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Conserved domains on  [gi|15239944|ref|NP_196799|]
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proline-tRNA ligase (DUF1680) [Arabidopsis thaliana]

Protein Classification

glycoside hydrolase family 127 protein( domain architecture ID 10546261)

glycoside hydrolase family 127 (GH127) protein similar to Bifidobacterium longum beta-L-arabinofuranosidase HypBA1, which releases L-arabinose from the non-reducing end of various substrates such as L-arabinofuranose (Araf)-beta1,2-Araf disaccharide and also transglycosylates 1-alkanols with retention of the anomeric configuration

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Glyco_hydro_127 pfam07944
Beta-L-arabinofuranosidase, GH127; One member of this family, from Bidobacterium longicum, ...
111-635 0e+00

Beta-L-arabinofuranosidase, GH127; One member of this family, from Bidobacterium longicum, UniProtKB:E8MGH8, has been characterized as an unusual beta-L-arabinofuranosidase enzyme, EC:3.2.1.185. It rleases l-arabinose from the l-arabinofuranose (Araf)-beta1,2-Araf disaccharide and also transglycosylates 1-alkanols with retention of the anomeric configuration. Terminal beta-l-arabinofuranosyl residues have been found in arabinogalactan proteins from a mumber of different plantt species. beta-l-Arabinofuranosyl linkages with 1-4 arabinofuranosides are also found in the sugar chains of extensin and solanaceous lectins, hydroxyproline (Hyp)2-rich glycoproteins that are widely observed in plant cell wall fractions. The critical residue for catalytic activity is Glu-338, in a ET/SCAS sequence context.


:

Pssm-ID: 400342 [Multi-domain]  Cd Length: 503  Bit Score: 596.22  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239944   111 DVRLDpDSFHWRAQQTNLEYLLMLDVDGLAWSFRKEAGLDAPGDYYGGWERPDSELRGHFVGHYLSATAYMWASTHNDTL 190
Cdd:pfam07944   1 DVRLT-DSFFGDRQQTNREYLLPLDPDRLLHTFRKEAGLPSKAIAYGGWEHPGFPFRGHDLGHWLSAVAYMLASTGDPEL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239944   191 KEKMSALVSALSECQQksGTGYLSAFPSSFFDRFEAITPVWAP---YYTIHKILAGLVDQYKLAGNSQALKMATGMADYF 267
Cdd:pfam07944  80 EARLDRLVDELAEAQQ--GDGYLGTYPESNFDRNEAGKGVWAPnheLYNLGKLIAGLVDYYQLTGKTQALDVATRLADWL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239944   268 YGRVrNVIRKYSVERHWQSlneETGGMNDVLYQLYSITGDSKYLLLAHLFDKPCFLGVLAIQADDISGFHANTHIPIVV- 346
Cdd:pfam07944 158 YDVT-DVLGDEQGQRVLVP---EHGGINEALVELYELTGDKRYLDLAKRFIHNRGLDPLAYGQDELPGRHQNTAIGHAVr 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239944   347 GSQQRYEITGDLLHKEISMFFMDIFNASHSYATGGTSVS-EFWQDPKRMATalQTENEESCTTYNMLKVSRNLFRWTKEV 425
Cdd:pfam07944 234 GAADVYEETGDDALLKAAEFFWDNVVTHHMYVTGGNGARhEHFGPPYELPN--RLAYCETCASYNMLKLTRRLFCWTPDA 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239944   426 SYADYYERALTNGVLGIQRGTQpGLMIYMLPLGKGVSKAVtyhgwgTPYDSFWCCYGTGIESFSKLGDSIYFQEDgatPA 505
Cdd:pfam07944 312 KYADYYERALYNHILAGQSPDG-GMFFYFNPLESGSYRLR------WPWDSFWCCPGNGAETHAKFGDYIYAHSD---DG 381
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239944   506 LYVTQYISSSLDWKSAGLSISQKVNpvVSWDPYMRVTFTLssskvGVAKESTLNLRIPVWtnSIGAKVSLNGRPL-NVPT 584
Cdd:pfam07944 382 IYVNLYIPSTADWKLKGVELEQETD--YPWEGKVRLTVNT-----AKKADFTLYLRIPGW--AAGATLTVNGKPTvVAPK 452
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|.
gi 15239944   585 SGNFLSIKQKWKSGDQVTMELPMSIRTEAIKDDRPEYASLQAILYGPYLLA 635
Cdd:pfam07944 453 SDGYLSIEREWKDGDRVELELPMPVRLEAAHPLVPDDPNKVAVLRGPLVLA 503
beta-trefoil_ABD_ABFB-like super family cl49624
Arabinose-binding domain (ABD), beta-trefoil fold, found in the ABFB family; The ABFB family ...
723-854 1.94e-08

Arabinose-binding domain (ABD), beta-trefoil fold, found in the ABFB family; The ABFB family includes alpha-L-arabinofuranosidase B (ABF B)-like proteins and otogelin-like proteins. Alpha-L-arabinofuranosidase (EC 3.2.1.55), also called ABF, or non-reducing end alpha-L-arabinofuranosidase, or arabinofuranosidase, or arabinosidase, is involved in the degradation of arabinoxylan, a major component of plant hemicellulose. It can hydrolyze 1,5-, 1,3- and 1,2-alpha-linkages not only in L-arabinofuranosyl oligosaccharides, but also in polysaccharides containing terminal non-reducing L-arabinofuranoses in side chains, like L-arabinan, arabinogalactan and arabinoxylan. ABF belongs to the glycosyl hydrolase 54 family. Hungateiclostridium thermocellum anti-sigma-I factor RsgI5 shows high sequence similarity with ABF B. It negatively regulates SigI5 activity through direct interaction. The OTOG subfamily includes otogelin (OTOG) and otogelin-like protein (OTOGL). OTOG is a glycoprotein specific to acellular membranes of the inner ear. It may be required for the anchoring of otoconial membranes and cupula to the underlying neuroepithelia in the vestibule. OTOG may be involved in the organization and/or stabilization of the fibrillar network that compose the tectorial membrane in the cochlea. OTOGL is a mucin glycoprotein that is a component of the tectorial membrane. It acts as a gel-forming mucin that forms high-molecular-weight complexes and is glycosylated through mucin-type O-glycosylation. Mutations in OTOG or OTOGL genes may cause hearing loss. Members of the ABFB family contain an ABD with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ABD binds two arabinose molecules in the beta and gamma subdomains.


The actual alignment was detected with superfamily member cd23265:

Pssm-ID: 483964  Cd Length: 135  Bit Score: 53.82  E-value: 1.94e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239944 723 GRLVMLEPFDFPGMIVKQATDSSLTVQASSPSdKGASSFRLVSGLDGKlGSVSLRLESKKGCFVYSdqtlkQGTKLRLEC 802
Cdd:cd23265   3 GTPVRLRSASDPGYYIRHDGGSGSVTSDDDDS-AEDAFFRVVPGLAGE-GTVSFESVDKPGYYLRH-----RGGELRLEK 75
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 15239944 803 GSDATDekFKEAASFSLKTGMHQYNPMSFVMSGTQRNFVLSPLFSLRDETYN 854
Cdd:cd23265  76 NDGSAA--FREDATFRPRPGLADPGGVSFESVNYPGYYLRHRNNRLVLGKVD 125
 
Name Accession Description Interval E-value
Glyco_hydro_127 pfam07944
Beta-L-arabinofuranosidase, GH127; One member of this family, from Bidobacterium longicum, ...
111-635 0e+00

Beta-L-arabinofuranosidase, GH127; One member of this family, from Bidobacterium longicum, UniProtKB:E8MGH8, has been characterized as an unusual beta-L-arabinofuranosidase enzyme, EC:3.2.1.185. It rleases l-arabinose from the l-arabinofuranose (Araf)-beta1,2-Araf disaccharide and also transglycosylates 1-alkanols with retention of the anomeric configuration. Terminal beta-l-arabinofuranosyl residues have been found in arabinogalactan proteins from a mumber of different plantt species. beta-l-Arabinofuranosyl linkages with 1-4 arabinofuranosides are also found in the sugar chains of extensin and solanaceous lectins, hydroxyproline (Hyp)2-rich glycoproteins that are widely observed in plant cell wall fractions. The critical residue for catalytic activity is Glu-338, in a ET/SCAS sequence context.


Pssm-ID: 400342 [Multi-domain]  Cd Length: 503  Bit Score: 596.22  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239944   111 DVRLDpDSFHWRAQQTNLEYLLMLDVDGLAWSFRKEAGLDAPGDYYGGWERPDSELRGHFVGHYLSATAYMWASTHNDTL 190
Cdd:pfam07944   1 DVRLT-DSFFGDRQQTNREYLLPLDPDRLLHTFRKEAGLPSKAIAYGGWEHPGFPFRGHDLGHWLSAVAYMLASTGDPEL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239944   191 KEKMSALVSALSECQQksGTGYLSAFPSSFFDRFEAITPVWAP---YYTIHKILAGLVDQYKLAGNSQALKMATGMADYF 267
Cdd:pfam07944  80 EARLDRLVDELAEAQQ--GDGYLGTYPESNFDRNEAGKGVWAPnheLYNLGKLIAGLVDYYQLTGKTQALDVATRLADWL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239944   268 YGRVrNVIRKYSVERHWQSlneETGGMNDVLYQLYSITGDSKYLLLAHLFDKPCFLGVLAIQADDISGFHANTHIPIVV- 346
Cdd:pfam07944 158 YDVT-DVLGDEQGQRVLVP---EHGGINEALVELYELTGDKRYLDLAKRFIHNRGLDPLAYGQDELPGRHQNTAIGHAVr 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239944   347 GSQQRYEITGDLLHKEISMFFMDIFNASHSYATGGTSVS-EFWQDPKRMATalQTENEESCTTYNMLKVSRNLFRWTKEV 425
Cdd:pfam07944 234 GAADVYEETGDDALLKAAEFFWDNVVTHHMYVTGGNGARhEHFGPPYELPN--RLAYCETCASYNMLKLTRRLFCWTPDA 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239944   426 SYADYYERALTNGVLGIQRGTQpGLMIYMLPLGKGVSKAVtyhgwgTPYDSFWCCYGTGIESFSKLGDSIYFQEDgatPA 505
Cdd:pfam07944 312 KYADYYERALYNHILAGQSPDG-GMFFYFNPLESGSYRLR------WPWDSFWCCPGNGAETHAKFGDYIYAHSD---DG 381
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239944   506 LYVTQYISSSLDWKSAGLSISQKVNpvVSWDPYMRVTFTLssskvGVAKESTLNLRIPVWtnSIGAKVSLNGRPL-NVPT 584
Cdd:pfam07944 382 IYVNLYIPSTADWKLKGVELEQETD--YPWEGKVRLTVNT-----AKKADFTLYLRIPGW--AAGATLTVNGKPTvVAPK 452
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|.
gi 15239944   585 SGNFLSIKQKWKSGDQVTMELPMSIRTEAIKDDRPEYASLQAILYGPYLLA 635
Cdd:pfam07944 453 SDGYLSIEREWKDGDRVELELPMPVRLEAAHPLVPDDPNKVAVLRGPLVLA 503
HybA1 COG3533
Beta-L-arabinofuranosidase, GH127 family [Carbohydrate transport and metabolism];
104-636 9.37e-125

Beta-L-arabinofuranosidase, GH127 family [Carbohydrate transport and metabolism];


Pssm-ID: 442754 [Multi-domain]  Cd Length: 597  Bit Score: 388.43  E-value: 9.37e-125
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239944 104 LKDVSLHDVRLDpDSFhW-RAQQTNLEYLLM-----LDVDGLAWSFRKEAGLDaPGDYyGGWErpdseLRGHFVGHYLSA 177
Cdd:COG3533   3 LRPVPLSDVRLT-DGF-WgERQELNREYTLPhqweqLEPDGLLANFRIAAGLK-KGEY-GGWE-----FDDHDVGKWLEA 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239944 178 TAYMWASTHNDTLKEKMSALVSALSECQQKsgTGYLSAFpssfFDRfEAITPVWA-----PYYTIHKILAGLVDQYKLAG 252
Cdd:COG3533  74 AAYAYARTGDPELEARLDYVIDELAAAQEP--DGYLGTY----FTI-EGGEKRWVlrlshELYNAGHLIEGAVAHYRATG 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239944 253 NSQALKMATGMADYFYgrvrNVIRKYSVERHWqslNEETGGMNDVLYQLYSITGDSKYLLLAHLFDKPCFLGVLA----- 327
Cdd:COG3533 147 KRKLLDVAIRLADWID----DTFGPLPDQLQG---MLGHGGIEEALVELYRVTGDKRYLDLAKRFIDRRGRLPLRggeyf 219
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239944 328 ------IQADDISGfHANTHIPIVVGSQQRYEITGDLLHKEISMFFMDIFNASHSYATGGTSVS---EFWQDPKRMATAl 398
Cdd:COG3533 220 qdhdplREQTDAVG-HAVRAIYLYAGAADVAAETGDEEYLDALERLWDNVVNRKMYITGGNGSRhdgEAFGPDYDLPND- 297
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239944 399 qTENEESCTTYNMLKVSRNLFRWTKEVSYADYYERALTNGVLGiqrGTQP--GLMIYMLPLgkgvskAVTYHGWGTPYDS 476
Cdd:COG3533 298 -TAYAETCASIGMLKLNRRLLLLTGDAKYADVYERALYNHILS---GQSLdgGGFFYFNPL------RSGGYHERQPWFG 367
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239944 477 FWCCYGTGIESFSKLGDSIYFQEDGatpALYVTQYISSSLDWKSAG--LSISQKVN-PvvsWDPymRVTFTLSSSKvgvA 553
Cdd:COG3533 368 CACCPGNGARTLASLGGYIYATSDD---GLYVNLYIGSTLNWKLDGkgVKLRQETNyP---WDG--KVRITVDPAK---P 436
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239944 554 KESTLNLRIPVWtnSIGAKVSLNGRPLNVPTS-GNFLSIKQKWKSGDQVTMELPMSIRTEA----IKDDRPEYaslqAIL 628
Cdd:COG3533 437 GEFTLRLRIPGW--AKGATVKVNGKPVDAEVEpGSYATINRTWKKGDVVELDLPMPVRLVEanprVPDDRGKV----AVK 510

                ....*...
gi 15239944 629 YGPYLLAG 636
Cdd:COG3533 511 RGPLVYCA 518
beta-trefoil_ABD_ABFB-like cd23265
Arabinose-binding domain (ABD), beta-trefoil fold, found in the ABFB family; The ABFB family ...
723-854 1.94e-08

Arabinose-binding domain (ABD), beta-trefoil fold, found in the ABFB family; The ABFB family includes alpha-L-arabinofuranosidase B (ABF B)-like proteins and otogelin-like proteins. Alpha-L-arabinofuranosidase (EC 3.2.1.55), also called ABF, or non-reducing end alpha-L-arabinofuranosidase, or arabinofuranosidase, or arabinosidase, is involved in the degradation of arabinoxylan, a major component of plant hemicellulose. It can hydrolyze 1,5-, 1,3- and 1,2-alpha-linkages not only in L-arabinofuranosyl oligosaccharides, but also in polysaccharides containing terminal non-reducing L-arabinofuranoses in side chains, like L-arabinan, arabinogalactan and arabinoxylan. ABF belongs to the glycosyl hydrolase 54 family. Hungateiclostridium thermocellum anti-sigma-I factor RsgI5 shows high sequence similarity with ABF B. It negatively regulates SigI5 activity through direct interaction. The OTOG subfamily includes otogelin (OTOG) and otogelin-like protein (OTOGL). OTOG is a glycoprotein specific to acellular membranes of the inner ear. It may be required for the anchoring of otoconial membranes and cupula to the underlying neuroepithelia in the vestibule. OTOG may be involved in the organization and/or stabilization of the fibrillar network that compose the tectorial membrane in the cochlea. OTOGL is a mucin glycoprotein that is a component of the tectorial membrane. It acts as a gel-forming mucin that forms high-molecular-weight complexes and is glycosylated through mucin-type O-glycosylation. Mutations in OTOG or OTOGL genes may cause hearing loss. Members of the ABFB family contain an ABD with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ABD binds two arabinose molecules in the beta and gamma subdomains.


Pssm-ID: 467807  Cd Length: 135  Bit Score: 53.82  E-value: 1.94e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239944 723 GRLVMLEPFDFPGMIVKQATDSSLTVQASSPSdKGASSFRLVSGLDGKlGSVSLRLESKKGCFVYSdqtlkQGTKLRLEC 802
Cdd:cd23265   3 GTPVRLRSASDPGYYIRHDGGSGSVTSDDDDS-AEDAFFRVVPGLAGE-GTVSFESVDKPGYYLRH-----RGGELRLEK 75
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 15239944 803 GSDATDekFKEAASFSLKTGMHQYNPMSFVMSGTQRNFVLSPLFSLRDETYN 854
Cdd:cd23265  76 NDGSAA--FREDATFRPRPGLADPGGVSFESVNYPGYYLRHRNNRLVLGKVD 125
 
Name Accession Description Interval E-value
Glyco_hydro_127 pfam07944
Beta-L-arabinofuranosidase, GH127; One member of this family, from Bidobacterium longicum, ...
111-635 0e+00

Beta-L-arabinofuranosidase, GH127; One member of this family, from Bidobacterium longicum, UniProtKB:E8MGH8, has been characterized as an unusual beta-L-arabinofuranosidase enzyme, EC:3.2.1.185. It rleases l-arabinose from the l-arabinofuranose (Araf)-beta1,2-Araf disaccharide and also transglycosylates 1-alkanols with retention of the anomeric configuration. Terminal beta-l-arabinofuranosyl residues have been found in arabinogalactan proteins from a mumber of different plantt species. beta-l-Arabinofuranosyl linkages with 1-4 arabinofuranosides are also found in the sugar chains of extensin and solanaceous lectins, hydroxyproline (Hyp)2-rich glycoproteins that are widely observed in plant cell wall fractions. The critical residue for catalytic activity is Glu-338, in a ET/SCAS sequence context.


Pssm-ID: 400342 [Multi-domain]  Cd Length: 503  Bit Score: 596.22  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239944   111 DVRLDpDSFHWRAQQTNLEYLLMLDVDGLAWSFRKEAGLDAPGDYYGGWERPDSELRGHFVGHYLSATAYMWASTHNDTL 190
Cdd:pfam07944   1 DVRLT-DSFFGDRQQTNREYLLPLDPDRLLHTFRKEAGLPSKAIAYGGWEHPGFPFRGHDLGHWLSAVAYMLASTGDPEL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239944   191 KEKMSALVSALSECQQksGTGYLSAFPSSFFDRFEAITPVWAP---YYTIHKILAGLVDQYKLAGNSQALKMATGMADYF 267
Cdd:pfam07944  80 EARLDRLVDELAEAQQ--GDGYLGTYPESNFDRNEAGKGVWAPnheLYNLGKLIAGLVDYYQLTGKTQALDVATRLADWL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239944   268 YGRVrNVIRKYSVERHWQSlneETGGMNDVLYQLYSITGDSKYLLLAHLFDKPCFLGVLAIQADDISGFHANTHIPIVV- 346
Cdd:pfam07944 158 YDVT-DVLGDEQGQRVLVP---EHGGINEALVELYELTGDKRYLDLAKRFIHNRGLDPLAYGQDELPGRHQNTAIGHAVr 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239944   347 GSQQRYEITGDLLHKEISMFFMDIFNASHSYATGGTSVS-EFWQDPKRMATalQTENEESCTTYNMLKVSRNLFRWTKEV 425
Cdd:pfam07944 234 GAADVYEETGDDALLKAAEFFWDNVVTHHMYVTGGNGARhEHFGPPYELPN--RLAYCETCASYNMLKLTRRLFCWTPDA 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239944   426 SYADYYERALTNGVLGIQRGTQpGLMIYMLPLGKGVSKAVtyhgwgTPYDSFWCCYGTGIESFSKLGDSIYFQEDgatPA 505
Cdd:pfam07944 312 KYADYYERALYNHILAGQSPDG-GMFFYFNPLESGSYRLR------WPWDSFWCCPGNGAETHAKFGDYIYAHSD---DG 381
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239944   506 LYVTQYISSSLDWKSAGLSISQKVNpvVSWDPYMRVTFTLssskvGVAKESTLNLRIPVWtnSIGAKVSLNGRPL-NVPT 584
Cdd:pfam07944 382 IYVNLYIPSTADWKLKGVELEQETD--YPWEGKVRLTVNT-----AKKADFTLYLRIPGW--AAGATLTVNGKPTvVAPK 452
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|.
gi 15239944   585 SGNFLSIKQKWKSGDQVTMELPMSIRTEAIKDDRPEYASLQAILYGPYLLA 635
Cdd:pfam07944 453 SDGYLSIEREWKDGDRVELELPMPVRLEAAHPLVPDDPNKVAVLRGPLVLA 503
HybA1 COG3533
Beta-L-arabinofuranosidase, GH127 family [Carbohydrate transport and metabolism];
104-636 9.37e-125

Beta-L-arabinofuranosidase, GH127 family [Carbohydrate transport and metabolism];


Pssm-ID: 442754 [Multi-domain]  Cd Length: 597  Bit Score: 388.43  E-value: 9.37e-125
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239944 104 LKDVSLHDVRLDpDSFhW-RAQQTNLEYLLM-----LDVDGLAWSFRKEAGLDaPGDYyGGWErpdseLRGHFVGHYLSA 177
Cdd:COG3533   3 LRPVPLSDVRLT-DGF-WgERQELNREYTLPhqweqLEPDGLLANFRIAAGLK-KGEY-GGWE-----FDDHDVGKWLEA 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239944 178 TAYMWASTHNDTLKEKMSALVSALSECQQKsgTGYLSAFpssfFDRfEAITPVWA-----PYYTIHKILAGLVDQYKLAG 252
Cdd:COG3533  74 AAYAYARTGDPELEARLDYVIDELAAAQEP--DGYLGTY----FTI-EGGEKRWVlrlshELYNAGHLIEGAVAHYRATG 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239944 253 NSQALKMATGMADYFYgrvrNVIRKYSVERHWqslNEETGGMNDVLYQLYSITGDSKYLLLAHLFDKPCFLGVLA----- 327
Cdd:COG3533 147 KRKLLDVAIRLADWID----DTFGPLPDQLQG---MLGHGGIEEALVELYRVTGDKRYLDLAKRFIDRRGRLPLRggeyf 219
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239944 328 ------IQADDISGfHANTHIPIVVGSQQRYEITGDLLHKEISMFFMDIFNASHSYATGGTSVS---EFWQDPKRMATAl 398
Cdd:COG3533 220 qdhdplREQTDAVG-HAVRAIYLYAGAADVAAETGDEEYLDALERLWDNVVNRKMYITGGNGSRhdgEAFGPDYDLPND- 297
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239944 399 qTENEESCTTYNMLKVSRNLFRWTKEVSYADYYERALTNGVLGiqrGTQP--GLMIYMLPLgkgvskAVTYHGWGTPYDS 476
Cdd:COG3533 298 -TAYAETCASIGMLKLNRRLLLLTGDAKYADVYERALYNHILS---GQSLdgGGFFYFNPL------RSGGYHERQPWFG 367
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239944 477 FWCCYGTGIESFSKLGDSIYFQEDGatpALYVTQYISSSLDWKSAG--LSISQKVN-PvvsWDPymRVTFTLSSSKvgvA 553
Cdd:COG3533 368 CACCPGNGARTLASLGGYIYATSDD---GLYVNLYIGSTLNWKLDGkgVKLRQETNyP---WDG--KVRITVDPAK---P 436
                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239944 554 KESTLNLRIPVWtnSIGAKVSLNGRPLNVPTS-GNFLSIKQKWKSGDQVTMELPMSIRTEA----IKDDRPEYaslqAIL 628
Cdd:COG3533 437 GEFTLRLRIPGW--AKGATVKVNGKPVDAEVEpGSYATINRTWKKGDVVELDLPMPVRLVEanprVPDDRGKV----AVK 510

                ....*...
gi 15239944 629 YGPYLLAG 636
Cdd:COG3533 511 RGPLVYCA 518
beta-trefoil_ABD_ABFB-like cd23265
Arabinose-binding domain (ABD), beta-trefoil fold, found in the ABFB family; The ABFB family ...
723-854 1.94e-08

Arabinose-binding domain (ABD), beta-trefoil fold, found in the ABFB family; The ABFB family includes alpha-L-arabinofuranosidase B (ABF B)-like proteins and otogelin-like proteins. Alpha-L-arabinofuranosidase (EC 3.2.1.55), also called ABF, or non-reducing end alpha-L-arabinofuranosidase, or arabinofuranosidase, or arabinosidase, is involved in the degradation of arabinoxylan, a major component of plant hemicellulose. It can hydrolyze 1,5-, 1,3- and 1,2-alpha-linkages not only in L-arabinofuranosyl oligosaccharides, but also in polysaccharides containing terminal non-reducing L-arabinofuranoses in side chains, like L-arabinan, arabinogalactan and arabinoxylan. ABF belongs to the glycosyl hydrolase 54 family. Hungateiclostridium thermocellum anti-sigma-I factor RsgI5 shows high sequence similarity with ABF B. It negatively regulates SigI5 activity through direct interaction. The OTOG subfamily includes otogelin (OTOG) and otogelin-like protein (OTOGL). OTOG is a glycoprotein specific to acellular membranes of the inner ear. It may be required for the anchoring of otoconial membranes and cupula to the underlying neuroepithelia in the vestibule. OTOG may be involved in the organization and/or stabilization of the fibrillar network that compose the tectorial membrane in the cochlea. OTOGL is a mucin glycoprotein that is a component of the tectorial membrane. It acts as a gel-forming mucin that forms high-molecular-weight complexes and is glycosylated through mucin-type O-glycosylation. Mutations in OTOG or OTOGL genes may cause hearing loss. Members of the ABFB family contain an ABD with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ABD binds two arabinose molecules in the beta and gamma subdomains.


Pssm-ID: 467807  Cd Length: 135  Bit Score: 53.82  E-value: 1.94e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239944 723 GRLVMLEPFDFPGMIVKQATDSSLTVQASSPSdKGASSFRLVSGLDGKlGSVSLRLESKKGCFVYSdqtlkQGTKLRLEC 802
Cdd:cd23265   3 GTPVRLRSASDPGYYIRHDGGSGSVTSDDDDS-AEDAFFRVVPGLAGE-GTVSFESVDKPGYYLRH-----RGGELRLEK 75
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 15239944 803 GSDATDekFKEAASFSLKTGMHQYNPMSFVMSGTQRNFVLSPLFSLRDETYN 854
Cdd:cd23265  76 NDGSAA--FREDATFRPRPGLADPGGVSFESVNYPGYYLRHRNNRLVLGKVD 125
beta-trefoil_ABD_ABFB-like cd23265
Arabinose-binding domain (ABD), beta-trefoil fold, found in the ABFB family; The ABFB family ...
670-817 3.31e-03

Arabinose-binding domain (ABD), beta-trefoil fold, found in the ABFB family; The ABFB family includes alpha-L-arabinofuranosidase B (ABF B)-like proteins and otogelin-like proteins. Alpha-L-arabinofuranosidase (EC 3.2.1.55), also called ABF, or non-reducing end alpha-L-arabinofuranosidase, or arabinofuranosidase, or arabinosidase, is involved in the degradation of arabinoxylan, a major component of plant hemicellulose. It can hydrolyze 1,5-, 1,3- and 1,2-alpha-linkages not only in L-arabinofuranosyl oligosaccharides, but also in polysaccharides containing terminal non-reducing L-arabinofuranoses in side chains, like L-arabinan, arabinogalactan and arabinoxylan. ABF belongs to the glycosyl hydrolase 54 family. Hungateiclostridium thermocellum anti-sigma-I factor RsgI5 shows high sequence similarity with ABF B. It negatively regulates SigI5 activity through direct interaction. The OTOG subfamily includes otogelin (OTOG) and otogelin-like protein (OTOGL). OTOG is a glycoprotein specific to acellular membranes of the inner ear. It may be required for the anchoring of otoconial membranes and cupula to the underlying neuroepithelia in the vestibule. OTOG may be involved in the organization and/or stabilization of the fibrillar network that compose the tectorial membrane in the cochlea. OTOGL is a mucin glycoprotein that is a component of the tectorial membrane. It acts as a gel-forming mucin that forms high-molecular-weight complexes and is glycosylated through mucin-type O-glycosylation. Mutations in OTOG or OTOGL genes may cause hearing loss. Members of the ABFB family contain an ABD with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ABD binds two arabinose molecules in the beta and gamma subdomains.


Pssm-ID: 467807  Cd Length: 135  Bit Score: 38.80  E-value: 3.31e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239944 670 QQSGNVSYVFSNSNQTITMRVSPEPGTQDAVaatFRLVtdnskprisgpEGLIGR-LVMLEPFDFPGMIVKQAtDSSLTV 748
Cdd:cd23265   9 RSASDPGYYIRHDGGSGSVTSDDDDSAEDAF---FRVV-----------PGLAGEgTVSFESVDKPGYYLRHR-GGELRL 73
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15239944 749 QASSPSD--KGASSFRLVSGLDGKlGSVSLRLESKKGCFVYSDqtlkqGTKLRLecgSDATDEKFKEAASF 817
Cdd:cd23265  74 EKNDGSAafREDATFRPRPGLADP-GGVSFESVNYPGYYLRHR-----NNRLVL---GKVDSTAFKEDATF 135
beta-trefoil_ABD_ABFB cd23399
Arabinose-binding domain (ABD), beta-trefoil fold, found in alpha-L-arabinofuranosidase B (ABF ...
728-822 3.82e-03

Arabinose-binding domain (ABD), beta-trefoil fold, found in alpha-L-arabinofuranosidase B (ABF B) and similar proteins; Alpha-L-arabinofuranosidase (EC 3.2.1.55), also called ABF, or non-reducing end alpha-L-arabinofuranosidase, or arabinofuranosidase, or arabinosidase, is involved in the degradation of arabinoxylan, a major component of plant hemicellulose. It can hydrolyze 1,5-, 1,3- and 1,2-alpha-linkages not only in L-arabinofuranosyl oligosaccharides, but also in polysaccharides containing terminal non-reducing L-arabinofuranoses in side chains, like L-arabinan, arabinogalactan and arabinoxylan. ABF belongs to the glycosyl hydrolase 54 family. The family also includes Hungateiclostridium thermocellum anti-sigma-I factor RsgI5. It negatively regulates SigI5 activity through direct interaction. Binding of the polysaccharide substrate to the extracellular C-terminal sensing domain of RsgI5 may induce a conformational change in its N-terminal cytoplasmic region, leading to the release and activation of SigI5. Members of the ABFB family contain an ABD with a beta-trefoil fold, which is characterized by 12 beta strands folded into three similar trefoil subdomains (alpha, beta, and gamma) associated to give an overall structure with pseudo-3-fold symmetry. The ABD binds two arabinose molecules in the beta and gamma subdomains.


Pssm-ID: 467809  Cd Length: 138  Bit Score: 38.35  E-value: 3.82e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15239944 728 LEPFDFPGMIVKqATDSS--LTVQASSPSDKGASSFRLVSGLDGKlGSVSlrLESKKgcfvYSDQTLK-QGTKLRLEcGS 804
Cdd:cd23399   8 LRSTNYPGRYIR-HRNFLgrLDPVSSSSSDKADATFKVVPGLADS-GCVS--FESVN----YPGYYLRhYNFRLRLD-KN 78
                        90
                ....*....|....*...
gi 15239944 805 DATDeKFKEAASFSLKTG 822
Cdd:cd23399  79 DGSA-LFKEDATFCPRPG 95
 
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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