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Conserved domains on  [gi|937184879|gb|ALH43276|]
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DFA IIIase, partial [Paenarthrobacter aurescens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
IFTase cd21111
inulin fructotransferase; Inulin fructotransferase (IFTase; EC 4.2.2.17 and EC 4.2.2.18), a ...
4-450 1.10e-180

inulin fructotransferase; Inulin fructotransferase (IFTase; EC 4.2.2.17 and EC 4.2.2.18), a member of the glycoside hydrolase family 91, catalyzes depolymerization of beta-2,1-fructans inulin by successively removing the terminal difructosaccharide units as cyclic anhydrides via intramolecular fructosyl transfer. As a result, IFTase produces DFA-I (alpha-D-fructofuranose-beta-D-fructofuranose 2',1:2,1'-dianhydride) and DFA-III (alpha-D-fructofuranose-beta-D-fructofuranose 2',1:2,3'-dianhydride).


:

Pssm-ID: 411049 [Multi-domain]  Cd Length: 395  Bit Score: 510.72  E-value: 1.10e-180
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937184879   4 SNYYNVTAW--PIGDPFTGVGEVINSIIADIKDRQTatdENDGGKPGAVIYLPPGDYRLRTQVVIDVSFLRIEGSGHGFT 81
Cdd:cd21111    2 NNVYDVTTWslTSGSPYSDIGAVINDIIADIKARQT---NQDNAKPGAVIIIPPGDYGLLIQVVIDISYLIIIGSGHGFT 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937184879  82 SSSIRFNAPEAewPDLHELWPGGSRVMVDLPiidderpsdllpdqESKGAAFYVERSGSPRISSVEFSNFCIDGLHFtpd 161
Cdd:cd21111   79 SSSIRDNAGTR--SVWHEEWPGGSRIIVDNK--------------DGAPAAFLVLRDGDPRISGVEFSDFCIDGLHF--- 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937184879 162 gsglpaeNSYVNGKTGIYVASANDSFRVNGMGFVYLENALTICKADALSVHDNFIAECGSCIELRGWGQASKITDNLIGA 241
Cdd:cd21111  140 -------NSYTNGKTGIGVASDNDSFRITGMGFVYLETGIVIRGADALSIHNNFIAECGSCIELTGGGQASKITNNLLGA 212
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937184879 242 GFKGHSIYAQNHGGLLITANNIFPRGASSIHFEGVTRSSVSNNRLHSFYPGMVVLAEGSSENLVSTNHFLRDHEPWTPFL 321
Cdd:cd21111  213 GYNGYSIYAENAGGLLITGNNIFPRGASSIYLKGVNRSSITSNRLHSFYPGMIVLLGNCKENLISGNHFLRNVEPWPPFK 292
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937184879 322 GVDNGRDDLYGILRISGSNNSVIGNHFSEVVDAQSIWPSGATPVIIRLAEGTGNFVSNNHVVAMdvrsassdscfaaqvd 401
Cdd:cd21111  293 GNGNGLDDLYGILHIEGYNNIIVGNHISENVPPGNILPNGADPTIILIMSGSGNYVSNNHIVAD---------------- 356
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*....
gi 937184879 402 allttgasdgLAVTAVLVDSTSARNTILDSGNDAQVIADRGANAVRATP 450
Cdd:cd21111  357 ----------LVSNSVVVDVSSTGNTVLDSGSASQLEADGAVNAIVPTP 395
 
Name Accession Description Interval E-value
IFTase cd21111
inulin fructotransferase; Inulin fructotransferase (IFTase; EC 4.2.2.17 and EC 4.2.2.18), a ...
4-450 1.10e-180

inulin fructotransferase; Inulin fructotransferase (IFTase; EC 4.2.2.17 and EC 4.2.2.18), a member of the glycoside hydrolase family 91, catalyzes depolymerization of beta-2,1-fructans inulin by successively removing the terminal difructosaccharide units as cyclic anhydrides via intramolecular fructosyl transfer. As a result, IFTase produces DFA-I (alpha-D-fructofuranose-beta-D-fructofuranose 2',1:2,1'-dianhydride) and DFA-III (alpha-D-fructofuranose-beta-D-fructofuranose 2',1:2,3'-dianhydride).


Pssm-ID: 411049 [Multi-domain]  Cd Length: 395  Bit Score: 510.72  E-value: 1.10e-180
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937184879   4 SNYYNVTAW--PIGDPFTGVGEVINSIIADIKDRQTatdENDGGKPGAVIYLPPGDYRLRTQVVIDVSFLRIEGSGHGFT 81
Cdd:cd21111    2 NNVYDVTTWslTSGSPYSDIGAVINDIIADIKARQT---NQDNAKPGAVIIIPPGDYGLLIQVVIDISYLIIIGSGHGFT 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937184879  82 SSSIRFNAPEAewPDLHELWPGGSRVMVDLPiidderpsdllpdqESKGAAFYVERSGSPRISSVEFSNFCIDGLHFtpd 161
Cdd:cd21111   79 SSSIRDNAGTR--SVWHEEWPGGSRIIVDNK--------------DGAPAAFLVLRDGDPRISGVEFSDFCIDGLHF--- 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937184879 162 gsglpaeNSYVNGKTGIYVASANDSFRVNGMGFVYLENALTICKADALSVHDNFIAECGSCIELRGWGQASKITDNLIGA 241
Cdd:cd21111  140 -------NSYTNGKTGIGVASDNDSFRITGMGFVYLETGIVIRGADALSIHNNFIAECGSCIELTGGGQASKITNNLLGA 212
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937184879 242 GFKGHSIYAQNHGGLLITANNIFPRGASSIHFEGVTRSSVSNNRLHSFYPGMVVLAEGSSENLVSTNHFLRDHEPWTPFL 321
Cdd:cd21111  213 GYNGYSIYAENAGGLLITGNNIFPRGASSIYLKGVNRSSITSNRLHSFYPGMIVLLGNCKENLISGNHFLRNVEPWPPFK 292
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937184879 322 GVDNGRDDLYGILRISGSNNSVIGNHFSEVVDAQSIWPSGATPVIIRLAEGTGNFVSNNHVVAMdvrsassdscfaaqvd 401
Cdd:cd21111  293 GNGNGLDDLYGILHIEGYNNIIVGNHISENVPPGNILPNGADPTIILIMSGSGNYVSNNHIVAD---------------- 356
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*....
gi 937184879 402 allttgasdgLAVTAVLVDSTSARNTILDSGNDAQVIADRGANAVRATP 450
Cdd:cd21111  357 ----------LVSNSVVVDVSSTGNTVLDSGSASQLEADGAVNAIVPTP 395
Beta_helix_2 pfam18835
Beta helix repeat of Inulin fructotransferase; This region contains a right-handed parallel ...
357-450 1.35e-09

Beta helix repeat of Inulin fructotransferase; This region contains a right-handed parallel beta helix repeat unit found in Inulin fructotransferase. This Pfam entry includes sequences not found by pfam13229.


Pssm-ID: 465883  Cd Length: 68  Bit Score: 54.04  E-value: 1.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937184879  357 IWPSGATPVIIRLAEGTGNFVSNNHVVAmdvrsassdscfaaqvdallttgasdGLAVTAVLVDSTSARNTILDSGNDAQ 436
Cdd:pfam18835   1 IVPSGATPTIVLVASGARNVIATNHVVS--------------------------NVAVKHVVLDASTTGTKVLDSGTASQ 54
                          90
                  ....*....|....
gi 937184879  437 VIADRGANAVRATP 450
Cdd:pfam18835  55 LQAYTSDYAFVATP 68
NosD COG3420
Nitrous oxide reductase accessory protein NosD, contains tandem CASH domains [Inorganic ion ...
153-393 1.56e-03

Nitrous oxide reductase accessory protein NosD, contains tandem CASH domains [Inorganic ion transport and metabolism];


Pssm-ID: 442646 [Multi-domain]  Cd Length: 343  Bit Score: 40.67  E-value: 1.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937184879 153 IDGLHFTpdGSGlpaeNSYVNGKTGIYVASANDSF----RVNGMGF-VYLENAltickadalsvHDNFIAECgscielrg 227
Cdd:COG3420   82 VRGLTIT--GSG----DSLTDDDAGIYVRGADNAViennRIENNLFgIYLEGS-----------DNNVIRNN-------- 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937184879 228 wgqasKITDNLIGAGFKGHSIYAQNHGGLLItANNIFPRGASSIHFEGVTRSSVSNNRLHSFYPGmvVLAEGSSENLVST 307
Cdd:COG3420  137 -----TISGNRDLRADRGNGIHLWNSPGNVI-EGNTISGGRDGIYLEFSDNNVIRNNTIRNLRYG--IHYMYSNDNLVEG 208
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937184879 308 NHFLRDHE----PWTPFLGVDNGR---DDLYGILRISGSNNSVIGNHFSEVVDAqsiwpsgatpviIRLAEGTGNFVSNN 380
Cdd:COG3420  209 NTFRDNGAgialMYSKGNTVRGNTilgNSGYGILLKESSDSVIEGNTISGNGKG------------IFIYNSNRNTIRGN 276
                        250
                 ....*....|....*..
gi 937184879 381 HV----VAMDVRSASSD 393
Cdd:COG3420  277 LFagngIGIHLTAGSEG 293
 
Name Accession Description Interval E-value
IFTase cd21111
inulin fructotransferase; Inulin fructotransferase (IFTase; EC 4.2.2.17 and EC 4.2.2.18), a ...
4-450 1.10e-180

inulin fructotransferase; Inulin fructotransferase (IFTase; EC 4.2.2.17 and EC 4.2.2.18), a member of the glycoside hydrolase family 91, catalyzes depolymerization of beta-2,1-fructans inulin by successively removing the terminal difructosaccharide units as cyclic anhydrides via intramolecular fructosyl transfer. As a result, IFTase produces DFA-I (alpha-D-fructofuranose-beta-D-fructofuranose 2',1:2,1'-dianhydride) and DFA-III (alpha-D-fructofuranose-beta-D-fructofuranose 2',1:2,3'-dianhydride).


Pssm-ID: 411049 [Multi-domain]  Cd Length: 395  Bit Score: 510.72  E-value: 1.10e-180
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937184879   4 SNYYNVTAW--PIGDPFTGVGEVINSIIADIKDRQTatdENDGGKPGAVIYLPPGDYRLRTQVVIDVSFLRIEGSGHGFT 81
Cdd:cd21111    2 NNVYDVTTWslTSGSPYSDIGAVINDIIADIKARQT---NQDNAKPGAVIIIPPGDYGLLIQVVIDISYLIIIGSGHGFT 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937184879  82 SSSIRFNAPEAewPDLHELWPGGSRVMVDLPiidderpsdllpdqESKGAAFYVERSGSPRISSVEFSNFCIDGLHFtpd 161
Cdd:cd21111   79 SSSIRDNAGTR--SVWHEEWPGGSRIIVDNK--------------DGAPAAFLVLRDGDPRISGVEFSDFCIDGLHF--- 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937184879 162 gsglpaeNSYVNGKTGIYVASANDSFRVNGMGFVYLENALTICKADALSVHDNFIAECGSCIELRGWGQASKITDNLIGA 241
Cdd:cd21111  140 -------NSYTNGKTGIGVASDNDSFRITGMGFVYLETGIVIRGADALSIHNNFIAECGSCIELTGGGQASKITNNLLGA 212
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937184879 242 GFKGHSIYAQNHGGLLITANNIFPRGASSIHFEGVTRSSVSNNRLHSFYPGMVVLAEGSSENLVSTNHFLRDHEPWTPFL 321
Cdd:cd21111  213 GYNGYSIYAENAGGLLITGNNIFPRGASSIYLKGVNRSSITSNRLHSFYPGMIVLLGNCKENLISGNHFLRNVEPWPPFK 292
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937184879 322 GVDNGRDDLYGILRISGSNNSVIGNHFSEVVDAQSIWPSGATPVIIRLAEGTGNFVSNNHVVAMdvrsassdscfaaqvd 401
Cdd:cd21111  293 GNGNGLDDLYGILHIEGYNNIIVGNHISENVPPGNILPNGADPTIILIMSGSGNYVSNNHIVAD---------------- 356
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*....
gi 937184879 402 allttgasdgLAVTAVLVDSTSARNTILDSGNDAQVIADRGANAVRATP 450
Cdd:cd21111  357 ----------LVSNSVVVDVSSTGNTVLDSGSASQLEADGAVNAIVPTP 395
Beta_helix_2 pfam18835
Beta helix repeat of Inulin fructotransferase; This region contains a right-handed parallel ...
357-450 1.35e-09

Beta helix repeat of Inulin fructotransferase; This region contains a right-handed parallel beta helix repeat unit found in Inulin fructotransferase. This Pfam entry includes sequences not found by pfam13229.


Pssm-ID: 465883  Cd Length: 68  Bit Score: 54.04  E-value: 1.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937184879  357 IWPSGATPVIIRLAEGTGNFVSNNHVVAmdvrsassdscfaaqvdallttgasdGLAVTAVLVDSTSARNTILDSGNDAQ 436
Cdd:pfam18835   1 IVPSGATPTIVLVASGARNVIATNHVVS--------------------------NVAVKHVVLDASTTGTKVLDSGTASQ 54
                          90
                  ....*....|....
gi 937184879  437 VIADRGANAVRATP 450
Cdd:pfam18835  55 LQAYTSDYAFVATP 68
Beta_helix pfam13229
Right handed beta helix region; This region contains a parallel beta helix region that shares ...
221-350 1.45e-03

Right handed beta helix region; This region contains a parallel beta helix region that shares some similarity with Pectate lyases.


Pssm-ID: 463811 [Multi-domain]  Cd Length: 158  Bit Score: 39.31  E-value: 1.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937184879  221 SCIELRGwGQASKITDNLIgAGFKGHSIYAQNHGGLLITANNIFPRGASSIHFEGVTRSSVSNNRLHSFYPGMVVLaEGS 300
Cdd:pfam13229   1 SGILLNG-SSNATIKNNTI-SNNGGYGIYLRGSSNATIENNTITNNGGDGIEISGSSNNTISNNTISNNGGGGIAL-RGS 77
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 937184879  301 SENLVSTNHFLrdhepwtpflgvDNGRddlYGILRISGSNNSVIGNHFSE 350
Cdd:pfam13229  78 SNNLIENNTIS------------NNGG---AGIYLSDSSNNTIENNIIHN 112
NosD COG3420
Nitrous oxide reductase accessory protein NosD, contains tandem CASH domains [Inorganic ion ...
153-393 1.56e-03

Nitrous oxide reductase accessory protein NosD, contains tandem CASH domains [Inorganic ion transport and metabolism];


Pssm-ID: 442646 [Multi-domain]  Cd Length: 343  Bit Score: 40.67  E-value: 1.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937184879 153 IDGLHFTpdGSGlpaeNSYVNGKTGIYVASANDSF----RVNGMGF-VYLENAltickadalsvHDNFIAECgscielrg 227
Cdd:COG3420   82 VRGLTIT--GSG----DSLTDDDAGIYVRGADNAViennRIENNLFgIYLEGS-----------DNNVIRNN-------- 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937184879 228 wgqasKITDNLIGAGFKGHSIYAQNHGGLLItANNIFPRGASSIHFEGVTRSSVSNNRLHSFYPGmvVLAEGSSENLVST 307
Cdd:COG3420  137 -----TISGNRDLRADRGNGIHLWNSPGNVI-EGNTISGGRDGIYLEFSDNNVIRNNTIRNLRYG--IHYMYSNDNLVEG 208
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937184879 308 NHFLRDHE----PWTPFLGVDNGR---DDLYGILRISGSNNSVIGNHFSEVVDAqsiwpsgatpviIRLAEGTGNFVSNN 380
Cdd:COG3420  209 NTFRDNGAgialMYSKGNTVRGNTilgNSGYGILLKESSDSVIEGNTISGNGKG------------IFIYNSNRNTIRGN 276
                        250
                 ....*....|....*..
gi 937184879 381 HV----VAMDVRSASSD 393
Cdd:COG3420  277 LFagngIGIHLTAGSEG 293
 
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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