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Conserved domains on  [gi|24662113|ref|NP_729588|]
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uncharacterized protein Dmel_CG32054 [Drosophila melanogaster]

Protein Classification

MFS transporter( domain architecture ID 13866462)

major facilitator superfamily (MFS) transporter facilitates the transport across cytoplasmic or internal membranes of one or more from a variety of substrates including ions, sugar phosphates, drugs, neurotransmitters, nucleosides, amino acids, and peptides

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MFS super family cl28910
Major Facilitator Superfamily; The Major Facilitator Superfamily (MFS) is a large and diverse ...
 157-555 2.53e-23

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.


The actual alignment was detected with superfamily member pfam00083:

Pssm-ID: 475125 [Multi-domain]  Cd Length: 452  Bit Score: 102.74  E-value: 2.53e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662113   157 FAAWFIGGIIGAVISWFLINNVAKKYVLIFSSFLVMIGGILTTSTKNSG--DATLAASYLDGIANGL--VFAPfmALAGE 232
Cdd:pfam00083  52 VSIFSVGCFIGSLFAGKLGDRFGRKKSLLIANVLFVIGAVLQGAAKGKWsvYQLIVGRVLVGIGVGGasVLAP--MYISE 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662113   233 VSVSYMRGMVSaSIEQMCFGLGIFL-QIIYTSTWNSTAYPSYNSFSAenmkgvLSIIYGfLALIIGSLLCIESPVIMLAK 311
Cdd:pfam00083 130 IAPKKLRGALG-SLYQLAITFGILLaYIFGLGLNKTSNSDGWRIPLG------LQLVPA-LLLIIGLLFLPESPRWLVEK 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662113   312 NNDEQgAIDALRRLQRPYTLTNETFEQLAEHKKYLAQNKE--LSMGQSIGQALPTFIRLV-----FLRGLNA---MSISK 381
Cdd:pfam00083 202 GRLEE-AREVLAKLRGVPDVDRELDEIKDSLEAGQEAEKAswKELFSTKTRRQRLLIGVMlqifqQLTGINAifyYSTTI 280

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662113   382 FVMIGFVYSFAspygyvspsvgWFIGFGVCRWMGNFIATFCMESCGRKKPTLLGLIVCSVMSFVVAGQFNIFTYNTGNNI 461
Cdd:pfam00083 281 FENLGLSDSFL-----------VTIIVGVVNFVFTFIAIFLVDRFGRRPLLLLGAAGMAICFVILGIVALLGVSKSDWAG 349

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662113   462 MLLVFELFAGIAFTATSP------YLSEAFPLEVKQHFISFTFIGEMLV-FLV--LTLIRWSSSGGANYFYVMGGLYLFG 532
Cdd:pfam00083 350 IVAIVFIALFIAFFAMGWgpvpwvIVSELFPLSVRSKAMALATAANWLAnFLIgfLFPIITDAIGLGYTFFIFAGLLVLF 429

                         410       420
                  ....*....|....*....|...
gi 24662113   533 FFFGLVCLPETRRTTLREAQDKF 555
Cdd:pfam00083 430 IIFVFFFVPETKGRTLEEIDELF 452
Pro-rich pfam15240
Proline-rich protein; This family includes several eukaryotic proline-rich proteins.
 7-102 7.74e-08

Proline-rich protein; This family includes several eukaryotic proline-rich proteins.


:

Pssm-ID: 464580 [Multi-domain]  Cd Length: 167  Bit Score: 52.35  E-value: 7.74e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662113     7 SQQNPPPMG--FATAPPQQGYPRqgyPHTEFPQPGFPQPGHHQSGYPQPGHSWNPPPPQFGfSGYPPPPQQGYppqfygP 84
Cdd:pfam15240  73 PQQPPPQGGkqKPQGPPPQGGPR---PPPGKPQGPPPQGGNQQQGPPPPGKPQGPPPQGGG-PPPQGGNQQGP------P 142

                          90
                  ....*....|....*...
gi 24662113    85 PPGYGLPQAtlPPNPPQQ 102
Cdd:pfam15240 143 PPPPGNPQG--PPQRPPQ 158
 
Name Accession Description Interval E-value
Sugar_tr pfam00083
Sugar (and other) transporter;
157-555 2.53e-23

Sugar (and other) transporter;


Pssm-ID: 395036 [Multi-domain]  Cd Length: 452  Bit Score: 102.74  E-value: 2.53e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662113   157 FAAWFIGGIIGAVISWFLINNVAKKYVLIFSSFLVMIGGILTTSTKNSG--DATLAASYLDGIANGL--VFAPfmALAGE 232
Cdd:pfam00083  52 VSIFSVGCFIGSLFAGKLGDRFGRKKSLLIANVLFVIGAVLQGAAKGKWsvYQLIVGRVLVGIGVGGasVLAP--MYISE 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662113   233 VSVSYMRGMVSaSIEQMCFGLGIFL-QIIYTSTWNSTAYPSYNSFSAenmkgvLSIIYGfLALIIGSLLCIESPVIMLAK 311
Cdd:pfam00083 130 IAPKKLRGALG-SLYQLAITFGILLaYIFGLGLNKTSNSDGWRIPLG------LQLVPA-LLLIIGLLFLPESPRWLVEK 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662113   312 NNDEQgAIDALRRLQRPYTLTNETFEQLAEHKKYLAQNKE--LSMGQSIGQALPTFIRLV-----FLRGLNA---MSISK 381
Cdd:pfam00083 202 GRLEE-AREVLAKLRGVPDVDRELDEIKDSLEAGQEAEKAswKELFSTKTRRQRLLIGVMlqifqQLTGINAifyYSTTI 280

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662113   382 FVMIGFVYSFAspygyvspsvgWFIGFGVCRWMGNFIATFCMESCGRKKPTLLGLIVCSVMSFVVAGQFNIFTYNTGNNI 461
Cdd:pfam00083 281 FENLGLSDSFL-----------VTIIVGVVNFVFTFIAIFLVDRFGRRPLLLLGAAGMAICFVILGIVALLGVSKSDWAG 349

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662113   462 MLLVFELFAGIAFTATSP------YLSEAFPLEVKQHFISFTFIGEMLV-FLV--LTLIRWSSSGGANYFYVMGGLYLFG 532
Cdd:pfam00083 350 IVAIVFIALFIAFFAMGWgpvpwvIVSELFPLSVRSKAMALATAANWLAnFLIgfLFPIITDAIGLGYTFFIFAGLLVLF 429

                         410       420
                  ....*....|....*....|...
gi 24662113   533 FFFGLVCLPETRRTTLREAQDKF 555
Cdd:pfam00083 430 IIFVFFFVPETKGRTLEEIDELF 452
MFS_GLUT_Class1_2_like cd17357
Class 1 and Class 2 Glucose transporters (GLUTs) of the Major Facilitator Superfamily; This ...
 97-545 2.11e-15

Class 1 and Class 2 Glucose transporters (GLUTs) of the Major Facilitator Superfamily; This subfamily includes Class 1 and Class 2 glucose transporters (GLUTs) including Solute carrier family 2, facilitated glucose transporter member 1 (SLC2A1, also called glucose transporter type 1 or GLUT1), SLC2A2-5 (GLUT2-5), SLC2A7 (GLUT7), SLC2A9 (GLUT9), SLC2A11 (GLUT11), SLC2A14 (GLUT14), and similar proteins. GLUTs are a family of proteins that facilitate the transport of hexoses such as glucose and fructose. There are fourteen GLUTs found in humans; they display different substrate specificities and tissue expression. They have been categorized into three classes based on sequence similarity: Class 1 (GLUTs 1-4, 14); Class 2 (GLUTs 5, 7, 9, and 11); and Class 3 (GLUTs 6, 8, 10, 12, and HMIT). GLUTs 1-5 are the most thoroughly studied and are well-established as glucose and/or fructose transporters in various tissues and cell types. GLUT proteins are comprised of about 500 amino acid residues, possess a single N-linked oligosaccharide, and have 12 transmembrane segments. They belong to the Glucose transporter -like (GLUT-like) family of the Major Facilitator Superfamily (MFS) of membrane transport proteins. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.


Pssm-ID: 340915 [Multi-domain]  Cd Length: 447  Bit Score: 78.46  E-value: 2.11e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662113  97 PNPPQQTITV--NNSWYSRNqknkpqsnavgaaGLIFVSGGMNIAWSIgfrgvlhykttehNFAAWFIGGIIGAVISWFL 174
Cdd:cd17357  19 VNAPQEVFKEfiNDTLVDRY-------------GLNLSDSELDLLWSL-------------IVSIFFIGGAIGSFISAFL 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662113 175 INNVAKKYVLIFSSFLVMIGGILTTSTK--NSGDATLAASYLDGIANGLVFAPFMALAGEVSVSYMRGMVSaSIEQMCFG 252
Cdd:cd17357  73 ANRFGRKNGLLISNALLVVSSLLMFLSKsaKSPELLIFGRFLVGIACGLSTGFVPMYLQEISPSELRGALG-SLTQIGVT 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662113 253 LGIFL-QIIytstwnstAYPSYNSfSAENMKGVLSIIYGF-LALIIGSLLCIESPVIMLAKNNDEQGAIDALRRLQRpyt 330
Cdd:cd17357 152 LGILLgQVF--------GLPSVLG-TETLWPYLLFFPGIPaLLQLAALPFFPESPKFLLISKGDEEEAEKSLKFLRG--- 219

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662113 331 LTNETFEQLAEHKKYLAQN---KELSMGQ---SIGQALPTFIRLVF-----LRGLNAM---SISKFVMIGFVYSFASpyg 396
Cdd:cd17357 220 IEDDVDQELEEIKKESEQMgdqKQVSLMQllrDPSLRLPLLLVLVVsasqqFSGINAIffySTFIFENAGFSPQLAE--- 296

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662113 397 YVSpsvgwfIGFGVCRWMGNFIATFCMESCGRKKPTLLGLIVCSVMSFVVAGQFNIFTYNTGNNIMLLVFELFAGIAFT- 475
Cdd:cd17357 297 WAN------LGIGIVNVLSTIVGPFLIEKVGRRPLLLISLSVCAVALLLMSVFLFLSEQNSWMSYGCIVAIFLFIFFFAi 370

                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24662113 476 --ATSPYL--SEAFPLEVKQHFISF-TFIGEMLVFLVLTL-IRWSSSGGANYF--YVMGGLYLFGFFFglVCLPETRR 545
Cdd:cd17357 371 glGPIPWFigAELFPQAPRSAAQSLgSSVNWTSNFIVGMAfPPLQSIGGGFVFiiFAIPCALFLLYLY--RYLPETKG 446
Pro-rich pfam15240
Proline-rich protein; This family includes several eukaryotic proline-rich proteins.
 7-102 7.74e-08

Proline-rich protein; This family includes several eukaryotic proline-rich proteins.


Pssm-ID: 464580 [Multi-domain]  Cd Length: 167  Bit Score: 52.35  E-value: 7.74e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662113     7 SQQNPPPMG--FATAPPQQGYPRqgyPHTEFPQPGFPQPGHHQSGYPQPGHSWNPPPPQFGfSGYPPPPQQGYppqfygP 84
Cdd:pfam15240  73 PQQPPPQGGkqKPQGPPPQGGPR---PPPGKPQGPPPQGGNQQQGPPPPGKPQGPPPQGGG-PPPQGGNQQGP------P 142

                          90
                  ....*....|....*...
gi 24662113    85 PPGYGLPQAtlPPNPPQQ 102
Cdd:pfam15240 143 PPPPGNPQG--PPQRPPQ 158
Amelogenin smart00818
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ...
 7-104 1.74e-05

Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem to regulate formation of crystallites during the secretory stage of tooth enamel development and are thought to play a major role in the structural organisation and mineralisation of developing enamel. The extracellular matrix of the developing enamel comprises two major classes of protein: the hydrophobic amelogenins and the acidic enamelins. Circular dichroism studies of porcine amelogenin have shown that the protein consists of 3 discrete folding units: the N-terminal region appears to contain beta-strand structures, while the C-terminal region displays characteristics of a random coil conformation. Subsequent studies on the bovine protein have indicated the amelogenin structure to contain a repetitive beta-turn segment and a "beta-spiral" between Gln112 and Leu138, which sequester a (Pro, Leu, Gln) rich region. The beta-spiral offers a probable site for interactions with Ca2+ ions. Muatations in the human amelogenin gene (AMGX) cause X-linked hypoplastic amelogenesis imperfecta, a disease characterised by defective enamel. A 9bp deletion in exon 2 of AMGX results in the loss of codons for Ile5, Leu6, Phe7 and Ala8, and replacement by a new threonine codon, disrupting the 16-residue (Met1-Ala16) amelogenin signal peptide.


Pssm-ID: 197891 [Multi-domain]  Cd Length: 165  Bit Score: 45.17  E-value: 1.74e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662113      7 SQQNPPPMgfaTAPPQQGYPRQGYPHTEFPQ-PGFPQPGHHqSGYPQPGHSWNPPPPQFGFSGYPPPPQQGYPPQFYGPP 85
Cdd:smart00818  43 SQQHPPTH---TLQPHHHIPVLPAQQPVVPQqPLMPVPGQH-SMTPTQHHQPNLPQPAQQPFQPQPLQPPQPQQPMQPQP 118

                           90
                   ....*....|....*....
gi 24662113     86 PGygLPQATLPPNPPQQTI 104
Cdd:smart00818 119 PV--HPIPPLPPQPPLPPM 135
AraJ COG2814
Predicted arabinose efflux permease AraJ, MFS family [Carbohydrate transport and metabolism];
123-255 4.58e-05

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


Pssm-ID: 442063 [Multi-domain]  Cd Length: 348  Bit Score: 45.74  E-value: 4.58e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662113 123 AVGAAGLIFVSGGMNIAWSIGFRGVLHYKTTEHN--FAAWFIGGIIGAVISWFLINNVAKKYVLIFSsFLVMIGGILTTS 200
Cdd:COG2814 213 LLLAFLLGFGFFALFTYLPLYLQEVLGLSASAAGllLALFGLGGVLGALLAGRLADRFGRRRLLLIG-LLLLALGLLLLA 291

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 24662113 201 TKNSGDATLAASYLDGIANGLVFAPFMALAGEVSVSYMRGMVSASIeQMCFGLGI 255
Cdd:COG2814 292 LAGSLWLLLLALFLLGFGFGLLFPLLQALVAELAPPEARGRASGLY-NSAFFLGG 345
PHA03247 PHA03247
large tegument protein UL36; Provisional
 11-100 1.74e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.93  E-value: 1.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662113    11 PPPMGFATAPPQQGYPRQGYPHTE-FPQPGFPQPGHHQSGYPQPGHSWNPPPPQFGFSGYPPPPQQGYPPQFYGPPPG-Y 88
Cdd:PHA03247 2893 RSTESFALPPDQPERPPQPQAPPPpQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGrV 2972

                          90
                  ....*....|..
gi 24662113    89 GLPQATLPPNPP 100
Cdd:PHA03247 2973 AVPRFRVPQPAP 2984
2A0119 TIGR00898
cation transport protein; [Transport and binding proteins, Cations and iron carrying compounds]
 292-550 8.63e-03

cation transport protein; [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273328 [Multi-domain]  Cd Length: 505  Bit Score: 38.84  E-value: 8.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662113   292 LALIIGSLLC---IESPVIMLAKNNDEQgAIDALRRLQRpytlTNETfeQLAEHKKYLAQNKELSMGQSIgqalPTFIRL 368
Cdd:TIGR00898 251 LPTFLFFLLSwfvPESPRWLISQGRIEE-ALKILQRIAK----INGK--KLPAEVLSLSLEKDLSSSKKQ----YSFLDL 319

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662113   369 VFLRGLNAMSISkFVMIGFVYSFASpYGYV------SPSVGW-FIGFGVCRWMGNFIATFCMESCGRKKP----TLLGLI 437
Cdd:TIGR00898 320 FRTPNLRKTTLC-LMMLWFTTAFSY-YGLVldlgnlGGNIYLdLFISGLVELPAKLITLLLIDRLGRRYTmaasLLLAGV 397

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662113   438 VCSVMSFVVAGQFNIFTyntgnnIMLLVFELFAGIAFTATSPYLSEAFPLEVKQHFISFTF----IGEMLV-FLVLTLIR 512
Cdd:TIGR00898 398 ALLLLLFVPVDLYFLRT------ALAVLGKFGITSAFQMVYLYTAELYPTVVRNLGVGVCStmarVGSIISpFLVYLGEK 471

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 24662113   513 WSSSgganYFYVMGGLYLFGFFFGLVcLPETRRTTLRE 550
Cdd:TIGR00898 472 WLFL----PLVLFGGLALLAGILTLF-LPETKGVPLPE 504
 
Name Accession Description Interval E-value
Sugar_tr pfam00083
Sugar (and other) transporter;
157-555 2.53e-23

Sugar (and other) transporter;


Pssm-ID: 395036 [Multi-domain]  Cd Length: 452  Bit Score: 102.74  E-value: 2.53e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662113   157 FAAWFIGGIIGAVISWFLINNVAKKYVLIFSSFLVMIGGILTTSTKNSG--DATLAASYLDGIANGL--VFAPfmALAGE 232
Cdd:pfam00083  52 VSIFSVGCFIGSLFAGKLGDRFGRKKSLLIANVLFVIGAVLQGAAKGKWsvYQLIVGRVLVGIGVGGasVLAP--MYISE 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662113   233 VSVSYMRGMVSaSIEQMCFGLGIFL-QIIYTSTWNSTAYPSYNSFSAenmkgvLSIIYGfLALIIGSLLCIESPVIMLAK 311
Cdd:pfam00083 130 IAPKKLRGALG-SLYQLAITFGILLaYIFGLGLNKTSNSDGWRIPLG------LQLVPA-LLLIIGLLFLPESPRWLVEK 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662113   312 NNDEQgAIDALRRLQRPYTLTNETFEQLAEHKKYLAQNKE--LSMGQSIGQALPTFIRLV-----FLRGLNA---MSISK 381
Cdd:pfam00083 202 GRLEE-AREVLAKLRGVPDVDRELDEIKDSLEAGQEAEKAswKELFSTKTRRQRLLIGVMlqifqQLTGINAifyYSTTI 280

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662113   382 FVMIGFVYSFAspygyvspsvgWFIGFGVCRWMGNFIATFCMESCGRKKPTLLGLIVCSVMSFVVAGQFNIFTYNTGNNI 461
Cdd:pfam00083 281 FENLGLSDSFL-----------VTIIVGVVNFVFTFIAIFLVDRFGRRPLLLLGAAGMAICFVILGIVALLGVSKSDWAG 349

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662113   462 MLLVFELFAGIAFTATSP------YLSEAFPLEVKQHFISFTFIGEMLV-FLV--LTLIRWSSSGGANYFYVMGGLYLFG 532
Cdd:pfam00083 350 IVAIVFIALFIAFFAMGWgpvpwvIVSELFPLSVRSKAMALATAANWLAnFLIgfLFPIITDAIGLGYTFFIFAGLLVLF 429

                         410       420
                  ....*....|....*....|...
gi 24662113   533 FFFGLVCLPETRRTTLREAQDKF 555
Cdd:pfam00083 430 IIFVFFFVPETKGRTLEEIDELF 452
MFS_GLUT_Class1_2_like cd17357
Class 1 and Class 2 Glucose transporters (GLUTs) of the Major Facilitator Superfamily; This ...
 97-545 2.11e-15

Class 1 and Class 2 Glucose transporters (GLUTs) of the Major Facilitator Superfamily; This subfamily includes Class 1 and Class 2 glucose transporters (GLUTs) including Solute carrier family 2, facilitated glucose transporter member 1 (SLC2A1, also called glucose transporter type 1 or GLUT1), SLC2A2-5 (GLUT2-5), SLC2A7 (GLUT7), SLC2A9 (GLUT9), SLC2A11 (GLUT11), SLC2A14 (GLUT14), and similar proteins. GLUTs are a family of proteins that facilitate the transport of hexoses such as glucose and fructose. There are fourteen GLUTs found in humans; they display different substrate specificities and tissue expression. They have been categorized into three classes based on sequence similarity: Class 1 (GLUTs 1-4, 14); Class 2 (GLUTs 5, 7, 9, and 11); and Class 3 (GLUTs 6, 8, 10, 12, and HMIT). GLUTs 1-5 are the most thoroughly studied and are well-established as glucose and/or fructose transporters in various tissues and cell types. GLUT proteins are comprised of about 500 amino acid residues, possess a single N-linked oligosaccharide, and have 12 transmembrane segments. They belong to the Glucose transporter -like (GLUT-like) family of the Major Facilitator Superfamily (MFS) of membrane transport proteins. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.


Pssm-ID: 340915 [Multi-domain]  Cd Length: 447  Bit Score: 78.46  E-value: 2.11e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662113  97 PNPPQQTITV--NNSWYSRNqknkpqsnavgaaGLIFVSGGMNIAWSIgfrgvlhykttehNFAAWFIGGIIGAVISWFL 174
Cdd:cd17357  19 VNAPQEVFKEfiNDTLVDRY-------------GLNLSDSELDLLWSL-------------IVSIFFIGGAIGSFISAFL 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662113 175 INNVAKKYVLIFSSFLVMIGGILTTSTK--NSGDATLAASYLDGIANGLVFAPFMALAGEVSVSYMRGMVSaSIEQMCFG 252
Cdd:cd17357  73 ANRFGRKNGLLISNALLVVSSLLMFLSKsaKSPELLIFGRFLVGIACGLSTGFVPMYLQEISPSELRGALG-SLTQIGVT 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662113 253 LGIFL-QIIytstwnstAYPSYNSfSAENMKGVLSIIYGF-LALIIGSLLCIESPVIMLAKNNDEQGAIDALRRLQRpyt 330
Cdd:cd17357 152 LGILLgQVF--------GLPSVLG-TETLWPYLLFFPGIPaLLQLAALPFFPESPKFLLISKGDEEEAEKSLKFLRG--- 219

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662113 331 LTNETFEQLAEHKKYLAQN---KELSMGQ---SIGQALPTFIRLVF-----LRGLNAM---SISKFVMIGFVYSFASpyg 396
Cdd:cd17357 220 IEDDVDQELEEIKKESEQMgdqKQVSLMQllrDPSLRLPLLLVLVVsasqqFSGINAIffySTFIFENAGFSPQLAE--- 296

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662113 397 YVSpsvgwfIGFGVCRWMGNFIATFCMESCGRKKPTLLGLIVCSVMSFVVAGQFNIFTYNTGNNIMLLVFELFAGIAFT- 475
Cdd:cd17357 297 WAN------LGIGIVNVLSTIVGPFLIEKVGRRPLLLISLSVCAVALLLMSVFLFLSEQNSWMSYGCIVAIFLFIFFFAi 370

                       410       420       430       440       450       460       470
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24662113 476 --ATSPYL--SEAFPLEVKQHFISF-TFIGEMLVFLVLTL-IRWSSSGGANYF--YVMGGLYLFGFFFglVCLPETRR 545
Cdd:cd17357 371 glGPIPWFigAELFPQAPRSAAQSLgSSVNWTSNFIVGMAfPPLQSIGGGFVFiiFAIPCALFLLYLY--RYLPETKG 446
MFS_GLUT6_8_Class3_like cd17358
Glucose transporter (GLUT) types 6 and 8, Class 3 GLUTs, and similar transporters of the Major ...
 158-550 7.44e-13

Glucose transporter (GLUT) types 6 and 8, Class 3 GLUTs, and similar transporters of the Major Facilitator Superfamily; This subfamily is composed of glucose transporter type 6 (GLUT6), GLUT8, plant early dehydration-induced gene ERD6-like proteins, and similar insect proteins including facilitated trehalose transporter Tret1-1. GLUTs, also called Solute carrier family 2, facilitated glucose transporters (SLC2A), are a family of proteins that facilitate the transport of hexoses such as glucose and fructose. There are fourteen GLUTs found in humans; they display different substrate specificities and tissue expression. They have been categorized into three classes based on sequence similarity: Class 1 (GLUTs 1-4, 14); Class 2 (GLUTs 5, 7, 9, and 11); and Class 3 (GLUTs 6, 8, 10, 12, and HMIT). Insect Tret1-1 is a low-capacity facilitative transporter for trehalose that mediates the transport of trehalose synthesized in the fat body and the incorporation of trehalose into other tissues that require a carbon source. GLUT proteins are comprised of about 500 amino acid residues, possess a single N-linked oligosaccharide, and have 12 transmembrane segments. They belong to the Glucose transporter -like (GLUT-like) family of the Major Facilitator Superfamily (MFS) of membrane transport proteins. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.


Pssm-ID: 340916 [Multi-domain]  Cd Length: 436  Bit Score: 70.68  E-value: 7.44e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662113 158 AAWF-----IGGIIGAVISWFLINNVAKKYVLIFSSFLVMIGGILTTSTKNSGdATLAASYLDGIANGLVFAPFMALAGE 232
Cdd:cd17358  43 FSWFgslltLGALIGALLSGKLADRIGRKRTLLISAIPCILGWLLIAFAKDVW-MLYLGRFLAGFGGGAASVVVPVYIAE 121

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662113 233 VSVSYMRGMVSASIEQMC-------FGLGIFLQIIYTStwnstaypsynsfsaenmkgVLSIIYGFLALIigsLLCI--E 303
Cdd:cd17358 122 IAPKNVRGALGSLNQLLVnigillgYVLGSFLPWRTLA--------------------LIGAIPPVVFLI---LLFFipE 178

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662113 304 SPViMLAKNNDEQGAIDALRRLQ-RPYTLTNETFEQLAEHKKYLAQNKELSMGQSI-GQALPTFIRLVFLRGLNAMSISk 381
Cdd:cd17358 179 SPR-WLAKKGREEEAEKSLQFLRgKDADISKEAAEIQEELAELEKEAKESSFSDLFqRKYLKPLVIGLGLMLFQQLSGI- 256

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662113 382 FVMIgfVYS---FASPYGYVSPSVGwFIGFGVCRWMGNFIATFCMESCGRKkptLLGLIVCSVMSFVVAgQFNIFTYNTG 458
Cdd:cd17358 257 NAVI--FYAssiFDEAGSGLDPNTA-TIIIGVVQVVGTLVATLLVDRLGRR---PLLLVSAIGMGIGLL-ALGLYFYLQE 329

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662113 459 NNIMLLVFELFAGIAFTA----------TSPYL--SEAFPLEVKQHFISF-TFIGEMLVFLVLTL-----IRWSSSGgan 520
Cdd:cd17358 330 HGALLSSVSWLPLVGLVIyiisfsiglgPLPWVimSEIFPAKIKGLAGSLvTLVNWLFAFIVTKTfpfltLAWGASG--- 406

                       410       420       430
                ....*....|....*....|....*....|
gi 24662113 521 YFYVMGGLYLFGFFFGLVCLPETRRTTLRE 550
Cdd:cd17358 407 TFWIFAGICGLALVFVLLFVPETKGKSLEE 436
MFS_HXT cd17356
Fungal Hexose transporter subfamily of the Major Facilitator Superfamily of transporters and ...
 162-555 5.11e-10

Fungal Hexose transporter subfamily of the Major Facilitator Superfamily of transporters and similar proteins; The fungal hexose transporter (HXT) subfamily is comprised of functionally redundant proteins that function mainly in the transport of glucose, as well as other sugars such as galactose and fructose. Saccharomyces cerevisiae has 20 genes that encode proteins in this family (HXT1 to HXT17, GAL2, SNF3, and RGT2). Seven of these (HXT1-7) encode functional glucose transporters. Gal2p is a galactose transporter, while Rgt2p and Snf3p act as cell surface glucose receptors that initiate signal transduction in response to glucose, functioning in an induction pathway responsible for glucose uptake. Rgt2p is activated by high levels of glucose and stimulates expression of low affinity glucose transporters such as Hxt1p and Hxt3p, while Snf3p generates a glucose signal in response to low levels of glucose, stimulating the expression of high affinity glucose transporters such as Hxt2p and Hxt4p. Schizosaccharomyces pombe contains eight GHT genes (GHT1-8) belonging to this family. Ght1, Ght2, and Ght5 are high-affinity glucose transporters; Ght3 is a high-affinity gluconate transporter; and Ght6 high-affinity fructose transporter. The substrate specificities for Ght4, Ght7, and Ght8 remain undetermined. The HXT subfamily belongs to the Glucose transporter -like (GLUT-like) family of the Major Facilitator Superfamily (MFS) of membrane transport proteins. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.


Pssm-ID: 340914 [Multi-domain]  Cd Length: 403  Bit Score: 61.50  E-value: 5.11e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662113 162 IGGIIGAVISWFLINNVAKKYVLIFSSFLVMIGGILTTSTKNSGDATLAASYLDGIANGLVFAPFMALAGEVSVSYMRGM 241
Cdd:cd17356  56 LGSFFGALISSFLSDRIGRKKSIQIGCVIYIIGAIIQVAAIGKWYQLIVGRIIAGLGVGFASVLVPVYQSEVAPKHIRGT 135

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662113 242 VsASIEQMCFGLGIFLQIiytstWNSTAYPSYNSFSAENMKGVLSIIYGFLaLIIGSLLCIESPvimlaknndeqgaida 321
Cdd:cd17356 136 L-VSLYQLAITIGILVAY-----CINYGTHKLDGSAQWRIPLGLQIVWGLL-LLIGMFFLPESP---------------- 192

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662113 322 lRRLQRPYTLTnetfeqlaehkkylaqnkelsMGQSIGQalptfirlvfLRGLNAM---SISKFVMIGfvYSFASPYgyV 398
Cdd:cd17356 193 -RWLYRTILGI---------------------MLQLFQQ----------LTGINYFfyyGTTIFQSTG--LTGSSPL--L 236

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662113 399 SPSVGWFIGFGVCrwmgnFIATFCMESCGRKKPTLLGLIVCSVMSFVVAGQFNIFTYNTG---------NNIMLLVFELF 469
Cdd:cd17356 237 TSIILYIVNFVST-----IPGLFFVDKFGRRTCLLIGAAGMSICLFIYAAVGVRYLIPNPqsgtsnksaGNGMIVFICLF 311

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662113 470 AGIAFTATSP----YLSEAFPLEVKQHFISFTFIGEMLVFLVLTLI--RWSSSGGANYFYVMGGLYLFGFFFGLVCLPET 543
Cdd:cd17356 312 IFSFATTWGPiawvYVAEVFPLRVRSKGMALATAFNWLWNFLISFFtpFIIGSIGFKYYYIFAGCNLLAFIVVFFFVPET 391

                       410
                ....*....|..
gi 24662113 544 RRTTLREAQDKF 555
Cdd:cd17356 392 KGLTLEEIDELF 403
Pro-rich pfam15240
Proline-rich protein; This family includes several eukaryotic proline-rich proteins.
 7-102 7.74e-08

Proline-rich protein; This family includes several eukaryotic proline-rich proteins.


Pssm-ID: 464580 [Multi-domain]  Cd Length: 167  Bit Score: 52.35  E-value: 7.74e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662113     7 SQQNPPPMG--FATAPPQQGYPRqgyPHTEFPQPGFPQPGHHQSGYPQPGHSWNPPPPQFGfSGYPPPPQQGYppqfygP 84
Cdd:pfam15240  73 PQQPPPQGGkqKPQGPPPQGGPR---PPPGKPQGPPPQGGNQQQGPPPPGKPQGPPPQGGG-PPPQGGNQQGP------P 142

                          90
                  ....*....|....*...
gi 24662113    85 PPGYGLPQAtlPPNPPQQ 102
Cdd:pfam15240 143 PPPPGNPQG--PPQRPPQ 158
Pro-rich pfam15240
Proline-rich protein; This family includes several eukaryotic proline-rich proteins.
 9-100 8.68e-07

Proline-rich protein; This family includes several eukaryotic proline-rich proteins.


Pssm-ID: 464580 [Multi-domain]  Cd Length: 167  Bit Score: 49.27  E-value: 8.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662113     9 QNPPPMGFATAPP----QQGYPRQGYPHTEFPQPG--FPQ-PGHHQSGYPQPGHSWNPPPPQFGFSGY--PPPPQQGYPP 79
Cdd:pfam15240  47 QGPPPGGFPPQPPasddPPGPPPPGGPQQPPPQGGkqKPQgPPPQGGPRPPPGKPQGPPPQGGNQQQGppPPGKPQGPPP 126

                          90       100
                  ....*....|....*....|.
gi 24662113    80 QFYGPPPGYGLPQatLPPNPP 100
Cdd:pfam15240 127 QGGGPPPQGGNQQ--GPPPPP 145
MFS_GLUT_Class1 cd17431
Class 1 Glucose transporters (GLUTs) of the Major Facilitator Superfamily; GLUTs, also called ...
 162-455 9.85e-06

Class 1 Glucose transporters (GLUTs) of the Major Facilitator Superfamily; GLUTs, also called Solute carrier family 2, facilitated glucose transporters (SLC2A), are a family of proteins that facilitate the transport of hexoses such as glucose and fructose. There are fourteen GLUTs found in humans; they display different substrate specificities and tissue expression. They have been categorized into three classes based on sequence similarity: Class 1 (GLUTs 1-4, 14); Class 2 (GLUTs 5, 7, 9, and 11); and Class 3 (GLUTs 6, 8, 10, 12, and HMIT). GLUTs 1-4 are well-established as glucose and/or fructose transporters in various tissues and cell types. GLUT1, also called solute carrier family 2, facilitated glucose transporter member 1 (SLC2A1), displays broad substrate specificity and can transport a wide range of pentoses and hexoses including glucose, galactose, mannose, and glucosamine. It is found in the brain, erythrocytes, and in many fetal tissues. GLUT2 (or SLC2A2) is found in the liver, islet of Langerhans, intestine, and kidney, and is the isoform that likely mediates the bidirectional transfer of glucose across the plasma membrane of hepatocytes and is responsible for uptake of glucose by beta cells. GLUT3 (or SLC2A3) is found in the brain and can mediates the uptake of glucose, 2-deoxyglucose, galactose, mannose, xylose and fucose, and dehydroascorbate. GLUT4 (or SLC2A4) is an insulin-regulated facilitative glucose transporter found in adipose tissues, and in skeletal and cardiac muscle. GLUT14 (or SLC2A14) is an orphan transporter expressed mainly in the testis. GLUT proteins are comprised of about 500 amino acid residues, possess a single N-linked oligosaccharide, and have 12 transmembrane segments. They belong to the Glucose transporter -like (GLUT-like) family of the Major Facilitator Superfamily (MFS) of membrane transport proteins. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.


Pssm-ID: 340989 [Multi-domain]  Cd Length: 445  Bit Score: 48.10  E-value: 9.85e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662113 162 IGGIIGAVISWFLINNVAKKYVLIFSSFLVMIGGILTTSTK--NSGDATLAASYLDGIANGLVFAPFMALAGEVSVSYMR 239
Cdd:cd17431  61 VGGMIGSFSVGLFVNRFGRRNSMLYNNLLAFAGAALMGLSKlaKSYEMLILGRFIIGLYCGLTTGLVPMYIGEISPTALR 140

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662113 240 GMVsASIEQMCFGLGIFLQIIytstwnstaypsynsFSAENMKGV---------LSIIYGFLALIIgSLLCIESPVIMLA 310
Cdd:cd17431 141 GAL-GTLHQLGIVVGILISQI---------------FGLEFILGTeelwplllgFTIVPAILQLAL-LPFCPESPRYLLI 203

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662113 311 KNNDEQGAIDALRRLqRPYTLTNETFEQLAEHKKYLAQNKELSMGQSIGQAL---PTFIRLVF-----LRGLNAMsiskf 382
Cdd:cd17431 204 NRNEEEEAKSVLKKL-RGTTDVSEDIQEMKEESRQMMREKKVTILELFRSSSyrqPIIIAIVLqlsqqLSGINAV----- 277

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662113 383 vmigFVYS---FASpyGYVSPSVGWFIGFGVCRWMGNFIATFCMESCGRKKPTLLGL---IVCSVM---SFVVAGQFNIF 453
Cdd:cd17431 278 ----FYYStsiFEK--AGVQQPVYATIGAGVVNTIFTVVSLFLVERAGRRTLHLIGLggmAICAILmtiALLLLEGYPWM 351


                ..
gi 24662113 454 TY 455
Cdd:cd17431 352 SY 353
DUF3824 pfam12868
Domain of unknwon function (DUF3824); This is a repeating domain found in fungal proteins. It ...
 11-62 9.87e-06

Domain of unknwon function (DUF3824); This is a repeating domain found in fungal proteins. It is proline-rich, and the function is not known.


Pssm-ID: 372351 [Multi-domain]  Cd Length: 145  Bit Score: 45.50  E-value: 9.87e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 24662113    11 PPPMGFATAPPQQGYPRQGYPHTE----FPQPGFPQPGHHQSGYPQPGHSWNPPPP 62
Cdd:pfam12868  83 PPPPGSTPQPPVDPQPNAPPPPYNpadyPPPPGAAPPPQPYQYPPPPGPDPYAPRP 138
Amelogenin smart00818
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ...
 7-104 1.74e-05

Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem to regulate formation of crystallites during the secretory stage of tooth enamel development and are thought to play a major role in the structural organisation and mineralisation of developing enamel. The extracellular matrix of the developing enamel comprises two major classes of protein: the hydrophobic amelogenins and the acidic enamelins. Circular dichroism studies of porcine amelogenin have shown that the protein consists of 3 discrete folding units: the N-terminal region appears to contain beta-strand structures, while the C-terminal region displays characteristics of a random coil conformation. Subsequent studies on the bovine protein have indicated the amelogenin structure to contain a repetitive beta-turn segment and a "beta-spiral" between Gln112 and Leu138, which sequester a (Pro, Leu, Gln) rich region. The beta-spiral offers a probable site for interactions with Ca2+ ions. Muatations in the human amelogenin gene (AMGX) cause X-linked hypoplastic amelogenesis imperfecta, a disease characterised by defective enamel. A 9bp deletion in exon 2 of AMGX results in the loss of codons for Ile5, Leu6, Phe7 and Ala8, and replacement by a new threonine codon, disrupting the 16-residue (Met1-Ala16) amelogenin signal peptide.


Pssm-ID: 197891 [Multi-domain]  Cd Length: 165  Bit Score: 45.17  E-value: 1.74e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662113      7 SQQNPPPMgfaTAPPQQGYPRQGYPHTEFPQ-PGFPQPGHHqSGYPQPGHSWNPPPPQFGFSGYPPPPQQGYPPQFYGPP 85
Cdd:smart00818  43 SQQHPPTH---TLQPHHHIPVLPAQQPVVPQqPLMPVPGQH-SMTPTQHHQPNLPQPAQQPFQPQPLQPPQPQQPMQPQP 118

                           90
                   ....*....|....*....
gi 24662113     86 PGygLPQATLPPNPPQQTI 104
Cdd:smart00818 119 PV--HPIPPLPPQPPLPPM 135
AraJ COG2814
Predicted arabinose efflux permease AraJ, MFS family [Carbohydrate transport and metabolism];
123-255 4.58e-05

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


Pssm-ID: 442063 [Multi-domain]  Cd Length: 348  Bit Score: 45.74  E-value: 4.58e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662113 123 AVGAAGLIFVSGGMNIAWSIGFRGVLHYKTTEHN--FAAWFIGGIIGAVISWFLINNVAKKYVLIFSsFLVMIGGILTTS 200
Cdd:COG2814 213 LLLAFLLGFGFFALFTYLPLYLQEVLGLSASAAGllLALFGLGGVLGALLAGRLADRFGRRRLLLIG-LLLLALGLLLLA 291

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 24662113 201 TKNSGDATLAASYLDGIANGLVFAPFMALAGEVSVSYMRGMVSASIeQMCFGLGI 255
Cdd:COG2814 292 LAGSLWLLLLALFLLGFGFGLLFPLLQALVAELAPPEARGRASGLY-NSAFFLGG 345
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 8-123 5.29e-05

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 46.30  E-value: 5.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662113     8 QQNP---PPMGFATAPPQQGYPRQGYPHTEFPQPgFPQPGHHQSGYPQPgHSWNPPPPQFGFSgyppppqqgyppqfyGP 84
Cdd:pfam03154 232 QQTPtlhPQRLPSPHPPLQPMTQPPPPSQVSPQP-LPQPSLHGQMPPMP-HSLQTGPSHMQHP---------------VP 294

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 24662113    85 PPGYGLP----QATLPPnPPQQTITVNNSwySRNQKNKPQSNA 123
Cdd:pfam03154 295 PQPFPLTpqssQSQVPP-GPSPAAPGQSQ--QRIHTPPSQSQL 334
PHA03247 PHA03247
large tegument protein UL36; Provisional
 11-100 1.74e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.93  E-value: 1.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662113    11 PPPMGFATAPPQQGYPRQGYPHTE-FPQPGFPQPGHHQSGYPQPGHSWNPPPPQFGFSGYPPPPQQGYPPQFYGPPPG-Y 88
Cdd:PHA03247 2893 RSTESFALPPDQPERPPQPQAPPPpQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGrV 2972

                          90
                  ....*....|..
gi 24662113    89 GLPQATLPPNPP 100
Cdd:PHA03247 2973 AVPRFRVPQPAP 2984
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 19-119 6.74e-04

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 42.76  E-value: 6.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662113    19 APPQQGY--PRQGYPhtefPQPGFPQPGHHQSGYPQPGHSWNPPPPQFGFSGYPPPPQqgyppqfygPPPGYGLPQATLP 96
Cdd:PRK10263  772 VAPQPQYqqPQQPVA----PQPQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVA---------PQPQYQQPQQPVA 838

                          90       100
                  ....*....|....*....|...
gi 24662113    97 PNPPQQTItvnNSWYSRNQKNKP 119
Cdd:PRK10263  839 PQPQDTLL---HPLLMRNGDSRP 858
Extensin_2 pfam04554
Extensin-like region;
9-64 6.78e-04

Extensin-like region;


Pssm-ID: 252669 [Multi-domain]  Cd Length: 57  Bit Score: 37.82  E-value: 6.78e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 24662113     9 QNPPPmgfataPPQQGYPRqgyPHTEFPQPGFPQPGHHQSGyPQPGHSWNPPPPQF 64
Cdd:pfam04554   4 KSPPP------PVKQYSPP---PPYYYKSPPPPVKSPVYKS-PPPPVYKSPPPPKY 49
MFS_SV2_like cd17316
Metazoan Synaptic vesicle glycoprotein 2 (SV2) and related small molecule transporters of the ...
 361-537 7.85e-04

Metazoan Synaptic vesicle glycoprotein 2 (SV2) and related small molecule transporters of the Major Facilitator Superfamily; This family is composed of metazoan synaptic vesicle glycoprotein 2 (SV2) and related small molecule transporters including those that transport inorganic phosphate (Pht), aromatic compounds (PcaK and related proteins), proline/betaine (ProP), alpha-ketoglutarate (KgtP), citrate (CitA), shikimate (ShiA), and cis,cis-muconate (MucK), among others. SV2 is a transporter-like protein that serves as the receptor for botulinum neurotoxin A (BoNT/A), one of seven neurotoxins produced by the bacterium Clostridium botulinum. BoNT/A blocks neurotransmitter release by cleaving synaptosome-associated protein of 25 kD (SNAP-25) within presynaptic nerve terminals. Also included in this family is synaptic vesicle 2 (SV2)-related protein (SVOP) and similar proteins. SVOP is a transporter-like nucleotide binding protein that localizes to neurotransmitter-containing vesicles. The SV2-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: 340874 [Multi-domain]  Cd Length: 353  Bit Score: 41.82  E-value: 7.85e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662113 361 ALPTFIRLVFLRGLNAM-SISKFVMIGFVYSF-ASPYGYVSPSVGWFIGFGVCRWM-GNFIATFCMESCGRKKPTLLGLI 437
Cdd:cd17316 172 ALLLRRRTLLLILLWFFiSFGYYGLTTFLPTYlQTVLGLSPATSSLYLLLISLGALvGALIAGLLSDRIGRKKTLVIGLI 251

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662113 438 VCSVMSFVVAgqfnIFTYNTGNNIMLLVFEL--FAGIAFTATSPYLSEAFPLEVKQHFISFTF----IGEMLVFLVLTLI 511
Cdd:cd17316 252 LSGILALPLF----YLLSGSPTLLLLLLFILsfFVGGVWGALYAYLAELFPTEVRATGVGLSYnlgrLGGGGAPPLIALL 327

                       170       180
                ....*....|....*....|....*.
gi 24662113 512 RWSSSGGANYFYVMGGLYLFGFFFGL 537
Cdd:cd17316 328 LASTGGTGVPALILALLAIVALIVAL 353
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 8-100 3.76e-03

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 40.14  E-value: 3.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662113     8 QQNPPPMGFATAPPQqGYPRQGYPhTEFPQPGFPQPGhhqSGYPQPGHSWNPPPPQFGFSGYPPPPQQGyppqfygPPPG 87
Cdd:pfam03154 264 QPLPQPSLHGQMPPM-PHSLQTGP-SHMQHPVPPQPF---PLTPQSSQSQVPPGPSPAAPGQSQQRIHT-------PPSQ 331

                          90
                  ....*....|....*.
gi 24662113    88 YGLPQATLP---PNPP 100
Cdd:pfam03154 332 SQLQSQQPPreqPLPP 347
MFS_MMR_MDR_like cd17321
Methylenomycin A resistance protein (also called MMR peptide) and similar multidrug resistance ...
 121-302 4.44e-03

Methylenomycin A resistance protein (also called MMR peptide) and similar multidrug resistance (MDR) transporters of the Major Facilitator Superfamily; This family is composed of bacterial, fungal, and archaeal multidrug resistance (MDR) transporters including several proteins from Bacilli such as methylenomycin A resistance protein (also called MMR peptide), tetracycline resistance protein (TetB), and lincomycin resistance protein LmrB, as well as fungal proteins such as vacuolar basic amino acid transporters, which are involved in the transport into vacuoles of the basic amino acids histidine, lysine, and arginine in Saccharomyces cerevisiae, and aminotriazole/azole resistance proteins. 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. For example, MMR confers resistance to the epoxide antibiotic methylenomycin while TetB resistance to tetracycline by an active tetracycline efflux. MMR-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: 340879 [Multi-domain]  Cd Length: 370  Bit Score: 39.46  E-value: 4.44e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662113 121 SNAVGAAGLIFVS-GGMNIAWSIGFRGVLHYKTTEHNFA--AWFIGGIIGAVISWFLINNVAKKYVLIFSSFLVMIG-GI 196
Cdd:cd17321 171 SGAVLAAFLLGAAlGGLLFLLPLYLQGVLGYSPLQAGLAllPLALAMLVAAPLAGRLADRFGPRLVLVAGLLLTAVGlLL 250

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662113 197 LTTSTKNSGDATLAASY-LDGIANGLVFAPFMALAGEVSVSYMRGMVSAsIEQMC------FGLGIFLQIIYTSTWNSTA 269
Cdd:cd17321 251 LALLGADSSVWLLLPGLvLLGLGLGLFATPLTNAALSSVPKEKAGAASG-ILNTArqlggaLGVALLGALLTAGLSANLG 329

                       170       180       190
                ....*....|....*....|....*....|....
gi 24662113 270 YPSYNSFSAENmkgVLSIIYGF-LALIIGSLLCI 302
Cdd:cd17321 330 DSGVAALLSAA---AAAFAAGFhLAFLVAAALAL 360
AraJ COG2814
Predicted arabinose efflux permease AraJ, MFS family [Carbohydrate transport and metabolism];
354-560 5.06e-03

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


Pssm-ID: 442063 [Multi-domain]  Cd Length: 348  Bit Score: 39.19  E-value: 5.06e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662113 354 MGQSIGQALPTFIRLVFLRGLNAMSIskFVMIGFVYSFASPYGYVSPSVGWFIG-FGVCRWMGNFIATFCMESCGRKKPT 432
Cdd:COG2814   1 MPATPRRRWLALLALALGAFLSGLGI--GIVLPALPLIAADLGASPAQAGLVVTaYLLGAALGAPLAGRLADRFGRRRVL 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662113 433 LLGLIVCSVMSFVVAGQFNIftyntgnnIMLLVFELFAGIA----FTATSPYLSEAFPLEVKQHFISF--------TFIG 500
Cdd:COG2814  79 LLGLLLFALGSLLCALAPSL--------WLLLAARFLQGLGagalFPAALALIADLVPPERRGRALGLlgaglglgPALG 150

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662113 501 EMLVFLVLTLIRWSSSgganyFYVMGGLYLFGFFFGLVCLPETRRTTLREAQDKFSKFIS 560
Cdd:COG2814 151 PLLGGLLADLFGWRWV-----FLVNAVLALLALLLLLRLLPESRPAARARLRGSLRELLR 205
PTZ00395 PTZ00395
Sec24-related protein; Provisional
 24-123 5.08e-03

Sec24-related protein; Provisional


Pssm-ID: 185594 [Multi-domain]  Cd Length: 1560  Bit Score: 40.06  E-value: 5.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662113    24 GYPRQGYPHTEFPQPGFPQPGHHQSGYPQPGHSWNPpppqfgfsgyppppqqgyppqfYGPPPGYGLPQATLP-PNPPQQ 102
Cdd:PTZ00395  398 AQSNAAQSNAGFSNAGYSNPGNSNPGYNNAPNSNTP----------------------YNNPPNSNTPYSNPPnSNPPYS 455

                          90       100
                  ....*....|....*....|..
gi 24662113   103 TITVNNSWYSR-NQKNKPQSNA 123
Cdd:PTZ00395  456 NLPYSNTPYSNaPLSNAPPSSA 477
Cytadhesin_P30 pfam07271
Cytadhesin P30/P32; This family consists of several Mycoplasma species specific Cytadhesin P32 ...
 5-99 5.10e-03

Cytadhesin P30/P32; This family consists of several Mycoplasma species specific Cytadhesin P32 and P30 proteins. P30 has been found to be membrane associated and localized on the tip organelle. It is thought that it is important in cytadherence and virulence. The N-terminus contains two predicted transmembrane helices followed by a long region of a short 6 residue proline rich repeat.


Pssm-ID: 429374 [Multi-domain]  Cd Length: 275  Bit Score: 39.18  E-value: 5.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662113     5 NFSQQNPPPM---GFATAPPQQGYPRQGYPHTEF-PQPGF-PQPGHHQS----GYPQPGHSWNPP-PPQFGFSgyppppq 74
Cdd:pfam07271 184 NQMPGMPPNQmrpGFNQMPGMPPRPGFPNPMPNMqPRPGFrPQPGPMGNrpggGFPHPGTPMGPNrMPNPGMN------- 256

                          90       100
                  ....*....|....*....|....*
gi 24662113    75 qgyppqfygPPPGYGLPQATLPPNP 99
Cdd:pfam07271 257 ---------QRPGMAPPRPGFPPQN 272
2A0119 TIGR00898
cation transport protein; [Transport and binding proteins, Cations and iron carrying compounds]
 292-550 8.63e-03

cation transport protein; [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273328 [Multi-domain]  Cd Length: 505  Bit Score: 38.84  E-value: 8.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662113   292 LALIIGSLLC---IESPVIMLAKNNDEQgAIDALRRLQRpytlTNETfeQLAEHKKYLAQNKELSMGQSIgqalPTFIRL 368
Cdd:TIGR00898 251 LPTFLFFLLSwfvPESPRWLISQGRIEE-ALKILQRIAK----INGK--KLPAEVLSLSLEKDLSSSKKQ----YSFLDL 319

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662113   369 VFLRGLNAMSISkFVMIGFVYSFASpYGYV------SPSVGW-FIGFGVCRWMGNFIATFCMESCGRKKP----TLLGLI 437
Cdd:TIGR00898 320 FRTPNLRKTTLC-LMMLWFTTAFSY-YGLVldlgnlGGNIYLdLFISGLVELPAKLITLLLIDRLGRRYTmaasLLLAGV 397

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662113   438 VCSVMSFVVAGQFNIFTyntgnnIMLLVFELFAGIAFTATSPYLSEAFPLEVKQHFISFTF----IGEMLV-FLVLTLIR 512
Cdd:TIGR00898 398 ALLLLLFVPVDLYFLRT------ALAVLGKFGITSAFQMVYLYTAELYPTVVRNLGVGVCStmarVGSIISpFLVYLGEK 471

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 24662113   513 WSSSgganYFYVMGGLYLFGFFFGLVcLPETRRTTLRE 550
Cdd:TIGR00898 472 WLFL----PLVLFGGLALLAGILTLF-LPETKGVPLPE 504
MFS_XylE_like cd17359
D-xylose-proton symporter and similar transporters of the Major Facilitator Superfamily; This ...
 406-542 9.71e-03

D-xylose-proton symporter and similar transporters of the Major Facilitator Superfamily; This subfamily includes bacterial transporters such as D-xylose-proton symporter (XylE or XylT), arabinose-proton symporter (AraE), galactose-proton symporter (GalP), major myo-inositol transporter IolT, glucose transport protein, putative metabolite transport proteins YfiG, YncC, and YwtG, and similar proteins. The symporters XylE, AraE, and GalP facilitate the uptake of D-xylose, arabinose, and galactose, respectively, across the boundary membrane with the concomitant transport of protons into the cell. IolT is involved in polyol metabolism and myo-inositol degradation into acetyl-CoA. The XylE-like subfamily belongs to the Glucose transporter -like (GLUT-like) family of the Major Facilitator Superfamily (MFS) of membrane transport proteins. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.


Pssm-ID: 340917 [Multi-domain]  Cd Length: 383  Bit Score: 38.32  E-value: 9.71e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662113 406 IGFGVCRWMGNFIATFCMESCGRKKPTLLGLIVCSVMSFVVAGQFNIFTYNTGNNIMLLVFELFAgIAFTATS------P 479
Cdd:cd17359 239 IGIGVVNVIFTIIAILLVDKVGRKPLLLIGSIGMAISLLLIGTAFYFAPGSQASGIVALVLILLF-VAFFAMSwgpvtwV 317

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24662113 480 YLSEAFPLEVKQHFISFT----FIGEMLVFLVLTLIRwSSSGGANYFYVMGGLYLFGFFFGLVCLPE 542
Cdd:cd17359 318 LLSEIFPNRIRGLAMGIAvfflWIANFLVSLTFPILL-AAFGLAFTFLIFAVICVLAFLFVWKFVPE 383
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
 8-128 9.82e-03

Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division.


Pssm-ID: 401645 [Multi-domain]  Cd Length: 846  Bit Score: 38.86  E-value: 9.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24662113     8 QQNPPPMGFATAPPQQGYPRQGYPHTEFP-QPGFPQPGHHQSGYPQPGHSWNPPP-----PQfgfSGYPPPPQQgyppqf 81
Cdd:pfam09770 209 KPAQQPAPAPAQPPAAPPAQQAQQQQQFPpQIQQQQQPQQQPQQPQQHPGQGHPVtilqrPQ---SPQPDPAQP------ 279

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 24662113    82 YGPPPGYGLPQATlPPNPPQQT-ITVNNSWYSRNQKNKPQSNAVGAAG 128
Cdd:pfam09770 280 SIQPQAQQFHQQP-PPVPVQPTqILQNPNRLSAARVGYPQNPQPGVQP 326
 
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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