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cd11345: AmyAc_SLC3A2 
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Alpha amylase catalytic domain found in solute carrier family 3 member 2 proteins
4F2 cell-surface antigen heavy chain (hc) is a protein that in humans is encoded by the SLC3A2 gene. 4F2hc is a multifunctional type II membrane glycoprotein involved in amino acid transport and cell fusion, adhesion, and transformation. It is related to bacterial alpha-glycosidases, but lacks alpha-glycosidase activity. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.
Links
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Statistics
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PSSM-Id: 200483
View PSSM: cd11345
Aligned: 9 rows
Threshold Bit Score: 440.724
Threshold Setting Gi: 348529878
Created: 11-Jul-2011
Updated: 17-Jan-2013
Structure
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Program:
Drawing:
Aligned Rows:
Hierarchy
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Display:
 
homodimer
Conserved site includes 4 residues -Click on image for an interactive view with Cn3D
Feature 1:homodimer interface [polypeptide binding site]
Evidence:
  • Structure:2DH3: Human Ed-4f2hc forms a homodimer, contacts at 4A
    View structure with Cn3D
  • Comment:the dimer interface is primarily mediated by the C-terminal domain, which is not included in the alignment model

cd11345 is part of a hierarchy of related CD models.
Use the graphical representation to navigate this hierarchy.
cd11345 is a member of the superfamily cl07893.
cd00551:AmyAc_familycd11313:AmyAc_arch_bac_AmyAcd11314:AmyAc_arch_bac_plant_AmyAcd11315:AmyAc_bac1_AmyAcd11316:AmyAc_bac2_AmyAcd11317:AmyAc_bac_euk_AmyAcd11318:AmyAc_bac_fung_AmyAcd11319:AmyAc_euk_AmyAcd11320:AmyAc_AmyMalt_CGTase_likecd11321:AmyAc_bac_euk_BEcd11322:AmyAc_Glg_BEcd11323:AmyAc_AGScd11324:AmyAc_Amylosucrasecd11325:AmyAc_GTHasecd11326:AmyAc_Glg_debranchcd11327:AmyAc_Glg_debranch_2cd11328:AmyAc_maltasecd11329:AmyAc_maltase-likecd11330:AmyAc_OligoGlucd11331:AmyAc_OligoGlu_likecd11332:AmyAc_OligoGlu_TScd11333:AmyAc_SI_OligoGlu_DGasecd11334:AmyAc_TreScd11335:AmyAc_MTase_Ncd11336:AmyAc_MTSasecd11337:AmyAc_CMD_likecd11338:AmyAc_CMDcd11339:AmyAc_bac_CMD_like_2cd11340:AmyAc_bac_CMD_like_3cd11341:AmyAc_Pullulanase_LD-likecd11343:AmyAc_Sucrose_phosphorylase-likecd11344:AmyAc_GlgE_likecd11345:AmyAc_SLC3A2cd11346:AmyAc_plant_IsoAcd11347:AmyAc_1cd11348:AmyAc_2cd11349:AmyAc_3cd11350:AmyAc_4cd11352:AmyAc_5cd11353:AmyAc_euk_bac_CMD_likecd11354:AmyAc_bac_CMD_likecd11355:AmyAc_Sucrose_phosphorylasecd11356:AmyAc_Sucrose_phosphorylase-like_1cd11359:AmyAc_SLC3A12DH3 A334332603277691572236487684139318511545425472274603485298782135120492DH3 A33433260327769157223648768413931851154542547227460348529878213512049
cd11345 Sequence Cluster
cd11345 Sequence Cluster
Sub-family Hierarchy
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 cd11345 Branch
 Whole Hierarchy
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CD Hierarchy
Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1                # #                                                                     
2DH3_A         1 DRWGSELPAQKWWHTGALYRIGDLQAFQgh---gaGNLAGLKGRLDYLSSLKVKGLVLGPIHKnqkDDVAQTDLLQIDPN 77
gi 47227460   96 APRCKPIPEINWWNEGPLYQIPDAKSFS-------DGIKGIEAKLDSINQLKVKGLVLGPLHSvqaDQPSTLFLGEVDPN 168
gi 348529878  92 APRCKSIPEMNWWNEGPLYQITDLEVFS-------EGLKGVEEKLDDINELKVKGLVIGPLNIaqaNQKIILNFAEISLV 164
gi 213512049  94 APRCKPIPEMNWWNQGPLYQIADLNAFNh-----dKGIEGVVKVLDSLNQLKVKGLVLGPLHTvqqDQADTLDLVSMNPV 168
gi 27769157  105 APRCRPLPAMEWWNKGPLYQVGDPATFQed---gaGNIQSIEKRLESLTSLKVKGLIIGPIHVtkkDQIGETELTDIDPN 181
gi 334332603 109 APRCRELPTQRWWHQGPVYRLGALKAFQgqpsngtAGLAGVKARLDYLSTLKVKALVLGPIHKnvqDDLGGTDLQQIDPA 188
gi 11545425   93 APRCKPIPEMHWWNEGPLYQISNLDAFSk------NGLKGVEEKLDYLSQMKVKGLVLGPVHSvqaDQSSALELTSINPD 166
gi 223648768 101 APRCKDIPAMNWWNYGPLYQIGNVQAFSe-----sQNLKGVADKMNHLSQLKVKGLVIGPIHVaplDNLVSLNFEEISSD 175
gi 41393185  102 APRCKPLPEMNWRNNGPLYQIGDVGAFTn-----sSDIKDLAGKVQALDDLKVKGLIIGPIHVsseDKPNELNLIKISED 176
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1                                                                                        
2DH3_A        78 FGSKEDFDSLLQSAKKKSIRVILDLTPNYrgensw---fstqvdTVATKVKDALEFWLQAGVDGFQVRDIENLkdasSFL 154
gi 47227460  169 QGTKDELRSVLEKAHRKGISVMLDLTPNYlgsssw----fppikDDLEKVQAAAEYWFGLGVDGIKVSDLAAA----SAS 240
gi 348529878 165 HGKAEDLDNLLKAAHKKGISVVLDLTPNYegnpew----fsdseEIMERVKAAAEYWLEKGLDGIKISDLVDP----SNS 236
gi 213512049 169 LGTDQDLLVLLDKAHKKGISVVLNLTPNPgadpwf---ssnhlpKVLDKLRDAAEHWLGMGVDGVQVSGLAAA----SAS 241
gi 27769157  182 YGTMEQFTSLLEAARKKSIQIILDLTPNYrsenswfekaerennIFFEKVKEAVNVWLEHGVGGIYFGDSENFpnanSFI 261
gi 334332603 189 LGTLQDFTNLLLEAKKKNIHIVLDLTPNYrgrsswf--lphqseEVNERMKEALSFWLNNGVDGIQVLDVQNLtdasSAL 266
gi 11545425  167 FGSESELTSLLDRAHRKGISIVLDLTPNYrgvssw----fnnaaSVAEKLKKACVYWLNKGVDGIFLSDLNDI----MNT 238
gi 223648768 176 AGNLEQFKSLITAAHKKSINVVLDLTPYYlgsrpwf--anvsvpNVAERLKSALVFWLNQGVDGIQLSGVERVa--sVVP 251
gi 41393185  177 DGVLAQFKEVITAAHKRGISVILDLTPNYkgkdpw----fsdavNTVQKVEPALIFWLKQGVDGFLFYGVEKVa--aAAP 250
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1                                                     #                                  
2DH3_A       155 AEWQNITKGFSe--------DRLLIAGTNssdlqqi-lsllesnKDLLLTSSylsdsgstgehtk--slvtqylnatgnR 223
gi 47227460  241 AEWSKLQAAVQtnss-qdgkKRALMGVVKnvsatgaqqllntssVDLLLTDLvstkmegpvlm------htmdtlnseqR 313
gi 348529878 237 TDWAKLRMAVQgngt-ddtkKRLVWLLCKeri----------rdLETLHSEQ---------------------------R 278
gi 213512049 242 SGWSKFQGVVQgnrtemdvkKRAVIGVVDdqdssavsqllntsgVDLILSDVlnkansgierak----sihdlvstqkqS 317
gi 27769157  262 YEWGNMTANYSke-----gkPRVLLLSTSsaqnnlt--ggfnetIDGTLFYRflgaenkksfgsl-gesikqyveetgiQ 333
gi 334332603 267 SQWSNLTHSISe--------DNVLIVGTEaselsql--msllndTDLLSSSYledfgrrsssgrelkdlvtsyldatggH 336
gi 11545425  239 YAWSSIQAIFNktd---gtpKKALMGTASslsvdetslllnqsgVDLLLTKLpypaglsgrqat----lmqrlcsghqeA 311
gi 223648768 252 SLWADIRAIVQngt---egkRRILIGVTEktsavevsellnstgVDLLLSGAlrsksmtptdra---qtvqqllsshnqT 325
gi 41393185  251 TFWSDVVALIHnqtdaegktKKVLIGVTDqsspeeisatlnktgVDLLLSGAlrsksvrevaq-----aveslystynqT 325
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1                                                                                        
2DH3_A       224 WCSWSLSQARlltsf---lpaqLLRLYQLMLFtLPGTPVFSYGDEIGLDAaalpgqpmeapvmlw----dessfpdipga 296
gi 47227460  314 SLGWGIGAVDreqlskqattpaLIRLYHLLLFtLPGTPVFTYGDEIGLQSgqgseppkmiwd----------iekeaaeg 383
gi 348529878 279 KIGWGLGAAQkdrlskrattrgLIRLYQLLLFtLPGTPVFTYGDEIGLQAnqmsnktnqtre---------apkmvwnve 349
gi 213512049 318 SLAWGLGGTSgnhlasvvekpeLVRLYQLMLFtLPGTPVFNYGDELGLVDqgstspkmlwd-----------teeevaeg 386
gi 27769157  334 GNSWMIGAPQmrhmas-lvnekLLRVYQLLLFtLPGTPISLYGDEIGLKDlpgqpaqssrpnmqweevsvsnnspqiasd 412
gi 334332603 337 WCTWTYSQVGhlasl---vpahLLRLYHLLFFtLPGTPIFSYGDEIGLQAalpgqpaeapimlw------dektlgpses 407
gi 11545425  312 SLAWGLGQTAgsqas--rtpalPVKLYQTLLFaLPGTPVFSAGDELGLKAgea--------------------------- 362
gi 223648768 326 QLAWNIGDRKeghlat-lvgpdMVNFNQMLLLtLPGTPVFNYGDEIALADadtkspkml----------------wdsle 388
gi 41393185  326 RLAWNIGGRIaghlas-vvgfaKVKLSQLMLLtLPGTPVFNYGDEIGLEDevnky-----------------------pt 381
                        330       340       350
                 ....*....|....*....|....*....|....
Feature 1                                       #  
2DH3_A       297 vsaNMTVKGQSEDPGSLLSLFRRLSDQRSKERSL 330
gi 47227460  384 eavNETLQAENKQRAELREWFISLSDLRGKERSL 417
gi 348529878 350 keeTDGAKSNHTGYAEIRKWFRSLSDLRGKERSL 383
gi 213512049 387 tvkNETAEAQKTHRLTCRSWFKTLSDLRGKERSL 420
gi 27769157  413 vnaNITFKAQDADKGSFLNVYRKLSDLRGKERSL 446
gi 334332603 408 vnlNMTVQGQNENPGSLLSEFRKLSDSRGKERSL 441
gi 11545425  363 -mwEDVNSTAEEERTAVRNFFKTLSDLKGKERSL 395
gi 223648768 389 detNGTAKEEKEQRLSCRSFFKTLSELRGKERSL 422
gi 41393185  382 mlwKFNDEEKQKEMSTYHSFFKSVSVKRMKERSL 415

Citing CDD
Marchler-Bauer A et al. (2013), "CDD: conserved domains and protein three-dimensional structure.", Nucleic Acids Res. 41(D1):D384-52.
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Conserved site includes 4 residues -Click on image for an interactive view with Cn3D