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Conserved domains on  [gi|1063678590|ref|NP_173142|]
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trehalose-6-phosphate synthase [Arabidopsis thaliana]

Protein Classification

PLN03063 family protein( domain architecture ID 11477380)

PLN03063 family protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLN03063 PLN03063
alpha,alpha-trehalose-phosphate synthase (UDP-forming); Provisional
2-786 0e+00

alpha,alpha-trehalose-phosphate synthase (UDP-forming); Provisional


:

Pssm-ID: 215555 [Multi-domain]  Cd Length: 797  Bit Score: 1645.36  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590   2 MDYDDARGERPRLLVVANRLPVSAKRTGENSWSLEMSPGGLVSGLLGItSQFDTKWVGWPGVDVHDEIEKNALTESLAEM 81
Cdd:PLN03063    1 MNYDDARGERPRLLVVANRLPVSAKRTGEDSWSLEMSPGGLVSALLGV-KEFETKWIGWPGVDVHDEIGKAALTESLAEK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590  82 KCIPVFLNGVFDQYYNGYCNGILWPILHHMGLPQEDQHDTNQTFETQYDAYKKANRMFLDVIIDNYEEGDIVWCHDYHLM 161
Cdd:PLN03063   80 GCIPVFLNEVFDQYYNGYCNNILWPIFHYMGLPQEDRHDATRTFESQYDAYKKANRMFLDVVKENYEEGDVVWCHDYHLM 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590 162 FLPQYLKEYNNKIKVGWFLHSPFPSSEVYKTLPSRSELLRAILAADLLGFHTYDFARHFLSTCTRILGVEGTHEGVVYQG 241
Cdd:PLN03063  160 FLPQYLKEYNNKMKVGWFLHTPFPSSEIYKTLPSRSELLRAVLTADLIGFHTYDFARHFLSACTRILGVEGTHEGVVDQG 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590 242 RVTRVAVFPIGIDPDRFIRTCKLPEVTQQMNELQEKFAGKKVILGVDRLDMIKGIPQKYLAFEKFLEENPYWRDKVVLVQ 321
Cdd:PLN03063  240 KVTRVAVFPIGIDPERFINTCELPEVKQHMKELKRFFAGRKVILGVDRLDMIKGIPQKYLAFEKFLEENPEWRDKVMLVQ 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590 322 IAVPTRNDVPEYRKLKSQVHGLVGRINGRFGSVSSLPIHHLDCSVDFNYLCAIYAIADVMLVTSLRDGMNLVSYEFVACQ 401
Cdd:PLN03063  320 IAVPTRNDVPEYQKLKSQVHELVGRINGRFGSVSSVPIHHLDCSVDFNYLCALYAITDVMLVTSLRDGMNLVSYEFVACQ 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590 402 EAKKGVLVLSEFAGAGQSLGVGALIVNPWDVTEVSSAIKEALNMPAEERETRHRSNFQYVCTHSAEKWGLDFMSELNGII 481
Cdd:PLN03063  400 KAKKGVLVLSEFAGAGQSLGAGALLVNPWNITEVSSAIKEALNMSDEERETRHRHNFQYVKTHSAQKWADDFMSELNDII 479
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590 482 PESEMQMRKIPLQLPEQDVIQQYSQSNNRLIILGFFGTLAEPMNSGTKEMDLKLNPELKGTLKALCNDPKTTVVVLSRSG 561
Cdd:PLN03063  480 VEAELRTRNIPLELPEQDVIQQYSKSNNRLLILGFYGTLTEPRNSQIKEMDLGLHPELKETLKALCSDPKTTVVVLSRSG 559
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590 562 KNILNKNFGESNIWLAAENGMFEKQTTGEWVTNMPQNVNLDWVDGVKNVFKYFTDRTPRSYFEASETSLVWNYEYADVEF 641
Cdd:PLN03063  560 KDILDKNFGEYNIWLAAENGMFLRHTSGEWVTTMPEHMNLDWVDGVKNVFKYFTDRTPRSYVEKSETSLVWNYEYADVEF 639
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590 642 GRAQARDLLQYLWAGPISNASVDVVRGNHSVEVHAIGETKGAAIGRILGEIVHRKSMTTPIDFVFCSGYFLEKDEDIYTF 721
Cdd:PLN03063  640 GRAQARDMLQHLWAGPISNASVDVVRGQKSVEVHAIGVTKGAAIGRILGEIVHNKSMTTPIDFVFCSGYFLEKDEDVYTF 719
                         730       740       750       760       770       780       790
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063678590 722 FESKILSSK--------------SPNGLDLKKENYFSAAIGQARTKARYVIDSAHGVVDLLHKLAvVADTTMTDSFSDS 786
Cdd:PLN03063  720 FEPEILSKKkssssnysdsdkkvSSNLVDLKGENYFSCAIGQARTKARYVLDSSNDVVSLLHKLA-VANTTMTDSFSDV 797
 
Name Accession Description Interval E-value
PLN03063 PLN03063
alpha,alpha-trehalose-phosphate synthase (UDP-forming); Provisional
2-786 0e+00

alpha,alpha-trehalose-phosphate synthase (UDP-forming); Provisional


Pssm-ID: 215555 [Multi-domain]  Cd Length: 797  Bit Score: 1645.36  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590   2 MDYDDARGERPRLLVVANRLPVSAKRTGENSWSLEMSPGGLVSGLLGItSQFDTKWVGWPGVDVHDEIEKNALTESLAEM 81
Cdd:PLN03063    1 MNYDDARGERPRLLVVANRLPVSAKRTGEDSWSLEMSPGGLVSALLGV-KEFETKWIGWPGVDVHDEIGKAALTESLAEK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590  82 KCIPVFLNGVFDQYYNGYCNGILWPILHHMGLPQEDQHDTNQTFETQYDAYKKANRMFLDVIIDNYEEGDIVWCHDYHLM 161
Cdd:PLN03063   80 GCIPVFLNEVFDQYYNGYCNNILWPIFHYMGLPQEDRHDATRTFESQYDAYKKANRMFLDVVKENYEEGDVVWCHDYHLM 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590 162 FLPQYLKEYNNKIKVGWFLHSPFPSSEVYKTLPSRSELLRAILAADLLGFHTYDFARHFLSTCTRILGVEGTHEGVVYQG 241
Cdd:PLN03063  160 FLPQYLKEYNNKMKVGWFLHTPFPSSEIYKTLPSRSELLRAVLTADLIGFHTYDFARHFLSACTRILGVEGTHEGVVDQG 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590 242 RVTRVAVFPIGIDPDRFIRTCKLPEVTQQMNELQEKFAGKKVILGVDRLDMIKGIPQKYLAFEKFLEENPYWRDKVVLVQ 321
Cdd:PLN03063  240 KVTRVAVFPIGIDPERFINTCELPEVKQHMKELKRFFAGRKVILGVDRLDMIKGIPQKYLAFEKFLEENPEWRDKVMLVQ 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590 322 IAVPTRNDVPEYRKLKSQVHGLVGRINGRFGSVSSLPIHHLDCSVDFNYLCAIYAIADVMLVTSLRDGMNLVSYEFVACQ 401
Cdd:PLN03063  320 IAVPTRNDVPEYQKLKSQVHELVGRINGRFGSVSSVPIHHLDCSVDFNYLCALYAITDVMLVTSLRDGMNLVSYEFVACQ 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590 402 EAKKGVLVLSEFAGAGQSLGVGALIVNPWDVTEVSSAIKEALNMPAEERETRHRSNFQYVCTHSAEKWGLDFMSELNGII 481
Cdd:PLN03063  400 KAKKGVLVLSEFAGAGQSLGAGALLVNPWNITEVSSAIKEALNMSDEERETRHRHNFQYVKTHSAQKWADDFMSELNDII 479
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590 482 PESEMQMRKIPLQLPEQDVIQQYSQSNNRLIILGFFGTLAEPMNSGTKEMDLKLNPELKGTLKALCNDPKTTVVVLSRSG 561
Cdd:PLN03063  480 VEAELRTRNIPLELPEQDVIQQYSKSNNRLLILGFYGTLTEPRNSQIKEMDLGLHPELKETLKALCSDPKTTVVVLSRSG 559
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590 562 KNILNKNFGESNIWLAAENGMFEKQTTGEWVTNMPQNVNLDWVDGVKNVFKYFTDRTPRSYFEASETSLVWNYEYADVEF 641
Cdd:PLN03063  560 KDILDKNFGEYNIWLAAENGMFLRHTSGEWVTTMPEHMNLDWVDGVKNVFKYFTDRTPRSYVEKSETSLVWNYEYADVEF 639
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590 642 GRAQARDLLQYLWAGPISNASVDVVRGNHSVEVHAIGETKGAAIGRILGEIVHRKSMTTPIDFVFCSGYFLEKDEDIYTF 721
Cdd:PLN03063  640 GRAQARDMLQHLWAGPISNASVDVVRGQKSVEVHAIGVTKGAAIGRILGEIVHNKSMTTPIDFVFCSGYFLEKDEDVYTF 719
                         730       740       750       760       770       780       790
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063678590 722 FESKILSSK--------------SPNGLDLKKENYFSAAIGQARTKARYVIDSAHGVVDLLHKLAvVADTTMTDSFSDS 786
Cdd:PLN03063  720 FEPEILSKKkssssnysdsdkkvSSNLVDLKGENYFSCAIGQARTKARYVLDSSNDVVSLLHKLA-VANTTMTDSFSDV 797
Glyco_transf_20 pfam00982
Glycosyltransferase family 20; Members of this family belong to glycosyl transferase family 20. ...
12-478 0e+00

Glycosyltransferase family 20; Members of this family belong to glycosyl transferase family 20. OtsA (Trehalose-6-phosphate synthase) is homologous to regions in the subunits of yeast trehalose-6-phosphate synthase/phosphate complex,.


Pssm-ID: 425972 [Multi-domain]  Cd Length: 471  Bit Score: 668.22  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590  12 PRLLVVANRLPVSAKR---TGENSWSLEMSPGGLVSGLLGITSQFDTKWVGWPGVDVHDEIEKNALTESLAEM-KCIPVF 87
Cdd:pfam00982   1 SRLVVVSNRLPVTAVRdeeDGKWEFSIKMSSGGLVSALNGLSAATEGVWVGWPGVPVDESEPKDKVSQSLKEKfNCVPVF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590  88 LNG-VFDQYYNGYCNGILWPILHHM-GLPQEDQHDtnqtfETQYDAYKKANRMFLDVIIDNYEEGDIVWCHDYHLMFLPQ 165
Cdd:pfam00982  81 LSDeLFDSYYNGFSNSILWPLFHYMiPPNNEDAFD-----RSWWDAYVKVNKLFADKIVEVYKDGDLIWIHDYHLMLLPQ 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590 166 YLKEYNNKIKVGWFLHSPFPSSEVYKTLPSRSELLRAILAADLLGFHTYDFARHFLSTCTRILGVEGTHE-GVVYQGRVT 244
Cdd:pfam00982 156 MLRKRLPDAKIGFFLHTPFPSSEIFRCLPVREEILEGLLGADLIGFHTYDYARHFLSCCSRLLGLETRSDgGVEYGGRTV 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590 245 RVAVFPIGIDPDRFIRTCKLPEVTQQMNELQEKFAGK-KVILGVDRLDMIKGIPQKYLAFEKFLEENPYWRDKVVLVQIA 323
Cdd:pfam00982 236 SVKAFPIGIDPGRIESGLASPSVQEKIKELKERFGNKkKLIVGVDRLDYIKGIPQKLLAFERFLEEYPEWRGKVVLVQIA 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590 324 VPTRNDVPEYRKLKSQVHGLVGRINGRFGSVSSLPIHHLDCSVDFNYLCAIYAIADVMLVTSLRDGMNLVSYEFVACQEA 403
Cdd:pfam00982 316 VPSRGDVEEYQNLRSQIEELVGRINGEFGTLDYTPVHFLHRPLDFDELIALYAVADVCLVTSLRDGMNLVAYEYVACQQG 395
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063678590 404 KKGVLVLSEFAGAGQSLGVGALIVNPWDVTEVSSAIKEALNMPAEERETRHRSNFQYVCTHSAEKWGLDFMSELN 478
Cdd:pfam00982 396 RKGVLILSEFAGAAQSLNDGAILVNPWDIDEVAEAINEALTMSEEERKKRHKKLYKYISKHDSQHWAESFLSDLK 470
trehalose_OtsA TIGR02400
alpha,alpha-trehalose-phosphate synthase [UDP-forming]; This enzyme catalyzes the key, ...
13-478 0e+00

alpha,alpha-trehalose-phosphate synthase [UDP-forming]; This enzyme catalyzes the key, penultimate step in biosynthesis of trehalose, a compatible solute made as an osmoprotectant in some species in all three domains of life. The gene symbol OtsA stands for osmotically regulated trehalose synthesis A. Trehalose helps protect against both osmotic and thermal stresses, and is made from two glucose subunits. This model excludes glucosylglycerol-phosphate synthase, an enzyme of an analogous osmoprotectant system in many cyanobacterial strains. This model does not identify archaeal examples, as they are more divergent than glucosylglycerol-phosphate synthase. Sequences that score in the gray zone between the trusted and noise cutoffs include a number of yeast multidomain proteins in which the N-terminal domain may be functionally equivalent to this family. The gray zone also includes the OtsA of Cornyebacterium glutamicum (and related species), shown to be responsible for synthesis of only trace amounts of trehalose while the majority is synthesized by the TreYZ pathway; the significance of OtsA in this species is unclear (see Wolf, et al., ). [Cellular processes, Adaptations to atypical conditions]


Pssm-ID: 274112  Cd Length: 456  Bit Score: 664.36  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590  13 RLLVVANRLPVSAKRTGenswsLEMSPGGLVSGLLGITSQFDTKWVGWPGVDVHDEIEKNALTESLAEM-KCIPVFLNG- 90
Cdd:TIGR02400   1 RLIVVSNRLPVPITRGG-----LEPSAGGLAVALLGALKATGGVWFGWSGKTVEEDEGEPFLRTELEGKiTLAPVFLSEe 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590  91 VFDQYYNGYCNGILWPILHhmGLPQEDQHDtnqtfETQYDAYKKANRMFLDVIIDNYEEGDIVWCHDYHLMFLPQYLKEY 170
Cdd:TIGR02400  76 DVDGYYNGFSNSTLWPLFH--YRPDLIRYD-----RKAWEAYRRVNRLFAEALAPLLQPGDIVWVHDYHLMLLPAMLREL 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590 171 NNKIKVGWFLHSPFPSSEVYKTLPSRSELLRAILAADLLGFHTYDFARHFLSTCTRILGVEGTHEGVVYQGRVTRVAVFP 250
Cdd:TIGR02400 149 GVQNKIGFFLHIPFPSSEIYRTLPWRRELLEGLLAYDLVGFQTYDDARNFLSAVSRELGLETLPNGVESGGRTVRVGAFP 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590 251 IGIDPDRFIRTCKLPEVTQQMNELQEKFAGKKVILGVDRLDMIKGIPQKYLAFEKFLEENPYWRDKVVLVQIAVPTRNDV 330
Cdd:TIGR02400 229 IGIDVDRFAEQAKKPSVQKRIAELRESLKGRKLIIGVDRLDYSKGLPERLLAFERFLEEHPEWRGKVVLVQIAVPSRGDV 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590 331 PEYRKLKSQVHGLVGRINGRFGSVSSLPIHHLDCSVDFNYLCAIYAIADVMLVTSLRDGMNLVSYEFVACQEAKKGVLVL 410
Cdd:TIGR02400 309 PEYQQLRRQVEELVGRINGRFGTLDWTPIRYLNRSYDREELMALYRAADVGLVTPLRDGMNLVAKEYVAAQDPKDGVLIL 388
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063678590 411 SEFAGAGQSLGvGALIVNPWDVTEVSSAIKEALNMPAEERETRHRSNFQYVCTHSAEKWGLDFMSELN 478
Cdd:TIGR02400 389 SEFAGAAQELN-GALLVNPYDIDGMADAIARALTMPLEEREERHRAMMDKLRKNDVQRWREDFLSDLN 455
GT20_TPS cd03788
trehalose-6-phosphate synthase; Trehalose-6-Phosphate Synthase (TPS, EC 2.4.1.15) is a ...
13-478 0e+00

trehalose-6-phosphate synthase; Trehalose-6-Phosphate Synthase (TPS, EC 2.4.1.15) is a glycosyltransferase that catalyses the synthesis of alpha,alpha-1,1-trehalose-6-phosphate from glucose-6-phosphate using a UDP-glucose donor. It is a key enzyme in the trehalose synthesis pathway. Trehalose is a nonreducing disaccharide present in a wide variety of organisms and may serve as a source of energy and carbon. It is characterized most notably in insect, plant, and microbial cells. Its production is often associated with a variety of stress conditions, including desiccation, dehydration, heat, cold, and oxidation. This family represents the catalytic domain of the TPS. Some members of this domain family coexist with a C-terminal trehalose phosphatase domain.


Pssm-ID: 340820 [Multi-domain]  Cd Length: 463  Bit Score: 642.71  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590  13 RLLVVANRLPVSAKRTGENSWSLEMSPGGLVSGLLGITSQFDTKWVGWPGVDV-HDEIEKNALTESLAEMKCIPVFLN-G 90
Cdd:cd03788     1 RLIVVSNRLPVTLERDDDGEVEFRRSAGGLVTALKGLLKSTGGLWVGWPGIEAdEEESDQVVSPELLEEYNVVPVFLSdE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590  91 VFDQYYNGYCNGILWPILHHMglpqedQHDTNQTFETQ-YDAYKKANRMFLDVIIDNYEEGDIVWCHDYHLMFLPQYLKE 169
Cdd:cd03788    81 DFEGYYNGFSNSVLWPLFHYL------LPLPDGRFEREwWEAYVRVNQAFADAVVEVYRPGDLIWVHDYHLLLLPQMLRE 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590 170 YNNKIKVGWFLHSPFPSSEVYKTLPSRSELLRAILAADLLGFHTYDFARHFLSTCTRILGVEGTHEGVV-YQGRVTRVAV 248
Cdd:cd03788   155 RLPDARIGFFLHIPFPSSEIFRCLPWREEILRGLLGADLIGFQTFEYARHFLSCCSRLLGLETTSAGGVeYGGRRVRVGA 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590 249 FPIGIDPDRFIRTCKLPEVTQQMNELQEKFAGKKVILGVDRLDMIKGIPQKYLAFEKFLEENPYWRDKVVLVQIAVPTRN 328
Cdd:cd03788   235 FPIGIDPDRFRRLAASPEVQERARELRERYKGKKLIVGVDRLDYTKGIPEKLLAFERFLERYPEWRGKVVLVQVAVPSRT 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590 329 DVPEYRKLKSQVHGLVGRINGRFGSVSSLPIHHLDCSVDFNYLCAIYAIADVMLVTSLRDGMNLVSYEFVACQEAKKGVL 408
Cdd:cd03788   315 DVEEYQELRREVEELVGRINGRFGTLDWTPVVYLHQSLDREELLALYRAADVALVTSLRDGMNLVAKEYVACQRDNPGVL 394
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590 409 VLSEFAGAGQSLGvGALIVNPWDVTEVSSAIKEALNMPAEERETRHRSNFQYVCTHSAEKWGLDFMSELN 478
Cdd:cd03788   395 ILSEFAGAASELD-GAILVNPWDIEEVAEAINRALTMSPEERKERHQKLRKYVETHDVQAWANSFLDDLA 463
OtsA COG0380
Trehalose-6-phosphate synthase, GT20 family [Carbohydrate transport and metabolism];
13-480 0e+00

Trehalose-6-phosphate synthase, GT20 family [Carbohydrate transport and metabolism];


Pssm-ID: 440149  Cd Length: 474  Bit Score: 579.00  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590  13 RLLVVANRLPVSAKRTGeNSWSLEMSPGGLVSGLLGITSQFDTKWVGWPGVDVHDEIEKN---ALTESLAEMKCIPVFLN 89
Cdd:COG0380     3 RLVVVSNRLPVPHVRED-GSIRVKRSAGGLVTALEPVLRRRGGLWVGWSGGDADREAVEEprgPVPPDLGGYTLAPVDLS 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590  90 -GVFDQYYNGYCNGILWPILHHM-GLPQEDQHDtnqtfetqYDAYKKANRMFLDVIIDNYEEGDIVWCHDYHLMFLPQYL 167
Cdd:COG0380    82 aEEVDGYYEGFSNETLWPLFHYRlDLPEFDRED--------WEAYRRVNRRFAEALAEEAEPDDVVWVHDYHLLLVPAML 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590 168 KEYNNKIKVGWFLHSPFPSSEVYKTLPSRSELLRAILAADLLGFHTYDFARHFLSTCTRILGVEGTHEGVV-YQGRVTRV 246
Cdd:COG0380   154 RELGPDARIGFFLHIPFPPPEIFRILPWREEILEGLLGADLIGFQTPRDARNFLDCVRRLLGAEVDEGGTVrYGGRTVRV 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590 247 AVFPIGIDPDRFIRTCKLPEVTQQMNELQEKFAGKKVILGVDRLDMIKGIPQKYLAFEKFLEENPYWRDKVVLVQIAVPT 326
Cdd:COG0380   234 GAFPIGIDVEEFAELARSPEVRARAERLREELGGRKLILGVDRLDYTKGIPERLRAFERLLERHPELRGKVTLLQIAVPS 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590 327 RNDVPEYRKLKSQVHGLVGRINGRFGSVSSLPIHHLDCSVDFNYLCAIYAIADVMLVTSLRDGMNLVSYEFVACQEAKKG 406
Cdd:COG0380   314 REDVPAYRELRREIEELVGRINGRFGTLDWTPIRYLNRSLPREELAALYRAADVALVTPLRDGMNLVAKEYVAAQPDDPG 393
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063678590 407 VLVLSEFAGAGQSLGvGALIVNPWDVTEVSSAIKEALNMPAEERETRHRSNFQYVCTHSAEKWGLDFMSELNGI 480
Cdd:COG0380   394 VLVLSEFAGAAEELT-EALLVNPYDIDGMAEAIHRALTMPLEERRRRMRALRERVRRYDVHRWADDFLDALAAV 466
 
Name Accession Description Interval E-value
PLN03063 PLN03063
alpha,alpha-trehalose-phosphate synthase (UDP-forming); Provisional
2-786 0e+00

alpha,alpha-trehalose-phosphate synthase (UDP-forming); Provisional


Pssm-ID: 215555 [Multi-domain]  Cd Length: 797  Bit Score: 1645.36  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590   2 MDYDDARGERPRLLVVANRLPVSAKRTGENSWSLEMSPGGLVSGLLGItSQFDTKWVGWPGVDVHDEIEKNALTESLAEM 81
Cdd:PLN03063    1 MNYDDARGERPRLLVVANRLPVSAKRTGEDSWSLEMSPGGLVSALLGV-KEFETKWIGWPGVDVHDEIGKAALTESLAEK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590  82 KCIPVFLNGVFDQYYNGYCNGILWPILHHMGLPQEDQHDTNQTFETQYDAYKKANRMFLDVIIDNYEEGDIVWCHDYHLM 161
Cdd:PLN03063   80 GCIPVFLNEVFDQYYNGYCNNILWPIFHYMGLPQEDRHDATRTFESQYDAYKKANRMFLDVVKENYEEGDVVWCHDYHLM 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590 162 FLPQYLKEYNNKIKVGWFLHSPFPSSEVYKTLPSRSELLRAILAADLLGFHTYDFARHFLSTCTRILGVEGTHEGVVYQG 241
Cdd:PLN03063  160 FLPQYLKEYNNKMKVGWFLHTPFPSSEIYKTLPSRSELLRAVLTADLIGFHTYDFARHFLSACTRILGVEGTHEGVVDQG 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590 242 RVTRVAVFPIGIDPDRFIRTCKLPEVTQQMNELQEKFAGKKVILGVDRLDMIKGIPQKYLAFEKFLEENPYWRDKVVLVQ 321
Cdd:PLN03063  240 KVTRVAVFPIGIDPERFINTCELPEVKQHMKELKRFFAGRKVILGVDRLDMIKGIPQKYLAFEKFLEENPEWRDKVMLVQ 319
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590 322 IAVPTRNDVPEYRKLKSQVHGLVGRINGRFGSVSSLPIHHLDCSVDFNYLCAIYAIADVMLVTSLRDGMNLVSYEFVACQ 401
Cdd:PLN03063  320 IAVPTRNDVPEYQKLKSQVHELVGRINGRFGSVSSVPIHHLDCSVDFNYLCALYAITDVMLVTSLRDGMNLVSYEFVACQ 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590 402 EAKKGVLVLSEFAGAGQSLGVGALIVNPWDVTEVSSAIKEALNMPAEERETRHRSNFQYVCTHSAEKWGLDFMSELNGII 481
Cdd:PLN03063  400 KAKKGVLVLSEFAGAGQSLGAGALLVNPWNITEVSSAIKEALNMSDEERETRHRHNFQYVKTHSAQKWADDFMSELNDII 479
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590 482 PESEMQMRKIPLQLPEQDVIQQYSQSNNRLIILGFFGTLAEPMNSGTKEMDLKLNPELKGTLKALCNDPKTTVVVLSRSG 561
Cdd:PLN03063  480 VEAELRTRNIPLELPEQDVIQQYSKSNNRLLILGFYGTLTEPRNSQIKEMDLGLHPELKETLKALCSDPKTTVVVLSRSG 559
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590 562 KNILNKNFGESNIWLAAENGMFEKQTTGEWVTNMPQNVNLDWVDGVKNVFKYFTDRTPRSYFEASETSLVWNYEYADVEF 641
Cdd:PLN03063  560 KDILDKNFGEYNIWLAAENGMFLRHTSGEWVTTMPEHMNLDWVDGVKNVFKYFTDRTPRSYVEKSETSLVWNYEYADVEF 639
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590 642 GRAQARDLLQYLWAGPISNASVDVVRGNHSVEVHAIGETKGAAIGRILGEIVHRKSMTTPIDFVFCSGYFLEKDEDIYTF 721
Cdd:PLN03063  640 GRAQARDMLQHLWAGPISNASVDVVRGQKSVEVHAIGVTKGAAIGRILGEIVHNKSMTTPIDFVFCSGYFLEKDEDVYTF 719
                         730       740       750       760       770       780       790
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063678590 722 FESKILSSK--------------SPNGLDLKKENYFSAAIGQARTKARYVIDSAHGVVDLLHKLAvVADTTMTDSFSDS 786
Cdd:PLN03063  720 FEPEILSKKkssssnysdsdkkvSSNLVDLKGENYFSCAIGQARTKARYVLDSSNDVVSLLHKLA-VANTTMTDSFSDV 797
PLN03064 PLN03064
alpha,alpha-trehalose-phosphate synthase (UDP-forming); Provisional
5-778 0e+00

alpha,alpha-trehalose-phosphate synthase (UDP-forming); Provisional


Pssm-ID: 215556 [Multi-domain]  Cd Length: 934  Bit Score: 1334.44  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590   5 DDARGERPRLLVVANRLPVSAKRTGENSWSLEMSPGGLVSGLLGItSQFDTKWVGWPGVDVHDEIEKNALTESLAEMKCI 84
Cdd:PLN03064   87 EGRRPLRQRLLVVANRLPVSAVRRGEDSWSLEISAGGLVSALLGV-KEFEARWIGWAGVNVPDEVGQKALTKALAEKRCI 165
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590  85 PVFLN-GVFDQYYNGYCNGILWPILHHMGLPQEDQHDTNQTFETQYDAYKKANRMFLDVIIDNYEEGDIVWCHDYHLMFL 163
Cdd:PLN03064  166 PVFLDeEIVHQYYNGYCNNILWPLFHYLGLPQEDRLATTRSFQSQFAAYKKANQMFADVVNEHYEEGDVVWCHDYHLMFL 245
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590 164 PQYLKEYNNKIKVGWFLHSPFPSSEVYKTLPSRSELLRAILAADLLGFHTYDFARHFLSTCTRILGVEGTHEGVVYQGRV 243
Cdd:PLN03064  246 PKCLKEYNSNMKVGWFLHTPFPSSEIHRTLPSRSELLRSVLAADLVGFHTYDYARHFVSACTRILGLEGTPEGVEDQGRL 325
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590 244 TRVAVFPIGIDPDRFIRTCKLPEVTQQMNELQEKFAGKKVILGVDRLDMIKGIPQKYLAFEKFLEENPYWRDKVVLVQIA 323
Cdd:PLN03064  326 TRVAAFPIGIDSDRFIRALETPQVQQHIKELKERFAGRKVMLGVDRLDMIKGIPQKILAFEKFLEENPEWRDKVVLLQIA 405
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590 324 VPTRNDVPEYRKLKSQVHGLVGRINGRFGSVSSLPIHHLDCSVDFNYLCAIYAIADVMLVTSLRDGMNLVSYEFVACQEA 403
Cdd:PLN03064  406 VPTRTDVPEYQKLTSQVHEIVGRINGRFGTLTAVPIHHLDRSLDFHALCALYAVTDVALVTSLRDGMNLVSYEFVACQDS 485
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590 404 KKGVLVLSEFAGAGQSLGVGALIVNPWDVTEVSSAIKEALNMPAEERETRHRSNFQYVCTHSAEKWGLDFMSELNGIIPE 483
Cdd:PLN03064  486 KKGVLILSEFAGAAQSLGAGAILVNPWNITEVAASIAQALNMPEEEREKRHRHNFMHVTTHTAQEWAETFVSELNDTVVE 565
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590 484 SEMQMRKIPLQLPEQDVIQQYSQSNNRLIILGFFGTLAEPMNS------GTKEMDLKLNPELKGTLKALCNDPKTTVVVL 557
Cdd:PLN03064  566 AQLRTRQVPPQLPPEDAIQRYLQSNNRLLILGFNATLTEPVDTpgrrgdQIKEMELRLHPELKEPLRALCSDPKTTIVVL 645
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590 558 SRSGKNILNKNFGESNIWLAAENGMFEKQTTGEWVTNMPQNVNLDWVDGVKNVFKYFTDRTPRSYFEASETSLVWNYEYA 637
Cdd:PLN03064  646 SGSDRSVLDENFGEFDMWLAAENGMFLRHTKGEWMTTMPEHLNMDWVDSVKHVFEYFTERTPRSHFETRETSLVWNYKYA 725
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590 638 DVEFGRAQARDLLQYLWAGPISNASVDVVRGNHSVEVHAIGETKGAAIGRILGEIVHRKSMTTPIDFVFCSGYFLEKDED 717
Cdd:PLN03064  726 DVEFGRLQARDMLQHLWTGPISNAAVDVVQGSRSVEVRPVGVTKGAAIDRILGEIVHSKSMTTPIDYVLCIGHFLGKDED 805
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590 718 IYTFFE-----------------------SKILSSKSPNG---------------------------------------- 734
Cdd:PLN03064  806 IYTFFEpelpsdspaiarsrspdglkssgDRRPSGKLPSSrsnsknsqgkkqrsllssaksgvnhaashgsdrrpspeki 885
                         810       820       830       840
                  ....*....|....*....|....*....|....*....|....*...
gi 1063678590 735 ----LDLKKENYFSAAIGQARTKARYVIDSAHGVVDLLHKLAVVADTT 778
Cdd:PLN03064  886 gwsvLDLKGENYFSCAVGRKRSNARYLLGSSDDVVSFLKELANASSSF 933
PRK14501 PRK14501
putative bifunctional trehalose-6-phosphate synthase/HAD hydrolase subfamily IIB; Provisional
13-772 0e+00

putative bifunctional trehalose-6-phosphate synthase/HAD hydrolase subfamily IIB; Provisional


Pssm-ID: 184712 [Multi-domain]  Cd Length: 726  Bit Score: 711.31  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590  13 RLLVVANRLPVSAKRTgENSWSLEMSPGGLVSGLLGITSQFDTKWVGWPGVDVHDEIE--KNALTESLAEMKCIPVFL-N 89
Cdd:PRK14501    2 RLIIVSNRLPVTVVRE-DGGVELTPSVGGLATGLRSFHERGGGLWVGWPGLDLEEESEeqRARIEPRLEELGLVPVFLsA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590  90 GVFDQYYNGYCNGILWPILHHMG--LPQEDQHdtnqtfetqYDAYKKANRMFLDVIIDNYEEGDIVWCHDYHLMFLPQYL 167
Cdd:PRK14501   81 EEVDRYYEGFCNSTLWPLFHYFPeyTEFEDRF---------WESYERVNQRFAEAIAAIARPGDVVWVHDYQLMLLPAML 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590 168 KEYNNKIKVGWFLHSPFPSSEVYKTLPSRSELLRAILAADLLGFHTYDFARHFLSTCTRILGVEGTHEGVVYQGRVTRVA 247
Cdd:PRK14501  152 RERLPDARIGFFLHIPFPSFEVFRLLPWREEILEGLLGADLIGFHTYDYVRHFLSSVLRVLGYETELGEIRLGGRIVRVD 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590 248 VFPIGIDPDRFIRTCKLPEVTQQMNELQEKFAGKKVILGVDRLDMIKGIPQKYLAFEKFLEENPYWRDKVVLVQIAVPTR 327
Cdd:PRK14501  232 AFPMGIDYDKFHNSAQDPEVQEEIRRLRQDLRGRKIILSIDRLDYTKGIPRRLLAFERFLEKNPEWRGKVRLVQVAVPSR 311
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590 328 NDVPEYRKLKSQVHGLVGRINGRFGSVSSLPIHHLDCSVDFNYLCAIYAIADVMLVTSLRDGMNLVSYEFVACQEAKKGV 407
Cdd:PRK14501  312 TGVPQYQEMKREIDELVGRINGEFGTVDWTPIHYFYRSLPFEELVALYRAADVALVTPLRDGMNLVAKEYVASRTDGDGV 391
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590 408 LVLSEFAGAGQSLGvGALIVNPWDVTEVSSAIKEALNMPAEERETRHRSNFQYVCTHSAEKWGLDFMSELNGI-IPESEM 486
Cdd:PRK14501  392 LILSEMAGAAAELA-EALLVNPNDIEGIAAAIKRALEMPEEEQRERMQAMQERLRRYDVHKWASDFLDELREAaEKNKAF 470
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590 487 QMRKIPlQLPEQDVIQQYSQSNNRLIILGFFGTLAEPMNsgtKEMDLKLNPELKGTLKALCNDPKTTVVVLSRSGKNILN 566
Cdd:PRK14501  471 ASKPIT-PAAAEEIIARYRAASRRLLLLDYDGTLVPFAP---DPELAVPDKELRDLLRRLAADPNTDVAIISGRDRDTLE 546
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590 567 KNFGESNIWLAAENGMFEKQTTGEWVtnMPQNVNLDWVDGVKNVFKYFTDRTPRSYFEASETSLVWNYEYADVEFGRAQA 646
Cdd:PRK14501  547 RWFGDLPIHLVAEHGAWSRAPGGEWQ--LLEPVATEWKDAVRPILEEFVDRTPGSFIEEKEASLAWHYRNADPELGEARA 624
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590 647 RDLLQYLwAGPISNASVDVVRGNHSVEVHAIGETKGAAIGRILGeivhrksmTTPIDFVFCSG--YfleKDEDIYtffes 724
Cdd:PRK14501  625 NELILAL-SSLLSNAPLEVLRGNKVVEVRPAGVNKGRAVRRLLE--------AGPYDFVLAIGddT---TDEDMF----- 687
                         730       740       750       760
                  ....*....|....*....|....*....|....*....|....*...
gi 1063678590 725 KILssksPngldlkkENYFSAAIGQARTKARYVIDSAHGVVDLLHKLA 772
Cdd:PRK14501  688 RAL----P-------ETAITVKVGPGESRARYRLPSQREVRELLRRLL 724
Glyco_transf_20 pfam00982
Glycosyltransferase family 20; Members of this family belong to glycosyl transferase family 20. ...
12-478 0e+00

Glycosyltransferase family 20; Members of this family belong to glycosyl transferase family 20. OtsA (Trehalose-6-phosphate synthase) is homologous to regions in the subunits of yeast trehalose-6-phosphate synthase/phosphate complex,.


Pssm-ID: 425972 [Multi-domain]  Cd Length: 471  Bit Score: 668.22  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590  12 PRLLVVANRLPVSAKR---TGENSWSLEMSPGGLVSGLLGITSQFDTKWVGWPGVDVHDEIEKNALTESLAEM-KCIPVF 87
Cdd:pfam00982   1 SRLVVVSNRLPVTAVRdeeDGKWEFSIKMSSGGLVSALNGLSAATEGVWVGWPGVPVDESEPKDKVSQSLKEKfNCVPVF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590  88 LNG-VFDQYYNGYCNGILWPILHHM-GLPQEDQHDtnqtfETQYDAYKKANRMFLDVIIDNYEEGDIVWCHDYHLMFLPQ 165
Cdd:pfam00982  81 LSDeLFDSYYNGFSNSILWPLFHYMiPPNNEDAFD-----RSWWDAYVKVNKLFADKIVEVYKDGDLIWIHDYHLMLLPQ 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590 166 YLKEYNNKIKVGWFLHSPFPSSEVYKTLPSRSELLRAILAADLLGFHTYDFARHFLSTCTRILGVEGTHE-GVVYQGRVT 244
Cdd:pfam00982 156 MLRKRLPDAKIGFFLHTPFPSSEIFRCLPVREEILEGLLGADLIGFHTYDYARHFLSCCSRLLGLETRSDgGVEYGGRTV 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590 245 RVAVFPIGIDPDRFIRTCKLPEVTQQMNELQEKFAGK-KVILGVDRLDMIKGIPQKYLAFEKFLEENPYWRDKVVLVQIA 323
Cdd:pfam00982 236 SVKAFPIGIDPGRIESGLASPSVQEKIKELKERFGNKkKLIVGVDRLDYIKGIPQKLLAFERFLEEYPEWRGKVVLVQIA 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590 324 VPTRNDVPEYRKLKSQVHGLVGRINGRFGSVSSLPIHHLDCSVDFNYLCAIYAIADVMLVTSLRDGMNLVSYEFVACQEA 403
Cdd:pfam00982 316 VPSRGDVEEYQNLRSQIEELVGRINGEFGTLDYTPVHFLHRPLDFDELIALYAVADVCLVTSLRDGMNLVAYEYVACQQG 395
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063678590 404 KKGVLVLSEFAGAGQSLGVGALIVNPWDVTEVSSAIKEALNMPAEERETRHRSNFQYVCTHSAEKWGLDFMSELN 478
Cdd:pfam00982 396 RKGVLILSEFAGAAQSLNDGAILVNPWDIDEVAEAINEALTMSEEERKKRHKKLYKYISKHDSQHWAESFLSDLK 470
trehalose_OtsA TIGR02400
alpha,alpha-trehalose-phosphate synthase [UDP-forming]; This enzyme catalyzes the key, ...
13-478 0e+00

alpha,alpha-trehalose-phosphate synthase [UDP-forming]; This enzyme catalyzes the key, penultimate step in biosynthesis of trehalose, a compatible solute made as an osmoprotectant in some species in all three domains of life. The gene symbol OtsA stands for osmotically regulated trehalose synthesis A. Trehalose helps protect against both osmotic and thermal stresses, and is made from two glucose subunits. This model excludes glucosylglycerol-phosphate synthase, an enzyme of an analogous osmoprotectant system in many cyanobacterial strains. This model does not identify archaeal examples, as they are more divergent than glucosylglycerol-phosphate synthase. Sequences that score in the gray zone between the trusted and noise cutoffs include a number of yeast multidomain proteins in which the N-terminal domain may be functionally equivalent to this family. The gray zone also includes the OtsA of Cornyebacterium glutamicum (and related species), shown to be responsible for synthesis of only trace amounts of trehalose while the majority is synthesized by the TreYZ pathway; the significance of OtsA in this species is unclear (see Wolf, et al., ). [Cellular processes, Adaptations to atypical conditions]


Pssm-ID: 274112  Cd Length: 456  Bit Score: 664.36  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590  13 RLLVVANRLPVSAKRTGenswsLEMSPGGLVSGLLGITSQFDTKWVGWPGVDVHDEIEKNALTESLAEM-KCIPVFLNG- 90
Cdd:TIGR02400   1 RLIVVSNRLPVPITRGG-----LEPSAGGLAVALLGALKATGGVWFGWSGKTVEEDEGEPFLRTELEGKiTLAPVFLSEe 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590  91 VFDQYYNGYCNGILWPILHhmGLPQEDQHDtnqtfETQYDAYKKANRMFLDVIIDNYEEGDIVWCHDYHLMFLPQYLKEY 170
Cdd:TIGR02400  76 DVDGYYNGFSNSTLWPLFH--YRPDLIRYD-----RKAWEAYRRVNRLFAEALAPLLQPGDIVWVHDYHLMLLPAMLREL 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590 171 NNKIKVGWFLHSPFPSSEVYKTLPSRSELLRAILAADLLGFHTYDFARHFLSTCTRILGVEGTHEGVVYQGRVTRVAVFP 250
Cdd:TIGR02400 149 GVQNKIGFFLHIPFPSSEIYRTLPWRRELLEGLLAYDLVGFQTYDDARNFLSAVSRELGLETLPNGVESGGRTVRVGAFP 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590 251 IGIDPDRFIRTCKLPEVTQQMNELQEKFAGKKVILGVDRLDMIKGIPQKYLAFEKFLEENPYWRDKVVLVQIAVPTRNDV 330
Cdd:TIGR02400 229 IGIDVDRFAEQAKKPSVQKRIAELRESLKGRKLIIGVDRLDYSKGLPERLLAFERFLEEHPEWRGKVVLVQIAVPSRGDV 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590 331 PEYRKLKSQVHGLVGRINGRFGSVSSLPIHHLDCSVDFNYLCAIYAIADVMLVTSLRDGMNLVSYEFVACQEAKKGVLVL 410
Cdd:TIGR02400 309 PEYQQLRRQVEELVGRINGRFGTLDWTPIRYLNRSYDREELMALYRAADVGLVTPLRDGMNLVAKEYVAAQDPKDGVLIL 388
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063678590 411 SEFAGAGQSLGvGALIVNPWDVTEVSSAIKEALNMPAEERETRHRSNFQYVCTHSAEKWGLDFMSELN 478
Cdd:TIGR02400 389 SEFAGAAQELN-GALLVNPYDIDGMADAIARALTMPLEEREERHRAMMDKLRKNDVQRWREDFLSDLN 455
GT20_TPS cd03788
trehalose-6-phosphate synthase; Trehalose-6-Phosphate Synthase (TPS, EC 2.4.1.15) is a ...
13-478 0e+00

trehalose-6-phosphate synthase; Trehalose-6-Phosphate Synthase (TPS, EC 2.4.1.15) is a glycosyltransferase that catalyses the synthesis of alpha,alpha-1,1-trehalose-6-phosphate from glucose-6-phosphate using a UDP-glucose donor. It is a key enzyme in the trehalose synthesis pathway. Trehalose is a nonreducing disaccharide present in a wide variety of organisms and may serve as a source of energy and carbon. It is characterized most notably in insect, plant, and microbial cells. Its production is often associated with a variety of stress conditions, including desiccation, dehydration, heat, cold, and oxidation. This family represents the catalytic domain of the TPS. Some members of this domain family coexist with a C-terminal trehalose phosphatase domain.


Pssm-ID: 340820 [Multi-domain]  Cd Length: 463  Bit Score: 642.71  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590  13 RLLVVANRLPVSAKRTGENSWSLEMSPGGLVSGLLGITSQFDTKWVGWPGVDV-HDEIEKNALTESLAEMKCIPVFLN-G 90
Cdd:cd03788     1 RLIVVSNRLPVTLERDDDGEVEFRRSAGGLVTALKGLLKSTGGLWVGWPGIEAdEEESDQVVSPELLEEYNVVPVFLSdE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590  91 VFDQYYNGYCNGILWPILHHMglpqedQHDTNQTFETQ-YDAYKKANRMFLDVIIDNYEEGDIVWCHDYHLMFLPQYLKE 169
Cdd:cd03788    81 DFEGYYNGFSNSVLWPLFHYL------LPLPDGRFEREwWEAYVRVNQAFADAVVEVYRPGDLIWVHDYHLLLLPQMLRE 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590 170 YNNKIKVGWFLHSPFPSSEVYKTLPSRSELLRAILAADLLGFHTYDFARHFLSTCTRILGVEGTHEGVV-YQGRVTRVAV 248
Cdd:cd03788   155 RLPDARIGFFLHIPFPSSEIFRCLPWREEILRGLLGADLIGFQTFEYARHFLSCCSRLLGLETTSAGGVeYGGRRVRVGA 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590 249 FPIGIDPDRFIRTCKLPEVTQQMNELQEKFAGKKVILGVDRLDMIKGIPQKYLAFEKFLEENPYWRDKVVLVQIAVPTRN 328
Cdd:cd03788   235 FPIGIDPDRFRRLAASPEVQERARELRERYKGKKLIVGVDRLDYTKGIPEKLLAFERFLERYPEWRGKVVLVQVAVPSRT 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590 329 DVPEYRKLKSQVHGLVGRINGRFGSVSSLPIHHLDCSVDFNYLCAIYAIADVMLVTSLRDGMNLVSYEFVACQEAKKGVL 408
Cdd:cd03788   315 DVEEYQELRREVEELVGRINGRFGTLDWTPVVYLHQSLDREELLALYRAADVALVTSLRDGMNLVAKEYVACQRDNPGVL 394
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590 409 VLSEFAGAGQSLGvGALIVNPWDVTEVSSAIKEALNMPAEERETRHRSNFQYVCTHSAEKWGLDFMSELN 478
Cdd:cd03788   395 ILSEFAGAASELD-GAILVNPWDIEEVAEAINRALTMSPEERKERHQKLRKYVETHDVQAWANSFLDDLA 463
OtsA COG0380
Trehalose-6-phosphate synthase, GT20 family [Carbohydrate transport and metabolism];
13-480 0e+00

Trehalose-6-phosphate synthase, GT20 family [Carbohydrate transport and metabolism];


Pssm-ID: 440149  Cd Length: 474  Bit Score: 579.00  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590  13 RLLVVANRLPVSAKRTGeNSWSLEMSPGGLVSGLLGITSQFDTKWVGWPGVDVHDEIEKN---ALTESLAEMKCIPVFLN 89
Cdd:COG0380     3 RLVVVSNRLPVPHVRED-GSIRVKRSAGGLVTALEPVLRRRGGLWVGWSGGDADREAVEEprgPVPPDLGGYTLAPVDLS 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590  90 -GVFDQYYNGYCNGILWPILHHM-GLPQEDQHDtnqtfetqYDAYKKANRMFLDVIIDNYEEGDIVWCHDYHLMFLPQYL 167
Cdd:COG0380    82 aEEVDGYYEGFSNETLWPLFHYRlDLPEFDRED--------WEAYRRVNRRFAEALAEEAEPDDVVWVHDYHLLLVPAML 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590 168 KEYNNKIKVGWFLHSPFPSSEVYKTLPSRSELLRAILAADLLGFHTYDFARHFLSTCTRILGVEGTHEGVV-YQGRVTRV 246
Cdd:COG0380   154 RELGPDARIGFFLHIPFPPPEIFRILPWREEILEGLLGADLIGFQTPRDARNFLDCVRRLLGAEVDEGGTVrYGGRTVRV 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590 247 AVFPIGIDPDRFIRTCKLPEVTQQMNELQEKFAGKKVILGVDRLDMIKGIPQKYLAFEKFLEENPYWRDKVVLVQIAVPT 326
Cdd:COG0380   234 GAFPIGIDVEEFAELARSPEVRARAERLREELGGRKLILGVDRLDYTKGIPERLRAFERLLERHPELRGKVTLLQIAVPS 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590 327 RNDVPEYRKLKSQVHGLVGRINGRFGSVSSLPIHHLDCSVDFNYLCAIYAIADVMLVTSLRDGMNLVSYEFVACQEAKKG 406
Cdd:COG0380   314 REDVPAYRELRREIEELVGRINGRFGTLDWTPIRYLNRSLPREELAALYRAADVALVTPLRDGMNLVAKEYVAAQPDDPG 393
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063678590 407 VLVLSEFAGAGQSLGvGALIVNPWDVTEVSSAIKEALNMPAEERETRHRSNFQYVCTHSAEKWGLDFMSELNGI 480
Cdd:COG0380   394 VLVLSEFAGAAEELT-EALLVNPYDIDGMAEAIHRALTMPLEERRRRMRALRERVRRYDVHRWADDFLDALAAV 466
PLN02205 PLN02205
alpha,alpha-trehalose-phosphate synthase [UDP-forming]
10-780 1.38e-167

alpha,alpha-trehalose-phosphate synthase [UDP-forming]


Pssm-ID: 177855 [Multi-domain]  Cd Length: 854  Bit Score: 506.87  E-value: 1.38e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590  10 ERPRLLVVANRLPVSAKRT--GENSWSLEMSPGGLVSGL---LGiTSQFDTKWVGWPGVDVHDEiEKNALTESLAE-MKC 83
Cdd:PLN02205   58 PKDRIIIVANQLPIRAQRKsdGSKGWIFSWDENSLLLQLkdgLG-DDEIEVIYVGCLKEEIHLN-EQEEVSQILLEtFKC 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590  84 IPVFLN-GVFDQYYNGYCNGILWPILHHMgLPQEDqhDTNQTFE-TQYDAYKKANRMFLDVIIDNYE-EGDIVWCHDYHL 160
Cdd:PLN02205  136 VPTFLPpDLFTRYYHGFCKQQLWPLFHYM-LPLSP--DLGGRFNrSLWQAYVSVNKIFADRIMEVINpEDDFVWIHDYHL 212
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590 161 MFLPQYLKEYNNKIKVGWFLHSPFPSSEVYKTLPSRSELLRAILAADLLGFHTYDFARHFLSTCTRILGVegTHE----- 235
Cdd:PLN02205  213 MVLPTFLRKRFNRVKLGFFLHSPFPSSEIYKTLPIREELLRALLNSDLIGFHTFDYARHFLSCCSRMLGL--SYEskrgy 290
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590 236 -GVVYQGRVTRVAVFPIGIDPDRFIRTCKLPEVTQQMNELQEKFA--GKKVILGVDRLDMIKGIPQKYLAFEKFLEENPY 312
Cdd:PLN02205  291 iGLEYYGRTVSIKILPVGIHMGQLQSVLSLPETEAKVKELIKQFCdqDRIMLLGVDDMDIFKGISLKLLAMEQLLMQHPE 370
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590 313 WRDKVVLVQIAVPTRNDVPEYRKLKSQVHGLVGRINGRFGSVSSLPIHHLDCSVDFNYLCAIYAIADVMLVTSLRDGMNL 392
Cdd:PLN02205  371 WQGKVVLVQIANPARGKGKDVKEVQAETHSTVKRINETFGKPGYDPIVLIDAPLKFYERVAYYVVAECCLVTAVRDGMNL 450
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590 393 VSYEFVACQEA---------------KKGVLVLSEFAGAGQSLGvGALIVNPWDVTEVSSAIKEALNMPAEERETRHRSN 457
Cdd:PLN02205  451 IPYEYIISRQGnekldkllglepstpKKSMLVVSEFIGCSPSLS-GAIRVNPWNIDAVADAMDSALEMAEPEKQLRHEKH 529
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590 458 FQYVCTHSAEKWGLDFMSELNGIIPESE----------MQMRKIPL-----QLPEQDVIQQYSQSNNRLIILGFFGTLAe 522
Cdd:PLN02205  530 YRYVSTHDVGYWARSFLQDLERTCRDHSrrrcwgigfgLSFRVVALdpnfrKLSMEHIVSAYKRTTTRAILLDYDGTLM- 608
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590 523 PMNSgtkeMDLKLNPELKGTLKALCNDPKTTVVVLSRSGKNILNKNFGE-SNIWLAAENGMFEK-QTTGEWVTNMPQnVN 600
Cdd:PLN02205  609 PQAS----IDKSPSSKSIDILNTLCRDKNNMVFIVSARSRKTLADWFSPcEKLGIAAEHGYFLRlKRDVEWETCVPV-AD 683
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590 601 LDWVDGVKNVFKYFTDRTPRSYFEASETSLVWNYEYADVEFGRAQARDLLQYLwAGPISNASVDVVRGNHSVEVHAIGET 680
Cdd:PLN02205  684 CSWKQIAEPVMQLYTETTDGSTIEDKETALVWCYEDADPDFGSCQAKELLDHL-ESVLANEPVTVKSGQNIVEVKPQGVS 762
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590 681 KGAAIGRILGEIVHRKsmTTPiDFVFCSGYFlEKDEDIYTFFESKIL-SSKSPNGldlkkeNYFSAAIGQARTKARYVID 759
Cdd:PLN02205  763 KGLVAKRLLSIMQERG--MLP-DFVLCIGDD-RSDEDMFEVITSSMAgPSIAPRA------EVFACTVGQKPSKAKYYLD 832
                         810       820
                  ....*....|....*....|.
gi 1063678590 760 SAHGVVDLLHKLAVVADTTMT 780
Cdd:PLN02205  833 DTAEIVRLMQGLASVSEQILP 853
PRK10117 PRK10117
trehalose-6-phosphate synthase; Provisional
13-485 5.75e-89

trehalose-6-phosphate synthase; Provisional


Pssm-ID: 182249  Cd Length: 474  Bit Score: 289.34  E-value: 5.75e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590  13 RLLVVANRL-PVSAKRTgenswslemSPGGLVSGLLGITSQFDTKWVGWPGVDVHDEIEKNALTESLAEMKCIPVFLNGv 91
Cdd:PRK10117    3 RLVVVSNRIaPPDEHKA---------SAGGLAVGILGALKAAGGLWFGWSGETGNEDQPLKKVKKGNITWASFNLSEQD- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590  92 FDQYYNGYCNGILWPILHHmglpqedQHDTNQTFETQYDAYKKANRMFLDVIIDNYEEGDIVWCHDYHLMFLPQYLKE-- 169
Cdd:PRK10117   73 YDEYYNQFSNAVLWPAFHY-------RLDLVQFQRPAWEGYLRVNALLADKLLPLLKDDDIIWIHDYHLLPFASELRKrg 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590 170 YNNKIkvGWFLHSPFPSSEVYKTLPSRSELLRAILAADLLGFHTYDFARHFLSTCTRILGVEgTHEGVVYQ--GRVTRVA 247
Cdd:PRK10117  146 VNNRI--GFFLHIPFPTPEIFNALPPHDELLEQLCDYDLLGFQTENDRLAFLDCLSNLTRVT-TRSGKSHTawGKAFRTE 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590 248 VFPIGIDPDRFIRTCKLPeVTQQMNELQEKFAGKKVILGVDRLDMIKGIPQKYLAFEKFLEENPYWRDKVVLVQIAVPTR 327
Cdd:PRK10117  223 VYPIGIEPDEIAKQAAGP-LPPKLAQLKAELKNVQNIFSVERLDYSKGLPERFLAYEALLEKYPQHHGKIRYTQIAPTSR 301
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590 328 NDVPEYRKLKSQVHGLVGRINGRFGSVSSLPIHHLDCSVDFNYLCAIYAIADVMLVTSLRDGMNLVSYEFVACQE-AKKG 406
Cdd:PRK10117  302 GDVQAYQDIRHQLETEAGRINGKYGQLGWTPLYYLNQHFDRKLLMKIFRYSDVGLVTPLRDGMNLVAKEYVAAQDpANPG 381
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063678590 407 VLVLSEFAGAGQSLgVGALIVNPWDVTEVSSAIKEALNMPAEERETRHRSNFQYVCTHSAEKWGLDFMSELNGIIPESE 485
Cdd:PRK10117  382 VLVLSQFAGAANEL-TSALIVNPYDRDEVAAALDRALTMPLAERISRHAEMLDVIVKNDINHWQECFISDLKQIVPRSA 459
HAD_TPP cd01627
trehalose-phosphate phosphatase similar to Escherichia coli trehalose-6-phosphate phosphatase ...
511-765 7.46e-64

trehalose-phosphate phosphatase similar to Escherichia coli trehalose-6-phosphate phosphatase OtsB and Saccharomyces cerevisiae trehalose-phosphatase TPS2; Trehalose biosynthesis in bacteria is known through three pathways - OtsAB, TreYZ and TreS. The OtsAB pathway, also known as the trehalose 6-phosphate synthase (TSP)/ Trehalose-6-phosphate phosphatase (TPP) pathway, is the most common route known to be involved in the stress response of Escherichia coli. It involves converting glucose-6-phosphate and UDP-glucose to form trehalose-6-phosphate (T6P), catalyzed by TPS, the product of the otsA gene, this step is followed by the dephosphorylation of T6P to yield trehalose and inorganic phosphate, catalyzed by a specific TPP, the product of otsB gene. This OtsAB (or TSP/TPP) pathway, is also the most common route known to be involved in the stress response of yeast In Saccharomyces cerevisiae, the corresponding enzymes, TPS1p and TPS2p, form a multimeric synthase complex together with additional regulatory subunits encoded by Tsl1 and Tps3. Trehalose is a common disaccharide accumulated by organisms as a reservation of carbohydrate and in response to unfavorable growth conditions. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.


Pssm-ID: 319767 [Multi-domain]  Cd Length: 228  Bit Score: 213.69  E-value: 7.46e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590 511 LIILGFFGTLAEPMNsgtKEMDLKLNPELKGTLKALCNDPKTTVVVLSRSGKNILNKNFGESNIWLAAENGMFEKQTTG- 589
Cdd:cd01627     1 LLFLDYDGTLAPIVP---DPDAAVPSPELLEALKKLAADPKNAVAIVSGRDLDDLDKWLGLPGIGLAGEHGAEIRLPGGg 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590 590 EWVTNMPqNVNLDWVDGVKNVFKYFTDRTPRSYFEASETSLVWNY-------EYADVEFGRAQARDLLQYLwagpisnas 662
Cdd:cd01627    78 EWVTLAP-KADLEWKEEVEAIFKYFTERTPGSLVEDKGASLAWHYrnadpegARAALELALHLASDLLKAL--------- 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590 663 vDVVRGNHSVEVHAIGETKGAAIGRILGEIVHRKsmttpiDFVFCSGyFLEKDEDIYTFfeskilsskspngldLKKENY 742
Cdd:cd01627   148 -EVVPGKKVVEVRPVGVNKGEAVERILGELPFAG------DFVLCAG-DDVTDEDAFRA---------------LNGEGG 204
                         250       260
                  ....*....|....*....|...
gi 1063678590 743 FSAAIGQARTKARYVIDSAHGVV 765
Cdd:cd01627   205 FSVKVGEGPTAAKFRLDDPPDVV 227
Trehalose_PPase pfam02358
Trehalose-phosphatase; This family consist of trehalose-phosphatases EC:3.1.3.12 these enzyme ...
518-760 1.23e-55

Trehalose-phosphatase; This family consist of trehalose-phosphatases EC:3.1.3.12 these enzyme catalyze the de-phosphorylation of trehalose-6-phosphate to trehalose and orthophosphate. The aligned region is present in trehalose-phosphatases and comprises the entire length of the protein it is also found in the C-terminus of trehalose-6-phosphate synthase EC:2.4.1.15 adjacent to the trehalose-6-phosphate synthase domain - pfam00982. It would appear that the two equivalent genes in the E. coli otsBA operon otsA the trehalose-6-phosphate synthase and otsB trehalose-phosphatase (this family) have undergone gene fusion in most eukaryotes and Swiss:P93653. Trehalose is a common disaccharide of bacteria, fungi and invertebrates that appears to play a major role in desiccation tolerance.


Pssm-ID: 426737 [Multi-domain]  Cd Length: 234  Bit Score: 191.39  E-value: 1.23e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590 518 GTLAEPmnsGTKEMDLKLNPELKGTLKALCNDPKTTVVVLSRSGKNILNKNFGESNIWLAAENGMFEKQTTGEWVTNMPQ 597
Cdd:pfam02358   6 GTLSPI---VSDPIAAVPSDRMLSALQDLASDPPNTVAIISGRSRQEEDLFVGVPNLGLAAEHGAFVRLPGGGDWYNQAE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590 598 NVNLDWVDGVKNVFKYFTDRTPRSYFEASETSLVWNYEYADVEFGRAQARDLLQYLWAGPISNASVDVVRGNHSVEVHAI 677
Cdd:pfam02358  83 VEDLPWKKEVAPILEYYTERTPGSYVENKKSALSWHYRNADDDFGSFQAKELAEHLESVLQDNPPLRVTQGKKVVEVRPV 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590 678 GETKGAAIGRILGEIVHRKSmttPIDFVFCSGYFLEkDEDIYTFFESKILSSKSPngldlkkeNYFSAAIGQARTKARYV 757
Cdd:pfam02358 163 GVSKGKAVEFILEELGSAGS---LPDFPLCIGDDRT-DEDMFSVLRPTKPSGVGI--------EVFAVSVGSKPSSASYF 230

                  ...
gi 1063678590 758 IDS 760
Cdd:pfam02358 231 LDD 233
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
143-451 8.15e-13

phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 family of glycosyltransferases and named after PimA in Propionibacterium freudenreichii, which is involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIM) which are early precursors in the biosynthesis of lipomannans (LM) and lipoarabinomannans (LAM), and catalyzes the addition of a mannosyl residue from GDP-D-mannose (GDP-Man) to the position 2 of the carrier lipid phosphatidyl-myo-inositol (PI) to generate a phosphatidyl-myo-inositol bearing an alpha-1,2-linked mannose residue (PIM1). Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in certain bacteria and archaea.


Pssm-ID: 340831 [Multi-domain]  Cd Length: 366  Bit Score: 70.64  E-value: 8.15e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590 143 IIDNYEEGDIVWCHDYHLMFLPQYLKeYNNKIKVGWFLHSPFPSSEVYKTLPSR---SELLRAILAADLLGFHTYDFARH 219
Cdd:cd03801    76 PLLRLRKFDVVHAHGLLAALLAALLA-LLLGAPLVVTLHGAEPGRLLLLLAAERrllARAEALLRRADAVIAVSEALRDE 154
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590 220 FLStctrilgvegthegvVYQGRVTRVAVFPIGIDPDRFIRTCKLPEvtqqmnelqEKFAGKKVILGVDRLDMIKGIPQK 299
Cdd:cd03801   155 LRA---------------LGGIPPEKIVVIPNGVDLERFSPPLRRKL---------GIPPDRPVLLFVGRLSPRKGVDLL 210
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590 300 YLAFEKFLEENPYWRdkVVLVQiavptrNDVPEYRKLKSQVHGLVGRIngRFgsVSSLPIHHLDcsvdfnylcAIYAIAD 379
Cdd:cd03801   211 LEALAKLLRRGPDVR--LVIVG------GDGPLRAELEELELGLGDRV--RF--LGFVPDEELP---------ALYAAAD 269
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063678590 380 VMLVTSLRDGMNLVSYEFVACqeakkGVLVLSEFAGAGQSL---GVGALIVNPWDVTEVSSAIKEALNMPAEERE 451
Cdd:cd03801   270 VFVLPSRYEGFGLVVLEAMAA-----GLPVVATDVGGLPEVvedGEGGLVVPPDDVEALADALLRLLADPELRAR 339
GT4_WavL-like cd03819
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ...
245-463 5.44e-08

Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 family of glycosyltransferases. WavL in Vibrio cholerae has been shown to be involved in the biosynthesis of the lipopolysaccharide core.


Pssm-ID: 340846 [Multi-domain]  Cd Length: 345  Bit Score: 55.82  E-value: 5.44e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590 245 RVAVFPIGIDPDRFirtckLPEVTQQMNELQEKFAGKKVILGVDRLDMIKGIpqkyLAFEKFLEENPYWRDKVVLVQiav 324
Cdd:cd03819   151 RIRVIPNGVDTDRF-----PPEAEAEERAQLGLPEGKPVVGYVGRLSPEKGW----LLLVDAAAELKDEPDFRLLVA--- 218
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590 325 ptrNDVPEYRKLKSQV--HGLVGRIngrfgsvsSLPIHHLDcsvdfnyLCAIYAIADVMLVTSLRDGMNLVSYEFVACqe 402
Cdd:cd03819   219 ---GDGPERDEIRRLVerLGLRDRV--------TFTGFRED-------VPAALAASDVVVLPSLHEEFGRVALEAMAC-- 278
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063678590 403 akkGVLVLSeFAGAGQSLGVGA----LIVNPWDVTEVSSAIKEA-LNMPAEERETRHRSNFQYVCT 463
Cdd:cd03819   279 ---GTPVVA-TDVGGAREIVVHgrtgLLVPPGDAEALADAIRAAkLLPEAREKLQAAAALTEAVRE 340
GT4_WlbH-like cd03798
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ...
218-451 1.52e-07

Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Staphylococcus aureus CapJ may be involved in capsule polysaccharide biosynthesis. WlbH in Bordetella parapertussis has been shown to be required for the biosynthesis of a trisaccharide that, when attached to the B. pertussis lipopolysaccharide (LPS) core (band B), generates band A LPS.


Pssm-ID: 340828 [Multi-domain]  Cd Length: 376  Bit Score: 54.31  E-value: 1.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590 218 RHFLSTCTRILGV-EGTHEGVVYQGRV-TRVAVFPIGIDPDRFirtcklpevtQQMNELQEKFAGKKVILGVDRLDMIKG 295
Cdd:cd03798   145 RWALRRAARVIAVsKALAEELVALGVPrDRVDVIPNGVDPARF----------QPEDRGLGLPLDAFVILFVGRLIPRKG 214
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590 296 IPqkYL--AFEKFLEENPywrdKVVLVqIAvptrNDVPEYRKLKSQVHGLVGRINGRFgsVSSLPIHHLDcsvdfnylcA 373
Cdd:cd03798   215 ID--LLleAFARLAKARP----DVVLL-IV----GDGPLREALRALAEDLGLGDRVTF--TGRLPHEQVP---------A 272
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590 374 IYAIADVMLVTSLRDGMNLVSYEFVACqeakkGVLVLSEFAGaGQSLGVG----ALIVNPWDVTEVSSAIKEALNMPAEE 449
Cdd:cd03798   273 YYRACDVFVLPSRHEGFGLVLLEAMAC-----GLPVVATDVG-GIPEVVGdpetGLLVPPGDADALAAALRRALAEPYLR 346

                  ..
gi 1063678590 450 RE 451
Cdd:cd03798   347 EL 348
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
373-481 2.70e-06

Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 47.29  E-value: 2.70e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590 373 AIYAIADVMLVTSLRDGMNLVSYEFVACqeakkGVLVL-SEFAGAGQSL--GVGALIVNPWDVTEVSSAIKEALNMPaEE 449
Cdd:COG0438    16 ALLAAADVFVLPSRSEGFGLVLLEAMAA-----GLPVIaTDVGGLPEVIedGETGLLVPPGDPEALAEAILRLLEDP-EL 89
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1063678590 450 RETRHRSNFQYVCTH-SAEKWGLDFMSELNGII 481
Cdd:COG0438    90 RRRLGEAARERAEERfSWEAIAERLLALYEELL 122
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
280-455 1.22e-04

Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease (Paroxysmal Nocturnal haemoglobinuria). Members of this family transfer activated sugars to a variety of substrates, including glycogen, Fructose-6-phosphate and lipopolysaccharides. Members of this family transfer UDP, ADP, GDP or CMP linked sugars. The eukaryotic glycogen synthases may be distant members of this family.


Pssm-ID: 425737 [Multi-domain]  Cd Length: 158  Bit Score: 43.03  E-value: 1.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590 280 GKKVILGVDRLDMIKGIPQKYLAFEKFLEENPywrdKVVLVqIAvptrNDVPEYRKLKSQVHGLVGRINGRF-GSVSSLP 358
Cdd:pfam00534   1 KKKIILFVGRLEPEKGLDLLIKAFALLKEKNP----NLKLV-IA----GDGEEEKRLKKLAEKLGLGDNVIFlGFVSDED 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590 359 IHHLdcsvdfnylcaiYAIADVMLVTSLRDGMNLVSYEFVACqeakkGVLVLS-------EFAGAGQSlgvGALIVNPwD 431
Cdd:pfam00534  72 LPEL------------LKIADVFVLPSRYEGFGIVLLEAMAC-----GLPVIAsdvggppEVVKDGET---GFLVKPN-N 130
                         170       180
                  ....*....|....*....|....
gi 1063678590 432 VTEVSSAIKEALnmpaEERETRHR 455
Cdd:pfam00534 131 AEALAEAIDKLL----EDEELRER 150
GT4_sucrose_synthase cd03800
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ...
239-447 8.45e-04

sucrose-phosphate synthase and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. The sucrose-phosphate synthases in this family may be unique to plants and photosynthetic bacteria. This enzyme catalyzes the synthesis of sucrose 6-phosphate from fructose 6-phosphate and uridine 5'-diphosphate-glucose, a key regulatory step of sucrose metabolism. The activity of this enzyme is regulated by phosphorylation and moderated by the concentration of various metabolites and light.


Pssm-ID: 340830 [Multi-domain]  Cd Length: 398  Bit Score: 42.61  E-value: 8.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590 239 YQGRVTRVAVFPIGIDPDRFIRTcklPEVTQQMNELQEKFAgKKVILGVDRLDMIKGIPQKYLAFekflEENPYWRDKVV 318
Cdd:cd03800   182 YGADPSRINVVPPGVDLERFFPV---DRAEARRARLLLPPD-KPVVLALGRLDPRKGIDTLVRAF----AQLPELRELAN 253
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590 319 LVqIAVPTRND----VPEYRKLKSQVHGLVGRINgrfgsvssLPIHHLDcsvdfNYLCAIYAIADVMLVTSLRDGMNLVS 394
Cdd:cd03800   254 LV-LVGGPSDDplsmDREELAELAEELGLIDRVR--------FPGRVSR-----DDLPELYRAADVFVVPSLYEPFGLTA 319
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1063678590 395 YEFVACqeakkGVLVL-SEFAGAGQSL--GVGALIVNPWDVTEVSSAIKEALNMPA 447
Cdd:cd03800   320 IEAMAC-----GTPVVaTAVGGLQDIVrdGRTGLLVDPHDPEALAAALRRLLDDPA 370
GT4_Bme6-like cd03821
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ...
176-450 9.83e-04

Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Bme6 in Brucella melitensis has been shown to be involved in the biosynthesis of a polysaccharide.


Pssm-ID: 340848 [Multi-domain]  Cd Length: 377  Bit Score: 42.36  E-value: 9.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590 176 VGWFLHSPFPSSEVYKTLPSRsellRAILAADLLGFHTYDFARHflstcTRILGVEGthegvvyqgrvtRVAVFPIGIDP 255
Cdd:cd03821   127 DPWALQQKHWKKRIALHLIER----RNLNNAALVHFTSEQEADE-----LRRFGLEP------------PIAVIPNGVDI 185
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590 256 DRFIrtcKLPEVTQQMNELQekfaGKKVILGVDRLDMIKGIPqkYL--AFEKFLEENPYWRdkvvLVqIAVPTRNDVPEY 333
Cdd:cd03821   186 PEFD---PGLRDRRKHNGLE----DRRIILFLGRIHPKKGLD--LLirAARKLAEQGRDWH----LV-IAGPDDGAYPAF 251
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063678590 334 RKLKSQvHGLVGRIngRFGSvsslPIHHLDcsvdfnyLCAIYAIADVMLVTSLRDGMNLVSYEFVACqeakkG--VLVLS 411
Cdd:cd03821   252 LQLQSS-LGLGDRV--TFTG----PLYGEA-------KWALYASADLFVLPSYSENFGNVVAEALAC-----GlpVVITD 312
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1063678590 412 EFAGAGQSLGVGALIVNPwDVTEVSSAIKEALNMPAEER 450
Cdd:cd03821   313 KCGLSELVEAGCGVVVDP-NVSSLAEALAEALRDPADRK 350
 
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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