|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-500 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 956.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 1 MRWLFSTNHKDIGTLYILFGMWSGLVGTALSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLV 80
Cdd:MTH00153 2 NKWLFSTNHKDIGTLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 81 PLMLGAPDMAFPRLNNMSFWLLPPALLLLLSSAAVESGVGTGWTVYPPLAGNLAHAGGSVDLAIFSLHLAGVSSILGAVN 160
Cdd:MTH00153 82 PLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAIN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 161 FITTIINMRWRGMQFERLPLFVWSVKITAVLLLLSLPVLAGAITMLLTDRNFNTAFFDPAGGGDPILYQHLFWFFGHPEV 240
Cdd:MTH00153 162 FITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 241 YILILPGFGMISHIVSHYSSKKETFGTLGMIYAMLAIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSW 320
Cdd:MTH00153 242 YILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSW 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 321 LATIHGAKIKYETPMLWALGFIFLFTVGGLTGIVLSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFGAFNYWFPLLSGV 400
Cdd:MTH00153 322 LATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGL 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 401 TLHSRWTKAHFYIMFIGVNVTFFPQHFLGLSGMPRRYSDYPDCYTKWNVISSIGSMISFVAVLYFMVIVWEALVSQRSVI 480
Cdd:MTH00153 402 TMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPVL 481
|
490 500
....*....|....*....|
gi 1238821341 481 WSTHLSTALEWDNILPADFH 500
Cdd:MTH00153 482 FSLNLSSSIEWLQNLPPAEH 501
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
7-491 |
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: 884.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 7 TNHKDIGTLYILFGMWSGLVGTALSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGA 86
Cdd:cd01663 1 TNHKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 87 PDMAFPRLNNMSFWLLPPALLLLLSSAAVESGVGTGWTVYPPLAGNLAHAGGSVDLAIFSLHLAGVSSILGAVNFITTII 166
Cdd:cd01663 81 PDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 167 NMRWRGMQFERLPLFVWSVKITAVLLLLSLPVLAGAITMLLTDRNFNTAFFDPAGGGDPILYQHLFWFFGHPEVYILILP 246
Cdd:cd01663 161 NMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 247 GFGMISHIVSHYSSKKETFGTLGMIYAMLAIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHG 326
Cdd:cd01663 241 GFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 327 AKIKYETPMLWALGFIFLFTVGGLTGIVLSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFGAFNYWFPLLSGVTLHSRW 406
Cdd:cd01663 321 GSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 407 TKAHFYIMFIGVNVTFFPQHFLGLSGMPRRYSDYPDCYTKWNVISSIGSMISFVAVLYFMVIVWEALVSQRSVI-WSTHL 485
Cdd:cd01663 401 GKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIfNVGEG 480
|
....*.
gi 1238821341 486 STALEW 491
Cdd:cd01663 481 STSLEW 486
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
4-501 |
0e+00 |
|
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) of cytochrome c oxidases of bacterial origin. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits I-III form the functional core of the enzyme complex. Subunit I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit II and heme a of subunit I to the bimetallic center formed by heme a3 and copper B. This cytochrome c oxidase shows proton pump activity across the membrane in addition to the electron transfer. In the bacilli an apparent split (paralogism) has created a sister clade (TIGR02882) encoding subunits (QoxA) of the aa3-type quinone oxidase complex which reacts directly with quinones, bypassing the interaction with soluble cytochrome c. This model attempts to exclude these sequences, placing them between the trusted and noise cutoffs. These families, as well as archaeal and eukaryotic cytochrome c subunit I's are included within the superfamily model, pfam00115. [Energy metabolism, Electron transport]
Pssm-ID: 213748 Cd Length: 499 Bit Score: 571.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 4 LFSTNHKDIGTLYILFGMWSGLVGTALSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMiGGFGNWLVPLM 83
Cdd:TIGR02891 1 LTTVDHKRIGILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIPIL-AGFGNYLLPLM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 84 LGAPDMAFPRLNNMSFWLLPPALLLLLSSAAVESGVGTGWTVYPPLAGNLAHAGGSVDLAIFSLHLAGVSSILGAVNFIT 163
Cdd:TIGR02891 80 IGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 164 TIINMRWRGMQFERLPLFVWSVKITAVLLLLSLPVLAGAITMLLTDRNFNTAFFDPAGGGDPILYQHLFWFFGHPEVYIL 243
Cdd:TIGR02891 160 TILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYII 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 244 ILPGFGMISHIVSHYsSKKETFGTLGMIYAMLAIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLAT 323
Cdd:TIGR02891 240 FLPAFGIISEILPTF-ARKPIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIAT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 324 IHGAKIKYETPMLWALGFIFLFTVGGLTGIVLSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFGAFNYWFPLLSGVTLH 403
Cdd:TIGR02891 319 LWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYN 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 404 SRWTKAHFYIMFIGVNVTFFPQHFLGLSGMPRRYSDYPD--CYTKWNVISSIGSMISFVAVLYFMVIVWEALVSQRSV-- 479
Cdd:TIGR02891 399 ERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPqmGFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGPKAga 478
|
490 500
....*....|....*....|...
gi 1238821341 480 -IWSthlSTALEWDNILPADFHN 501
Cdd:TIGR02891 479 nPWG---ATTLEWTTSSPPPAHN 498
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
1-505 |
0e+00 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 566.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 1 MRWLFSTNHKDIGTLYILFGMWSGLVGTALSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMmIGGFGNWLV 80
Cdd:COG0843 7 RRWLTTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATPF-LAGFGNYLV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 81 PLMLGAPDMAFPRLNNMSFWLLPPALLLLLSSAAVESGVGTGWTVYPPLAGNLAHAGGSVDLAIFSLHLAGVSSILGAVN 160
Cdd:COG0843 86 PLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVN 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 161 FITTIINMRWRGMQFERLPLFVWSVKITAVLLLLSLPVLAGAITMLLTDRNFNTAFFDPAGGGDPILYQHLFWFFGHPEV 240
Cdd:COG0843 166 FIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEV 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 241 YILILPGFGMISHIVSHYSSKKeTFGTLGMIYAMLAIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSW 320
Cdd:COG0843 246 YILILPAFGIVSEIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNW 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 321 LATIHGAKIKYETPMLWALGFIFLFTVGGLTGIVLSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFGAFNYWFPLLSGV 400
Cdd:COG0843 325 IATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGR 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 401 TLHSRWTKAHFYIMFIGVNVTFFPQHFLGLSGMPRRYSDYP--DCYTKWNVISSIGSMISFVAVLYFMVIVWEALVSQRS 478
Cdd:COG0843 405 MLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAFILAVGFLLFLINLVVSLRKGPK 484
|
490 500
....*....|....*....|....*..
gi 1238821341 479 VIWSTHLSTALEWDNILPADFHNSAET 505
Cdd:COG0843 485 AGGNPWGARTLEWATPSPPPLYNFASI 511
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
11-457 |
1.67e-132 |
|
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: 391.17 E-value: 1.67e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 11 DIGTLYILFGMWSGLVGTALSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMmIGGFGNWLVPLMLGAPDMA 90
Cdd:pfam00115 1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATPF-LFGFGNYLVPLMIGARDMA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 91 FPRLNNMSFWLLPPALLLLLSSAAvesGVGTGWTVYPPLAGnlahaggsVDLAIFSLHLAGVSSILGAVNFITTIINMRW 170
Cdd:pfam00115 80 FPRLNALSFWLVVLGAVLLLASFG---GATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 171 RGMQFeRLPLFVWSVKITAVLLLLSLPVLAGAITMLLTDRNFNtaffdpAGGGDPILYQHLFWFFGHPEVYILILPGFGM 250
Cdd:pfam00115 149 PGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 251 ISHIVSHYSsKKETFGTLGMIYAMLAIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGAKIK 330
Cdd:pfam00115 222 IYYILPKFA-GRPLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIR 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 331 -YETPMLWALGFIFLFTVGGLTGIVLSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFGAFNYWFPLLSGVTLHSRWTKA 409
Cdd:pfam00115 301 fRTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKL 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1238821341 410 HFYIMFIGVNVTFFPQHFLGLSGMPRRYS----DYPDCYTKWNVISSIGSMI 457
Cdd:pfam00115 381 HFWLLFIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPLNWIRTIGGVL 432
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-500 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 956.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 1 MRWLFSTNHKDIGTLYILFGMWSGLVGTALSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLV 80
Cdd:MTH00153 2 NKWLFSTNHKDIGTLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 81 PLMLGAPDMAFPRLNNMSFWLLPPALLLLLSSAAVESGVGTGWTVYPPLAGNLAHAGGSVDLAIFSLHLAGVSSILGAVN 160
Cdd:MTH00153 82 PLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAIN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 161 FITTIINMRWRGMQFERLPLFVWSVKITAVLLLLSLPVLAGAITMLLTDRNFNTAFFDPAGGGDPILYQHLFWFFGHPEV 240
Cdd:MTH00153 162 FITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 241 YILILPGFGMISHIVSHYSSKKETFGTLGMIYAMLAIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSW 320
Cdd:MTH00153 242 YILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSW 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 321 LATIHGAKIKYETPMLWALGFIFLFTVGGLTGIVLSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFGAFNYWFPLLSGV 400
Cdd:MTH00153 322 LATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGL 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 401 TLHSRWTKAHFYIMFIGVNVTFFPQHFLGLSGMPRRYSDYPDCYTKWNVISSIGSMISFVAVLYFMVIVWEALVSQRSVI 480
Cdd:MTH00153 402 TMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPVL 481
|
490 500
....*....|....*....|
gi 1238821341 481 WSTHLSTALEWDNILPADFH 500
Cdd:MTH00153 482 FSLNLSSSIEWLQNLPPAEH 501
|
|
| COX1 |
MTH00223 |
cytochrome c oxidase subunit I; Provisional |
1-509 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177260 Cd Length: 512 Bit Score: 916.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 1 MRWLFSTNHKDIGTLYILFGMWSGLVGTALSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLV 80
Cdd:MTH00223 1 MRWLFSTNHKDIGTLYLIFGMWSGLVGTSLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 81 PLMLGAPDMAFPRLNNMSFWLLPPALLLLLSSAAVESGVGTGWTVYPPLAGNLAHAGGSVDLAIFSLHLAGVSSILGAVN 160
Cdd:MTH00223 81 PLMLGAPDMAFPRLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 161 FITTIINMRWRGMQFERLPLFVWSVKITAVLLLLSLPVLAGAITMLLTDRNFNTAFFDPAGGGDPILYQHLFWFFGHPEV 240
Cdd:MTH00223 161 FITTIINMRSPGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 241 YILILPGFGMISHIVSHYSSKKETFGTLGMIYAMLAIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSW 320
Cdd:MTH00223 241 YILILPGFGMISHIVSHYSSKKEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSW 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 321 LATIHGAKIKYETPMLWALGFIFLFTVGGLTGIVLSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFGAFNYWFPLLSGV 400
Cdd:MTH00223 321 LATIYGSKIKYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLFTGV 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 401 TLHSRWTKAHFYIMFIGVNVTFFPQHFLGLSGMPRRYSDYPDCYTKWNVISSIGSMISFVAVLYFMVIVWEALVSQRSVI 480
Cdd:MTH00223 401 TLHRRWAKAHFFLMFLGVNLTFFPQHFLGLAGMPRRYSDYPDCYTKWNQVSSFGSMISFVSVLFFMFIVWEAFVSQRSVV 480
|
490 500
....*....|....*....|....*....
gi 1238821341 481 WSTHLSTALEWDNILPADFHNSAETGALV 509
Cdd:MTH00223 481 WSGHLSTSLEWDNLLPADFHNNSETGALV 509
|
|
| COX1 |
MTH00142 |
cytochrome c oxidase subunit I; Provisional |
1-509 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214431 Cd Length: 511 Bit Score: 895.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 1 MRWLFSTNHKDIGTLYILFGMWSGLVGTALSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLV 80
Cdd:MTH00142 2 MRWLFSTNHKDIGTLYFLFGAWAGMVGTGLSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 81 PLMLGAPDMAFPRLNNMSFWLLPPALLLLLSSAAVESGVGTGWTVYPPLAGNLAHAGGSVDLAIFSLHLAGVSSILGAVN 160
Cdd:MTH00142 82 PLMLGAPDMAFPRMNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAIN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 161 FITTIINMRWRGMQFERLPLFVWSVKITAVLLLLSLPVLAGAITMLLTDRNFNTAFFDPAGGGDPILYQHLFWFFGHPEV 240
Cdd:MTH00142 162 FITTVINMRAGGMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 241 YILILPGFGMISHIVSHYSSKKETFGTLGMIYAMLAIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSW 320
Cdd:MTH00142 242 YILILPGFGMISHIINHYSGKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFSW 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 321 LATIHGAKIKYETPMLWALGFIFLFTVGGLTGIVLSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFGAFNYWFPLLSGV 400
Cdd:MTH00142 322 LATLHGSKVKYEPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLFTGL 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 401 TLHSRWTKAHFYIMFIGVNVTFFPQHFLGLSGMPRRYSDYPDCYTKWNVISSIGSMISFVAVLYFMVIVWEALVSQRSVI 480
Cdd:MTH00142 402 TLNPRWLKAHFYTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSSLGSMISFIAVLMFVFIVWESFVSQRLVM 481
|
490 500
....*....|....*....|....*....
gi 1238821341 481 WSTHLSTALEWDNILPADFHNSAETGALV 509
Cdd:MTH00142 482 WSSHLSTSLEWSHRLPPDFHTYDELPILV 510
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
7-491 |
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: 884.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 7 TNHKDIGTLYILFGMWSGLVGTALSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPLMLGA 86
Cdd:cd01663 1 TNHKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 87 PDMAFPRLNNMSFWLLPPALLLLLSSAAVESGVGTGWTVYPPLAGNLAHAGGSVDLAIFSLHLAGVSSILGAVNFITTII 166
Cdd:cd01663 81 PDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 167 NMRWRGMQFERLPLFVWSVKITAVLLLLSLPVLAGAITMLLTDRNFNTAFFDPAGGGDPILYQHLFWFFGHPEVYILILP 246
Cdd:cd01663 161 NMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 247 GFGMISHIVSHYSSKKETFGTLGMIYAMLAIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHG 326
Cdd:cd01663 241 GFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 327 AKIKYETPMLWALGFIFLFTVGGLTGIVLSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFGAFNYWFPLLSGVTLHSRW 406
Cdd:cd01663 321 GSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 407 TKAHFYIMFIGVNVTFFPQHFLGLSGMPRRYSDYPDCYTKWNVISSIGSMISFVAVLYFMVIVWEALVSQRSVI-WSTHL 485
Cdd:cd01663 401 GKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIfNVGEG 480
|
....*.
gi 1238821341 486 STALEW 491
Cdd:cd01663 481 STSLEW 486
|
|
| COX1 |
MTH00167 |
cytochrome c oxidase subunit I; Provisional |
1-500 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177222 Cd Length: 512 Bit Score: 859.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 1 MRWLFSTNHKDIGTLYILFGMWSGLVGTALSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLV 80
Cdd:MTH00167 4 NRWLFSTNHKDIGTLYFIFGAWAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 81 PLMLGAPDMAFPRLNNMSFWLLPPALLLLLSSAAVESGVGTGWTVYPPLAGNLAHAGGSVDLAIFSLHLAGVSSILGAVN 160
Cdd:MTH00167 84 PLMIGAPDMAFPRMNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSIN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 161 FITTIINMRWRGMQFERLPLFVWSVKITAVLLLLSLPVLAGAITMLLTDRNFNTAFFDPAGGGDPILYQHLFWFFGHPEV 240
Cdd:MTH00167 164 FITTIINMKPPGITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 241 YILILPGFGMISHIVSHYSSKKETFGTLGMIYAMLAIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSW 320
Cdd:MTH00167 244 YILILPGFGMISHIVVYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSW 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 321 LATIHGAKIKYETPMLWALGFIFLFTVGGLTGIVLSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFGAFNYWFPLLSGV 400
Cdd:MTH00167 324 LATLHGGKIKWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGL 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 401 TLHSRWTKAHFYIMFIGVNVTFFPQHFLGLSGMPRRYSDYPDCYTKWNVISSIGSMISFVAVLYFMVIVWEALVSQRSVI 480
Cdd:MTH00167 404 TLNETWTKIHFFVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNVVSSIGSLISLVAVILFLFIIWEAFSSKRKLL 483
|
490 500
....*....|....*....|
gi 1238821341 481 WSTHLSTALEWDNILPADFH 500
Cdd:MTH00167 484 PVELTSTNVEWLHGCPPPHH 503
|
|
| COX1 |
MTH00116 |
cytochrome c oxidase subunit I; Provisional |
2-505 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177177 Cd Length: 515 Bit Score: 849.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 2 RWLFSTNHKDIGTLYILFGMWSGLVGTALSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVP 81
Cdd:MTH00116 5 RWLFSTNHKDIGTLYLIFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 82 LMLGAPDMAFPRLNNMSFWLLPPALLLLLSSAAVESGVGTGWTVYPPLAGNLAHAGGSVDLAIFSLHLAGVSSILGAVNF 161
Cdd:MTH00116 85 LMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 162 ITTIINMRWRGMQFERLPLFVWSVKITAVLLLLSLPVLAGAITMLLTDRNFNTAFFDPAGGGDPILYQHLFWFFGHPEVY 241
Cdd:MTH00116 165 ITTCINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVY 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 242 ILILPGFGMISHIVSHYSSKKETFGTLGMIYAMLAIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWL 321
Cdd:MTH00116 245 ILILPGFGIISHIVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSWL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 322 ATIHGAKIKYETPMLWALGFIFLFTVGGLTGIVLSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFGAFNYWFPLLSGVT 401
Cdd:MTH00116 325 ATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGYT 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 402 LHSRWTKAHFYIMFIGVNVTFFPQHFLGLSGMPRRYSDYPDCYTKWNVISSIGSMISFVAVLYFMVIVWEALVSQRSVIW 481
Cdd:MTH00116 405 LHQTWTKAQFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTISSIGSLISMTAVIMLMFIIWEAFSSKRKVLQ 484
|
490 500
....*....|....*....|....
gi 1238821341 482 STHLSTALEWDNILPADFHNSAET 505
Cdd:MTH00116 485 PELTTTNIEWIHGCPPPYHTFEEP 508
|
|
| COX1 |
MTH00007 |
cytochrome c oxidase subunit I; Validated |
1-506 |
0e+00 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 133649 Cd Length: 511 Bit Score: 826.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 1 MRWLFSTNHKDIGTLYILFGMWSGLVGTALSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLV 80
Cdd:MTH00007 1 MRWLYSTNHKDIGTLYFILGVWGGLLGTSMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 81 PLMLGAPDMAFPRLNNMSFWLLPPALLLLLSSAAVESGVGTGWTVYPPLAGNLAHAGGSVDLAIFSLHLAGVSSILGAVN 160
Cdd:MTH00007 81 PLMLGAPDMAFPRLNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 161 FITTIINMRWRGMQFERLPLFVWSVKITAVLLLLSLPVLAGAITMLLTDRNFNTAFFDPAGGGDPILYQHLFWFFGHPEV 240
Cdd:MTH00007 161 FITTVINMRWKGLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 241 YILILPGFGMISHIVSHYSSKKETFGTLGMIYAMLAIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSW 320
Cdd:MTH00007 241 YILILPGFGAISHIVTHYAGKLEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSW 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 321 LATIHGAKIKYETPMLWALGFIFLFTVGGLTGIVLSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFGAFNYWFPLLSGV 400
Cdd:MTH00007 321 LATIHGSPIKYETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTGL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 401 TLHSRWTKAHFYIMFIGVNVTFFPQHFLGLSGMPRRYSDYPDCYTKWNVISSIGSMISFVAVLYFMVIVWEALVSQRSVI 480
Cdd:MTH00007 401 TLHDRWAKAHFFLMFLGVNLTFFPQHFLGLSGMPRRYSDYPDAYTKWNVVSSFGSMLSFVALLLFIFILWEAFSAQRGVI 480
|
490 500
....*....|....*....|....*.
gi 1238821341 481 WSTHLSTALEWDNILPADFHNSAETG 506
Cdd:MTH00007 481 ASPHMSSSLEWQDTLPLDFHNLPETG 506
|
|
| COX1 |
MTH00183 |
cytochrome c oxidase subunit I; Provisional |
2-504 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177234 Cd Length: 516 Bit Score: 764.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 2 RWLFSTNHKDIGTLYILFGMWSGLVGTALSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVP 81
Cdd:MTH00183 5 RWFFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 82 LMLGAPDMAFPRLNNMSFWLLPPALLLLLSSAAVESGVGTGWTVYPPLAGNLAHAGGSVDLAIFSLHLAGVSSILGAVNF 161
Cdd:MTH00183 85 LMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 162 ITTIINMRWRGMQFERLPLFVWSVKITAVLLLLSLPVLAGAITMLLTDRNFNTAFFDPAGGGDPILYQHLFWFFGHPEVY 241
Cdd:MTH00183 165 ITTIINMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVY 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 242 ILILPGFGMISHIVSHYSSKKETFGTLGMIYAMLAIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWL 321
Cdd:MTH00183 245 ILILPGFGMISHIVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 322 ATIHGAKIKYETPMLWALGFIFLFTVGGLTGIVLSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFGAFNYWFPLLSGVT 401
Cdd:MTH00183 325 ATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLFSGYT 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 402 LHSRWTKAHFYIMFIGVNVTFFPQHFLGLSGMPRRYSDYPDCYTKWNVISSIGSMISFVAVLYFMVIVWEALVSQRSVIW 481
Cdd:MTH00183 405 LHSTWTKIHFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMFLFILWEAFAAKREVLS 484
|
490 500
....*....|....*....|...
gi 1238821341 482 STHLSTALEWDNILPADFHNSAE 504
Cdd:MTH00183 485 VELTSTNVEWLHGCPPPYHTFEE 507
|
|
| COX1 |
MTH00037 |
cytochrome c oxidase subunit I; Provisional |
2-505 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177112 Cd Length: 517 Bit Score: 758.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 2 RWLFSTNHKDIGTLYILFGMWSGLVGTALSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVP 81
Cdd:MTH00037 5 RWLFSTNHKDIGTLYLIFGAWAGMVGTAMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 82 LMLGAPDMAFPRLNNMSFWLLPPALLLLLSSAAVESGVGTGWTVYPPLAGNLAHAGGSVDLAIFSLHLAGVSSILGAVNF 161
Cdd:MTH00037 85 LMIGAPDMAFPRMNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 162 ITTIINMRWRGMQFERLPLFVWSVKITAVLLLLSLPVLAGAITMLLTDRNFNTAFFDPAGGGDPILYQHLFWFFGHPEVY 241
Cdd:MTH00037 165 ITTIINMRTPGMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPEVY 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 242 ILILPGFGMISHIVSHYSSKKETFGTLGMIYAMLAIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWL 321
Cdd:MTH00037 245 ILILPGFGMISHVIAHYSGKQEPFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWM 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 322 ATIHGAKIKYETPMLWALGFIFLFTVGGLTGIVLSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFGAFNYWFPLLSGVT 401
Cdd:MTH00037 325 ATLQGSNLRWETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLFSGVS 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 402 LHSRWTKAHFYIMFIGVNVTFFPQHFLGLSGMPRRYSDYPDCYTKWNVISSIGSMISFVAVLYFMVIVWEALVSQRSVIW 481
Cdd:MTH00037 405 LHPLWSKVHFFLMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSTISLVATLFFLFLIWEAFASQREVIS 484
|
490 500
....*....|....*....|....*
gi 1238821341 482 STHLSTALEWD-NILPADFHNSAET 505
Cdd:MTH00037 485 PEFSSSSLEWQySSFPPSHHTFDET 509
|
|
| COX1 |
MTH00103 |
cytochrome c oxidase subunit I; Validated |
2-504 |
0e+00 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 177165 Cd Length: 513 Bit Score: 752.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 2 RWLFSTNHKDIGTLYILFGMWSGLVGTALSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVP 81
Cdd:MTH00103 5 RWLFSTNHKDIGTLYLLFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 82 LMLGAPDMAFPRLNNMSFWLLPPALLLLLSSAAVESGVGTGWTVYPPLAGNLAHAGGSVDLAIFSLHLAGVSSILGAVNF 161
Cdd:MTH00103 85 LMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 162 ITTIINMRWRGMQFERLPLFVWSVKITAVLLLLSLPVLAGAITMLLTDRNFNTAFFDPAGGGDPILYQHLFWFFGHPEVY 241
Cdd:MTH00103 165 ITTIINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVY 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 242 ILILPGFGMISHIVSHYSSKKETFGTLGMIYAMLAIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWL 321
Cdd:MTH00103 245 ILILPGFGMISHIVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 322 ATIHGAKIKYETPMLWALGFIFLFTVGGLTGIVLSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFGAFNYWFPLLSGVT 401
Cdd:MTH00103 325 ATLHGGNIKWSPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYT 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 402 LHSRWTKAHFYIMFIGVNVTFFPQHFLGLSGMPRRYSDYPDCYTKWNVISSIGSMISFVAVLYFMVIVWEALVSQRSVIW 481
Cdd:MTH00103 405 LNDTWAKIHFTIMFVGVNMTFFPQHFLGLSGMPRRYSDYPDAYTTWNTVSSMGSFISLTAVMLMIFMIWEAFASKREVLT 484
|
490 500
....*....|....*....|...
gi 1238821341 482 STHLSTALEWDNILPADFHNSAE 504
Cdd:MTH00103 485 VELTTTNLEWLHGCPPPYHTFEE 507
|
|
| COX1 |
MTH00077 |
cytochrome c oxidase subunit I; Provisional |
2-505 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214419 Cd Length: 514 Bit Score: 747.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 2 RWLFSTNHKDIGTLYILFGMWSGLVGTALSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVP 81
Cdd:MTH00077 5 RWLFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 82 LMLGAPDMAFPRLNNMSFWLLPPALLLLLSSAAVESGVGTGWTVYPPLAGNLAHAGGSVDLAIFSLHLAGVSSILGAVNF 161
Cdd:MTH00077 85 LMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 162 ITTIINMRWRGMQFERLPLFVWSVKITAVLLLLSLPVLAGAITMLLTDRNFNTAFFDPAGGGDPILYQHLFWFFGHPEVY 241
Cdd:MTH00077 165 ITTSINMKPPSMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVY 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 242 ILILPGFGMISHIVSHYSSKKETFGTLGMIYAMLAIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWL 321
Cdd:MTH00077 245 ILILPGFGMISHIVTYYSAKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVFSWL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 322 ATIHGAKIKYETPMLWALGFIFLFTVGGLTGIVLSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFGAFNYWFPLLSGVT 401
Cdd:MTH00077 325 ATMHGGAIKWDAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYT 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 402 LHSRWTKAHFYIMFIGVNVTFFPQHFLGLSGMPRRYSDYPDCYTKWNVISSIGSMISFVAVLYFMVIVWEALVSQRSVIW 481
Cdd:MTH00077 405 LHSTWSKIHFGVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMMMFIIWEAFSSKREVLT 484
|
490 500
....*....|....*....|....
gi 1238821341 482 STHLSTALEWDNILPADFHNSAET 505
Cdd:MTH00077 485 TELTSTNIEWLHGCPPPYHTFEEP 508
|
|
| COX1 |
MTH00182 |
cytochrome c oxidase subunit I; Provisional |
2-504 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214451 Cd Length: 525 Bit Score: 702.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 2 RWLFSTNHKDIGTLYILFGMWSGLVGTALSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVP 81
Cdd:MTH00182 7 RWVFSTNHKDIGTLYLVFGAGAGMIGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 82 LMLGAPDMAFPRLNNMSFWLLPPALLLLLSSAAVESGVGTGWTVYPPLAGNLAHAGGSVDLAIFSLHLAGVSSILGAVNF 161
Cdd:MTH00182 87 LYIGAPDMAFPRLNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 162 ITTIINMRWRGMQFERLPLFVWSVKITAVLLLLSLPVLAGAITMLLTDRNFNTAFFDPAGGGDPILYQHLFWFFGHPEVY 241
Cdd:MTH00182 167 ITTIFNMRAPGVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVY 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 242 ILILPGFGMISHIVSHYSSKKETFGTLGMIYAMLAIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWL 321
Cdd:MTH00182 247 ILILPGFGMISQIIPTFVAKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWL 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 322 ATIHGAKIKYETPMLWALGFIFLFTVGGLTGIVLSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFGAFNYWFPLLSGVT 401
Cdd:MTH00182 327 ATIYGGTLRLDTPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYC 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 402 LHSRWTKAHFYIMFIGVNVTFFPQHFLGLSGMPRRYSDYPDCYTKWNVISSIGSMISFVAVLYFMVIVWEALVSQRSVI- 480
Cdd:MTH00182 407 YNELYGKIHFWLMFIGVNLTFFPQHFLGLAGFPRRYSDFADAFAGWNLVSSLGSIISIVGVVWFIYIIYDAYVREEKFIg 486
|
490 500
....*....|....*....|....*..
gi 1238821341 481 WSTHLST---ALEWDNILPADFHNSAE 504
Cdd:MTH00182 487 WKEGTGEswaSLEWVHSSPPLFHTYNE 513
|
|
| COX1 |
MTH00184 |
cytochrome c oxidase subunit I; Provisional |
2-504 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177235 Cd Length: 519 Bit Score: 687.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 2 RWLFSTNHKDIGTLYILFGMWSGLVGTALSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVP 81
Cdd:MTH00184 7 RWLFSTNHKDIGTLYLLFGAFAGMIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 82 LMLGAPDMAFPRLNNMSFWLLPPALLLLLSSAAVESGVGTGWTVYPPLAGNLAHAGGSVDLAIFSLHLAGVSSILGAVNF 161
Cdd:MTH00184 87 LYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 162 ITTIINMRWRGMQFERLPLFVWSVKITAVLLLLSLPVLAGAITMLLTDRNFNTAFFDPAGGGDPILYQHLFWFFGHPEVY 241
Cdd:MTH00184 167 ITTIFNMRAPGITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVY 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 242 ILILPGFGMISHIVSHYSSKKETFGTLGMIYAMLAIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWL 321
Cdd:MTH00184 247 ILILPGFGIISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWI 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 322 ATIHGAKIKYETPMLWALGFIFLFTVGGLTGIVLSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFGAFNYWFPLLSGVT 401
Cdd:MTH00184 327 ATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGYC 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 402 LHSRWTKAHFYIMFIGVNVTFFPQHFLGLSGMPRRYSDYPDCYTKWNVISSIGSMISFVAVLYFMVIVWEALVSQRSVI- 480
Cdd:MTH00184 407 YNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDSFAGWNQISSLGSVISIVGVVWFIYIVYDAYVREIKFVg 486
|
490 500
....*....|....*....|....*.
gi 1238821341 481 WS--THLSTALEWDNILPADFHNSAE 504
Cdd:MTH00184 487 WVedSGHYPSLEWAQTSPPAHHTYNE 512
|
|
| COX1 |
MTH00079 |
cytochrome c oxidase subunit I; Provisional |
1-491 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177148 Cd Length: 508 Bit Score: 664.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 1 MRWLFSTNHKDIGTLYILFGMWSGLVGTALSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLV 80
Cdd:MTH00079 5 SVWLESSNHKDIGTLYFLFGLWSGMVGTSLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWML 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 81 PLMLGAPDMAFPRLNNMSFWLLPPALLLLLSSAAVESGVGTGWTVYPPLAgNLAHAGGSVDLAIFSLHLAGVSSILGAVN 160
Cdd:MTH00079 85 PLMLGAPDMSFPRLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLS-TLGHPGSSVDLAIFSLHCAGISSILGGIN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 161 FITTIINMRWRGMQFERLPLFVWSVKITAVLLLLSLPVLAGAITMLLTDRNFNTAFFDPAGGGDPILYQHLFWFFGHPEV 240
Cdd:MTH00079 164 FMVTTKNLRSSSISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPEV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 241 YILILPGFGMISHIVSHYSSKKETFGTLGMIYAMLAIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSW 320
Cdd:MTH00079 244 YILILPAFGIISQSTLYLTGKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSW 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 321 LATIHGAKIKYETPMLWALGFIFLFTVGGLTGIVLSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFGAFNYWFPLLSGV 400
Cdd:MTH00079 324 LATLFGMKMKFQPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFMTGI 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 401 TLHSRWTKAHFYIMFIGVNVTFFPQHFLGLSGMPRRYSDYPDCYTKWNVISSIGSMISFVAVLYFMVIVWEALVSQRSVI 480
Cdd:MTH00079 404 VYDKLMMSAVFFLMFVGVNLTFFPLHFAGLHGMPRKYLDYPDVYSVWNVISSYGSMISVFALFLFIYVLLESFFSYRLVL 483
|
490
....*....|.
gi 1238821341 481 WSTHLSTALEW 491
Cdd:MTH00079 484 HDNYINSSPEY 494
|
|
| COX1 |
MTH00026 |
cytochrome c oxidase subunit I; Provisional |
1-472 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 164599 Cd Length: 534 Bit Score: 615.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 1 MRWLFSTNHKDIGTLYILFGMWSGLVGTALSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLV 80
Cdd:MTH00026 5 VRWFFSCNHKDIGSLYLVFGALSGAIGTAFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 81 PLMLGAPDMAFPRLNNMSFWLLPPALLLLLSSAAVESGVGTGWTVYPPLAGNLAHAGGSVDLAIFSLHLAGVSSILGAVN 160
Cdd:MTH00026 85 PLMIGAPDMAFPRLNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMN 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 161 FITTIINMRWRGMQFERLPLFVWSVKITAVLLLLSLPVLAGAITMLLTDRNFNTAFFDPAGGGDPILYQHLFWFFGHPEV 240
Cdd:MTH00026 165 FITTVMNMRTPGMTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEV 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 241 YILILPGFGMISHIVSHYSSKKETFGTLGMIYAMLAIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSW 320
Cdd:MTH00026 245 YILILPGFGIISQILSLFSYKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSW 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 321 LATIHGA--KIKYETPMLWALGFIFLFTVGGLTGIVLSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFGAFNYWFPLLS 398
Cdd:MTH00026 325 LATVSGSgrNLIFTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWFGKIT 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1238821341 399 GVTLHSRWTKAHFYIMFIGVNVTFFPQHFLGLSGMPRRYSDYPDCYTKWNVISSIGSMISFVAVLYFMVIVWEA 472
Cdd:MTH00026 405 GYAYKDIYGLIHFWLMFIGVNITFFPQHFLGLAGLPRRYADYPDNFEDFNQISSFGSIISIIAVIWFIVVIFDA 478
|
|
| Heme_Cu_Oxidase_I |
cd00919 |
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ... |
9-473 |
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: 595.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 9 HKDIGTLYILFGMWSGLVGTALSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVPlMLGAPD 88
Cdd:cd00919 1 HKDIGLLYLIFAFVALLLGGLLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 89 MAFPRLNNMSFWLLPPALLLLLSSAAVESGVGTGWTVYPPLAGNLAHAGGSVDLAIFSLHLAGVSSILGAVNFITTIINM 168
Cdd:cd00919 80 LAFPRLNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 169 RWRGMQFERLPLFVWSVKITAVLLLLSLPVLAGAITMLLTDRNFNTAFFDPAGGGDPILYQHLFWFFGHPEVYILILPGF 248
Cdd:cd00919 160 RAPGMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 249 GMISHIVSHYSsKKETFGTLGMIYAMLAIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGAK 328
Cdd:cd00919 240 GAISEIIPTFS-GKPLFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 329 IKYETPMLWALGFIFLFTVGGLTGIVLSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFGAFNYWFPLLSGVTLHSRWTK 408
Cdd:cd00919 319 IRFDPPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKLGK 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1238821341 409 AHFYIMFIGVNVTFFPQHFLGLSGMPRRYSDYPDCYTKWNVISSIGSMISFVAVLYFMVIVWEAL 473
Cdd:cd00919 399 IHFWLWFIGFNLTFFPMHFLGLLGMPRRYADYPDGFAPWNFISSVGAFILGLGLLLFLGNLFLSL 463
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
4-501 |
0e+00 |
|
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) of cytochrome c oxidases of bacterial origin. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits I-III form the functional core of the enzyme complex. Subunit I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit II and heme a of subunit I to the bimetallic center formed by heme a3 and copper B. This cytochrome c oxidase shows proton pump activity across the membrane in addition to the electron transfer. In the bacilli an apparent split (paralogism) has created a sister clade (TIGR02882) encoding subunits (QoxA) of the aa3-type quinone oxidase complex which reacts directly with quinones, bypassing the interaction with soluble cytochrome c. This model attempts to exclude these sequences, placing them between the trusted and noise cutoffs. These families, as well as archaeal and eukaryotic cytochrome c subunit I's are included within the superfamily model, pfam00115. [Energy metabolism, Electron transport]
Pssm-ID: 213748 Cd Length: 499 Bit Score: 571.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 4 LFSTNHKDIGTLYILFGMWSGLVGTALSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMiGGFGNWLVPLM 83
Cdd:TIGR02891 1 LTTVDHKRIGILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIPIL-AGFGNYLLPLM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 84 LGAPDMAFPRLNNMSFWLLPPALLLLLSSAAVESGVGTGWTVYPPLAGNLAHAGGSVDLAIFSLHLAGVSSILGAVNFIT 163
Cdd:TIGR02891 80 IGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 164 TIINMRWRGMQFERLPLFVWSVKITAVLLLLSLPVLAGAITMLLTDRNFNTAFFDPAGGGDPILYQHLFWFFGHPEVYIL 243
Cdd:TIGR02891 160 TILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYII 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 244 ILPGFGMISHIVSHYsSKKETFGTLGMIYAMLAIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLAT 323
Cdd:TIGR02891 240 FLPAFGIISEILPTF-ARKPIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIAT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 324 IHGAKIKYETPMLWALGFIFLFTVGGLTGIVLSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFGAFNYWFPLLSGVTLH 403
Cdd:TIGR02891 319 LWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYN 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 404 SRWTKAHFYIMFIGVNVTFFPQHFLGLSGMPRRYSDYPD--CYTKWNVISSIGSMISFVAVLYFMVIVWEALVSQRSV-- 479
Cdd:TIGR02891 399 ERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPqmGFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGPKAga 478
|
490 500
....*....|....*....|...
gi 1238821341 480 -IWSthlSTALEWDNILPADFHN 501
Cdd:TIGR02891 479 nPWG---ATTLEWTTSSPPPAHN 498
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
1-505 |
0e+00 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 566.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 1 MRWLFSTNHKDIGTLYILFGMWSGLVGTALSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMmIGGFGNWLV 80
Cdd:COG0843 7 RRWLTTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATPF-LAGFGNYLV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 81 PLMLGAPDMAFPRLNNMSFWLLPPALLLLLSSAAVESGVGTGWTVYPPLAGNLAHAGGSVDLAIFSLHLAGVSSILGAVN 160
Cdd:COG0843 86 PLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVN 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 161 FITTIINMRWRGMQFERLPLFVWSVKITAVLLLLSLPVLAGAITMLLTDRNFNTAFFDPAGGGDPILYQHLFWFFGHPEV 240
Cdd:COG0843 166 FIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEV 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 241 YILILPGFGMISHIVSHYSSKKeTFGTLGMIYAMLAIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSW 320
Cdd:COG0843 246 YILILPAFGIVSEIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNW 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 321 LATIHGAKIKYETPMLWALGFIFLFTVGGLTGIVLSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFGAFNYWFPLLSGV 400
Cdd:COG0843 325 IATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGR 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 401 TLHSRWTKAHFYIMFIGVNVTFFPQHFLGLSGMPRRYSDYP--DCYTKWNVISSIGSMISFVAVLYFMVIVWEALVSQRS 478
Cdd:COG0843 405 MLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAFILAVGFLLFLINLVVSLRKGPK 484
|
490 500
....*....|....*....|....*..
gi 1238821341 479 VIWSTHLSTALEWDNILPADFHNSAET 505
Cdd:COG0843 485 AGGNPWGARTLEWATPSPPPLYNFASI 511
|
|
| COX1 |
MTH00048 |
cytochrome c oxidase subunit I; Provisional |
1-480 |
2.12e-173 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177123 Cd Length: 511 Bit Score: 498.43 E-value: 2.12e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 1 MRWLFSTNHKDIGTLYILFGMWSGLVGTALSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLV 80
Cdd:MTH00048 5 LSWLFTLDHKRIGVIYTLLGVWSGFVGLSLSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 81 PLMLGAPDMAFPRLNNMSFWLLPPALLLLLSSAAVesGVGTGWTVYPPLAGNLAHAGGSVDLAIFSLHLAGVSSILGAVN 160
Cdd:MTH00048 85 PLLLGLSDLNLPRLNALSAWLLVPSIVFLLLSMCL--GAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSIN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 161 FITTIINMrWRGMQFERLPLFVWSVKITAVLLLLSLPVLAGAITMLLTDRNFNTAFFDPAGGGDPILYQHLFWFFGHPEV 240
Cdd:MTH00048 163 FICTIYSA-FMTNVFSRTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPEV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 241 YILILPGFGMISHIVSHYSSKKETFGTLGMIYAMLAIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSW 320
Cdd:MTH00048 242 YVLILPGFGIISHICLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFSW 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 321 LATIHGAKIKYETPML-WALGFIFLFTVGGLTGIVLSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFGAFNYWFPLLSG 399
Cdd:MTH00048 322 LYMLLNSRVRKSDPVVwWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWPLITG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 400 VTLHSRWTKAHFYIMFIGVNVTFFPQHFLGLSGMPRRYSDYPDCYTKWNVISSIGSMISFVAVLYFMVIVWEALVSQRSV 479
Cdd:MTH00048 402 LSLNKYLLQCHCIISMIGFNLCFFPMHYFGLCGLPRRVCVYEPSYYWINVVCTVGSFISAFSGCFFVFILWESLVVKNEV 481
|
.
gi 1238821341 480 I 480
Cdd:MTH00048 482 L 482
|
|
| Ubiquinol_Oxidase_I |
cd01662 |
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ... |
3-501 |
4.19e-172 |
|
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: 494.79 E-value: 4.19e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 3 WLFSTNHKDIGTLYILFGMWSGLVGTALSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGgFGNWLVPL 82
Cdd:cd01662 1 WLTTVDHKRIGIMYIITAFVFFLRGGVDALLMRTQLALPGNDFLSPEHYNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 83 MLGAPDMAFPRLNNMSFWLLPPALLLLLSSAAVESGVGTGWTVYPPLAGNLAHAGGSVDLAIFSLHLAGVSSILGAVNFI 162
Cdd:cd01662 80 QIGARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 163 TTIINMRWRGMQFERLPLFVWSVKITAVLLLLSLPVLAGAITMLLTDRNFNTAFFDPAGGGDPILYQHLFWFFGHPEVYI 242
Cdd:cd01662 160 VTILKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 243 LILPGFGMISHIVSHYSsKKETFGTLGMIYAMLAIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLA 322
Cdd:cd01662 240 LILPAFGIFSEIVPTFS-RKPLFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 323 TIHGAKIKYETPMLWALGFIFLFTVGGLTGIVLSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFGAFNYWFPLLSGVTL 402
Cdd:cd01662 319 TMWRGRIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRML 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 403 HSRWTKAHFYIMFIGVNVTFFPQHFLGLSGMPRRYSDYP--DCYTKWNVISSIGSMISFVAVLYFMV-IVWEALVSQRSV 479
Cdd:cd01662 399 NERLGKWSFWLWFIGFNLTFFPMHILGLMGMPRRVYTYLpgPGWDPLNLISTIGAFLIAAGVLLFLInVIVSIRKGKRDA 478
|
490 500
....*....|....*....|..
gi 1238821341 480 IWSTHLSTALEWDNILPADFHN 501
Cdd:cd01662 479 TGDPWGARTLEWATSSPPPAYN 500
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
11-457 |
1.67e-132 |
|
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: 391.17 E-value: 1.67e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 11 DIGTLYILFGMWSGLVGTALSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMmIGGFGNWLVPLMLGAPDMA 90
Cdd:pfam00115 1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATPF-LFGFGNYLVPLMIGARDMA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 91 FPRLNNMSFWLLPPALLLLLSSAAvesGVGTGWTVYPPLAGnlahaggsVDLAIFSLHLAGVSSILGAVNFITTIINMRW 170
Cdd:pfam00115 80 FPRLNALSFWLVVLGAVLLLASFG---GATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 171 RGMQFeRLPLFVWSVKITAVLLLLSLPVLAGAITMLLTDRNFNtaffdpAGGGDPILYQHLFWFFGHPEVYILILPGFGM 250
Cdd:pfam00115 149 PGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 251 ISHIVSHYSsKKETFGTLGMIYAMLAIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLATIHGAKIK 330
Cdd:pfam00115 222 IYYILPKFA-GRPLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIR 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 331 -YETPMLWALGFIFLFTVGGLTGIVLSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFGAFNYWFPLLSGVTLHSRWTKA 409
Cdd:pfam00115 301 fRTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKL 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1238821341 410 HFYIMFIGVNVTFFPQHFLGLSGMPRRYS----DYPDCYTKWNVISSIGSMI 457
Cdd:pfam00115 381 HFWLLFIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPLNWIRTIGGVL 432
|
|
| CyoB |
TIGR02843 |
cytochrome o ubiquinol oxidase, subunit I; Cytochrome o terminal oxidase complex is the ... |
3-505 |
2.92e-122 |
|
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: 372.08 E-value: 2.92e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 3 WLFSTNHKDIGTLYILFGMWSGLVGTALSLLIRAEL-----GQPGALLGDDqlYNVIVTAHAFVMIFFLVMPMMIGGFgN 77
Cdd:TIGR02843 47 WLTTVDHKKIGIMYIIVALVMLLRGFADAIMMRTQQalasgGSAGYLPPHH--YDQIFTAHGVIMIFFVAMPFVFGLM-N 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 78 WLVPLMLGAPDMAFPRLNNMSFWLLPPALLLLLSSAAVESGVGTGWTVYPPLAGNLAHAGGSVDLAIFSLHLAGVSSILG 157
Cdd:TIGR02843 124 LVVPLQIGARDVAFPFLNSLSFWLTVVGAILVNVSLGVGEFAQTGWLAYPPLSELQYSPGVGVDYYIWALQISGIGTLLT 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 158 AVNFITTIINMRWRGMQFERLPLFVWSVKITAVLLLLSLPVLAGAITMLLTDRNFNTAFFDPAGGGDPILYQHLFWFFGH 237
Cdd:TIGR02843 204 GINFFVTIIKMRAPGMTLMKMPVFTWTSLCSNVLIIASFPILTVTLALLTLDRYLGMHFFTNEAGGNPMMYVNLIWAWGH 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 238 PEVYILILPGFGMISHIVSHYSSKKeTFGTLGMIYAMLAIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKV 317
Cdd:TIGR02843 284 PEVYILILPAFGIFSEVVATFSRKR-LFGYTSMVWATIAITVLSFIVWLHHFFTMGAGANVNAFFGIATMIIAIPTGVKI 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 318 FSWLATIHGAKIKYETPMLWALGFIFLFTVGGLTGIVLSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFGAFNYWFPLL 397
Cdd:TIGR02843 363 FNWLFTMYKGRIRFETPMLWTIGFMVTFSIGGMTGVLLAVPPADFVLHNSLFLIAHFHNVIIGGVVFGCFAGLTYWFPKA 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 398 SGVTLHSRWTKAHFYIMFIGVNVTFFPQHFLGLSGMPRRYSDYPD-CYTKWNVISSIGSMISFVAVLYFMVIVWEAlVSQ 476
Cdd:TIGR02843 443 FGFKLNEKLGKRSFWCWFIGFYLAFMPLYILGFMGMTRRLNHYDNpEWHPMLIIAAFGAFLIACGILCQIIQIFVS-IRD 521
|
490 500 510
....*....|....*....|....*....|...
gi 1238821341 477 RSVIWSTHLST----ALEWDNILPADFHNSAET 505
Cdd:TIGR02843 522 RDQNRDTTGDPwggrTLEWSTSSPPPFYNFAVI 554
|
|
| QoxB |
TIGR02882 |
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ... |
3-505 |
6.77e-115 |
|
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: 353.00 E-value: 6.77e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 3 WLFSTNHKDIGTLYILFGMWSGLVGTALSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGgFGNWLVPL 82
Cdd:TIGR02882 44 WLTTVDHKKIGVMYIICAVLMLFRGGIDALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 83 MLGAPDMAFPRLNNMSFWLLPPALLLLLSSAAVESGVGTGWTVYPPLAGNLAHAGGSVDLAIFSLHLAGVSSILGAVNFI 162
Cdd:TIGR02882 123 QIGARDVAFPVLNALSFWLFFAGAMLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFF 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 163 TTIINMRWRGMQFERLPLFVWSVKITAVLLLLSLPVLAGAITMLLTDRNFNTAFFDPAGGGDPILYQHLFWFFGHPEVYI 242
Cdd:TIGR02882 203 VTILKMRAPGMKLMQMPMFTWTTLITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLFWIWGHPEVYI 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 243 LILPGFGMISHIVSHYsSKKETFGTLGMIYAMLAIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWLA 322
Cdd:TIGR02882 283 VILPAFGIYSEIISTF-AQKRLFGYKSMVWSTVGIAFLSFLVWVHHFFTMGNGALINSFFSITTMAIAIPTGVKIFNWLL 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 323 TIHGAKIKYETPMLWALGFIFLFTVGGLTGIVLSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFGAFNYWFPLLSGVTL 402
Cdd:TIGR02882 362 TLYKGKIRFTTPMLFSLAFIPNFLIGGVTGVMLAMASADYQYHNTYFLVAHFHYVLITGVVFACLAGLIYWYPKMFGYKL 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 403 HSRWTKAHFYIMFIGVNVTFFPQHFLGLSGMPRRYSDY--PDCYTKWNVISSIGSMISFVAVLYFMV-IVWEALVSQRSV 479
Cdd:TIGR02882 442 NERLGKWCFWFFMIGFNVCFFPMYILGLDGMPRRMYTYspSDGWFPLNLISTIGALLMAIGFIFLVYnIYYSHRKSPREA 521
|
490 500
....*....|....*....|....*.
gi 1238821341 480 IWSTHLSTALEWDNILPADFHNSAET 505
Cdd:TIGR02882 522 TGDPWNGRTLEWATASPPPKYNFAVT 547
|
|
| PRK15017 |
PRK15017 |
cytochrome o ubiquinol oxidase subunit I; Provisional |
3-503 |
4.23e-104 |
|
cytochrome o ubiquinol oxidase subunit I; Provisional
Pssm-ID: 184978 Cd Length: 663 Bit Score: 325.74 E-value: 4.23e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 3 WLFSTNHKDIGTLYILFGMWSGLVGTALSLLIR-----AELGQPGALlgDDQLYNVIVTAHAFVMIFFLVMPMMIGgFGN 77
Cdd:PRK15017 48 WLTSVDHKRLGIMYIIVAIVMLLRGFADAIMMRsqqalASAGEAGFL--PPHHYDQIFTAHGVIMIFFVAMPFVIG-LMN 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 78 WLVPLMLGAPDMAFPRLNNMSFWLLPPALLLLLSSAAVESGVGTGWTVYPPLAGNLAHAGGSVDLAIFSLHLAGVSSILG 157
Cdd:PRK15017 125 LVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTTLT 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 158 AVNFITTIINMRWRGMQFERLPLFVWSVKITAVLLLLSLPVLAGAITMLLTDRNFNTAFFDPAGGGDPILYQHLFWFFGH 237
Cdd:PRK15017 205 GINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWGH 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 238 PEVYILILPGFGMISHIVSHYSsKKETFGTLGMIYAMLAIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKV 317
Cdd:PRK15017 285 PEVYILILPVFGVFSEIAATFS-RKRLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVKI 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 318 FSWLATIHGAKIKYETPMLWALGFIFLFTVGGLTGIVLSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFGAFNYWFPLL 397
Cdd:PRK15017 364 FNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYWWPKA 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 398 SGVTLHSRWTKAHFYIMFIGVNVTFFPQHFLGLSGMPRRYSDYPD-CYTKWNVISSIGSMISFVAVLYFMVIVWEALVSQ 476
Cdd:PRK15017 444 FGFKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMTRRLSQQIDpQFHTMLMIAASGAALIALGILCQVIQMYVSIRDR 523
|
490 500 510
....*....|....*....|....*....|
gi 1238821341 477 ---RSVIWSTHLSTALEWDNILPADFHNSA 503
Cdd:PRK15017 524 dqnRDLTGDPWGGRTLEWATSSPPPFYNFA 553
|
|
| ba3-like_Oxidase_I |
cd01660 |
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ... |
17-469 |
2.14e-19 |
|
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are transmembrane protein complexes in the respiratory chains of prokaryotes and some archaea which catalyze the reduction of O2 and simultaneously pump protons across the membrane. It has been proposed that Archaea acquired heme-copper oxidases through gene transfer from Gram-positive bacteria. The ba3 family contains oxidases that lack the conserved residues that form the D- and K-pathways in CcO and ubiquinol oxidase. Instead they contain a potential alternative K-pathway. Additional proton channels have been proposed for this family of oxidases but none have been identified definitively. For general information on the heme-copper oxidase superfamily, please see cd00919.
Pssm-ID: 238830 Cd Length: 473 Bit Score: 90.81 E-value: 2.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 17 ILFGMWSGLVGTALslliraelgqpGALLGDDQLYNVIVTAHAFVMIFFLVMpMMIGGFGNWLVPLMLGAPDMAfPRLNN 96
Cdd:cd01660 21 GLFGLLQVLVRTGV-----------FPLPSSGILYYQGLTLHGVLLAIVFTT-FFIMGFFYAIVARALLRSLFN-RRLAW 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 97 MSFWLLPPALLLLLSSaaVESGVGTG-WTVYPPLAGNLAHAGGSVDLAIFSLhlagvssILGAVNFITTIInmRWRGMQF 175
Cdd:cd01660 88 AGFWLMVIGTVMAAVP--ILLGQASVlYTFYPPLQAHPLFYIGAALVVVGSW-------ISGFAMFVTLWR--WKKANPG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 176 ERLPLFVWSVKITAVLLLLSLPVLAGAITMLLTDRNFNTAffdpaGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIV 255
Cdd:cd01660 157 KKVPLATFMVVTTMILWLVASLGVALEVLFQLLPWSLGLV-----DTVDVLLSRTLFWWFGHPLVYFWLLPAYIAWYTIL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 256 SHYSSKKETFGTLGMIyAMLAIGVLGFIVWAHHMFT-VGMDVDTRAYFTAATMIIAVPTGIKVFSWLATI-HGAKIK--- 330
Cdd:cd01660 232 PKIAGGKLFSDPLARL-AFILFLLFSTPVGFHHQFAdPGIGPGWKFIHMVLTFMVALPSLLTAFTVFASLeIAGRLRggk 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 331 ----------YETPMLWALGF-IFLFTVGGLTGIVLSNSSLDIMLHDTYYVVAHFHyvLSMGAVFAL-FGAFNYWF-PLL 397
Cdd:cd01660 311 glfgwiralpWGDPMFLALFLaMLMFIPGGAGGIINASYQLNYVVHNTAWVPGHFH--LTVGGAVALtFMAVAYWLvPHL 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1238821341 398 SGVTLHSRW-TKAHFYIMFIGVNVTFFPQHFLGLSGMPRR--YSDYPDCY-----TKWNVISSIGSMISFVAVLYFMVIV 469
Cdd:cd01660 389 TGRELAAKRlALAQPWLWFVGMTIMSTAMHVAGLLGAPRRtaEAQYGGLPaagewAPYQQLMAIGGTILFVSGALFLYIL 468
|
|
| |
