|
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 ... |
28-512 |
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: 756.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 28 TNHKDIGTMYLWFAFAMFLLGGSFAMVIRAELFQPGLQIVQPAFFNQMTTMHGLIMVFGAVMPA-FVGLANWMIPLMIGA 106
Cdd:cd01663 1 TNHKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPAlIGGFGNWLVPLMIGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 107 PDMALPRMNNFSFWLLPAAFLLLVSTLFTPGGgPNFGWTFYAPLSTTYA--PESVTFFIFAIHLMGISSIMGAINVVATI 184
Cdd:cd01663 81 PDMAFPRLNNLSFWLLPPSLLLLLLSALVEGG-AGTGWTVYPPLSSILAhsGPSVDLAIFSLHLAGISSILGAINFITTI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 185 LNLRAPGMTLMKMPLFVWTWLITAFLLIAVMPVLAGCVTMMLMDIHFGTSFFSAAGGGDPVLFQHVFWFFGHPEVYIMIL 264
Cdd:cd01663 160 FNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILIL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 265 PAFGAVSSIIPTFS-RKPLFGYTSMVYATASIAFLSFIVWAHHMFVVGIPLVGELFFMYATLLIAVPTGVKVFNWVSTMW 343
Cdd:cd01663 240 PGFGIISHIISTFSgKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMW 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 344 QGSLTFETPMLFAVAFVILFTIGGFSGLMLAIAPADFQYHDTYFVVAHFHYVLVPGAIFGIFASAYYWLPKWTGHMYDET 423
Cdd:cd01663 320 GGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNET 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 424 LGKLHFWLSFVGMNMAFFPMHFVGLAGMPRRVPDYNLQFADFNMVSSIGAFMFGATQIFFLFIVIKCIRGGTPAPAKPWD 503
Cdd:cd01663 400 LGKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFNVGE 479
|
....*....
gi 1236859391 504 GAEGLEWSV 512
Cdd:cd01663 480 GSTSLEWTL 488
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
16-527 |
0e+00 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 688.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 16 GPAKGLMRWVLTTNHKDIGTMYLWFAFAMFLLGGSFAMVIRAELFQPGLQIVQPAFFNQMTTMHGLIMVFGAVMPAFVGL 95
Cdd:COG0843 1 EWGSGWRRWLTTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATPFLAGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 96 ANWMIPLMIGAPDMALPRMNNFSFWLLPAAFLLLVSTLFTpGGGPNFGWTFYAPLSTTYA--PESVTFFIFAIHLMGISS 173
Cdd:COG0843 81 GNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFV-GGAADVGWTFYPPLSGLEAspGVGVDLWLLGLALFGVGS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 174 IMGAINVVATILNLRAPGMTLMKMPLFVWTWLITAFLLIAVMPVLAGCVTMMLMDIHFGTSFFSAAGGGDPVLFQHVFWF 253
Cdd:COG0843 160 ILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 254 FGHPEVYIMILPAFGAVSSIIPTFSRKPLFGYTSMVYATASIAFLSFIVWAHHMFVVGIPLVGELFFMYATLLIAVPTGV 333
Cdd:COG0843 240 FGHPEVYILILPAFGIVSEIIPTFSRKPLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 334 KVFNWVSTMWQGSLTFETPMLFAVAFVILFTIGGFSGLMLAIAPADFQYHDTYFVVAHFHYVLVPGAIFGIFASAYYWLP 413
Cdd:COG0843 320 KVFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFP 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 414 KWTGHMYDETLGKLHFWLSFVGMNMAFFPMHFVGLAGMPRRVPDY--NLQFADFNMVSSIGAFMFGATQIFFLFIVIKCI 491
Cdd:COG0843 400 KMTGRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYppEPGWQPLNLISTIGAFILAVGFLLFLINLVVSL 479
|
490 500 510
....*....|....*....|....*....|....*.
gi 1236859391 492 RGGTPAPAKPWdGAEGLEWSVPSPAPYHTFTTPPEV 527
Cdd:COG0843 480 RKGPKAGGNPW-GARTLEWATPSPPPLYNFASIPVV 514
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
25-521 |
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: 660.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 25 VLTTNHKDIGTMYLWFAFAMFLLGGSFAMVIRAELFQPGLQIVQPAFFNQMTTMHGLIMVFGAVMPAFVGLANWMIPLMI 104
Cdd:TIGR02891 1 LTTVDHKRIGILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIPILAGFGNYLLPLMI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 105 GAPDMALPRMNNFSFWLLPAAFLLLVSTLFTPGGgPNFGWTFYAPLSTT-YAP-ESVTFFIFAIHLMGISSIMGAINVVA 182
Cdd:TIGR02891 81 GARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGA-PDTGWTMYPPLSSTsGSPgVGVDLWLLGLHLLGISSILGAVNFIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 183 TILNLRAPGMTLMKMPLFVWTWLITAFLLIAVMPVLAGCVTMMLMDIHFGTSFFSAAGGGDPVLFQHVFWFFGHPEVYIM 262
Cdd:TIGR02891 160 TILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYII 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 263 ILPAFGAVSSIIPTFSRKPLFGYTSMVYATASIAFLSFIVWAHHMFVVGIPLVGELFFMYATLLIAVPTGVKVFNWVSTM 342
Cdd:TIGR02891 240 FLPAFGIISEILPTFARKPIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 343 WQGSLTFETPMLFAVAFVILFTIGGFSGLMLAIAPADFQYHDTYFVVAHFHYVLVPGAIFGIFASAYYWLPKWTGHMYDE 422
Cdd:TIGR02891 320 WGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 423 TLGKLHFWLSFVGMNMAFFPMHFVGLAGMPRRVPDYNLQ--FADFNMVSSIGAFMFGATQIFFLFIVIKCIRGGTPAPAK 500
Cdd:TIGR02891 400 RLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGPKAGAN 479
|
490 500
....*....|....*....|.
gi 1236859391 501 PWdGAEGLEWSVPSPAPYHTF 521
Cdd:TIGR02891 480 PW-GATTLEWTTSSPPPAHNF 499
|
|
| COX1 |
MTH00223 |
cytochrome c oxidase subunit I; Provisional |
22-522 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177260 Cd Length: 512 Bit Score: 531.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 22 MRWVLTTNHKDIGTMYLWFAFAMFLLGGSFAMVIRAELFQPGLQIVQPAFFNQMTTMHGLIMVFGAVMPAFVG-LANWMI 100
Cdd:MTH00223 1 MRWLFSTNHKDIGTLYLIFGMWSGLVGTSLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGgFGNWLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 101 PLMIGAPDMALPRMNNFSFWLLPAAFLLLVSTLFTpGGGPNFGWTFYAPLSTT--YAPESVTFFIFAIHLMGISSIMGAI 178
Cdd:MTH00223 81 PLMLGAPDMAFPRLNNMSFWLLPPSLYLLLSSSAV-ESGVGTGWTVYPPLSSNlaHAGPSVDLAIFSLHLAGVSSILGAI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 179 NVVATILNLRAPGMTLMKMPLFVWTWLITAFLLIAVMPVLAGCVTMMLMDIHFGTSFFSAAGGGDPVLFQHVFWFFGHPE 258
Cdd:MTH00223 160 NFITTIINMRSPGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 259 VYIMILPAFGAVSSIIPTFSRK-PLFGYTSMVYATASIAFLSFIVWAHHMFVVGIPLVGELFFMYATLLIAVPTGVKVFN 337
Cdd:MTH00223 240 VYILILPGFGMISHIVSHYSSKkEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 338 WVSTMWQGSLTFETPMLFAVAFVILFTIGGFSGLMLAIAPADFQYHDTYFVVAHFHYVLVPGAIFGIFASAYYWLPKWTG 417
Cdd:MTH00223 320 WLATIYGSKIKYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLFTG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 418 HMYDETLGKLHFWLSFVGMNMAFFPMHFVGLAGMPRRVPDYNLQFADFNMVSSIGAFMFGATQIFFLFIVIKCIRGGTPa 497
Cdd:MTH00223 400 VTLHRRWAKAHFFLMFLGVNLTFFPQHFLGLAGMPRRYSDYPDCYTKWNQVSSFGSMISFVSVLFFMFIVWEAFVSQRS- 478
|
490 500
....*....|....*....|....*
gi 1236859391 498 PAKPWDGAEGLEWSVPSPAPYHTFT 522
Cdd:MTH00223 479 VVWSGHLSTSLEWDNLLPADFHNNS 503
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
32-475 |
1.25e-151 |
|
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: 440.47 E-value: 1.25e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 32 DIGTMYLWFAFAMFLLGGSFAMVIRAELFQPGLQIVQPAFFNQMTTMHGLIMVFGAVMPAFVGLANWMIPLMIGAPDMAL 111
Cdd:pfam00115 1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATPFLFGFGNYLVPLMIGARDMAF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 112 PRMNNFSFWLLPAAFLLLVSTLftpgGGPNFGWTFYAPLSttyapeSVTFFIFAIHLMGISSIMGAINVVATILNLRAPG 191
Cdd:pfam00115 81 PRLNALSFWLVVLGAVLLLASF----GGATTGWTEYPPLV------GVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 192 MTlMKMPLFVWTWLITAFLLIAVMPVLAGCVTMMLMDIHFGtsffsaAGGGDPVLFQHVFWFFGHPEVYIMILPAFGAVS 271
Cdd:pfam00115 151 MT-LRMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGIIY 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 272 SIIPTFSRKPLFGYTSMVYATASIAFLSFIVWAHHMFVVGIPLVGELFFMYATLLIAVPTGVKVFNWVSTMWQGSLTF-E 350
Cdd:pfam00115 224 YILPKFAGRPLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFrT 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 351 TPMLFAVAFVILFTIGGFSGLMLAIAPADFQYHDTYFVVAHFHYVLVPGAIFGIFASAYYWLPKWTGHMYDETLGKLHFW 430
Cdd:pfam00115 304 TPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFW 383
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1236859391 431 LSFVGMNMAFFPMHFVGLAGMPRRVPDYNL----QFADFNMVSSIGAFM 475
Cdd:pfam00115 384 LLFIGFNLTFFPMHILGLLGMPRRYAPPFIetvpAFQPLNWIRTIGGVL 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 ... |
28-512 |
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: 756.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 28 TNHKDIGTMYLWFAFAMFLLGGSFAMVIRAELFQPGLQIVQPAFFNQMTTMHGLIMVFGAVMPA-FVGLANWMIPLMIGA 106
Cdd:cd01663 1 TNHKDIGTLYLIFGLWSGLVGTSLSLLIRLELSQPGSQLGNDQLYNVIVTAHALIMIFFMVMPAlIGGFGNWLVPLMIGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 107 PDMALPRMNNFSFWLLPAAFLLLVSTLFTPGGgPNFGWTFYAPLSTTYA--PESVTFFIFAIHLMGISSIMGAINVVATI 184
Cdd:cd01663 81 PDMAFPRLNNLSFWLLPPSLLLLLLSALVEGG-AGTGWTVYPPLSSILAhsGPSVDLAIFSLHLAGISSILGAINFITTI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 185 LNLRAPGMTLMKMPLFVWTWLITAFLLIAVMPVLAGCVTMMLMDIHFGTSFFSAAGGGDPVLFQHVFWFFGHPEVYIMIL 264
Cdd:cd01663 160 FNMRAPGMTLEKMPLFVWSVLITAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPEVYILIL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 265 PAFGAVSSIIPTFS-RKPLFGYTSMVYATASIAFLSFIVWAHHMFVVGIPLVGELFFMYATLLIAVPTGVKVFNWVSTMW 343
Cdd:cd01663 240 PGFGIISHIISTFSgKKPVFGYLGMVYAMLSIGILGFIVWAHHMFTVGLDVDTRAYFTAATMIIAVPTGIKVFSWLATMW 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 344 QGSLTFETPMLFAVAFVILFTIGGFSGLMLAIAPADFQYHDTYFVVAHFHYVLVPGAIFGIFASAYYWLPKWTGHMYDET 423
Cdd:cd01663 320 GGSIKFETPMLWALGFIFLFTIGGLTGVVLANSSLDIALHDTYYVVAHFHYVLSMGAVFAIFAGFYYWFPKITGLSYNET 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 424 LGKLHFWLSFVGMNMAFFPMHFVGLAGMPRRVPDYNLQFADFNMVSSIGAFMFGATQIFFLFIVIKCIRGGTPAPAKPWD 503
Cdd:cd01663 400 LGKIHFWLMFIGVNLTFFPQHFLGLAGMPRRYPDYPDAYAGWNMISSIGSLISFVSVLLFLFIVWESFVSGRKVIFNVGE 479
|
....*....
gi 1236859391 504 GAEGLEWSV 512
Cdd:cd01663 480 GSTSLEWTL 488
|
|
| CyoB |
COG0843 |
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion]; |
16-527 |
0e+00 |
|
Heme/copper-type cytochrome/quinol oxidase, subunit 1 [Energy production and conversion];
Pssm-ID: 440605 Cd Length: 535 Bit Score: 688.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 16 GPAKGLMRWVLTTNHKDIGTMYLWFAFAMFLLGGSFAMVIRAELFQPGLQIVQPAFFNQMTTMHGLIMVFGAVMPAFVGL 95
Cdd:COG0843 1 EWGSGWRRWLTTVDHKRIGIMYLVTAFVFLLIGGLLALLMRLQLAGPGLGLLSPETYNQLFTMHGTIMIFFFATPFLAGF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 96 ANWMIPLMIGAPDMALPRMNNFSFWLLPAAFLLLVSTLFTpGGGPNFGWTFYAPLSTTYA--PESVTFFIFAIHLMGISS 173
Cdd:COG0843 81 GNYLVPLQIGARDMAFPRLNALSFWLYLFGGLLLLISLFV-GGAADVGWTFYPPLSGLEAspGVGVDLWLLGLALFGVGS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 174 IMGAINVVATILNLRAPGMTLMKMPLFVWTWLITAFLLIAVMPVLAGCVTMMLMDIHFGTSFFSAAGGGDPVLFQHVFWF 253
Cdd:COG0843 160 ILGGVNFIVTILKMRAPGMTLMRMPLFTWAALVTSILILLAFPVLAAALLLLLLDRSLGTHFFDPAGGGDPLLWQHLFWF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 254 FGHPEVYIMILPAFGAVSSIIPTFSRKPLFGYTSMVYATASIAFLSFIVWAHHMFVVGIPLVGELFFMYATLLIAVPTGV 333
Cdd:COG0843 240 FGHPEVYILILPAFGIVSEIIPTFSRKPLFGYKAMVLATVAIAFLSFLVWAHHMFTPGISPLVKAFFSIATMLIAVPTGV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 334 KVFNWVSTMWQGSLTFETPMLFAVAFVILFTIGGFSGLMLAIAPADFQYHDTYFVVAHFHYVLVPGAIFGIFASAYYWLP 413
Cdd:COG0843 320 KVFNWIATMWRGRIRFTTPMLFALGFIILFVIGGLTGVMLASVPLDYQVHDTYFVVAHFHYVLIGGVVFAFFAGLYYWFP 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 414 KWTGHMYDETLGKLHFWLSFVGMNMAFFPMHFVGLAGMPRRVPDY--NLQFADFNMVSSIGAFMFGATQIFFLFIVIKCI 491
Cdd:COG0843 400 KMTGRMLNERLGKIHFWLWFIGFNLTFFPMHILGLLGMPRRYATYppEPGWQPLNLISTIGAFILAVGFLLFLINLVVSL 479
|
490 500 510
....*....|....*....|....*....|....*.
gi 1236859391 492 RGGTPAPAKPWdGAEGLEWSVPSPAPYHTFTTPPEV 527
Cdd:COG0843 480 RKGPKAGGNPW-GARTLEWATPSPPPLYNFASIPVV 514
|
|
| CtaD_CoxA |
TIGR02891 |
cytochrome c oxidase, subunit I; This large family represents subunit I's (CtaD, CoxA, CaaA) ... |
25-521 |
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: 660.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 25 VLTTNHKDIGTMYLWFAFAMFLLGGSFAMVIRAELFQPGLQIVQPAFFNQMTTMHGLIMVFGAVMPAFVGLANWMIPLMI 104
Cdd:TIGR02891 1 LTTVDHKRIGILYLVTAFAFFLVGGVLALLMRAQLATPGNTFMDAETYNQLFTMHGTIMIFLFAIPILAGFGNYLLPLMI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 105 GAPDMALPRMNNFSFWLLPAAFLLLVSTLFTPGGgPNFGWTFYAPLSTT-YAP-ESVTFFIFAIHLMGISSIMGAINVVA 182
Cdd:TIGR02891 81 GARDMAFPRLNAFSYWLYLFGGLLLLASFFTGGA-PDTGWTMYPPLSSTsGSPgVGVDLWLLGLHLLGISSILGAVNFIV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 183 TILNLRAPGMTLMKMPLFVWTWLITAFLLIAVMPVLAGCVTMMLMDIHFGTSFFSAAGGGDPVLFQHVFWFFGHPEVYIM 262
Cdd:TIGR02891 160 TILNMRAPGMTLMRMPLFVWGILVTSILILLAFPVLIAALILLLLDRLFGTHFFDPARGGDPLLWQHLFWFFGHPEVYII 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 263 ILPAFGAVSSIIPTFSRKPLFGYTSMVYATASIAFLSFIVWAHHMFVVGIPLVGELFFMYATLLIAVPTGVKVFNWVSTM 342
Cdd:TIGR02891 240 FLPAFGIISEILPTFARKPIFGYRAMVYATVAIGFLSFGVWAHHMFTTGMPPLALAFFSAATMLIAVPTGVKVFNWIATL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 343 WQGSLTFETPMLFAVAFVILFTIGGFSGLMLAIAPADFQYHDTYFVVAHFHYVLVPGAIFGIFASAYYWLPKWTGHMYDE 422
Cdd:TIGR02891 320 WGGSIRFTTPMLFALGFIFLFVIGGLTGVMLASVPLDWQLHDTYFVVAHFHYVLVGGSVFAIFAAIYYWFPKVTGRMYNE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 423 TLGKLHFWLSFVGMNMAFFPMHFVGLAGMPRRVPDYNLQ--FADFNMVSSIGAFMFGATQIFFLFIVIKCIRGGTPAPAK 500
Cdd:TIGR02891 400 RLGRWHFWLTFVGFNLTFFPMHLLGLLGMPRRYYTYPPQmgFATLNLISTIGAFILAAGFLVFLWNLIWSLRKGPKAGAN 479
|
490 500
....*....|....*....|.
gi 1236859391 501 PWdGAEGLEWSVPSPAPYHTF 521
Cdd:TIGR02891 480 PW-GATTLEWTTSSPPPAHNF 499
|
|
| Ubiquinol_Oxidase_I |
cd01662 |
Ubiquinol oxidase subunit I. Ubiquinol oxidase, the terminal oxidase in the respiratory ... |
24-521 |
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: 598.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 24 WVLTTNHKDIGTMYLWFAFAMFLLGGSFAMVIRAELFQPGLQIVQPAFFNQMTTMHGLIMVFGAVMPAFVGLANWMIPLM 103
Cdd:cd01662 1 WLTTVDHKRIGIMYIITAFVFFLRGGVDALLMRTQLALPGNDFLSPEHYNQIFTMHGTIMIFLFAMPLVFGLMNYLVPLQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 104 IGAPDMALPRMNNFSFWLLPAAFLLLVSTLFTpGGGPNFGWTFYAPLST-TYAP-ESVTFFIFAIHLMGISSIMGAINVV 181
Cdd:cd01662 81 IGARDVAFPRLNALSFWLFLFGGLLLNASLLI-GGFPDAGWFAYPPLSGlEYSPgVGVDYWILGLQFSGIGTLLGAINFI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 182 ATILNLRAPGMTLMKMPLFVWTWLITAFLLIAVMPVLAGCVTMMLMDIHFGTSFFSAAGGGDPVLFQHVFWFFGHPEVYI 261
Cdd:cd01662 160 VTILKMRAPGMTLMRMPIFTWTTLVTSILILFAFPVLTAALALLELDRYFGTHFFTNALGGNPMLWQHLFWIFGHPEVYI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 262 MILPAFGAVSSIIPTFSRKPLFGYTSMVYATASIAFLSFIVWAHHMFVVGIPLVGELFFMYATLLIAVPTGVKVFNWVST 341
Cdd:cd01662 240 LILPAFGIFSEIVPTFSRKPLFGYRSMVYATVAIGFLSFGVWVHHMFTTGAGALVNAFFSIATMIIAVPTGVKIFNWLFT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 342 MWQGSLTFETPMLFAVAFVILFTIGGFSGLMLAIAPADFQYHDTYFVVAHFHYVLVPGAIFGIFASAYYWLPKWTGHMYD 421
Cdd:cd01662 320 MWRGRIRFETPMLWAIGFLVTFVIGGLTGVMLASPPADFQVHDTYFVVAHFHYVLIGGVVFPLFAGFYYWFPKMFGRMLN 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 422 ETLGKLHFWLSFVGMNMAFFPMHFVGLAGMPRRVPDY--NLQFADFNMVSSIGAFMFGATQIFFLFIVIKCIR-GGTPAP 498
Cdd:cd01662 400 ERLGKWSFWLWFIGFNLTFFPMHILGLMGMPRRVYTYlpGPGWDPLNLISTIGAFLIAAGVLLFLINVIVSIRkGKRDAT 479
|
490 500
....*....|....*....|...
gi 1236859391 499 AKPWdGAEGLEWSVPSPAPYHTF 521
Cdd:cd01662 480 GDPW-GARTLEWATSSPPPAYNF 501
|
|
| Heme_Cu_Oxidase_I |
cd00919 |
Heme-copper oxidase subunit I. Heme-copper oxidases are transmembrane protein complexes in ... |
30-491 |
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: 558.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 30 HKDIGTMYLWFAFAMFLLGGSFAMVIRAELFQPGLQIVQPAFFNQMTTMHGLIMVFGAVMPAFVGLANWMIPLMIGAPDM 109
Cdd:cd00919 1 HKDIGLLYLIFAFVALLLGGLLALLIRLELATPGSLFLDPQLYNQLVTAHGVIMIFFFVMPAIFGGFGNLLPPLIGARDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 110 ALPRMNNFSFWLLPAAFLLLVSTLFTpGGGPNFGWTFYAPLSTTYAPE--SVTFFIFAIHLMGISSIMGAINVVATILNL 187
Cdd:cd00919 81 AFPRLNNLSFWLFPPGLLLLLSSVLV-GGGAGTGWTFYPPLSTLSYSSgvGVDLAILGLHLAGVSSILGAINFITTILNM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 188 RAPGMTLMKMPLFVWTWLITAFLLIAVMPVLAGCVTMMLMDIHFGTSFFSAAGGGDPVLFQHVFWFFGHPEVYIMILPAF 267
Cdd:cd00919 160 RAPGMTLDKMPLFVWSVLVTAILLLLALPVLAAALVMLLLDRNFGTSFFDPAGGGDPVLYQHLFWFFGHPEVYILILPAF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 268 GAVSSIIPTFSRKPLFGYTSMVYATASIAFLSFIVWAHHMFVVGIPLVGELFFMYATLLIAVPTGVKVFNWVSTMWQGSL 347
Cdd:cd00919 240 GAISEIIPTFSGKPLFGYKLMVYAFLAIGFLSFLVWAHHMFTVGLPVDTRAYFTAATMIIAVPTGIKVFNWLATLWGGRI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 348 TFETPMLFAVAFVILFTIGGFSGLMLAIAPADFQYHDTYFVVAHFHYVLVPGAIFGIFASAYYWLPKWTGHMYDETLGKL 427
Cdd:cd00919 320 RFDPPMLFALGFLFLFTIGGLTGVVLANVPLDIVLHDTYYVVAHFHYVLSGGVVFAIFAGLYYWFPKMTGRMLSEKLGKI 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1236859391 428 HFWLSFVGMNMAFFPMHFVGLAGMPRRVPDYNLQFADFNMVSSIGAFMFGATQIFFLFIVIKCI 491
Cdd:cd00919 400 HFWLWFIGFNLTFFPMHFLGLLGMPRRYADYPDGFAPWNFISSVGAFILGLGLLLFLGNLFLSL 463
|
|
| COX1 |
MTH00223 |
cytochrome c oxidase subunit I; Provisional |
22-522 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177260 Cd Length: 512 Bit Score: 531.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 22 MRWVLTTNHKDIGTMYLWFAFAMFLLGGSFAMVIRAELFQPGLQIVQPAFFNQMTTMHGLIMVFGAVMPAFVG-LANWMI 100
Cdd:MTH00223 1 MRWLFSTNHKDIGTLYLIFGMWSGLVGTSLSLLIRAELGQPGALLGDDQLYNVIVTAHAFVMIFFLVMPMMIGgFGNWLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 101 PLMIGAPDMALPRMNNFSFWLLPAAFLLLVSTLFTpGGGPNFGWTFYAPLSTT--YAPESVTFFIFAIHLMGISSIMGAI 178
Cdd:MTH00223 81 PLMLGAPDMAFPRLNNMSFWLLPPSLYLLLSSSAV-ESGVGTGWTVYPPLSSNlaHAGPSVDLAIFSLHLAGVSSILGAI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 179 NVVATILNLRAPGMTLMKMPLFVWTWLITAFLLIAVMPVLAGCVTMMLMDIHFGTSFFSAAGGGDPVLFQHVFWFFGHPE 258
Cdd:MTH00223 160 NFITTIINMRSPGMQLERLPLFVWSVKVTAFLLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHPE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 259 VYIMILPAFGAVSSIIPTFSRK-PLFGYTSMVYATASIAFLSFIVWAHHMFVVGIPLVGELFFMYATLLIAVPTGVKVFN 337
Cdd:MTH00223 240 VYILILPGFGMISHIVSHYSSKkEVFGTLGMIYAMLSIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 338 WVSTMWQGSLTFETPMLFAVAFVILFTIGGFSGLMLAIAPADFQYHDTYFVVAHFHYVLVPGAIFGIFASAYYWLPKWTG 417
Cdd:MTH00223 320 WLATIYGSKIKYEAPMLWALGFIFLFTVGGLTGIILSNSSLDIMLHDTYYVVAHFHYVLSMGAVFALFAGFNHWFPLFTG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 418 HMYDETLGKLHFWLSFVGMNMAFFPMHFVGLAGMPRRVPDYNLQFADFNMVSSIGAFMFGATQIFFLFIVIKCIRGGTPa 497
Cdd:MTH00223 400 VTLHRRWAKAHFFLMFLGVNLTFFPQHFLGLAGMPRRYSDYPDCYTKWNQVSSFGSMISFVSVLFFMFIVWEAFVSQRS- 478
|
490 500
....*....|....*....|....*
gi 1236859391 498 PAKPWDGAEGLEWSVPSPAPYHTFT 522
Cdd:MTH00223 479 VVWSGHLSTSLEWDNLLPADFHNNS 503
|
|
| COX1 |
MTH00153 |
cytochrome c oxidase subunit I; Provisional |
21-487 |
0e+00 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177210 Cd Length: 511 Bit Score: 529.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 21 LMRWVLTTNHKDIGTMYLWFAFAMFLLGGSFAMVIRAELFQPGLQIVQPAFFNQMTTMHGLIMVFGAVMPAFVG-LANWM 99
Cdd:MTH00153 1 MNKWLFSTNHKDIGTLYFIFGAWSGMVGTSLSLLIRAELGQPGSLIGDDQIYNVIVTAHAFIMIFFMVMPIMIGgFGNWL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 100 IPLMIGAPDMALPRMNNFSFWLLPAA-FLLLVSTLFTPGGGPnfGWTFYAPLSTT--YAPESVTFFIFAIHLMGISSIMG 176
Cdd:MTH00153 81 VPLMLGAPDMAFPRMNNMSFWLLPPSlTLLLSSSMVESGAGT--GWTVYPPLSSNiaHSGASVDLAIFSLHLAGISSILG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 177 AINVVATILNLRAPGMTLMKMPLFVWTWLITAFLLIAVMPVLAGCVTMMLMDIHFGTSFFSAAGGGDPVLFQHVFWFFGH 256
Cdd:MTH00153 159 AINFITTIINMRSKGMTLDRMPLFVWSVLITAILLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 257 PEVYIMILPAFGAVSSIIPTFS-RKPLFGYTSMVYATASIAFLSFIVWAHHMFVVGIPLVGELFFMYATLLIAVPTGVKV 335
Cdd:MTH00153 239 PEVYILILPGFGMISHIISQESgKKETFGTLGMIYAMLAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 336 FNWVSTMWQGSLTFETPMLFAVAFVILFTIGGFSGLMLAIAPADFQYHDTYFVVAHFHYVLVPGAIFGIFASAYYWLPKW 415
Cdd:MTH00153 319 FSWLATLHGSQINYSPSLLWALGFVFLFTIGGLTGVVLANSSIDIILHDTYYVVAHFHYVLSMGAVFAIMGGFIHWFPLF 398
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1236859391 416 TGHMYDETLGKLHFWLSFVGMNMAFFPMHFVGLAGMPRRVPDYNLQFADFNMVSSIGAFMFGATQIFFLFIV 487
Cdd:MTH00153 399 TGLTMNPKWLKIQFFIMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTSWNVISSIGSTISLISILFFIFII 470
|
|
| COX1 |
MTH00116 |
cytochrome c oxidase subunit I; Provisional |
21-525 |
6.17e-179 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177177 Cd Length: 515 Bit Score: 513.49 E-value: 6.17e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 21 LMRWVLTTNHKDIGTMYLWFAFAMFLLGGSFAMVIRAELFQPGLQIVQPAFFNQMTTMHGLIMVFGAVMPAFVG-LANWM 99
Cdd:MTH00116 3 ITRWLFSTNHKDIGTLYLIFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGgFGNWL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 100 IPLMIGAPDMALPRMNNFSFWLLPAAFLLLVSTLFTpGGGPNFGWTFYAPLST--TYAPESVTFFIFAIHLMGISSIMGA 177
Cdd:MTH00116 83 VPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSTV-EAGAGTGWTVYPPLAGnlAHAGASVDLAIFSLHLAGVSSILGA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 178 INVVATILNLRAPGMTLMKMPLFVWTWLITAFLLIAVMPVLAGCVTMMLMDIHFGTSFFSAAGGGDPVLFQHVFWFFGHP 257
Cdd:MTH00116 162 INFITTCINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 258 EVYIMILPAFGAVSSIIPTFS-RKPLFGYTSMVYATASIAFLSFIVWAHHMFVVGIPLVGELFFMYATLLIAVPTGVKVF 336
Cdd:MTH00116 242 EVYILILPGFGIISHIVTYYAgKKEPFGYMGMVWAMLSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGIKVF 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 337 NWVSTMWQGSLTFETPMLFAVAFVILFTIGGFSGLMLAIAPADFQYHDTYFVVAHFHYVLVPGAIFGIFASAYYWLPKWT 416
Cdd:MTH00116 322 SWLATLHGGTIKWDPPMLWALGFIFLFTIGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFT 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 417 GHMYDETLGKLHFWLSFVGMNMAFFPMHFVGLAGMPRRVPDYNLQFADFNMVSSIGAFMFGATQIFFLFIVIKCIRGGTP 496
Cdd:MTH00116 402 GYTLHQTWTKAQFGVMFTGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTISSIGSLISMTAVIMLMFIIWEAFSSKRK 481
|
490 500
....*....|....*....|....*....
gi 1236859391 497 aPAKPWDGAEGLEWSVPSPAPYHTFTTPP 525
Cdd:MTH00116 482 -VLQPELTTTNIEWIHGCPPPYHTFEEPA 509
|
|
| COX1 |
MTH00167 |
cytochrome c oxidase subunit I; Provisional |
21-528 |
5.31e-178 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177222 Cd Length: 512 Bit Score: 510.76 E-value: 5.31e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 21 LMRWVLTTNHKDIGTMYLWFAFAMFLLGGSFAMVIRAELFQPGLQIVQPAFFNQMTTMHGLIMVFGAVMPAFVG-LANWM 99
Cdd:MTH00167 3 INRWLFSTNHKDIGTLYFIFGAWAGMVGTALSLLIRAELSQPGSLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGgFGNWL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 100 IPLMIGAPDMALPRMNNFSFWLLPAAFLLLVSTLFTpGGGPNFGWTFYAPLSTT--YAPESVTFFIFAIHLMGISSIMGA 177
Cdd:MTH00167 83 VPLMIGAPDMAFPRMNNMSFWLLPPSLLLLLASSGV-EAGAGTGWTVYPPLAGNlaHAGASVDLAIFSLHLAGVSSILGS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 178 INVVATILNLRAPGMTLMKMPLFVWTWLITAFLLIAVMPVLAGCVTMMLMDIHFGTSFFSAAGGGDPVLFQHVFWFFGHP 257
Cdd:MTH00167 162 INFITTIINMKPPGITQYQTPLFVWSILVTTILLLLSLPVLAAAITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 258 EVYIMILPAFGAVSSIIPTFS-RKPLFGYTSMVYATASIAFLSFIVWAHHMFVVGIPLVGELFFMYATLLIAVPTGVKVF 336
Cdd:MTH00167 242 EVYILILPGFGMISHIVVYYSgKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKVF 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 337 NWVSTMWQGSLTFETPMLFAVAFVILFTIGGFSGLMLAIAPADFQYHDTYFVVAHFHYVLVPGAIFGIFASAYYWLPKWT 416
Cdd:MTH00167 322 SWLATLHGGKIKWETPMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFTHWFPLFT 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 417 GHMYDETLGKLHFWLSFVGMNMAFFPMHFVGLAGMPRRVPDYNLQFADFNMVSSIGAFMFGATQIFFLFIVIKCIRGGTP 496
Cdd:MTH00167 402 GLTLNETWTKIHFFVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNVVSSIGSLISLVAVILFLFIIWEAFSSKRK 481
|
490 500 510
....*....|....*....|....*....|..
gi 1236859391 497 APAKPWDGaEGLEWSVPSPAPYHTFTTPPEVK 528
Cdd:MTH00167 482 LLPVELTS-TNVEWLHGCPPPHHTWEEPPFVQ 512
|
|
| COX1 |
MTH00184 |
cytochrome c oxidase subunit I; Provisional |
21-527 |
4.70e-171 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177235 Cd Length: 519 Bit Score: 493.57 E-value: 4.70e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 21 LMRWVLTTNHKDIGTMYLWFAFAMFLLGGSFAMVIRAELFQPGLQIVQPAFFNQMTTMHGLIMVFGAVMPAFVG-LANWM 99
Cdd:MTH00184 5 LSRWLFSTNHKDIGTLYLLFGAFAGMIGTAFSMLIRLELSAPGSMLGDDHLYNVIVTAHAFVMIFFLVMPVMIGgFGNWF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 100 IPLMIGAPDMALPRMNNFSFWLLPAAFLLLVSTLFTPGGGPNfGWTFYAPLST--TYAPESVTFFIFAIHLMGISSIMGA 177
Cdd:MTH00184 85 VPLYIGAPDMAFPRLNNISFWLLPPALTLLLGSAFVEQGAGT-GWTVYPPLSSiqAHSGGSVDMAIFSLHLAGISSILGA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 178 INVVATILNLRAPGMTLMKMPLFVWTWLITAFLLIAVMPVLAGCVTMMLMDIHFGTSFFSAAGGGDPVLFQHVFWFFGHP 257
Cdd:MTH00184 164 MNFITTIFNMRAPGITMDRMPLFVWSILVTTFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGHP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 258 EVYIMILPAFGAVSSIIPTFS-RKPLFGYTSMVYATASIAFLSFIVWAHHMFVVGIPLVGELFFMYATLLIAVPTGVKVF 336
Cdd:MTH00184 244 EVYILILPGFGIISQIIPTFAaKKQIFGYLGMVYAMVSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKIF 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 337 NWVSTMWQGSLTFETPMLFAVAFVILFTIGGFSGLMLAIAPADFQYHDTYFVVAHFHYVLVPGAIFGIFASAYYWLPKWT 416
Cdd:MTH00184 324 SWIATIFGGSLRLDTPMLWAIGFVFLFTMGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKIT 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 417 GHMYDETLGKLHFWLSFVGMNMAFFPMHFVGLAGMPRRVPDYNLQFADFNMVSSIGAFMFGATQIFFLFIVIKCIRGGTP 496
Cdd:MTH00184 404 GYCYNEVYGKIHFWLMFIGVNLTFFPQHFLGLAGLPRRYSDFHDSFAGWNQISSLGSVISIVGVVWFIYIVYDAYVREIK 483
|
490 500 510
....*....|....*....|....*....|...
gi 1236859391 497 --APAKPWDGAEGLEWSVPSPAPYHTFTTPPEV 527
Cdd:MTH00184 484 fvGWVEDSGHYPSLEWAQTSPPAHHTYNELPYV 516
|
|
| COX1 |
MTH00182 |
cytochrome c oxidase subunit I; Provisional |
21-527 |
7.33e-171 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214451 Cd Length: 525 Bit Score: 493.18 E-value: 7.33e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 21 LMRWVLTTNHKDIGTMYLWFAFAMFLLGGSFAMVIRAELFQPGLQIVQPAFFNQMTTMHGLIMVFGAVMPAFVG-LANWM 99
Cdd:MTH00182 5 LTRWVFSTNHKDIGTLYLVFGAGAGMIGTAFSMLIRLELSAPGAMLGDDHLYNVIVTAHAFIMIFFLVMPVMIGgFGNWL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 100 IPLMIGAPDMALPRMNNFSFWLLPAAFLLLVSTLFTPGGGPNfGWTFYAPLSTTYAPE--SVTFFIFAIHLMGISSIMGA 177
Cdd:MTH00182 85 VPLYIGAPDMAFPRLNNISFWLLPPALILLLGSAFVEQGAGT-GWTVYPPLSSIQAHSggAVDMAIFSLHLAGVSSILGA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 178 INVVATILNLRAPGMTLMKMPLFVWTWLITAFLLIAVMPVLAGCVTMMLMDIHFGTSFFSAAGGGDPVLFQHVFWFFGHP 257
Cdd:MTH00182 164 INFITTIFNMRAPGVTFNRLPLFVWSILITAFLLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILFQHLFWFFGHP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 258 EVYIMILPAFGAVSSIIPTFS-RKPLFGYTSMVYATASIAFLSFIVWAHHMFVVGIPLVGELFFMYATLLIAVPTGVKVF 336
Cdd:MTH00182 244 EVYILILPGFGMISQIIPTFVaKKQIFGYLGMVYAMLSIGILGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVF 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 337 NWVSTMWQGSLTFETPMLFAVAFVILFTIGGFSGLMLAIAPADFQYHDTYFVVAHFHYVLVPGAIFGIFASAYYWLPKWT 416
Cdd:MTH00182 324 SWLATIYGGTLRLDTPMLWAMGFVFLFTLGGLTGVVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIFGGFYYWFGKIT 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 417 GHMYDETLGKLHFWLSFVGMNMAFFPMHFVGLAGMPRRVPDYNLQFADFNMVSSIGAFMFGATQIFFLFIVIKCIRGGTP 496
Cdd:MTH00182 404 GYCYNELYGKIHFWLMFIGVNLTFFPQHFLGLAGFPRRYSDFADAFAGWNLVSSLGSIISIVGVVWFIYIIYDAYVREEK 483
|
490 500 510
....*....|....*....|....*....|....
gi 1236859391 497 APA---KPWDGAEGLEWSVPSPAPYHTFTTPPEV 527
Cdd:MTH00182 484 FIGwkeGTGESWASLEWVHSSPPLFHTYNELPFV 517
|
|
| COX1 |
MTH00142 |
cytochrome c oxidase subunit I; Provisional |
21-525 |
2.08e-168 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214431 Cd Length: 511 Bit Score: 486.54 E-value: 2.08e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 21 LMRWVLTTNHKDIGTMYLWFAFAMFLLGGSFAMVIRAELFQPGLQIVQPAFFNQMTTMHGLIMVFGAVMPAFVG-LANWM 99
Cdd:MTH00142 1 MMRWLFSTNHKDIGTLYFLFGAWAGMVGTGLSLLIRAELGQPGSLLGDDQLYNVIVTAHAFVMIFFMVMPVMIGgFGNWL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 100 IPLMIGAPDMALPRMNNFSFWLLPAAFLLLVSTLFTpGGGPNFGWTFYAPLST--TYAPESVTFFIFAIHLMGISSIMGA 177
Cdd:MTH00142 81 VPLMLGAPDMAFPRMNNMSFWLLPPALLLLLSSAAV-ESGAGTGWTVYPPLSSnlAHSGGSVDLAIFSLHLAGVSSILGA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 178 INVVATILNLRAPGMTLMKMPLFVWTWLITAFLLIAVMPVLAGCVTMMLMDIHFGTSFFSAAGGGDPVLFQHVFWFFGHP 257
Cdd:MTH00142 160 INFITTVINMRAGGMKFERVPLFVWSVKITAILLLLSLPVLAGAITMLLTDRNFNTSFFDPAGGGDPILYQHLFWFFGHP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 258 EVYIMILPAFGAVSSIIPTFS-RKPLFGYTSMVYATASIAFLSFIVWAHHMFVVGIPLVGELFFMYATLLIAVPTGVKVF 336
Cdd:MTH00142 240 EVYILILPGFGMISHIINHYSgKKEVFGTLGMIYAMLSIGLLGFIVWAHHMFTVGMDVDTRAYFTAATMVIAVPTGIKVF 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 337 NWVSTMWQGSLTFETPMLFAVAFVILFTIGGFSGLMLAIAPADFQYHDTYFVVAHFHYVLVPGAIFGIFASAYYWLPKWT 416
Cdd:MTH00142 320 SWLATLHGSKVKYEPPMLWALGFIFLFTVGGLTGIVLANSSLDVVLHDTYYVVAHFHYVLSMGAVFALFAGFIHWFPLFT 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 417 GHMYDETLGKLHFWLSFVGMNMAFFPMHFVGLAGMPRRVPDYNLQFADFNMVSSIGAFMFGATQIFFLFIVIKCIRGGTP 496
Cdd:MTH00142 400 GLTLNPRWLKAHFYTMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTTWNVVSSLGSMISFIAVLMFVFIVWESFVSQRL 479
|
490 500
....*....|....*....|....*....
gi 1236859391 497 APAKPWdGAEGLEWSVPSPAPYHTFTTPP 525
Cdd:MTH00142 480 VMWSSH-LSTSLEWSHRLPPDFHTYDELP 507
|
|
| COX1 |
MTH00079 |
cytochrome c oxidase subunit I; Provisional |
19-491 |
6.47e-162 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177148 Cd Length: 508 Bit Score: 469.55 E-value: 6.47e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 19 KGLMRWVLTTNHKDIGTMYLWFAFAMFLLGGSFAMVIRAELFQPGLQIVQPAFFNQMTTMHGLIMVFGAVMPAFVG-LAN 97
Cdd:MTH00079 2 GGLSVWLESSNHKDIGTLYFLFGLWSGMVGTSLSLIIRLELSKPGLLLGNGQLYNSVITAHAILMIFFMVMPSMIGgFGN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 98 WMIPLMIGAPDMALPRMNNFSFWLLPAAFLLLVSTLFTpGGGPNFGWTFYAPLSTTYAPE-SVTFFIFAIHLMGISSIMG 176
Cdd:MTH00079 82 WMLPLMLGAPDMSFPRLNNLSFWLLPTSLFLILDSCFV-DMGPGTSWTVYPPLSTLGHPGsSVDLAIFSLHCAGISSILG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 177 AINVVATILNLRAPGMTLMKMPLFVWTWLITAFLLIAVMPVLAGCVTMMLMDIHFGTSFFSAAGGGDPVLFQHVFWFFGH 256
Cdd:MTH00079 161 GINFMVTTKNLRSSSISLEHMSLFVWTVFVTVFLLVLSLPVLAGAITMLLTDRNLNTSFFDPSTGGNPLLYQHLFWFFGH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 257 PEVYIMILPAFGAVSSIIPTFS-RKPLFGYTSMVYATASIAFLSFIVWAHHMFVVGIPLVGELFFMYATLLIAVPTGVKV 335
Cdd:MTH00079 241 PEVYILILPAFGIISQSTLYLTgKKEVFGSLGMVYAILSIGLIGCVVWAHHMYTVGMDLDSRAYFTAATMVIAVPTGVKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 336 FNWVSTMWQGSLTFETPMLFAVAFVILFTIGGFSGLMLAIAPADFQYHDTYFVVAHFHYVLVPGAIFGIFASAYYWLPKW 415
Cdd:MTH00079 321 FSWLATLFGMKMKFQPLLLWVLGFIFLFTIGGLTGVILSNSSLDIILHDTYYVVSHFHYVLSLGAVFGIFTGISLWWPFM 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1236859391 416 TGHMYDETLGKLHFWLSFVGMNMAFFPMHFVGLAGMPRRVPDYNLQFADFNMVSSIGAFMFGATQIFFLFIVIKCI 491
Cdd:MTH00079 401 TGIVYDKLMMSAVFFLMFVGVNLTFFPLHFAGLHGMPRKYLDYPDVYSVWNVISSYGSMISVFALFLFIYVLLESF 476
|
|
| COX1 |
MTH00183 |
cytochrome c oxidase subunit I; Provisional |
21-528 |
5.07e-159 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177234 Cd Length: 516 Bit Score: 462.47 E-value: 5.07e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 21 LMRWVLTTNHKDIGTMYLWFAFAMFLLGGSFAMVIRAELFQPGLQIVQPAFFNQMTTMHGLIMVFGAVMPAFVG-LANWM 99
Cdd:MTH00183 3 ITRWFFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGALLGDDQIYNVIVTAHAFVMIFFMVMPIMIGgFGNWL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 100 IPLMIGAPDMALPRMNNFSFWLLPAAFLLLVSTLFTPGGGPNfGWTFYAPLS--TTYAPESVTFFIFAIHLMGISSIMGA 177
Cdd:MTH00183 83 IPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGT-GWTVYPPLAgnLAHAGASVDLTIFSLHLAGVSSILGA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 178 INVVATILNLRAPGMTLMKMPLFVWTWLITAFLLIAVMPVLAGCVTMMLMDIHFGTSFFSAAGGGDPVLFQHVFWFFGHP 257
Cdd:MTH00183 162 INFITTIINMKPPAISQYQTPLFVWAVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 258 EVYIMILPAFGAVSSIIPTFS-RKPLFGYTSMVYATASIAFLSFIVWAHHMFVVGIPLVGELFFMYATLLIAVPTGVKVF 336
Cdd:MTH00183 242 EVYILILPGFGMISHIVAYYSgKKEPFGYMGMVWAMMAIGLLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVF 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 337 NWVSTMWQGSLTFETPMLFAVAFVILFTIGGFSGLMLAIAPADFQYHDTYFVVAHFHYVLVPGAIFGIFASAYYWLPKWT 416
Cdd:MTH00183 322 SWLATLHGGSIKWETPLLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMAAFVHWFPLFS 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 417 GHMYDETLGKLHFWLSFVGMNMAFFPMHFVGLAGMPRRVPDYNLQFADFNMVSSIGAFMFGATQIFFLFIVIKCIRGGTP 496
Cdd:MTH00183 402 GYTLHSTWTKIHFGVMFVGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMFLFILWEAFAAKRE 481
|
490 500 510
....*....|....*....|....*....|..
gi 1236859391 497 APAKPWdGAEGLEWSVPSPAPYHTFTTPPEVK 528
Cdd:MTH00183 482 VLSVEL-TSTNVEWLHGCPPPYHTFEEPAFVQ 512
|
|
| COX1 |
MTH00037 |
cytochrome c oxidase subunit I; Provisional |
21-525 |
6.45e-158 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177112 Cd Length: 517 Bit Score: 459.68 E-value: 6.45e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 21 LMRWVLTTNHKDIGTMYLWFAFAMFLLGGSFAMVIRAELFQPGLQIVQPAFFNQMTTMHGLIMVFGAVMPAFVG-LANWM 99
Cdd:MTH00037 3 LSRWLFSTNHKDIGTLYLIFGAWAGMVGTAMSVIIRTELAQPGSLLQDDQIYNVIVTAHALVMIFFMVMPIMIGgFGNWL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 100 IPLMIGAPDMALPRMNNFSFWLLPAAFLLLVSTLFTPGGGPNfGWTFYAPLS--TTYAPESVTFFIFAIHLMGISSIMGA 177
Cdd:MTH00037 83 IPLMIGAPDMAFPRMNNMSFWLIPPSFLLLLASAGVESGAGT-GWTIYPPLSsnIAHAGGSVDLAIFSLHLAGASSILAS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 178 INVVATILNLRAPGMTLMKMPLFVWTWLITAFLLIAVMPVLAGCVTMMLMDIHFGTSFFSAAGGGDPVLFQHVFWFFGHP 257
Cdd:MTH00037 162 INFITTIINMRTPGMTFDRLPLFVWSVFITAFLLLLSLPVLAGAITMLLTDRNINTTFFDPAGGGDPILFQHLFWFFGHP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 258 EVYIMILPAFGAVSSIIPTFSRKPL-FGYTSMVYATASIAFLSFIVWAHHMFVVGIPLVGELFFMYATLLIAVPTGVKVF 336
Cdd:MTH00037 242 EVYILILPGFGMISHVIAHYSGKQEpFGYLGMVYAMIAIGILGFLVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVF 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 337 NWVSTMWQGSLTFETPMLFAVAFVILFTIGGFSGLMLAIAPADFQYHDTYFVVAHFHYVLVPGAIFGIFASAYYWLPKWT 416
Cdd:MTH00037 322 SWMATLQGSNLRWETPLLWALGFVFLFTIGGLTGIVLANSSIDVVLHDTYYVVAHFHYVLSMGAVFAIFAGFTHWFPLFS 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 417 GHMYDETLGKLHFWLSFVGMNMAFFPMHFVGLAGMPRRVPDYNLQFADFNMVSSIGAFMFGATQIFFLFIVIKCIrGGTP 496
Cdd:MTH00037 402 GVSLHPLWSKVHFFLMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSTISLVATLFFLFLIWEAF-ASQR 480
|
490 500 510
....*....|....*....|....*....|
gi 1236859391 497 APAKPWDGAEGLEWSVPS-PAPYHTFTTPP 525
Cdd:MTH00037 481 EVISPEFSSSSLEWQYSSfPPSHHTFDETP 510
|
|
| COX1 |
MTH00007 |
cytochrome c oxidase subunit I; Validated |
22-519 |
1.91e-157 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 133649 Cd Length: 511 Bit Score: 458.60 E-value: 1.91e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 22 MRWVLTTNHKDIGTMYLWFAFAMFLLGGSFAMVIRAELFQPGLQIVQPAFFNQMTTMHGLIMVFGAVMPAFVG-LANWMI 100
Cdd:MTH00007 1 MRWLYSTNHKDIGTLYFILGVWGGLLGTSMSLLIRIELGQPGAFLGSDQLYNTIVTAHAFLMIFFLVMPVFIGgFGNWLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 101 PLMIGAPDMALPRMNNFSFWLLPAAFLLLVSTLFTpGGGPNFGWTFYAPLSTT--YAPESVTFFIFAIHLMGISSIMGAI 178
Cdd:MTH00007 81 PLMLGAPDMAFPRLNNMSFWLLPPALILLVSSAAV-EKGVGTGWTVYPPLASNlaHAGPSVDLAIFSLHLAGVSSILGAI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 179 NVVATILNLRAPGMTLMKMPLFVWTWLITAFLLIAVMPVLAGCVTMMLMDIHFGTSFFSAAGGGDPVLFQHVFWFFGHPE 258
Cdd:MTH00007 160 NFITTVINMRWKGLRLERIPLFVWAVVITVVLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 259 VYIMILPAFGAVSSIIPTFSRKP-LFGYTSMVYATASIAFLSFIVWAHHMFVVGIPLVGELFFMYATLLIAVPTGVKVFN 337
Cdd:MTH00007 240 VYILILPGFGAISHIVTHYAGKLePFGTLGMIYAMLGIGVLGFIVWAHHMFTVGMDVDTRAYFTAATMIIAVPTGIKVFS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 338 WVSTMWQGSLTFETPMLFAVAFVILFTIGGFSGLMLAIAPADFQYHDTYFVVAHFHYVLVPGAIFGIFASAYYWLPKWTG 417
Cdd:MTH00007 320 WLATIHGSPIKYETPMLWALGFIFLFTTGGLTGIVLSNSSLDIILHDTYYVVAHFHYVLSMGAVFAIFAAFNHWFPLFTG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 418 HMYDETLGKLHFWLSFVGMNMAFFPMHFVGLAGMPRRVPDYNLQFADFNMVSSIGAFMFGATQIFFLFIVIKCIRGGTPA 497
Cdd:MTH00007 400 LTLHDRWAKAHFFLMFLGVNLTFFPQHFLGLSGMPRRYSDYPDAYTKWNVVSSFGSMLSFVALLLFIFILWEAFSAQRGV 479
|
490 500
....*....|....*....|..
gi 1236859391 498 PAKPWDGAeGLEWSVPSPAPYH 519
Cdd:MTH00007 480 IASPHMSS-SLEWQDTLPLDFH 500
|
|
| COX1 |
MTH00103 |
cytochrome c oxidase subunit I; Validated |
23-528 |
1.31e-156 |
|
cytochrome c oxidase subunit I; Validated
Pssm-ID: 177165 Cd Length: 513 Bit Score: 456.27 E-value: 1.31e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 23 RWVLTTNHKDIGTMYLWFAFAMFLLGGSFAMVIRAELFQPGLQIVQPAFFNQMTTMHGLIMVFGAVMPAFVG-LANWMIP 101
Cdd:MTH00103 5 RWLFSTNHKDIGTLYLLFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGgFGNWLVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 102 LMIGAPDMALPRMNNFSFWLLPAAFLLLVSTLFTPGGGPNfGWTFYAPLS--TTYAPESVTFFIFAIHLMGISSIMGAIN 179
Cdd:MTH00103 85 LMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGT-GWTVYPPLAgnLAHAGASVDLTIFSLHLAGVSSILGAIN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 180 VVATILNLRAPGMTLMKMPLFVWTWLITAFLLIAVMPVLAGCVTMMLMDIHFGTSFFSAAGGGDPVLFQHVFWFFGHPEV 259
Cdd:MTH00103 164 FITTIINMKPPAMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 260 YIMILPAFGAVSSIIPTFS-RKPLFGYTSMVYATASIAFLSFIVWAHHMFVVGIPLVGELFFMYATLLIAVPTGVKVFNW 338
Cdd:MTH00103 244 YILILPGFGMISHIVTYYSgKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVDTRAYFTSATMIIAIPTGVKVFSW 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 339 VSTMWQGSLTFETPMLFAVAFVILFTIGGFSGLMLAIAPADFQYHDTYFVVAHFHYVLVPGAIFGIFASAYYWLPKWTGH 418
Cdd:MTH00103 324 LATLHGGNIKWSPAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGY 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 419 MYDETLGKLHFWLSFVGMNMAFFPMHFVGLAGMPRRVPDYNLQFADFNMVSSIGAFMFGATQIFFLFIVIKCIRGGTPAP 498
Cdd:MTH00103 404 TLNDTWAKIHFTIMFVGVNMTFFPQHFLGLSGMPRRYSDYPDAYTTWNTVSSMGSFISLTAVMLMIFMIWEAFASKREVL 483
|
490 500 510
....*....|....*....|....*....|
gi 1236859391 499 AKPWDgAEGLEWSVPSPAPYHTFTTPPEVK 528
Cdd:MTH00103 484 TVELT-TTNLEWLHGCPPPYHTFEEPTYVK 512
|
|
| COX1 |
MTH00077 |
cytochrome c oxidase subunit I; Provisional |
21-524 |
2.79e-156 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 214419 Cd Length: 514 Bit Score: 455.55 E-value: 2.79e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 21 LMRWVLTTNHKDIGTMYLWFAFAMFLLGGSFAMVIRAELFQPGLQIVQPAFFNQMTTMHGLIMVFGAVMPAFVG-LANWM 99
Cdd:MTH00077 3 ITRWLFSTNHKDIGTLYLVFGAWAGMVGTALSLLIRAELSQPGTLLGDDQIYNVIVTAHAFVMIFFMVMPIMIGgFGNWL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 100 IPLMIGAPDMALPRMNNFSFWLLPAAFLLLVSTLFTPGGGPNfGWTFYAPLS--TTYAPESVTFFIFAIHLMGISSIMGA 177
Cdd:MTH00077 83 VPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSGVEAGAGT-GWTVYPPLAgnLAHAGASVDLTIFSLHLAGVSSILGA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 178 INVVATILNLRAPGMTLMKMPLFVWTWLITAFLLIAVMPVLAGCVTMMLMDIHFGTSFFSAAGGGDPVLFQHVFWFFGHP 257
Cdd:MTH00077 162 INFITTSINMKPPSMSQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPVLYQHLFWFFGHP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 258 EVYIMILPAFGAVSSIIPTFS-RKPLFGYTSMVYATASIAFLSFIVWAHHMFVVGIPLVGELFFMYATLLIAVPTGVKVF 336
Cdd:MTH00077 242 EVYILILPGFGMISHIVTYYSaKKEPFGYMGMVWAMMSIGLLGFIVWAHHMFTVDLNVDTRAYFTSATMIIAIPTGVKVF 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 337 NWVSTMWQGSLTFETPMLFAVAFVILFTIGGFSGLMLAIAPADFQYHDTYFVVAHFHYVLVPGAIFGIFASAYYWLPKWT 416
Cdd:MTH00077 322 SWLATMHGGAIKWDAAMLWALGFIFLFTVGGLTGIVLANSSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFS 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 417 GHMYDETLGKLHFWLSFVGMNMAFFPMHFVGLAGMPRRVPDYNLQFADFNMVSSIGAFMFGATQIFFLFIVIKCIrggtp 496
Cdd:MTH00077 402 GYTLHSTWSKIHFGVMFIGVNLTFFPQHFLGLAGMPRRYSDYPDAYTLWNTVSSIGSLISLVAVIMMMFIIWEAF----- 476
|
490 500 510
....*....|....*....|....*....|..
gi 1236859391 497 APAKPWDGAE----GLEWSVPSPAPYHTFTTP 524
Cdd:MTH00077 477 SSKREVLTTEltstNIEWLHGCPPPYHTFEEP 508
|
|
| COX1 |
pfam00115 |
Cytochrome C and Quinol oxidase polypeptide I; Cytochrome c oxidase (E.C:7.1.1.9) is a key ... |
32-475 |
1.25e-151 |
|
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: 440.47 E-value: 1.25e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 32 DIGTMYLWFAFAMFLLGGSFAMVIRAELFQPGLQIVQPAFFNQMTTMHGLIMVFGAVMPAFVGLANWMIPLMIGAPDMAL 111
Cdd:pfam00115 1 RIGLLYLVTALVWFLVGGLLGLLIRLQLAFPGLNFLSPLTYNQLRTLHGNLMIFWFATPFLFGFGNYLVPLMIGARDMAF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 112 PRMNNFSFWLLPAAFLLLVSTLftpgGGPNFGWTFYAPLSttyapeSVTFFIFAIHLMGISSIMGAINVVATILNLRAPG 191
Cdd:pfam00115 81 PRLNALSFWLVVLGAVLLLASF----GGATTGWTEYPPLV------GVDLWYIGLLLAGVSSLLGAINFIVTILKRRAPG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 192 MTlMKMPLFVWTWLITAFLLIAVMPVLAGCVTMMLMDIHFGtsffsaAGGGDPVLFQHVFWFFGHPEVYIMILPAFGAVS 271
Cdd:pfam00115 151 MT-LRMPLFVWAILATAILILLAFPVLAAALLLLLLDRSLG------AGGGDPLLDQHLFWWFGHPEVYILILPAFGIIY 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 272 SIIPTFSRKPLFGYTSMVYATASIAFLSFIVWAHHMFVVGIPLVGELFFMYATLLIAVPTGVKVFNWVSTMWQGSLTF-E 350
Cdd:pfam00115 224 YILPKFAGRPLFGYKLSVLAFWLIAFLGFLVWAHHLFTTGLPPWLQALFSVFSMLIAVPSGVKVFNWLATLWGGWIRFrT 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 351 TPMLFAVAFVILFTIGGFSGLMLAIAPADFQYHDTYFVVAHFHYVLVPGAIFGIFASAYYWLPKWTGHMYDETLGKLHFW 430
Cdd:pfam00115 304 TPMLFFLGFAFLFIIGGLTGVMLALPPVNYYVHDTYFVVAHFHYVLFGGVVFALFGGIYYWLPKLTGRMYSEKLGKLHFW 383
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1236859391 431 LSFVGMNMAFFPMHFVGLAGMPRRVPDYNL----QFADFNMVSSIGAFM 475
Cdd:pfam00115 384 LLFIGFNLTFFPMHILGLLGMPRRYAPPFIetvpAFQPLNWIRTIGGVL 432
|
|
| COX1 |
MTH00026 |
cytochrome c oxidase subunit I; Provisional |
21-527 |
3.24e-145 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 164599 Cd Length: 534 Bit Score: 427.89 E-value: 3.24e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 21 LMRWVLTTNHKDIGTMYLWFAFAMFLLGGSFAMVIRAELFQPGLQIVQPAFFNQMTTMHGLIMVFGAVMPAFVG-LANWM 99
Cdd:MTH00026 4 FVRWFFSCNHKDIGSLYLVFGALSGAIGTAFSMLIRLELSSPGSMLGDDHLYNVIVTAHAFVMIFFLVMPTMIGgFGNWF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 100 IPLMIGAPDMALPRMNNFSFWLLPAA-FLLLVSTLFTPGGGPnfGWTFYAPLSTTYAPE--SVTFFIFAIHLMGISSIMG 176
Cdd:MTH00026 84 VPLMIGAPDMAFPRLNNISFWLLPPAlFLLLGSSLVEQGAGT--GWTVYPPLASIQAHSggSVDMAIFSLHLAGLSSILG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 177 AINVVATILNLRAPGMTLMKMPLFVWTWLITAFLLIAVMPVLAGCVTMMLMDIHFGTSFFSAAGGGDPVLFQHVFWFFGH 256
Cdd:MTH00026 162 AMNFITTVMNMRTPGMTMSRIPLFVWSVFITAILLLLSLPVLAGAITMLLTDRNFNTTFFDPAGGGDPILYQHLFWFFGH 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 257 PEVYIMILPAFGAVSSIIPTFS-RKPLFGYTSMVYATASIAFLSFIVWAHHMFVVGIPLVGELFFMYATLLIAVPTGVKV 335
Cdd:MTH00026 242 PEVYILILPGFGIISQILSLFSyKKQIFGYLGMVYAMLAIGVLGFIVWAHHMYVVGMDVDTRAYFTAATMIIAVPTGIKI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 336 FNWVSTMWQG--SLTFETPMLFAVAFVILFTIGGFSGLMLAIAPADFQYHDTYFVVAHFHYVLVPGAIFGIFASAYYWLP 413
Cdd:MTH00026 322 FSWLATVSGSgrNLIFTTPMAWALGFIFLFTIGGLTGIVLSNSSLDILLHDTYYVVAHFHFVLSMGAVFAIFGGFYLWFG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 414 KWTGHMYDETLGKLHFWLSFVGMNMAFFPMHFVGLAGMPRRVPDYNLQFADFNMVSSIGAFMFGATQIFFLFIVIKCIRG 493
Cdd:MTH00026 402 KITGYAYKDIYGLIHFWLMFIGVNITFFPQHFLGLAGLPRRYADYPDNFEDFNQISSFGSIISIIAVIWFIVVIFDAYYR 481
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1236859391 494 GTP--------APAKPWDGA----EGLEWSVPSPAPYHTFTTPPEV 527
Cdd:MTH00026 482 EEPfdinimakGPLIPFSCQpahfDTLEWSLTSPPEHHTYNELPYI 527
|
|
| COX1 |
MTH00048 |
cytochrome c oxidase subunit I; Provisional |
20-487 |
4.16e-129 |
|
cytochrome c oxidase subunit I; Provisional
Pssm-ID: 177123 Cd Length: 511 Bit Score: 385.96 E-value: 4.16e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 20 GLMRWVLTTNHKDIGTMYLWFAFAMFLLGGSFAMVIRAELFQPGLQIVQPAFFNQMTTMHGLIMVFGAVMPAFVG-LANW 98
Cdd:MTH00048 3 SLLSWLFTLDHKRIGVIYTLLGVWSGFVGLSLSLLIRLNFLDPYYNVISLDVYNFLITNHGIIMIFFFLMPVLIGgFGNY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 99 MIPLMIGAPDMALPRMNNFSFWLL-PAAFLLLVSTLFtpggGPNFGWTFYAPLSTTYAPES--VTFFIFAIHLMGISSIM 175
Cdd:MTH00048 83 LLPLLLGLSDLNLPRLNALSAWLLvPSIVFLLLSMCL----GAGVGWTFYPPLSSSLFSSSwgVDFLMFSLHLAGVSSLF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 176 GAINVVATILNLRAPGMTLmKMPLFVWTWLITAFLLIAVMPVLAGCVTMMLMDIHFGTSFFSAAGGGDPVLFQHVFWFFG 255
Cdd:MTH00048 159 GSINFICTIYSAFMTNVFS-RTSIILWSYLFTSILLLLSLPVLAAAITMLLFDRNFGSAFFDPLGGGDPVLFQHMFWFFG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 256 HPEVYIMILPAFGAVSSIIPTFSRKP-LFGYTSMVYATASIAFLSFIVWAHHMFVVGIPLVGELFFMYATLLIAVPTGVK 334
Cdd:MTH00048 238 HPEVYVLILPGFGIISHICLSLSNNDdPFGYYGLVFAMFSIVCLGSVVWAHHMFTVGLDVKTAVFFSSVTMIIGVPTGIK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 335 VFNWVSTMWQGSLTFETPML-FAVAFVILFTIGGFSGLMLAIAPADFQYHDTYFVVAHFHYVLVPGAIFGIFASAYYWLP 413
Cdd:MTH00048 318 VFSWLYMLLNSRVRKSDPVVwWVVSFIVLFTIGGVTGIVLSASVLDNVLHDTWFVVAHFHYVLSLGSYSSVVIMFIWWWP 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1236859391 414 KWTGHMYDETLGKLHFWLSFVGMNMAFFPMHFVGLAGMPRRVPDYNLQFADFNMVSSIGAFMFGATQIFFLFIV 487
Cdd:MTH00048 398 LITGLSLNKYLLQCHCIISMIGFNLCFFPMHYFGLCGLPRRVCVYEPSYYWINVVCTVGSFISAFSGCFFVFIL 471
|
|
| PRK15017 |
PRK15017 |
cytochrome o ubiquinol oxidase subunit I; Provisional |
24-527 |
4.69e-121 |
|
cytochrome o ubiquinol oxidase subunit I; Provisional
Pssm-ID: 184978 Cd Length: 663 Bit Score: 370.42 E-value: 4.69e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 24 WVLTTNHKDIGTMYLWFAFAMFLLGGSFAMVIRAE--LFQPG-LQIVQPAFFNQMTTMHGLIMVFGAVMPAFVGLANWMI 100
Cdd:PRK15017 48 WLTSVDHKRLGIMYIIVAIVMLLRGFADAIMMRSQqaLASAGeAGFLPPHHYDQIFTAHGVIMIFFVAMPFVIGLMNLVV 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 101 PLMIGAPDMALPRMNNFSFWLlPAAFLLLVSTLFTPGGGPNFGWTFYAPLS-TTYAPE-SVTFFIFAIHLMGISSIMGAI 178
Cdd:PRK15017 128 PLQIGARDVAFPFLNNLSFWF-TVVGVILVNVSLGVGEFAQTGWLAYPPLSgIEYSPGvGVDYWIWSLQLSGIGTTLTGI 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 179 NVVATILNLRAPGMTLMKMPLFVWTWLITAFLLIAVMPVLAGCVTMMLMDIHFGTSFFSAAGGGDPVLFQHVFWFFGHPE 258
Cdd:PRK15017 207 NFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWGHPE 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 259 VYIMILPAFGAVSSIIPTFSRKPLFGYTSMVYATASIAFLSFIVWAHHMFVVGIPLVGELFFMYATLLIAVPTGVKVFNW 338
Cdd:PRK15017 287 VYILILPVFGVFSEIAATFSRKRLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVKIFNW 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 339 VSTMWQGSLTFETPMLFAVAFVILFTIGGFSGLMLAIAPADFQYHDTYFVVAHFHYVLVPGAIFGIFASAYYWLPKWTGH 418
Cdd:PRK15017 367 LFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYWWPKAFGF 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 419 MYDETLGKLHFWLSFVGMNMAFFPMHFVGLAGMPRRVP-DYNLQFADFNMVSSIGAFMFG---ATQIFFLFIVIKCIRGG 494
Cdd:PRK15017 447 KLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMTRRLSqQIDPQFHTMLMIAASGAALIAlgiLCQVIQMYVSIRDRDQN 526
|
490 500 510
....*....|....*....|....*....|...
gi 1236859391 495 TPAPAKPWdGAEGLEWSVPSPAPYHTFTTPPEV 527
Cdd:PRK15017 527 RDLTGDPW-GGRTLEWATSSPPPFYNFAVVPHV 558
|
|
| ba3-like_Oxidase_I |
cd01660 |
ba3-like heme-copper oxidase subunit I. The ba3 family of heme-copper oxidases are ... |
37-489 |
7.38e-28 |
|
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: 116.23 E-value: 7.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 37 YLWFAFAMFLLGGSFAMV---IRAELFQpglQIVQPAFFNQMTTMHGLIMVFgaVMPAF--VGLANWMIPLMIGAPDMAl 111
Cdd:cd01660 9 HFVVAFLALLLGGLFGLLqvlVRTGVFP---LPSSGILYYQGLTLHGVLLAI--VFTTFfiMGFFYAIVARALLRSLFN- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 112 PRMNNFSFWLLPAAFLLLVSTLFTpgGGPNFGWTFYAPLSTtyapeSVTFFIFAIHLMGISSIMGAINVVATILNLRA-P 190
Cdd:cd01660 83 RRLAWAGFWLMVIGTVMAAVPILL--GQASVLYTFYPPLQA-----HPLFYIGAALVVVGSWISGFAMFVTLWRWKKAnP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 191 GMtlmKMPLFVWTWLITAFLLIAVMPVLAGCVTMMLMDIHFGTsffsaAGGGDPVLFQHVFWFFGHPEVYIMILPAFGAV 270
Cdd:cd01660 156 GK---KVPLATFMVVTTMILWLVASLGVALEVLFQLLPWSLGL-----VDTVDVLLSRTLFWWFGHPLVYFWLLPAYIAW 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 271 SSIIPTFSRKPLFGYTsmvyaTASIAFLSFIVWA-----HHMFV-VGIPLVGELFFMYATLLIAVPTGVKVFNWVSTM-- 342
Cdd:cd01660 228 YTILPKIAGGKLFSDP-----LARLAFILFLLFStpvgfHHQFAdPGIGPGWKFIHMVLTFMVALPSLLTAFTVFASLei 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 343 ------------WQGSLTFETPMLFAVAF-VILFTIGGFSGLMLAIAPADFQYHDTYFVVAHFHYVLVPGAIFGIFASAY 409
Cdd:cd01660 303 agrlrggkglfgWIRALPWGDPMFLALFLaMLMFIPGGAGGIINASYQLNYVVHNTAWVPGHFHLTVGGAVALTFMAVAY 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 410 YWLPKWTGH-MYDETLGKLHFWLSFVGMNMAFFPMHFVGLAGMPRRV--PDYN-----LQFADFNMVSSIGAFMFGATQI 481
Cdd:cd01660 383 WLVPHLTGReLAAKRLALAQPWLWFVGMTIMSTAMHVAGLLGAPRRTaeAQYGglpaaGEWAPYQQLMAIGGTILFVSGA 462
|
....*...
gi 1236859391 482 FFLFIVIK 489
Cdd:cd01660 463 LFLYILFR 470
|
|
| cbb3_Oxidase_I |
cd01661 |
Cytochrome cbb3 oxidase subunit I. Cytochrome cbb3 oxidase, the terminal oxidase in the ... |
199-448 |
8.54e-07 |
|
Cytochrome cbb3 oxidase subunit I. Cytochrome cbb3 oxidase, the terminal oxidase in the respiratory chains of proteobacteria, is a multi-chain transmembrane protein located in the cell membrane. Like other cytochrome oxidases, it catalyzes the reduction of O2 and simultaneously pumps protons across the membrane. Found mainly in proteobacteria, cbb3 is believed to be a modern enzyme that has evolved independently to perform a specialized function in microaerobic energy metabolism. 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 to the binuclear center. The cbb3 operon contains four genes (ccoNOQP or fixNOQP), with ccoN coding for subunit I. Instead of a CuA-containing subunit II analogous to other cytochrome oxidases, cbb3 utilizes subunits ccoO and ccoP, which contain one and two hemes, respectively, to transfer electrons to the binuclear center. The fourth subunit (ccoQ) has been shown to protect the core complex from proteolytic degradation by serine proteases. 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. The polar residues that form the D- and K-pathways in subunit I of other cytochrome c and ubiquinol oxidases are absent in cbb3. The proton pathways remain undefined. A pathway for the transfer of pumped protons beyond the binuclear center also remains undefined. It is believed that electrons are passed from cytochrome c (the electron donor) to the low-spin heme via ccoP and ccoO, respectively, and directly from the low-spin heme to the binuclear center.
Pssm-ID: 238831 Cd Length: 493 Bit Score: 51.59 E-value: 8.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 199 LFVWTWLITAFLLiaVMPVLAGCVTMMLMDIHFGTSFFSAAGGGDPVLFQhvfWFFGHPEVYIMILPAF-GAVSSIIPTF 277
Cdd:cd01661 190 IYVANWYYLAFIV--TVAVLHIVNNLAVPVSWFGSKSYSAHAGVQDATTQ---WWYGHNAVGFFLTAGFlAMMYYFLPKI 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 278 SRKPLFGYTSMVYATASIAFLSFIVWAHHMFVVGIPLVGELFFMYATLLIAVPTGVKVFNWVSTM---WQGSLTFETP-- 352
Cdd:cd01661 265 AERPVYSYRLSIIGFWALAFLYIWAGPHHLHYTALPDWLQTLGMVFSVMLWMPSWAGMINGLLTLrgaWDKLRTDPTLrf 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 353 MLFAVAFvilFTIGGFSGLMLAIAPADFQYHDTYFVVAHFHYVLVPGAIFGIFASAYYWLPK-WTGHMYDETLGKLHFWL 431
Cdd:cd01661 345 MVVGGAF---YGLSTFEGSFMAIRAVNSLSHYTDWTVGHVHLGALGWVGFITFGAIYFLVPRiWKREWPSPKLVEWHFWL 421
|
250
....*....|....*..
gi 1236859391 432 SFVGMNMAFFPMHFVGL 448
Cdd:cd01661 422 ATIGIVIYFVAMWISGI 438
|
|
| PRK14485 |
PRK14485 |
putative bifunctional cbb3-type cytochrome c oxidase subunit I/II; Provisional |
177-496 |
9.45e-07 |
|
putative bifunctional cbb3-type cytochrome c oxidase subunit I/II; Provisional
Pssm-ID: 184703 [Multi-domain] Cd Length: 712 Bit Score: 51.62 E-value: 9.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 177 AINVVATILNLRapgmtlmKMPLFVWTWL-ITAFLLIAVMPVlagcVTMMLMDIHFGTSFFSAAGGGDPVlfqhVFWFFG 255
Cdd:PRK14485 141 GVNFFGTLIKRR-------ERHLYVAIWFyIATIVTVAVLHI----VNSLELPVSALKSYSVYAGVQDAL----VQWWYG 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 256 HPEV-YIMILPAFGAVSSIIPTFSRKPLFGYTSMVYATASIAFLsfIVWA--HHMFVVGIP-LVGELFFMYATLLIAVPT 331
Cdd:PRK14485 206 HNAVaFFLTTPFLGLMYYFVPKAANRPVYSYRLSIIHFWSLIFI--YIWAgpHHLLYTALPdWAQNLGVVFSVMLIAPSW 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 332 GvkvfnwvsTMWQGSLTF--------ETPML-FAVAFVILFTIGGFSGLMLAIAPADFQYHDTYFVVAHFHYvlvpGAI- 401
Cdd:PRK14485 284 G--------GMINGLLTLrgawdkvrTDPVLkFFVVAITFYGMATFEGPMLSLKNVNAIAHYTDWIIAHVHV----GALg 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1236859391 402 ---FGIFASAYYWLPK-WTGHMYDETLGKLHFWLSFVGMNMAFFPMHFVGL--AGMPRRV-PDYNLQFADF--------- 465
Cdd:PRK14485 352 wngFLTFGMLYWLLPRlFKTKLYSTKLANFHFWIGTLGIILYALPMYVAGFtqGLMWKEFtPDGTLAYPNFletvlairp 431
|
330 340 350
....*....|....*....|....*....|..
gi 1236859391 466 -NMVSSIGAFMFGATQIFFLFIVIKCIRGGTP 496
Cdd:PRK14485 432 mYWMRAIGGSLYLVGMIVMAYNIIKTVRAGSA 463
|
|
| |
