDYPDCYTKWNQVSSFGSMISFVSVLFFMFIVWEAFVSQRSVV 480

                         490       500       510
                  ....*....|....*....|....*....|
gi 2172617464 481 NFYYKNSASEWTHSFPPMNHAFNESSILTK 510
Cdd:MTH00223  481 WSGHLSTSLEWDNLLPADFHNNSETGALVI 510
COX1 MTH00142
cytochrome c oxidase subunit I; Provisional
 6-508 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214431  Cd Length: 511  Bit Score: 690.69  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464   6 MKWMLSTNHKDIGTLYFYFGVWAGMLGSAMSALIRMELSVPGMLIGNDQIYNSIVTSHAFIMIFFMVMPIMLGGFGNWLV 85
Cdd:MTH00142    2 MRWLFSTNHKDIGTLYFLFGAWAGMVGTGLSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464  86 PLMINAPDMAFPRLNNMSFWLLIPSLILLIYSNIFGSGTGTGWTVYPPLSSQL---NPSIDLTIFSLHIAGISSILSSIN 162
Cdd:MTH00142   82 PLMLGAPDMAFPRMNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLahsGGSVDLAIFSLHLAGVSSILGAIN 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 163 FLCTIINMSNTSMN--NWTLFTWSVLITTILLLLSLPVLAGAITMILTDRNLNTAFFNPAGGGDPILYQHLFWFFGHPEV 240
Cdd:MTH00142  162 FITTVINMRAGGMKfeRVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEV 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 241 YILILPGFGLISHMICLESGKKETFGMLGMIYAMISIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMVIAIPTGIKVFSW 320
Cdd:MTH00142  242 YILILPGFGMISHIINHYSGKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFSW 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 321 MATINGMKIKLTPSMLWILGFIFLFTIGGLTGIILSNSSIDIILHDTYYVVAHFHYVLSMGAVFSIIGAFITWFPLLTGC 400
Cdd:MTH00142  322 LATLHGSKVKYEPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLFTGL 401

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 401 TMNNFSLKIQFLTMFVGVNMTFFPQHFLGLSGMPRRYSDYPDFYLMWNKISSLGSMISIISIIHLMTIIVSSMKNKNLMI 480
Cdd:MTH00142  402 TLNPRWLKAHFYTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSSLGSMISFIAVLMFVFIVWESFVSQRLVM 481

                         490       500
                  ....*....|....*....|....*...
gi 2172617464 481 NFYYKNSASEWTHSFPPMNHAFNESSIL 508
Cdd:MTH00142  482 WSSHLSTSLEWSHRLPPDFHTYDELPIL 509
COX1 MTH00103
cytochrome c oxidase subunit I; Validated
 7-506 0e+00

cytochrome c oxidase subunit I; Validated


Pssm-ID: 177165  Cd Length: 513  Bit Score: 643.86  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464   7 KWMLSTNHKDIGTLYFYFGVWAGMLGSAMSALIRMELSVPGMLIGNDQIYNSIVTSHAFIMIFFMVMPIMLGGFGNWLVP 86
Cdd:MTH00103    5 RWLFSTNHKDIGTLYLLFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVP 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464  87 LMINAPDMAFPRLNNMSFWLLIPSLILLIYSNIFGSGTGTGWTVYPPLSSQL---NPSIDLTIFSLHIAGISSILSSINF 163
Cdd:MTH00103   85 LMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLahaGASVDLTIFSLHLAGVSSILGAINF 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 164 LCTIINMSNTSMNNWT--LFTWSVLITTILLLLSLPVLAGAITMILTDRNLNTAFFNPAGGGDPILYQHLFWFFGHPEVY 241
Cdd:MTH00103  165 ITTIINMKPPAMSQYQtpLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVY 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 242 ILILPGFGLISHMICLESGKKETFGMLGMIYAMISIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMVIAIPTGIKVFSWM 321
Cdd:MTH00103  245 ILILPGFGMISHIVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWL 324

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 322 ATINGMKIKLTPSMLWILGFIFLFTIGGLTGIILSNSSIDIILHDTYYVVAHFHYVLSMGAVFSIIGAFITWFPLLTGCT 401
Cdd:MTH00103  325 ATLHGGNIKWSPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYT 404

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 402 MNNFSLKIQFLTMFVGVNMTFFPQHFLGLSGMPRRYSDYPDFYLMWNKISSLGSMISIISIIHLMTIIVSSMKNKNLMIN 481
Cdd:MTH00103  405 LNDTWAKIHFTIMFVGVNMTFFPQHFLGLSGMPRRYSDYPDAYTTWNTVSSMGSFISLTAVMLMIFMIWEAFASKREVLT 484

                         490       500
                  ....*....|....*....|....*
gi 2172617464 482 FYYKNSASEWTHSFPPMNHAFNESS 506
Cdd:MTH00103  485 VELTTTNLEWLHGCPPPYHTFEEPT 509
COX1 MTH00077
cytochrome c oxidase subunit I; Provisional
 5-510 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214419  Cd Length: 514  Bit Score: 641.99  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464   5 FMKWMLSTNHKDIGTLYFYFGVWAGMLGSAMSALIRMELSVPGMLIGNDQIYNSIVTSHAFIMIFFMVMPIMLGGFGNWL 84
Cdd:MTH00077    3 ITRWLFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464  85 VPLMINAPDMAFPRLNNMSFWLLIPSLILLIYSNIFGSGTGTGWTVYPPLSSQL---NPSIDLTIFSLHIAGISSILSSI 161
Cdd:MTH00077   83 VPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLahaGASVDLTIFSLHLAGVSSILGAI 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 162 NFLCTIINMSNTSMNNWT--LFTWSVLITTILLLLSLPVLAGAITMILTDRNLNTAFFNPAGGGDPILYQHLFWFFGHPE 239
Cdd:MTH00077  163 NFITTSINMKPPSMSQYQtpLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPE 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 240 VYILILPGFGLISHMICLESGKKETFGMLGMIYAMISIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMVIAIPTGIKVFS 319
Cdd:MTH00077  243 VYILILPGFGMISHIVTYYSAKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVFS 322

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 320 WMATINGMKIKLTPSMLWILGFIFLFTIGGLTGIILSNSSIDIILHDTYYVVAHFHYVLSMGAVFSIIGAFITWFPLLTG 399
Cdd:MTH00077  323 WLATMHGGAIKWDAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSG 402

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 400 CTMNNFSLKIQFLTMFVGVNMTFFPQHFLGLSGMPRRYSDYPDFYLMWNKISSLGSMISIISIIHLMTIIVSSMKNKNLM 479
Cdd:MTH00077  403 YTLHSTWSKIHFGVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMMMFIIWEAFSSKREV 482

                         490       500       510
                  ....*....|....*....|....*....|.
gi 2172617464 480 INFYYKNSASEWTHSFPPMNHAFNESSILTK 510
Cdd:MTH00077  483 LTTELTSTNIEWLHGCPPPYHTFEEPSFVQT 513
COX1 MTH00183
cytochrome c oxidase subunit I; Provisional
 7-504 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177234  Cd Length: 516  Bit Score: 634.65  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464   7 KWMLSTNHKDIGTLYFYFGVWAGMLGSAMSALIRMELSVPGMLIGNDQIYNSIVTSHAFIMIFFMVMPIMLGGFGNWLVP 86
Cdd:MTH00183    5 RWFFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIP 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464  87 LMINAPDMAFPRLNNMSFWLLIPSLILLIYSNIFGSGTGTGWTVYPPLSSQL---NPSIDLTIFSLHIAGISSILSSINF 163
Cdd:MTH00183   85 LMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLahaGASVDLTIFSLHLAGVSSILGAINF 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 164 LCTIINMSNTSMNNWT--LFTWSVLITTILLLLSLPVLAGAITMILTDRNLNTAFFNPAGGGDPILYQHLFWFFGHPEVY 241
Cdd:MTH00183  165 ITTIINMKPPAISQYQtpLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVY 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 242 ILILPGFGLISHMICLESGKKETFGMLGMIYAMISIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMVIAIPTGIKVFSWM 321
Cdd:MTH00183  245 ILILPGFGMISHIVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWL 324

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 322 ATINGMKIKLTPSMLWILGFIFLFTIGGLTGIILSNSSIDIILHDTYYVVAHFHYVLSMGAVFSIIGAFITWFPLLTGCT 401
Cdd:MTH00183  325 ATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLFSGYT 404

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 402 MNNFSLKIQFLTMFVGVNMTFFPQHFLGLSGMPRRYSDYPDFYLMWNKISSLGSMISIISIIHLMTIIVSSMKNKNLMIN 481
Cdd:MTH00183  405 LHSTWTKIHFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMFLFILWEAFAAKREVLS 484

                         490       500
                  ....*....|....*....|...
gi 2172617464 482 FYYKNSASEWTHSFPPMNHAFNE 504
Cdd:MTH00183  485 VELTSTNVEWLHGCPPPYHTFEE 507
COX1 MTH00037
cytochrome c oxidase subunit I; Provisional
 4-507 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177112  Cd Length: 517  Bit Score: 632.64  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464   4 NFMKWMLSTNHKDIGTLYFYFGVWAGMLGSAMSALIRMELSVPGMLIGNDQIYNSIVTSHAFIMIFFMVMPIMLGGFGNW 83
Cdd:MTH00037    2 QLSRWLFSTNHKDIGTLYLIFGAWAGMVGTAMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNW 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464  84 LVPLMINAPDMAFPRLNNMSFWLLIPSLILLIYSNIFGSGTGTGWTVYPPLSSQL---NPSIDLTIFSLHIAGISSILSS 160
Cdd:MTH00037   82 LIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIahaGGSVDLAIFSLHLAGASSILAS 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 161 INFLCTIINMSN--TSMNNWTLFTWSVLITTILLLLSLPVLAGAITMILTDRNLNTAFFNPAGGGDPILYQHLFWFFGHP 238
Cdd:MTH00037  162 INFITTIINMRTpgMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHP 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 239 EVYILILPGFGLISHMICLESGKKETFGMLGMIYAMISIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMVIAIPTGIKVF 318
Cdd:MTH00037  242 EVYILILPGFGMISHVIAHYSGKQEPFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVF 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 319 SWMATINGMKIKLTPSMLWILGFIFLFTIGGLTGIILSNSSIDIILHDTYYVVAHFHYVLSMGAVFSIIGAFITWFPLLT 398
Cdd:MTH00037  322 SWMATLQGSNLRWETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLFS 401

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 399 GCTMNNFSLKIQFLTMFVGVNMTFFPQHFLGLSGMPRRYSDYPDFYLMWNKISSLGSMISIISIIHLMTIIVSSMKNKNL 478
Cdd:MTH00037  402 GVSLHPLWSKVHFFLMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSTISLVATLFFLFLIWEAFASQRE 481

                         490       500       510
                  ....*....|....*....|....*....|
gi 2172617464 479 MINFYYKNSASEWTH-SFPPMNHAFNESSI 507
Cdd:MTH00037  482 VISPEFSSSSLEWQYsSFPPSHHTFDETPS 511
COX1 MTH00007
cytochrome c oxidase subunit I; Validated
 6-509 0e+00

cytochrome c oxidase subunit I; Validated


Pssm-ID: 133649  Cd Length: 511  Bit Score: 631.17  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464   6 MKWMLSTNHKDIGTLYFYFGVWAGMLGSAMSALIRMELSVPGMLIGNDQIYNSIVTSHAFIMIFFMVMPIMLGGFGNWLV 85
Cdd:MTH00007    1 MRWLYSTNHKDIGTLYFILGVWGGLLGTSMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464  86 PLMINAPDMAFPRLNNMSFWLLIPSLILLIYSNIFGSGTGTGWTVYPPLSSQL---NPSIDLTIFSLHIAGISSILSSIN 162
Cdd:MTH00007   81 PLMLGAPDMAFPRLNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLahaGPSVDLAIFSLHLAGVSSILGAIN 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 163 FLCTIINM--SNTSMNNWTLFTWSVLITTILLLLSLPVLAGAITMILTDRNLNTAFFNPAGGGDPILYQHLFWFFGHPEV 240
Cdd:MTH00007  161 FITTVINMrwKGLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEV 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 241 YILILPGFGLISHMICLESGKKETFGMLGMIYAMISIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMVIAIPTGIKVFSW 320
Cdd:MTH00007  241 YILILPGFGAISHIVTHYAGKLEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSW 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 321 MATINGMKIKLTPSMLWILGFIFLFTIGGLTGIILSNSSIDIILHDTYYVVAHFHYVLSMGAVFSIIGAFITWFPLLTGC 400
Cdd:MTH00007  321 LATIHGSPIKYETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTGL 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 401 TMNNFSLKIQFLTMFVGVNMTFFPQHFLGLSGMPRRYSDYPDFYLMWNKISSLGSMISIISIIHLMTIIVSSMKNKNLMI 480
Cdd:MTH00007  401 TLHDRWAKAHFFLMFLGVNLTFFPQHFLGLSGMPRRYSDYPDAYTKWNVVSSFGSMLSFVALLLFIFILWEAFSAQRGVI 480

                         490       500
                  ....*....|....*....|....*....
gi 2172617464 481 NFYYKNSASEWTHSFPPMNHAFNESSILT 509
Cdd:MTH00007  481 ASPHMSSSLEWQDTLPLDFHNLPETGIIT 509
COX1 MTH00079
cytochrome c oxidase subunit I; Provisional
 3-504 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177148  Cd Length: 508  Bit Score: 611.69  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464   3 KNFMKWMLSTNHKDIGTLYFYFGVWAGMLGSAMSALIRMELSVPGMLIGNDQIYNSIVTSHAFIMIFFMVMPIMLGGFGN 82
Cdd:MTH00079    2 GGLSVWLESSNHKDIGTLYFLFGLWSGMVGTSLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464  83 WLVPLMINAPDMAFPRLNNMSFWLLIPSLILLIYSNIFGSGTGTGWTVYPPLSS--QLNPSIDLTIFSLHIAGISSILSS 160
Cdd:MTH00079   82 WMLPLMLGAPDMSFPRLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLSTlgHPGSSVDLAIFSLHCAGISSILGG 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 161 INFLCTIINMSNTSM--NNWTLFTWSVLITTILLLLSLPVLAGAITMILTDRNLNTAFFNPAGGGDPILYQHLFWFFGHP 238
Cdd:MTH00079  162 INFMVTTKNLRSSSIslEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHP 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 239 EVYILILPGFGLISHMICLESGKKETFGMLGMIYAMISIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMVIAIPTGIKVF 318
Cdd:MTH00079  242 EVYILILPAFGIISQSTLYLTGKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVF 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 319 SWMATINGMKIKLTPSMLWILGFIFLFTIGGLTGIILSNSSIDIILHDTYYVVAHFHYVLSMGAVFSIIGAFITWFPLLT 398
Cdd:MTH00079  322 SWLATLFGMKMKFQPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFMT 401

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 399 GCTMNNFSLKIQFLTMFVGVNMTFFPQHFLGLSGMPRRYSDYPDFYLMWNKISSLGSMISIISIIHLMTIIVSSMKNKNL 478
Cdd:MTH00079  402 GIVYDKLMMSAVFFLMFVGVNLTFFPLHFAGLHGMPRKYLDYPDVYSVWNVISSYGSMISVFALFLFIYVLLESFFSYRL 481

                         490       500
                  ....*....|....*....|....*.
gi 2172617464 479 MINFYYKNSASEWTHSFPPMNHAFNE 504
Cdd:MTH00079  482 VLHDNYINSSPEYSLSSYVFGHSYQS 507
COX1 MTH00182
cytochrome c oxidase subunit I; Provisional
 1-504 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 214451  Cd Length: 525  Bit Score: 585.25  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464   1 MYKNFMKWMLSTNHKDIGTLYFYFGVWAGMLGSAMSALIRMELSVPGMLIGNDQIYNSIVTSHAFIMIFFMVMPIMLGGF 80
Cdd:MTH00182    1 KNLYLTRWVFSTNHKDIGTLYLVFGAGAGMIGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464  81 GNWLVPLMINAPDMAFPRLNNMSFWLLIPSLILLIYSNIFGSGTGTGWTVYPPLSSQLNPS---IDLTIFSLHIAGISSI 157
Cdd:MTH00182   81 GNWLVPLYIGAPDMAFPRLNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSggaVDMAIFSLHLAGVSSI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 158 LSSINFLCTIINMS--NTSMNNWTLFTWSVLITTILLLLSLPVLAGAITMILTDRNLNTAFFNPAGGGDPILYQHLFWFF 235
Cdd:MTH00182  161 LGAINFITTIFNMRapGVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFF 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 236 GHPEVYILILPGFGLISHMICLESGKKETFGMLGMIYAMISIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMVIAIPTGI 315
Cdd:MTH00182  241 GHPEVYILILPGFGMISQIIPTFVAKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGI 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 316 KVFSWMATINGMKIKLTPSMLWILGFIFLFTIGGLTGIILSNSSIDIILHDTYYVVAHFHYVLSMGAVFSIIGAFITWFP 395
Cdd:MTH00182  321 KVFSWLATIYGGTLRLDTPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFG 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 396 LLTGCTMNNFSLKIQFLTMFVGVNMTFFPQHFLGLSGMPRRYSDYPDFYLMWNKISSLGSMISIISIIHLMTIIVSSMKN 475
Cdd:MTH00182  401 KITGYCYNELYGKIHFWLMFIGVNLTFFPQHFLGLAGFPRRYSDFADAFAGWNLVSSLGSIISIVGVVWFIYIIYDAYVR 480

                         490       500       510
                  ....*....|....*....|....*....|...
gi 2172617464 476 KNLMINFYYKNSAS----EWTHSFPPMNHAFNE 504
Cdd:MTH00182  481 EEKFIGWKEGTGESwaslEWVHSSPPLFHTYNE 513
COX1 MTH00184
cytochrome c oxidase subunit I; Provisional
 7-504 0e+00

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177235  Cd Length: 519  Bit Score: 578.70  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464   7 KWMLSTNHKDIGTLYFYFGVWAGMLGSAMSALIRMELSVPGMLIGNDQIYNSIVTSHAFIMIFFMVMPIMLGGFGNWLVP 86
Cdd:MTH00184    7 RWLFSTNHKDIGTLYLLFGAFAGMIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVP 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464  87 LMINAPDMAFPRLNNMSFWLLIPSLILLIYSNIFGSGTGTGWTVYPPLSS---QLNPSIDLTIFSLHIAGISSILSSINF 163
Cdd:MTH00184   87 LYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSiqaHSGGSVDMAIFSLHLAGISSILGAMNF 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 164 LCTIINM--SNTSMNNWTLFTWSVLITTILLLLSLPVLAGAITMILTDRNLNTAFFNPAGGGDPILYQHLFWFFGHPEVY 241
Cdd:MTH00184  167 ITTIFNMraPGITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVY 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 242 ILILPGFGLISHMICLESGKKETFGMLGMIYAMISIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMVIAIPTGIKVFSWM 321
Cdd:MTH00184  247 ILILPGFGIISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWI 326

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 322 ATINGMKIKLTPSMLWILGFIFLFTIGGLTGIILSNSSIDIILHDTYYVVAHFHYVLSMGAVFSIIGAFITWFPLLTGCT 401
Cdd:MTH00184  327 ATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYC 406

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 402 MNNFSLKIQFLTMFVGVNMTFFPQHFLGLSGMPRRYSDYPDFYLMWNKISSLGSMISIISIIHLMTIIVSSMKNKNLMIN 481
Cdd:MTH00184  407 YNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDSFAGWNQISSLGSVISIVGVVWFIYIVYDAYVREIKFVG 486

                         490       500
                  ....*....|....*....|....*.
gi 2172617464 482 FYYKN---SASEWTHSFPPMNHAFNE 504
Cdd:MTH00184  487 WVEDSghyPSLEWAQTSPPAHHTYNE 512
Heme_Cu_Oxidase_I cd00919
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ...
 14-448 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: 517.85  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464  14 HKDIGTLYFYFGVWAGMLGSAMSALIRMELSVPGMLIGNDQIYNSIVTSHAFIMIFFMVMPIMLGGFGNWLVPlMINAPD 93
Cdd:cd00919     1 HKDIGLLYLIFAFVALLLGGLLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464  94 MAFPRLNNMSFWLLIPSLILLIYSNIFGSGTGTGWTVYPPLSSQL---NPSIDLTIFSLHIAGISSILSSINFLCTIINM 170
Cdd:cd00919    80 LAFPRLNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSyssGVGVDLAILGLHLAGVSSILGAINFITTILNM 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 171 S--NTSMNNWTLFTWSVLITTILLLLSLPVLAGAITMILTDRNLNTAFFNPAGGGDPILYQHLFWFFGHPEVYILILPGF 248
Cdd:cd00919   160 RapGMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAF 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 249 GLISHMICLESGKKeTFGMLGMIYAMISIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMVIAIPTGIKVFSWMATINGMK 328
Cdd:cd00919   240 GAISEIIPTFSGKP-LFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGR 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 329 IKLTPSMLWILGFIFLFTIGGLTGIILSNSSIDIILHDTYYVVAHFHYVLSMGAVFSIIGAFITWFPLLTGCTMNNFSLK 408
Cdd:cd00919   319 IRFDPPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKLGK 398

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|
gi 2172617464 409 IQFLTMFVGVNMTFFPQHFLGLSGMPRRYSDYPDFYLMWN 448
Cdd:cd00919   399 IHFWLWFIGFNLTFFPMHFLGLLGMPRRYADYPDGFAPWN 438
COX1 MTH00026
cytochrome c oxidase subunit I; Provisional
 4-504 4.77e-179

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 164599  Cd Length: 534  Bit Score: 513.79  E-value: 4.77e-179
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464   4 NFMKWMLSTNHKDIGTLYFYFGVWAGMLGSAMSALIRMELSVPGMLIGNDQIYNSIVTSHAFIMIFFMVMPIMLGGFGNW 83
Cdd:MTH00026    3 SFVRWFFSCNHKDIGSLYLVFGALSGAIGTAFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNW 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464  84 LVPLMINAPDMAFPRLNNMSFWLLIPSLILLIYSNIFGSGTGTGWTVYPPLSS---QLNPSIDLTIFSLHIAGISSILSS 160
Cdd:MTH00026   83 FVPLMIGAPDMAFPRLNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASiqaHSGGSVDMAIFSLHLAGLSSILGA 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 161 INFLCTIINMSN--TSMNNWTLFTWSVLITTILLLLSLPVLAGAITMILTDRNLNTAFFNPAGGGDPILYQHLFWFFGHP 238
Cdd:MTH00026  163 MNFITTVMNMRTpgMTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHP 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 239 EVYILILPGFGLISHMICLESGKKETFGMLGMIYAMISIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMVIAIPTGIKVF 318
Cdd:MTH00026  243 EVYILILPGFGIISQILSLFSYKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIF 322

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 319 SWMATI--NGMKIKLTPSMLWILGFIFLFTIGGLTGIILSNSSIDIILHDTYYVVAHFHYVLSMGAVFSIIGAFITWFPL 396
Cdd:MTH00026  323 SWLATVsgSGRNLIFTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWFGK 402

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 397 LTGCTMNNFSLKIQFLTMFVGVNMTFFPQHFLGLSGMPRRYSDYPDFYLMWNKISSLGSMISIISIIHLMTIIVSS-MKN 475
Cdd:MTH00026  403 ITGYAYKDIYGLIHFWLMFIGVNITFFPQHFLGLAGLPRRYADYPDNFEDFNQISSFGSIISIIAVIWFIVVIFDAyYRE 482

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|.
gi 2172617464 476 KNLMINFYYKN------------SASEWTHSFPPMNHAFNE 504
Cdd:MTH00026  483 EPFDINIMAKGplipfscqpahfDTLEWSLTSPPEHHTYNE 523
CtaD_CoxA TIGR02891
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ...
 11-442 1.55e-166

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: 480.57  E-value: 1.55e-166
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464  11 STNHKDIGTLYFYFGVWAGMLGSAMSALIRMELSVPGMLIGNDQIYNSIVTSHAFIMIFFMVMPiMLGGFGNWLVPLMIN 90
Cdd:TIGR02891   3 TVDHKRIGILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIP-ILAGFGNYLLPLMIG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464  91 APDMAFPRLNNMSFWLLIPSLILLIYSNIFGSGTGTGWTVYPPLSSQL---NPSIDLTIFSLHIAGISSILSSINFLCTI 167
Cdd:TIGR02891  82 ARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSgspGVGVDLWLLGLHLLGISSILGAVNFIVTI 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 168 INM--SNTSMNNWTLFTWSVLITTILLLLSLPVLAGAITMILTDRNLNTAFFNPAGGGDPILYQHLFWFFGHPEVYILIL 245
Cdd:TIGR02891 162 LNMraPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFL 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 246 PGFGLISHMICLESGKKeTFGMLGMIYAMISIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMVIAIPTGIKVFSWMATIN 325
Cdd:TIGR02891 242 PAFGIISEILPTFARKP-IFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLW 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 326 GMKIKLTPSMLWILGFIFLFTIGGLTGIILSNSSIDIILHDTYYVVAHFHYVLSMGAVFSIIGAFITWFPLLTGCTMNNF 405
Cdd:TIGR02891 321 GGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNER 400

                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 2172617464 406 SLKIQFLTMFVGVNMTFFPQHFLGLSGMPRRYSDYPD 442
Cdd:TIGR02891 401 LGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPP 437
CyoB COG0843
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
5-442 7.85e-166

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


Pssm-ID: 440605  Cd Length: 535  Bit Score: 480.01  E-value: 7.85e-166
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464   5 FMKWMLSTNHKDIGTLYFYFGVWAGMLGSAMSALIRMELSVPGMLIGNDQIYNSIVTSHAFIMIFFMVMPiMLGGFGNWL 84
Cdd:COG0843     6 WRRWLTTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464  85 VPLMINAPDMAFPRLNNMSFWLLIPSLILLIYSNIFGSGTGTGWTVYPPLSSQL---NPSIDLTIFSLHIAGISSILSSI 161
Cdd:COG0843    85 VPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEaspGVGVDLWLLGLALFGVGSILGGV 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 162 NFLCTIINM--SNTSMNNWTLFTWSVLITTILLLLSLPVLAGAITMILTDRNLNTAFFNPAGGGDPILYQHLFWFFGHPE 239
Cdd:COG0843   165 NFIVTILKMraPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPE 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 240 VYILILPGFGLISHMICLESGKKeTFGMLGMIYAMISIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMVIAIPTGIKVFS 319
Cdd:COG0843   245 VYILILPAFGIVSEIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFN 323

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 320 WMATINGMKIKLTPSMLWILGFIFLFTIGGLTGIILSNSSIDIILHDTYYVVAHFHYVLSMGAVFSIIGAFITWFPLLTG 399
Cdd:COG0843   324 WIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTG 403

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|...
gi 2172617464 400 CTMNNFSLKIQFLTMFVGVNMTFFPQHFLGLSGMPRRYSDYPD 442
Cdd:COG0843   404 RMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPP 446
COX1 MTH00048
cytochrome c oxidase subunit I; Provisional
 4-487 1.32e-156

cytochrome c oxidase subunit I; Provisional


Pssm-ID: 177123  Cd Length: 511  Bit Score: 455.68  E-value: 1.32e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464   4 NFMKWMLSTNHKDIGTLYFYFGVWAGMLGSAMSALIRMELSVPGMLIGNDQIYNSIVTSHAFIMIFFMVMPIMLGGFGNW 83
Cdd:MTH00048    3 SLLSWLFTLDHKRIGVIYTLLGVWSGFVGLSLSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFGNY 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464  84 LVPLMINAPDMAFPRLNNMSFWLLIPSLILLIYSNIFGSGTGtgWTVYPPLSSQLNPS---IDLTIFSLHIAGISSILSS 160
Cdd:MTH00048   83 LLPLLLGLSDLNLPRLNALSAWLLVPSIVFLLLSMCLGAGVG--WTFYPPLSSSLFSSswgVDFLMFSLHLAGVSSLFGS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 161 INFLCTIINMSNTSMNNWT-LFTWSVLITTILLLLSLPVLAGAITMILTDRNLNTAFFNPAGGGDPILYQHLFWFFGHPE 239
Cdd:MTH00048  161 INFICTIYSAFMTNVFSRTsIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPE 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 240 VYILILPGFGLISHmICLE-SGKKETFGMLGMIYAMISIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMVIAIPTGIKVF 318
Cdd:MTH00048  241 VYVLILPGFGIISH-ICLSlSNNDDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVF 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 319 SWMATINGMKIKLT-PSMLWILGFIFLFTIGGLTGIILSNSSIDIILHDTYYVVAHFHYVLSMGAVFSIIGAFITWFPLL 397
Cdd:MTH00048  320 SWLYMLLNSRVRKSdPVVWWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWPLI 399

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 398 TGCTMNNFSLKIQFLTMFVGVNMTFFPQHFLGLSGMPRRYSDYPDFYLMWNKISSLGSMISIISIIHLMTIIVSSMKNKN 477
Cdd:MTH00048  400 TGLSLNKYLLQCHCIISMIGFNLCFFPMHYFGLCGLPRRVCVYEPSYYWINVVCTVGSFISAFSGCFFVFILWESLVVKN 479

                         490
                  ....*....|
gi 2172617464 478 LMINFYYKNS 487
Cdd:MTH00048  480 EVLGLWGSSS 489
Ubiquinol_Oxidase_I cd01662
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ...
 8-442 2.37e-142

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: 418.91  E-value: 2.37e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464   8 WMLSTNHKDIGTLYFYFGVWAGMLGSAMSALIRMELSVPGM-LIGNDQiYNSIVTSHAFIMIFFMVMPIMLGgFGNWLVP 86
Cdd:cd01662     1 WLTTVDHKRIGIMYIITAFVFFLRGGVDALLMRTQLALPGNdFLSPEH-YNQIFTMHGTIMIFLFAMPLVFG-LMNYLVP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464  87 LMINAPDMAFPRLNNMSFWLLIPSLILLIYSNIFGSGTGTGWTVYPPLSSQLN---PSIDLTIFSLHIAGISSILSSINF 163
Cdd:cd01662    79 LQIGARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYspgVGVDYWILGLQFSGIGTLLGAINF 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 164 LCTIINM--SNTSMNNWTLFTWSVLITTILLLLSLPVLAGAITMILTDRNLNTAFFNPAGGGDPILYQHLFWFFGHPEVY 241
Cdd:cd01662   159 IVTILKMraPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVY 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 242 ILILPGFGLISHMICLESGKKeTFGMLGMIYAMISIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMVIAIPTGIKVFSWM 321
Cdd:cd01662   239 ILILPAFGIFSEIVPTFSRKP-LFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWL 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 322 ATINGMKIKLTPSMLWILGFIFLFTIGGLTGIILSNSSIDIILHDTYYVVAHFHYVLSMGAVFSIIGAFITWFPLLTGCT 401
Cdd:cd01662   318 FTMWRGRIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRM 397

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|.
gi 2172617464 402 MNNFSLKIQFLTMFVGVNMTFFPQHFLGLSGMPRRYSDYPD 442
Cdd:cd01662   398 LNERLGKWSFWLWFIGFNLTFFPMHILGLMGMPRRVYTYLP 438
COX1 pfam00115
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ...
 16-439 6.29e-116

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: 348.79  E-value: 6.29e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464  16 DIGTLYFYFGVWAGMLGSAMSALIRMELSVPGMLIGNDQIYNSIVTSHAFIMIFFMVMPIMlGGFGNWLVPLMINAPDMA 95
Cdd:pfam00115   1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATPFL-FGFGNYLVPLMIGARDMA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464  96 FPRLNNMSFWLLIPSLILLIYSniFGSGTgTGWTVYPPLssqlnPSIDLTIFSLHIAGISSILSSINFLCTIINMSNTSM 175
Cdd:pfam00115  80 FPRLNALSFWLVVLGAVLLLAS--FGGAT-TGWTEYPPL-----VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPGM 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 176 N-NWTLFTWSVLITTILLLLSLPVLAGAITMILTDRNLNtaffnpAGGGDPILYQHLFWFFGHPEVYILILPGFGLISHM 254
Cdd:pfam00115 152 TlRMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGIIYYI 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 255 ICLESGKKeTFGMLGMIYAMISIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMVIAIPTGIKVFSWMATINGMKIKL-TP 333
Cdd:pfam00115 226 LPKFAGRP-LFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFrTT 304

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 334 SMLWILGFIFLFTIGGLTGIILSNSSIDIILHDTYYVVAHFHYVLSMGAVFSIIGAFITWFPLLTGCTMNNFSLKIQFLT 413
Cdd:pfam00115 305 PMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFWL 384

                         410       420
                  ....*....|....*....|....*.
gi 2172617464 414 MFVGVNMTFFPQHFLGLSGMPRRYSD 439
Cdd:pfam00115 385 LFIGFNLTFFPMHILGLLGMPRRYAP 410
CyoB TIGR02843
cytochrome o ubiquinol oxidase, subunit I; Cytochrome o terminal oxidase complex is the ...
 8-442 4.45e-101

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: 317.38  E-value: 4.45e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464   8 WMLSTNHKDIGTLYFYFGVWAGMLGSAMSALIRMELSV-----PGMLIgnDQIYNSIVTSHAFIMIFFMVMPIMLGGFgN 82
Cdd:TIGR02843  47 WLTTVDHKKIGIMYIIVALVMLLRGFADAIMMRTQQALasggsAGYLP--PHHYDQIFTAHGVIMIFFVAMPFVFGLM-N 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464  83 WLVPLMINAPDMAFPRLNNMSFWLLIPSLILLIYSNIFGSGTGTGWTVYPPLSS-QLNPS--IDLTIFSLHIAGISSILS 159
Cdd:TIGR02843 124 LVVPLQIGARDVAFPFLNSLSFWLTVVGAILVNVSLGVGEFAQTGWLAYPPLSElQYSPGvgVDYYIWALQISGIGTLLT 203

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 160 SINFLCTIINMSNTSMN--NWTLFTWSVLITTILLLLSLPVLAGAITMILTDRNLNTAFFNPAGGGDPILYQHLFWFFGH 237
Cdd:TIGR02843 204 GINFFVTIIKMRAPGMTlmKMPVFTWTSLCSNVLIIASFPILTVTLALLTLDRYLGMHFFTNEAGGNPMMYVNLIWAWGH 283

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 238 PEVYILILPGFGLISHMICLESGKKeTFGMLGMIYAMISIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMVIAIPTGIKV 317
Cdd:TIGR02843 284 PEVYILILPAFGIFSEVVATFSRKR-LFGYTSMVWATIAITVLSFIVWLHHFFTMGAGANVNAFFGIATMIIAIPTGVKI 362

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 318 FSWMATINGMKIKLTPSMLWILGFIFLFTIGGLTGIILSNSSIDIILHDTYYVVAHFHYVLSMGAVFSIIGAFITWFPLL 397
Cdd:TIGR02843 363 FNWLFTMYKGRIRFETPMLWTIGFMVTFSIGGMTGVLLAVPPADFVLHNSLFLIAHFHNVIIGGVVFGCFAGLTYWFPKA 442

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*
gi 2172617464 398 TGCTMNNFSLKIQFLTMFVGVNMTFFPQHFLGLSGMPRRYSDYPD 442
Cdd:TIGR02843 443 FGFKLNEKLGKRSFWCWFIGFYLAFMPLYILGFMGMTRRLNHYDN 487
QoxB TIGR02882
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ...
 7-440 5.54e-96

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: 304.08  E-value: 5.54e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464   7 KWMLSTNHKDIGTLYFYFGVWAGMLGSAMSALIRMELSVPGMLIGNDQIYNSIVTSHAFIMIFFMVMPIMLGgFGNWLVP 86
Cdd:TIGR02882  43 EWLTTVDHKKIGVMYIICAVLMLFRGGIDALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVP 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464  87 LMINAPDMAFPRLNNMSFWLLIPSLILLIYSNIFGSGTGTGWTVYPPLSS---QLNPSIDLTIFSLHIAGISSILSSINF 163
Cdd:TIGR02882 122 LQIGARDVAFPVLNALSFWLFFAGAMLFNISFVIGGSPDAGWTNYAPLAGpefSPGVGVNYYLIALQISGIGTLMTGINF 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 164 LCTIINMSNTSMN--NWTLFTWSVLITTILLLLSLPVLAGAITMILTDRNLNTAFFNPAGGGDPILYQHLFWFFGHPEVY 241
Cdd:TIGR02882 202 FVTILKMRAPGMKlmQMPMFTWTTLITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLFWIWGHPEVY 281

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 242 ILILPGFGLISHMICLESgKKETFGMLGMIYAMISIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMVIAIPTGIKVFSWM 321
Cdd:TIGR02882 282 IVILPAFGIYSEIISTFA-QKRLFGYKSMVWSTVGIAFLSFLVWVHHFFTMGNGALINSFFSITTMAIAIPTGVKIFNWL 360

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 322 ATINGMKIKLTPSMLWILGFIFLFTIGGLTGIILSNSSIDIILHDTYYVVAHFHYVLSMGAVFSIIGAFITWFPLLTGCT 401
Cdd:TIGR02882 361 LTLYKGKIRFTTPMLFSLAFIPNFLIGGVTGVMLAMASADYQYHNTYFLVAHFHYVLITGVVFACLAGLIYWYPKMFGYK 440

                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 2172617464 402 MNNFSLKIQFLTMFVGVNMTFFPQHFLGLSGMPRRYSDY 440
Cdd:TIGR02882 441 LNERLGKWCFWFFMIGFNVCFFPMYILGLDGMPRRMYTY 479
PRK15017 PRK15017
cytochrome o ubiquinol oxidase subunit I; Provisional
 7-442 6.44e-85

cytochrome o ubiquinol oxidase subunit I; Provisional


Pssm-ID: 184978  Cd Length: 663  Bit Score: 275.66  E-value: 6.44e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464   7 KWMLSTNHKDIGTLYFYFGVWAGMLGSAMSALIRMELSVP-----GMLIGNDqiYNSIVTSHAFIMIFFMVMPIMLGgFG 81
Cdd:PRK15017   47 EWLTSVDHKRLGIMYIIVAIVMLLRGFADAIMMRSQQALAsageaGFLPPHH--YDQIFTAHGVIMIFFVAMPFVIG-LM 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464  82 NWLVPLMINAPDMAFPRLNNMSFWLLIPSLILLIYSNIFGSGTGTGWTVYPPLSS-QLNPSI--DLTIFSLHIAGISSIL 158
Cdd:PRK15017  124 NLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLSGiEYSPGVgvDYWIWSLQLSGIGTTL 203

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 159 SSINFLCTIINMSNTSMNNWTL--FTWSVLITTILLLLSLPVLAGAITMILTDRNLNTAFFNPAGGGDPILYQHLFWFFG 236
Cdd:PRK15017  204 TGINFFVTILKMRAPGMTMFKMpvFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWG 283

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 237 HPEVYILILPGFGLISHMICLESgKKETFGMLGMIYAMISIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMVIAIPTGIK 316
Cdd:PRK15017  284 HPEVYILILPVFGVFSEIAATFS-RKRLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVK 362

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 317 VFSWMATINGMKIKLTPSMLWILGFIFLFTIGGLTGIILSNSSIDIILHDTYYVVAHFHYVLSMGAVFSIIGAFITWFPL 396
Cdd:PRK15017  363 IFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYWWPK 442

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*.
gi 2172617464 397 LTGCTMNNFSLKIQFLTMFVGVNMTFFPQHFLGLSGMPRRYSDYPD 442
Cdd:PRK15017  443 AFGFKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMTRRLSQQID 488
ba3-like_Oxidase_I cd01660
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ...
 224-446 3.91e-14

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


Pssm-ID: 238830  Cd Length: 473  Bit Score: 74.63  E-value: 3.91e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 224 DPILYQHLFWFFGHPEVYILILPGFGLISHMICLESGKKeTFGMLGMIYAMISIGFLGFIVWAHHMFT-VGMDVDTRAYF 302
Cdd:cd01660   200 DVLLSRTLFWWFGHPLVYFWLLPAYIAWYTILPKIAGGK-LFSDPLARLAFILFLLFSTPVGFHHQFAdPGIGPGWKFIH 278

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 303 TSATMVIAIPTGIKVFSWMATIN------------GMKIKL---TPSMLWILGFIFLFTIGGLTGIILSNSSIDIILHDT 367
Cdd:cd01660   279 MVLTFMVALPSLLTAFTVFASLEiagrlrggkglfGWIRALpwgDPMFLALFLAMLMFIPGGAGGIINASYQLNYVVHNT 358

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2172617464 368 YYVVAHFHYVLSMGAVFSIIGAFITWFPLLTGCTMNNFSL-KIQFLTMFVGVNMTFFPQHFLGLSGMPRR--YSDYPDFY 444
Cdd:cd01660   359 AWVPGHFHLTVGGAVALTFMAVAYWLVPHLTGRELAAKRLaLAQPWLWFVGMTIMSTAMHVAGLLGAPRRtaEAQYGGLP 438


                  ..
gi 2172617464 445 LM 446
Cdd:cd01660   439 AA 440
 
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