|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00116 |
cytochrome c oxidase subunit I; Provisional |
1-514 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177177 Cd Length: 515 Bit Score: 953.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 1 MAITRWFFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGN 80
Cdd:MTH00116 1 MFITRWLFSTNHKDIGTLYLIFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 81 WLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLASNLAHAGASVDLTIFSLHLAGISSILG 160
Cdd:MTH00116 81 WLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 161 AINFITTILNMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGH 240
Cdd:MTH00116 161 AINFITTCINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 241 PEVYILILPGFGMISHIVAYYAGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMLQ-GMDVDTRAYFTSATMIIAIPTGVKV 319
Cdd:MTH00116 241 PEVYILILPGFGIISHIVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTvGMDVDTRAYFTSATMIIAIPTGIKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 320 FSWLATLHGGSIKWETPLLWSLGFIFLFTVGGLTGIVLANSSLDITLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLL 399
Cdd:MTH00116 321 FSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 400 TGYTLHNTWSKAHFGVMFLGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSLGSLISLIAVIMFLFIIWEAFAAKR 479
Cdd:MTH00116 401 TGYTLHQTWTKAQFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTISSIGSLISMTAVIMLMFIIWEAFSSKR 480
|
490 500 510
....*....|....*....|....*....|....*
gi 1861254773 480 VVASVPLTTTNIEWLHGCPPPYHTFEEPAFVQVQQ 514
Cdd:MTH00116 481 KVLQPELTTTNIEWIHGCPPPYHTFEEPAFVQVQE 515
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
10-495 |
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: 875.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 10 TNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGA 89
Cdd:cd01663 1 TNHKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 90 PDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLASNLAHAGASVDLTIFSLHLAGISSILGAINFITTIL 169
Cdd:cd01663 81 PDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 170 NMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILP 249
Cdd:cd01663 161 NMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 250 GFGMISHIVAYYAGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMLQ-GMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHG 328
Cdd:cd01663 241 GFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTvGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 329 GSIKWETPLLWSLGFIFLFTVGGLTGIVLANSSLDITLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLLTGYTLHNTW 408
Cdd:cd01663 321 GSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 409 SKAHFGVMFLGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSLGSLISLIAVIMFLFIIWEAFAAKRVV-ASVPLT 487
Cdd:cd01663 401 GKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKViFNVGEG 480
|
....*...
gi 1861254773 488 TTNIEWLH 495
Cdd:cd01663 481 STSLEWTL 488
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
3-507 |
0e+00 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 574.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 3 ITRWFFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPiMIGGFGNWL 82
Cdd:COG0843 6 WRRWLTTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 83 IPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLASNLAHAGASVDLTIFSLHLAGISSILGAI 162
Cdd:COG0843 85 VPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 163 NFITTILNMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPE 242
Cdd:COG0843 165 NFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 243 VYILILPGFGMISHIVAYYAGKKePFGYMGMVWAMMAIGLLGFIVWAHHMLQ-GMDVDTRAYFTSATMIIAIPTGVKVFS 321
Cdd:COG0843 245 VYILILPAFGIVSEIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTpGISPLVKAFFSIATMLIAVPTGVKVFN 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 322 WLATLHGGSIKWETPLLWSLGFIFLFTVGGLTGIVLANSSLDITLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLLTG 401
Cdd:COG0843 324 WIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTG 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 402 YTLHNTWSKAHFGVMFLGVNLTFFPQHFLGLAGMPRRYSDYP--DAYTLWNTVSSLGSLISLIAVIMFLFIIWEAFAAKR 479
Cdd:COG0843 404 RMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAFILAVGFLLFLINLVVSLRKGP 483
|
490 500
....*....|....*....|....*...
gi 1861254773 480 VVASVPLTTTNIEWLHGCPPPYHTFEEP 507
Cdd:COG0843 484 KAGGNPWGARTLEWATPSPPPLYNFASI 511
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
7-504 |
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: 568.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 7 FFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMiGGFGNWLIPLM 86
Cdd:TIGR02891 1 LTTVDHKRIGILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIPIL-AGFGNYLLPLM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 87 IGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLASNLAHAGASVDLTIFSLHLAGISSILGAINFIT 166
Cdd:TIGR02891 80 IGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 167 TILNMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYIL 246
Cdd:TIGR02891 160 TILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYII 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 247 ILPGFGMISHIVAYYAGKKePFGYMGMVWAMMAIGLLGFIVWAHHML-QGMDVDTRAYFTSATMIIAIPTGVKVFSWLAT 325
Cdd:TIGR02891 240 FLPAFGIISEILPTFARKP-IFGYRAMVYATVAIGFLSFGVWAHHMFtTGMPPLALAFFSAATMLIAVPTGVKVFNWIAT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 326 LHGGSIKWETPLLWSLGFIFLFTVGGLTGIVLANSSLDITLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLLTGYTLH 405
Cdd:TIGR02891 319 LWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYN 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 406 NTWSKAHFGVMFLGVNLTFFPQHFLGLAGMPRRYSDYPDA--YTLWNTVSSLGSLISLIAVIMFLFIIWEAFAAKRVVAS 483
Cdd:TIGR02891 399 ERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGPKAGA 478
|
490 500
....*....|....*....|.
gi 1861254773 484 VPLTTTNIEWLHGCPPPYHTF 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 ... |
14-459 |
6.90e-130 |
|
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: 384.62 E-value: 6.90e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 14 DIGTLYLVFGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPiMIGGFGNWLIPLMIGAPDMA 93
Cdd:pfam00115 1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 94 FPRMNNMSFWLLPPSFLLLLASSGveaGAGTGWTVYPPLASnlahagasVDLTIFSLHLAGISSILGAINFITTILNMKP 173
Cdd:pfam00115 80 FPRLNALSFWLVVLGAVLLLASFG---GATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 174 PAISQyQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNtsffdpAGGGDPILYQHLFWFFGHPEVYILILPGFGM 253
Cdd:pfam00115 149 PGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 254 ISHIVAYYAGKKePFGYMGMVWAMMAIGLLGFIVWAHHMLQ-GMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGSIK 332
Cdd:pfam00115 222 IYYILPKFAGRP-LFGYKLSVLAFWLIAFLGFLVWAHHLFTtGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIR 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 333 W-ETPLLWSLGFIFLFTVGGLTGIVLANSSLDITLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLLTGYTLHNTWSKA 411
Cdd:pfam00115 301 FrTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKL 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1861254773 412 HFGVMFLGVNLTFFPQHFLGLAGMPRRYS----DYPDAYTLWNTVSSLGSLI 459
Cdd:pfam00115 381 HFWLLFIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPLNWIRTIGGVL 432
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COX1 |
MTH00116 |
cytochrome c oxidase subunit I; Provisional |
1-514 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177177 Cd Length: 515 Bit Score: 953.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 1 MAITRWFFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGN 80
Cdd:MTH00116 1 MFITRWLFSTNHKDIGTLYLIFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 81 WLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLASNLAHAGASVDLTIFSLHLAGISSILG 160
Cdd:MTH00116 81 WLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 161 AINFITTILNMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGH 240
Cdd:MTH00116 161 AINFITTCINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 241 PEVYILILPGFGMISHIVAYYAGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMLQ-GMDVDTRAYFTSATMIIAIPTGVKV 319
Cdd:MTH00116 241 PEVYILILPGFGIISHIVTYYAGKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTvGMDVDTRAYFTSATMIIAIPTGIKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 320 FSWLATLHGGSIKWETPLLWSLGFIFLFTVGGLTGIVLANSSLDITLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLL 399
Cdd:MTH00116 321 FSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 400 TGYTLHNTWSKAHFGVMFLGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSLGSLISLIAVIMFLFIIWEAFAAKR 479
Cdd:MTH00116 401 TGYTLHQTWTKAQFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTISSIGSLISMTAVIMLMFIIWEAFSSKR 480
|
490 500 510
....*....|....*....|....*....|....*
gi 1861254773 480 VVASVPLTTTNIEWLHGCPPPYHTFEEPAFVQVQQ 514
Cdd:MTH00116 481 KVLQPELTTTNIEWIHGCPPPYHTFEEPAFVQVQE 515
|
|
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
5-506 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 947.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 5 RWFFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIP 84
Cdd:MTH00153 3 KWLFSTNHKDIGTLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWLVP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 85 LMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLASNLAHAGASVDLTIFSLHLAGISSILGAINF 164
Cdd:MTH00153 83 LMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAINF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 165 ITTILNMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 244
Cdd:MTH00153 163 ITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 245 ILILPGFGMISHIVAYYAGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMLQ-GMDVDTRAYFTSATMIIAIPTGVKVFSWL 323
Cdd:MTH00153 243 ILILPGFGMISHIISQESGKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTvGMDVDTRAYFTSATMIIAVPTGIKIFSWL 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 324 ATLHGGSIKWETPLLWSLGFIFLFTVGGLTGIVLANSSLDITLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLLTGYT 403
Cdd:MTH00153 323 ATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFTGLT 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 404 LHNTWSKAHFGVMFLGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSLGSLISLIAVIMFLFIIWEAFAAKRVVAS 483
Cdd:MTH00153 403 MNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKRPVLF 482
|
490 500
....*....|....*....|...
gi 1861254773 484 VPLTTTNIEWLHGCPPPYHTFEE 506
Cdd:MTH00153 483 SLNLSSSIEWLQNLPPAEHSYSE 505
|
|
| COX1 |
MTH00167 |
cytochrome c oxidase subunit I; Provisional |
1-511 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177222 Cd Length: 512 Bit Score: 925.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 1 MAITRWFFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGN 80
Cdd:MTH00167 1 MWINRWLFSTNHKDIGTLYFIFGAWAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 81 WLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLASNLAHAGASVDLTIFSLHLAGISSILG 160
Cdd:MTH00167 81 WLVPLMIGAPDMAFPRMNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSILG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 161 AINFITTILNMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGH 240
Cdd:MTH00167 161 SINFITTIINMKPPGITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 241 PEVYILILPGFGMISHIVAYYAGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMLQ-GMDVDTRAYFTSATMIIAIPTGVKV 319
Cdd:MTH00167 241 PEVYILILPGFGMISHIVVYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTvGMDVDTRAYFTSATMIIAVPTGIKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 320 FSWLATLHGGSIKWETPLLWSLGFIFLFTVGGLTGIVLANSSLDITLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLL 399
Cdd:MTH00167 321 FSWLATLHGGKIKWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 400 TGYTLHNTWSKAHFGVMFLGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSLGSLISLIAVIMFLFIIWEAFAAKR 479
Cdd:MTH00167 401 TGLTLNETWTKIHFFVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNVVSSIGSLISLVAVILFLFIIWEAFSSKR 480
|
490 500 510
....*....|....*....|....*....|..
gi 1861254773 480 VVASVPLTTTNIEWLHGCPPPYHTFEEPAFVQ 511
Cdd:MTH00167 481 KLLPVELTSTNVEWLHGCPPPHHTWEEPPFVQ 512
|
|
| COX1 |
MTH00183 |
cytochrome c oxidase subunit I; Provisional |
1-515 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177234 Cd Length: 516 Bit Score: 910.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 1 MAITRWFFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGN 80
Cdd:MTH00183 1 MAITRWFFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 81 WLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLASNLAHAGASVDLTIFSLHLAGISSILG 160
Cdd:MTH00183 81 WLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 161 AINFITTILNMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGH 240
Cdd:MTH00183 161 AINFITTIINMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 241 PEVYILILPGFGMISHIVAYYAGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMLQ-GMDVDTRAYFTSATMIIAIPTGVKV 319
Cdd:MTH00183 241 PEVYILILPGFGMISHIVAYYSGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTvGMDVDTRAYFTSATMIIAIPTGVKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 320 FSWLATLHGGSIKWETPLLWSLGFIFLFTVGGLTGIVLANSSLDITLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLL 399
Cdd:MTH00183 321 FSWLATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 400 TGYTLHNTWSKAHFGVMFLGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSLGSLISLIAVIMFLFIIWEAFAAKR 479
Cdd:MTH00183 401 SGYTLHSTWTKIHFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMFLFILWEAFAAKR 480
|
490 500 510
....*....|....*....|....*....|....*.
gi 1861254773 480 VVASVPLTTTNIEWLHGCPPPYHTFEEPAFVQVQQR 515
Cdd:MTH00183 481 EVLSVELTSTNVEWLHGCPPPYHTFEEPAFVQVQSN 516
|
|
| COX1 |
MTH00077 |
cytochrome c oxidase subunit I; Provisional |
1-513 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214419 Cd Length: 514 Bit Score: 877.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 1 MAITRWFFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGN 80
Cdd:MTH00077 1 MMITRWLFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 81 WLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLASNLAHAGASVDLTIFSLHLAGISSILG 160
Cdd:MTH00077 81 WLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 161 AINFITTILNMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGH 240
Cdd:MTH00077 161 AINFITTSINMKPPSMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 241 PEVYILILPGFGMISHIVAYYAGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMLQ-GMDVDTRAYFTSATMIIAIPTGVKV 319
Cdd:MTH00077 241 PEVYILILPGFGMISHIVTYYSAKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTvDLNVDTRAYFTSATMIIAIPTGVKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 320 FSWLATLHGGSIKWETPLLWSLGFIFLFTVGGLTGIVLANSSLDITLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLL 399
Cdd:MTH00077 321 FSWLATMHGGAIKWDAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 400 TGYTLHNTWSKAHFGVMFLGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSLGSLISLIAVIMFLFIIWEAFAAKR 479
Cdd:MTH00077 401 SGYTLHSTWSKIHFGVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMMMFIIWEAFSSKR 480
|
490 500 510
....*....|....*....|....*....|....
gi 1861254773 480 VVASVPLTTTNIEWLHGCPPPYHTFEEPAFVQVQ 513
Cdd:MTH00077 481 EVLTTELTSTNIEWLHGCPPPYHTFEEPSFVQTR 514
|
|
| Cyt_c_Oxidase_I |
cd01663 |
Cytochrome C oxidase subunit I. Cytochrome c oxidase (CcO), the terminal oxidase in the ... |
10-495 |
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: 875.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 10 TNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPLMIGA 89
Cdd:cd01663 1 TNHKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMIGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 90 PDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLASNLAHAGASVDLTIFSLHLAGISSILGAINFITTIL 169
Cdd:cd01663 81 PDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITTIF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 170 NMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILP 249
Cdd:cd01663 161 NMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 250 GFGMISHIVAYYAGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMLQ-GMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHG 328
Cdd:cd01663 241 GFGIISHIISTFSGKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTvGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMWG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 329 GSIKWETPLLWSLGFIFLFTVGGLTGIVLANSSLDITLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLLTGYTLHNTW 408
Cdd:cd01663 321 GSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNETL 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 409 SKAHFGVMFLGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSLGSLISLIAVIMFLFIIWEAFAAKRVV-ASVPLT 487
Cdd:cd01663 401 GKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKViFNVGEG 480
|
....*...
gi 1861254773 488 TTNIEWLH 495
Cdd:cd01663 481 STSLEWTL 488
|
|
| COX1 |
MTH00103 |
cytochrome c oxidase subunit I; Validated |
1-512 |
0e+00 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 177165 Cd Length: 513 Bit Score: 864.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 1 MAITRWFFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGN 80
Cdd:MTH00103 1 MFINRWLFSTNHKDIGTLYLLFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 81 WLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLASNLAHAGASVDLTIFSLHLAGISSILG 160
Cdd:MTH00103 81 WLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 161 AINFITTILNMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGH 240
Cdd:MTH00103 161 AINFITTIINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 241 PEVYILILPGFGMISHIVAYYAGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMLQ-GMDVDTRAYFTSATMIIAIPTGVKV 319
Cdd:MTH00103 241 PEVYILILPGFGMISHIVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTvGMDVDTRAYFTSATMIIAIPTGVKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 320 FSWLATLHGGSIKWETPLLWSLGFIFLFTVGGLTGIVLANSSLDITLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLL 399
Cdd:MTH00103 321 FSWLATLHGGNIKWSPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 400 TGYTLHNTWSKAHFGVMFLGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSLGSLISLIAVIMFLFIIWEAFAAKR 479
Cdd:MTH00103 401 SGYTLNDTWAKIHFTIMFVGVNMTFFPQHFLGLSGMPRRYSDYPDAYTTWNTVSSMGSFISLTAVMLMIFMIWEAFASKR 480
|
490 500 510
....*....|....*....|....*....|...
gi 1861254773 480 VVASVPLTTTNIEWLHGCPPPYHTFEEPAFVQV 512
Cdd:MTH00103 481 EVLTVELTTTNLEWLHGCPPPYHTFEEPTYVKL 513
|
|
| COX1 |
MTH00142 |
cytochrome c oxidase subunit I; Provisional |
3-507 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214431 Cd Length: 511 Bit Score: 829.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 3 ITRWFFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWL 82
Cdd:MTH00142 1 MMRWLFSTNHKDIGTLYFLFGAWAGMVGTGLSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNWL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 83 IPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLASNLAHAGASVDLTIFSLHLAGISSILGAI 162
Cdd:MTH00142 81 VPLMLGAPDMAFPRMNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 163 NFITTILNMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPE 242
Cdd:MTH00142 161 NFITTVINMRAGGMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 243 VYILILPGFGMISHIVAYYAGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMLQ-GMDVDTRAYFTSATMIIAIPTGVKVFS 321
Cdd:MTH00142 241 VYILILPGFGMISHIINHYSGKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTvGMDVDTRAYFTAATMVIAVPTGIKVFS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 322 WLATLHGGSIKWETPLLWSLGFIFLFTVGGLTGIVLANSSLDITLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLLTG 401
Cdd:MTH00142 321 WLATLHGSKVKYEPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLFTG 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 402 YTLHNTWSKAHFGVMFLGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSLGSLISLIAVIMFLFIIWEAFAAKRVV 481
Cdd:MTH00142 401 LTLNPRWLKAHFYTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSSLGSMISFIAVLMFVFIVWESFVSQRLV 480
|
490 500
....*....|....*....|....*.
gi 1861254773 482 ASVPLTTTNIEWLHGCPPPYHTFEEP 507
Cdd:MTH00142 481 MWSSHLSTSLEWSHRLPPDFHTYDEL 506
|
|
| COX1 |
MTH00223 |
cytochrome c oxidase subunit I; Provisional |
5-510 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177260 Cd Length: 512 Bit Score: 828.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 5 RWFFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIP 84
Cdd:MTH00223 2 RWLFSTNHKDIGTLYLIFGMWSGLVGTSLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNWLVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 85 LMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLASNLAHAGASVDLTIFSLHLAGISSILGAINF 164
Cdd:MTH00223 82 LMLGAPDMAFPRLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGAINF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 165 ITTILNMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 244
Cdd:MTH00223 162 ITTIINMRSPGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVY 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 245 ILILPGFGMISHIVAYYAGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMLQ-GMDVDTRAYFTSATMIIAIPTGVKVFSWL 323
Cdd:MTH00223 242 ILILPGFGMISHIVSHYSSKKEVFGTLGMIYAMLSIGVLGFIVWAHHMFTvGMDVDTRAYFTAATMIIAVPTGIKVFSWL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 324 ATLHGGSIKWETPLLWSLGFIFLFTVGGLTGIVLANSSLDITLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLLTGYT 403
Cdd:MTH00223 322 ATIYGSKIKYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLFTGVT 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 404 LHNTWSKAHFGVMFLGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSLGSLISLIAVIMFLFIIWEAFAAKRVVAS 483
Cdd:MTH00223 402 LHRRWAKAHFFLMFLGVNLTFFPQHFLGLAGMPRRYSDYPDCYTKWNQVSSFGSMISFVSVLFFMFIVWEAFVSQRSVVW 481
|
490 500
....*....|....*....|....*..
gi 1861254773 484 VPLTTTNIEWLHGCPPPYHTFEEPAFV 510
Cdd:MTH00223 482 SGHLSTSLEWDNLLPADFHNNSETGAL 508
|
|
| COX1 |
MTH00037 |
cytochrome c oxidase subunit I; Provisional |
1-510 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177112 Cd Length: 517 Bit Score: 775.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 1 MAITRWFFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGN 80
Cdd:MTH00037 1 MQLSRWLFSTNHKDIGTLYLIFGAWAGMVGTAMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGGFGN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 81 WLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLASNLAHAGASVDLTIFSLHLAGISSILG 160
Cdd:MTH00037 81 WLIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 161 AINFITTILNMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGH 240
Cdd:MTH00037 161 SINFITTIINMRTPGMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 241 PEVYILILPGFGMISHIVAYYAGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMLQ-GMDVDTRAYFTSATMIIAIPTGVKV 319
Cdd:MTH00037 241 PEVYILILPGFGMISHVIAHYSGKQEPFGYLGMVYAMIAIGILGFLVWAHHMFTvGMDVDTRAYFTAATMIIAVPTGIKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 320 FSWLATLHGGSIKWETPLLWSLGFIFLFTVGGLTGIVLANSSLDITLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLL 399
Cdd:MTH00037 321 FSWMATLQGSNLRWETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 400 TGYTLHNTWSKAHFGVMFLGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSLGSLISLIAVIMFLFIIWEAFAAKR 479
Cdd:MTH00037 401 SGVSLHPLWSKVHFFLMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSTISLVATLFFLFLIWEAFASQR 480
|
490 500 510
....*....|....*....|....*....|..
gi 1861254773 480 VVASVPLTTTNIEWLHGC-PPPYHTFEEPAFV 510
Cdd:MTH00037 481 EVISPEFSSSSLEWQYSSfPPSHHTFDETPST 512
|
|
| COX1 |
MTH00007 |
cytochrome c oxidase subunit I; Validated |
5-510 |
0e+00 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 133649 Cd Length: 511 Bit Score: 741.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 5 RWFFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIP 84
Cdd:MTH00007 2 RWLYSTNHKDIGTLYFILGVWGGLLGTSMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWLVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 85 LMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLASNLAHAGASVDLTIFSLHLAGISSILGAINF 164
Cdd:MTH00007 82 LMLGAPDMAFPRLNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAINF 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 165 ITTILNMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 244
Cdd:MTH00007 162 ITTVINMRWKGLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVY 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 245 ILILPGFGMISHIVAYYAGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMLQ-GMDVDTRAYFTSATMIIAIPTGVKVFSWL 323
Cdd:MTH00007 242 ILILPGFGAISHIVTHYAGKLEPFGTLGMIYAMLGIGVLGFIVWAHHMFTvGMDVDTRAYFTAATMIIAVPTGIKVFSWL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 324 ATLHGGSIKWETPLLWSLGFIFLFTVGGLTGIVLANSSLDITLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLLTGYT 403
Cdd:MTH00007 322 ATIHGSPIKYETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTGLT 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 404 LHNTWSKAHFGVMFLGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSLGSLISLIAVIMFLFIIWEAFAAKRVVAS 483
Cdd:MTH00007 402 LHDRWAKAHFFLMFLGVNLTFFPQHFLGLSGMPRRYSDYPDAYTKWNVVSSFGSMLSFVALLLFIFILWEAFSAQRGVIA 481
|
490 500
....*....|....*....|....*..
gi 1861254773 484 VPLTTTNIEWLHGCPPPYHTFEEPAFV 510
Cdd:MTH00007 482 SPHMSSSLEWQDTLPLDFHNLPETGII 508
|
|
| COX1 |
MTH00182 |
cytochrome c oxidase subunit I; Provisional |
3-511 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214451 Cd Length: 525 Bit Score: 692.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 3 ITRWFFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWL 82
Cdd:MTH00182 5 LTRWVFSTNHKDIGTLYLVFGAGAGMIGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGGFGNWL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 83 IPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLASNLAHAGASVDLTIFSLHLAGISSILGAI 162
Cdd:MTH00182 85 VPLYIGAPDMAFPRLNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVSSILGAI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 163 NFITTILNMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPE 242
Cdd:MTH00182 165 NFITTIFNMRAPGVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHPE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 243 VYILILPGFGMISHIVAYYAGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMLQ-GMDVDTRAYFTSATMIIAIPTGVKVFS 321
Cdd:MTH00182 245 VYILILPGFGMISQIIPTFVAKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTvGMDVDTRAYFTAATMIIAVPTGIKVFS 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 322 WLATLHGGSIKWETPLLWSLGFIFLFTVGGLTGIVLANSSLDITLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLLTG 401
Cdd:MTH00182 325 WLATIYGGTLRLDTPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 402 YTLHNTWSKAHFGVMFLGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSLGSLISLIAVIMFLFIIWEAFAAKRV- 480
Cdd:MTH00182 405 YCYNELYGKIHFWLMFIGVNLTFFPQHFLGLAGFPRRYSDFADAFAGWNLVSSLGSIISIVGVVWFIYIIYDAYVREEKf 484
|
490 500 510
....*....|....*....|....*....|....
gi 1861254773 481 ---VASVPLTTTNIEWLHGCPPPYHTFEEPAFVQ 511
Cdd:MTH00182 485 igwKEGTGESWASLEWVHSSPPLFHTYNELPFVY 518
|
|
| COX1 |
MTH00184 |
cytochrome c oxidase subunit I; Provisional |
3-510 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177235 Cd Length: 519 Bit Score: 677.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 3 ITRWFFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWL 82
Cdd:MTH00184 5 LSRWLFSTNHKDIGTLYLLFGAFAGMIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGGFGNWF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 83 IPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLASNLAHAGASVDLTIFSLHLAGISSILGAI 162
Cdd:MTH00184 85 VPLYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSILGAM 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 163 NFITTILNMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPE 242
Cdd:MTH00184 165 NFITTIFNMRAPGITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 243 VYILILPGFGMISHIVAYYAGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMLQ-GMDVDTRAYFTSATMIIAIPTGVKVFS 321
Cdd:MTH00184 245 VYILILPGFGIISQIIPTFAAKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTvGMDVDTRAYFTAATMIIAVPTGIKIFS 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 322 WLATLHGGSIKWETPLLWSLGFIFLFTVGGLTGIVLANSSLDITLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLLTG 401
Cdd:MTH00184 325 WIATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKITG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 402 YTLHNTWSKAHFGVMFLGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSLGSLISLIAVIMFLFIIWEAFAAKRVV 481
Cdd:MTH00184 405 YCYNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDSFAGWNQISSLGSVISIVGVVWFIYIVYDAYVREIKF 484
|
490 500 510
....*....|....*....|....*....|..
gi 1861254773 482 ---ASVPLTTTNIEWLHGCPPPYHTFEEPAFV 510
Cdd:MTH00184 485 vgwVEDSGHYPSLEWAQTSPPAHHTYNELPYV 516
|
|
| COX1 |
MTH00079 |
cytochrome c oxidase subunit I; Provisional |
6-506 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177148 Cd Length: 508 Bit Score: 652.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 6 WFFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPL 85
Cdd:MTH00079 7 WLESSNHKDIGTLYFLFGLWSGMVGTSLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNWMLPL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 86 MIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLaSNLAHAGASVDLTIFSLHLAGISSILGAINFI 165
Cdd:MTH00079 87 MLGAPDMSFPRLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPL-STLGHPGSSVDLAIFSLHCAGISSILGGINFM 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 166 TTILNMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYI 245
Cdd:MTH00079 166 VTTKNLRSSSISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHPEVYI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 246 LILPGFGMISHIVAYYAGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMLQ-GMDVDTRAYFTSATMIIAIPTGVKVFSWLA 324
Cdd:MTH00079 246 LILPAFGIISQSTLYLTGKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTvGMDLDSRAYFTAATMVIAVPTGVKVFSWLA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 325 TLHGGSIKWETPLLWSLGFIFLFTVGGLTGIVLANSSLDITLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLLTGYTL 404
Cdd:MTH00079 326 TLFGMKMKFQPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFMTGIVY 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 405 HNTWSKAHFGVMFLGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSLGSLISLIAVIMFLFIIWEAFAAKRVVASV 484
Cdd:MTH00079 406 DKLMMSAVFFLMFVGVNLTFFPLHFAGLHGMPRKYLDYPDVYSVWNVISSYGSMISVFALFLFIYVLLESFFSYRLVLHD 485
|
490 500
....*....|....*....|..
gi 1861254773 485 PLTTTNIEWLHGCPPPYHTFEE 506
Cdd:MTH00079 486 NYINSSPEYSLSSYVFGHSYQS 507
|
|
| COX1 |
MTH00026 |
cytochrome c oxidase subunit I; Provisional |
2-510 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 164599 Cd Length: 534 Bit Score: 602.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 2 AITRWFFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNW 81
Cdd:MTH00026 3 SFVRWFFSCNHKDIGSLYLVFGALSGAIGTAFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNW 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 82 LIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLASNLAHAGASVDLTIFSLHLAGISSILGA 161
Cdd:MTH00026 83 FVPLMIGAPDMAFPRLNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 162 INFITTILNMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHP 241
Cdd:MTH00026 163 MNFITTVMNMRTPGMTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHP 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 242 EVYILILPGFGMISHIVAYYAGKKEPFGYMGMVWAMMAIGLLGFIVWAHHM-LQGMDVDTRAYFTSATMIIAIPTGVKVF 320
Cdd:MTH00026 243 EVYILILPGFGIISQILSLFSYKKQIFGYLGMVYAMLAIGVLGFIVWAHHMyVVGMDVDTRAYFTAATMIIAVPTGIKIF 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 321 SWLATLHGG--SIKWETPLLWSLGFIFLFTVGGLTGIVLANSSLDITLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPL 398
Cdd:MTH00026 323 SWLATVSGSgrNLIFTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWFGK 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 399 LTGYTLHNTWSKAHFGVMFLGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSLGSLISLIAVIMFLFIIWEAFAAK 478
Cdd:MTH00026 403 ITGYAYKDIYGLIHFWLMFIGVNITFFPQHFLGLAGLPRRYADYPDNFEDFNQISSFGSIISIIAVIWFIVVIFDAYYRE 482
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1861254773 479 R-----VVASVPLTT--------TNIEWLHGCPPPYHTFEEPAFV 510
Cdd:MTH00026 483 EpfdinIMAKGPLIPfscqpahfDTLEWSLTSPPEHHTYNELPYI 527
|
|
| Heme_Cu_Oxidase_I |
cd00919 |
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ... |
12-475 |
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: 584.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 12 HKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPlMIGAPD 91
Cdd:cd00919 1 HKDIGLLYLIFAFVALLLGGLLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPP-LIGARD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 92 MAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLASNLAHAGASVDLTIFSLHLAGISSILGAINFITTILNM 171
Cdd:cd00919 80 LAFPRLNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTILNM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 172 KPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGF 251
Cdd:cd00919 160 RAPGMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 252 GMISHIVAYYAGKKePFGYMGMVWAMMAIGLLGFIVWAHHML-QGMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGS 330
Cdd:cd00919 240 GAISEIIPTFSGKP-LFGYKLMVYAFLAIGFLSFLVWAHHMFtVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 331 IKWETPLLWSLGFIFLFTVGGLTGIVLANSSLDITLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLLTGYTLHNTWSK 410
Cdd:cd00919 319 IRFDPPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKLGK 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1861254773 411 AHFGVMFLGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSLGSLISLIAVIMFLFIIWEAF 475
Cdd:cd00919 399 IHFWLWFIGFNLTFFPMHFLGLLGMPRRYADYPDGFAPWNFISSVGAFILGLGLLLFLGNLFLSL 463
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
3-507 |
0e+00 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 574.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 3 ITRWFFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPiMIGGFGNWL 82
Cdd:COG0843 6 WRRWLTTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATP-FLAGFGNYL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 83 IPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLASNLAHAGASVDLTIFSLHLAGISSILGAI 162
Cdd:COG0843 85 VPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 163 NFITTILNMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPE 242
Cdd:COG0843 165 NFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 243 VYILILPGFGMISHIVAYYAGKKePFGYMGMVWAMMAIGLLGFIVWAHHMLQ-GMDVDTRAYFTSATMIIAIPTGVKVFS 321
Cdd:COG0843 245 VYILILPAFGIVSEIIPTFSRKP-LFGYKAMVLATVAIAFLSFLVWAHHMFTpGISPLVKAFFSIATMLIAVPTGVKVFN 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 322 WLATLHGGSIKWETPLLWSLGFIFLFTVGGLTGIVLANSSLDITLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLLTG 401
Cdd:COG0843 324 WIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTG 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 402 YTLHNTWSKAHFGVMFLGVNLTFFPQHFLGLAGMPRRYSDYP--DAYTLWNTVSSLGSLISLIAVIMFLFIIWEAFAAKR 479
Cdd:COG0843 404 RMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAFILAVGFLLFLINLVVSLRKGP 483
|
490 500
....*....|....*....|....*...
gi 1861254773 480 VVASVPLTTTNIEWLHGCPPPYHTFEEP 507
Cdd:COG0843 484 KAGGNPWGARTLEWATPSPPPLYNFASI 511
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
7-504 |
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: 568.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 7 FFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMiGGFGNWLIPLM 86
Cdd:TIGR02891 1 LTTVDHKRIGILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIPIL-AGFGNYLLPLM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 87 IGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLASNLAHAGASVDLTIFSLHLAGISSILGAINFIT 166
Cdd:TIGR02891 80 IGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNFIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 167 TILNMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYIL 246
Cdd:TIGR02891 160 TILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYII 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 247 ILPGFGMISHIVAYYAGKKePFGYMGMVWAMMAIGLLGFIVWAHHML-QGMDVDTRAYFTSATMIIAIPTGVKVFSWLAT 325
Cdd:TIGR02891 240 FLPAFGIISEILPTFARKP-IFGYRAMVYATVAIGFLSFGVWAHHMFtTGMPPLALAFFSAATMLIAVPTGVKVFNWIAT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 326 LHGGSIKWETPLLWSLGFIFLFTVGGLTGIVLANSSLDITLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLLTGYTLH 405
Cdd:TIGR02891 319 LWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYN 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 406 NTWSKAHFGVMFLGVNLTFFPQHFLGLAGMPRRYSDYPDA--YTLWNTVSSLGSLISLIAVIMFLFIIWEAFAAKRVVAS 483
Cdd:TIGR02891 399 ERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGPKAGA 478
|
490 500
....*....|....*....|.
gi 1861254773 484 VPLTTTNIEWLHGCPPPYHTF 504
Cdd:TIGR02891 479 NPWGATTLEWTTSSPPPAHNF 499
|
|
| Ubiquinol_Oxidase_I |
cd01662 |
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ... |
6-504 |
2.08e-174 |
|
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: 500.96 E-value: 2.08e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 6 WFFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGgFGNWLIPL 85
Cdd:cd01662 1 WLTTVDHKRIGIMYIITAFVFFLRGGVDALLMRTQLALPGNDFLSPEHYNQIFTMHGTIMIFLFAMPLVFG-LMNYLVPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 86 MIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLASNLAHAGASVDLTIFSLHLAGISSILGAINFI 165
Cdd:cd01662 80 QIGARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAINFI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 166 TTILNMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYI 245
Cdd:cd01662 160 VTILKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 246 LILPGFGMISHIVAYYAGKKePFGYMGMVWAMMAIGLLGFIVWAHHML-QGMDVDTRAYFTSATMIIAIPTGVKVFSWLA 324
Cdd:cd01662 240 LILPAFGIFSEIVPTFSRKP-LFGYRSMVYATVAIGFLSFGVWVHHMFtTGAGALVNAFFSIATMIIAVPTGVKIFNWLF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 325 TLHGGSIKWETPLLWSLGFIFLFTVGGLTGIVLANSSLDITLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLLTGYTL 404
Cdd:cd01662 319 TMWRGRIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRML 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 405 HNTWSKAHFGVMFLGVNLTFFPQHFLGLAGMPRRYSDYP--DAYTLWNTVSSLGSLISLIAVIMFLF-IIWEAFAAKRVV 481
Cdd:cd01662 399 NERLGKWSFWLWFIGFNLTFFPMHILGLMGMPRRVYTYLpgPGWDPLNLISTIGAFLIAAGVLLFLInVIVSIRKGKRDA 478
|
490 500
....*....|....*....|...
gi 1861254773 482 ASVPLTTTNIEWLHGCPPPYHTF 504
Cdd:cd01662 479 TGDPWGARTLEWATSSPPPAYNF 501
|
|
| COX1 |
MTH00048 |
cytochrome c oxidase subunit I; Provisional |
6-481 |
3.02e-174 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177123 Cd Length: 511 Bit Score: 500.74 E-value: 3.02e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 6 WFFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNWLIPL 85
Cdd:MTH00048 7 WLFTLDHKRIGVIYTLLGVWSGFVGLSLSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGGFGNYLLPL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 86 MIGAPDMAFPRMNNMSFWLLPPSFLLLLASsgVEAGAGTGWTVYPPLASNLAHAGASVDLTIFSLHLAGISSILGAINFI 165
Cdd:MTH00048 87 LLGLSDLNLPRLNALSAWLLVPSIVFLLLS--MCLGAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLFGSINFI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 166 TTILNMKPPAISqYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYI 245
Cdd:MTH00048 165 CTIYSAFMTNVF-SRTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFGHPEVYV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 246 LILPGFGMISHIVAYYAGKKEPFGYMGMVWAMMAIGLLGFIVWAHHMLQ-GMDVDTRAYFTSATMIIAIPTGVKVFSWLA 324
Cdd:MTH00048 244 LILPGFGIISHICLSLSNNDDPFGYYGLVFAMFSIVCLGSVVWAHHMFTvGLDVKTAVFFSSVTMIIGVPTGIKVFSWLY 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 325 TLHGGSIKWETPLL-WSLGFIFLFTVGGLTGIVLANSSLDITLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLLTGYT 403
Cdd:MTH00048 324 MLLNSRVRKSDPVVwWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWPLITGLS 403
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1861254773 404 LHNTWSKAHFGVMFLGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSLGSLISLIAVIMFLFIIWEAFAAKRVV 481
Cdd:MTH00048 404 LNKYLLQCHCIISMIGFNLCFFPMHYFGLCGLPRRVCVYEPSYYWINVVCTVGSFISAFSGCFFVFILWESLVVKNEV 481
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
14-459 |
6.90e-130 |
|
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: 384.62 E-value: 6.90e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 14 DIGTLYLVFGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPiMIGGFGNWLIPLMIGAPDMA 93
Cdd:pfam00115 1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATP-FLFGFGNYLVPLMIGARDMA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 94 FPRMNNMSFWLLPPSFLLLLASSGveaGAGTGWTVYPPLASnlahagasVDLTIFSLHLAGISSILGAINFITTILNMKP 173
Cdd:pfam00115 80 FPRLNALSFWLVVLGAVLLLASFG---GATTGWTEYPPLVG--------VDLWYIGLLLAGVSSLLGAINFIVTILKRRA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 174 PAISQyQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNtsffdpAGGGDPILYQHLFWFFGHPEVYILILPGFGM 253
Cdd:pfam00115 149 PGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 254 ISHIVAYYAGKKePFGYMGMVWAMMAIGLLGFIVWAHHMLQ-GMDVDTRAYFTSATMIIAIPTGVKVFSWLATLHGGSIK 332
Cdd:pfam00115 222 IYYILPKFAGRP-LFGYKLSVLAFWLIAFLGFLVWAHHLFTtGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIR 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 333 W-ETPLLWSLGFIFLFTVGGLTGIVLANSSLDITLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLLTGYTLHNTWSKA 411
Cdd:pfam00115 301 FrTTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKL 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1861254773 412 HFGVMFLGVNLTFFPQHFLGLAGMPRRYS----DYPDAYTLWNTVSSLGSLI 459
Cdd:pfam00115 381 HFWLLFIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPLNWIRTIGGVL 432
|
|
| CyoB |
TIGR02843 |
cytochrome o ubiquinol oxidase, subunit I; Cytochrome o terminal oxidase complex is the ... |
4-511 |
1.74e-121 |
|
cytochrome o ubiquinol oxidase, subunit I; Cytochrome o terminal oxidase complex is the component of the aerobic respiratory chain which reacts with oxygen, reducing it to water with the concomitant transport of 4 protons across the membrane. Also known as the cytochrome bo complex, cytochrome o ubiquinol oxidase contains four subunits, two heme b cofactors and a copper atom which is believed to be the oxygen active site. This complex is structurally related to the cytochrome caa3 oxidases which utilize cytochrome c as the reductant and contain heme a cofactors, as well as the intermediate form aa3 oxidases which also react directly with quinones as the reductant. [Energy metabolism, Electron transport]
Pssm-ID: 131890 Cd Length: 646 Bit Score: 370.54 E-value: 1.74e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 4 TRWFFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELS-----QPGALLGDDqiYNVIVTAHAFVMIFFMVMPIMIGGF 78
Cdd:TIGR02843 45 NEWLTTVDHKKIGIMYIIVALVMLLRGFADAIMMRTQQAlasggSAGYLPPHH--YDQIFTAHGVIMIFFVAMPFVFGLM 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 79 gNWLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLASNLAHAGASVDLTIFSLHLAGISSI 158
Cdd:TIGR02843 123 -NLVVPLQIGARDVAFPFLNSLSFWLTVVGAILVNVSLGVGEFAQTGWLAYPPLSELQYSPGVGVDYYIWALQISGIGTL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 159 LGAINFITTILNMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFF 238
Cdd:TIGR02843 202 LTGINFFVTIIKMRAPGMTLMKMPVFTWTSLCSNVLIIASFPILTVTLALLTLDRYLGMHFFTNEAGGNPMMYVNLIWAW 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 239 GHPEVYILILPGFGMISHIVAYYAGKKEpFGYMGMVWAMMAIGLLGFIVWAHHML-QGMDVDTRAYFTSATMIIAIPTGV 317
Cdd:TIGR02843 282 GHPEVYILILPAFGIFSEVVATFSRKRL-FGYTSMVWATIAITVLSFIVWLHHFFtMGAGANVNAFFGIATMIIAIPTGV 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 318 KVFSWLATLHGGSIKWETPLLWSLGFIFLFTVGGLTGIVLANSSLDITLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFP 397
Cdd:TIGR02843 361 KIFNWLFTMYKGRIRFETPMLWTIGFMVTFSIGGMTGVLLAVPPADFVLHNSLFLIAHFHNVIIGGVVFGCFAGLTYWFP 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 398 LLTGYTLHNTWSKAHFGVMFLGVNLTFFPQHFLGLAGMPRRYSDYPD-AYTLWNTVSSLGSLISLIAVIMFLFIIWEAFA 476
Cdd:TIGR02843 441 KAFGFKLNEKLGKRSFWCWFIGFYLAFMPLYILGFMGMTRRLNHYDNpEWHPMLIIAAFGAFLIACGILCQIIQIFVSIR 520
|
490 500 510
....*....|....*....|....*....|....*...
gi 1861254773 477 AK---RVVASVPLTTTNIEWLHGCPPPYHTFEEPAFVQ 511
Cdd:TIGR02843 521 DRdqnRDTTGDPWGGRTLEWSTSSPPPFYNFAVIPKVQ 558
|
|
| QoxB |
TIGR02882 |
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ... |
6-504 |
2.00e-117 |
|
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: 359.94 E-value: 2.00e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 6 WFFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGgFGNWLIPL 85
Cdd:TIGR02882 44 WLTTVDHKKIGVMYIICAVLMLFRGGIDALLMRAQLTVPDNKFLDAQHYNEIFTTHGVIMIIFMAMPFIIG-LMNIVVPL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 86 MIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLASNLAHAGASVDLTIFSLHLAGISSILGAINFI 165
Cdd:TIGR02882 123 QIGARDVAFPVLNALSFWLFFAGAMLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGINFF 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 166 TTILNMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYI 245
Cdd:TIGR02882 203 VTILKMRAPGMKLMQMPMFTWTTLITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLFWIWGHPEVYI 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 246 LILPGFGMISHIVAYYAgKKEPFGYMGMVWAMMAIGLLGFIVWAHHML-QGMDVDTRAYFTSATMIIAIPTGVKVFSWLA 324
Cdd:TIGR02882 283 VILPAFGIYSEIISTFA-QKRLFGYKSMVWSTVGIAFLSFLVWVHHFFtMGNGALINSFFSITTMAIAIPTGVKIFNWLL 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 325 TLHGGSIKWETPLLWSLGFIFLFTVGGLTGIVLANSSLDITLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLLTGYTL 404
Cdd:TIGR02882 362 TLYKGKIRFTTPMLFSLAFIPNFLIGGVTGVMLAMASADYQYHNTYFLVAHFHYVLITGVVFACLAGLIYWYPKMFGYKL 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 405 HNTWSKAHFGVMFLGVNLTFFPQHFLGLAGMPRRYSDY--PDAYTLWNTVSSLGSLISLIAVIMFLF-IIWEAFAAKRVV 481
Cdd:TIGR02882 442 NERLGKWCFWFFMIGFNVCFFPMYILGLDGMPRRMYTYspSDGWFPLNLISTIGALLMAIGFIFLVYnIYYSHRKSPREA 521
|
490 500
....*....|....*....|...
gi 1861254773 482 ASVPLTTTNIEWLHGCPPPYHTF 504
Cdd:TIGR02882 522 TGDPWNGRTLEWATASPPPKYNF 544
|
|
| PRK15017 |
PRK15017 |
cytochrome o ubiquinol oxidase subunit I; Provisional |
4-504 |
3.39e-108 |
|
cytochrome o ubiquinol oxidase subunit I; Provisional
Pssm-ID: 184978 Cd Length: 663 Bit Score: 336.52 E-value: 3.39e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 4 TRWFFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAE--LSQPG-ALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGgFGN 80
Cdd:PRK15017 46 KEWLTSVDHKRLGIMYIIVAIVMLLRGFADAIMMRSQqaLASAGeAGFLPPHHYDQIFTAHGVIMIFFVAMPFVIG-LMN 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 81 WLIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLASNLAHAGASVDLTIFSLHLAGISSILG 160
Cdd:PRK15017 125 LVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTTLT 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 161 AINFITTILNMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGH 240
Cdd:PRK15017 205 GINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWGH 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 241 PEVYILILPGFGMISHIVAYYAgKKEPFGYMGMVWAMMAIGLLGFIVWAHHML-QGMDVDTRAYFTSATMIIAIPTGVKV 319
Cdd:PRK15017 285 PEVYILILPVFGVFSEIAATFS-RKRLFGYTSLVWATVCITVLSFIVWLHHFFtMGAGANVNAFFGITTMIIAIPTGVKI 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 320 FSWLATLHGGSIKWETPLLWSLGFIFLFTVGGLTGIVLANSSLDITLHDTYYVVAHFHYVLSMGAVFAIMAGFVHWFPLL 399
Cdd:PRK15017 364 FNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYWWPKA 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 400 TGYTLHNTWSKAHFGVMFLGVNLTFFPQHFLGLAGMPRRYSDY--PDAYTLWNTVSSLGSLIS--LIAVIMFLFIIWEAF 475
Cdd:PRK15017 444 FGFKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMTRRLSQQidPQFHTMLMIAASGAALIAlgILCQVIQMYVSIRDR 523
|
490 500
....*....|....*....|....*....
gi 1861254773 476 AAKRVVASVPLTTTNIEWLHGCPPPYHTF 504
Cdd:PRK15017 524 DQNRDLTGDPWGGRTLEWATSSPPPFYNF 552
|
|
| ba3-like_Oxidase_I |
cd01660 |
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ... |
227-471 |
2.07e-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: 87.73 E-value: 2.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 227 DPILYQHLFWFFGHPEVYILILPGFGMISHIVAYYAGKKEPFGYMGMVwAMMAIGLLGFIVWAHHmlQGMDVDTRAYF-- 304
Cdd:cd01660 200 DVLLSRTLFWWFGHPLVYFWLLPAYIAWYTILPKIAGGKLFSDPLARL-AFILFLLFSTPVGFHH--QFADPGIGPGWkf 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 305 --TSATMIIAIPTGVKVFSWLATL--------HGGSIKWETPLLWS--------LGFIFlFTVGGLTGIVLANSSLDITL 366
Cdd:cd01660 277 ihMVLTFMVALPSLLTAFTVFASLeiagrlrgGKGLFGWIRALPWGdpmflalfLAMLM-FIPGGAGGIINASYQLNYVV 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1861254773 367 HDTYYVVAHFHyvLSMGAVFAIMA-GFVHWF-PLLTGYTL-HNTWSKAHFGVMFLGVNLTFFPQHFLGLAGMPRR--YSD 441
Cdd:cd01660 356 HNTAWVPGHFH--LTVGGAVALTFmAVAYWLvPHLTGRELaAKRLALAQPWLWFVGMTIMSTAMHVAGLLGAPRRtaEAQ 433
|
250 260 270
....*....|....*....|....*....|....*
gi 1861254773 442 YPDAY-----TLWNTVSSLGSLISLIAVIMFLFII 471
Cdd:cd01660 434 YGGLPaagewAPYQQLMAIGGTILFVSGALFLYIL 468
|
|
| |
