NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|489182154|ref|WP_003091605|]
View 

MULTISPECIES: MFS transporter [Pseudomonas]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
PRK06814 super family cl35510
acyl-[ACP]--phospholipid O-acyltransferase;
6-594 9.54e-164

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


The actual alignment was detected with superfamily member PRK06814:

Pssm-ID: 235865 [Multi-domain]  Cd Length: 1140  Bit Score: 498.34  E-value: 9.54e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182154    6 QFALLGKRRFLPFFITQLLGAFNDNIFKQSLILAILYHLSVSGDRS--LLVNLCALLFILPFFLFSALGGQFGEKYNKDA 83
Cdd:PRK06814    4 KLYLMKSRRFAPLFWTQFFGAFNDNFLKNALVILILYGLSGALGAYnnALVTLAGAVFILPFFIFSALAGQLADKYDKAK 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182154   84 LMRALKLAEVGIMLVGAAGFVFGSLPLMFVALFAMGTHSALFGPVKYSILPQHLHEDELVGGNALVEMGTFLAILAGTIG 163
Cdd:PRK06814   84 LAKILKFAEIGIAALAIYGFHLNSVPLLFAALFLMGIHSALFGPIKYSILPDHLNKDELLGANALVEAGTFIAILLGTII 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182154  164 AGVLMSHAHYAAAVATAVVLVAACgYLASRGIPRAAAALPGLKLDWNIFAQSWSILRLgLGQRPAVSRSLVGNSWFWFLG 243
Cdd:PRK06814  164 GGLATISGNFVILVALLMGIAVLG-WLASLFIPKTGNAAPDLKIDRNIIRSTITLLKY-AKADKRIWLAILGISWFWLVG 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182154  244 AVYLTQIPTFAKEWLHGDESVVTLILTVFSVGIALGSMLCEKLSGRKVEIGLVPFGSIGLTVFGILLWWHAGGIPPGEA- 322
Cdd:PRK06814  242 AVVLSQLPLLAKETLGGDENVATLFLAVFSVGVAVGSFLASKLSEGRITLLYVPIGALLMGLFGLDLAFASSSVPAEPAq 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182154  323 PYDWLAVLRHHETWAVLADILFIGIFGGFYIVPLYALIQARTDEDKRARVIAANNILNALFMVAAAL-VSILFLsvAKLS 401
Cdd:PRK06814  322 LKSILVFLSKRHGWRILIDLFGLAAAGGLYIVPLFAALQAWANPAHRARVIAANNVLNAAFMVAGTIiLALLQA--LGFS 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182154  402 IPQLFLALSLMNVAVNVYIFKIVPEFTMRFLVWLLSHTMYRVRHVNLEAIPDEG-AAVLVCNHVSYVDALLIAGSIRRPV 480
Cdd:PRK06814  400 IPWIILFIALANLIVAILILRLLPTNLLRDIFSILFRAFYRVEVKGLENLQKAGkKAVIAANHVSFLDGPLLAAYLPEEP 479
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182154  481 RFVMYYRI----FSLPVLnfvfRTAGAVPI------AARHedegiyerafqrIADYLRDGELVCIFPEGKLTADGEMNEF 550
Cdd:PRK06814  480 TFAIDTDIakawWVKPFL----KLAKALPVdptnpmATRT------------LIKEVQKGEKLVIFPEGRITVTGSLMKI 543
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....
gi 489182154  551 RAGIERIIEETPVPVIPMALQGLWGSFFSRDPNKgFFRRLWSRV 594
Cdd:PRK06814  544 YDGPGMIADKAGAMVVPVRIDGLQFTHFSRLKNQ-VRRKWFPKV 586
 
Name Accession Description Interval E-value
PRK06814 PRK06814
acyl-[ACP]--phospholipid O-acyltransferase;
6-594 9.54e-164

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


Pssm-ID: 235865 [Multi-domain]  Cd Length: 1140  Bit Score: 498.34  E-value: 9.54e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182154    6 QFALLGKRRFLPFFITQLLGAFNDNIFKQSLILAILYHLSVSGDRS--LLVNLCALLFILPFFLFSALGGQFGEKYNKDA 83
Cdd:PRK06814    4 KLYLMKSRRFAPLFWTQFFGAFNDNFLKNALVILILYGLSGALGAYnnALVTLAGAVFILPFFIFSALAGQLADKYDKAK 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182154   84 LMRALKLAEVGIMLVGAAGFVFGSLPLMFVALFAMGTHSALFGPVKYSILPQHLHEDELVGGNALVEMGTFLAILAGTIG 163
Cdd:PRK06814   84 LAKILKFAEIGIAALAIYGFHLNSVPLLFAALFLMGIHSALFGPIKYSILPDHLNKDELLGANALVEAGTFIAILLGTII 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182154  164 AGVLMSHAHYAAAVATAVVLVAACgYLASRGIPRAAAALPGLKLDWNIFAQSWSILRLgLGQRPAVSRSLVGNSWFWFLG 243
Cdd:PRK06814  164 GGLATISGNFVILVALLMGIAVLG-WLASLFIPKTGNAAPDLKIDRNIIRSTITLLKY-AKADKRIWLAILGISWFWLVG 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182154  244 AVYLTQIPTFAKEWLHGDESVVTLILTVFSVGIALGSMLCEKLSGRKVEIGLVPFGSIGLTVFGILLWWHAGGIPPGEA- 322
Cdd:PRK06814  242 AVVLSQLPLLAKETLGGDENVATLFLAVFSVGVAVGSFLASKLSEGRITLLYVPIGALLMGLFGLDLAFASSSVPAEPAq 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182154  323 PYDWLAVLRHHETWAVLADILFIGIFGGFYIVPLYALIQARTDEDKRARVIAANNILNALFMVAAAL-VSILFLsvAKLS 401
Cdd:PRK06814  322 LKSILVFLSKRHGWRILIDLFGLAAAGGLYIVPLFAALQAWANPAHRARVIAANNVLNAAFMVAGTIiLALLQA--LGFS 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182154  402 IPQLFLALSLMNVAVNVYIFKIVPEFTMRFLVWLLSHTMYRVRHVNLEAIPDEG-AAVLVCNHVSYVDALLIAGSIRRPV 480
Cdd:PRK06814  400 IPWIILFIALANLIVAILILRLLPTNLLRDIFSILFRAFYRVEVKGLENLQKAGkKAVIAANHVSFLDGPLLAAYLPEEP 479
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182154  481 RFVMYYRI----FSLPVLnfvfRTAGAVPI------AARHedegiyerafqrIADYLRDGELVCIFPEGKLTADGEMNEF 550
Cdd:PRK06814  480 TFAIDTDIakawWVKPFL----KLAKALPVdptnpmATRT------------LIKEVQKGEKLVIFPEGRITVTGSLMKI 543
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....
gi 489182154  551 RAGIERIIEETPVPVIPMALQGLWGSFFSRDPNKgFFRRLWSRV 594
Cdd:PRK06814  544 YDGPGMIADKAGAMVVPVRIDGLQFTHFSRLKNQ-VRRKWFPKV 586
MFS_MefA_like cd06173
Macrolide efflux protein A and similar proteins of the Major Facilitator Superfamily of ...
15-423 1.61e-51

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: 182.04  E-value: 1.61e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182154  15 FLPFFITQLLGAFNDNIFKQSLILAILYHlsvsGDRSLLVNLCALLFILPFFLFSALGGQFGEKYNKDALMRALKLAEVG 94
Cdd:cd06173    1 FRLLWLAQLLSALGDWIFTVALPWLVLQL----TGSALLVGLVLAAFFLPFLLFSPFAGVLADRFDRRRLLILADLLRAL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182154  95 IMLVGAAGFVFG--SLPLMFVALFAMGTHSALFGPVKYSILPQHLHEDELVGGNALVEMGTFLAILAGTIGAGVLMSHAH 172
Cdd:cd06173   77 LAAVLALLALLGslSLWLLLVLAFLLGIASAFFGPARQALLPELVPKEQLVRANALNSLATQLARIIGPALGGLLVALLG 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182154 173 yAAAVATAVVLVAACGYLASRGIPRAAAALPGLKLDWNIfaQSWSILRLGLGQRPAVSRSLVGNSWFWFLGAVYLTQIPT 252
Cdd:cd06173  157 -PGGAFAINALSFLLSALLLLFIRRPPPAAPGESSSLLL--RDLREGLRYLRRSPLLRLLLLALALFALLGGALTVLLPL 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182154 253 FAKEWLHGDESVVTLILTVFSVGIALGSMLCEKLSGRKVEIGLVPFGSIGLTVFGILLWWhaggippgeapydwlavlrH 332
Cdd:cd06173  234 LAKEVLGGGAAGYGLLLAAFGVGALLGALLLGRLSKRRRRGRLLLIGALLLGLALLVLGL-------------------S 294
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182154 333 HETWAVLADILFIGIFGGFYIVPLYALIQARTDEDKRARVIAANNILNALFMVAAALVSILFLsvAKLSIPQLFLALSLM 412
Cdd:cd06173  295 PSLWLLLAALFLLGLAGGLFNVPLNTLLQLRVPDELRGRVFSVYNALNSGAMPLGALLAGLLA--DALGLSAVFLLAGAL 372
                        410
                 ....*....|.
gi 489182154 413 NVAVNVYIFKI 423
Cdd:cd06173  373 LLLAALLLLLL 383
PlsC COG0204
1-acyl-sn-glycerol-3-phosphate acyltransferase [Lipid transport and metabolism]; ...
429-624 8.04e-41

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: 147.85  E-value: 8.04e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182154 429 MRFLVWLLSHTM-YRVRHVNLEAIPDEGAAVLVCNHVSYVDALLIAGSIRRPVRFVMYYRIFSLPVLNFVFRTAGAVPI- 506
Cdd:COG0204   16 VRLWARLLLRLLgVRVRVEGLENLPADGPVLIVANHQSWLDILLLLAALPRPVRFVAKKELFKIPLLGWLLRALGAIPVd 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182154 507 -AARHEDegiyERAFQRIADYLRDGELVCIFPEGKLTADGEMNEFRAGIERIIEETPVPVIPMALQGLWGSFFsrdpnKG 585
Cdd:COG0204   96 rSKRRAA----LRALRQAVEALKAGESLVIFPEGTRSPDGRLLPFKTGAARLALEAGVPIVPVAIDGTERALP-----KG 166
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 489182154 586 FFRRLwSRVSLVAGESVAPGAVERLD-------LQARVTSLRGEAR 624
Cdd:COG0204  167 FLPRP-GKVTVRIGPPIDPSDLEGEDrrelaerLRAAIEALLAELR 211
Acyltransferase pfam01553
Acyltransferase; This family contains acyltransferases involved in phospholipid biosynthesis ...
442-570 6.83e-25

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: 100.05  E-value: 6.83e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182154  442 RVRHVNLEAIPDEGAAVLVCNHVSYVDALL---IAGSIRRPVRFVMYYRIFSLPVLNFVFRTAGAVPIaaRHEDEGIYER 518
Cdd:pfam01553   1 RIEVHGLENLPRGGPAIVVANHQSYLDVLLlslALYKRGRPLVFVAKKELFDIPLVGWLMRLLGCIFI--DRKNRKDAAG 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 489182154  519 AFQRIADYLRDGELVCIFPEGKLTADGEMNEFRAGIERIIEETPVPVIPMAL 570
Cdd:pfam01553  79 TLEYLVELLREGKLVVIFPEGTRSREGELLPFKKGAFRLAIEAGVPIVPVAI 130
PlsC smart00563
Phosphate acyltransferases; Function in phospholipid biosynthesis and have either ...
457-573 2.76e-24

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: 98.20  E-value: 2.76e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182154   457 AVLVCNHVSYVDALL---IAGSIRRPVRFVMYYRIFSLPVLNFVFRTAGAVPIaaRHEDEGIYERAFQRIADYLRDGELV 533
Cdd:smart00563   1 ALVVANHQSFLDPLVlsaLLPRKLGRVRFVAKKELFYVPLLGWLLRLLGAIFI--DRSNGRKARAALREAVELLKEGEWL 78
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 489182154   534 CIFPEGKLTADGEMNEFRAGIERIIEETPVPVIPMALQGL 573
Cdd:smart00563  79 LIFPEGTRSRPGKLLPFKKGAARLALEAGVPIVPVAIRGT 118
AGP_acyltrn TIGR00530
1-acyl-sn-glycerol-3-phosphate acyltransferases; This model describes the core homologous ...
443-571 1.81e-17

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: 78.93  E-value: 1.81e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182154  443 VRHVNLEAIPDEGAAVLVCNHVSYVDALLIAGSIRRPVRFVMYYRIFSLPVLNFVFRTAGAVPIaARHEDEGI--YERAF 520
Cdd:TIGR00530   4 VEVVGPENLPAKSPVLVVANHQSNLDPLTLSAAFPPPIVFIAKKELKWIPFFGIMLWLTGAIFI-DRENIRAIatALKAA 82
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 489182154  521 QRIadyLRDGELVCIFPEGKLTADGEMNEFRAGIERIIEETPVPVIPMALQ 571
Cdd:TIGR00530  83 IEV---LKQGRSIGVFPEGTRSRGRDILPFKKGAFHIAIKAGVPILPVVLS 130
 
Name Accession Description Interval E-value
PRK06814 PRK06814
acyl-[ACP]--phospholipid O-acyltransferase;
6-594 9.54e-164

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


Pssm-ID: 235865 [Multi-domain]  Cd Length: 1140  Bit Score: 498.34  E-value: 9.54e-164
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182154    6 QFALLGKRRFLPFFITQLLGAFNDNIFKQSLILAILYHLSVSGDRS--LLVNLCALLFILPFFLFSALGGQFGEKYNKDA 83
Cdd:PRK06814    4 KLYLMKSRRFAPLFWTQFFGAFNDNFLKNALVILILYGLSGALGAYnnALVTLAGAVFILPFFIFSALAGQLADKYDKAK 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182154   84 LMRALKLAEVGIMLVGAAGFVFGSLPLMFVALFAMGTHSALFGPVKYSILPQHLHEDELVGGNALVEMGTFLAILAGTIG 163
Cdd:PRK06814   84 LAKILKFAEIGIAALAIYGFHLNSVPLLFAALFLMGIHSALFGPIKYSILPDHLNKDELLGANALVEAGTFIAILLGTII 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182154  164 AGVLMSHAHYAAAVATAVVLVAACgYLASRGIPRAAAALPGLKLDWNIFAQSWSILRLgLGQRPAVSRSLVGNSWFWFLG 243
Cdd:PRK06814  164 GGLATISGNFVILVALLMGIAVLG-WLASLFIPKTGNAAPDLKIDRNIIRSTITLLKY-AKADKRIWLAILGISWFWLVG 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182154  244 AVYLTQIPTFAKEWLHGDESVVTLILTVFSVGIALGSMLCEKLSGRKVEIGLVPFGSIGLTVFGILLWWHAGGIPPGEA- 322
Cdd:PRK06814  242 AVVLSQLPLLAKETLGGDENVATLFLAVFSVGVAVGSFLASKLSEGRITLLYVPIGALLMGLFGLDLAFASSSVPAEPAq 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182154  323 PYDWLAVLRHHETWAVLADILFIGIFGGFYIVPLYALIQARTDEDKRARVIAANNILNALFMVAAAL-VSILFLsvAKLS 401
Cdd:PRK06814  322 LKSILVFLSKRHGWRILIDLFGLAAAGGLYIVPLFAALQAWANPAHRARVIAANNVLNAAFMVAGTIiLALLQA--LGFS 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182154  402 IPQLFLALSLMNVAVNVYIFKIVPEFTMRFLVWLLSHTMYRVRHVNLEAIPDEG-AAVLVCNHVSYVDALLIAGSIRRPV 480
Cdd:PRK06814  400 IPWIILFIALANLIVAILILRLLPTNLLRDIFSILFRAFYRVEVKGLENLQKAGkKAVIAANHVSFLDGPLLAAYLPEEP 479
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182154  481 RFVMYYRI----FSLPVLnfvfRTAGAVPI------AARHedegiyerafqrIADYLRDGELVCIFPEGKLTADGEMNEF 550
Cdd:PRK06814  480 TFAIDTDIakawWVKPFL----KLAKALPVdptnpmATRT------------LIKEVQKGEKLVIFPEGRITVTGSLMKI 543
                         570       580       590       600
                  ....*....|....*....|....*....|....*....|....
gi 489182154  551 RAGIERIIEETPVPVIPMALQGLWGSFFSRDPNKgFFRRLWSRV 594
Cdd:PRK06814  544 YDGPGMIADKAGAMVVPVRIDGLQFTHFSRLKNQ-VRRKWFPKV 586
PRK08633 PRK08633
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
9-593 1.21e-142

2-acyl-glycerophospho-ethanolamine acyltransferase; Validated


Pssm-ID: 236315 [Multi-domain]  Cd Length: 1146  Bit Score: 443.21  E-value: 1.21e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182154    9 LLGKRRFLPFFITQLLGAFNDNIFKqSLILAILYHlSVSGDRSLLVNLCALLFILP-FFLFSALGGQFGEKYNKDALMRA 87
Cdd:PRK08633    5 LLKIIGFLPLLLTQFLNAFNDLGHK-ILIQNTLIK-AYDGSEQVILTAIVNALFLLpFLLLSSPAGFLADKFSKNRVIRI 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182154   88 LKLAEVGIMLVGAAGFVFGSLPLMFVALFAMGTHSALFGPVKYSILPQHLHEDELVGGNALVEMGTFLAILAGTIGAGVL 167
Cdd:PRK08633   83 VKLFEVGLTLLIVLAYYLGWFWLAFAVTFLLGAQSAIYSPAKYGIIPELVGKENLSRANGLLEAFTIVAILAGTALFSFL 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182154  168 MSHA---------HYAAAVATAVVLVAACGYLASRGIPR--AAAALPGLKLDWNIFAQSWSILRLGLGQRPaVSRSLVGN 236
Cdd:PRK08633  163 FESVngntpseilGRIAPAGLVLLAVAVLGLIFAYRLPKvpAAAPEVFDKKKYLFPKLLWRNLKLLRSDRV-LWLAIIGL 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182154  237 SWFWFLGAVYLTQIPTFAKEWLHGDES-VVTLILTVFSVGIALGSMLCEKLSGRKVEIGLVPFGSIGLTVFGILLWWhAG 315
Cdd:PRK08633  242 SYFWFISQLAQANFPAYAKEVLGLDNTfQVQYLLAASAIGIGIGSLLAGRLSGRHIELGLVPLGALGLALSLFLLPT-AP 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182154  316 GIppgeapydwlavlrhhetWAVLADILFIGIFGGFYIVPLYALIQARTDEDKRARVIAANNILNALFMVAAALVSILFl 395
Cdd:PRK08633  321 SL------------------ASVLVLFFLFGFSAGLFIVPLNALIQFRAPEKELGKVLAANNFLQNVGMLLFLALTTLF- 381
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182154  396 SVAKLSIPQLFLALSLMNVAVNVYIFKIVPEFTMRFLVWLLSHTMYRVRHVNLEAIPDEGAAVLVCNHVSYVDALLIAGS 475
Cdd:PRK08633  382 SGLGLSPAGLFYLIALVTLIGTLYTLLLLPDSLLRFLLLLLMHTRYRLRVEGRENIPAKGGALLLGNHVSWIDWALLQAA 461
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182154  476 IRRPVRFVMYYRIFSLPVLNFVFRTAGAVPIAARHEDEGIyerafQRIADYLRDGELVCIFPEGKLTADGEMNEFRAGIE 555
Cdd:PRK08633  462 SPRPIRFVMERSIYEKWYLKWFFKLFGVIPISSGGSKESL-----EFIRKALDDGEVVCIFPEGAITRNGQLNEFKRGFE 536
                         570       580       590
                  ....*....|....*....|....*....|....*...
gi 489182154  556 RIIEETPVPVIPMALQGLWGSFFSRDpnKGFFRRLWSR 593
Cdd:PRK08633  537 LIVKGTDVPIIPFYIRGLWGSIFSRA--SGKFLWRWPT 572
MFS_MefA_like cd06173
Macrolide efflux protein A and similar proteins of the Major Facilitator Superfamily of ...
15-423 1.61e-51

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: 182.04  E-value: 1.61e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182154  15 FLPFFITQLLGAFNDNIFKQSLILAILYHlsvsGDRSLLVNLCALLFILPFFLFSALGGQFGEKYNKDALMRALKLAEVG 94
Cdd:cd06173    1 FRLLWLAQLLSALGDWIFTVALPWLVLQL----TGSALLVGLVLAAFFLPFLLFSPFAGVLADRFDRRRLLILADLLRAL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182154  95 IMLVGAAGFVFG--SLPLMFVALFAMGTHSALFGPVKYSILPQHLHEDELVGGNALVEMGTFLAILAGTIGAGVLMSHAH 172
Cdd:cd06173   77 LAAVLALLALLGslSLWLLLVLAFLLGIASAFFGPARQALLPELVPKEQLVRANALNSLATQLARIIGPALGGLLVALLG 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182154 173 yAAAVATAVVLVAACGYLASRGIPRAAAALPGLKLDWNIfaQSWSILRLGLGQRPAVSRSLVGNSWFWFLGAVYLTQIPT 252
Cdd:cd06173  157 -PGGAFAINALSFLLSALLLLFIRRPPPAAPGESSSLLL--RDLREGLRYLRRSPLLRLLLLALALFALLGGALTVLLPL 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182154 253 FAKEWLHGDESVVTLILTVFSVGIALGSMLCEKLSGRKVEIGLVPFGSIGLTVFGILLWWhaggippgeapydwlavlrH 332
Cdd:cd06173  234 LAKEVLGGGAAGYGLLLAAFGVGALLGALLLGRLSKRRRRGRLLLIGALLLGLALLVLGL-------------------S 294
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182154 333 HETWAVLADILFIGIFGGFYIVPLYALIQARTDEDKRARVIAANNILNALFMVAAALVSILFLsvAKLSIPQLFLALSLM 412
Cdd:cd06173  295 PSLWLLLAALFLLGLAGGLFNVPLNTLLQLRVPDELRGRVFSVYNALNSGAMPLGALLAGLLA--DALGLSAVFLLAGAL 372
                        410
                 ....*....|.
gi 489182154 413 NVAVNVYIFKI 423
Cdd:cd06173  373 LLLAALLLLLL 383
LPLAT_AGPAT-like cd07989
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: AGPAT-like; ...
429-615 6.80e-41

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: 147.03  E-value: 6.80e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182154 429 MRFLVWLLshtMYRVRHVNLEAIPDEGAAVLVCNHVSYVDALLIAGSIRRPVRFVMYYRIFSLPVLNFVFRTAGAVPIAa 508
Cdd:cd07989    1 LRLLLRLL---GVRVRVEGLENLPPKGPVIIVANHQSYLDPLVLGAALPRPIRFVAKKELFKIPFLGWLLRLLGAIPID- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182154 509 RhEDEGIYERAFQRIADYLRDGELVCIFPEGKLTADGEMNEFRAGIERIIEETPVPVIPMALQGLWGSFFsrdpnKGFFR 588
Cdd:cd07989   77 R-GNGRSAREALREAIEALKEGESVVIFPEGTRSRDGELLPFKSGAFRLAKEAGVPIVPVAISGTWGSLP-----KGKKL 150
                        170       180
                 ....*....|....*....|....*..
gi 489182154 589 RLWSRVSLVAGESVAPGAVERLDLQAR 615
Cdd:cd07989  151 PRPGRVTVRIGEPIPPEGLELAEEDRK 177
PlsC COG0204
1-acyl-sn-glycerol-3-phosphate acyltransferase [Lipid transport and metabolism]; ...
429-624 8.04e-41

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: 147.85  E-value: 8.04e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182154 429 MRFLVWLLSHTM-YRVRHVNLEAIPDEGAAVLVCNHVSYVDALLIAGSIRRPVRFVMYYRIFSLPVLNFVFRTAGAVPI- 506
Cdd:COG0204   16 VRLWARLLLRLLgVRVRVEGLENLPADGPVLIVANHQSWLDILLLLAALPRPVRFVAKKELFKIPLLGWLLRALGAIPVd 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182154 507 -AARHEDegiyERAFQRIADYLRDGELVCIFPEGKLTADGEMNEFRAGIERIIEETPVPVIPMALQGLWGSFFsrdpnKG 585
Cdd:COG0204   96 rSKRRAA----LRALRQAVEALKAGESLVIFPEGTRSPDGRLLPFKTGAARLALEAGVPIVPVAIDGTERALP-----KG 166
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 489182154 586 FFRRLwSRVSLVAGESVAPGAVERLD-------LQARVTSLRGEAR 624
Cdd:COG0204  167 FLPRP-GKVTVRIGPPIDPSDLEGEDrrelaerLRAAIEALLAELR 211
Acyltransferase pfam01553
Acyltransferase; This family contains acyltransferases involved in phospholipid biosynthesis ...
442-570 6.83e-25

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: 100.05  E-value: 6.83e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182154  442 RVRHVNLEAIPDEGAAVLVCNHVSYVDALL---IAGSIRRPVRFVMYYRIFSLPVLNFVFRTAGAVPIaaRHEDEGIYER 518
Cdd:pfam01553   1 RIEVHGLENLPRGGPAIVVANHQSYLDVLLlslALYKRGRPLVFVAKKELFDIPLVGWLMRLLGCIFI--DRKNRKDAAG 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 489182154  519 AFQRIADYLRDGELVCIFPEGKLTADGEMNEFRAGIERIIEETPVPVIPMAL 570
Cdd:pfam01553  79 TLEYLVELLREGKLVVIFPEGTRSREGELLPFKKGAFRLAIEAGVPIVPVAI 130
PlsC smart00563
Phosphate acyltransferases; Function in phospholipid biosynthesis and have either ...
457-573 2.76e-24

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: 98.20  E-value: 2.76e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182154   457 AVLVCNHVSYVDALL---IAGSIRRPVRFVMYYRIFSLPVLNFVFRTAGAVPIaaRHEDEGIYERAFQRIADYLRDGELV 533
Cdd:smart00563   1 ALVVANHQSFLDPLVlsaLLPRKLGRVRFVAKKELFYVPLLGWLLRLLGAIFI--DRSNGRKARAALREAVELLKEGEWL 78
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 489182154   534 CIFPEGKLTADGEMNEFRAGIERIIEETPVPVIPMALQGL 573
Cdd:smart00563  79 LIFPEGTRSRPGKLLPFKKGAARLALEAGVPIVPVAIRGT 118
LPLAT_AAK14816-like cd07992
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: Unknown ...
429-571 2.89e-18

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: 83.47  E-value: 2.89e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182154 429 MRFLVWLLSHTMYR-VRHVNLEAIPDEGAAVLVCNHV-SYVDALLIAGSIRRPVRFVMYYRIFSLPVLNFVFRTAGAVPI 506
Cdd:cd07992    1 VRLLSRVILRIYFRrITVVGRENVPKDGPVIFLGNHPnALIDPLLLAATLRRPVRFLAKADLFKNPLIGWLLESFGAIPV 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489182154 507 ------AARHEDEGIYERAFQRIADYLRDGELVCIFPEGKLTADGEMNEFRAGIERIIEE------TPVPVIPMALQ 571
Cdd:cd07992   81 yrpkdlARGGIGKISNAAVFDAVGEALKAGGAIGIFPEGGSHDRPRLLPLKAGAARMALEaleagqKDVKIVPVGLN 157
AGP_acyltrn TIGR00530
1-acyl-sn-glycerol-3-phosphate acyltransferases; This model describes the core homologous ...
443-571 1.81e-17

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: 78.93  E-value: 1.81e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182154  443 VRHVNLEAIPDEGAAVLVCNHVSYVDALLIAGSIRRPVRFVMYYRIFSLPVLNFVFRTAGAVPIaARHEDEGI--YERAF 520
Cdd:TIGR00530   4 VEVVGPENLPAKSPVLVVANHQSNLDPLTLSAAFPPPIVFIAKKELKWIPFFGIMLWLTGAIFI-DRENIRAIatALKAA 82
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 489182154  521 QRIadyLRDGELVCIFPEGKLTADGEMNEFRAGIERIIEETPVPVIPMALQ 571
Cdd:TIGR00530  83 IEV---LKQGRSIGVFPEGTRSRGRDILPFKKGAFHIAIKAGVPILPVVLS 130
PRK11195 PRK11195
lysophospholipid transporter LplT; Provisional
94-363 1.44e-14

lysophospholipid transporter LplT; Provisional


Pssm-ID: 236879 [Multi-domain]  Cd Length: 393  Bit Score: 76.03  E-value: 1.44e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182154  94 GIMLVGAAGFVFGSLPLMFVALFAMGthSALFGPVKYSILPQHLHEDELVGGNALVEMGTFLAILAGTIGAGVLMSHAHY 173
Cdd:PRK11195  76 GIKLLGCLLMLFGIHPLLAYGLVGIG--AAAYSPAKYGILTELLPGEKLVKANGWMEGSTIAAILLGTVLGGALADPHAE 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182154 174 AAAVATAVVLVAacGYLASRGIPRAAAALPGLKldWNI------FAQSWSIL-RLGLGQrpavsRSLVGNSWFWFLGAVY 246
Cdd:PRK11195 154 AALAVCALIYLL--AALFNLFIPRLGARRPGQS--WNPiallrdFFHACRVLwRDKLGR-----FSLAGTTLFWGAGATL 224
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182154 247 LTQIPTFAKEWLHGDESVVTLILTVFSVGIALGSMLCEKLSGRKVEIGLVPFG-SIGLTVFGILLwwhaggippgeapyd 325
Cdd:PRK11195 225 RFLVLAWAPVALGITLNQPAYLQAVVAIGIAVGAGAAARLVTLETVLRVLPAGiLMGLVVLLMAL--------------- 289
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 489182154 326 wlavlrHHETWAVLADILFIGIFGGFYIVPLYALIQAR 363
Cdd:PRK11195 290 ------QHSLLPAYPLLILIGALGGFFVVPMNALLQHR 321
AraJ COG2814
Predicted arabinose efflux permease AraJ, MFS family [Carbohydrate transport and metabolism];
95-387 2.07e-13

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


Pssm-ID: 442063 [Multi-domain]  Cd Length: 348  Bit Score: 71.93  E-value: 2.07e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182154  95 IMLVGAAGFVFGSL--------PLMFVALFAMGTHSALFGPVKYSILPQHLHEDELVGGNALVEMGTFLAILAGTIGAGV 166
Cdd:COG2814   77 VLLLGLLLFALGSLlcalapslWLLLAARFLQGLGAGALFPAALALIADLVPPERRGRALGLLGAGLGLGPALGPLLGGL 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182154 167 LMSHAHYAAAVATAVVLVAACGYLASRGIPRAAAALPGlkldwNIFAQSWSILRlglgqRPAVSRSLVGNSWFWFLGAVY 246
Cdd:COG2814  157 LADLFGWRWVFLVNAVLALLALLLLLRLLPESRPAARA-----RLRGSLRELLR-----RPRLLLLLLLAFLLGFGFFAL 226
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182154 247 LTQIPTFAKEWLHGDESVVTLILTVFSVGIALGSMLCEKLSGRkVEIGLVPFGSIGLTVFGILLWWHAGGIppgeapydw 326
Cdd:COG2814  227 FTYLPLYLQEVLGLSASAAGLLLALFGLGGVLGALLAGRLADR-FGRRRLLLIGLLLLALGLLLLALAGSL--------- 296
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489182154 327 lavlrhhetWAVLADILFIGIFGGFYIVPLYALIQARTDEDKRARVIAANNILNALFMVAA 387
Cdd:COG2814  297 ---------WLLLLALFLLGFGFGLLFPLLQALVAELAPPEARGRASGLYNSAFFLGGPLA 348
PLN02901 PLN02901
1-acyl-sn-glycerol-3-phosphate acyltransferase
441-572 3.64e-12

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


Pssm-ID: 215488 [Multi-domain]  Cd Length: 214  Bit Score: 65.91  E-value: 3.64e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182154 441 YRVRHVNLEAIP-DEGAAVLVCNHVSYVD--ALLiagSIRRPVRFVMYYRIFSLPVLNFVFRTAGAVPIaaRHEDEGIYE 517
Cdd:PLN02901  35 YKIEVEGLENLPsPDEPAVYVSNHQSFLDiyTLF---HLGRPFKFISKTSIFLIPIIGWAMYMTGHIPL--KRMDRRSQL 109
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 489182154 518 RAFQRIADYLRDGELVCIFPEGKLTADGEMNEFRAGIERIIEETPVPVIPMALQG 572
Cdd:PLN02901 110 ECLKRCMELLKKGASVFFFPEGTRSKDGKLAAFKKGAFSVAAKTGVPVVPITLVG 164
LPLAT cd06551
Lysophospholipid acyltransferases (LPLATs) of glycerophospholipid biosynthesis; ...
429-611 3.76e-12

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: 65.51  E-value: 3.76e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182154 429 MRFLVWLLSHtMYRVRHVNLEAIPDEGAAVLVCNHVSYVDAL----LIAGSIRRPVRFVMYYriFSLPVLNFvFRTAGAV 504
Cdd:cd06551    1 FRYLLLNFFG-FVRLEVKGPPPPPGGGPVLFVSNHSSWWDGLilflLLERGLRRDVYGLMDE--ELLERYPF-FTRLGAF 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182154 505 PIAARHEDEGIyeRAFQRIADYLRD-GELVCIFPEGKLTADGEMN-EFRAGIERIIEETPVPVIPMALQGLWGSFFSRDP 582
Cdd:cd06551   77 SVDRDSPRSAA--KSLKYVARLLSKpGSVVWIFPEGTRTRRDKRPlQFKPGVAHLAEKAGVPIVPVALRYTFELFEQFPE 154
                        170       180
                 ....*....|....*....|....*....
gi 489182154 583 NKGFFRRLWSRVSLVAGESVAPGAVERLD 611
Cdd:cd06551  155 IFVRIGPPIPYAETALGEELAAELANRLT 183
LPLAT_MGAT-like cd07987
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: MGAT-like; ...
441-590 2.46e-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: 60.76  E-value: 2.46e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182154 441 YRVRHV-NLEAIPDEGAAVLVCNH-VSYVDALLIAGSIR-----RPVRFVMYYRIFSLPVLNFVFRTAGAVPIAARHede 513
Cdd:cd07987    5 FRVYEVrGLENIPDEGPALLVHPHgGLPIDGALLAAAFLllfpgRLPRALADHFLFPLPGLRDLLRRLGAVPGSREN--- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182154 514 giyerafqrIADYLRDGELVCIFPEGKLTA-DGEMNE------FRAGIERIIEETPVPVIPMALQGL-----WGSFFSRD 581
Cdd:cd07987   82 ---------CVRLLREGELVLIFPGGAREAlKSKREEyyllwkKRKGFARLALRAGAPIVPVFTFGEeelfrVLGDPDGP 152

                 ....*....
gi 489182154 582 PNKGFFRRL 590
Cdd:cd07987  153 VGKRLFRLL 161
MFS_MdtG_SLC18_like cd17325
bacterial MdtG-like and eukaryotic solute carrier 18 (SLC18) family of the Major Facilitator ...
93-424 2.60e-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: 56.43  E-value: 2.60e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182154  93 VGIMLVGAAGFVFG---SLPLMFVALFAMGTHSALFGPVKYSILPQHLHEDELVGGNALVEMGTFLAILAGTIGAGVLMS 169
Cdd:cd17325   66 LGLLLLAVSTLLFAfatSYWQLLLARFLQGLASAAVWPAAMALIADIAPPEERGRAMGIFSSAIGLGFLIGPLLGGLLAD 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182154 170 HAHYAAAVATAVVLVAACGYLASRGIPRAAAALPGLKLDWNIFAQSWSILRLglgqRPAVSRSLVGNSWFWFLGAVYLTQ 249
Cdd:cd17325  146 ALGYRAPFLVCAALALLALVLALLLLPEPRPPPNKRAVSAARLRSGLRLLLR----DRRLLALFLAIFVLAFAFGALEPF 221
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182154 250 IPTFAKEWLHGDESVVTLILTVFSVGIALGSMLCEKLSGRKVEIGLVPFGSIgLTVFGILLWWHAGGIppgeapydwlav 329
Cdd:cd17325  222 LPLYAAELGGLSPAQIGLLFGAQGLASALSQPPAGKLSDRIGRKPLILIGLL-LSAVALLLLPLATSF------------ 288
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182154 330 lrhhetWAVLADILFIGIFGGFYIVPLYALIQARTDEDKRARVIAANNILNALFMVAAALVSILFlsVAKLSIPQLFLAL 409
Cdd:cd17325  289 ------WLLLLLLALLGLGLGLVFPATLALLADIVPPEGRGTAMGLFNTAFSLGMVLGPLLGGFL--YDAFGFATPFLAA 360
                        330
                 ....*....|....*
gi 489182154 410 SLMNVAVNVYIFKIV 424
Cdd:cd17325  361 AALLLLAAVLFLLLR 375
LPLAT_LPCAT1-like cd07991
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: LPCAT1-like; ...
429-571 8.40e-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: 52.99  E-value: 8.40e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182154 429 MRFLVWLLSHtmYRVRHVNLEAiPDEGAAVLVCNHVSYVDALLIagSIRRPVRFVMYYRIFSLPVLNFVFRTAGAVPIaa 508
Cdd:cd07991    1 ARVLLFAFGF--YVIKVHGKPD-PPEAPRIIVANHTSFIDPLIL--FSDLFPSIVAKKELGKLPFIGTILRALGCIFV-- 73
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489182154 509 RHEDEGIYERAFQRIADYLRDGEL--VCIFPEGKLTADGEMNEFRAGieriIEETPVPVIPMALQ 571
Cdd:cd07991   74 DRSEPKDRKKVVEEIKERATDPNWppILIFPEGTTTNGKALIMFKKG----AFEPGVPVQPVAIR 134
LPLAT_ACT14924-like cd07986
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: Unknown ...
441-572 1.79e-07

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: 52.25  E-value: 1.79e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182154 441 YRVRHVNLEAIPDEGAAVLVCNH-VSYVDALL---IAGSIRRPVRFVMYYRIFSLPVLNFVFrtagaVPIAARHEDEGIY 516
Cdd:cd07986    8 LEVDVSGLENIPKDGPVVIVANHpFGILDGLIladLLGSVRPDVRILANQLLSKIPELRDLF-----IPVDPLEGRAALA 82
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489182154 517 E--RAFQRIADYLRDGELVCIFPEGKL-TADGEMNEFR-----AGIERIIEETPVPVIPMALQG 572
Cdd:cd07986   83 KnrESLREALRHLKNGGALIIFPAGRVsTASPPFGRVSdrpwnPFVARLARKAKAPVVPVYFSG 146
MFS cd06174
Major Facilitator Superfamily; The Major Facilitator Superfamily (MFS) is a large and diverse ...
86-414 9.02e-07

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: 51.66  E-value: 9.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182154  86 RALKLAEVGIMLVGAAGFVFGSLPLMFVALFAMGTHSALFGPVKYSILPQHLHEDELVGGNALVEMGTFLAILAGTIGAG 165
Cdd:cd06174   62 PVLLLGLLLFALGALLFAFAPSFWLLLLGRFLLGLGSGLIDPAVLALIADLFPERERGRALGLLQAFGSVGGILGPLLGG 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182154 166 VLMSHAHYA-AAVATAVVLVAACGYLASRGIPRAAAALPGLKLDWNIFAQSWSILRLgLGQRPAVSRSLVGNSWFWFLGA 244
Cdd:cd06174  142 ILASSLGFGwRAVFLIAAALALLAAILLLLVVPDPPESARAKNEEASSKSVLKLLKR-VLKNPGLWLLLLAIFLVNLAYY 220
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182154 245 VYLTQIPTFAKEWLHGDESVVTLILTVFSVGIALGSMLCEKLSGRKVEIGLVPFGSIGLTVFGILLWWHAGGippgeapy 324
Cdd:cd06174  221 SFSTLLPLFLLDLGGLSVAVAGLLLSLFGLAGALGSLLLGLLSDRLIGRKPLLLIGLLLMALGLALLLLAPS-------- 292
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182154 325 dwlavlrhheTWAVLADILFIGIFGGFYIVPLYALIQARTDEDKRARVIAANNILNALFMVAAALVSIlFLSVAKLSIPQ 404
Cdd:cd06174  293 ----------LLLLLLLLLLLGFGLGGLLPLSFALIAELFPPEIRGTAFGLLNTFGFLGGAIGPLLAG-FLLAATFGLTG 361
                        330
                 ....*....|
gi 489182154 405 LFLALSLMNV 414
Cdd:cd06174  362 AFLVLAVLLL 371
MFS_1 pfam07690
Major Facilitator Superfamily;
95-388 3.36e-06

Major Facilitator Superfamily;


Pssm-ID: 429598 [Multi-domain]  Cd Length: 344  Bit Score: 49.34  E-value: 3.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182154   95 IMLVGAAGFVFG--------SLPLMFVALFAMGTHSALFGPVKYSILPQHLHEDELVGGNALVEMGTFLAILAGTIGAGV 166
Cdd:pfam07690  64 VLLIGLLLFALGlllllfasSLWLLLVLRVLQGLGAGALFPAALALIADWFPPEERGRALGLVSAGFGLGAALGPLLGGL 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182154  167 LMSHAHYAAAVATAVVLVAACGYLASRGIPRAAAALP-GLKLDWNIFAQSWSILRlglgqRPAVSRSLVGNSWFWFLGAV 245
Cdd:pfam07690 144 LASLFGWRAAFLILAILSLLAAVLLLLPRPPPESKRPkPAEEARLSLIVAWKALL-----RDPVLWLLLALLLFGFAFFG 218
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182154  246 YLTQIPTFAKEwLHGDESVVTLILTVFSVGIALGSMLCEKLSGRKVEIGLVPFGSIGLTVFGILLWWHAGGippgeapyd 325
Cdd:pfam07690 219 LLTYLPLYQEV-LGLSALLAGLLLGLGGLLGAIGRLLLGRLSDRLGRRRRLLLALLLLILAALGLLLLSLT--------- 288
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489182154  326 wlavlrhHETWAVLADILFIGIFGGFYIVPLYALIQARTDEDKRARVIAANNILNALFMVAAA 388
Cdd:pfam07690 289 -------LSSLWLLLALLLLGFGFGLVFPALNALVSDLAPKEERGTASGLYNTAGSLGGALGP 344
PRK08043 PRK08043
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
430-596 3.52e-06

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


Pssm-ID: 181207 [Multi-domain]  Cd Length: 718  Bit Score: 50.09  E-value: 3.52e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182154 430 RFLVWLLSHtMYRVRHVNLEAIPDEGAAVLVCNHVSYVDALLIAgsIRRPVR--FVMYYRIFSLPVLNFVFRTAGAVPIa 507
Cdd:PRK08043   4 SFFRNLFRV-LYRVRVTGDTQALKGERVLITPNHVSFLDGILLA--LFLPVRpvFAVYTSISQQWYMRWLKPYIDFVPL- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182154 508 arhedEGIYERAFQRIADYLRDGELVCIFPEGKLTADGEMNEFRAGIERIIEETPVPVIPMALQGLWGSFFSRdpNKGFF 587
Cdd:PRK08043  80 -----DPTKPMAIKHLVRLVEQGRPVVIFPEGRITVTGSLMKIYDGAGFVAAKSGATVIPVRIEGAELTHFSR--LKGLV 152
                        170
                 ....*....|
gi 489182154 588 -RRLWSRVSL 596
Cdd:PRK08043 153 kRRLFPQITL 162
AraJ COG2814
Predicted arabinose efflux permease AraJ, MFS family [Carbohydrate transport and metabolism];
225-426 1.13e-04

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


Pssm-ID: 442063 [Multi-domain]  Cd Length: 348  Bit Score: 44.58  E-value: 1.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182154 225 QRPAVSRSLVGNSWFWFLGAVYLTQIPTFAKEwLHGDESVVTLILTVFSVGIALGSMLCEKLSGRKVEIGLVPFGSIGLT 304
Cdd:COG2814    8 RWLALLALALGAFLSGLGIGIVLPALPLIAAD-LGASPAQAGLVVTAYLLGAALGAPLAGRLADRFGRRRVLLLGLLLFA 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182154 305 VFGILLWWHAGgippgeapYDWLAVLRhhetwavladiLFIGIFGGFYIVPLYALIQARTDEDKRARVIAANNILNALFM 384
Cdd:COG2814   87 LGSLLCALAPS--------LWLLLAAR-----------FLQGLGAGALFPAALALIADLVPPERRGRALGLLGAGLGLGP 147
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 489182154 385 VAAALVSILFLSVakLSIPQLFLALSLMNVAVNVYIFKIVPE 426
Cdd:COG2814  148 ALGPLLGGLLADL--FGWRWVFLVNAVLALLALLLLLRLLPE 187
MelB COG2211
Na+/melibiose symporter or related transporter [Carbohydrate transport and metabolism];
231-398 1.19e-04

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


Pssm-ID: 441813 [Multi-domain]  Cd Length: 447  Bit Score: 44.89  E-value: 1.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182154 231 RSLVGNSWFWFLGAVYLTQ----------IPTFAKEWLHGDESVVTLILTVFSVGIALGSMLCEKLSGRkveIGLVPFGS 300
Cdd:COG2211  222 KALLKNRPFLLLLLAYLLFflalalvaalLLYYFKYVLGLSAALVGLLLALYFLAALLGAPLWPRLAKR---FGKKKAFI 298
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182154 301 IGLTVFGILLWwhaggippgeapydWLAVLRHHETWAVLADILFIGIFGGFYIVPLYALI-------QARTDEDKRARVI 373
Cdd:COG2211  299 IGLLLAALGLL--------------LLFFLGPGNLWLLLVLAALAGIGLGAILVLPWAMLadvvdydEWKTGRRREGLYF 364
                        170       180
                 ....*....|....*....|....*
gi 489182154 374 AANNILNALFMVAAALVSILFLSVA 398
Cdd:COG2211  365 GIFTFAIKLGQALAGALAGLLLALF 389
UhpC COG2271
Sugar phosphate permease [Carbohydrate transport and metabolism];
93-394 2.06e-04

Sugar phosphate permease [Carbohydrate transport and metabolism];


Pssm-ID: 441872 [Multi-domain]  Cd Length: 363  Bit Score: 44.09  E-value: 2.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182154  93 VGIMLVGAAGFVFG---SLPLMFVALFAMGTHSALFGPVKYSILPQHLHEDELVGGNALVEMGTFLAILAGTIGAGVLMS 169
Cdd:COG2271   80 IGLLLWGLATLLFGfatSFWQLLLLRFLLGLGEAGFFPAALKLIAEWFPPKERGRALGIFNAGGPLGGALAPPLLGWLLA 159
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182154 170 HAHYaaavatavvlvaacgylasrgipRAAAALPGlkldwnIFAQSWSILRLGLGqrpavsrsLVGNSWFWFLGAVYLTQ 249
Cdd:COG2271  160 AFGW-----------------------RAAFLILG------LPGLLLALLRFWLL--------ALAYFLVYFALYGFLTW 202
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182154 250 IPTFAKEWLHGDESVVTLILTVFSVGIALGSMLCEKLSGR-KVEIGLVPFGSIGLTVFGILLWWHAGGippgeapydwla 328
Cdd:COG2271  203 LPTYLVEVRGLSLAQAGLLLSLPFLAGIVGSLLGGWLSDRlGRRRKLVLAIGLLLAALALLLLALLPS------------ 270
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489182154 329 vlrhheTWAVLADILFIGIFGGFYIVPLYALIQARTDEDKRARVIAannILNALFMVAAALVSILF 394
Cdd:COG2271  271 ------PALAIALLFLAGFGLGGAFGLLWALAAELFPKKARGTASG---LVNTFGFLGGALGPLLV 327
MFS_1 pfam07690
Major Facilitator Superfamily;
239-426 2.87e-04

Major Facilitator Superfamily;


Pssm-ID: 429598 [Multi-domain]  Cd Length: 344  Bit Score: 43.56  E-value: 2.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182154  239 FWFLGAVYLTQIPTFAKEWLHGDESVVTLILTVFSVGIALGSMLCEKLSGRkveIGLVPFGSIGLTVFGILLwwhaggip 318
Cdd:pfam07690   8 AALGRSLLGPALPLLLAEDLGISPTEIGLLLTLFSLGYALAQPLAGRLSDR---FGRRRVLLIGLLLFALGL-------- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182154  319 pgeapydwLAVLRHHETWAVLADILFIGIFGGFYIVPLYALIQARTDEDKRARVIAANNILNALFMVAAALVSILFLSVa 398
Cdd:pfam07690  77 --------LLLLFASSLWLLLVLRVLQGLGAGALFPAALALIADWFPPEERGRALGLVSAGFGLGAALGPLLGGLLASL- 147
                         170       180
                  ....*....|....*....|....*...
gi 489182154  399 kLSIPQLFLALSLMNVAVNVYIFKIVPE 426
Cdd:pfam07690 148 -FGWRAAFLILAILSLLAAVLLLLPRPP 174
LPLAT_LCLAT1-like cd07990
Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: LCLAT1-like; ...
457-539 4.13e-04

Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: LCLAT1-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 Lysocardiolipin acyltransferase 1 (LCLAT1) or 1-acyl-sn-glycerol-3-phosphate acyltransferase and similar proteins.


Pssm-ID: 153252 [Multi-domain]  Cd Length: 193  Bit Score: 41.84  E-value: 4.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182154 457 AVLVCNHVSYVDALLI------AGSIRRpVRFVMYYRIFSLPVLNFVFRTAGAVPIAARHE-DEGIYERAFQRIADYlRD 529
Cdd:cd07990   26 ALIISNHRSEVDWLVLwmladrFGRLGR-LKIVLKDSLKYPPLGGWGWQLGEFIFLKRKWEkDEKTIKRQLKRLKDS-PE 103
                         90
                 ....*....|
gi 489182154 530 GELVCIFPEG 539
Cdd:cd07990  104 PFWLLIFPEG 113
MFS_arabinose_efflux_permease_like cd17473
Putative arabinose efflux permease family transporters of the Major Facilitator Superfamily; ...
248-416 7.49e-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: 42.18  E-value: 7.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182154 248 TQIPTFAKEWLHGDESVVTLILTVFSVGIALGSMLCEKLSGRKVEIGLVPFGSIgLTVFGILLWWHAGGIppgeapydwl 327
Cdd:cd17473  218 IQLPFLLQERGGGSAALIGLALAIASLAGAIGALLFGRLKRRLGKRRLLAIGFA-LMALGFLLLALASGL---------- 286
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182154 328 avlrhhetWAVLADILFIGIFGGFYIVPLYALIQARTDEDKRARVIAANNILNALFMVAAALVSIlFLSVAKLSIPQLFL 407
Cdd:cd17473  287 --------WVVLLGAILAGLGFGLLLPTLNSWAMSLVPPELRGRAMGIVTSAFFLGQFLSPLVLG-PLVNLTGGLSGAFL 357

                 ....*....
gi 489182154 408 ALSLMNVAV 416
Cdd:cd17473  358 ILGVLALVL 366
COG3176 COG3176
Putative hemolysin [General function prediction only];
441-578 9.21e-04

Putative hemolysin [General function prediction only];


Pssm-ID: 442409  Cd Length: 270  Bit Score: 41.56  E-value: 9.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182154 441 YRVRHVNLEAIPDEGAAVLVCNH-VSYVDALL---IAGSIRRPvrfvmyYRIFSlpvlNFVFRTAgavpiaarheDEGIY 516
Cdd:COG3176   57 LEVPEGDLDRIDADGHLLVVANHpLGILDGLAllkLVGTVRPD------YRILA----NDLALRI----------PGGFY 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182154 517 E-----------RAFQRIADYLRDGELVCIFPegkltaDGEMNEFRAGIE--------RIIEETPVPVIPMALQGLWGSF 577
Cdd:COG3176  117 SelefpvdpfnlETLKAARRHLLEGGRSCVFP------AGRVSGARRVIDllwsglaaKLARKAGAPVVPVYFDGRNSGL 190

                 .
gi 489182154 578 F 578
Cdd:COG3176  191 F 191
MFS_MdtH_MDR_like cd17329
Multidrug resistance protein MdtH and similar multidrug resistance (MDR) transporters of the ...
239-430 2.50e-03

Multidrug resistance protein MdtH and similar multidrug resistance (MDR) transporters of the Major Facilitator Superfamily; This family is composed of Escherichia coli MdtH and similar multidrug resistance (MDR) transporters from bacteria and archaea, many of which remain uncharacterized. 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. MdtH confers resistance to norfloxacin and enoxacin. MdtH-like MDR transporters 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: 340887 [Multi-domain]  Cd Length: 376  Bit Score: 40.67  E-value: 2.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182154 239 FWFLGAVYLTQIptfakewLHGDESVVTLILTVFSVGIALGSMLCEKLSGRkveiglvpFGSIGLTVFGILLWwhAGGIp 318
Cdd:cd17329   18 VWPFMAIYLHQQ-------LGLSASIVGLVLALSAVAGIVASLIGGRLADR--------FGRKPVMLAGLLLR--ALGF- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489182154 319 pgeapydwLAVLRHHETWAVLADILFIGIFGGFYIVPLYALIQARTDEDKRARVIAANNILNALFMVAAALVSILFLsva 398
Cdd:cd17329   80 --------ALLGFAHSPWLFAIALVLTGFGGGLFEPASEAMIADVTTPENRTRAFSLLYWAINLGVAIGPLLGGLLL--- 148
                        170       180       190
                 ....*....|....*....|....*....|..
gi 489182154 399 KLSIPQLFLALSLMNVAVNVYIFKIVPEFTMR 430
Cdd:cd17329  149 LYSFRLLFLAAAVLFLLAALVLLFLLPETRPK 180
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH