|
Name |
Accession |
Description |
Interval |
E-value |
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
7-494 |
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: 774.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 7 TNHKDIGTLYFIVGLWAGLMGMSLSLAIRMNLRVPGSQLFDPHLYNVIVTAHALIMIFFMVMPVMMGGFGNWLVPLMLGV 86
Cdd:cd01663 1 TNHKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 87 PDMCYPRLNNLSFWLVPFALLCLIFSMVVEKGAGTGWTIYPPLSSYLFHTGASVDLACFSLHLSGLSSLLAAVNFMATVI 166
Cdd:cd01663 81 PDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 167 MMRPNDQNWEKVPLFACSMCVTSFLLLISLPVLAGGVTMLIADRHFNTTFFIPSGGGDPILFQHLFWFFGHPEVYVLILP 246
Cdd:cd01663 161 NMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 247 GFGMISHVYVHYCRKERVFGKIGMVYAMVSIGILGFIVWAHHMFTVGLNVDTRAYFTAATMIIAVPTGVKVFSWVATAWG 326
Cdd:cd01663 241 GFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 327 SpRISFSASMLYGVGFLVLFTVGGLTGIMLSNSCLDVVLHDTYYVTGHFHYVLSMGAVFSIFSGFYYWFPLFTGICFDLP 406
Cdd:cd01663 321 G-SIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNET 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 407 LTRAQFFINFFGVNITFFPHHFMGLNGMPRRYVDYCDVFKVWHGISSYGSFMSFLASYFFLMLLGETFLVQRPMLF-SLH 485
Cdd:cd01663 400 LGKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFnVGE 479
|
....*....
gi 2732679549 486 SRCAREWLI 494
Cdd:cd01663 480 GSTSLEWTL 488
|
|
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-502 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 774.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 1 MRWFVSTNHKDIGTLYFIVGLWAGLMGMSLSLAIRMNLRVPGSQLFDPHLYNVIVTAHALIMIFFMVMPVMMGGFGNWLV 80
Cdd:MTH00153 2 NKWLFSTNHKDIGTLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 81 PLMLGVPDMCYPRLNNLSFWLVPFALLCLIFSMVVEKGAGTGWTIYPPLSSYLFHTGASVDLACFSLHLSGLSSLLAAVN 160
Cdd:MTH00153 82 PLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAIN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 161 FMATVIMMRPNDQNWEKVPLFACSMCVTSFLLLISLPVLAGGVTMLIADRHFNTTFFIPSGGGDPILFQHLFWFFGHPEV 240
Cdd:MTH00153 162 FITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 241 YVLILPGFGMISHVYVHYCRKERVFGKIGMVYAMVSIGILGFIVWAHHMFTVGLNVDTRAYFTAATMIIAVPTGVKVFSW 320
Cdd:MTH00153 242 YILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSW 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 321 VATAWGSpRISFSASMLYGVGFLVLFTVGGLTGIMLSNSCLDVVLHDTYYVTGHFHYVLSMGAVFSIFSGFYYWFPLFTG 400
Cdd:MTH00153 322 LATLHGS-QINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 401 ICFDLPLTRAQFFINFFGVNITFFPHHFMGLNGMPRRYVDYCDVFKVWHGISSYGSFMSFLASYFFLMLLGETFLVQRPM 480
Cdd:MTH00153 401 LTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPV 480
|
490 500
....*....|....*....|..
gi 2732679549 481 LFSLHSRCAREWLIDSSVPRHT 502
Cdd:MTH00153 481 LFSLNLSSSIEWLQNLPPAEHS 502
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
6-503 |
1.31e-180 |
|
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: 517.16 E-value: 1.31e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 6 STNHKDIGTLYFIVGLWAGLMGMSLSLAIRMNLRVPGSQLFDPHLYNVIVTAHALIMIFFMVMPvMMGGFGNWLVPLMLG 85
Cdd:TIGR02891 3 TVDHKRIGILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIP-ILAGFGNYLLPLMIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 86 VPDMCYPRLNNLSFWLVPFALLCLIFSMVVEKGAGTGWTIYPPLSSYLFHTGASVDLACFSLHLSGLSSLLAAVNFMATV 165
Cdd:TIGR02891 82 ARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 166 IMMRPNDQNWEKVPLFACSMCVTSFLLLISLPVLAGGVTMLIADRHFNTTFFIPSGGGDPILFQHLFWFFGHPEVYVLIL 245
Cdd:TIGR02891 162 LNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 246 PGFGMISHVYVHYCRKeRVFGKIGMVYAMVSIGILGFIVWAHHMFTVGLNVDTRAYFTAATMIIAVPTGVKVFSWVATAW 325
Cdd:TIGR02891 242 PAFGIISEILPTFARK-PIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLW 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 326 GSpRISFSASMLYGVGFLVLFTVGGLTGIMLSNSCLDVVLHDTYYVTGHFHYVLSMGAVFSIFSGFYYWFPLFTGICFDL 405
Cdd:TIGR02891 321 GG-SIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 406 PLTRAQFFINFFGVNITFFPHHFMGLNGMPRRYVDYCD--VFKVWHGISSYGSFMSFLASYFFLMLLGETFLVQRpmlfs 483
Cdd:TIGR02891 400 RLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPqmGFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGP----- 474
|
490 500
....*....|....*....|....*...
gi 2732679549 484 lhsRCAR--------EWLIDSSVPRHTW 503
Cdd:TIGR02891 475 ---KAGAnpwgattlEWTTSSPPPAHNF 499
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
1-467 |
1.07e-179 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 516.22 E-value: 1.07e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 1 MRWFVSTNHKDIGTLYFIVGLWAGLMGMSLSLAIRMNLRVPGSQLFDPHLYNVIVTAHALIMIFFMVMPvMMGGFGNWLV 80
Cdd:COG0843 7 RRWLTTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 81 PLMLGVPDMCYPRLNNLSFWLVPFALLCLIFSMVVEKGAGTGWTIYPPLSSYLFHTGASVDLACFSLHLSGLSSLLAAVN 160
Cdd:COG0843 86 PLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVN 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 161 FMATVIMMRPNDQNWEKVPLFACSMCVTSFLLLISLPVLAGGVTMLIADRHFNTTFFIPSGGGDPILFQHLFWFFGHPEV 240
Cdd:COG0843 166 FIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEV 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 241 YVLILPGFGMISHVYVHYCRKeRVFGKIGMVYAMVSIGILGFIVWAHHMFTVGLNVDTRAYFTAATMIIAVPTGVKVFSW 320
Cdd:COG0843 246 YILILPAFGIVSEIIPTFSRK-PLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNW 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 321 VATAWGSpRISFSASMLYGVGFLVLFTVGGLTGIMLSNSCLDVVLHDTYYVTGHFHYVLSMGAVFSIFSGFYYWFPLFTG 400
Cdd:COG0843 325 IATMWRG-RIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTG 403
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2732679549 401 ICFDLPLTRAQFFINFFGVNITFFPHHFMGLNGMPRRYVDY--CDVFKVWHGISSYGSFMSFLASYFFL 467
Cdd:COG0843 404 RMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYppEPGWQPLNLISTIGAFILAVGFLLFL 472
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
11-458 |
3.65e-124 |
|
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: 370.75 E-value: 3.65e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 11 DIGTLYFIVGLWAGLMGMSLSLAIRMNLRVPGSQLFDPHLYNVIVTAHALIMIFFMVMPVMMGgFGNWLVPLMLGVPDMC 90
Cdd:pfam00115 1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATPFLFG-FGNYLVPLMIGARDMA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 91 YPRLNNLSFWLVPFALLCLIFSMVvekGAGTGWTIYPPLssylfhtgASVDLACFSLHLSGLSSLLAAVNFMATVIMMRP 170
Cdd:pfam00115 80 FPRLNALSFWLVVLGAVLLLASFG---GATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 171 NDQNWeKVPLFACSMCVTSFLLLISLPVLAGGVTMLIADRHFNTtffipsGGGDPILFQHLFWFFGHPEVYVLILPGFGM 250
Cdd:pfam00115 149 PGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLGA------GGGDPLLDQHLFWWFGHPEVYILILPAFGI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 251 ISHVYVHYCRKeRVFGKIGMVYAMVSIGILGFIVWAHHMFTVGLNVDTRAYFTAATMIIAVPTGVKVFSWVATAWGSPRI 330
Cdd:pfam00115 222 IYYILPKFAGR-PLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIR 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 331 SFSASMLYGVGFLVLFTVGGLTGIMLSNSCLDVVLHDTYYVTGHFHYVLSMGAVFSIFSGFYYWFPLFTGICFDLPLTRA 410
Cdd:pfam00115 301 FRTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKL 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 2732679549 411 QFFINFFGVNITFFPHHFMGLNGMPRRY----VDYCDVFKVWHGISSYGSFM 458
Cdd:pfam00115 381 HFWLLFIGFNLTFFPMHILGLLGMPRRYappfIETVPAFQPLNWIRTIGGVL 432
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
7-494 |
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: 774.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 7 TNHKDIGTLYFIVGLWAGLMGMSLSLAIRMNLRVPGSQLFDPHLYNVIVTAHALIMIFFMVMPVMMGGFGNWLVPLMLGV 86
Cdd:cd01663 1 TNHKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 87 PDMCYPRLNNLSFWLVPFALLCLIFSMVVEKGAGTGWTIYPPLSSYLFHTGASVDLACFSLHLSGLSSLLAAVNFMATVI 166
Cdd:cd01663 81 PDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 167 MMRPNDQNWEKVPLFACSMCVTSFLLLISLPVLAGGVTMLIADRHFNTTFFIPSGGGDPILFQHLFWFFGHPEVYVLILP 246
Cdd:cd01663 161 NMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 247 GFGMISHVYVHYCRKERVFGKIGMVYAMVSIGILGFIVWAHHMFTVGLNVDTRAYFTAATMIIAVPTGVKVFSWVATAWG 326
Cdd:cd01663 241 GFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 327 SpRISFSASMLYGVGFLVLFTVGGLTGIMLSNSCLDVVLHDTYYVTGHFHYVLSMGAVFSIFSGFYYWFPLFTGICFDLP 406
Cdd:cd01663 321 G-SIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNET 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 407 LTRAQFFINFFGVNITFFPHHFMGLNGMPRRYVDYCDVFKVWHGISSYGSFMSFLASYFFLMLLGETFLVQRPMLF-SLH 485
Cdd:cd01663 400 LGKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFnVGE 479
|
....*....
gi 2732679549 486 SRCAREWLI 494
Cdd:cd01663 480 GSTSLEWTL 488
|
|
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
1-502 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 774.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 1 MRWFVSTNHKDIGTLYFIVGLWAGLMGMSLSLAIRMNLRVPGSQLFDPHLYNVIVTAHALIMIFFMVMPVMMGGFGNWLV 80
Cdd:MTH00153 2 NKWLFSTNHKDIGTLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 81 PLMLGVPDMCYPRLNNLSFWLVPFALLCLIFSMVVEKGAGTGWTIYPPLSSYLFHTGASVDLACFSLHLSGLSSLLAAVN 160
Cdd:MTH00153 82 PLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAIN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 161 FMATVIMMRPNDQNWEKVPLFACSMCVTSFLLLISLPVLAGGVTMLIADRHFNTTFFIPSGGGDPILFQHLFWFFGHPEV 240
Cdd:MTH00153 162 FITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 241 YVLILPGFGMISHVYVHYCRKERVFGKIGMVYAMVSIGILGFIVWAHHMFTVGLNVDTRAYFTAATMIIAVPTGVKVFSW 320
Cdd:MTH00153 242 YILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSW 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 321 VATAWGSpRISFSASMLYGVGFLVLFTVGGLTGIMLSNSCLDVVLHDTYYVTGHFHYVLSMGAVFSIFSGFYYWFPLFTG 400
Cdd:MTH00153 322 LATLHGS-QINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 401 ICFDLPLTRAQFFINFFGVNITFFPHHFMGLNGMPRRYVDYCDVFKVWHGISSYGSFMSFLASYFFLMLLGETFLVQRPM 480
Cdd:MTH00153 401 LTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPV 480
|
490 500
....*....|....*....|..
gi 2732679549 481 LFSLHSRCAREWLIDSSVPRHT 502
Cdd:MTH00153 481 LFSLNLSSSIEWLQNLPPAEHS 502
|
|
| COX1 |
MTH00223 |
cytochrome c oxidase subunit I; Provisional |
1-502 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177260 Cd Length: 512 Bit Score: 753.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 1 MRWFVSTNHKDIGTLYFIVGLWAGLMGMSLSLAIRMNLRVPGSQLFDPHLYNVIVTAHALIMIFFMVMPVMMGGFGNWLV 80
Cdd:MTH00223 1 MRWLFSTNHKDIGTLYLIFGMWSGLVGTSLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 81 PLMLGVPDMCYPRLNNLSFWLVPFALLCLIFSMVVEKGAGTGWTIYPPLSSYLFHTGASVDLACFSLHLSGLSSLLAAVN 160
Cdd:MTH00223 81 PLMLGAPDMAFPRLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 161 FMATVIMMRPNDQNWEKVPLFACSMCVTSFLLLISLPVLAGGVTMLIADRHFNTTFFIPSGGGDPILFQHLFWFFGHPEV 240
Cdd:MTH00223 161 FITTIINMRSPGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 241 YVLILPGFGMISHVYVHYCRKERVFGKIGMVYAMVSIGILGFIVWAHHMFTVGLNVDTRAYFTAATMIIAVPTGVKVFSW 320
Cdd:MTH00223 241 YILILPGFGMISHIVSHYSSKKEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSW 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 321 VATAWGSpRISFSASMLYGVGFLVLFTVGGLTGIMLSNSCLDVVLHDTYYVTGHFHYVLSMGAVFSIFSGFYYWFPLFTG 400
Cdd:MTH00223 321 LATIYGS-KIKYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLFTG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 401 ICFDLPLTRAQFFINFFGVNITFFPHHFMGLNGMPRRYVDYCDVFKVWHGISSYGSFMSFLASYFFLMLLGETFLVQRPM 480
Cdd:MTH00223 400 VTLHRRWAKAHFFLMFLGVNLTFFPQHFLGLAGMPRRYSDYPDCYTKWNQVSSFGSMISFVSVLFFMFIVWEAFVSQRSV 479
|
490 500
....*....|....*....|..
gi 2732679549 481 LFSLHSRCAREWLIDSSVPRHT 502
Cdd:MTH00223 480 VWSGHLSTSLEWDNLLPADFHN 501
|
|
| COX1 |
MTH00167 |
cytochrome c oxidase subunit I; Provisional |
1-506 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177222 Cd Length: 512 Bit Score: 706.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 1 MRWFVSTNHKDIGTLYFIVGLWAGLMGMSLSLAIRMNLRVPGSQLFDPHLYNVIVTAHALIMIFFMVMPVMMGGFGNWLV 80
Cdd:MTH00167 4 NRWLFSTNHKDIGTLYFIFGAWAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 81 PLMLGVPDMCYPRLNNLSFWLVPFALLCLIFSMVVEKGAGTGWTIYPPLSSYLFHTGASVDLACFSLHLSGLSSLLAAVN 160
Cdd:MTH00167 84 PLMIGAPDMAFPRMNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGSIN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 161 FMATVIMMRPNDQNWEKVPLFACSMCVTSFLLLISLPVLAGGVTMLIADRHFNTTFFIPSGGGDPILFQHLFWFFGHPEV 240
Cdd:MTH00167 164 FITTIINMKPPGITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 241 YVLILPGFGMISHVYVHYCRKERVFGKIGMVYAMVSIGILGFIVWAHHMFTVGLNVDTRAYFTAATMIIAVPTGVKVFSW 320
Cdd:MTH00167 244 YILILPGFGMISHIVVYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVFSW 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 321 VATAWGSpRISFSASMLYGVGFLVLFTVGGLTGIMLSNSCLDVVLHDTYYVTGHFHYVLSMGAVFSIFSGFYYWFPLFTG 400
Cdd:MTH00167 324 LATLHGG-KIKWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTG 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 401 ICFDLPLTRAQFFINFFGVNITFFPHHFMGLNGMPRRYVDYCDVFKVWHGISSYGSFMSFLASYFFLMLLGETFLVQRPM 480
Cdd:MTH00167 403 LTLNETWTKIHFFVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNVVSSIGSLISLVAVILFLFIIWEAFSSKRKL 482
|
490 500
....*....|....*....|....*.
gi 2732679549 481 LFSLHSRCAREWLIDSSVPRHTWCNG 506
Cdd:MTH00167 483 LPVELTSTNVEWLHGCPPPHHTWEEP 508
|
|
| COX1 |
MTH00116 |
cytochrome c oxidase subunit I; Provisional |
2-502 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177177 Cd Length: 515 Bit Score: 688.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 2 RWFVSTNHKDIGTLYFIVGLWAGLMGMSLSLAIRMNLRVPGSQLFDPHLYNVIVTAHALIMIFFMVMPVMMGGFGNWLVP 81
Cdd:MTH00116 5 RWLFSTNHKDIGTLYLIFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 82 LMLGVPDMCYPRLNNLSFWLVPFALLCLIFSMVVEKGAGTGWTIYPPLSSYLFHTGASVDLACFSLHLSGLSSLLAAVNF 161
Cdd:MTH00116 85 LMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILGAINF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 162 MATVIMMRPNDQNWEKVPLFACSMCVTSFLLLISLPVLAGGVTMLIADRHFNTTFFIPSGGGDPILFQHLFWFFGHPEVY 241
Cdd:MTH00116 165 ITTCINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVY 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 242 VLILPGFGMISHVYVHYCRKERVFGKIGMVYAMVSIGILGFIVWAHHMFTVGLNVDTRAYFTAATMIIAVPTGVKVFSWV 321
Cdd:MTH00116 245 ILILPGFGIISHIVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVFSWL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 322 ATAWGSpRISFSASMLYGVGFLVLFTVGGLTGIMLSNSCLDVVLHDTYYVTGHFHYVLSMGAVFSIFSGFYYWFPLFTGI 401
Cdd:MTH00116 325 ATLHGG-TIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFTGY 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 402 CFDLPLTRAQFFINFFGVNITFFPHHFMGLNGMPRRYVDYCDVFKVWHGISSYGSFMSFLASYFFLMLLGETFLVQRPML 481
Cdd:MTH00116 404 TLHQTWTKAQFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTISSIGSLISMTAVIMLMFIIWEAFSSKRKVL 483
|
490 500
....*....|....*....|.
gi 2732679549 482 FSLHSRCAREWLIDSSVPRHT 502
Cdd:MTH00116 484 QPELTTTNIEWIHGCPPPYHT 504
|
|
| COX1 |
MTH00142 |
cytochrome c oxidase subunit I; Provisional |
1-492 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214431 Cd Length: 511 Bit Score: 681.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 1 MRWFVSTNHKDIGTLYFIVGLWAGLMGMSLSLAIRMNLRVPGSQLFDPHLYNVIVTAHALIMIFFMVMPVMMGGFGNWLV 80
Cdd:MTH00142 2 MRWLFSTNHKDIGTLYFLFGAWAGMVGTGLSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 81 PLMLGVPDMCYPRLNNLSFWLVPFALLCLIFSMVVEKGAGTGWTIYPPLSSYLFHTGASVDLACFSLHLSGLSSLLAAVN 160
Cdd:MTH00142 82 PLMLGAPDMAFPRMNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAIN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 161 FMATVIMMRPNDQNWEKVPLFACSMCVTSFLLLISLPVLAGGVTMLIADRHFNTTFFIPSGGGDPILFQHLFWFFGHPEV 240
Cdd:MTH00142 162 FITTVINMRAGGMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 241 YVLILPGFGMISHVYVHYCRKERVFGKIGMVYAMVSIGILGFIVWAHHMFTVGLNVDTRAYFTAATMIIAVPTGVKVFSW 320
Cdd:MTH00142 242 YILILPGFGMISHIINHYSGKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVFSW 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 321 VATAWGSpRISFSASMLYGVGFLVLFTVGGLTGIMLSNSCLDVVLHDTYYVTGHFHYVLSMGAVFSIFSGFYYWFPLFTG 400
Cdd:MTH00142 322 LATLHGS-KVKYEPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLFTG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 401 ICFDLPLTRAQFFINFFGVNITFFPHHFMGLNGMPRRYVDYCDVFKVWHGISSYGSFMSFLASYFFLMLLGETFLVQRPM 480
Cdd:MTH00142 401 LTLNPRWLKAHFYTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSSLGSMISFIAVLMFVFIVWESFVSQRLV 480
|
490
....*....|..
gi 2732679549 481 LFSLHSRCAREW 492
Cdd:MTH00142 481 MWSSHLSTSLEW 492
|
|
| COX1 |
MTH00007 |
cytochrome c oxidase subunit I; Validated |
1-492 |
0e+00 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 133649 Cd Length: 511 Bit Score: 636.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 1 MRWFVSTNHKDIGTLYFIVGLWAGLMGMSLSLAIRMNLRVPGSQLFDPHLYNVIVTAHALIMIFFMVMPVMMGGFGNWLV 80
Cdd:MTH00007 1 MRWLYSTNHKDIGTLYFILGVWGGLLGTSMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 81 PLMLGVPDMCYPRLNNLSFWLVPFALLCLIFSMVVEKGAGTGWTIYPPLSSYLFHTGASVDLACFSLHLSGLSSLLAAVN 160
Cdd:MTH00007 81 PLMLGAPDMAFPRLNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 161 FMATVIMMRPNDQNWEKVPLFACSMCVTSFLLLISLPVLAGGVTMLIADRHFNTTFFIPSGGGDPILFQHLFWFFGHPEV 240
Cdd:MTH00007 161 FITTVINMRWKGLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 241 YVLILPGFGMISHVYVHYCRKERVFGKIGMVYAMVSIGILGFIVWAHHMFTVGLNVDTRAYFTAATMIIAVPTGVKVFSW 320
Cdd:MTH00007 241 YILILPGFGAISHIVTHYAGKLEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSW 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 321 VATAWGSPrISFSASMLYGVGFLVLFTVGGLTGIMLSNSCLDVVLHDTYYVTGHFHYVLSMGAVFSIFSGFYYWFPLFTG 400
Cdd:MTH00007 321 LATIHGSP-IKYETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 401 ICFDLPLTRAQFFINFFGVNITFFPHHFMGLNGMPRRYVDYCDVFKVWHGISSYGSFMSFLASYFFLMLLGETFLVQRPM 480
Cdd:MTH00007 400 LTLHDRWAKAHFFLMFLGVNLTFFPQHFLGLSGMPRRYSDYPDAYTKWNVVSSFGSMLSFVALLLFIFILWEAFSAQRGV 479
|
490
....*....|..
gi 2732679549 481 LFSLHSRCAREW 492
Cdd:MTH00007 480 IASPHMSSSLEW 491
|
|
| COX1 |
MTH00037 |
cytochrome c oxidase subunit I; Provisional |
2-501 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177112 Cd Length: 517 Bit Score: 634.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 2 RWFVSTNHKDIGTLYFIVGLWAGLMGMSLSLAIRMNLRVPGSQLFDPHLYNVIVTAHALIMIFFMVMPVMMGGFGNWLVP 81
Cdd:MTH00037 5 RWLFSTNHKDIGTLYLIFGAWAGMVGTAMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNWLIP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 82 LMLGVPDMCYPRLNNLSFWLVPFALLCLIFSMVVEKGAGTGWTIYPPLSSYLFHTGASVDLACFSLHLSGLSSLLAAVNF 161
Cdd:MTH00037 85 LMIGAPDMAFPRMNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILASINF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 162 MATVIMMRPNDQNWEKVPLFACSMCVTSFLLLISLPVLAGGVTMLIADRHFNTTFFIPSGGGDPILFQHLFWFFGHPEVY 241
Cdd:MTH00037 165 ITTIINMRTPGMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHPEVY 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 242 VLILPGFGMISHVYVHYCRKERVFGKIGMVYAMVSIGILGFIVWAHHMFTVGLNVDTRAYFTAATMIIAVPTGVKVFSWV 321
Cdd:MTH00037 245 ILILPGFGMISHVIAHYSGKQEPFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWM 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 322 ATAWGSPrISFSASMLYGVGFLVLFTVGGLTGIMLSNSCLDVVLHDTYYVTGHFHYVLSMGAVFSIFSGFYYWFPLFTGI 401
Cdd:MTH00037 325 ATLQGSN-LRWETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLFSGV 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 402 CFDLPLTRAQFFINFFGVNITFFPHHFMGLNGMPRRYVDYCDVFKVWHGISSYGSFMSFLASYFFLMLLGETFLVQRPML 481
Cdd:MTH00037 404 SLHPLWSKVHFFLMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSTISLVATLFFLFLIWEAFASQREVI 483
|
490 500
....*....|....*....|
gi 2732679549 482 FSLHSRCAREWLIDSSVPRH 501
Cdd:MTH00037 484 SPEFSSSSLEWQYSSFPPSH 503
|
|
| COX1 |
MTH00079 |
cytochrome c oxidase subunit I; Provisional |
1-498 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177148 Cd Length: 508 Bit Score: 620.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 1 MRWFVSTNHKDIGTLYFIVGLWAGLMGMSLSLAIRMNLRVPGSQLFDPHLYNVIVTAHALIMIFFMVMPVMMGGFGNWLV 80
Cdd:MTH00079 5 SVWLESSNHKDIGTLYFLFGLWSGMVGTSLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWML 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 81 PLMLGVPDMCYPRLNNLSFWLVPFALLCLIFSMVVEKGAGTGWTIYPPLSSyLFHTGASVDLACFSLHLSGLSSLLAAVN 160
Cdd:MTH00079 85 PLMLGAPDMSFPRLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPLST-LGHPGSSVDLAIFSLHCAGISSILGGIN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 161 FMATVIMMRPNDQNWEKVPLFACSMCVTSFLLLISLPVLAGGVTMLIADRHFNTTFFIPSGGGDPILFQHLFWFFGHPEV 240
Cdd:MTH00079 164 FMVTTKNLRSSSISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPEV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 241 YVLILPGFGMISHVYVHYCRKERVFGKIGMVYAMVSIGILGFIVWAHHMFTVGLNVDTRAYFTAATMIIAVPTGVKVFSW 320
Cdd:MTH00079 244 YILILPAFGIISQSTLYLTGKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVFSW 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 321 VATAWGSpRISFSASMLYGVGFLVLFTVGGLTGIMLSNSCLDVVLHDTYYVTGHFHYVLSMGAVFSIFSGFYYWFPLFTG 400
Cdd:MTH00079 324 LATLFGM-KMKFQPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFMTG 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 401 ICFDLPLTRAQFFINFFGVNITFFPHHFMGLNGMPRRYVDYCDVFKVWHGISSYGSFMSFLASYFFLMLLGETFLVQRPM 480
Cdd:MTH00079 403 IVYDKLMMSAVFFLMFVGVNLTFFPLHFAGLHGMPRKYLDYPDVYSVWNVISSYGSMISVFALFLFIYVLLESFFSYRLV 482
|
490
....*....|....*...
gi 2732679549 481 LFSLHSRCAREWLIDSSV 498
Cdd:MTH00079 483 LHDNYINSSPEYSLSSYV 500
|
|
| COX1 |
MTH00103 |
cytochrome c oxidase subunit I; Validated |
2-503 |
0e+00 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 177165 Cd Length: 513 Bit Score: 615.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 2 RWFVSTNHKDIGTLYFIVGLWAGLMGMSLSLAIRMNLRVPGSQLFDPHLYNVIVTAHALIMIFFMVMPVMMGGFGNWLVP 81
Cdd:MTH00103 5 RWLFSTNHKDIGTLYLLFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 82 LMLGVPDMCYPRLNNLSFWLVPFALLCLIFSMVVEKGAGTGWTIYPPLSSYLFHTGASVDLACFSLHLSGLSSLLAAVNF 161
Cdd:MTH00103 85 LMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 162 MATVIMMRPNDQNWEKVPLFACSMCVTSFLLLISLPVLAGGVTMLIADRHFNTTFFIPSGGGDPILFQHLFWFFGHPEVY 241
Cdd:MTH00103 165 ITTIINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVY 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 242 VLILPGFGMISHVYVHYCRKERVFGKIGMVYAMVSIGILGFIVWAHHMFTVGLNVDTRAYFTAATMIIAVPTGVKVFSWV 321
Cdd:MTH00103 245 ILILPGFGMISHIVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 322 ATAWGSpRISFSASMLYGVGFLVLFTVGGLTGIMLSNSCLDVVLHDTYYVTGHFHYVLSMGAVFSIFSGFYYWFPLFTGI 401
Cdd:MTH00103 325 ATLHGG-NIKWSPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGY 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 402 CFDLPLTRAQFFINFFGVNITFFPHHFMGLNGMPRRYVDYCDVFKVWHGISSYGSFMSFLASYFFLMLLGETFLVQRPML 481
Cdd:MTH00103 404 TLNDTWAKIHFTIMFVGVNMTFFPQHFLGLSGMPRRYSDYPDAYTTWNTVSSMGSFISLTAVMLMIFMIWEAFASKREVL 483
|
490 500
....*....|....*....|..
gi 2732679549 482 FSLHSRCAREWLIDSSVPRHTW 503
Cdd:MTH00103 484 TVELTTTNLEWLHGCPPPYHTF 505
|
|
| COX1 |
MTH00183 |
cytochrome c oxidase subunit I; Provisional |
2-503 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177234 Cd Length: 516 Bit Score: 615.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 2 RWFVSTNHKDIGTLYFIVGLWAGLMGMSLSLAIRMNLRVPGSQLFDPHLYNVIVTAHALIMIFFMVMPVMMGGFGNWLVP 81
Cdd:MTH00183 5 RWFFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 82 LMLGVPDMCYPRLNNLSFWLVPFALLCLIFSMVVEKGAGTGWTIYPPLSSYLFHTGASVDLACFSLHLSGLSSLLAAVNF 161
Cdd:MTH00183 85 LMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 162 MATVIMMRPNDQNWEKVPLFACSMCVTSFLLLISLPVLAGGVTMLIADRHFNTTFFIPSGGGDPILFQHLFWFFGHPEVY 241
Cdd:MTH00183 165 ITTIINMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVY 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 242 VLILPGFGMISHVYVHYCRKERVFGKIGMVYAMVSIGILGFIVWAHHMFTVGLNVDTRAYFTAATMIIAVPTGVKVFSWV 321
Cdd:MTH00183 245 ILILPGFGMISHIVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSWL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 322 ATAWGSpRISFSASMLYGVGFLVLFTVGGLTGIMLSNSCLDVVLHDTYYVTGHFHYVLSMGAVFSIFSGFYYWFPLFTGI 401
Cdd:MTH00183 325 ATLHGG-SIKWETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLFSGY 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 402 CFDLPLTRAQFFINFFGVNITFFPHHFMGLNGMPRRYVDYCDVFKVWHGISSYGSFMSFLASYFFLMLLGETFLVQRPML 481
Cdd:MTH00183 404 TLHSTWTKIHFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMFLFILWEAFAAKREVL 483
|
490 500
....*....|....*....|..
gi 2732679549 482 FSLHSRCAREWLIDSSVPRHTW 503
Cdd:MTH00183 484 SVELTSTNVEWLHGCPPPYHTF 505
|
|
| COX1 |
MTH00077 |
cytochrome c oxidase subunit I; Provisional |
2-503 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214419 Cd Length: 514 Bit Score: 610.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 2 RWFVSTNHKDIGTLYFIVGLWAGLMGMSLSLAIRMNLRVPGSQLFDPHLYNVIVTAHALIMIFFMVMPVMMGGFGNWLVP 81
Cdd:MTH00077 5 RWLFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 82 LMLGVPDMCYPRLNNLSFWLVPFALLCLIFSMVVEKGAGTGWTIYPPLSSYLFHTGASVDLACFSLHLSGLSSLLAAVNF 161
Cdd:MTH00077 85 LMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 162 MATVIMMRPNDQNWEKVPLFACSMCVTSFLLLISLPVLAGGVTMLIADRHFNTTFFIPSGGGDPILFQHLFWFFGHPEVY 241
Cdd:MTH00077 165 ITTSINMKPPSMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHPEVY 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 242 VLILPGFGMISHVYVHYCRKERVFGKIGMVYAMVSIGILGFIVWAHHMFTVGLNVDTRAYFTAATMIIAVPTGVKVFSWV 321
Cdd:MTH00077 245 ILILPGFGMISHIVTYYSAKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVFSWL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 322 ATAWGSPrISFSASMLYGVGFLVLFTVGGLTGIMLSNSCLDVVLHDTYYVTGHFHYVLSMGAVFSIFSGFYYWFPLFTGI 401
Cdd:MTH00077 325 ATMHGGA-IKWDAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGY 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 402 CFDLPLTRAQFFINFFGVNITFFPHHFMGLNGMPRRYVDYCDVFKVWHGISSYGSFMSFLASYFFLMLLGETFLVQRPML 481
Cdd:MTH00077 404 TLHSTWSKIHFGVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMMMFIIWEAFSSKREVL 483
|
490 500
....*....|....*....|..
gi 2732679549 482 FSLHSRCAREWLIDSSVPRHTW 503
Cdd:MTH00077 484 TTELTSTNIEWLHGCPPPYHTF 505
|
|
| COX1 |
MTH00182 |
cytochrome c oxidase subunit I; Provisional |
2-503 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214451 Cd Length: 525 Bit Score: 591.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 2 RWFVSTNHKDIGTLYFIVGLWAGLMGMSLSLAIRMNLRVPGSQLFDPHLYNVIVTAHALIMIFFMVMPVMMGGFGNWLVP 81
Cdd:MTH00182 7 RWVFSTNHKDIGTLYLVFGAGAGMIGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWLVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 82 LMLGVPDMCYPRLNNLSFWLVPFALLCLIFSMVVEKGAGTGWTIYPPLSSYLFHTGASVDLACFSLHLSGLSSLLAAVNF 161
Cdd:MTH00182 87 LYIGAPDMAFPRLNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAINF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 162 MATVIMMRPNDQNWEKVPLFACSMCVTSFLLLISLPVLAGGVTMLIADRHFNTTFFIPSGGGDPILFQHLFWFFGHPEVY 241
Cdd:MTH00182 167 ITTIFNMRAPGVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPEVY 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 242 VLILPGFGMISHVYVHYCRKERVFGKIGMVYAMVSIGILGFIVWAHHMFTVGLNVDTRAYFTAATMIIAVPTGVKVFSWV 321
Cdd:MTH00182 247 ILILPGFGMISQIIPTFVAKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFSWL 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 322 ATAWGSpRISFSASMLYGVGFLVLFTVGGLTGIMLSNSCLDVVLHDTYYVTGHFHYVLSMGAVFSIFSGFYYWFPLFTGI 401
Cdd:MTH00182 327 ATIYGG-TLRLDTPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGY 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 402 CFDLPLTRAQFFINFFGVNITFFPHHFMGLNGMPRRYVDYCDVFKVWHGISSYGSFMSFLASYFFLMLLGETFLVQRPML 481
Cdd:MTH00182 406 CYNELYGKIHFWLMFIGVNLTFFPQHFLGLAGFPRRYSDFADAFAGWNLVSSLGSIISIVGVVWFIYIIYDAYVREEKFI 485
|
490 500
....*....|....*....|....*.
gi 2732679549 482 ----FSLHSRCAREWLIDSSVPRHTW 503
Cdd:MTH00182 486 gwkeGTGESWASLEWVHSSPPLFHTY 511
|
|
| COX1 |
MTH00184 |
cytochrome c oxidase subunit I; Provisional |
2-479 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177235 Cd Length: 519 Bit Score: 585.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 2 RWFVSTNHKDIGTLYFIVGLWAGLMGMSLSLAIRMNLRVPGSQLFDPHLYNVIVTAHALIMIFFMVMPVMMGGFGNWLVP 81
Cdd:MTH00184 7 RWLFSTNHKDIGTLYLLFGAFAGMIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWFVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 82 LMLGVPDMCYPRLNNLSFWLVPFALLCLIFSMVVEKGAGTGWTIYPPLSSYLFHTGASVDLACFSLHLSGLSSLLAAVNF 161
Cdd:MTH00184 87 LYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAMNF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 162 MATVIMMRPNDQNWEKVPLFACSMCVTSFLLLISLPVLAGGVTMLIADRHFNTTFFIPSGGGDPILFQHLFWFFGHPEVY 241
Cdd:MTH00184 167 ITTIFNMRAPGITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEVY 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 242 VLILPGFGMISHVYVHYCRKERVFGKIGMVYAMVSIGILGFIVWAHHMFTVGLNVDTRAYFTAATMIIAVPTGVKVFSWV 321
Cdd:MTH00184 247 ILILPGFGIISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIFSWI 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 322 ATAWGSpRISFSASMLYGVGFLVLFTVGGLTGIMLSNSCLDVVLHDTYYVTGHFHYVLSMGAVFSIFSGFYYWFPLFTGI 401
Cdd:MTH00184 327 ATIFGG-SLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITGY 405
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2732679549 402 CFDLPLTRAQFFINFFGVNITFFPHHFMGLNGMPRRYVDYCDVFKVWHGISSYGSFMSFLASYFFLMLLGETFLVQRP 479
Cdd:MTH00184 406 CYNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDSFAGWNQISSLGSVISIVGVVWFIYIVYDAYVREIK 483
|
|
| Heme_Cu_Oxidase_I |
cd00919 |
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ... |
9-474 |
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: 535.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 9 HKDIGTLYFIVGLWAGLMGMSLSLAIRMNLRVPGSQLFDPHLYNVIVTAHALIMIFFMVMPVMMGGFGNWLVPlMLGVPD 88
Cdd:cd00919 1 HKDIGLLYLIFAFVALLLGGLLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 89 MCYPRLNNLSFWLVPFALLCLIFSMVVEKGAGTGWTIYPPLSSYLFHTGASVDLACFSLHLSGLSSLLAAVNFMATVIMM 168
Cdd:cd00919 80 LAFPRLNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 169 RPNDQNWEKVPLFACSMCVTSFLLLISLPVLAGGVTMLIADRHFNTTFFIPSGGGDPILFQHLFWFFGHPEVYVLILPGF 248
Cdd:cd00919 160 RAPGMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 249 GMISHVYVHYCRKeRVFGKIGMVYAMVSIGILGFIVWAHHMFTVGLNVDTRAYFTAATMIIAVPTGVKVFSWVATAWGSp 328
Cdd:cd00919 240 GAISEIIPTFSGK-PLFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGG- 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 329 RISFSASMLYGVGFLVLFTVGGLTGIMLSNSCLDVVLHDTYYVTGHFHYVLSMGAVFSIFSGFYYWFPLFTGICFDLPLT 408
Cdd:cd00919 318 RIRFDPPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKLG 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2732679549 409 RAQFFINFFGVNITFFPHHFMGLNGMPRRYVDYCDVFKVWHGISSYGSFMSFLASYFFLMLLGETF 474
Cdd:cd00919 398 KIHFWLWFIGFNLTFFPMHFLGLLGMPRRYADYPDGFAPWNFISSVGAFILGLGLLLFLGNLFLSL 463
|
|
| COX1 |
MTH00026 |
cytochrome c oxidase subunit I; Provisional |
1-479 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 164599 Cd Length: 534 Bit Score: 530.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 1 MRWFVSTNHKDIGTLYFIVGLWAGLMGMSLSLAIRMNLRVPGSQLFDPHLYNVIVTAHALIMIFFMVMPVMMGGFGNWLV 80
Cdd:MTH00026 5 VRWFFSCNHKDIGSLYLVFGALSGAIGTAFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWFV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 81 PLMLGVPDMCYPRLNNLSFWLVPFALLCLIFSMVVEKGAGTGWTIYPPLSSYLFHTGASVDLACFSLHLSGLSSLLAAVN 160
Cdd:MTH00026 85 PLMIGAPDMAFPRLNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAMN 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 161 FMATVIMMRPNDQNWEKVPLFACSMCVTSFLLLISLPVLAGGVTMLIADRHFNTTFFIPSGGGDPILFQHLFWFFGHPEV 240
Cdd:MTH00026 165 FITTVMNMRTPGMTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPEV 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 241 YVLILPGFGMISHVYVHYCRKERVFGKIGMVYAMVSIGILGFIVWAHHMFTVGLNVDTRAYFTAATMIIAVPTGVKVFSW 320
Cdd:MTH00026 245 YILILPGFGIISQILSLFSYKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFSW 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 321 VATAWGSPR-ISFSASMLYGVGFLVLFTVGGLTGIMLSNSCLDVVLHDTYYVTGHFHYVLSMGAVFSIFSGFYYWFPLFT 399
Cdd:MTH00026 325 LATVSGSGRnLIFTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWFGKIT 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 400 GICFDLPLTRAQFFINFFGVNITFFPHHFMGLNGMPRRYVDYCDVFKVWHGISSYGSFMSFLASYFFLMLLGETFLVQRP 479
Cdd:MTH00026 405 GYAYKDIYGLIHFWLMFIGVNITFFPQHFLGLAGLPRRYADYPDNFEDFNQISSFGSIISIIAVIWFIVVIFDAYYREEP 484
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
6-503 |
1.31e-180 |
|
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: 517.16 E-value: 1.31e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 6 STNHKDIGTLYFIVGLWAGLMGMSLSLAIRMNLRVPGSQLFDPHLYNVIVTAHALIMIFFMVMPvMMGGFGNWLVPLMLG 85
Cdd:TIGR02891 3 TVDHKRIGILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIP-ILAGFGNYLLPLMIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 86 VPDMCYPRLNNLSFWLVPFALLCLIFSMVVEKGAGTGWTIYPPLSSYLFHTGASVDLACFSLHLSGLSSLLAAVNFMATV 165
Cdd:TIGR02891 82 ARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIVTI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 166 IMMRPNDQNWEKVPLFACSMCVTSFLLLISLPVLAGGVTMLIADRHFNTTFFIPSGGGDPILFQHLFWFFGHPEVYVLIL 245
Cdd:TIGR02891 162 LNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYIIFL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 246 PGFGMISHVYVHYCRKeRVFGKIGMVYAMVSIGILGFIVWAHHMFTVGLNVDTRAYFTAATMIIAVPTGVKVFSWVATAW 325
Cdd:TIGR02891 242 PAFGIISEILPTFARK-PIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATLW 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 326 GSpRISFSASMLYGVGFLVLFTVGGLTGIMLSNSCLDVVLHDTYYVTGHFHYVLSMGAVFSIFSGFYYWFPLFTGICFDL 405
Cdd:TIGR02891 321 GG-SIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 406 PLTRAQFFINFFGVNITFFPHHFMGLNGMPRRYVDYCD--VFKVWHGISSYGSFMSFLASYFFLMLLGETFLVQRpmlfs 483
Cdd:TIGR02891 400 RLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPqmGFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGP----- 474
|
490 500
....*....|....*....|....*...
gi 2732679549 484 lhsRCAR--------EWLIDSSVPRHTW 503
Cdd:TIGR02891 475 ---KAGAnpwgattlEWTTSSPPPAHNF 499
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
1-467 |
1.07e-179 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 516.22 E-value: 1.07e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 1 MRWFVSTNHKDIGTLYFIVGLWAGLMGMSLSLAIRMNLRVPGSQLFDPHLYNVIVTAHALIMIFFMVMPvMMGGFGNWLV 80
Cdd:COG0843 7 RRWLTTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYLV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 81 PLMLGVPDMCYPRLNNLSFWLVPFALLCLIFSMVVEKGAGTGWTIYPPLSSYLFHTGASVDLACFSLHLSGLSSLLAAVN 160
Cdd:COG0843 86 PLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGVN 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 161 FMATVIMMRPNDQNWEKVPLFACSMCVTSFLLLISLPVLAGGVTMLIADRHFNTTFFIPSGGGDPILFQHLFWFFGHPEV 240
Cdd:COG0843 166 FIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPEV 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 241 YVLILPGFGMISHVYVHYCRKeRVFGKIGMVYAMVSIGILGFIVWAHHMFTVGLNVDTRAYFTAATMIIAVPTGVKVFSW 320
Cdd:COG0843 246 YILILPAFGIVSEIIPTFSRK-PLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNW 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 321 VATAWGSpRISFSASMLYGVGFLVLFTVGGLTGIMLSNSCLDVVLHDTYYVTGHFHYVLSMGAVFSIFSGFYYWFPLFTG 400
Cdd:COG0843 325 IATMWRG-RIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTG 403
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2732679549 401 ICFDLPLTRAQFFINFFGVNITFFPHHFMGLNGMPRRYVDY--CDVFKVWHGISSYGSFMSFLASYFFL 467
Cdd:COG0843 404 RMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYppEPGWQPLNLISTIGAFILAVGFLLFL 472
|
|
| COX1 |
MTH00048 |
cytochrome c oxidase subunit I; Provisional |
1-502 |
1.37e-156 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177123 Cd Length: 511 Bit Score: 456.45 E-value: 1.37e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 1 MRWFVSTNHKDIGTLYFIVGLWAGLMGMSLSLAIRMNLRVPGSQLFDPHLYNVIVTAHALIMIFFMVMPVMMGGFGNWLV 80
Cdd:MTH00048 5 LSWLFTLDHKRIGVIYTLLGVWSGFVGLSLSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 81 PLMLGVPDMCYPRLNNLSFWLVPFALLCLIFSMVveKGAGTGWTIYPPLSSYLFHTGASVDLACFSLHLSGLSSLLAAVN 160
Cdd:MTH00048 85 PLLLGLSDLNLPRLNALSAWLLVPSIVFLLLSMC--LGAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSIN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 161 FMATVIMMRPNDQNwEKVPLFACSMCVTSFLLLISLPVLAGGVTMLIADRHFNTTFFIPSGGGDPILFQHLFWFFGHPEV 240
Cdd:MTH00048 163 FICTIYSAFMTNVF-SRTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPEV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 241 YVLILPGFGMISHVYVHYCRKERVFGKIGMVYAMVSIGILGFIVWAHHMFTVGLNVDTRAYFTAATMIIAVPTGVKVFSW 320
Cdd:MTH00048 242 YVLILPGFGIISHICLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIKVFSW 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 321 VATAWGSPRISFSASMLYGVGFLVLFTVGGLTGIMLSNSCLDVVLHDTYYVTGHFHYVLSMGAVFSIFSGFYYWFPLFTG 400
Cdd:MTH00048 322 LYMLLNSRVRKSDPVVWWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWPLITG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 401 ICFDLPLTRAQFFINFFGVNITFFPHHFMGLNGMPRRYVDYCDVFKVWHGISSYGSFMSFLASYFFLMLLGETFLVQRPM 480
Cdd:MTH00048 402 LSLNKYLLQCHCIISMIGFNLCFFPMHYFGLCGLPRRVCVYEPSYYWINVVCTVGSFISAFSGCFFVFILWESLVVKNEV 481
|
490 500
....*....|....*....|..
gi 2732679549 481 LFSLHSRCAREWLIDSSVPRHT 502
Cdd:MTH00048 482 LGLWGSSSCVVNVLMSPVPYHN 503
|
|
| Ubiquinol_Oxidase_I |
cd01662 |
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ... |
3-501 |
1.54e-155 |
|
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: 453.19 E-value: 1.54e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 3 WFVSTNHKDIGTLYFIVGLWAGLMGMSLSLAIRMNLRVPGSQLFDPHLYNVIVTAHALIMIFFMVMPvMMGGFGNWLVPL 82
Cdd:cd01662 1 WLTTVDHKRIGIMYIITAFVFFLRGGVDALLMRTQLALPGNDFLSPEHYNQIFTMHGTIMIFLFAMP-LVFGLMNYLVPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 83 MLGVPDMCYPRLNNLSFWLVPFALLCLIFSMVVEKGAGTGWTIYPPLSSYLFHTGASVDLACFSLHLSGLSSLLAAVNFM 162
Cdd:cd01662 80 QIGARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 163 ATVIMMRPNDQNWEKVPLFACSMCVTSFLLLISLPVLAGGVTMLIADRHFNTTFFIPSGGGDPILFQHLFWFFGHPEVYV 242
Cdd:cd01662 160 VTILKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 243 LILPGFGMISHVYVHYCRKeRVFGKIGMVYAMVSIGILGFIVWAHHMFTVGLNVDTRAYFTAATMIIAVPTGVKVFSWVA 322
Cdd:cd01662 240 LILPAFGIFSEIVPTFSRK-PLFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 323 TAWGSpRISFSASMLYGVGFLVLFTVGGLTGIMLSNSCLDVVLHDTYYVTGHFHYVLSMGAVFSIFSGFYYWFPLFTGIC 402
Cdd:cd01662 319 TMWRG-RIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRM 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 403 FDLPLTRAQFFINFFGVNITFFPHHFMGLNGMPRRYVDYCDV--FKVWHGISSYGSFMSFLASYFFLMLLGETFLvQRPM 480
Cdd:cd01662 398 LNERLGKWSFWLWFIGFNLTFFPMHILGLMGMPRRVYTYLPGpgWDPLNLISTIGAFLIAAGVLLFLINVIVSIR-KGKR 476
|
490 500
....*....|....*....|...
gi 2732679549 481 LFSLHSRCAR--EWLIDSSVPRH 501
Cdd:cd01662 477 DATGDPWGARtlEWATSSPPPAY 499
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
11-458 |
3.65e-124 |
|
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: 370.75 E-value: 3.65e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 11 DIGTLYFIVGLWAGLMGMSLSLAIRMNLRVPGSQLFDPHLYNVIVTAHALIMIFFMVMPVMMGgFGNWLVPLMLGVPDMC 90
Cdd:pfam00115 1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATPFLFG-FGNYLVPLMIGARDMA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 91 YPRLNNLSFWLVPFALLCLIFSMVvekGAGTGWTIYPPLssylfhtgASVDLACFSLHLSGLSSLLAAVNFMATVIMMRP 170
Cdd:pfam00115 80 FPRLNALSFWLVVLGAVLLLASFG---GATTGWTEYPPL--------VGVDLWYIGLLLAGVSSLLGAINFIVTILKRRA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 171 NDQNWeKVPLFACSMCVTSFLLLISLPVLAGGVTMLIADRHFNTtffipsGGGDPILFQHLFWFFGHPEVYVLILPGFGM 250
Cdd:pfam00115 149 PGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLGA------GGGDPLLDQHLFWWFGHPEVYILILPAFGI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 251 ISHVYVHYCRKeRVFGKIGMVYAMVSIGILGFIVWAHHMFTVGLNVDTRAYFTAATMIIAVPTGVKVFSWVATAWGSPRI 330
Cdd:pfam00115 222 IYYILPKFAGR-PLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIR 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 331 SFSASMLYGVGFLVLFTVGGLTGIMLSNSCLDVVLHDTYYVTGHFHYVLSMGAVFSIFSGFYYWFPLFTGICFDLPLTRA 410
Cdd:pfam00115 301 FRTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKL 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 2732679549 411 QFFINFFGVNITFFPHHFMGLNGMPRRY----VDYCDVFKVWHGISSYGSFM 458
Cdd:pfam00115 381 HFWLLFIGFNLTFFPMHILGLLGMPRRYappfIETVPAFQPLNWIRTIGGVL 432
|
|
| CyoB |
TIGR02843 |
cytochrome o ubiquinol oxidase, subunit I; Cytochrome o terminal oxidase complex is the ... |
3-468 |
2.14e-109 |
|
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: 339.73 E-value: 2.14e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 3 WFVSTNHKDIGTLYFIVGLWAGLMGMSLSLAIRMN--LRVPGSQLF-DPHLYNVIVTAHALIMIFFMVMPVMMGGFgNWL 79
Cdd:TIGR02843 47 WLTTVDHKKIGIMYIIVALVMLLRGFADAIMMRTQqaLASGGSAGYlPPHHYDQIFTAHGVIMIFFVAMPFVFGLM-NLV 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 80 VPLMLGVPDMCYPRLNNLSFWLVPFALLCLIFSMVVEKGAGTGWTIYPPLSSYLFHTGASVDLACFSLHLSGLSSLLAAV 159
Cdd:TIGR02843 126 VPLQIGARDVAFPFLNSLSFWLTVVGAILVNVSLGVGEFAQTGWLAYPPLSELQYSPGVGVDYYIWALQISGIGTLLTGI 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 160 NFMATVIMMRPNDQNWEKVPLFACSMCVTSFLLLISLPVLAGGVTMLIADRHFNTTFFIPSGGGDPILFQHLFWFFGHPE 239
Cdd:TIGR02843 206 NFFVTIIKMRAPGMTLMKMPVFTWTSLCSNVLIIASFPILTVTLALLTLDRYLGMHFFTNEAGGNPMMYVNLIWAWGHPE 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 240 VYVLILPGFGMISHVYVHYCRKeRVFGKIGMVYAMVSIGILGFIVWAHHMFTVGLNVDTRAYFTAATMIIAVPTGVKVFS 319
Cdd:TIGR02843 286 VYILILPAFGIFSEVVATFSRK-RLFGYTSMVWATIAITVLSFIVWLHHFFTMGAGANVNAFFGIATMIIAIPTGVKIFN 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 320 WVATAWGSpRISFSASMLYGVGFLVLFTVGGLTGIMLSNSCLDVVLHDTYYVTGHFHYVLSMGAVFSIFSGFYYWFPLFT 399
Cdd:TIGR02843 365 WLFTMYKG-RIRFETPMLWTIGFMVTFSIGGMTGVLLAVPPADFVLHNSLFLIAHFHNVIIGGVVFGCFAGLTYWFPKAF 443
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 400 GICFDLPLTRAQFFINFFGVNITFFPHHFMGLNGMPRRYVDYCDV-FKVWHGISSYGSFMSFLASYFFLM 468
Cdd:TIGR02843 444 GFKLNEKLGKRSFWCWFIGFYLAFMPLYILGFMGMTRRLNHYDNPeWHPMLIIAAFGAFLIACGILCQII 513
|
|
| QoxB |
TIGR02882 |
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ... |
3-441 |
6.88e-98 |
|
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: 309.86 E-value: 6.88e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 3 WFVSTNHKDIGTLYFIVGLWAGLMGMSLSLAIRMNLRVPGSQLFDPHLYNVIVTAHALIMIFFMVMPVMMGgFGNWLVPL 82
Cdd:TIGR02882 44 WLTTVDHKKIGVMYIICAVLMLFRGGIDALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 83 MLGVPDMCYPRLNNLSFWLVPFALLCLIFSMVVEKGAGTGWTIYPPLSSYLFHTGASVDLACFSLHLSGLSSLLAAVNFM 162
Cdd:TIGR02882 123 QIGARDVAFPVLNALSFWLFFAGAMLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFF 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 163 ATVIMMRPNDQNWEKVPLFACSMCVTSFLLLISLPVLAGGVTMLIADRHFNTTFFIPSGGGDPILFQHLFWFFGHPEVYV 242
Cdd:TIGR02882 203 VTILKMRAPGMKLMQMPMFTWTTLITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLFWIWGHPEVYI 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 243 LILPGFGMISHVYVHYCRKeRVFGKIGMVYAMVSIGILGFIVWAHHMFTVGLNVDTRAYFTAATMIIAVPTGVKVFSWVA 322
Cdd:TIGR02882 283 VILPAFGIYSEIISTFAQK-RLFGYKSMVWSTVGIAFLSFLVWVHHFFTMGNGALINSFFSITTMAIAIPTGVKIFNWLL 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 323 TAWGSpRISFSASMLYGVGFLVLFTVGGLTGIMLSNSCLDVVLHDTYYVTGHFHYVLSMGAVFSIFSGFYYWFPLFTGIC 402
Cdd:TIGR02882 362 TLYKG-KIRFTTPMLFSLAFIPNFLIGGVTGVMLAMASADYQYHNTYFLVAHFHYVLITGVVFACLAGLIYWYPKMFGYK 440
|
410 420 430
....*....|....*....|....*....|....*....
gi 2732679549 403 FDLPLTRAQFFINFFGVNITFFPHHFMGLNGMPRRYVDY 441
Cdd:TIGR02882 441 LNERLGKWCFWFFMIGFNVCFFPMYILGLDGMPRRMYTY 479
|
|
| PRK15017 |
PRK15017 |
cytochrome o ubiquinol oxidase subunit I; Provisional |
3-437 |
7.27e-95 |
|
cytochrome o ubiquinol oxidase subunit I; Provisional
Pssm-ID: 184978 Cd Length: 663 Bit Score: 302.62 E-value: 7.27e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 3 WFVSTNHKDIGTLYFIVGLWAGLMGMSLSLAIRMNLRVPGSQ---LFDPHLYNVIVTAHALIMIFFMVMPVMMGgFGNWL 79
Cdd:PRK15017 48 WLTSVDHKRLGIMYIIVAIVMLLRGFADAIMMRSQQALASAGeagFLPPHHYDQIFTAHGVIMIFFVAMPFVIG-LMNLV 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 80 VPLMLGVPDMCYPRLNNLSFWLVPFALLCLIFSMVVEKGAGTGWTIYPPLSSYLFHTGASVDLACFSLHLSGLSSLLAAV 159
Cdd:PRK15017 127 VPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTTLTGI 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 160 NFMATVIMMRPNDQNWEKVPLFACSMCVTSFLLLISLPVLAGGVTMLIADRHFNTTFFIPSGGGDPILFQHLFWFFGHPE 239
Cdd:PRK15017 207 NFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWGHPE 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 240 VYVLILPGFGMISHVYVHYCRKeRVFGKIGMVYAMVSIGILGFIVWAHHMFTVGLNVDTRAYFTAATMIIAVPTGVKVFS 319
Cdd:PRK15017 287 VYILILPVFGVFSEIAATFSRK-RLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVKIFN 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 320 WVATAWGSpRISFSASMLYGVGFLVLFTVGGLTGIMLSNSCLDVVLHDTYYVTGHFHYVLSMGAVFSIFSGFYYWFPLFT 399
Cdd:PRK15017 366 WLFTMYQG-RIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYWWPKAF 444
|
410 420 430
....*....|....*....|....*....|....*...
gi 2732679549 400 GICFDLPLTRAQFFINFFGVNITFFPHHFMGLNGMPRR 437
Cdd:PRK15017 445 GFKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMTRR 482
|
|
| ba3-like_Oxidase_I |
cd01660 |
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ... |
45-475 |
3.47e-18 |
|
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: 87.34 E-value: 3.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 45 LFDPHLYNVIVTAHALIMIFFMVMPVMMGgFGNWLVPLMLGVPDMcYPRLNNLSFWLVPFALLCLIFSMVVEKgAGTGWT 124
Cdd:cd01660 38 PSSGILYYQGLTLHGVLLAIVFTTFFIMG-FFYAIVARALLRSLF-NRRLAWAGFWLMVIGTVMAAVPILLGQ-ASVLYT 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 125 IYPPL-SSYLFHTGASVdlacfslhLSGLSSLLAAVNFMATVIMMRPNDQnwEKVPLFAcSMCVTSFLL--LISLPVLAG 201
Cdd:cd01660 115 FYPPLqAHPLFYIGAAL--------VVVGSWISGFAMFVTLWRWKKANPG--KKVPLAT-FMVVTTMILwlVASLGVALE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 202 GVTMLIADRHFNTTffipsgGGDPILFQHLFWFFGHPEVYVLILPGFgMISHVYVHYCRKERVFGKIGMVYAMVSIGILG 281
Cdd:cd01660 184 VLFQLLPWSLGLVD------TVDVLLSRTLFWWFGHPLVYFWLLPAY-IAWYTILPKIAGGKLFSDPLARLAFILFLLFS 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 282 FIVWAHHMFT-VGLNVDTRAYFTAATMIIAVPTGVKVFSWVAT--------------------AWGSPRisFSASMLYgv 340
Cdd:cd01660 257 TPVGFHHQFAdPGIGPGWKFIHMVLTFMVALPSLLTAFTVFASleiagrlrggkglfgwiralPWGDPM--FLALFLA-- 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732679549 341 gfLVLFTVGGLTGIMLSNSCLDVVLHDTYYVTGHFHYVLSmGAVFSIFSGFYYWF-PLFTGICFDLP-LTRAQFFINFFG 418
Cdd:cd01660 333 --MLMFIPGGAGGIINASYQLNYVVHNTAWVPGHFHLTVG-GAVALTFMAVAYWLvPHLTGRELAAKrLALAQPWLWFVG 409
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2732679549 419 VNITFFPHHFMGLNGMPRR--YVDYCDVFKV-----WHGISSYGSFMSFLASYFFLMLLGETFL 475
Cdd:cd01660 410 MTIMSTAMHVAGLLGAPRRtaEAQYGGLPAAgewapYQQLMAIGGTILFVSGALFLYILFRTLL 473
|
|
| |
