|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
2-506 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 938.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 2 LTRWVFSTNHKDIGTLYLLFGAWAGMIGTGLSLLIRAELSQPGTLLGDDQIFNVLVTAHAFVMIFFMVMPILIGGFGNWL 81
Cdd:MTH00153 1 MNKWLFSTNHKDIGTLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 82 VPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGVGTGWTVYPPLAGNMAHAGPSVDLAIFSLHLAGVSSILGAI 161
Cdd:MTH00153 81 VPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 162 NFITTIMNMKPPSASQHQTPLFVWSVYITAILLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPE 241
Cdd:MTH00153 161 NFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 242 VYILILPGFGIVSHVVAASCGKKEPFGYMGMVWAMLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFS 321
Cdd:MTH00153 241 VYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 322 WLATMYGGNIKWDAPFLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVYWFPLFTG 401
Cdd:MTH00153 321 WLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 402 FSLNDSWSKIQFYIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTISSIGSMISLIGVMVLMFIIWEAFVSKRPT 481
Cdd:MTH00153 401 LTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPV 480
|
490 500
....*....|....*....|....*
gi 575669765 482 PGVNFPATNVEWRLNFPPHYHTFEE 506
Cdd:MTH00153 481 LFSLNLSSSIEWLQNLPPAEHSYSE 505
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
9-493 |
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: 881.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 9 TNHKDIGTLYLLFGAWAGMIGTGLSLLIRAELSQPGTLLGDDQIFNVLVTAHAFVMIFFMVMPILIGGFGNWLVPLMIGA 88
Cdd:cd01663 1 TNHKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 89 PDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGVGTGWTVYPPLAGNMAHAGPSVDLAIFSLHLAGVSSILGAINFITTIM 168
Cdd:cd01663 81 PDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 169 NMKPPSASQHQTPLFVWSVYITAILLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILP 248
Cdd:cd01663 161 NMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 249 GFGIVSHVVAASCGKKEPFGYMGMVWAMLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMYG 328
Cdd:cd01663 241 GFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 329 GNIKWDAPFLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVYWFPLFTGFSLNDSW 408
Cdd:cd01663 321 GSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 409 SKIQFYIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTISSIGSMISLIGVMVLMFIIWEAFVSKRPTPG-VNFP 487
Cdd:cd01663 401 GKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFnVGEG 480
|
....*.
gi 575669765 488 ATNVEW 493
Cdd:cd01663 481 STSLEW 486
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
2-507 |
0e+00 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 582.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 2 LTRWVFSTNHKDIGTLYLLFGAWAGMIGTGLSLLIRAELSQPGTLLGDDQIFNVLVTAHAFVMIFFMVMPIlIGGFGNWL 81
Cdd:COG0843 6 WRRWLTTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATPF-LAGFGNYL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 82 VPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGVGTGWTVYPPLAGNMAHAGPSVDLAIFSLHLAGVSSILGAI 161
Cdd:COG0843 85 VPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 162 NFITTIMNMKPPSASQHQTPLFVWSVYITAILLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPE 241
Cdd:COG0843 165 NFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 242 VYILILPGFGIVSHVVAASCGKKePFGYMGMVWAMLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFS 321
Cdd:COG0843 245 VYILILPAFGIVSEIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFN 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 322 WLATMYGGNIKWDAPFLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVYWFPLFTG 401
Cdd:COG0843 324 WIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTG 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 402 FSLNDSWSKIQFYIMFIGVNLTFFPQHFLGLAGMPRRYSDYP--DAYTLWNTISSIGSMISLIGVMVLMFIIWEAFVSKR 479
Cdd:COG0843 404 RMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAFILAVGFLLFLINLVVSLRKGP 483
|
490 500
....*....|....*....|....*...
gi 575669765 480 PTPGVNFPATNVEWRLNFPPHYHTFEEP 507
Cdd:COG0843 484 KAGGNPWGARTLEWATPSPPPLYNFASI 511
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
6-504 |
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: 566.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 6 VFSTNHKDIGTLYLLFGAWAGMIGTGLSLLIRAELSQPGTLLGDDQIFNVLVTAHAFVMIFFMVMPILiGGFGNWLVPLM 85
Cdd:TIGR02891 1 LTTVDHKRIGILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIPIL-AGFGNYLLPLM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 86 IGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGVGTGWTVYPPLAGNMAHAGPSVDLAIFSLHLAGVSSILGAINFIT 165
Cdd:TIGR02891 80 IGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 166 TIMNMKPPSASQHQTPLFVWSVYITAILLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYIL 245
Cdd:TIGR02891 160 TILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYII 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 246 ILPGFGIVSHVVAASCGKKePFGYMGMVWAMLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLAT 325
Cdd:TIGR02891 240 FLPAFGIISEILPTFARKP-IFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIAT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 326 MYGGNIKWDAPFLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVYWFPLFTGFSLN 405
Cdd:TIGR02891 319 LWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYN 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 406 DSWSKIQFYIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDA--YTLWNTISSIGSMISLIGVMVLMFIIWEAFVSKRPTPG 483
Cdd:TIGR02891 399 ERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGPKAGA 478
|
490 500
....*....|....*....|.
gi 575669765 484 VNFPATNVEWRLNFPPHYHTF 504
Cdd:TIGR02891 479 NPWGATTLEWTTSSPPPAHNF 499
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
13-459 |
1.19e-135 |
|
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: 399.25 E-value: 1.19e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 13 DIGTLYLLFGAWAGMIGTGLSLLIRAELSQPGTLLGDDQIFNVLVTAHAFVMIFFMVMPIlIGGFGNWLVPLMIGAPDMA 92
Cdd:pfam00115 1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATPF-LFGFGNYLVPLMIGARDMA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 93 FPRMNNMSFWLLPPSFLLLLASStveAGVGTGWTVYPPLAGnmahagpsVDLAIFSLHLAGVSSILGAINFITTIMNMKP 172
Cdd:pfam00115 80 FPRLNALSFWLVVLGAVLLLASF---GGATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 173 PSASQhQTPLFVWSVYITAILLLLSLPVLAAGITMLLTDRNLNttffdpAGGGDPILYQHLFWFFGHPEVYILILPGFGI 252
Cdd:pfam00115 149 PGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 253 VSHVVAASCGKKePFGYMGMVWAMLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMYGGNIK 332
Cdd:pfam00115 222 IYYILPKFAGRP-LFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIR 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 333 W-DAPFLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVYWFPLFTGFSLNDSWSKI 411
Cdd:pfam00115 301 FrTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKL 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 575669765 412 QFYIMFIGVNLTFFPQHFLGLAGMPRRYS----DYPDAYTLWNTISSIGSMI 459
Cdd:pfam00115 381 HFWLLFIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPLNWIRTIGGVL 432
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
2-506 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 938.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 2 LTRWVFSTNHKDIGTLYLLFGAWAGMIGTGLSLLIRAELSQPGTLLGDDQIFNVLVTAHAFVMIFFMVMPILIGGFGNWL 81
Cdd:MTH00153 1 MNKWLFSTNHKDIGTLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 82 VPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGVGTGWTVYPPLAGNMAHAGPSVDLAIFSLHLAGVSSILGAI 161
Cdd:MTH00153 81 VPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 162 NFITTIMNMKPPSASQHQTPLFVWSVYITAILLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPE 241
Cdd:MTH00153 161 NFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 242 VYILILPGFGIVSHVVAASCGKKEPFGYMGMVWAMLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFS 321
Cdd:MTH00153 241 VYILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 322 WLATMYGGNIKWDAPFLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVYWFPLFTG 401
Cdd:MTH00153 321 WLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 402 FSLNDSWSKIQFYIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTISSIGSMISLIGVMVLMFIIWEAFVSKRPT 481
Cdd:MTH00153 401 LTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPV 480
|
490 500
....*....|....*....|....*
gi 575669765 482 PGVNFPATNVEWRLNFPPHYHTFEE 506
Cdd:MTH00153 481 LFSLNLSSSIEWLQNLPPAEHSYSE 505
|
|
| COX1 |
MTH00116 |
cytochrome c oxidase subunit I; Provisional |
1-509 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177177 Cd Length: 515 Bit Score: 929.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 1 MLTRWVFSTNHKDIGTLYLLFGAWAGMIGTGLSLLIRAELSQPGTLLGDDQIFNVLVTAHAFVMIFFMVMPILIGGFGNW 80
Cdd:MTH00116 2 FITRWLFSTNHKDIGTLYLIFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 81 LVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGVGTGWTVYPPLAGNMAHAGPSVDLAIFSLHLAGVSSILGA 160
Cdd:MTH00116 82 LVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 161 INFITTIMNMKPPSASQHQTPLFVWSVYITAILLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHP 240
Cdd:MTH00116 162 INFITTCINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 241 EVYILILPGFGIVSHVVAASCGKKEPFGYMGMVWAMLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVF 320
Cdd:MTH00116 242 EVYILILPGFGIISHIVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVF 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 321 SWLATMYGGNIKWDAPFLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVYWFPLFT 400
Cdd:MTH00116 322 SWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFT 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 401 GFSLNDSWSKIQFYIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTISSIGSMISLIGVMVLMFIIWEAFVSKRP 480
Cdd:MTH00116 402 GYTLHQTWTKAQFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTISSIGSLISMTAVIMLMFIIWEAFSSKRK 481
|
490 500
....*....|....*....|....*....
gi 575669765 481 TPGVNFPATNVEWRLNFPPHYHTFEEPAF 509
Cdd:MTH00116 482 VLQPELTTTNIEWIHGCPPPYHTFEEPAF 510
|
|
| COX1 |
MTH00167 |
cytochrome c oxidase subunit I; Provisional |
1-509 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177222 Cd Length: 512 Bit Score: 900.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 1 MLTRWVFSTNHKDIGTLYLLFGAWAGMIGTGLSLLIRAELSQPGTLLGDDQIFNVLVTAHAFVMIFFMVMPILIGGFGNW 80
Cdd:MTH00167 2 WINRWLFSTNHKDIGTLYFIFGAWAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 81 LVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGVGTGWTVYPPLAGNMAHAGPSVDLAIFSLHLAGVSSILGA 160
Cdd:MTH00167 82 LVPLMIGAPDMAFPRMNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 161 INFITTIMNMKPPSASQHQTPLFVWSVYITAILLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHP 240
Cdd:MTH00167 162 INFITTIINMKPPGITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 241 EVYILILPGFGIVSHVVAASCGKKEPFGYMGMVWAMLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVF 320
Cdd:MTH00167 242 EVYILILPGFGMISHIVVYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVF 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 321 SWLATMYGGNIKWDAPFLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVYWFPLFT 400
Cdd:MTH00167 322 SWLATLHGGKIKWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFT 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 401 GFSLNDSWSKIQFYIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTISSIGSMISLIGVMVLMFIIWEAFVSKRP 480
Cdd:MTH00167 402 GLTLNETWTKIHFFVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNVVSSIGSLISLVAVILFLFIIWEAFSSKRK 481
|
490 500
....*....|....*....|....*....
gi 575669765 481 TPGVNFPATNVEWRLNFPPHYHTFEEPAF 509
Cdd:MTH00167 482 LLPVELTSTNVEWLHGCPPPHHTWEEPPF 510
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
9-493 |
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: 881.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 9 TNHKDIGTLYLLFGAWAGMIGTGLSLLIRAELSQPGTLLGDDQIFNVLVTAHAFVMIFFMVMPILIGGFGNWLVPLMIGA 88
Cdd:cd01663 1 TNHKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 89 PDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGVGTGWTVYPPLAGNMAHAGPSVDLAIFSLHLAGVSSILGAINFITTIM 168
Cdd:cd01663 81 PDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 169 NMKPPSASQHQTPLFVWSVYITAILLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILP 248
Cdd:cd01663 161 NMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 249 GFGIVSHVVAASCGKKEPFGYMGMVWAMLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMYG 328
Cdd:cd01663 241 GFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 329 GNIKWDAPFLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVYWFPLFTGFSLNDSW 408
Cdd:cd01663 321 GSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 409 SKIQFYIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTISSIGSMISLIGVMVLMFIIWEAFVSKRPTPG-VNFP 487
Cdd:cd01663 401 GKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFnVGEG 480
|
....*.
gi 575669765 488 ATNVEW 493
Cdd:cd01663 481 STSLEW 486
|
|
| COX1 |
MTH00077 |
cytochrome c oxidase subunit I; Provisional |
1-512 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214419 Cd Length: 514 Bit Score: 871.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 1 MLTRWVFSTNHKDIGTLYLLFGAWAGMIGTGLSLLIRAELSQPGTLLGDDQIFNVLVTAHAFVMIFFMVMPILIGGFGNW 80
Cdd:MTH00077 2 MITRWLFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 81 LVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGVGTGWTVYPPLAGNMAHAGPSVDLAIFSLHLAGVSSILGA 160
Cdd:MTH00077 82 LVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 161 INFITTIMNMKPPSASQHQTPLFVWSVYITAILLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHP 240
Cdd:MTH00077 162 INFITTSINMKPPSMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 241 EVYILILPGFGIVSHVVAASCGKKEPFGYMGMVWAMLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVF 320
Cdd:MTH00077 242 EVYILILPGFGMISHIVTYYSAKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVF 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 321 SWLATMYGGNIKWDAPFLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVYWFPLFT 400
Cdd:MTH00077 322 SWLATMHGGAIKWDAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFS 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 401 GFSLNDSWSKIQFYIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTISSIGSMISLIGVMVLMFIIWEAFVSKRP 480
Cdd:MTH00077 402 GYTLHSTWSKIHFGVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMMMFIIWEAFSSKRE 481
|
490 500 510
....*....|....*....|....*....|..
gi 575669765 481 TPGVNFPATNVEWRLNFPPHYHTFEEPAFSIK 512
Cdd:MTH00077 482 VLTTELTSTNIEWLHGCPPPYHTFEEPSFVQT 513
|
|
| COX1 |
MTH00183 |
cytochrome c oxidase subunit I; Provisional |
1-509 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177234 Cd Length: 516 Bit Score: 847.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 1 MLTRWVFSTNHKDIGTLYLLFGAWAGMIGTGLSLLIRAELSQPGTLLGDDQIFNVLVTAHAFVMIFFMVMPILIGGFGNW 80
Cdd:MTH00183 2 AITRWFFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 81 LVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGVGTGWTVYPPLAGNMAHAGPSVDLAIFSLHLAGVSSILGA 160
Cdd:MTH00183 82 LIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 161 INFITTIMNMKPPSASQHQTPLFVWSVYITAILLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHP 240
Cdd:MTH00183 162 INFITTIINMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 241 EVYILILPGFGIVSHVVAASCGKKEPFGYMGMVWAMLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVF 320
Cdd:MTH00183 242 EVYILILPGFGMISHIVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVF 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 321 SWLATMYGGNIKWDAPFLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVYWFPLFT 400
Cdd:MTH00183 322 SWLATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLFS 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 401 GFSLNDSWSKIQFYIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTISSIGSMISLIGVMVLMFIIWEAFVSKRP 480
Cdd:MTH00183 402 GYTLHSTWTKIHFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMFLFILWEAFAAKRE 481
|
490 500
....*....|....*....|....*....
gi 575669765 481 TPGVNFPATNVEWRLNFPPHYHTFEEPAF 509
Cdd:MTH00183 482 VLSVELTSTNVEWLHGCPPPYHTFEEPAF 510
|
|
| COX1 |
MTH00103 |
cytochrome c oxidase subunit I; Validated |
1-509 |
0e+00 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 177165 Cd Length: 513 Bit Score: 836.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 1 MLTRWVFSTNHKDIGTLYLLFGAWAGMIGTGLSLLIRAELSQPGTLLGDDQIFNVLVTAHAFVMIFFMVMPILIGGFGNW 80
Cdd:MTH00103 2 FINRWLFSTNHKDIGTLYLLFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 81 LVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGVGTGWTVYPPLAGNMAHAGPSVDLAIFSLHLAGVSSILGA 160
Cdd:MTH00103 82 LVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 161 INFITTIMNMKPPSASQHQTPLFVWSVYITAILLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHP 240
Cdd:MTH00103 162 INFITTIINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 241 EVYILILPGFGIVSHVVAASCGKKEPFGYMGMVWAMLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVF 320
Cdd:MTH00103 242 EVYILILPGFGMISHIVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVF 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 321 SWLATMYGGNIKWDAPFLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVYWFPLFT 400
Cdd:MTH00103 322 SWLATLHGGNIKWSPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFS 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 401 GFSLNDSWSKIQFYIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTISSIGSMISLIGVMVLMFIIWEAFVSKRP 480
Cdd:MTH00103 402 GYTLNDTWAKIHFTIMFVGVNMTFFPQHFLGLSGMPRRYSDYPDAYTTWNTVSSMGSFISLTAVMLMIFMIWEAFASKRE 481
|
490 500
....*....|....*....|....*....
gi 575669765 481 TPGVNFPATNVEWRLNFPPHYHTFEEPAF 509
Cdd:MTH00103 482 VLTVELTTTNLEWLHGCPPPYHTFEEPTY 510
|
|
| COX1 |
MTH00223 |
cytochrome c oxidase subunit I; Provisional |
4-512 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177260 Cd Length: 512 Bit Score: 830.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 4 RWVFSTNHKDIGTLYLLFGAWAGMIGTGLSLLIRAELSQPGTLLGDDQIFNVLVTAHAFVMIFFMVMPILIGGFGNWLVP 83
Cdd:MTH00223 2 RWLFSTNHKDIGTLYLIFGMWSGLVGTSLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 84 LMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGVGTGWTVYPPLAGNMAHAGPSVDLAIFSLHLAGVSSILGAINF 163
Cdd:MTH00223 82 LMLGAPDMAFPRLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 164 ITTIMNMKPPSASQHQTPLFVWSVYITAILLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVY 243
Cdd:MTH00223 162 ITTIINMRSPGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVY 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 244 ILILPGFGIVSHVVAASCGKKEPFGYMGMVWAMLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWL 323
Cdd:MTH00223 242 ILILPGFGMISHIVSHYSSKKEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 324 ATMYGGNIKWDAPFLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVYWFPLFTGFS 403
Cdd:MTH00223 322 ATIYGSKIKYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLFTGVT 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 404 LNDSWSKIQFYIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTISSIGSMISLIGVMVLMFIIWEAFVSKRPTPG 483
Cdd:MTH00223 402 LHRRWAKAHFFLMFLGVNLTFFPQHFLGLAGMPRRYSDYPDCYTKWNQVSSFGSMISFVSVLFFMFIVWEAFVSQRSVVW 481
|
490 500
....*....|....*....|....*....
gi 575669765 484 VNFPATNVEWRLNFPPHYHTFEEPAFSIK 512
Cdd:MTH00223 482 SGHLSTSLEWDNLLPADFHNNSETGALVI 510
|
|
| COX1 |
MTH00142 |
cytochrome c oxidase subunit I; Provisional |
2-507 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214431 Cd Length: 511 Bit Score: 824.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 2 LTRWVFSTNHKDIGTLYLLFGAWAGMIGTGLSLLIRAELSQPGTLLGDDQIFNVLVTAHAFVMIFFMVMPILIGGFGNWL 81
Cdd:MTH00142 1 MMRWLFSTNHKDIGTLYFLFGAWAGMVGTGLSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 82 VPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGVGTGWTVYPPLAGNMAHAGPSVDLAIFSLHLAGVSSILGAI 161
Cdd:MTH00142 81 VPLMLGAPDMAFPRMNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 162 NFITTIMNMKPPSASQHQTPLFVWSVYITAILLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPE 241
Cdd:MTH00142 161 NFITTVINMRAGGMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 242 VYILILPGFGIVSHVVAASCGKKEPFGYMGMVWAMLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFS 321
Cdd:MTH00142 241 VYILILPGFGMISHIINHYSGKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 322 WLATMYGGNIKWDAPFLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVYWFPLFTG 401
Cdd:MTH00142 321 WLATLHGSKVKYEPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLFTG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 402 FSLNDSWSKIQFYIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTISSIGSMISLIGVMVLMFIIWEAFVSKRPT 481
Cdd:MTH00142 401 LTLNPRWLKAHFYTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSSLGSMISFIAVLMFVFIVWESFVSQRLV 480
|
490 500
....*....|....*....|....*.
gi 575669765 482 PGVNFPATNVEWRLNFPPHYHTFEEP 507
Cdd:MTH00142 481 MWSSHLSTSLEWSHRLPPDFHTYDEL 506
|
|
| COX1 |
MTH00037 |
cytochrome c oxidase subunit I; Provisional |
2-515 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177112 Cd Length: 517 Bit Score: 766.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 2 LTRWVFSTNHKDIGTLYLLFGAWAGMIGTGLSLLIRAELSQPGTLLGDDQIFNVLVTAHAFVMIFFMVMPILIGGFGNWL 81
Cdd:MTH00037 3 LSRWLFSTNHKDIGTLYLIFGAWAGMVGTAMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 82 VPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGVGTGWTVYPPLAGNMAHAGPSVDLAIFSLHLAGVSSILGAI 161
Cdd:MTH00037 83 IPLMIGAPDMAFPRMNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 162 NFITTIMNMKPPSASQHQTPLFVWSVYITAILLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPE 241
Cdd:MTH00037 163 NFITTIINMRTPGMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 242 VYILILPGFGIVSHVVAASCGKKEPFGYMGMVWAMLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFS 321
Cdd:MTH00037 243 VYILILPGFGMISHVIAHYSGKQEPFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFS 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 322 WLATMYGGNIKWDAPFLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVYWFPLFTG 401
Cdd:MTH00037 323 WMATLQGSNLRWETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLFSG 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 402 FSLNDSWSKIQFYIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTISSIGSMISLIGVMVLMFIIWEAFVSKRPT 481
Cdd:MTH00037 403 VSLHPLWSKVHFFLMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSTISLVATLFFLFLIWEAFASQREV 482
|
490 500 510
....*....|....*....|....*....|....*
gi 575669765 482 PGVNFPATNVEWRLN-FPPHYHTFEEPAFSIKISR 515
Cdd:MTH00037 483 ISPEFSSSSLEWQYSsFPPSHHTFDETPSTVILIK 517
|
|
| COX1 |
MTH00007 |
cytochrome c oxidase subunit I; Validated |
4-506 |
0e+00 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 133649 Cd Length: 511 Bit Score: 733.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 4 RWVFSTNHKDIGTLYLLFGAWAGMIGTGLSLLIRAELSQPGTLLGDDQIFNVLVTAHAFVMIFFMVMPILIGGFGNWLVP 83
Cdd:MTH00007 2 RWLYSTNHKDIGTLYFILGVWGGLLGTSMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 84 LMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGVGTGWTVYPPLAGNMAHAGPSVDLAIFSLHLAGVSSILGAINF 163
Cdd:MTH00007 82 LMLGAPDMAFPRLNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 164 ITTIMNMKPPSASQHQTPLFVWSVYITAILLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVY 243
Cdd:MTH00007 162 ITTVINMRWKGLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 244 ILILPGFGIVSHVVAASCGKKEPFGYMGMVWAMLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWL 323
Cdd:MTH00007 242 ILILPGFGAISHIVTHYAGKLEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 324 ATMYGGNIKWDAPFLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVYWFPLFTGFS 403
Cdd:MTH00007 322 ATIHGSPIKYETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTGLT 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 404 LNDSWSKIQFYIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTISSIGSMISLIGVMVLMFIIWEAFVSKRPTPG 483
Cdd:MTH00007 402 LHDRWAKAHFFLMFLGVNLTFFPQHFLGLSGMPRRYSDYPDAYTKWNVVSSFGSMLSFVALLLFIFILWEAFSAQRGVIA 481
|
490 500
....*....|....*....|...
gi 575669765 484 VNFPATNVEWRLNFPPHYHTFEE 506
Cdd:MTH00007 482 SPHMSSSLEWQDTLPLDFHNLPE 504
|
|
| COX1 |
MTH00182 |
cytochrome c oxidase subunit I; Provisional |
2-514 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214451 Cd Length: 525 Bit Score: 696.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 2 LTRWVFSTNHKDIGTLYLLFGAWAGMIGTGLSLLIRAELSQPGTLLGDDQIFNVLVTAHAFVMIFFMVMPILIGGFGNWL 81
Cdd:MTH00182 5 LTRWVFSTNHKDIGTLYLVFGAGAGMIGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 82 VPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGVGTGWTVYPPLAGNMAHAGPSVDLAIFSLHLAGVSSILGAI 161
Cdd:MTH00182 85 VPLYIGAPDMAFPRLNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 162 NFITTIMNMKPPSASQHQTPLFVWSVYITAILLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPE 241
Cdd:MTH00182 165 NFITTIFNMRAPGVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 242 VYILILPGFGIVSHVVAASCGKKEPFGYMGMVWAMLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFS 321
Cdd:MTH00182 245 VYILILPGFGMISQIIPTFVAKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFS 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 322 WLATMYGGNIKWDAPFLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVYWFPLFTG 401
Cdd:MTH00182 325 WLATIYGGTLRLDTPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 402 FSLNDSWSKIQFYIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTISSIGSMISLIGVMVLMFIIWEAFVSKRP- 480
Cdd:MTH00182 405 YCYNELYGKIHFWLMFIGVNLTFFPQHFLGLAGFPRRYSDFADAFAGWNLVSSLGSIISIVGVVWFIYIIYDAYVREEKf 484
|
490 500 510
....*....|....*....|....*....|....*..
gi 575669765 481 ---TPGVNFPATNVEWRLNFPPHYHTFEEPAFSIKIS 514
Cdd:MTH00182 485 igwKEGTGESWASLEWVHSSPPLFHTYNELPFVYKSK 521
|
|
| COX1 |
MTH00184 |
cytochrome c oxidase subunit I; Provisional |
2-513 |
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 575669765 2 LTRWVFSTNHKDIGTLYLLFGAWAGMIGTGLSLLIRAELSQPGTLLGDDQIFNVLVTAHAFVMIFFMVMPILIGGFGNWL 81
Cdd:MTH00184 5 LSRWLFSTNHKDIGTLYLLFGAFAGMIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 82 VPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGVGTGWTVYPPLAGNMAHAGPSVDLAIFSLHLAGVSSILGAI 161
Cdd:MTH00184 85 VPLYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAM 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 162 NFITTIMNMKPPSASQHQTPLFVWSVYITAILLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPE 241
Cdd:MTH00184 165 NFITTIFNMRAPGITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 242 VYILILPGFGIVSHVVAASCGKKEPFGYMGMVWAMLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFS 321
Cdd:MTH00184 245 VYILILPGFGIISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFS 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 322 WLATMYGGNIKWDAPFLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVYWFPLFTG 401
Cdd:MTH00184 325 WIATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 402 FSLNDSWSKIQFYIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTISSIGSMISLIGVMVLMFIIWEAFVSKRPT 481
Cdd:MTH00184 405 YCYNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDSFAGWNQISSLGSVISIVGVVWFIYIVYDAYVREIKF 484
|
490 500 510
....*....|....*....|....*....|....*
gi 575669765 482 PGV---NFPATNVEWRLNFPPHYHTFEEPAFSIKI 513
Cdd:MTH00184 485 VGWvedSGHYPSLEWAQTSPPAHHTYNELPYVYKG 519
|
|
| COX1 |
MTH00079 |
cytochrome c oxidase subunit I; Provisional |
2-506 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177148 Cd Length: 508 Bit Score: 664.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 2 LTRWVFSTNHKDIGTLYLLFGAWAGMIGTGLSLLIRAELSQPGTLLGDDQIFNVLVTAHAFVMIFFMVMPILIGGFGNWL 81
Cdd:MTH00079 4 LSVWLESSNHKDIGTLYFLFGLWSGMVGTSLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 82 VPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGVGTGWTVYPPLAgNMAHAGPSVDLAIFSLHLAGVSSILGAI 161
Cdd:MTH00079 84 LPLMLGAPDMSFPRLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLS-TLGHPGSSVDLAIFSLHCAGISSILGGI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 162 NFITTIMNMKPPSASQHQTPLFVWSVYITAILLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPE 241
Cdd:MTH00079 163 NFMVTTKNLRSSSISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 242 VYILILPGFGIVSHVVAASCGKKEPFGYMGMVWAMLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFS 321
Cdd:MTH00079 243 VYILILPAFGIISQSTLYLTGKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFS 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 322 WLATMYGGNIKWDAPFLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVYWFPLFTG 401
Cdd:MTH00079 323 WLATLFGMKMKFQPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFMTG 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 402 FSLNDSWSKIQFYIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTISSIGSMISLIGVMVLMFIIWEAFVSKRPT 481
Cdd:MTH00079 403 IVYDKLMMSAVFFLMFVGVNLTFFPLHFAGLHGMPRKYLDYPDVYSVWNVISSYGSMISVFALFLFIYVLLESFFSYRLV 482
|
490 500
....*....|....*....|....*
gi 575669765 482 PGVNFPATNVEWRLNFPPHYHTFEE 506
Cdd:MTH00079 483 LHDNYINSSPEYSLSSYVFGHSYQS 507
|
|
| COX1 |
MTH00026 |
cytochrome c oxidase subunit I; Provisional |
2-506 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 164599 Cd Length: 534 Bit Score: 598.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 2 LTRWVFSTNHKDIGTLYLLFGAWAGMIGTGLSLLIRAELSQPGTLLGDDQIFNVLVTAHAFVMIFFMVMPILIGGFGNWL 81
Cdd:MTH00026 4 FVRWFFSCNHKDIGSLYLVFGALSGAIGTAFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 82 VPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGVGTGWTVYPPLAGNMAHAGPSVDLAIFSLHLAGVSSILGAI 161
Cdd:MTH00026 84 VPLMIGAPDMAFPRLNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAM 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 162 NFITTIMNMKPPSASQHQTPLFVWSVYITAILLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPE 241
Cdd:MTH00026 164 NFITTVMNMRTPGMTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 242 VYILILPGFGIVSHVVAASCGKKEPFGYMGMVWAMLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFS 321
Cdd:MTH00026 244 VYILILPGFGIISQILSLFSYKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 322 WLATMYGG--NIKWDAPFLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVYWFPLF 399
Cdd:MTH00026 324 WLATVSGSgrNLIFTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWFGKI 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 400 TGFSLNDSWSKIQFYIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTISSIGSMISLIGVMVLMFIIWEAFVSKR 479
Cdd:MTH00026 404 TGYAYKDIYGLIHFWLMFIGVNITFFPQHFLGLAGLPRRYADYPDNFEDFNQISSFGSIISIIAVIWFIVVIFDAYYREE 483
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 575669765 480 P--------TPGVNFPAT-----NVEWRLNFPPHYHTFEE 506
Cdd:MTH00026 484 PfdinimakGPLIPFSCQpahfdTLEWSLTSPPEHHTYNE 523
|
|
| Heme_Cu_Oxidase_I |
cd00919 |
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ... |
11-475 |
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: 597.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 11 HKDIGTLYLLFGAWAGMIGTGLSLLIRAELSQPGTLLGDDQIFNVLVTAHAFVMIFFMVMPILIGGFGNWLVPlMIGAPD 90
Cdd:cd00919 1 HKDIGLLYLIFAFVALLLGGLLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 91 MAFPRMNNMSFWLLPPSFLLLLASSTVEAGVGTGWTVYPPLAGNMAHAGPSVDLAIFSLHLAGVSSILGAINFITTIMNM 170
Cdd:cd00919 80 LAFPRLNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 171 KPPSASQHQTPLFVWSVYITAILLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGF 250
Cdd:cd00919 160 RAPGMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 251 GIVSHVVAASCGKKePFGYMGMVWAMLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMYGGN 330
Cdd:cd00919 240 GAISEIIPTFSGKP-LFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 331 IKWDAPFLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVYWFPLFTGFSLNDSWSK 410
Cdd:cd00919 319 IRFDPPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKLGK 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 575669765 411 IQFYIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTISSIGSMISLIGVMVLMFIIWEAF 475
Cdd:cd00919 399 IHFWLWFIGFNLTFFPMHFLGLLGMPRRYADYPDGFAPWNFISSVGAFILGLGLLLFLGNLFLSL 463
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
2-507 |
0e+00 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 582.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 2 LTRWVFSTNHKDIGTLYLLFGAWAGMIGTGLSLLIRAELSQPGTLLGDDQIFNVLVTAHAFVMIFFMVMPIlIGGFGNWL 81
Cdd:COG0843 6 WRRWLTTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATPF-LAGFGNYL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 82 VPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGVGTGWTVYPPLAGNMAHAGPSVDLAIFSLHLAGVSSILGAI 161
Cdd:COG0843 85 VPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 162 NFITTIMNMKPPSASQHQTPLFVWSVYITAILLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPE 241
Cdd:COG0843 165 NFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 242 VYILILPGFGIVSHVVAASCGKKePFGYMGMVWAMLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFS 321
Cdd:COG0843 245 VYILILPAFGIVSEIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFN 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 322 WLATMYGGNIKWDAPFLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVYWFPLFTG 401
Cdd:COG0843 324 WIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTG 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 402 FSLNDSWSKIQFYIMFIGVNLTFFPQHFLGLAGMPRRYSDYP--DAYTLWNTISSIGSMISLIGVMVLMFIIWEAFVSKR 479
Cdd:COG0843 404 RMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAFILAVGFLLFLINLVVSLRKGP 483
|
490 500
....*....|....*....|....*...
gi 575669765 480 PTPGVNFPATNVEWRLNFPPHYHTFEEP 507
Cdd:COG0843 484 KAGGNPWGARTLEWATPSPPPLYNFASI 511
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
6-504 |
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: 566.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 6 VFSTNHKDIGTLYLLFGAWAGMIGTGLSLLIRAELSQPGTLLGDDQIFNVLVTAHAFVMIFFMVMPILiGGFGNWLVPLM 85
Cdd:TIGR02891 1 LTTVDHKRIGILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIPIL-AGFGNYLLPLM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 86 IGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGVGTGWTVYPPLAGNMAHAGPSVDLAIFSLHLAGVSSILGAINFIT 165
Cdd:TIGR02891 80 IGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 166 TIMNMKPPSASQHQTPLFVWSVYITAILLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYIL 245
Cdd:TIGR02891 160 TILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYII 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 246 ILPGFGIVSHVVAASCGKKePFGYMGMVWAMLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLAT 325
Cdd:TIGR02891 240 FLPAFGIISEILPTFARKP-IFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIAT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 326 MYGGNIKWDAPFLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVYWFPLFTGFSLN 405
Cdd:TIGR02891 319 LWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYN 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 406 DSWSKIQFYIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDA--YTLWNTISSIGSMISLIGVMVLMFIIWEAFVSKRPTPG 483
Cdd:TIGR02891 399 ERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGPKAGA 478
|
490 500
....*....|....*....|.
gi 575669765 484 VNFPATNVEWRLNFPPHYHTF 504
Cdd:TIGR02891 479 NPWGATTLEWTTSSPPPAHNF 499
|
|
| COX1 |
MTH00048 |
cytochrome c oxidase subunit I; Provisional |
1-479 |
1.52e-176 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177123 Cd Length: 511 Bit Score: 506.52 E-value: 1.52e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 1 MLTRWVFSTNHKDIGTLYLLFGAWAGMIGTGLSLLIRAELSQPGTLLGDDQIFNVLVTAHAFVMIFFMVMPILIGGFGNW 80
Cdd:MTH00048 3 SLLSWLFTLDHKRIGVIYTLLGVWSGFVGLSLSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFGNY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 81 LVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASstVEAGVGTGWTVYPPLAGNMAHAGPSVDLAIFSLHLAGVSSILGA 160
Cdd:MTH00048 83 LLPLLLGLSDLNLPRLNALSAWLLVPSIVFLLLS--MCLGAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 161 INFITTIMNMKPPSASqHQTPLFVWSVYITAILLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHP 240
Cdd:MTH00048 161 INFICTIYSAFMTNVF-SRTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 241 EVYILILPGFGIVSHVVAASCGKKEPFGYMGMVWAMLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVF 320
Cdd:MTH00048 240 EVYVLILPGFGIISHICLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVF 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 321 SWLATMYGGNIKWDAPFL-WALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVYWFPLF 399
Cdd:MTH00048 320 SWLYMLLNSRVRKSDPVVwWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWPLI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 400 TGFSLNDSWSKIQFYIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTISSIGSMISLIGVMVLMFIIWEAFVSKR 479
Cdd:MTH00048 400 TGLSLNKYLLQCHCIISMIGFNLCFFPMHYFGLCGLPRRVCVYEPSYYWINVVCTVGSFISAFSGCFFVFILWESLVVKN 479
|
|
| Ubiquinol_Oxidase_I |
cd01662 |
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ... |
5-504 |
1.64e-176 |
|
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: 505.96 E-value: 1.64e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 5 WVFSTNHKDIGTLYLLFGAWAGMIGTGLSLLIRAELSQPGTLLGDDQIFNVLVTAHAFVMIFFMVMPILIGgFGNWLVPL 84
Cdd:cd01662 1 WLTTVDHKRIGIMYIITAFVFFLRGGVDALLMRTQLALPGNDFLSPEHYNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 85 MIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGVGTGWTVYPPLAGNMAHAGPSVDLAIFSLHLAGVSSILGAINFI 164
Cdd:cd01662 80 QIGARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 165 TTIMNMKPPSASQHQTPLFVWSVYITAILLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYI 244
Cdd:cd01662 160 VTILKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 245 LILPGFGIVSHVVAASCGKKePFGYMGMVWAMLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLA 324
Cdd:cd01662 240 LILPAFGIFSEIVPTFSRKP-LFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 325 TMYGGNIKWDAPFLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVYWFPLFTGFSL 404
Cdd:cd01662 319 TMWRGRIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRML 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 405 NDSWSKIQFYIMFIGVNLTFFPQHFLGLAGMPRRYSDYP--DAYTLWNTISSIGSMISLIGVMVLMF-IIWEAFVSKRPT 481
Cdd:cd01662 399 NERLGKWSFWLWFIGFNLTFFPMHILGLMGMPRRVYTYLpgPGWDPLNLISTIGAFLIAAGVLLFLInVIVSIRKGKRDA 478
|
490 500
....*....|....*....|...
gi 575669765 482 PGVNFPATNVEWRLNFPPHYHTF 504
Cdd:cd01662 479 TGDPWGARTLEWATSSPPPAYNF 501
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
13-459 |
1.19e-135 |
|
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: 399.25 E-value: 1.19e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 13 DIGTLYLLFGAWAGMIGTGLSLLIRAELSQPGTLLGDDQIFNVLVTAHAFVMIFFMVMPIlIGGFGNWLVPLMIGAPDMA 92
Cdd:pfam00115 1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATPF-LFGFGNYLVPLMIGARDMA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 93 FPRMNNMSFWLLPPSFLLLLASStveAGVGTGWTVYPPLAGnmahagpsVDLAIFSLHLAGVSSILGAINFITTIMNMKP 172
Cdd:pfam00115 80 FPRLNALSFWLVVLGAVLLLASF---GGATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 173 PSASQhQTPLFVWSVYITAILLLLSLPVLAAGITMLLTDRNLNttffdpAGGGDPILYQHLFWFFGHPEVYILILPGFGI 252
Cdd:pfam00115 149 PGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 253 VSHVVAASCGKKePFGYMGMVWAMLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLATMYGGNIK 332
Cdd:pfam00115 222 IYYILPKFAGRP-LFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIR 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 333 W-DAPFLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVYWFPLFTGFSLNDSWSKI 411
Cdd:pfam00115 301 FrTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKL 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 575669765 412 QFYIMFIGVNLTFFPQHFLGLAGMPRRYS----DYPDAYTLWNTISSIGSMI 459
Cdd:pfam00115 381 HFWLLFIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPLNWIRTIGGVL 432
|
|
| CyoB |
TIGR02843 |
cytochrome o ubiquinol oxidase, subunit I; Cytochrome o terminal oxidase complex is the ... |
3-506 |
4.82e-126 |
|
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: 382.10 E-value: 4.82e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 3 TRWVFSTNHKDIGTLYLLFGAWAGMIGTGLSLLIRAELS-----QPGTLLGD--DQIFnvlvTAHAFVMIFFMVMPILIG 75
Cdd:TIGR02843 45 NEWLTTVDHKKIGIMYIIVALVMLLRGFADAIMMRTQQAlasggSAGYLPPHhyDQIF----TAHGVIMIFFVAMPFVFG 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 76 GFgNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGVGTGWTVYPPLAGNMAHAGPSVDLAIFSLHLAGVS 155
Cdd:TIGR02843 121 LM-NLVVPLQIGARDVAFPFLNSLSFWLTVVGAILVNVSLGVGEFAQTGWLAYPPLSELQYSPGVGVDYYIWALQISGIG 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 156 SILGAINFITTIMNMKPPSASQHQTPLFVWSVYITAILLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFW 235
Cdd:TIGR02843 200 TLLTGINFFVTIIKMRAPGMTLMKMPVFTWTSLCSNVLIIASFPILTVTLALLTLDRYLGMHFFTNEAGGNPMMYVNLIW 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 236 FFGHPEVYILILPGFGIVSHVVAaSCGKKEPFGYMGMVWAMLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPT 315
Cdd:TIGR02843 280 AWGHPEVYILILPAFGIFSEVVA-TFSRKRLFGYTSMVWATIAITVLSFIVWLHHFFTMGAGANVNAFFGIATMIIAIPT 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 316 GVKVFSWLATMYGGNIKWDAPFLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVYW 395
Cdd:TIGR02843 359 GVKIFNWLFTMYKGRIRFETPMLWTIGFMVTFSIGGMTGVLLAVPPADFVLHNSLFLIAHFHNVIIGGVVFGCFAGLTYW 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 396 FPLFTGFSLNDSWSKIQFYIMFIGVNLTFFPQHFLGLAGMPRRYSDYPD-AYTLWNTISSIGSMISLIGVMVLMFIIWEA 474
Cdd:TIGR02843 439 FPKAFGFKLNEKLGKRSFWCWFIGFYLAFMPLYILGFMGMTRRLNHYDNpEWHPMLIIAAFGAFLIACGILCQIIQIFVS 518
|
490 500 510
....*....|....*....|....*....|....*
gi 575669765 475 FVSK---RPTPGVNFPATNVEWRLNFPPHYHTFEE 506
Cdd:TIGR02843 519 IRDRdqnRDTTGDPWGGRTLEWSTSSPPPFYNFAV 553
|
|
| QoxB |
TIGR02882 |
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ... |
5-504 |
3.66e-120 |
|
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: 366.87 E-value: 3.66e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 5 WVFSTNHKDIGTLYLLFGAWAGMIGTGLSLLIRAELSQPGTLLGDDQIFNVLVTAHAFVMIFFMVMPILIGgFGNWLVPL 84
Cdd:TIGR02882 44 WLTTVDHKKIGVMYIICAVLMLFRGGIDALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 85 MIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGVGTGWTVYPPLAGNMAHAGPSVDLAIFSLHLAGVSSILGAINFI 164
Cdd:TIGR02882 123 QIGARDVAFPVLNALSFWLFFAGAMLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFF 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 165 TTIMNMKPPSASQHQTPLFVWSVYITAILLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYI 244
Cdd:TIGR02882 203 VTILKMRAPGMKLMQMPMFTWTTLITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLFWIWGHPEVYI 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 245 LILPGFGIVSHVVaASCGKKEPFGYMGMVWAMLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAIPTGVKVFSWLA 324
Cdd:TIGR02882 283 VILPAFGIYSEII-STFAQKRLFGYKSMVWSTVGIAFLSFLVWVHHFFTMGNGALINSFFSITTMAIAIPTGVKIFNWLL 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 325 TMYGGNIKWDAPFLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFVYWFPLFTGFSL 404
Cdd:TIGR02882 362 TLYKGKIRFTTPMLFSLAFIPNFLIGGVTGVMLAMASADYQYHNTYFLVAHFHYVLITGVVFACLAGLIYWYPKMFGYKL 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 405 NDSWSKIQFYIMFIGVNLTFFPQHFLGLAGMPRRYSDY--PDAYTLWNTISSIGSMISLIGVMVLMF-IIWEAFVSKRPT 481
Cdd:TIGR02882 442 NERLGKWCFWFFMIGFNVCFFPMYILGLDGMPRRMYTYspSDGWFPLNLISTIGALLMAIGFIFLVYnIYYSHRKSPREA 521
|
490 500
....*....|....*....|...
gi 575669765 482 PGVNFPATNVEWRLNFPPHYHTF 504
Cdd:TIGR02882 522 TGDPWNGRTLEWATASPPPKYNF 544
|
|
| PRK15017 |
PRK15017 |
cytochrome o ubiquinol oxidase subunit I; Provisional |
1-504 |
7.95e-109 |
|
cytochrome o ubiquinol oxidase subunit I; Provisional
Pssm-ID: 184978 Cd Length: 663 Bit Score: 338.06 E-value: 7.95e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 1 MLTRWVFSTNHKDIGTLYLLFGAWAGMIGTGLSLLIR-----AELSQPGTLLGD--DQIFnvlvTAHAFVMIFFMVMPIL 73
Cdd:PRK15017 44 LWKEWLTSVDHKRLGIMYIIVAIVMLLRGFADAIMMRsqqalASAGEAGFLPPHhyDQIF----TAHGVIMIFFVAMPFV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 74 IGgFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGVGTGWTVYPPLAGNMAHAGPSVDLAIFSLHLAG 153
Cdd:PRK15017 120 IG-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSG 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 154 VSSILGAINFITTIMNMKPPSASQHQTPLFVWSVYITAILLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHL 233
Cdd:PRK15017 199 IGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINL 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 234 FWFFGHPEVYILILPGFGIVSHVvAASCGKKEPFGYMGMVWAMLSIGLLGFIVWAHHMFTTDLNVDTRAYFTSATMIIAI 313
Cdd:PRK15017 279 IWAWGHPEVYILILPVFGVFSEI-AATFSRKRLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAI 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 314 PTGVKVFSWLATMYGGNIKWDAPFLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFV 393
Cdd:PRK15017 358 PTGVKIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMT 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 394 YWFPLFTGFSLNDSWSKIQFYIMFIGVNLTFFPQHFLGLAGMPRRYSDYPD-AYTLWNTISSIGSMISLIGVMVLMFIIW 472
Cdd:PRK15017 438 YWWPKAFGFKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMTRRLSQQIDpQFHTMLMIAASGAALIALGILCQVIQMY 517
|
490 500 510
....*....|....*....|....*....|....*
gi 575669765 473 EAFVSK---RPTPGVNFPATNVEWRLNFPPHYHTF 504
Cdd:PRK15017 518 VSIRDRdqnRDLTGDPWGGRTLEWATSSPPPFYNF 552
|
|
| ba3-like_Oxidase_I |
cd01660 |
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ... |
226-471 |
1.20e-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: 91.58 E-value: 1.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 226 DPILYQHLFWFFGHPEVYILILPGFGIVSHVVAASCGKKEPFGYMGMVWAMLSIgLLGFIVWAHHMFTtDLNVDTRAYF- 304
Cdd:cd01660 200 DVLLSRTLFWWFGHPLVYFWLLPAYIAWYTILPKIAGGKLFSDPLARLAFILFL-LFSTPVGFHHQFA-DPGIGPGWKFi 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 305 -TSATMIIAIPT-------------------GVKVFSWLATMYGGNIKWDAPFLWALGFIFlftvGGLTGIVLANSSLDI 364
Cdd:cd01660 278 hMVLTFMVALPSlltaftvfasleiagrlrgGKGLFGWIRALPWGDPMFLALFLAMLMFIP----GGAGGIINASYQLNY 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 575669765 365 VLHDTYYVVAHFHyvLSMGAVFAIMA-GFVYWF-PLFTGFSLNDSW-SKIQFYIMFIGVNLTFFPQHFLGLAGMPRR--Y 439
Cdd:cd01660 354 VVHNTAWVPGHFH--LTVGGAVALTFmAVAYWLvPHLTGRELAAKRlALAQPWLWFVGMTIMSTAMHVAGLLGAPRRtaE 431
|
250 260 270
....*....|....*....|....*....|....*..
gi 575669765 440 SDYPDAY-----TLWNTISSIGSMISLIGVMVLMFII 471
Cdd:cd01660 432 AQYGGLPaagewAPYQQLMAIGGTILFVSGALFLYIL 468
|
|
| |
