|
Name |
Accession |
Description |
Interval |
E-value |
| MMPL |
COG1033 |
Predicted exporter protein, RND superfamily [General function prediction only]; |
448-604 |
1.63e-11 |
|
Predicted exporter protein, RND superfamily [General function prediction only];
Pssm-ID: 440656 [Multi-domain] Cd Length: 767 Bit Score: 69.12 E-value: 1.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564342364 448 LLSLVIIFFGMSLYLRSLFITFMSLLGVLGSLMVAFFLyhvafrMAYF--PFvNLASLLLLS---GVCVNYTLIFFDlwR 522
Cdd:COG1033 612 LLALLLIFLLLLLAFRSLRLGLISLIPNLLPILLTFGL------MGLLgiPL-NIATAVVASialGIGVDYTIHFLS--R 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564342364 523 LSRGQVPSGGLAHRVGRTMHHFGYLLLVSGLTTSAAFYGSYLSRLPTVRCFALFMGTAVLVHMGLTLLWLPATVVLHERY 602
Cdd:COG1033 683 YREERRKGGDLEEAIRRALRTTGKAILFTSLTLAAGFGVLLFSSFPPLADFGLLLALGLLVALLAALLLLPALLLLLDPR 762
|
..
gi 564342364 603 LA 604
Cdd:COG1033 763 IA 764
|
|
| MMPL |
pfam03176 |
MMPL family; Members of this family are putative integral membrane proteins from bacteria. ... |
448-598 |
3.42e-07 |
|
MMPL family; Members of this family are putative integral membrane proteins from bacteria. Several of the members are mycobacterial proteins. Many of the proteins contain two copies of this aligned region. The function of these proteins is not known, although it has been suggested that they may be involved in lipid transport.
Pssm-ID: 308676 [Multi-domain] Cd Length: 332 Bit Score: 53.83 E-value: 3.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564342364 448 LLSLVIIFFGMSLYLRSLFITFMSLLGVLGSLMVAF-----FLYHVAFRMAYFPfVNLASLLLLsGVCVNYTLIFFDLWR 522
Cdd:pfam03176 149 AVTLVVIFIILLIVYRSVVAALLPLLTVGLSLGAAQglvaiLAHILGIGLSTFA-LNLLVVLLI-AVGTDYALFLVSRYR 226
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564342364 523 LSRGQVPSGGLAhrVGRTMHHFGYLLLVSGLTTSAAFYGSYLSRLPTVRCFALFMGTAVLVHMGLTLLWLPATVVL 598
Cdd:pfam03176 227 EELRAGEDREEA--VIRAVRGTGKVVTAAGLTVAIAMLALSFARLPVFAQVGPTIAIGVLVDVLAALTLLPALLAL 300
|
|
| 2A060601 |
TIGR00917 |
Niemann-Pick C type protein family; The model describes Niemann-Pick C type protein in ... |
448-601 |
1.93e-06 |
|
Niemann-Pick C type protein family; The model describes Niemann-Pick C type protein in eukaryotes. The defective protein has been associated with Niemann-Pick disease which is described in humans as autosomal recessive lipidosis. It is characterized by the lysosomal accumulation of unestrified cholesterol. It is an integral membrane protein, which indicates that this protein is most likely involved in cholesterol transport or acts as some component of cholesterol homeostasis. [Transport and binding proteins, Other]
Pssm-ID: 273337 [Multi-domain] Cd Length: 1205 Bit Score: 52.60 E-value: 1.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564342364 448 LLSLVIIFFGMSLYL------RSLFITFMSLLGVLGSLMVAFflyHVAFRMAYFPFVNLASLLLLS----------GVCV 511
Cdd:TIGR00917 578 AISYLVMFAYISLTLgdsprlKSLYVTSKVLLGLSGILIVML---SVLGSVGVFSAVGLKSTLIIMevipflvlavGVDN 654
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564342364 512 NYTLI--FFDLWRLsRGQVPSGG-----LAHRVGRTMHHFGYLLLVSGLTTSAAFYGSYLSRLPTVRCFALFMGTAVLVH 584
Cdd:TIGR00917 655 IFILVffYFYLEYF-YRQVGVDNeqeltLERRLSRALMEVGPSITLASLSEILAFALGALIKMPAVRVFSMFAVLAVFLD 733
|
170
....*....|....*..
gi 564342364 585 MGLTLLWLPATVVLHER 601
Cdd:TIGR00917 734 FLLQITAFVALLVLDFK 750
|
|
| BI-1-like_bacterial |
cd10432 |
Bacterial BAX inhibitor (BI)-1/YccA-like proteins; This family is comprised of bacterial ... |
377-526 |
2.40e-04 |
|
Bacterial BAX inhibitor (BI)-1/YccA-like proteins; This family is comprised of bacterial relatives of the mammalian members of the BAX inhibitor (BI)-1 like family of small transmembrane proteins, which have been shown to have an antiapoptotic effect either by stimulating the antiapoptotic function of Bcl-2, a well-characterized oncogene, or by inhibiting the proapoptotic effect of Bax, another member of the Bcl-2 family. In plants, BI-1 like proteins play a role in pathogen resistance. A characterized prokaryotic member, Escherichia coli YccA, has been shown to interact with ATP-dependent protease FtsH, which degrades abnormal membrane proteins as part of a quality control mechanism to keep the integrity of biological membranes.
Pssm-ID: 198414 Cd Length: 211 Bit Score: 44.09 E-value: 2.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564342364 377 SPQTADYQVPSLKFALLFLPIIktsslLDIYLDGLGDPIKVSDN------YTSISGMDLGLkprLLKYYLAEDTMYPLLS 450
Cdd:cd10432 30 TPALLLIAGSPLMWVLLIAELA-----LVFGLSFRINKMSVATAlplffaFAALTGLTLSP---ILLVYTGASIAQAFFT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564342364 451 LVIIFFGMSLY-------LRSL-FITFMSLLGVLGSLMVAFFLYHVAFRMAyfpfVNLASLLLLSGvcvnytLIFFDLWR 522
Cdd:cd10432 102 TAATFGGLSLYgyttkkdLSFLgSFLFMGLIGLIIASLVNIFLQSSALQFA----ISAIGVLIFSG------LIAYDTQR 171
|
....
gi 564342364 523 LSRG 526
Cdd:cd10432 172 IKRM 175
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| MMPL |
COG1033 |
Predicted exporter protein, RND superfamily [General function prediction only]; |
448-604 |
1.63e-11 |
|
Predicted exporter protein, RND superfamily [General function prediction only];
Pssm-ID: 440656 [Multi-domain] Cd Length: 767 Bit Score: 69.12 E-value: 1.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564342364 448 LLSLVIIFFGMSLYLRSLFITFMSLLGVLGSLMVAFFLyhvafrMAYF--PFvNLASLLLLS---GVCVNYTLIFFDlwR 522
Cdd:COG1033 612 LLALLLIFLLLLLAFRSLRLGLISLIPNLLPILLTFGL------MGLLgiPL-NIATAVVASialGIGVDYTIHFLS--R 682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564342364 523 LSRGQVPSGGLAHRVGRTMHHFGYLLLVSGLTTSAAFYGSYLSRLPTVRCFALFMGTAVLVHMGLTLLWLPATVVLHERY 602
Cdd:COG1033 683 YREERRKGGDLEEAIRRALRTTGKAILFTSLTLAAGFGVLLFSSFPPLADFGLLLALGLLVALLAALLLLPALLLLLDPR 762
|
..
gi 564342364 603 LA 604
Cdd:COG1033 763 IA 764
|
|
| MMPL |
COG1033 |
Predicted exporter protein, RND superfamily [General function prediction only]; |
439-778 |
9.36e-11 |
|
Predicted exporter protein, RND superfamily [General function prediction only];
Pssm-ID: 440656 [Multi-domain] Cd Length: 767 Bit Score: 66.42 E-value: 9.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564342364 439 YLAEDTM-YPLLSLVIIFFGMSLYLRSLFITFMSLLGVLGSLMVAF-FLYHVAFRMaYFPFVNLASLLLlsGVCVNYTLI 516
Cdd:COG1033 215 AIQSDLAiFFPLALLLILLLLFLFFRSLRGVLLPLLVVLLAVIWTLgLMGLLGIPL-SPLTILVPPLLL--AIGIDYGIH 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564342364 517 FFDLWRLSRGQVPSGGLAhrVGRTMHHFGYLLLVSGLTTSAAFYGSYLSRLPTVRCFALFMGTAVLVHMGLTLLWLPATV 596
Cdd:COG1033 292 LLNRYREERRKGLDKREA--LREALRKLGPPVLLTSLTTAIGFLSLLFSDIPPIRDFGIVAAIGVLLAFLTSLTLLPALL 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564342364 597 VLherylahgcvaqaqgqrggSDPLRLLLALHRRIRILRKIFSILSRLlfqrllpcgVIKFRY-IWICWFAALAAGGAYI 675
Cdd:COG1033 370 SL-------------------LPRPKPKTRRLKKPPELGRLLAKLARF---------VLRRPKvILVVALVLAVVSLYGI 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564342364 676 GGVSPRLRLPillplggQFFRSSHPFERFDAEYRQQFlfedlppneGGNLPVVLVwgilpVDTsdpldprtnssvvsDPD 755
Cdd:COG1033 422 SRLKVEYDFE-------DYLPEDSPIRQDLDFIEENF---------GGSDPLEVV-----VDT--------------GEP 466
|
330 340
....*....|....*....|...
gi 564342364 756 FSPSSPEAQEWLQALCQGAQNQS 778
Cdd:COG1033 467 DGLKDPEVLKEIDRLQDYLESLP 489
|
|
| MMPL |
pfam03176 |
MMPL family; Members of this family are putative integral membrane proteins from bacteria. ... |
448-598 |
3.42e-07 |
|
MMPL family; Members of this family are putative integral membrane proteins from bacteria. Several of the members are mycobacterial proteins. Many of the proteins contain two copies of this aligned region. The function of these proteins is not known, although it has been suggested that they may be involved in lipid transport.
Pssm-ID: 308676 [Multi-domain] Cd Length: 332 Bit Score: 53.83 E-value: 3.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564342364 448 LLSLVIIFFGMSLYLRSLFITFMSLLGVLGSLMVAF-----FLYHVAFRMAYFPfVNLASLLLLsGVCVNYTLIFFDLWR 522
Cdd:pfam03176 149 AVTLVVIFIILLIVYRSVVAALLPLLTVGLSLGAAQglvaiLAHILGIGLSTFA-LNLLVVLLI-AVGTDYALFLVSRYR 226
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564342364 523 LSRGQVPSGGLAhrVGRTMHHFGYLLLVSGLTTSAAFYGSYLSRLPTVRCFALFMGTAVLVHMGLTLLWLPATVVL 598
Cdd:pfam03176 227 EELRAGEDREEA--VIRAVRGTGKVVTAAGLTVAIAMLALSFARLPVFAQVGPTIAIGVLVDVLAALTLLPALLAL 300
|
|
| 2A060601 |
TIGR00917 |
Niemann-Pick C type protein family; The model describes Niemann-Pick C type protein in ... |
448-601 |
1.93e-06 |
|
Niemann-Pick C type protein family; The model describes Niemann-Pick C type protein in eukaryotes. The defective protein has been associated with Niemann-Pick disease which is described in humans as autosomal recessive lipidosis. It is characterized by the lysosomal accumulation of unestrified cholesterol. It is an integral membrane protein, which indicates that this protein is most likely involved in cholesterol transport or acts as some component of cholesterol homeostasis. [Transport and binding proteins, Other]
Pssm-ID: 273337 [Multi-domain] Cd Length: 1205 Bit Score: 52.60 E-value: 1.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564342364 448 LLSLVIIFFGMSLYL------RSLFITFMSLLGVLGSLMVAFflyHVAFRMAYFPFVNLASLLLLS----------GVCV 511
Cdd:TIGR00917 578 AISYLVMFAYISLTLgdsprlKSLYVTSKVLLGLSGILIVML---SVLGSVGVFSAVGLKSTLIIMevipflvlavGVDN 654
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564342364 512 NYTLI--FFDLWRLsRGQVPSGG-----LAHRVGRTMHHFGYLLLVSGLTTSAAFYGSYLSRLPTVRCFALFMGTAVLVH 584
Cdd:TIGR00917 655 IFILVffYFYLEYF-YRQVGVDNeqeltLERRLSRALMEVGPSITLASLSEILAFALGALIKMPAVRVFSMFAVLAVFLD 733
|
170
....*....|....*..
gi 564342364 585 MGLTLLWLPATVVLHER 601
Cdd:TIGR00917 734 FLLQITAFVALLVLDFK 750
|
|
| YdfJ |
COG2409 |
Predicted lipid transporter YdfJ, MMPL/SSD domain, RND superfamily [General function ... |
451-598 |
4.62e-06 |
|
Predicted lipid transporter YdfJ, MMPL/SSD domain, RND superfamily [General function prediction only];
Pssm-ID: 441964 [Multi-domain] Cd Length: 697 Bit Score: 51.30 E-value: 4.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564342364 451 LVIIFfgmslylRSLFITFMSLLGVLGSLMVAF-FLYHVAFRMAYFPFV-NLASLLLLsGVCVNYTLIFFDLWR--LSRG 526
Cdd:COG2409 186 LLLVF-------RSLVAALLPLLTAGLAVGVALgLLALLAAFTDVSSFApNLLTMLGL-GVGIDYALFLVSRYReeLRAG 257
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564342364 527 QVPsgglAHRVGRTMHHFGYLLLVSGLTTSAAFYGSYLSRLPTVRCFALFMGTAVLVHM--GLTLlwLPATVVL 598
Cdd:COG2409 258 EDR----EEAVARAVATAGRAVLFSGLTVAIALLGLLLAGLPFLRSMGPAAAIGVAVAVlaALTL--LPALLAL 325
|
|
| 2A067 |
TIGR00921 |
The (Largely Archaeal Putative) Hydrophobe/Amphiphile Efflux-3 (HAE3) Family; Characterized ... |
468-598 |
5.94e-05 |
|
The (Largely Archaeal Putative) Hydrophobe/Amphiphile Efflux-3 (HAE3) Family; Characterized members of the RND superfamily all probably catalyze substrate efflux via an H+ antiport mechanism. These proteins are found ubiquitously in bacteria, archaea and eukaryotes. They fall into seven phylogenetic families, this family (2.A.6.7) consists of uncharacterised putative transporters, largely in the Archaea. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 273340 [Multi-domain] Cd Length: 719 Bit Score: 47.52 E-value: 5.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564342364 468 TFMSLLGVLGSLMVAFFLYHvAFRMAYFPFVNLAS-------LLLLSGVCVNYTLIFFDLWRLSRGQVPSGGLAHR---- 536
Cdd:TIGR00921 570 RRMTIAGAILVLMILLAVFR-NPIKAVFPLIAIGSgilwaigLMGLRGIPSFLAMATTISIILGLGMDYSIHLAERyfee 648
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564342364 537 ---------VGRTMHHFGYLLLVSGLTTSAAFYGSYLSRLPTVRCFALFMGTAVLVHMGLTLLWLPATVVL 598
Cdd:TIGR00921 649 rkehgpkeaITHTMERTGPGILFSGLTTAGGFLSLLLSHFPIMRNFGLVQGIGVLSSLTAALVVFPALLVL 719
|
|
| BI-1-like_bacterial |
cd10432 |
Bacterial BAX inhibitor (BI)-1/YccA-like proteins; This family is comprised of bacterial ... |
377-526 |
2.40e-04 |
|
Bacterial BAX inhibitor (BI)-1/YccA-like proteins; This family is comprised of bacterial relatives of the mammalian members of the BAX inhibitor (BI)-1 like family of small transmembrane proteins, which have been shown to have an antiapoptotic effect either by stimulating the antiapoptotic function of Bcl-2, a well-characterized oncogene, or by inhibiting the proapoptotic effect of Bax, another member of the Bcl-2 family. In plants, BI-1 like proteins play a role in pathogen resistance. A characterized prokaryotic member, Escherichia coli YccA, has been shown to interact with ATP-dependent protease FtsH, which degrades abnormal membrane proteins as part of a quality control mechanism to keep the integrity of biological membranes.
Pssm-ID: 198414 Cd Length: 211 Bit Score: 44.09 E-value: 2.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564342364 377 SPQTADYQVPSLKFALLFLPIIktsslLDIYLDGLGDPIKVSDN------YTSISGMDLGLkprLLKYYLAEDTMYPLLS 450
Cdd:cd10432 30 TPALLLIAGSPLMWVLLIAELA-----LVFGLSFRINKMSVATAlplffaFAALTGLTLSP---ILLVYTGASIAQAFFT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564342364 451 LVIIFFGMSLY-------LRSL-FITFMSLLGVLGSLMVAFFLYHVAFRMAyfpfVNLASLLLLSGvcvnytLIFFDLWR 522
Cdd:cd10432 102 TAATFGGLSLYgyttkkdLSFLgSFLFMGLIGLIIASLVNIFLQSSALQFA----ISAIGVLIFSG------LIAYDTQR 171
|
....
gi 564342364 523 LSRG 526
Cdd:cd10432 172 IKRM 175
|
|
| 2A067 |
TIGR00921 |
The (Largely Archaeal Putative) Hydrophobe/Amphiphile Efflux-3 (HAE3) Family; Characterized ... |
435-600 |
4.42e-04 |
|
The (Largely Archaeal Putative) Hydrophobe/Amphiphile Efflux-3 (HAE3) Family; Characterized members of the RND superfamily all probably catalyze substrate efflux via an H+ antiport mechanism. These proteins are found ubiquitously in bacteria, archaea and eukaryotes. They fall into seven phylogenetic families, this family (2.A.6.7) consists of uncharacterised putative transporters, largely in the Archaea. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 273340 [Multi-domain] Cd Length: 719 Bit Score: 44.83 E-value: 4.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564342364 435 LLKYYLAEDTMYPLLSLVIIFFGMSLYLrslfiTFMSLLGVlgslmvafflyhvafrmayfPF--VNLASLLLLSGVCVN 512
Cdd:TIGR00921 208 LVLLLDFKRWWRPLLPLVIILFGVAWVL-----GIMGWLGI--------------------PLyaTTLLAVPMLIGVGID 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564342364 513 YTLIFFDLWRLSR--GQVPSGGLAHRVGRTmhhfGYLLLVSGLTTSAAFYGSYLSRLPTVRCFALFMGTAVLVHMGLTLL 590
Cdd:TIGR00921 263 YGIQTLNRYEEERdiGRAKGEAIVTAVRRT----GRAVLIALLTTSAGFAALALSEFPMVSEFGLGLVAGLITAYLLTLL 338
|
170
....*....|
gi 564342364 591 WLPATVVLHE 600
Cdd:TIGR00921 339 VLPALLQSID 348
|
|
| COG4258 |
COG4258 |
Predicted exporter [General function prediction only]; |
448-594 |
5.76e-04 |
|
Predicted exporter [General function prediction only];
Pssm-ID: 443400 [Multi-domain] Cd Length: 783 Bit Score: 44.46 E-value: 5.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564342364 448 LLSLVIIFFGMSLYLRSLFITFMSLLGVLGSLMVAfflyHVAFRMayfpfVNLASLLLLSGVCVNYTlIFFDLWRLSRGQ 527
Cdd:COG4258 653 LLLLLLRLRSLRRALRVLLPPLLAVLLTLAILGLL----GIPLNL-----FHLIALLLVLGIGIDYA-LFFTEGLLDKGE 722
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564342364 528 VPsgglahrvgRTMHhfgyLLLVSGLTTSAAFyGSY-LSRLPTVRCFALFMGTAVLVHMGLTLLWLPA 594
Cdd:COG4258 723 LA---------RTLL----SILLAALTTLLGF-GLLaFSSTPALRSFGLTVLLGILLALLLAPLLAPR 776
|
|
| Sterol-sensing |
pfam12349 |
Sterol-sensing domain of SREBP cleavage-activation; Sterol regulatory element-binding proteins ... |
529-601 |
1.56e-03 |
|
Sterol-sensing domain of SREBP cleavage-activation; Sterol regulatory element-binding proteins (SREBPs) are membrane-bound transcription factors that promote lipid synthesis in animal cells. They are embedded in the membranes of the endoplasmic reticulum (ER) in a helical hairpin orientation and are released from the ER by a two-step proteolytic process. Proteolysis begins when the SREBPs are cleaved at Site-1, which is located at a leucine residue in the middle of the hydrophobic loop in the lumen of the ER. Upon proteolytic processing SREBP can activate the expression of genes involved in cholesterol biosynthesis and uptake. SCAP stimulates cleavage of SREBPs via fusion of the their two C-termini. This domain is the transmembrane region that traverses the membrane eight times and is the sterol-sensing domain of the cleavage protein. WD40 domains are found towards the C-terminus.
Pssm-ID: 463544 [Multi-domain] Cd Length: 153 Bit Score: 40.64 E-value: 1.56e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564342364 529 PSGGLAHRVGRTMHHFGYLLLVSGLTTSAAFYGSYLSRLPTVRCFALFMGTAVLVHMGLTLLWLPATVVLHER 601
Cdd:pfam12349 66 RSLDVSERIAEALGEVGPSITLTSLTEILAFLLGALTDMPAVQEFCLFAAVAVLFDFLLQMTFFVAVLSLDIR 138
|
|
| COG4258 |
COG4258 |
Predicted exporter [General function prediction only]; |
448-594 |
9.16e-03 |
|
Predicted exporter [General function prediction only];
Pssm-ID: 443400 [Multi-domain] Cd Length: 783 Bit Score: 40.61 E-value: 9.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564342364 448 LLSLVIIFFGMSLYLRSLFITFMSLLGVLGSLMVAFFLYHVAFRMayfpfVNLASLLL---LSGVCVNYTLIFFdLWRLS 524
Cdd:COG4258 256 LISLLGILLLLLLVFRSLRPLLLGLLPVAVGALAGLAAVSLVFGS-----VHGITLGFgssLIGVAVDYSLHYL-THRRA 329
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564342364 525 RGQVPSGGLAHRVGRTmhhfgylLLVSGLTTSAAFYGSYLSRLPTVRCFALFMGTAVLVHMGLTLLWLPA 594
Cdd:COG4258 330 AGEWDPRAALRRIWPT-------LLLGLLTTVLGYLALLFSPFPGLRQLGVFAAAGLLAAALTTLLWLPL 392
|
|
|