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Conserved domains on  [gi|1524484190|gb|AZF31293|]
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Lysophospholipid transporter LplT [Pseudomonas sp. R4-35-07]

Protein Classification

acyl-[ACP]--phospholipid O-acyltransferase( domain architecture ID 1004368)

acyl-[ACP]--phospholipid O-acyltransferase may be involved in lysophospholipid acylation and transport across cytoplasmic or internal membranes of one or more from a variety of substrates

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK06814 super family cl35510
acyl-[ACP]--phospholipid O-acyltransferase;
3-590 2.27e-156

acyl-[ACP]--phospholipid O-acyltransferase;


The actual alignment was detected with superfamily member PRK06814:

Pssm-ID: 235865 [Multi-domain]  Cd Length: 1140  Bit Score: 479.08  E-value: 2.27e-156
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524484190    3 HPSQFTLLRTRRFLPFFITQLLGAFNDNIFKQSLILAILYKL--TLDGDRSIWVNLCALLFILPFFLFSALAGQFGEKFN 80
Cdd:PRK06814     1 DTMKLYLMKSRRFAPLFWTQFFGAFNDNFLKNALVILILYGLsgALGAYNNALVTLAGAVFILPFFIFSALAGQLADKYD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524484190   81 KDALIRAIKLGEIVIMAVGATGFLFDHLELMLLALFAMGTHSALFGPVKYSIMPQALHDDELVGGNGLVEMGTFLAILAG 160
Cdd:PRK06814    81 KAKLAKILKFAEIGIAALAIYGFHLNSVPLLFAALFLMGIHSALFGPIKYSILPDHLNKDELLGANALVEAGTFIAILLG 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524484190  161 TIGAGIMMSStHYAPVVAVAIVGVALLGYLASRSIPRAAASTPQLRLDWNIFTQSWATLRMgLGQTPAVSRSIVGNSWFW 240
Cdd:PRK06814   161 TIIGGLATIS-GNFVILVALLMGIAVLGWLASLFIPKTGNAAPDLKIDRNIIRSTITLLKY-AKADKRIWLAILGISWFW 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524484190  241 FVGAIYLTQIPAYAKEWLYGDETVVTLILTVFSVGIALGSMLCEKLSGRKVEIGLVPFGSFGLTVFGLLLWWHSGGFVQN 320
Cdd:PRK06814   239 LVGAVVLSQLPLLAKETLGGDENVATLFLAVFSVGVAVGSFLASKLSEGRITLLYVPIGALLMGLFGLDLAFASSSVPAE 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524484190  321 V-QPNDWLAVLGYGQAWWVLFDILGLGVFGGFYIVPLYALIQSRTAENQRARVIAANNILNALFMVVSAIVSILLLSvAK 399
Cdd:PRK06814   319 PaQLKSILVFLSKRHGWRILIDLFGLAAAGGLYIVPLFAALQAWANPAHRARVIAANNVLNAAFMVAGTIILALLQA-LG 397
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524484190  400 LSIPELFLVVSLLNIAVNTYIFRIVPEFTMRFMIWLLSHSMYRVEHRNLEQIPDEG-AALLVCNHVSFVDALLIGGAVRR 478
Cdd:PRK06814   398 FSIPWIILFIALANLIVAILILRLLPTNLLRDIFSILFRAFYRVEVKGLENLQKAGkKAVIAANHVSFLDGPLLAAYLPE 477
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524484190  479 PIRFVMYYKIYRL----PVLnfifRTAGAIPI------AGRHediqiyekaftrIAKYLKDGELVCIFPEGKLTGDGEMN 548
Cdd:PRK06814   478 EPTFAIDTDIAKAwwvkPFL----KLAKALPVdptnpmATRT------------LIKEVQKGEKLVIFPEGRITVTGSLM 541
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|....*
gi 1524484190  549 EFRGGVTRILEETPVPVIPMALQGLWGSFFSR---DPDKGLFHRI 590
Cdd:PRK06814   542 KIYDGPGMIADKAGAMVVPVRIDGLQFTHFSRlknQVRRKWFPKV 586
 
Name Accession Description Interval E-value
PRK06814 PRK06814
acyl-[ACP]--phospholipid O-acyltransferase;
3-590 2.27e-156

acyl-[ACP]--phospholipid O-acyltransferase;


Pssm-ID: 235865 [Multi-domain]  Cd Length: 1140  Bit Score: 479.08  E-value: 2.27e-156
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524484190    3 HPSQFTLLRTRRFLPFFITQLLGAFNDNIFKQSLILAILYKL--TLDGDRSIWVNLCALLFILPFFLFSALAGQFGEKFN 80
Cdd:PRK06814     1 DTMKLYLMKSRRFAPLFWTQFFGAFNDNFLKNALVILILYGLsgALGAYNNALVTLAGAVFILPFFIFSALAGQLADKYD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524484190   81 KDALIRAIKLGEIVIMAVGATGFLFDHLELMLLALFAMGTHSALFGPVKYSIMPQALHDDELVGGNGLVEMGTFLAILAG 160
Cdd:PRK06814    81 KAKLAKILKFAEIGIAALAIYGFHLNSVPLLFAALFLMGIHSALFGPIKYSILPDHLNKDELLGANALVEAGTFIAILLG 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524484190  161 TIGAGIMMSStHYAPVVAVAIVGVALLGYLASRSIPRAAASTPQLRLDWNIFTQSWATLRMgLGQTPAVSRSIVGNSWFW 240
Cdd:PRK06814   161 TIIGGLATIS-GNFVILVALLMGIAVLGWLASLFIPKTGNAAPDLKIDRNIIRSTITLLKY-AKADKRIWLAILGISWFW 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524484190  241 FVGAIYLTQIPAYAKEWLYGDETVVTLILTVFSVGIALGSMLCEKLSGRKVEIGLVPFGSFGLTVFGLLLWWHSGGFVQN 320
Cdd:PRK06814   239 LVGAVVLSQLPLLAKETLGGDENVATLFLAVFSVGVAVGSFLASKLSEGRITLLYVPIGALLMGLFGLDLAFASSSVPAE 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524484190  321 V-QPNDWLAVLGYGQAWWVLFDILGLGVFGGFYIVPLYALIQSRTAENQRARVIAANNILNALFMVVSAIVSILLLSvAK 399
Cdd:PRK06814   319 PaQLKSILVFLSKRHGWRILIDLFGLAAAGGLYIVPLFAALQAWANPAHRARVIAANNVLNAAFMVAGTIILALLQA-LG 397
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524484190  400 LSIPELFLVVSLLNIAVNTYIFRIVPEFTMRFMIWLLSHSMYRVEHRNLEQIPDEG-AALLVCNHVSFVDALLIGGAVRR 478
Cdd:PRK06814   398 FSIPWIILFIALANLIVAILILRLLPTNLLRDIFSILFRAFYRVEVKGLENLQKAGkKAVIAANHVSFLDGPLLAAYLPE 477
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524484190  479 PIRFVMYYKIYRL----PVLnfifRTAGAIPI------AGRHediqiyekaftrIAKYLKDGELVCIFPEGKLTGDGEMN 548
Cdd:PRK06814   478 EPTFAIDTDIAKAwwvkPFL----KLAKALPVdptnpmATRT------------LIKEVQKGEKLVIFPEGRITVTGSLM 541
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|....*
gi 1524484190  549 EFRGGVTRILEETPVPVIPMALQGLWGSFFSR---DPDKGLFHRI 590
Cdd:PRK06814   542 KIYDGPGMIADKAGAMVVPVRIDGLQFTHFSRlknQVRRKWFPKV 586
MFS_MefA_like cd06173
Macrolide efflux protein A and similar proteins of the Major Facilitator Superfamily of ...
15-423 8.89e-48

Macrolide efflux protein A and similar proteins of the Major Facilitator Superfamily of transporters; This family is composed of Streptococcus pyogenes macrolide efflux protein A (MefA) and similar transporters, many of which remain uncharacterized. Some members may be multidrug resistance (MDR) transporters, which are drug/H+ antiporters (DHAs) that mediate the efflux of a variety of drugs and toxic compounds, conferring resistance to these compounds. MefA confers resistance to 14-membered macrolides including erythromycin and to 15-membered macrolides. It functions as an efflux pump to regulate intracellular macrolide levels. The MefA-like family belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.


Pssm-ID: 340863 [Multi-domain]  Cd Length: 383  Bit Score: 172.03  E-value: 8.89e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524484190  15 FLPFFITQLLGAFNDNIFKQSLILAILYKltldGDRSIWVNLCALLFILPFFLFSALAGQFGEKFNKDALIRAIKLGEIV 94
Cdd:cd06173     1 FRLLWLAQLLSALGDWIFTVALPWLVLQL----TGSALLVGLVLAAFFLPFLLFSPFAGVLADRFDRRRLLILADLLRAL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524484190  95 IMAVGATGFLFDHLEL--MLLALFAMGTHSALFGPVKYSIMPQALHDDELVGGNGLVEMGTFLAILAGTIGAGIMMSSTH 172
Cdd:cd06173    77 LAAVLALLALLGSLSLwlLLVLAFLLGIASAFFGPARQALLPELVPKEQLVRANALNSLATQLARIIGPALGGLLVALLG 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524484190 173 yAPVVAVAIVGVALLGYLASRSIPRAAASTPQLRLDWNIftQSWATLRMGLGQTPAVSRSIVGNSWFWFVGAIYLTQIPA 252
Cdd:cd06173   157 -PGGAFAINALSFLLSALLLLFIRRPPPAAPGESSSLLL--RDLREGLRYLRRSPLLRLLLLALALFALLGGALTVLLPL 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524484190 253 YAKEWLYGDETVVTLILTVFSVGIALGSMLCEKLSGRKVEIGLVPFGSFGLTVFGLLLWWHSggfvqnvqpndwlavlgy 332
Cdd:cd06173   234 LAKEVLGGGAAGYGLLLAAFGVGALLGALLLGRLSKRRRRGRLLLIGALLLGLALLVLGLSP------------------ 295
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524484190 333 gQAWWVLFDILGLGVFGGFYIVPLYALIQSRTAENQRARVIAANNILNALFMVVSAIVSILLLsvAKLSIPELFLVVSLL 412
Cdd:cd06173   296 -SLWLLLAALFLLGLAGGLFNVPLNTLLQLRVPDELRGRVFSVYNALNSGAMPLGALLAGLLA--DALGLSAVFLLAGAL 372
                         410
                  ....*....|.
gi 1524484190 413 NIAVNTYIFRI 423
Cdd:cd06173   373 LLLAALLLLLL 383
PlsC COG0204
1-acyl-sn-glycerol-3-phosphate acyltransferase [Lipid transport and metabolism]; ...
418-624 1.61e-42

1-acyl-sn-glycerol-3-phosphate acyltransferase [Lipid transport and metabolism]; 1-acyl-sn-glycerol-3-phosphate acyltransferase is part of the Pathway/BioSystem: Phospholipid biosynthesis


Pssm-ID: 439974 [Multi-domain]  Cd Length: 215  Bit Score: 152.47  E-value: 1.61e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524484190 418 TYIFRIVPEFTMRFMIWLLSHSM-YRVEHRNLEQIPDEGAALLVCNHVSFVDALLIGGAVRRPIRFVMYYKIYRLPVLNF 496
Cdd:COG0204     5 FLLLRRFRYRLVRLWARLLLRLLgVRVRVEGLENLPADGPVLIVANHQSWLDILLLLAALPRPVRFVAKKELFKIPLLGW 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524484190 497 IFRTAGAIPI--AGRHEDIqiyeKAFTRIAKYLKDGELVCIFPEGKLTGDGEMNEFRGGVTRILEETPVPVIPMALQGLW 574
Cdd:COG0204    85 LLRALGAIPVdrSKRRAAL----RALRQAVEALKAGESLVIFPEGTRSPDGRLLPFKTGAARLALEAGVPIVPVAIDGTE 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1524484190 575 GSFFsrdpdKGLFHRIwSRVVLVAGAPVPVEEATPAQLQAVVGVLRGSVR 624
Cdd:COG0204   161 RALP-----KGFLPRP-GKVTVRIGPPIDPSDLEGEDRRELAERLRAAIE 204
Acyltransferase pfam01553
Acyltransferase; This family contains acyltransferases involved in phospholipid biosynthesis ...
442-570 6.92e-24

Acyltransferase; This family contains acyltransferases involved in phospholipid biosynthesis and other proteins of unknown function. This family also includes tafazzin, the Barth syndrome gene.


Pssm-ID: 366704 [Multi-domain]  Cd Length: 131  Bit Score: 97.35  E-value: 6.92e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524484190 442 RVEHRNLEQIPDEGAALLVCNHVSFVDALLIGGAV---RRPIRFVMYYKIYRLPVLNFIFRTAGAIPIagRHEDIQIYEK 518
Cdd:pfam01553   1 RIEVHGLENLPRGGPAIVVANHQSYLDVLLLSLALykrGRPLVFVAKKELFDIPLVGWLMRLLGCIFI--DRKNRKDAAG 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1524484190 519 AFTRIAKYLKDGELVCIFPEGKLTGDGEMNEFRGGVTRILEETPVPVIPMAL 570
Cdd:pfam01553  79 TLEYLVELLREGKLVVIFPEGTRSREGELLPFKKGAFRLAIEAGVPIVPVAI 130
PlsC smart00563
Phosphate acyltransferases; Function in phospholipid biosynthesis and have either ...
457-573 1.15e-22

Phosphate acyltransferases; Function in phospholipid biosynthesis and have either glycerolphosphate, 1-acylglycerolphosphate, or 2-acylglycerolphosphoethanolamine acyltransferase activities. Tafazzin, the product of the gene mutated in patients with Barth syndrome, is a member of this family.


Pssm-ID: 214724 [Multi-domain]  Cd Length: 118  Bit Score: 93.57  E-value: 1.15e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524484190  457 ALLVCNHVSFVDALLIGGAVRR---PIRFVMYYKIYRLPVLNFIFRTAGAIPIagRHEDIQIYEKAFTRIAKYLKDGELV 533
Cdd:smart00563   1 ALVVANHQSFLDPLVLSALLPRklgRVRFVAKKELFYVPLLGWLLRLLGAIFI--DRSNGRKARAALREAVELLKEGEWL 78
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1524484190  534 CIFPEGKLTGDGEMNEFRGGVTRILEETPVPVIPMALQGL 573
Cdd:smart00563  79 LIFPEGTRSRPGKLLPFKKGAARLALEAGVPIVPVAIRGT 118
AGP_acyltrn TIGR00530
1-acyl-sn-glycerol-3-phosphate acyltransferases; This model describes the core homologous ...
443-571 7.33e-18

1-acyl-sn-glycerol-3-phosphate acyltransferases; This model describes the core homologous region of a collection of related proteins, several of which are known to act as 1-acyl-sn-glycerol-3-phosphate acyltransferases (EC 2.3.1.51). Proteins scoring above the trusted cutoff are likely to have the same general activity. However, there is variation among characterized members as to whether the acyl group can be donated by acyl carrier protein or coenzyme A, and in the length and saturation of the donated acyl group. 1-acyl-sn-glycerol-3-phosphate acyltransferase is also called 1-AGP acyltransferase, lysophosphatidic acid acyltransferase, and LPA acyltransferase. [Fatty acid and phospholipid metabolism, Biosynthesis]


Pssm-ID: 129621 [Multi-domain]  Cd Length: 130  Bit Score: 80.08  E-value: 7.33e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524484190 443 VEHRNLEQIPDEGAALLVCNHVSFVDALLIGGAVRRPIRFVMYYKIYRLPVLNFIFRTAGAIPIagRHEDIQIYEKAFTR 522
Cdd:TIGR00530   4 VEVVGPENLPAKSPVLVVANHQSNLDPLTLSAAFPPPIVFIAKKELKWIPFFGIMLWLTGAIFI--DRENIRAIATALKA 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1524484190 523 IAKYLKDGELVCIFPEGKLTGDGEMNEFRGGVTRILEETPVPVIPMALQ 571
Cdd:TIGR00530  82 AIEVLKQGRSIGVFPEGTRSRGRDILPFKKGAFHIAIKAGVPILPVVLS 130
 
Name Accession Description Interval E-value
PRK06814 PRK06814
acyl-[ACP]--phospholipid O-acyltransferase;
3-590 2.27e-156

acyl-[ACP]--phospholipid O-acyltransferase;


Pssm-ID: 235865 [Multi-domain]  Cd Length: 1140  Bit Score: 479.08  E-value: 2.27e-156
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524484190    3 HPSQFTLLRTRRFLPFFITQLLGAFNDNIFKQSLILAILYKL--TLDGDRSIWVNLCALLFILPFFLFSALAGQFGEKFN 80
Cdd:PRK06814     1 DTMKLYLMKSRRFAPLFWTQFFGAFNDNFLKNALVILILYGLsgALGAYNNALVTLAGAVFILPFFIFSALAGQLADKYD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524484190   81 KDALIRAIKLGEIVIMAVGATGFLFDHLELMLLALFAMGTHSALFGPVKYSIMPQALHDDELVGGNGLVEMGTFLAILAG 160
Cdd:PRK06814    81 KAKLAKILKFAEIGIAALAIYGFHLNSVPLLFAALFLMGIHSALFGPIKYSILPDHLNKDELLGANALVEAGTFIAILLG 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524484190  161 TIGAGIMMSStHYAPVVAVAIVGVALLGYLASRSIPRAAASTPQLRLDWNIFTQSWATLRMgLGQTPAVSRSIVGNSWFW 240
Cdd:PRK06814   161 TIIGGLATIS-GNFVILVALLMGIAVLGWLASLFIPKTGNAAPDLKIDRNIIRSTITLLKY-AKADKRIWLAILGISWFW 238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524484190  241 FVGAIYLTQIPAYAKEWLYGDETVVTLILTVFSVGIALGSMLCEKLSGRKVEIGLVPFGSFGLTVFGLLLWWHSGGFVQN 320
Cdd:PRK06814   239 LVGAVVLSQLPLLAKETLGGDENVATLFLAVFSVGVAVGSFLASKLSEGRITLLYVPIGALLMGLFGLDLAFASSSVPAE 318
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524484190  321 V-QPNDWLAVLGYGQAWWVLFDILGLGVFGGFYIVPLYALIQSRTAENQRARVIAANNILNALFMVVSAIVSILLLSvAK 399
Cdd:PRK06814   319 PaQLKSILVFLSKRHGWRILIDLFGLAAAGGLYIVPLFAALQAWANPAHRARVIAANNVLNAAFMVAGTIILALLQA-LG 397
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524484190  400 LSIPELFLVVSLLNIAVNTYIFRIVPEFTMRFMIWLLSHSMYRVEHRNLEQIPDEG-AALLVCNHVSFVDALLIGGAVRR 478
Cdd:PRK06814   398 FSIPWIILFIALANLIVAILILRLLPTNLLRDIFSILFRAFYRVEVKGLENLQKAGkKAVIAANHVSFLDGPLLAAYLPE 477
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524484190  479 PIRFVMYYKIYRL----PVLnfifRTAGAIPI------AGRHediqiyekaftrIAKYLKDGELVCIFPEGKLTGDGEMN 548
Cdd:PRK06814   478 EPTFAIDTDIAKAwwvkPFL----KLAKALPVdptnpmATRT------------LIKEVQKGEKLVIFPEGRITVTGSLM 541
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|....*
gi 1524484190  549 EFRGGVTRILEETPVPVIPMALQGLWGSFFSR---DPDKGLFHRI 590
Cdd:PRK06814   542 KIYDGPGMIADKAGAMVVPVRIDGLQFTHFSRlknQVRRKWFPKV 586
PRK08633 PRK08633
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
8-616 2.22e-143

2-acyl-glycerophospho-ethanolamine acyltransferase; Validated


Pssm-ID: 236315 [Multi-domain]  Cd Length: 1146  Bit Score: 445.14  E-value: 2.22e-143
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524484190    8 TLLRTRRFLPFFITQLLGAFNDNIFKqSLILAILYKlTLDGDRSIWVNLCALLFILP-FFLFSALAGQFGEKFNKDALIR 86
Cdd:PRK08633     4 NLLKIIGFLPLLLTQFLNAFNDLGHK-ILIQNTLIK-AYDGSEQVILTAIVNALFLLpFLLLSSPAGFLADKFSKNRVIR 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524484190   87 AIKLGEIVIMAVGATGFLFDHLELMLLALFAMGTHSALFGPVKYSIMPQALHDDELVGGNGLVEMGTFLAILAGTIGAGI 166
Cdd:PRK08633    82 IVKLFEVGLTLLIVLAYYLGWFWLAFAVTFLLGAQSAIYSPAKYGIIPELVGKENLSRANGLLEAFTIVAILAGTALFSF 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524484190  167 MMSST---------HYAPVVAVAIVGVALLGYLASRSIPR--AAASTPQLRLDWNIFTQSWATLRMgLGQTPAVSRSIVG 235
Cdd:PRK08633   162 LFESVngntpseilGRIAPAGLVLLAVAVLGLIFAYRLPKvpAAAPEVFDKKKYLFPKLLWRNLKL-LRSDRVLWLAIIG 240
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524484190  236 NSWFWFVGAIYLTQIPAYAKEWLYGDET-VVTLILTVFSVGIALGSMLCEKLSGRKVEIGLVPFGSFGLTVFGLLLwwhs 314
Cdd:PRK08633   241 LSYFWFISQLAQANFPAYAKEVLGLDNTfQVQYLLAASAIGIGIGSLLAGRLSGRHIELGLVPLGALGLALSLFLL---- 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524484190  315 gGFVQNVqpndwlavlgygqaWWVLFDILGLGVFGGFYIVPLYALIQSRTAENQRARVIAANNILNALFMVVSAIVSILL 394
Cdd:PRK08633   317 -PTAPSL--------------ASVLVLFFLFGFSAGLFIVPLNALIQFRAPEKELGKVLAANNFLQNVGMLLFLALTTLF 381
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524484190  395 lSVAKLSIPELFLVVSLLNIAVNTYIFRIVPEFTMRFMIWLLSHSMYRVEHRNLEQIPDEGAALLVCNHVSFVDALLIGG 474
Cdd:PRK08633   382 -SGLGLSPAGLFYLIALVTLIGTLYTLLLLPDSLLRFLLLLLMHTRYRLRVEGRENIPAKGGALLLGNHVSWIDWALLQA 460
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524484190  475 AVRRPIRFVMYYKIYRLPVLNFIFRTAGAIPI--AGRHEDIQIyekaftrIAKYLKDGELVCIFPEGKLTGDGEMNEFRG 552
Cdd:PRK08633   461 ASPRPIRFVMERSIYEKWYLKWFFKLFGVIPIssGGSKESLEF-------IRKALDDGEVVCIFPEGAITRNGQLNEFKR 533
                          570       580       590       600       610       620
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1524484190  553 GVTRILEETPVPVIPMALQGLWGSFFSRDpDKGLFHRIWSRV---VLVA-GAPVPvEEATPAQL-QAVV 616
Cdd:PRK08633   534 GFELIVKGTDVPIIPFYIRGLWGSIFSRA-SGKFLWRWPTRIpypVTVAfGKPMP-AHSTAHEVkQAVF 600
MFS_MefA_like cd06173
Macrolide efflux protein A and similar proteins of the Major Facilitator Superfamily of ...
15-423 8.89e-48

Macrolide efflux protein A and similar proteins of the Major Facilitator Superfamily of transporters; This family is composed of Streptococcus pyogenes macrolide efflux protein A (MefA) and similar transporters, many of which remain uncharacterized. Some members may be multidrug resistance (MDR) transporters, which are drug/H+ antiporters (DHAs) that mediate the efflux of a variety of drugs and toxic compounds, conferring resistance to these compounds. MefA confers resistance to 14-membered macrolides including erythromycin and to 15-membered macrolides. It functions as an efflux pump to regulate intracellular macrolide levels. The MefA-like family belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.


Pssm-ID: 340863 [Multi-domain]  Cd Length: 383  Bit Score: 172.03  E-value: 8.89e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524484190  15 FLPFFITQLLGAFNDNIFKQSLILAILYKltldGDRSIWVNLCALLFILPFFLFSALAGQFGEKFNKDALIRAIKLGEIV 94
Cdd:cd06173     1 FRLLWLAQLLSALGDWIFTVALPWLVLQL----TGSALLVGLVLAAFFLPFLLFSPFAGVLADRFDRRRLLILADLLRAL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524484190  95 IMAVGATGFLFDHLEL--MLLALFAMGTHSALFGPVKYSIMPQALHDDELVGGNGLVEMGTFLAILAGTIGAGIMMSSTH 172
Cdd:cd06173    77 LAAVLALLALLGSLSLwlLLVLAFLLGIASAFFGPARQALLPELVPKEQLVRANALNSLATQLARIIGPALGGLLVALLG 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524484190 173 yAPVVAVAIVGVALLGYLASRSIPRAAASTPQLRLDWNIftQSWATLRMGLGQTPAVSRSIVGNSWFWFVGAIYLTQIPA 252
Cdd:cd06173   157 -PGGAFAINALSFLLSALLLLFIRRPPPAAPGESSSLLL--RDLREGLRYLRRSPLLRLLLLALALFALLGGALTVLLPL 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524484190 253 YAKEWLYGDETVVTLILTVFSVGIALGSMLCEKLSGRKVEIGLVPFGSFGLTVFGLLLWWHSggfvqnvqpndwlavlgy 332
Cdd:cd06173   234 LAKEVLGGGAAGYGLLLAAFGVGALLGALLLGRLSKRRRRGRLLLIGALLLGLALLVLGLSP------------------ 295
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524484190 333 gQAWWVLFDILGLGVFGGFYIVPLYALIQSRTAENQRARVIAANNILNALFMVVSAIVSILLLsvAKLSIPELFLVVSLL 412
Cdd:cd06173   296 -SLWLLLAALFLLGLAGGLFNVPLNTLLQLRVPDELRGRVFSVYNALNSGAMPLGALLAGLLA--DALGLSAVFLLAGAL 372
                         410
                  ....*....|.
gi 1524484190 413 NIAVNTYIFRI 423
Cdd:cd06173   373 LLLAALLLLLL 383
PlsC COG0204
1-acyl-sn-glycerol-3-phosphate acyltransferase [Lipid transport and metabolism]; ...
418-624 1.61e-42

1-acyl-sn-glycerol-3-phosphate acyltransferase [Lipid transport and metabolism]; 1-acyl-sn-glycerol-3-phosphate acyltransferase is part of the Pathway/BioSystem: Phospholipid biosynthesis


Pssm-ID: 439974 [Multi-domain]  Cd Length: 215  Bit Score: 152.47  E-value: 1.61e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524484190 418 TYIFRIVPEFTMRFMIWLLSHSM-YRVEHRNLEQIPDEGAALLVCNHVSFVDALLIGGAVRRPIRFVMYYKIYRLPVLNF 496
Cdd:COG0204     5 FLLLRRFRYRLVRLWARLLLRLLgVRVRVEGLENLPADGPVLIVANHQSWLDILLLLAALPRPVRFVAKKELFKIPLLGW 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524484190 497 IFRTAGAIPI--AGRHEDIqiyeKAFTRIAKYLKDGELVCIFPEGKLTGDGEMNEFRGGVTRILEETPVPVIPMALQGLW 574
Cdd:COG0204    85 LLRALGAIPVdrSKRRAAL----RALRQAVEALKAGESLVIFPEGTRSPDGRLLPFKTGAARLALEAGVPIVPVAIDGTE 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1524484190 575 GSFFsrdpdKGLFHRIwSRVVLVAGAPVPVEEATPAQLQAVVGVLRGSVR 624
Cdd:COG0204   161 RALP-----KGFLPRP-GKVTVRIGPPIDPSDLEGEDRRELAERLRAAIE 204
LPLAT_AGPAT-like cd07989
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: AGPAT-like; ...
434-611 5.70e-42

Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: AGPAT-like; Lysophospholipid acyltransferase (LPLAT) superfamily member: acyltransferases of de novo and remodeling pathways of glycerophospholipid biosynthesis which catalyze the incorporation of an acyl group from either acylCoAs or acyl-acyl carrier proteins (acylACPs) into acceptors such as glycerol 3-phosphate, dihydroxyacetone phosphate or lyso-phosphatidic acid. Included in this subgroup are such LPLATs as 1-acyl-sn-glycerol-3-phosphate acyltransferase (AGPAT, PlsC), Tafazzin (product of Barth syndrome gene), and similar proteins.


Pssm-ID: 153251 [Multi-domain]  Cd Length: 184  Bit Score: 149.73  E-value: 5.70e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524484190 434 WLLSHSMYRVEHRNLEQIPDEGAALLVCNHVSFVDALLIGGAVRRPIRFVMYYKIYRLPVLNFIFRTAGAIPIAgRhEDI 513
Cdd:cd07989     3 LLLRLLGVRVRVEGLENLPPKGPVIIVANHQSYLDPLVLGAALPRPIRFVAKKELFKIPFLGWLLRLLGAIPID-R-GNG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524484190 514 QIYEKAFTRIAKYLKDGELVCIFPEGKLTGDGEMNEFRGGVTRILEETPVPVIPMALQGLWGSFFsrdpdKGLFHRIWSR 593
Cdd:cd07989    81 RSAREALREAIEALKEGESVVIFPEGTRSRDGELLPFKSGAFRLAKEAGVPIVPVAISGTWGSLP-----KGKKLPRPGR 155
                         170
                  ....*....|....*...
gi 1524484190 594 VVLVAGAPVPVEEATPAQ 611
Cdd:cd07989   156 VTVRIGEPIPPEGLELAE 173
Acyltransferase pfam01553
Acyltransferase; This family contains acyltransferases involved in phospholipid biosynthesis ...
442-570 6.92e-24

Acyltransferase; This family contains acyltransferases involved in phospholipid biosynthesis and other proteins of unknown function. This family also includes tafazzin, the Barth syndrome gene.


Pssm-ID: 366704 [Multi-domain]  Cd Length: 131  Bit Score: 97.35  E-value: 6.92e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524484190 442 RVEHRNLEQIPDEGAALLVCNHVSFVDALLIGGAV---RRPIRFVMYYKIYRLPVLNFIFRTAGAIPIagRHEDIQIYEK 518
Cdd:pfam01553   1 RIEVHGLENLPRGGPAIVVANHQSYLDVLLLSLALykrGRPLVFVAKKELFDIPLVGWLMRLLGCIFI--DRKNRKDAAG 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1524484190 519 AFTRIAKYLKDGELVCIFPEGKLTGDGEMNEFRGGVTRILEETPVPVIPMAL 570
Cdd:pfam01553  79 TLEYLVELLREGKLVVIFPEGTRSREGELLPFKKGAFRLAIEAGVPIVPVAI 130
PlsC smart00563
Phosphate acyltransferases; Function in phospholipid biosynthesis and have either ...
457-573 1.15e-22

Phosphate acyltransferases; Function in phospholipid biosynthesis and have either glycerolphosphate, 1-acylglycerolphosphate, or 2-acylglycerolphosphoethanolamine acyltransferase activities. Tafazzin, the product of the gene mutated in patients with Barth syndrome, is a member of this family.


Pssm-ID: 214724 [Multi-domain]  Cd Length: 118  Bit Score: 93.57  E-value: 1.15e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524484190  457 ALLVCNHVSFVDALLIGGAVRR---PIRFVMYYKIYRLPVLNFIFRTAGAIPIagRHEDIQIYEKAFTRIAKYLKDGELV 533
Cdd:smart00563   1 ALVVANHQSFLDPLVLSALLPRklgRVRFVAKKELFYVPLLGWLLRLLGAIFI--DRSNGRKARAALREAVELLKEGEWL 78
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1524484190  534 CIFPEGKLTGDGEMNEFRGGVTRILEETPVPVIPMALQGL 573
Cdd:smart00563  79 LIFPEGTRSRPGKLLPFKKGAARLALEAGVPIVPVAIRGT 118
LPLAT_AAK14816-like cd07992
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: Unknown ...
429-605 1.51e-20

Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: Unknown AAK14816-like; Lysophospholipid acyltransferase (LPLAT) superfamily member: acyltransferases of de novo and remodeling pathways of glycerophospholipid biosynthesis which catalyze the incorporation of an acyl group from either acylCoAs or acyl-acyl carrier proteins (acylACPs) into acceptors such as glycerol 3-phosphate, dihydroxyacetone phosphate or lyso-phosphatidic acid. Included in this subgroup are uncharacterized glycerol-3-phosphate acyltransferases such as the Plasmodium falciparum locus AAK14816 putative acyltransferase, and similar proteins.


Pssm-ID: 153254 [Multi-domain]  Cd Length: 203  Bit Score: 90.01  E-value: 1.51e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524484190 429 MRFMIWLLSHSMYR-VEHRNLEQIPDEGAALLVCNHV-SFVDALLIGGAVRRPIRFVMYYKIYRLPVLNFIFRTAGAIPI 506
Cdd:cd07992     1 VRLLSRVILRIYFRrITVVGRENVPKDGPVIFLGNHPnALIDPLLLAATLRRPVRFLAKADLFKNPLIGWLLESFGAIPV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524484190 507 -----AGRHEDIQI-YEKAFTRIAKYLKDGELVCIFPEGKLTGDGEMNEFRGGVTRILEE------TPVPVIPMALQglw 574
Cdd:cd07992    81 yrpkdLARGGIGKIsNAAVFDAVGEALKAGGAIGIFPEGGSHDRPRLLPLKAGAARMALEaleagqKDVKIVPVGLN--- 157
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1524484190 575 gsFFSRdpdkglfHRIWSRVVLVAGAPVPVE 605
Cdd:cd07992   158 --YEDK-------SRFRSRVLVEFGKPISVS 179
AGP_acyltrn TIGR00530
1-acyl-sn-glycerol-3-phosphate acyltransferases; This model describes the core homologous ...
443-571 7.33e-18

1-acyl-sn-glycerol-3-phosphate acyltransferases; This model describes the core homologous region of a collection of related proteins, several of which are known to act as 1-acyl-sn-glycerol-3-phosphate acyltransferases (EC 2.3.1.51). Proteins scoring above the trusted cutoff are likely to have the same general activity. However, there is variation among characterized members as to whether the acyl group can be donated by acyl carrier protein or coenzyme A, and in the length and saturation of the donated acyl group. 1-acyl-sn-glycerol-3-phosphate acyltransferase is also called 1-AGP acyltransferase, lysophosphatidic acid acyltransferase, and LPA acyltransferase. [Fatty acid and phospholipid metabolism, Biosynthesis]


Pssm-ID: 129621 [Multi-domain]  Cd Length: 130  Bit Score: 80.08  E-value: 7.33e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524484190 443 VEHRNLEQIPDEGAALLVCNHVSFVDALLIGGAVRRPIRFVMYYKIYRLPVLNFIFRTAGAIPIagRHEDIQIYEKAFTR 522
Cdd:TIGR00530   4 VEVVGPENLPAKSPVLVVANHQSNLDPLTLSAAFPPPIVFIAKKELKWIPFFGIMLWLTGAIFI--DRENIRAIATALKA 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1524484190 523 IAKYLKDGELVCIFPEGKLTGDGEMNEFRGGVTRILEETPVPVIPMALQ 571
Cdd:TIGR00530  82 AIEVLKQGRSIGVFPEGTRSRGRDILPFKKGAFHIAIKAGVPILPVVLS 130
AraJ COG2814
Predicted arabinose efflux permease AraJ, MFS family [Carbohydrate transport and metabolism];
93-387 2.61e-11

Predicted arabinose efflux permease AraJ, MFS family [Carbohydrate transport and metabolism];


Pssm-ID: 442063 [Multi-domain]  Cd Length: 348  Bit Score: 65.38  E-value: 2.61e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524484190  93 IVIMAVGATGFLF-DHLELMLLALFAMGTHSALFGPVKYSIMPQALHDDELVGGNGLVEMGTFLAILAGTIGAGIMMSST 171
Cdd:COG2814    82 LLLFALGSLLCALaPSLWLLLAARFLQGLGAGALFPAALALIADLVPPERRGRALGLLGAGLGLGPALGPLLGGLLADLF 161
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524484190 172 HYAPVVAVAIVGVALLGYLASRSIPRAAASTPqlrldwnifTQSWATLRMGLGqTPAVSRSIVGNSWFWFVGAIYLTQIP 251
Cdd:COG2814   162 GWRWVFLVNAVLALLALLLLLRLLPESRPAAR---------ARLRGSLRELLR-RPRLLLLLLLAFLLGFGFFALFTYLP 231
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524484190 252 AYAKEWLYGDETVVTLILTVFSVGIALGSMLCEKLSGRkVEIGLVPFGSFGLTVFGLLLWWHSGGFvqnvqpndwlavlg 331
Cdd:COG2814   232 LYLQEVLGLSASAAGLLLALFGLGGVLGALLAGRLADR-FGRRRLLLIGLLLLALGLLLLALAGSL-------------- 296
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1524484190 332 ygqaWWVLFDILGLGVFGGFYIVPLYALIQSRTAENQRARVIAANNILNALFMVVS 387
Cdd:COG2814   297 ----WLLLLALFLLGFGFGLLFPLLQALVAELAPPEARGRASGLYNSAFFLGGPLA 348
PLN02901 PLN02901
1-acyl-sn-glycerol-3-phosphate acyltransferase
441-572 3.13e-11

1-acyl-sn-glycerol-3-phosphate acyltransferase


Pssm-ID: 215488 [Multi-domain]  Cd Length: 214  Bit Score: 63.21  E-value: 3.13e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524484190 441 YRVEHRNLEQIP-DEGAALLVCNHVSFVD--ALLiggAVRRPIRFVMYYKIYRLPVLNFIFRTAGAIPIagRHEDIQIYE 517
Cdd:PLN02901   35 YKIEVEGLENLPsPDEPAVYVSNHQSFLDiyTLF---HLGRPFKFISKTSIFLIPIIGWAMYMTGHIPL--KRMDRRSQL 109
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1524484190 518 KAFTRIAKYLKDGELVCIFPEGKLTGDGEMNEFRGGVTRILEETPVPVIPMALQG 572
Cdd:PLN02901  110 ECLKRCMELLKKGASVFFFPEGTRSKDGKLAAFKKGAFSVAAKTGVPVVPITLVG 164
PRK11195 PRK11195
lysophospholipid transporter LplT; Provisional
70-363 9.64e-11

lysophospholipid transporter LplT; Provisional


Pssm-ID: 236879 [Multi-domain]  Cd Length: 393  Bit Score: 64.09  E-value: 9.64e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524484190  70 ALAGQFGEKFNKD---ALIRAIKLGEIVIMAVGAtgflfdHLelmLLALFAMGTHSALFGPVKYSIMPQALHDDELVGGN 146
Cdd:PRK11195   56 PFVGAFADSFPKGrvmFIANGIKLLGCLLMLFGI------HP---LLAYGLVGIGAAAYSPAKYGILTELLPGEKLVKAN 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524484190 147 GLVEMGTFLAILAGTIGAGIMMSstHYAPVVAVAIVGVALLGYLASRSIPRAAASTPQLRldWNI------FTQSWATL- 219
Cdd:PRK11195  127 GWMEGSTIAAILLGTVLGGALAD--PHAEAALAVCALIYLLAALFNLFIPRLGARRPGQS--WNPiallrdFFHACRVLw 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524484190 220 RMGLGQTpavsrSIVGNSWFWFVGAIYLTQIPAYAKEWLYGDETVVTLILTVFSVGIALGSMLCEKLSGRKVEIGLVPFG 299
Cdd:PRK11195  203 RDKLGRF-----SLAGTTLFWGAGATLRFLVLAWAPVALGITLNQPAYLQAVVAIGIAVGAGAAARLVTLETVLRVLPAG 277
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1524484190 300 -SFGLTVFGLllwwhsggfvqNVQPNDWLAVLGygqawwvlfdILGLGVFGGFYIVPLYALIQSR 363
Cdd:PRK11195  278 iLMGLVVLLM-----------ALQHSLLPAYPL----------LILIGALGGFFVVPMNALLQHR 321
LPLAT cd06551
Lysophospholipid acyltransferases (LPLATs) of glycerophospholipid biosynthesis; ...
429-606 3.30e-10

Lysophospholipid acyltransferases (LPLATs) of glycerophospholipid biosynthesis; Lysophospholipid acyltransferase (LPLAT) superfamily members are acyltransferases of de novo and remodeling pathways of glycerophospholipid biosynthesis. These proteins catalyze the incorporation of an acyl group from either acylCoAs or acyl-acyl carrier proteins (acylACPs) into acceptors such as glycerol 3-phosphate, dihydroxyacetone phosphate or lyso-phosphatidic acid. Included in this superfamily are LPLATs such as glycerol-3-phosphate 1-acyltransferase (GPAT, PlsB), 1-acyl-sn-glycerol-3-phosphate acyltransferase (AGPAT, PlsC), lysophosphatidylcholine acyltransferase 1 (LPCAT-1), lysophosphatidylethanolamine acyltransferase (LPEAT, also known as, MBOAT2, membrane-bound O-acyltransferase domain-containing protein 2), lipid A biosynthesis lauroyl/myristoyl acyltransferase, 2-acylglycerol O-acyltransferase (MGAT), dihydroxyacetone phosphate acyltransferase (DHAPAT, also known as 1 glycerol-3-phosphate O-acyltransferase 1) and Tafazzin (the protein product of the Barth syndrome (TAZ) gene).


Pssm-ID: 153244 [Multi-domain]  Cd Length: 187  Bit Score: 59.74  E-value: 3.30e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524484190 429 MRFMIWLLSHsMYRVEHRNLEQIPDEGAALLVCNHVSFVDAL----LIGGAVRRPIRFVM-YYKIYRLPVlnfiFRTAGA 503
Cdd:cd06551     1 FRYLLLNFFG-FVRLEVKGPPPPPGGGPVLFVSNHSSWWDGLilflLLERGLRRDVYGLMdEELLERYPF----FTRLGA 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524484190 504 IPIA--GRHEDIQIYEKAFTRIAKYlkdGELVCIFPEGKlTGDGEMN--EFRGGVTRILEETPVPVIPMALQglwGSFFS 579
Cdd:cd06551    76 FSVDrdSPRSAAKSLKYVARLLSKP---GSVVWIFPEGT-RTRRDKRplQFKPGVAHLAEKAGVPIVPVALR---YTFEL 148
                         170       180
                  ....*....|....*....|....*..
gi 1524484190 580 RDPDKGLFHRIwsrvvlvaGAPVPVEE 606
Cdd:cd06551   149 FEQFPEIFVRI--------GPPIPYAE 167
LPLAT_MGAT-like cd07987
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: MGAT-like; ...
444-572 4.21e-10

Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: MGAT-like; Lysophospholipid acyltransferase (LPLAT) superfamily member: acyltransferases of de novo and remodeling pathways of glycerophospholipid biosynthesis which catalyze the incorporation of an acyl group from either acylCoAs or acyl-acyl carrier proteins (acylACPs) into acceptors such as glycerol 3-phosphate, dihydroxyacetone phosphate or lyso-phosphatidic acid. Included in this suubgroup are such LPLATs as 2-acylglycerol O-acyltransferase (MGAT), and similar proteins.


Pssm-ID: 153249 [Multi-domain]  Cd Length: 212  Bit Score: 59.99  E-value: 4.21e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524484190 444 EHRNLEQIPDEGAALLVCNH-VSFVDALLIGGAVR-----RPIRFVMYYKIYRLPVLNFIFRTAGAIPIAGRHediqiye 517
Cdd:cd07987     9 EVRGLENIPDEGPALLVHPHgGLPIDGALLAAAFLllfpgRLPRALADHFLFPLPGLRDLLRRLGAVPGSREN------- 81
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1524484190 518 kaftrIAKYLKDGELVCIFPEG----KLTGDGEMN---EFRGGVTRILEETPVPVIPMALQG 572
Cdd:cd07987    82 -----CVRLLREGELVLIFPGGareaLKSKREEYYllwKKRKGFARLALRAGAPIVPVFTFG 138
LPLAT_LPCAT1-like cd07991
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: LPCAT1-like; ...
429-571 3.62e-08

Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: LPCAT1-like; Lysophospholipid acyltransferase (LPLAT) superfamily member: acyltransferases of de novo and remodeling pathways of glycerophospholipid biosynthesis which catalyze the incorporation of an acyl group from either acylCoAs or acyl-acyl carrier proteins (acylACPs) into acceptors such as glycerol 3-phosphate, dihydroxyacetone phosphate or lyso-phosphatidic acid. Included in this subgroup are such LPLATs as lysophosphatidylcholine acyltransferase 1 (LPCAT-1), glycerol-3-phosphate acyltransferase 3 (GPAT3), and similar sequences.


Pssm-ID: 153253 [Multi-domain]  Cd Length: 211  Bit Score: 54.15  E-value: 3.62e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524484190 429 MRFMIWLLSHsmYRVEHRNlEQIPDEGAALLVCNHVSFVDALLIggAVRRPIRFVMYYKIYRLPVLNFIFRTAGAIPIaG 508
Cdd:cd07991     1 ARVLLFAFGF--YVIKVHG-KPDPPEAPRIIVANHTSFIDPLIL--FSDLFPSIVAKKELGKLPFIGTILRALGCIFV-D 74
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1524484190 509 RhEDIQIYEKAFTRIAKYLKDGEL--VCIFPEGKLT-GDGEMnEFRGGVTrileETPVPVIPMALQ 571
Cdd:cd07991    75 R-SEPKDRKKVVEEIKERATDPNWppILIFPEGTTTnGKALI-MFKKGAF----EPGVPVQPVAIR 134
MFS_MdtG_SLC18_like cd17325
bacterial MdtG-like and eukaryotic solute carrier 18 (SLC18) family of the Major Facilitator ...
86-424 7.17e-08

bacterial MdtG-like and eukaryotic solute carrier 18 (SLC18) family of the Major Facilitator Superfamily of transporters; This family is composed of eukaryotic solute carrier 18 (SLC18) family transporters and related bacterial multidrug resistance (MDR) transporters including several proteins from Escherichia coli such as multidrug resistance protein MdtG, from Bacillus subtilis such as multidrug resistance proteins 1 (Bmr1) and 2 (Bmr2), and from Staphylococcus aureus such as quinolone resistance protein NorA. The family also includes Escherichia coli arabinose efflux transporters YfcJ and YhhS. MDR transporters are drug/H+ antiporters (DHA) that mediate the efflux of a variety of drugs and toxic compounds, and confer resistance to these compounds. The SLC18 transporter family includes vesicular monoamine transporters (VAT1 and VAT2), vesicular acetylcholine transporter (VAChT), and SLC18B1, which is proposed to be a vesicular polyamine transporter (VPAT). The MdtG/SLC18 family belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.


Pssm-ID: 340883 [Multi-domain]  Cd Length: 375  Bit Score: 54.89  E-value: 7.17e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524484190  86 RAIKLGEIVIMAVGATGFLFDHLELMLLALFAMGTHSALFGPVKYSIMPQALHDDELVGGNGLVEMGTFLAILAGTIGAG 165
Cdd:cd17325    62 RLLLLGLLLLAVSTLLFAFATSYWQLLLARFLQGLASAAVWPAAMALIADIAPPEERGRAMGIFSSAIGLGFLIGPLLGG 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524484190 166 IMMSSTHYAPVVAVAIVGVALLGYLASRSIPRAAASTPQLRLDWNIFTQSWATLRMGlgqtPAVSRSIVGNSWFWFVGAI 245
Cdd:cd17325   142 LLADALGYRAPFLVCAALALLALVLALLLLPEPRPPPNKRAVSAARLRSGLRLLLRD----RRLLALFLAIFVLAFAFGA 217
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524484190 246 YLTQIPAYAKEWLYGDETVVTLILTVFSVGIALGSMLCEKLSGRKVEIGLVPFGSFgLTVFGLLLWWHSGGFvqnvqpnd 325
Cdd:cd17325   218 LEPFLPLYAAELGGLSPAQIGLLFGAQGLASALSQPPAGKLSDRIGRKPLILIGLL-LSAVALLLLPLATSF-------- 288
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524484190 326 wlavlgygqaWWVLFDILGLGVFGGFYIVPLYALIQSRTAENQRARVIAANNILNALFMVVSAIVSILLlsVAKLSIPEL 405
Cdd:cd17325   289 ----------WLLLLLLALLGLGLGLVFPATLALLADIVPPEGRGTAMGLFNTAFSLGMVLGPLLGGFL--YDAFGFATP 356
                         330
                  ....*....|....*....
gi 1524484190 406 FLVVSLLNIAVNTYIFRIV 424
Cdd:cd17325   357 FLAAAALLLLAAVLFLLLR 375
MFS cd06174
Major Facilitator Superfamily; The Major Facilitator Superfamily (MFS) is a large and diverse ...
86-414 4.12e-06

Major Facilitator Superfamily; The Major Facilitator Superfamily (MFS) is a large and diverse group of secondary transporters that includes uniporters, symporters, and antiporters. MFS proteins facilitate the transport across cytoplasmic or internal membranes of a variety of substrates including ions, sugar phosphates, drugs, neurotransmitters, nucleosides, amino acids, and peptides. They do so using the electrochemical potential of the transported substrates. Uniporters transport a single substrate, while symporters and antiporters transport two substrates in the same or in opposite directions, respectively, across membranes. MFS proteins are typically 400 to 600 amino acids in length, and the majority contain 12 transmembrane alpha helices (TMs) connected by hydrophilic loops. The N- and C-terminal halves of these proteins display weak similarity and may be the result of a gene duplication/fusion event. Based on kinetic studies and the structures of a few bacterial superfamily members, GlpT (glycerol-3-phosphate transporter), LacY (lactose permease), and EmrD (multidrug transporter), MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement. Bacterial members function primarily for nutrient uptake, and as drug-efflux pumps to confer antibiotic resistance. Some MFS proteins have medical significance in humans such as the glucose transporter Glut4, which is impaired in type II diabetes, and glucose-6-phosphate transporter (G6PT), which causes glycogen storage disease when mutated.


Pssm-ID: 349949 [Multi-domain]  Cd Length: 378  Bit Score: 49.35  E-value: 4.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524484190  86 RAIKLGEIVIMAVGATGFLFDHLELMLLALFAMGTHSALFGPVKYSIMPQALHDDELVGGNGLVEMGTFLAILAGTIGAG 165
Cdd:cd06174    62 PVLLLGLLLFALGALLFAFAPSFWLLLLGRFLLGLGSGLIDPAVLALIADLFPERERGRALGLLQAFGSVGGILGPLLGG 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524484190 166 IMMSSTHYAPVVAVAIVGVALLGYLASRSIPRAAASTPQLRLDWNIFTQSWATLRMGLGQTPAVSRSIVGNSWFWFVGAI 245
Cdd:cd06174   142 ILASSLGFGWRAVFLIAAALALLAAILLLLVVPDPPESARAKNEEASSKSVLKLLKRVLKNPGLWLLLLAIFLVNLAYYS 221
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524484190 246 YLTQIPAYAKEWLYGDETVVTLILTVFSVGIALGSMLCEKLSGRKVEIGLVPFGSFGLTVFGLLLWWHSggfvqnvqpnd 325
Cdd:cd06174   222 FSTLLPLFLLDLGGLSVAVAGLLLSLFGLAGALGSLLLGLLSDRLIGRKPLLLIGLLLMALGLALLLLA----------- 290
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524484190 326 wlavlgyGQAWWVLFDILGLGVFGGFYIVPLYALIQSRTAENQRARVIAANNILNALFMVVSAIVSILLLsVAKLSIPEL 405
Cdd:cd06174   291 -------PSLLLLLLLLLLLGFGLGGLLPLSFALIAELFPPEIRGTAFGLLNTFGFLGGAIGPLLAGFLL-AATFGLTGA 362

                  ....*....
gi 1524484190 406 FLVVSLLNI 414
Cdd:cd06174   363 FLVLAVLLL 371
MFS_1 pfam07690
Major Facilitator Superfamily;
93-388 6.70e-06

Major Facilitator Superfamily;


Pssm-ID: 429598 [Multi-domain]  Cd Length: 344  Bit Score: 48.57  E-value: 6.70e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524484190  93 IVIMAVGATGFLFDH-LELMLLALFAMGTHSALFGPVKYSIMPQALHDDELVGGNGLVEMGTFLAILAGTIGAGIMMSST 171
Cdd:pfam07690  69 LLLFALGLLLLLFASsLWLLLVLRVLQGLGAGALFPAALALIADWFPPEERGRALGLVSAGFGLGAALGPLLGGLLASLF 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524484190 172 HYAPVVAVAIVGVALLGYLASRSIPRAAASTP-QLRLDWNIFTQSWATLRmglgqTPAVSRSIVGNSWFWFVGAIYLTQI 250
Cdd:pfam07690 149 GWRAAFLILAILSLLAAVLLLLPRPPPESKRPkPAEEARLSLIVAWKALL-----RDPVLWLLLALLLFGFAFFGLLTYL 223
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524484190 251 PAYAKEwLYGDETVVTLILTVFSVGIALGSMLCEKLSGRKVEIGLVPFGSFGLTVFGLLLWWhsggfvqnvqpndwlaVL 330
Cdd:pfam07690 224 PLYQEV-LGLSALLAGLLLGLGGLLGAIGRLLLGRLSDRLGRRRRLLLALLLLILAALGLLL----------------LS 286
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1524484190 331 GYGQAWWVLFDILGLGVFGGFYIVPLYALIQSRTAENQRARVIAANNILNALFMVVSA 388
Cdd:pfam07690 287 LTLSSLWLLLALLLLGFGFGLVFPALNALVSDLAPKEERGTASGLYNTAGSLGGALGP 344
LPLAT_ACT14924-like cd07986
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: Unknown ...
441-572 8.35e-06

Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: Unknown ACT14924; Lysophospholipid acyltransferase (LPLAT) superfamily member: acyltransferases of de novo and remodeling pathways of glycerophospholipid biosynthesis which catalyze the incorporation of an acyl group from either acylCoAs or acyl-acyl carrier proteins (acylACPs) into acceptors such as glycerol 3-phosphate, dihydroxyacetone phosphate or lyso-phosphatidic acid. Included in this subgroup are uncharacterized phospholipid/glycerol acyltransferases such as the Pectobacterium carotovorum subsp. carotovorum PC1 locus ACT14924 putative acyltransferase, and similar proteins.


Pssm-ID: 153248 [Multi-domain]  Cd Length: 210  Bit Score: 47.24  E-value: 8.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524484190 441 YRVEHRNLEQIPDEGAALLVCNH-VSFVDALLIG---GAVRRPIRFVMYYKIYRLPVLNFIFrtagaIPIAGRHEDIQIY 516
Cdd:cd07986     8 LEVDVSGLENIPKDGPVVIVANHpFGILDGLILAdllGSVRPDVRILANQLLSKIPELRDLF-----IPVDPLEGRAALA 82
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1524484190 517 EKAFTR--IAKYLKDGELVCIFPEGKLTgdgEMNEFRGGVT---------RILEETPVPVIPMALQG 572
Cdd:cd07986    83 KNRESLreALRHLKNGGALIIFPAGRVS---TASPPFGRVSdrpwnpfvaRLARKAKAPVVPVYFSG 146
PRK08043 PRK08043
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
430-591 8.44e-06

bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;


Pssm-ID: 181207 [Multi-domain]  Cd Length: 718  Bit Score: 48.94  E-value: 8.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524484190 430 RFMIWLLSHsMYRVEHRNLEQIPDEGAALLVCNHVSFVDALLIggAVRRPIR--FVMYYKIYRLPVLNFIFRTAGAIPIA 507
Cdd:PRK08043    4 SFFRNLFRV-LYRVRVTGDTQALKGERVLITPNHVSFLDGILL--ALFLPVRpvFAVYTSISQQWYMRWLKPYIDFVPLD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524484190 508 GRHediqiyEKAFTRIAKYLKDGELVCIFPEGKLTGDGEMNEFRGGVTRILEETPVPVIPMALQGLWGSFFSRdpDKGLF 587
Cdd:PRK08043   81 PTK------PMAIKHLVRLVEQGRPVVIFPEGRITVTGSLMKIYDGAGFVAAKSGATVIPVRIEGAELTHFSR--LKGLV 152

                  ....
gi 1524484190 588 HRIW 591
Cdd:PRK08043  153 KRRL 156
COG3176 COG3176
Putative hemolysin [General function prediction only];
441-578 1.17e-05

Putative hemolysin [General function prediction only];


Pssm-ID: 442409  Cd Length: 270  Bit Score: 47.34  E-value: 1.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524484190 441 YRVEHRNLEQIPDEGAALLVCNH-VSFVDALLIG---GAVRRPIRFVMYYKIYRLPvlnFIFRTAGAIPIAGRHediqiy 516
Cdd:COG3176    57 LEVPEGDLDRIDADGHLLVVANHpLGILDGLALLklvGTVRPDYRILANDLALRIP---GGFYSELEFPVDPFN------ 127
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1524484190 517 EKAFTRIAKYLKDGELVCIFPEGKLTGDGEMNE--FRGGVTRILEETPVPVIPMALQGLWGSFF 578
Cdd:COG3176   128 LETLKAARRHLLEGGRSCVFPAGRVSGARRVIDllWSGLAAKLARKAGAPVVPVYFDGRNSGLF 191
MFS_arabinose_efflux_permease_like cd17473
Putative arabinose efflux permease family transporters of the Major Facilitator Superfamily; ...
248-416 3.08e-04

Putative arabinose efflux permease family transporters of the Major Facilitator Superfamily; This family includes a group of putative arabinose efflux permease family transporters, such as alpha proteobacterium quinolone resistance protein NorA (characterized Staphylococcus aureus Quinolone resistance protein NorA belongs to a different group), Desulfovibrio dechloracetivorans bacillibactin exporter, Vibrio aerogenes antiseptic resistance protein. The biological function of those transporters remain unclear. They belong to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.


Pssm-ID: 341026 [Multi-domain]  Cd Length: 374  Bit Score: 43.33  E-value: 3.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524484190 248 TQIPAYAKEWLYGDETVVTLILTVFSVGIALGSMLCEKLSGRKVEIGLVPFGsFGLTVFGLLLWWHSGGFvqnvqpndwl 327
Cdd:cd17473   218 IQLPFLLQERGGGSAALIGLALAIASLAGAIGALLFGRLKRRLGKRRLLAIG-FALMALGFLLLALASGL---------- 286
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524484190 328 avlgygqaWWVLFDILGLGVFGGFYIVPLYALIQSRTAENQRARVIAANNILNALFMVVSAIVSILLLSVAkLSIPELFL 407
Cdd:cd17473   287 --------WVVLLGAILAGLGFGLLLPTLNSWAMSLVPPELRGRAMGIVTSAFFLGQFLSPLVLGPLVNLT-GGLSGAFL 357

                  ....*....
gi 1524484190 408 VVSLLNIAV 416
Cdd:cd17473   358 ILGVLALVL 366
MelB COG2211
Na+/melibiose symporter or related transporter [Carbohydrate transport and metabolism];
239-398 4.23e-04

Na+/melibiose symporter or related transporter [Carbohydrate transport and metabolism];


Pssm-ID: 441813 [Multi-domain]  Cd Length: 447  Bit Score: 42.97  E-value: 4.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524484190 239 FWFVGAIYLTQIPAYAKEWLYGDETVVTLILTVFSVGIALGSMLCEKLSGRkveiglvpFGSFGLTVFGLLLWwhSGGFV 318
Cdd:COG2211   240 FFLALALVAALLLYYFKYVLGLSAALVGLLLALYFLAALLGAPLWPRLAKR--------FGKKKAFIIGLLLA--ALGLL 309
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524484190 319 qnvqpndWLAVLGYGQAWWVLFDILGLGVFGGFYIVPLYALI-------QSRTAENQRARVIAANNILNALFMVVSAIVS 391
Cdd:COG2211   310 -------LLFFLGPGNLWLLLVLAALAGIGLGAILVLPWAMLadvvdydEWKTGRRREGLYFGIFTFAIKLGQALAGALA 382

                  ....*..
gi 1524484190 392 ILLLSVA 398
Cdd:COG2211   383 GLLLALF 389
AraJ COG2814
Predicted arabinose efflux permease AraJ, MFS family [Carbohydrate transport and metabolism];
233-426 4.29e-04

Predicted arabinose efflux permease AraJ, MFS family [Carbohydrate transport and metabolism];


Pssm-ID: 442063 [Multi-domain]  Cd Length: 348  Bit Score: 43.04  E-value: 4.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524484190 233 IVGNSWFWFVGAIYLTQIPAYAKEwLYGDETVVTLILTVFSVGIALGSMLCEKLSGRKVEIGLVPFGSFGLTVFGLLLww 312
Cdd:COG2814    16 ALGAFLSGLGIGIVLPALPLIAAD-LGASPAQAGLVVTAYLLGAALGAPLAGRLADRFGRRRVLLLGLLLFALGSLLC-- 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524484190 313 hsgGFVQNVqpndwlavlgygqaWWVLFDILGLGVFGGFYIVPLYALIQSRTAENQRARVIAANNILNALFMVVSAIVSI 392
Cdd:COG2814    93 ---ALAPSL--------------WLLLAARFLQGLGAGALFPAALALIADLVPPERRGRALGLLGAGLGLGPALGPLLGG 155
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1524484190 393 LLLSVakLSIPELFLVVSLLNIAVNTYIFRIVPE 426
Cdd:COG2814   156 LLADL--FGWRWVFLVNAVLALLALLLLLRLLPE 187
MFS_1 pfam07690
Major Facilitator Superfamily;
239-426 4.11e-03

Major Facilitator Superfamily;


Pssm-ID: 429598 [Multi-domain]  Cd Length: 344  Bit Score: 39.71  E-value: 4.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524484190 239 FWFVGAIYLTQIPAYAKEWLYGDETVVTLILTVFSVGIALGSMLCEKLSGRkveIGLVPFGSFGLTVFGLLLWWhsGGFV 318
Cdd:pfam07690   8 AALGRSLLGPALPLLLAEDLGISPTEIGLLLTLFSLGYALAQPLAGRLSDR---FGRRRVLLIGLLLFALGLLL--LLFA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524484190 319 QNVqpndwlavlgygqaWWVLFDILGLGVFGGFYIVPLYALIQSRTAENQRARVIAANNILNALFMVVSAIVSILLLSVa 398
Cdd:pfam07690  83 SSL--------------WLLLVLRVLQGLGAGALFPAALALIADWFPPEERGRALGLVSAGFGLGAALGPLLGGLLASL- 147
                         170       180
                  ....*....|....*....|....*...
gi 1524484190 399 kLSIPELFLVVSLLNIAVNTYIFRIVPE 426
Cdd:pfam07690 148 -FGWRAAFLILAILSLLAAVLLLLPRPP 174
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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