|
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 ... |
17-501 |
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: 874.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 17 TNHKDIGTLYLIFAAAAGIVGSIFSLLIRLELAHPGNQIlgGNHQLYNVIVTAHAFLMIFFLIMPALIGGFGNWFVPMMI 96
Cdd:cd01663 1 TNHKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQL--GNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 97 GAPDMAFPRLNNISFWLLPPALILLVSSSLVEVGVGTGWTVYPPLASIQAHSGAAVDLAIFSLHLAGISSILGAINFITT 176
Cdd:cd01663 79 GAPDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 177 VINMRLPGMYAHRIPLFVWSIFVTAVLLLLAVPVLAGGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYIII 256
Cdd:cd01663 159 IFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 257 LPAFGIISHVVSTFSS-KQVFGYIGMVYAMSSIGLLGFIVWAHHMYTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATM 335
Cdd:cd01663 239 LPGFGIISHIISTFSGkKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATM 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 336 WHGTIRLYTPMMFAVGFIFLFTLGGVTGVILSNSGLDVSLHDTYYVVGHFHYVLSMGALFGLFAGFYYWIGKMTGAQYNE 415
Cdd:cd01663 319 WGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 416 TLGQVHFWLTFVGVNVTFFPMHFLGLAGMPRRIPDYPDAFAGWNEIASLGSLISIFAALFFFYVVFETFTSGRVCPRNPW 495
Cdd:cd01663 399 TLGKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFNVG 478
|
....*.
gi 1315028919 496 KLNPKL 501
Cdd:cd01663 479 EGSTSL 484
|
|
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
12-488 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 801.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 12 RWLFSTNHKDIGTLYLIFAAAAGIVGSIFSLLIRLELAHPGNQIlgGNHQLYNVIVTAHAFLMIFFLIMPALIGGFGNWF 91
Cdd:MTH00153 3 KWLFSTNHKDIGTLYFIFGAWSGMVGTSLSLLIRAELGQPGSLI--GDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 92 VPMMIGAPDMAFPRLNNISFWLLPPALILLVSSSLVEVGVGTGWTVYPPLASIQAHSGAAVDLAIFSLHLAGISSILGAI 171
Cdd:MTH00153 81 VPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 172 NFITTVINMRLPGMYAHRIPLFVWSIFVTAVLLLLAVPVLAGGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPE 251
Cdd:MTH00153 161 NFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 252 VYIIILPAFGIISHVVSTFSSK-QVFGYIGMVYAMSSIGLLGFIVWAHHMYTVGMDVDTRAYFTAATMIIAVPTGIKIFS 330
Cdd:MTH00153 241 VYILILPGFGMISHIISQESGKkETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 331 WIATMwHGTIRLYTP-MMFAVGFIFLFTLGGVTGVILSNSGLDVSLHDTYYVVGHFHYVLSMGALFGLFAGFYYWIGKMT 409
Cdd:MTH00153 321 WLATL-HGSQINYSPsLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFT 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1315028919 410 GAQYNETLGQVHFWLTFVGVNVTFFPMHFLGLAGMPRRIPDYPDAFAGWNEIASLGSLISIFAALFFFYVVFETFTSGR 488
Cdd:MTH00153 400 GLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKR 478
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
14-495 |
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: 624.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 14 LFSTNHKDIGTLYLIFAAAAGIVGSIFSLLIRLELAHPGNQILGGnhQLYNVIVTAHAFLMIFFLIMPaLIGGFGNWFVP 93
Cdd:TIGR02891 1 LTTVDHKRIGILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDA--ETYNQLFTMHGTIMIFLFAIP-ILAGFGNYLLP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 94 MMIGAPDMAFPRLNNISFWLLPPALILLVSSSLVEVGVGTGWTVYPPLASIQAHSGAAVDLAIFSLHLAGISSILGAINF 173
Cdd:TIGR02891 78 LMIGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 174 ITTVINMRLPGMYAHRIPLFVWSIFVTAVLLLLAVPVLAGGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVY 253
Cdd:TIGR02891 158 IVTILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVY 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 254 IIILPAFGIISHVVSTFSSKQVFGYIGMVYAMSSIGLLGFIVWAHHMYTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIA 333
Cdd:TIGR02891 238 IIFLPAFGIISEILPTFARKPIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 334 TMWHGTIRLYTPMMFAVGFIFLFTLGGVTGVILSNSGLDVSLHDTYYVVGHFHYVLSMGALFGLFAGFYYWIGKMTGAQY 413
Cdd:TIGR02891 318 TLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMY 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 414 NETLGQVHFWLTFVGVNVTFFPMHFLGLAGMPRRIPDYPDA--FAGWNEIASLGSLISIFAALFFFYVVFETFTSGRVCP 491
Cdd:TIGR02891 398 NERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGPKAG 477
|
....
gi 1315028919 492 RNPW 495
Cdd:TIGR02891 478 ANPW 481
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
12-496 |
0e+00 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 617.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 12 RWLFSTNHKDIGTLYLIFAAAAGIVGSIFSLLIRLELAHPGNQILGGNHqlYNVIVTAHAFLMIFFLIMPaLIGGFGNWF 91
Cdd:COG0843 8 RWLTTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPET--YNQLFTMHGTIMIFFFATP-FLAGFGNYL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 92 VPMMIGAPDMAFPRLNNISFWLLPPALILLVSSSLVEVGVGTGWTVYPPLASIQAHSGAAVDLAIFSLHLAGISSILGAI 171
Cdd:COG0843 85 VPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 172 NFITTVINMRLPGMYAHRIPLFVWSIFVTAVLLLLAVPVLAGGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPE 251
Cdd:COG0843 165 NFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 252 VYIIILPAFGIISHVVSTFSSKQVFGYIGMVYAMSSIGLLGFIVWAHHMYTVGMDVDTRAYFTAATMIIAVPTGIKIFSW 331
Cdd:COG0843 245 VYILILPAFGIVSEIIPTFSRKPLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNW 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 332 IATMWHGTIRLYTPMMFAVGFIFLFTLGGVTGVILSNSGLDVSLHDTYYVVGHFHYVLSMGALFGLFAGFYYWIGKMTGA 411
Cdd:COG0843 325 IATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGR 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 412 QYNETLGQVHFWLTFVGVNVTFFPMHFLGLAGMPRRIPDYP--DAFAGWNEIASLGSLISIFAALFFFYVVFETFTSGRV 489
Cdd:COG0843 405 MLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAFILAVGFLLFLINLVVSLRKGPK 484
|
....*..
gi 1315028919 490 CPRNPWK 496
Cdd:COG0843 485 AGGNPWG 491
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
21-468 |
1.28e-141 |
|
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: 413.89 E-value: 1.28e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 21 DIGTLYLIFAAAAGIVGSIFSLLIRLELAHPGNQILGGnhQLYNVIVTAHAFLMIFFLIMPAlIGGFGNWFVPMMIGAPD 100
Cdd:pfam00115 1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSP--LTYNQLRTLHGNLMIFWFATPF-LFGFGNYLVPLMIGARD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 101 MAFPRLNNISFWLLPPALILLVSSSLvevGVGTGWTVYPPLAsiqahsgaAVDLAIFSLHLAGISSILGAINFITTVINM 180
Cdd:pfam00115 78 MAFPRLNALSFWLVVLGAVLLLASFG---GATTGWTEYPPLV--------GVDLWYIGLLLAGVSSLLGAINFIVTILKR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 181 RLPGMYAhRIPLFVWSIFVTAVLLLLAVPVLAGGITMLLTDRNLNttffdpAGGGDPILYQHLFWFFGHPEVYIIILPAF 260
Cdd:pfam00115 147 RAPGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAF 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 261 GIISHVVSTFSSKQVFGYIGMVYAMSSIGLLGFIVWAHHMYTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATMWHGTI 340
Cdd:pfam00115 220 GIIYYILPKFAGRPLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWI 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 341 RLY-TPMMFAVGFIFLFTLGGVTGVILSNSGLDVSLHDTYYVVGHFHYVLSMGALFGLFAGFYYWIGKMTGAQYNETLGQ 419
Cdd:pfam00115 300 RFRtTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGK 379
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1315028919 420 VHFWLTFVGVNVTFFPMHFLGLAGMPRRIP----DYPDAFAGWNEIASLGSLI 468
Cdd:pfam00115 380 LHFWLLFIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPLNWIRTIGGVL 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 ... |
17-501 |
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: 874.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 17 TNHKDIGTLYLIFAAAAGIVGSIFSLLIRLELAHPGNQIlgGNHQLYNVIVTAHAFLMIFFLIMPALIGGFGNWFVPMMI 96
Cdd:cd01663 1 TNHKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQL--GNDQLYNVIVTAHALIMIFFMVMPALIGGFGNWLVPLMI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 97 GAPDMAFPRLNNISFWLLPPALILLVSSSLVEVGVGTGWTVYPPLASIQAHSGAAVDLAIFSLHLAGISSILGAINFITT 176
Cdd:cd01663 79 GAPDMAFPRLNNLSFWLLPPSLLLLLLSALVEGGAGTGWTVYPPLSSILAHSGPSVDLAIFSLHLAGISSILGAINFITT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 177 VINMRLPGMYAHRIPLFVWSIFVTAVLLLLAVPVLAGGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYIII 256
Cdd:cd01663 159 IFNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 257 LPAFGIISHVVSTFSS-KQVFGYIGMVYAMSSIGLLGFIVWAHHMYTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATM 335
Cdd:cd01663 239 LPGFGIISHIISTFSGkKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATM 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 336 WHGTIRLYTPMMFAVGFIFLFTLGGVTGVILSNSGLDVSLHDTYYVVGHFHYVLSMGALFGLFAGFYYWIGKMTGAQYNE 415
Cdd:cd01663 319 WGGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 416 TLGQVHFWLTFVGVNVTFFPMHFLGLAGMPRRIPDYPDAFAGWNEIASLGSLISIFAALFFFYVVFETFTSGRVCPRNPW 495
Cdd:cd01663 399 TLGKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFNVG 478
|
....*.
gi 1315028919 496 KLNPKL 501
Cdd:cd01663 479 EGSTSL 484
|
|
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
12-488 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 801.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 12 RWLFSTNHKDIGTLYLIFAAAAGIVGSIFSLLIRLELAHPGNQIlgGNHQLYNVIVTAHAFLMIFFLIMPALIGGFGNWF 91
Cdd:MTH00153 3 KWLFSTNHKDIGTLYFIFGAWSGMVGTSLSLLIRAELGQPGSLI--GDDQIYNVIVTAHAFIMIFFMVMPIMIGGFGNWL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 92 VPMMIGAPDMAFPRLNNISFWLLPPALILLVSSSLVEVGVGTGWTVYPPLASIQAHSGAAVDLAIFSLHLAGISSILGAI 171
Cdd:MTH00153 81 VPLMLGAPDMAFPRMNNMSFWLLPPSLTLLLSSSMVESGAGTGWTVYPPLSSNIAHSGASVDLAIFSLHLAGISSILGAI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 172 NFITTVINMRLPGMYAHRIPLFVWSIFVTAVLLLLAVPVLAGGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPE 251
Cdd:MTH00153 161 NFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 252 VYIIILPAFGIISHVVSTFSSK-QVFGYIGMVYAMSSIGLLGFIVWAHHMYTVGMDVDTRAYFTAATMIIAVPTGIKIFS 330
Cdd:MTH00153 241 VYILILPGFGMISHIISQESGKkETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 331 WIATMwHGTIRLYTP-MMFAVGFIFLFTLGGVTGVILSNSGLDVSLHDTYYVVGHFHYVLSMGALFGLFAGFYYWIGKMT 409
Cdd:MTH00153 321 WLATL-HGSQINYSPsLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLFT 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1315028919 410 GAQYNETLGQVHFWLTFVGVNVTFFPMHFLGLAGMPRRIPDYPDAFAGWNEIASLGSLISIFAALFFFYVVFETFTSGR 488
Cdd:MTH00153 400 GLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFIIWESMISKR 478
|
|
| COX1 |
MTH00167 |
cytochrome c oxidase subunit I; Provisional |
9-489 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177222 Cd Length: 512 Bit Score: 754.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 9 WSSRWLFSTNHKDIGTLYLIFAAAAGIVGSIFSLLIRLELAHPGNQIlgGNHQLYNVIVTAHAFLMIFFLIMPALIGGFG 88
Cdd:MTH00167 2 WINRWLFSTNHKDIGTLYFIFGAWAGMVGTALSLLIRAELSQPGSLL--GDDQIYNVIVTAHAFVMIFFMVMPIMIGGFG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 89 NWFVPMMIGAPDMAFPRLNNISFWLLPPALILLVSSSLVEVGVGTGWTVYPPLASIQAHSGAAVDLAIFSLHLAGISSIL 168
Cdd:MTH00167 80 NWLVPLMIGAPDMAFPRMNNMSFWLLPPSLLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSIL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 169 GAINFITTVINMRLPGMYAHRIPLFVWSIFVTAVLLLLAVPVLAGGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFG 248
Cdd:MTH00167 160 GSINFITTIINMKPPGITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 249 HPEVYIIILPAFGIISHVVSTFSSKQ-VFGYIGMVYAMSSIGLLGFIVWAHHMYTVGMDVDTRAYFTAATMIIAVPTGIK 327
Cdd:MTH00167 240 HPEVYILILPGFGMISHIVVYYSGKKePFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 328 IFSWIATMWHGTIRLYTPMMFAVGFIFLFTLGGVTGVILSNSGLDVSLHDTYYVVGHFHYVLSMGALFGLFAGFYYWIGK 407
Cdd:MTH00167 320 VFSWLATLHGGKIKWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 408 MTGAQYNETLGQVHFWLTFVGVNVTFFPMHFLGLAGMPRRIPDYPDAFAGWNEIASLGSLISIFAALFFFYVVFETFTSG 487
Cdd:MTH00167 400 FTGLTLNETWTKIHFFVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNVVSSIGSLISLVAVILFLFIIWEAFSSK 479
|
..
gi 1315028919 488 RV 489
Cdd:MTH00167 480 RK 481
|
|
| COX1 |
MTH00223 |
cytochrome c oxidase subunit I; Provisional |
11-488 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177260 Cd Length: 512 Bit Score: 746.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 11 SRWLFSTNHKDIGTLYLIFAAAAGIVGSIFSLLIRLELAHPGnqILGGNHQLYNVIVTAHAFLMIFFLIMPALIGGFGNW 90
Cdd:MTH00223 1 MRWLFSTNHKDIGTLYLIFGMWSGLVGTSLSLLIRAELGQPG--ALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGGFGNW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 91 FVPMMIGAPDMAFPRLNNISFWLLPPALILLVSSSLVEVGVGTGWTVYPPLASIQAHSGAAVDLAIFSLHLAGISSILGA 170
Cdd:MTH00223 79 LVPLMLGAPDMAFPRLNNMSFWLLPPSLYLLLSSSAVESGVGTGWTVYPPLSSNLAHAGPSVDLAIFSLHLAGVSSILGA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 171 INFITTVINMRLPGMYAHRIPLFVWSIFVTAVLLLLAVPVLAGGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHP 250
Cdd:MTH00223 159 INFITTIINMRSPGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 251 EVYIIILPAFGIISHVVSTFSSK-QVFGYIGMVYAMSSIGLLGFIVWAHHMYTVGMDVDTRAYFTAATMIIAVPTGIKIF 329
Cdd:MTH00223 239 EVYILILPGFGMISHIVSHYSSKkEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVF 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 330 SWIATMWHGTIRLYTPMMFAVGFIFLFTLGGVTGVILSNSGLDVSLHDTYYVVGHFHYVLSMGALFGLFAGFYYWIGKMT 409
Cdd:MTH00223 319 SWLATIYGSKIKYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLFT 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1315028919 410 GAQYNETLGQVHFWLTFVGVNVTFFPMHFLGLAGMPRRIPDYPDAFAGWNEIASLGSLISIFAALFFFYVVFETFTSGR 488
Cdd:MTH00223 399 GVTLHRRWAKAHFFLMFLGVNLTFFPQHFLGLAGMPRRYSDYPDCYTKWNQVSSFGSMISFVSVLFFMFIVWEAFVSQR 477
|
|
| COX1 |
MTH00116 |
cytochrome c oxidase subunit I; Provisional |
9-488 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177177 Cd Length: 515 Bit Score: 735.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 9 WSSRWLFSTNHKDIGTLYLIFAAAAGIVGSIFSLLIRLELAHPGNqiLGGNHQLYNVIVTAHAFLMIFFLIMPALIGGFG 88
Cdd:MTH00116 2 FITRWLFSTNHKDIGTLYLIFGAWAGMVGTALSLLIRAELGQPGT--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 89 NWFVPMMIGAPDMAFPRLNNISFWLLPPALILLVSSSLVEVGVGTGWTVYPPLASIQAHSGAAVDLAIFSLHLAGISSIL 168
Cdd:MTH00116 80 NWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTVEAGAGTGWTVYPPLAGNLAHAGASVDLAIFSLHLAGVSSIL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 169 GAINFITTVINMRLPGMYAHRIPLFVWSIFVTAVLLLLAVPVLAGGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFG 248
Cdd:MTH00116 160 GAINFITTCINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 249 HPEVYIIILPAFGIISHVVSTFSS-KQVFGYIGMVYAMSSIGLLGFIVWAHHMYTVGMDVDTRAYFTAATMIIAVPTGIK 327
Cdd:MTH00116 240 HPEVYILILPGFGIISHIVTYYAGkKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 328 IFSWIATMWHGTIRLYTPMMFAVGFIFLFTLGGVTGVILSNSGLDVSLHDTYYVVGHFHYVLSMGALFGLFAGFYYWIGK 407
Cdd:MTH00116 320 VFSWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 408 MTGAQYNETLGQVHFWLTFVGVNVTFFPMHFLGLAGMPRRIPDYPDAFAGWNEIASLGSLISIFAALFFFYVVFETFTSG 487
Cdd:MTH00116 400 FTGYTLHQTWTKAQFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTISSIGSLISMTAVIMLMFIIWEAFSSK 479
|
.
gi 1315028919 488 R 488
Cdd:MTH00116 480 R 480
|
|
| COX1 |
MTH00142 |
cytochrome c oxidase subunit I; Provisional |
11-495 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214431 Cd Length: 511 Bit Score: 718.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 11 SRWLFSTNHKDIGTLYLIFAAAAGIVGSIFSLLIRLELAHPGNqiLGGNHQLYNVIVTAHAFLMIFFLIMPALIGGFGNW 90
Cdd:MTH00142 2 MRWLFSTNHKDIGTLYFLFGAWAGMVGTGLSLLIRAELGQPGS--LLGDDQLYNVIVTAHAFVMIFFMVMPVMIGGFGNW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 91 FVPMMIGAPDMAFPRLNNISFWLLPPALILLVSSSLVEVGVGTGWTVYPPLASIQAHSGAAVDLAIFSLHLAGISSILGA 170
Cdd:MTH00142 80 LVPLMLGAPDMAFPRMNNMSFWLLPPALLLLLSSAAVESGAGTGWTVYPPLSSNLAHSGGSVDLAIFSLHLAGVSSILGA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 171 INFITTVINMRLPGMYAHRIPLFVWSIFVTAVLLLLAVPVLAGGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHP 250
Cdd:MTH00142 160 INFITTVINMRAGGMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 251 EVYIIILPAFGIISHVVSTFSSK-QVFGYIGMVYAMSSIGLLGFIVWAHHMYTVGMDVDTRAYFTAATMIIAVPTGIKIF 329
Cdd:MTH00142 240 EVYILILPGFGMISHIINHYSGKkEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVF 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 330 SWIATMWHGTIRLYTPMMFAVGFIFLFTLGGVTGVILSNSGLDVSLHDTYYVVGHFHYVLSMGALFGLFAGFYYWIGKMT 409
Cdd:MTH00142 320 SWLATLHGSKVKYEPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLFT 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 410 GAQYNETLGQVHFWLTFVGVNVTFFPMHFLGLAGMPRRIPDYPDAFAGWNEIASLGSLISIFAALFFFYVVFETFTSGRV 489
Cdd:MTH00142 400 GLTLNPRWLKAHFYTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSSLGSMISFIAVLMFVFIVWESFVSQRL 479
|
....*.
gi 1315028919 490 CPRNPW 495
Cdd:MTH00142 480 VMWSSH 485
|
|
| COX1 |
MTH00182 |
cytochrome c oxidase subunit I; Provisional |
6-486 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214451 Cd Length: 525 Bit Score: 694.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 6 LYQWSSRWLFSTNHKDIGTLYLIFAAAAGIVGSIFSLLIRLELAHPGnQILGGNHqLYNVIVTAHAFLMIFFLIMPALIG 85
Cdd:MTH00182 1 KNLYLTRWVFSTNHKDIGTLYLVFGAGAGMIGTAFSMLIRLELSAPG-AMLGDDH-LYNVIVTAHAFIMIFFLVMPVMIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 86 GFGNWFVPMMIGAPDMAFPRLNNISFWLLPPALILLVSSSLVEVGVGTGWTVYPPLASIQAHSGAAVDLAIFSLHLAGIS 165
Cdd:MTH00182 79 GFGNWLVPLYIGAPDMAFPRLNNISFWLLPPALILLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGAVDMAIFSLHLAGVS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 166 SILGAINFITTVINMRLPGMYAHRIPLFVWSIFVTAVLLLLAVPVLAGGITMLLTDRNLNTTFFDPAGGGDPILYQHLFW 245
Cdd:MTH00182 159 SILGAINFITTIFNMRAPGVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFW 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 246 FFGHPEVYIIILPAFGIISHVVSTFSSK-QVFGYIGMVYAMSSIGLLGFIVWAHHMYTVGMDVDTRAYFTAATMIIAVPT 324
Cdd:MTH00182 239 FFGHPEVYILILPGFGMISQIIPTFVAKkQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPT 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 325 GIKIFSWIATMWHGTIRLYTPMMFAVGFIFLFTLGGVTGVILSNSGLDVSLHDTYYVVGHFHYVLSMGALFGLFAGFYYW 404
Cdd:MTH00182 319 GIKVFSWLATIYGGTLRLDTPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYW 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 405 IGKMTGAQYNETLGQVHFWLTFVGVNVTFFPMHFLGLAGMPRRIPDYPDAFAGWNEIASLGSLISIFAALFFFYVVFETF 484
Cdd:MTH00182 399 FGKITGYCYNELYGKIHFWLMFIGVNLTFFPQHFLGLAGFPRRYSDFADAFAGWNLVSSLGSIISIVGVVWFIYIIYDAY 478
|
..
gi 1315028919 485 TS 486
Cdd:MTH00182 479 VR 480
|
|
| COX1 |
MTH00184 |
cytochrome c oxidase subunit I; Provisional |
9-484 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177235 Cd Length: 519 Bit Score: 688.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 9 WSSRWLFSTNHKDIGTLYLIFAAAAGIVGSIFSLLIRLELAHPGNQIlgGNHQLYNVIVTAHAFLMIFFLIMPALIGGFG 88
Cdd:MTH00184 4 YLSRWLFSTNHKDIGTLYLLFGAFAGMIGTAFSMLIRLELSAPGSML--GDDHLYNVIVTAHAFVMIFFLVMPVMIGGFG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 89 NWFVPMMIGAPDMAFPRLNNISFWLLPPALILLVSSSLVEVGVGTGWTVYPPLASIQAHSGAAVDLAIFSLHLAGISSIL 168
Cdd:MTH00184 82 NWFVPLYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGAGTGWTVYPPLSSIQAHSGGSVDMAIFSLHLAGISSIL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 169 GAINFITTVINMRLPGMYAHRIPLFVWSIFVTAVLLLLAVPVLAGGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFG 248
Cdd:MTH00184 162 GAMNFITTIFNMRAPGITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 249 HPEVYIIILPAFGIISHVVSTFSS-KQVFGYIGMVYAMSSIGLLGFIVWAHHMYTVGMDVDTRAYFTAATMIIAVPTGIK 327
Cdd:MTH00184 242 HPEVYILILPGFGIISQIIPTFAAkKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 328 IFSWIATMWHGTIRLYTPMMFAVGFIFLFTLGGVTGVILSNSGLDVSLHDTYYVVGHFHYVLSMGALFGLFAGFYYWIGK 407
Cdd:MTH00184 322 IFSWIATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGK 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1315028919 408 MTGAQYNETLGQVHFWLTFVGVNVTFFPMHFLGLAGMPRRIPDYPDAFAGWNEIASLGSLISIFAALFFFYVVFETF 484
Cdd:MTH00184 402 ITGYCYNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDSFAGWNQISSLGSVISIVGVVWFIYIVYDAY 478
|
|
| COX1 |
MTH00183 |
cytochrome c oxidase subunit I; Provisional |
11-488 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177234 Cd Length: 516 Bit Score: 655.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 11 SRWLFSTNHKDIGTLYLIFAAAAGIVGSIFSLLIRLELAHPGNqiLGGNHQLYNVIVTAHAFLMIFFLIMPALIGGFGNW 90
Cdd:MTH00183 4 TRWFFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGA--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 91 FVPMMIGAPDMAFPRLNNISFWLLPPALILLVSSSLVEVGVGTGWTVYPPLASIQAHSGAAVDLAIFSLHLAGISSILGA 170
Cdd:MTH00183 82 LIPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 171 INFITTVINMRLPGMYAHRIPLFVWSIFVTAVLLLLAVPVLAGGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHP 250
Cdd:MTH00183 162 INFITTIINMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 251 EVYIIILPAFGIISHVVSTFSSK-QVFGYIGMVYAMSSIGLLGFIVWAHHMYTVGMDVDTRAYFTAATMIIAVPTGIKIF 329
Cdd:MTH00183 242 EVYILILPGFGMISHIVAYYSGKkEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVF 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 330 SWIATMWHGTIRLYTPMMFAVGFIFLFTLGGVTGVILSNSGLDVSLHDTYYVVGHFHYVLSMGALFGLFAGFYYWIGKMT 409
Cdd:MTH00183 322 SWLATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLFS 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1315028919 410 GAQYNETLGQVHFWLTFVGVNVTFFPMHFLGLAGMPRRIPDYPDAFAGWNEIASLGSLISIFAALFFFYVVFETFTSGR 488
Cdd:MTH00183 402 GYTLHSTWTKIHFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMFLFILWEAFAAKR 480
|
|
| COX1 |
MTH00037 |
cytochrome c oxidase subunit I; Provisional |
11-489 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177112 Cd Length: 517 Bit Score: 652.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 11 SRWLFSTNHKDIGTLYLIFAAAAGIVGSIFSLLIRLELAHPGNQIlgGNHQLYNVIVTAHAFLMIFFLIMPALIGGFGNW 90
Cdd:MTH00037 4 SRWLFSTNHKDIGTLYLIFGAWAGMVGTAMSVIIRTELAQPGSLL--QDDQIYNVIVTAHALVMIFFMVMPIMIGGFGNW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 91 FVPMMIGAPDMAFPRLNNISFWLLPPALILLVSSSLVEVGVGTGWTVYPPLASIQAHSGAAVDLAIFSLHLAGISSILGA 170
Cdd:MTH00037 82 LIPLMIGAPDMAFPRMNNMSFWLIPPSFLLLLASAGVESGAGTGWTIYPPLSSNIAHAGGSVDLAIFSLHLAGASSILAS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 171 INFITTVINMRLPGMYAHRIPLFVWSIFVTAVLLLLAVPVLAGGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHP 250
Cdd:MTH00037 162 INFITTIINMRTPGMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 251 EVYIIILPAFGIISHVVSTFSSKQ-VFGYIGMVYAMSSIGLLGFIVWAHHMYTVGMDVDTRAYFTAATMIIAVPTGIKIF 329
Cdd:MTH00037 242 EVYILILPGFGMISHVIAHYSGKQePFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVF 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 330 SWIATMWHGTIRLYTPMMFAVGFIFLFTLGGVTGVILSNSGLDVSLHDTYYVVGHFHYVLSMGALFGLFAGFYYWIGKMT 409
Cdd:MTH00037 322 SWMATLQGSNLRWETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLFS 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 410 GAQYNETLGQVHFWLTFVGVNVTFFPMHFLGLAGMPRRIPDYPDAFAGWNEIASLGSLISIFAALFFFYVVFETFTSGRV 489
Cdd:MTH00037 402 GVSLHPLWSKVHFFLMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSTISLVATLFFLFLIWEAFASQRE 481
|
|
| COX1 |
MTH00077 |
cytochrome c oxidase subunit I; Provisional |
11-489 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214419 Cd Length: 514 Bit Score: 650.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 11 SRWLFSTNHKDIGTLYLIFAAAAGIVGSIFSLLIRLELAHPGNqiLGGNHQLYNVIVTAHAFLMIFFLIMPALIGGFGNW 90
Cdd:MTH00077 4 TRWLFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGT--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 91 FVPMMIGAPDMAFPRLNNISFWLLPPALILLVSSSLVEVGVGTGWTVYPPLASIQAHSGAAVDLAIFSLHLAGISSILGA 170
Cdd:MTH00077 82 LVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 171 INFITTVINMRLPGMYAHRIPLFVWSIFVTAVLLLLAVPVLAGGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHP 250
Cdd:MTH00077 162 INFITTSINMKPPSMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 251 EVYIIILPAFGIISHVVSTFSS-KQVFGYIGMVYAMSSIGLLGFIVWAHHMYTVGMDVDTRAYFTAATMIIAVPTGIKIF 329
Cdd:MTH00077 242 EVYILILPGFGMISHIVTYYSAkKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVF 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 330 SWIATMWHGTIRLYTPMMFAVGFIFLFTLGGVTGVILSNSGLDVSLHDTYYVVGHFHYVLSMGALFGLFAGFYYWIGKMT 409
Cdd:MTH00077 322 SWLATMHGGAIKWDAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFS 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 410 GAQYNETLGQVHFWLTFVGVNVTFFPMHFLGLAGMPRRIPDYPDAFAGWNEIASLGSLISIFAALFFFYVVFETFTSGRV 489
Cdd:MTH00077 402 GYTLHSTWSKIHFGVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMMMFIIWEAFSSKRE 481
|
|
| COX1 |
MTH00007 |
cytochrome c oxidase subunit I; Validated |
12-488 |
0e+00 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 133649 Cd Length: 511 Bit Score: 650.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 12 RWLFSTNHKDIGTLYLIFAAAAGIVGSIFSLLIRLELAHPGNQIlgGNHQLYNVIVTAHAFLMIFFLIMPALIGGFGNWF 91
Cdd:MTH00007 2 RWLYSTNHKDIGTLYFILGVWGGLLGTSMSLLIRIELGQPGAFL--GSDQLYNTIVTAHAFLMIFFLVMPVFIGGFGNWL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 92 VPMMIGAPDMAFPRLNNISFWLLPPALILLVSSSLVEVGVGTGWTVYPPLASIQAHSGAAVDLAIFSLHLAGISSILGAI 171
Cdd:MTH00007 80 VPLMLGAPDMAFPRLNNMSFWLLPPALILLVSSAAVEKGVGTGWTVYPPLASNLAHAGPSVDLAIFSLHLAGVSSILGAI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 172 NFITTVINMRLPGMYAHRIPLFVWSIFVTAVLLLLAVPVLAGGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPE 251
Cdd:MTH00007 160 NFITTVINMRWKGLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 252 VYIIILPAFGIISHVVSTFSSK-QVFGYIGMVYAMSSIGLLGFIVWAHHMYTVGMDVDTRAYFTAATMIIAVPTGIKIFS 330
Cdd:MTH00007 240 VYILILPGFGAISHIVTHYAGKlEPFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 331 WIATMWHGTIRLYTPMMFAVGFIFLFTLGGVTGVILSNSGLDVSLHDTYYVVGHFHYVLSMGALFGLFAGFYYWIGKMTG 410
Cdd:MTH00007 320 WLATIHGSPIKYETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTG 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1315028919 411 AQYNETLGQVHFWLTFVGVNVTFFPMHFLGLAGMPRRIPDYPDAFAGWNEIASLGSLISIFAALFFFYVVFETFTSGR 488
Cdd:MTH00007 400 LTLHDRWAKAHFFLMFLGVNLTFFPQHFLGLSGMPRRYSDYPDAYTKWNVVSSFGSMLSFVALLLFIFILWEAFSAQR 477
|
|
| COX1 |
MTH00103 |
cytochrome c oxidase subunit I; Validated |
11-488 |
0e+00 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 177165 Cd Length: 513 Bit Score: 650.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 11 SRWLFSTNHKDIGTLYLIFAAAAGIVGSIFSLLIRLELAHPGNqiLGGNHQLYNVIVTAHAFLMIFFLIMPALIGGFGNW 90
Cdd:MTH00103 4 NRWLFSTNHKDIGTLYLLFGAWAGMVGTALSLLIRAELGQPGT--LLGDDQIYNVIVTAHAFVMIFFMVMPIMIGGFGNW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 91 FVPMMIGAPDMAFPRLNNISFWLLPPALILLVSSSLVEVGVGTGWTVYPPLASIQAHSGAAVDLAIFSLHLAGISSILGA 170
Cdd:MTH00103 82 LVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 171 INFITTVINMRLPGMYAHRIPLFVWSIFVTAVLLLLAVPVLAGGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHP 250
Cdd:MTH00103 162 INFITTIINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 251 EVYIIILPAFGIISHVVSTFS-SKQVFGYIGMVYAMSSIGLLGFIVWAHHMYTVGMDVDTRAYFTAATMIIAVPTGIKIF 329
Cdd:MTH00103 242 EVYILILPGFGMISHIVTYYSgKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVF 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 330 SWIATMWHGTIRLYTPMMFAVGFIFLFTLGGVTGVILSNSGLDVSLHDTYYVVGHFHYVLSMGALFGLFAGFYYWIGKMT 409
Cdd:MTH00103 322 SWLATLHGGNIKWSPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFS 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1315028919 410 GAQYNETLGQVHFWLTFVGVNVTFFPMHFLGLAGMPRRIPDYPDAFAGWNEIASLGSLISIFAALFFFYVVFETFTSGR 488
Cdd:MTH00103 402 GYTLNDTWAKIHFTIMFVGVNMTFFPQHFLGLSGMPRRYSDYPDAYTTWNTVSSMGSFISLTAVMLMIFMIWEAFASKR 480
|
|
| COX1 |
MTH00079 |
cytochrome c oxidase subunit I; Provisional |
11-488 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177148 Cd Length: 508 Bit Score: 632.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 11 SRWLFSTNHKDIGTLYLIFAAAAGIVGSIFSLLIRLELAHPGnqILGGNHQLYNVIVTAHAFLMIFFLIMPALIGGFGNW 90
Cdd:MTH00079 5 SVWLESSNHKDIGTLYFLFGLWSGMVGTSLSLIIRLELSKPG--LLLGNGQLYNSVITAHAILMIFFMVMPSMIGGFGNW 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 91 FVPMMIGAPDMAFPRLNNISFWLLPPALILLVSSSLVEVGVGTGWTVYPPLaSIQAHSGAAVDLAIFSLHLAGISSILGA 170
Cdd:MTH00079 83 MLPLMLGAPDMSFPRLNNLSFWLLPTSLFLILDSCFVDMGPGTSWTVYPPL-STLGHPGSSVDLAIFSLHCAGISSILGG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 171 INFITTVINMRLPGMYAHRIPLFVWSIFVTAVLLLLAVPVLAGGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHP 250
Cdd:MTH00079 162 INFMVTTKNLRSSSISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGHP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 251 EVYIIILPAFGIISHVVSTFSSKQ-VFGYIGMVYAMSSIGLLGFIVWAHHMYTVGMDVDTRAYFTAATMIIAVPTGIKIF 329
Cdd:MTH00079 242 EVYILILPAFGIISQSTLYLTGKKeVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKVF 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 330 SWIATMWHGTIRLYTPMMFAVGFIFLFTLGGVTGVILSNSGLDVSLHDTYYVVGHFHYVLSMGALFGLFAGFYYWIGKMT 409
Cdd:MTH00079 322 SWLATLFGMKMKFQPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFMT 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1315028919 410 GAQYNETLGQVHFWLTFVGVNVTFFPMHFLGLAGMPRRIPDYPDAFAGWNEIASLGSLISIFAALFFFYVVFETFTSGR 488
Cdd:MTH00079 402 GIVYDKLMMSAVFFLMFVGVNLTFFPLHFAGLHGMPRKYLDYPDVYSVWNVISSYGSMISVFALFLFIYVLLESFFSYR 480
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
14-495 |
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: 624.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 14 LFSTNHKDIGTLYLIFAAAAGIVGSIFSLLIRLELAHPGNQILGGnhQLYNVIVTAHAFLMIFFLIMPaLIGGFGNWFVP 93
Cdd:TIGR02891 1 LTTVDHKRIGILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDA--ETYNQLFTMHGTIMIFLFAIP-ILAGFGNYLLP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 94 MMIGAPDMAFPRLNNISFWLLPPALILLVSSSLVEVGVGTGWTVYPPLASIQAHSGAAVDLAIFSLHLAGISSILGAINF 173
Cdd:TIGR02891 78 LMIGARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGAPDTGWTMYPPLSSTSGSPGVGVDLWLLGLHLLGISSILGAVNF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 174 ITTVINMRLPGMYAHRIPLFVWSIFVTAVLLLLAVPVLAGGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVY 253
Cdd:TIGR02891 158 IVTILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVY 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 254 IIILPAFGIISHVVSTFSSKQVFGYIGMVYAMSSIGLLGFIVWAHHMYTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIA 333
Cdd:TIGR02891 238 IIFLPAFGIISEILPTFARKPIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 334 TMWHGTIRLYTPMMFAVGFIFLFTLGGVTGVILSNSGLDVSLHDTYYVVGHFHYVLSMGALFGLFAGFYYWIGKMTGAQY 413
Cdd:TIGR02891 318 TLWGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMY 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 414 NETLGQVHFWLTFVGVNVTFFPMHFLGLAGMPRRIPDYPDA--FAGWNEIASLGSLISIFAALFFFYVVFETFTSGRVCP 491
Cdd:TIGR02891 398 NERLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGPKAG 477
|
....
gi 1315028919 492 RNPW 495
Cdd:TIGR02891 478 ANPW 481
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
12-496 |
0e+00 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 617.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 12 RWLFSTNHKDIGTLYLIFAAAAGIVGSIFSLLIRLELAHPGNQILGGNHqlYNVIVTAHAFLMIFFLIMPaLIGGFGNWF 91
Cdd:COG0843 8 RWLTTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPET--YNQLFTMHGTIMIFFFATP-FLAGFGNYL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 92 VPMMIGAPDMAFPRLNNISFWLLPPALILLVSSSLVEVGVGTGWTVYPPLASIQAHSGAAVDLAIFSLHLAGISSILGAI 171
Cdd:COG0843 85 VPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFVGGAADVGWTFYPPLSGLEASPGVGVDLWLLGLALFGVGSILGGV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 172 NFITTVINMRLPGMYAHRIPLFVWSIFVTAVLLLLAVPVLAGGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPE 251
Cdd:COG0843 165 NFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWFFGHPE 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 252 VYIIILPAFGIISHVVSTFSSKQVFGYIGMVYAMSSIGLLGFIVWAHHMYTVGMDVDTRAYFTAATMIIAVPTGIKIFSW 331
Cdd:COG0843 245 VYILILPAFGIVSEIIPTFSRKPLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGVKVFNW 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 332 IATMWHGTIRLYTPMMFAVGFIFLFTLGGVTGVILSNSGLDVSLHDTYYVVGHFHYVLSMGALFGLFAGFYYWIGKMTGA 411
Cdd:COG0843 325 IATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFPKMTGR 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 412 QYNETLGQVHFWLTFVGVNVTFFPMHFLGLAGMPRRIPDYP--DAFAGWNEIASLGSLISIFAALFFFYVVFETFTSGRV 489
Cdd:COG0843 405 MLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYPpePGWQPLNLISTIGAFILAVGFLLFLINLVVSLRKGPK 484
|
....*..
gi 1315028919 490 CPRNPWK 496
Cdd:COG0843 485 AGGNPWG 491
|
|
| COX1 |
MTH00026 |
cytochrome c oxidase subunit I; Provisional |
12-484 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 164599 Cd Length: 534 Bit Score: 608.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 12 RWLFSTNHKDIGTLYLIFAAAAGIVGSIFSLLIRLELAHPGNQIlgGNHQLYNVIVTAHAFLMIFFLIMPALIGGFGNWF 91
Cdd:MTH00026 6 RWFFSCNHKDIGSLYLVFGALSGAIGTAFSMLIRLELSSPGSML--GDDHLYNVIVTAHAFVMIFFLVMPTMIGGFGNWF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 92 VPMMIGAPDMAFPRLNNISFWLLPPALILLVSSSLVEVGVGTGWTVYPPLASIQAHSGAAVDLAIFSLHLAGISSILGAI 171
Cdd:MTH00026 84 VPLMIGAPDMAFPRLNNISFWLLPPALFLLLGSSLVEQGAGTGWTVYPPLASIQAHSGGSVDMAIFSLHLAGLSSILGAM 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 172 NFITTVINMRLPGMYAHRIPLFVWSIFVTAVLLLLAVPVLAGGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPE 251
Cdd:MTH00026 164 NFITTVMNMRTPGMTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHPE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 252 VYIIILPAFGIISHVVSTFS-SKQVFGYIGMVYAMSSIGLLGFIVWAHHMYTVGMDVDTRAYFTAATMIIAVPTGIKIFS 330
Cdd:MTH00026 244 VYILILPGFGIISQILSLFSyKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKIFS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 331 WIATMWHGTIRLY--TPMMFAVGFIFLFTLGGVTGVILSNSGLDVSLHDTYYVVGHFHYVLSMGALFGLFAGFYYWIGKM 408
Cdd:MTH00026 324 WLATVSGSGRNLIftTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWFGKI 403
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1315028919 409 TGAQYNETLGQVHFWLTFVGVNVTFFPMHFLGLAGMPRRIPDYPDAFAGWNEIASLGSLISIFAALFFFYVVFETF 484
Cdd:MTH00026 404 TGYAYKDIYGLIHFWLMFIGVNITFFPQHFLGLAGLPRRYADYPDNFEDFNQISSFGSIISIIAVIWFIVVIFDAY 479
|
|
| Heme_Cu_Oxidase_I |
cd00919 |
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ... |
19-484 |
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: 604.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 19 HKDIGTLYLIFAAAAGIVGSIFSLLIRLELAHPGNQILggNHQLYNVIVTAHAFLMIFFLIMPALIGGFGNWFVPMmIGA 98
Cdd:cd00919 1 HKDIGLLYLIFAFVALLLGGLLALLIRLELATPGSLFL--DPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPPL-IGA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 99 PDMAFPRLNNISFWLLPPALILLVSSSLVEVGVGTGWTVYPPLASIQAHSGAAVDLAIFSLHLAGISSILGAINFITTVI 178
Cdd:cd00919 78 RDLAFPRLNNLSFWLFPPGLLLLLSSVLVGGGAGTGWTFYPPLSTLSYSSGVGVDLAILGLHLAGVSSILGAINFITTIL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 179 NMRLPGMYAHRIPLFVWSIFVTAVLLLLAVPVLAGGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYIIILP 258
Cdd:cd00919 158 NMRAPGMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 259 AFGIISHVVSTFSSKQVFGYIGMVYAMSSIGLLGFIVWAHHMYTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATMWHG 338
Cdd:cd00919 238 AFGAISEIIPTFSGKPLFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 339 TIRLYTPMMFAVGFIFLFTLGGVTGVILSNSGLDVSLHDTYYVVGHFHYVLSMGALFGLFAGFYYWIGKMTGAQYNETLG 418
Cdd:cd00919 318 RIRFDPPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKLG 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1315028919 419 QVHFWLTFVGVNVTFFPMHFLGLAGMPRRIPDYPDAFAGWNEIASLGSLISIFAALFFFYVVFETF 484
Cdd:cd00919 398 KIHFWLWFIGFNLTFFPMHFLGLLGMPRRYADYPDGFAPWNFISSVGAFILGLGLLLFLGNLFLSL 463
|
|
| Ubiquinol_Oxidase_I |
cd01662 |
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ... |
13-495 |
0e+00 |
|
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: 527.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 13 WLFSTNHKDIGTLYLIFAAAAGIVGSIFSLLIRLELAHPGNQILGGNHqlYNVIVTAHAFLMIFFLIMPALIGgFGNWFV 92
Cdd:cd01662 1 WLTTVDHKRIGIMYIITAFVFFLRGGVDALLMRTQLALPGNDFLSPEH--YNQIFTMHGTIMIFLFAMPLVFG-LMNYLV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 93 PMMIGAPDMAFPRLNNISFWLLPPALILLVSSSLVEVGVGTGWTVYPPLASIQAHSGAAVDLAIFSLHLAGISSILGAIN 172
Cdd:cd01662 78 PLQIGARDVAFPRLNALSFWLFLFGGLLLNASLLIGGFPDAGWFAYPPLSGLEYSPGVGVDYWILGLQFSGIGTLLGAIN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 173 FITTVINMRLPGMYAHRIPLFVWSIFVTAVLLLLAVPVLAGGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEV 252
Cdd:cd01662 158 FIVTILKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 253 YIIILPAFGIISHVVSTFSSKQVFGYIGMVYAMSSIGLLGFIVWAHHMYTVGMDVDTRAYFTAATMIIAVPTGIKIFSWI 332
Cdd:cd01662 238 YILILPAFGIFSEIVPTFSRKPLFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 333 ATMWHGTIRLYTPMMFAVGFIFLFTLGGVTGVILSNSGLDVSLHDTYYVVGHFHYVLSMGALFGLFAGFYYWIGKMTGAQ 412
Cdd:cd01662 318 FTMWRGRIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRM 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 413 YNETLGQVHFWLTFVGVNVTFFPMHFLGLAGMPRRIPDYP--DAFAGWNEIASLGSLISIFAALFFFYVVFETFTSG-RV 489
Cdd:cd01662 398 LNERLGKWSFWLWFIGFNLTFFPMHILGLMGMPRRVYTYLpgPGWDPLNLISTIGAFLIAAGVLLFLINVIVSIRKGkRD 477
|
....*.
gi 1315028919 490 CPRNPW 495
Cdd:cd01662 478 ATGDPW 483
|
|
| COX1 |
MTH00048 |
cytochrome c oxidase subunit I; Provisional |
9-489 |
7.17e-161 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177123 Cd Length: 511 Bit Score: 466.08 E-value: 7.17e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 9 WSSRWLFSTNHKDIGTLYLIFAAAAGIVGSIFSLLIRLELAHPGNQILggNHQLYNVIVTAHAFLMIFFLIMPALIGGFG 88
Cdd:MTH00048 3 SLLSWLFTLDHKRIGVIYTLLGVWSGFVGLSLSLLIRLNFLDPYYNVI--SLDVYNFLITNHGIIMIFFFLMPVLIGGFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 89 NWFVPMMIGAPDMAFPRLNNISFWLLPPALILLVSSSLVevGVGTGWTVYPPLASIQAHSGAAVDLAIFSLHLAGISSIL 168
Cdd:MTH00048 81 NYLLPLLLGLSDLNLPRLNALSAWLLVPSIVFLLLSMCL--GAGVGWTFYPPLSSSLFSSSWGVDFLMFSLHLAGVSSLF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 169 GAINFITTVINMRLPGMYaHRIPLFVWSIFVTAVLLLLAVPVLAGGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFG 248
Cdd:MTH00048 159 GSINFICTIYSAFMTNVF-SRTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 249 HPEVYIIILPAFGIISHVVSTFS-SKQVFGYIGMVYAMSSIGLLGFIVWAHHMYTVGMDVDTRAYFTAATMIIAVPTGIK 327
Cdd:MTH00048 238 HPEVYVLILPGFGIISHICLSLSnNDDPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 328 IFSWIATMWHGTIRLYTPMM-FAVGFIFLFTLGGVTGVILSNSGLDVSLHDTYYVVGHFHYVLSMGALFGLFAGFYYWIG 406
Cdd:MTH00048 318 VFSWLYMLLNSRVRKSDPVVwWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWP 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 407 KMTGAQYNETLGQVHFWLTFVGVNVTFFPMHFLGLAGMPRRIPDYPDAFAGWNEIASLGSLISIFAALFFFYVVFETFTS 486
Cdd:MTH00048 398 LITGLSLNKYLLQCHCIISMIGFNLCFFPMHYFGLCGLPRRVCVYEPSYYWINVVCTVGSFISAFSGCFFVFILWESLVV 477
|
...
gi 1315028919 487 GRV 489
Cdd:MTH00048 478 KNE 480
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
21-468 |
1.28e-141 |
|
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: 413.89 E-value: 1.28e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 21 DIGTLYLIFAAAAGIVGSIFSLLIRLELAHPGNQILGGnhQLYNVIVTAHAFLMIFFLIMPAlIGGFGNWFVPMMIGAPD 100
Cdd:pfam00115 1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSP--LTYNQLRTLHGNLMIFWFATPF-LFGFGNYLVPLMIGARD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 101 MAFPRLNNISFWLLPPALILLVSSSLvevGVGTGWTVYPPLAsiqahsgaAVDLAIFSLHLAGISSILGAINFITTVINM 180
Cdd:pfam00115 78 MAFPRLNALSFWLVVLGAVLLLASFG---GATTGWTEYPPLV--------GVDLWYIGLLLAGVSSLLGAINFIVTILKR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 181 RLPGMYAhRIPLFVWSIFVTAVLLLLAVPVLAGGITMLLTDRNLNttffdpAGGGDPILYQHLFWFFGHPEVYIIILPAF 260
Cdd:pfam00115 147 RAPGMTL-RMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAF 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 261 GIISHVVSTFSSKQVFGYIGMVYAMSSIGLLGFIVWAHHMYTVGMDVDTRAYFTAATMIIAVPTGIKIFSWIATMWHGTI 340
Cdd:pfam00115 220 GIIYYILPKFAGRPLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWI 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 341 RLY-TPMMFAVGFIFLFTLGGVTGVILSNSGLDVSLHDTYYVVGHFHYVLSMGALFGLFAGFYYWIGKMTGAQYNETLGQ 419
Cdd:pfam00115 300 RFRtTPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGK 379
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1315028919 420 VHFWLTFVGVNVTFFPMHFLGLAGMPRRIP----DYPDAFAGWNEIASLGSLI 468
Cdd:pfam00115 380 LHFWLLFIGFNLTFFPMHILGLLGMPRRYAppfiETVPAFQPLNWIRTIGGVL 432
|
|
| QoxB |
TIGR02882 |
cytochrome aa3 quinol oxidase, subunit I; This family (QoxB) encodes subunit I of the aa3-type ... |
13-495 |
7.27e-124 |
|
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: 376.12 E-value: 7.27e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 13 WLFSTNHKDIGTLYLIFAAAAGIVGSIFSLLIRLELAHPGNQILGGNHqlYNVIVTAHAFLMIFFLIMPALIGgFGNWFV 92
Cdd:TIGR02882 44 WLTTVDHKKIGVMYIICAVLMLFRGGIDALLMRAQLTVPDNKFLDAQH--YNEIFTTHGVIMIIFMAMPFIIG-LMNIVV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 93 PMMIGAPDMAFPRLNNISFWLLPPALILLVSSSLVEVGVGTGWTVYPPLASIQAHSGAAVDLAIFSLHLAGISSILGAIN 172
Cdd:TIGR02882 121 PLQIGARDVAFPVLNALSFWLFFAGAMLFNISFVIGGSPDAGWTNYAPLAGPEFSPGVGVNYYLIALQISGIGTLMTGIN 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 173 FITTVINMRLPGMYAHRIPLFVWSIFVTAVLLLLAVPVLAGGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEV 252
Cdd:TIGR02882 201 FFVTILKMRAPGMKLMQMPMFTWTTLITTLIIIFAFPVLTVALALMTTDRIFDTAFFTVAHGGMPMLWANLFWIWGHPEV 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 253 YIIILPAFGIISHVVSTFSSKQVFGYIGMVYAMSSIGLLGFIVWAHHMYTVGMDVDTRAYFTAATMIIAVPTGIKIFSWI 332
Cdd:TIGR02882 281 YIVILPAFGIYSEIISTFAQKRLFGYKSMVWSTVGIAFLSFLVWVHHFFTMGNGALINSFFSITTMAIAIPTGVKIFNWL 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 333 ATMWHGTIRLYTPMMFAVGFIFLFTLGGVTGVILSNSGLDVSLHDTYYVVGHFHYVLSMGALFGLFAGFYYWIGKMTGAQ 412
Cdd:TIGR02882 361 LTLYKGKIRFTTPMLFSLAFIPNFLIGGVTGVMLAMASADYQYHNTYFLVAHFHYVLITGVVFACLAGLIYWYPKMFGYK 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 413 YNETLGQVHFWLTFVGVNVTFFPMHFLGLAGMPRRIPDYPDAfAGWNEIASLGSLISIFAALFFFYVVFETFTSGRVCPR 492
Cdd:TIGR02882 441 LNERLGKWCFWFFMIGFNVCFFPMYILGLDGMPRRMYTYSPS-DGWFPLNLISTIGALLMAIGFIFLVYNIYYSHRKSPR 519
|
....*..
gi 1315028919 493 N----PW 495
Cdd:TIGR02882 520 EatgdPW 526
|
|
| PRK15017 |
PRK15017 |
cytochrome o ubiquinol oxidase subunit I; Provisional |
7-495 |
3.34e-111 |
|
cytochrome o ubiquinol oxidase subunit I; Provisional
Pssm-ID: 184978 Cd Length: 663 Bit Score: 343.84 E-value: 3.34e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 7 YQWSsRWLFSTNHKDIGTLYLIFAAAAGIVGSIFSLLIRLE--LAHPGNQILGGNHQlYNVIVTAHAFLMIFFLIMPALI 84
Cdd:PRK15017 43 YLWK-EWLTSVDHKRLGIMYIIVAIVMLLRGFADAIMMRSQqaLASAGEAGFLPPHH-YDQIFTAHGVIMIFFVAMPFVI 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 85 GgFGNWFVPMMIGAPDMAFPRLNNISFWLLPPALILLVSSSLVEVGVGTGWTVYPPLASIQAHSGAAVDLAIFSLHLAGI 164
Cdd:PRK15017 121 G-LMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGI 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 165 SSILGAINFITTVINMRLPGMYAHRIPLFVWSIFVTAVLLLLAVPVLAGGITMLLTDRNLNTTFFDPAGGGDPILYQHLF 244
Cdd:PRK15017 200 GTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLI 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 245 WFFGHPEVYIIILPAFGIISHVVSTFSSKQVFGYIGMVYAMSSIGLLGFIVWAHHMYTVGMDVDTRAYFTAATMIIAVPT 324
Cdd:PRK15017 280 WAWGHPEVYILILPVFGVFSEIAATFSRKRLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPT 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 325 GIKIFSWIATMWHGTIRLYTPMMFAVGFIFLFTLGGVTGVILSNSGLDVSLHDTYYVVGHFHYVLSMGALFGLFAGFYYW 404
Cdd:PRK15017 360 GVKIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYW 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 405 IGKMTGAQYNETLGQVHFWLTFVGVNVTFFPMHFLGLAGMPRRIPDYPD-AFAGWNEIASLGSLI---SIFAALFFFYVV 480
Cdd:PRK15017 440 WPKAFGFKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMTRRLSQQIDpQFHTMLMIAASGAALialGILCQVIQMYVS 519
|
490
....*....|....*
gi 1315028919 481 FETFTSGRVCPRNPW 495
Cdd:PRK15017 520 IRDRDQNRDLTGDPW 534
|
|
| ba3-like_Oxidase_I |
cd01660 |
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ... |
26-483 |
1.05e-21 |
|
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: 97.74 E-value: 1.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 26 YLIFAAAAGIVGSIFSLLIRLElaHPGNQILGGNHQLYNVIVTAHAFLMIF----FLIMpaligGFGNWFVPMMIGAPDM 101
Cdd:cd01660 9 HFVVAFLALLLGGLFGLLQVLV--RTGVFPLPSSGILYYQGLTLHGVLLAIvfttFFIM-----GFFYAIVARALLRSLF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 102 AfPRLNNISFWLLppalilLVSSSLVEVGVGTG-----WTVYPPLasiQAHSGAAVDLAIFSLHlagiSSILGAINFITT 176
Cdd:cd01660 82 N-RRLAWAGFWLM------VIGTVMAAVPILLGqasvlYTFYPPL---QAHPLFYIGAALVVVG----SWISGFAMFVTL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 177 VINMRL-PGmyaHRIPLFVWSIFVTAVLLLLAVPVLAGGITMLLTDRNLNTTffdpaGGGDPILYQHLFWFFGHPEVYII 255
Cdd:cd01660 148 WRWKKAnPG---KKVPLATFMVVTTMILWLVASLGVALEVLFQLLPWSLGLV-----DTVDVLLSRTLFWWFGHPLVYFW 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 256 ILPAFGIISHVVSTFSSKQVFGYIGMVYAMSSIGLLGFIVWAHHMYT-VGMDVDTRAYFTAATMIIAVPTGIKIFSWIAT 334
Cdd:cd01660 220 LLPAYIAWYTILPKIAGGKLFSDPLARLAFILFLLFSTPVGFHHQFAdPGIGPGWKFIHMVLTFMVALPSLLTAFTVFAS 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 335 MWH-----------GTIRLY---TPMMFAVGF-IFLFTLGGVTGVILSNSGLDVSLHDTYYVVGHFHYVLSMGALFGLFA 399
Cdd:cd01660 300 LEIagrlrggkglfGWIRALpwgDPMFLALFLaMLMFIPGGAGGIINASYQLNYVVHNTAWVPGHFHLTVGGAVALTFMA 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1315028919 400 GFYYWIGKMTG-AQYNETLGQVHFWLTFVGVNVTFFPMHFLGLAGMPRRI-------PDYPDAFAGWNEIASLGSLISIF 471
Cdd:cd01660 380 VAYWLVPHLTGrELAAKRLALAQPWLWFVGMTIMSTAMHVAGLLGAPRRTaeaqyggLPAAGEWAPYQQLMAIGGTILFV 459
|
490
....*....|..
gi 1315028919 472 AALFFFYVVFET 483
Cdd:cd01660 460 SGALFLYILFRT 471
|
|
| |
