|
Name |
Accession |
Description |
Interval |
E-value |
| PRK14501 |
PRK14501 |
putative bifunctional trehalose-6-phosphate synthase/HAD hydrolase subfamily IIB; Provisional |
3-720 |
0e+00 |
|
putative bifunctional trehalose-6-phosphate synthase/HAD hydrolase subfamily IIB; Provisional
Pssm-ID: 184712 [Multi-domain] Cd Length: 726 Bit Score: 1116.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 3 RLLIISNRLPVSVERRKNELRFSSSVGGLATGLNALHQRYESVWVGWPGIAINR---EETDYVESKLSEFNCYPVFLSQG 79
Cdd:PRK14501 2 RLIIVSNRLPVTVVREDGGVELTPSVGGLATGLRSFHERGGGLWVGWPGLDLEEeseEQRARIEPRLEELGLVPVFLSAE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 80 EVEKYYYGFSNKTLWPLFHYFPQYAKYEHSEWSAYEHVNRKFCERVAEIAKPEDIIWIHDYHLMLLPGLIRERFPDATIG 159
Cdd:PRK14501 82 EVDRYYEGFCNSTLWPLFHYFPEYTEFEDRFWESYERVNQRFAEAIAAIARPGDVVWVHDYQLMLLPAMLRERLPDARIG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 160 FFLHIPFPSADLFRLIPWRRRILEGVLGADLIGFHTYDYAHNFLCSVLRLLGYEHEFGKLAIGDRIVQVDVHPMGVEVQK 239
Cdd:PRK14501 162 FFLHIPFPSFEVFRLLPWREEILEGLLGADLIGFHTYDYVRHFLSSVLRVLGYETELGEIRLGGRIVRVDAFPMGIDYDK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 240 FVRATSGRGIKREVARLRSRFKNCKIIFSMDRLDYTKGIPERLYAFEHFLETHPEWHEKVVFILKIAPSRTKVGQYRVLK 319
Cdd:PRK14501 242 FHNSAQDPEVQEEIRRLRQDLRGRKIILSIDRLDYTKGIPRRLLAFERFLEKNPEWRGKVRLVQVAVPSRTGVPQYQEMK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 320 QEIDELVGRINGKYGTPEWVPISYFYRSLPFQTIVAFYLAADVALLTSMRDGMNLIAKEFVASRVDGKGVLILSEMAGAA 399
Cdd:PRK14501 322 REIDELVGRINGEFGTVDWTPIHYFYRSLPFEELVALYRAADVALVTPLRDGMNLVAKEYVASRTDGDGVLILSEMAGAA 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 400 RELGEALVVNPNNKEEVAEALNEALRMPEEEQKSRNEEMQKRLSHYDVFHWGSGFIRSVLETKRLQEELNMKKLSEKIRE 479
Cdd:PRK14501 402 AELAEALLVNPNDIEGIAAAIKRALEMPEEEQRERMQAMQERLRRYDVHKWASDFLDELREAAEKNKAFASKPITPAAAE 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 480 ELKNAYKAADKCLLLLDYDGTLVPFADKPERAKPDKELLYLFRALSEPPENTVVIISGRDKETLERWFGDTGVCLVAEHG 559
Cdd:PRK14501 482 EIIARYRAASRRLLLLDYDGTLVPFAPDPELAVPDKELRDLLRRLAADPNTDVAIISGRDRDTLERWFGDLPIHLVAEHG 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 560 VRLKEEEGEWKEIELLKEDWKEKIIPILDLFVDRAPGSFIEEKSFSLVWHYRKVDPELGELRAKELTDQLIDLTACTELQ 639
Cdd:PRK14501 562 AWSRAPGGEWQLLEPVATEWKDAVRPILEEFVDRTPGSFIEEKEASLAWHYRNADPELGEARANELILALSSLLSNAPLE 641
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 640 VMKGNKVVEVKDGRVNKGIAASHWLTKG-FGFILAVGDDLTDEDMFKVLPEGAYSVKIGFTPSKARFYLGSPKEVRALLD 718
Cdd:PRK14501 642 VLRGNKVVEVRPAGVNKGRAVRRLLEAGpYDFVLAIGDDTTDEDMFRALPETAITVKVGPGESRARYRLPSQREVRELLR 721
|
..
gi 52548412 719 EM 720
Cdd:PRK14501 722 RL 723
|
|
| OtsA |
COG0380 |
Trehalose-6-phosphate synthase, GT20 family [Carbohydrate transport and metabolism]; |
1-468 |
0e+00 |
|
Trehalose-6-phosphate synthase, GT20 family [Carbohydrate transport and metabolism];
Pssm-ID: 440149 Cd Length: 474 Bit Score: 715.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 1 MRRLLIISNRLPVSVERRKNELRFSSSVGGLATGLNALHQRYESVWVGWPGIAINREETDY----VESKLSEFNCYPVFL 76
Cdd:COG0380 1 GSRLVVVSNRLPVPHVREDGSIRVKRSAGGLVTALEPVLRRRGGLWVGWSGGDADREAVEEprgpVPPDLGGYTLAPVDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 77 SQGEVEKYYYGFSNKTLWPLFHYFPQYAKYEHSEWSAYEHVNRKFCERVAEIAKPEDIIWIHDYHLMLLPGLIRERFPDA 156
Cdd:COG0380 81 SAEEVDGYYEGFSNETLWPLFHYRLDLPEFDREDWEAYRRVNRRFAEALAEEAEPDDVVWVHDYHLLLVPAMLRELGPDA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 157 TIGFFLHIPFPSADLFRLIPWRRRILEGVLGADLIGFHTYDYAHNFLCSVLRLLGYE-HEFGKLAIGDRIVQVDVHPMGV 235
Cdd:COG0380 161 RIGFFLHIPFPPPEIFRILPWREEILEGLLGADLIGFQTPRDARNFLDCVRRLLGAEvDEGGTVRYGGRTVRVGAFPIGI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 236 EVQKFVRATSGRGIKREVARLRSRFKNCKIIFSMDRLDYTKGIPERLYAFEHFLETHPEWHEKVVFILKIAPSRTKVGQY 315
Cdd:COG0380 241 DVEEFAELARSPEVRARAERLREELGGRKLILGVDRLDYTKGIPERLRAFERLLERHPELRGKVTLLQIAVPSREDVPAY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 316 RVLKQEIDELVGRINGKYGTPEWVPISYFYRSLPFQTIVAFYLAADVALLTSMRDGMNLIAKEFVASRVDGKGVLILSEM 395
Cdd:COG0380 321 RELRREIEELVGRINGRFGTLDWTPIRYLNRSLPREELAALYRAADVALVTPLRDGMNLVAKEYVAAQPDDPGVLVLSEF 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 52548412 396 AGAARELGEALVVNPNNKEEVAEALNEALRMPEEEQKSRNEEMQKRLSHYDVFHWGSGFIRSVLETKRLQEEL 468
Cdd:COG0380 401 AGAAEELTEALLVNPYDIDGMAEAIHRALTMPLEERRRRMRALRERVRRYDVHRWADDFLDALAAVRAAASPL 473
|
|
| GT20_TPS |
cd03788 |
trehalose-6-phosphate synthase; Trehalose-6-Phosphate Synthase (TPS, EC 2.4.1.15) is a ... |
3-457 |
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: 683.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 3 RLLIISNRLPVSVERRK-NELRFSSSVGGLATGLNALHQRYESVWVGWPGIAINREETDYVESK--LSEFNCYPVFLSQG 79
Cdd:cd03788 1 RLIVVSNRLPVTLERDDdGEVEFRRSAGGLVTALKGLLKSTGGLWVGWPGIEADEEESDQVVSPelLEEYNVVPVFLSDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 80 EVEKYYYGFSNKTLWPLFHYFPQY--AKYEHSEWSAYEHVNRKFCERVAEIAKPEDIIWIHDYHLMLLPGLIRERFPDAT 157
Cdd:cd03788 81 DFEGYYNGFSNSVLWPLFHYLLPLpdGRFEREWWEAYVRVNQAFADAVVEVYRPGDLIWVHDYHLLLLPQMLRERLPDAR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 158 IGFFLHIPFPSADLFRLIPWRRRILEGVLGADLIGFHTYDYAHNFLCSVLRLLGYEHEF-GKLAIGDRIVQVDVHPMGVE 236
Cdd:cd03788 161 IGFFLHIPFPSSEIFRCLPWREEILRGLLGADLIGFQTFEYARHFLSCCSRLLGLETTSaGGVEYGGRRVRVGAFPIGID 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 237 VQKFVRATSGRGIKREVARLRSRFKNCKIIFSMDRLDYTKGIPERLYAFEHFLETHPEWHEKVVFILKIAPSRTKVGQYR 316
Cdd:cd03788 241 PDRFRRLAASPEVQERARELRERYKGKKLIVGVDRLDYTKGIPEKLLAFERFLERYPEWRGKVVLVQVAVPSRTDVEEYQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 317 VLKQEIDELVGRINGKYGTPEWVPISYFYRSLPFQTIVAFYLAADVALLTSMRDGMNLIAKEFVASRVDGKGVLILSEMA 396
Cdd:cd03788 321 ELRREVEELVGRINGRFGTLDWTPVVYLHQSLDREELLALYRAADVALVTSLRDGMNLVAKEYVACQRDNPGVLILSEFA 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 52548412 397 GAARELGEALVVNPNNKEEVAEALNEALRMPEEEQKSRNEEMQKRLSHYDVFHWGSGFIRS 457
Cdd:cd03788 401 GAASELDGAILVNPWDIEEVAEAINRALTMSPEERKERHQKLRKYVETHDVQAWANSFLDD 461
|
|
| trehalose_OtsA |
TIGR02400 |
alpha,alpha-trehalose-phosphate synthase [UDP-forming]; This enzyme catalyzes the key, ... |
3-457 |
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: 615.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 3 RLLIISNRLPVSVERRKNElrfsSSVGGLATGLNALHQRYESVWVGWPGIAINREETDYVESK--LSEFNCYPVFLSQGE 80
Cdd:TIGR02400 1 RLIVVSNRLPVPITRGGLE----PSAGGLAVALLGALKATGGVWFGWSGKTVEEDEGEPFLRTelEGKITLAPVFLSEED 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 81 VEKYYYGFSNKTLWPLFHYFPQYAKYEHSEWSAYEHVNRKFCERVAEIAKPEDIIWIHDYHLMLLPGLIRERFPDATIGF 160
Cdd:TIGR02400 77 VDGYYNGFSNSTLWPLFHYRPDLIRYDRKAWEAYRRVNRLFAEALAPLLQPGDIVWVHDYHLMLLPAMLRELGVQNKIGF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 161 FLHIPFPSADLFRLIPWRRRILEGVLGADLIGFHTYDYAHNFLCSVLRLLGYEHEFGKLAIGDRIVQVDVHPMGVEVQKF 240
Cdd:TIGR02400 157 FLHIPFPSSEIYRTLPWRRELLEGLLAYDLVGFQTYDDARNFLSAVSRELGLETLPNGVESGGRTVRVGAFPIGIDVDRF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 241 VRATSGRGIKREVARLRSRFKNCKIIFSMDRLDYTKGIPERLYAFEHFLETHPEWHEKVVFILKIAPSRTKVGQYRVLKQ 320
Cdd:TIGR02400 237 AEQAKKPSVQKRIAELRESLKGRKLIIGVDRLDYSKGLPERLLAFERFLEEHPEWRGKVVLVQIAVPSRGDVPEYQQLRR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 321 EIDELVGRINGKYGTPEWVPISYFYRSLPFQTIVAFYLAADVALLTSMRDGMNLIAKEFVASRVDGKGVLILSEMAGAAR 400
Cdd:TIGR02400 317 QVEELVGRINGRFGTLDWTPIRYLNRSYDREELMALYRAADVGLVTPLRDGMNLVAKEYVAAQDPKDGVLILSEFAGAAQ 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 52548412 401 ELGEALVVNPNNKEEVAEALNEALRMPEEEQKSRNEEMQKRLSHYDVFHWGSGFIRS 457
Cdd:TIGR02400 397 ELNGALLVNPYDIDGMADAIARALTMPLEEREERHRAMMDKLRKNDVQRWREDFLSD 453
|
|
| Glyco_transf_20 |
pfam00982 |
Glycosyltransferase family 20; Members of this family belong to glycosyl transferase family 20. ... |
3-457 |
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: 561.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 3 RLLIISNRLPVSVERR----KNELRFSSSVGGLATGLNALHQRYESVWVGWPGIAIN-REETDYVESKLSE-FNCYPVFL 76
Cdd:pfam00982 2 RLVVVSNRLPVTAVRDeedgKWEFSIKMSSGGLVSALNGLSAATEGVWVGWPGVPVDeSEPKDKVSQSLKEkFNCVPVFL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 77 SQGEVEKYYYGFSNKTLWPLFHYFP---QYAKYEHSEWSAYEHVNRKFCERVAEIAKPEDIIWIHDYHLMLLPGLIRERF 153
Cdd:pfam00982 82 SDELFDSYYNGFSNSILWPLFHYMIppnNEDAFDRSWWDAYVKVNKLFADKIVEVYKDGDLIWIHDYHLMLLPQMLRKRL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 154 PDATIGFFLHIPFPSADLFRLIPWRRRILEGVLGADLIGFHTYDYAHNFLCSVLRLLG--YEHEFGkLAIGDRIVQVDVH 231
Cdd:pfam00982 162 PDAKIGFFLHTPFPSSEIFRCLPVREEILEGLLGADLIGFHTYDYARHFLSCCSRLLGleTRSDGG-VEYGGRTVSVKAF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 232 PMGVEVQKFVRATSGRGIKREVARLRSRFKN-CKIIFSMDRLDYTKGIPERLYAFEHFLETHPEWHEKVVFILKIAPSRT 310
Cdd:pfam00982 241 PIGIDPGRIESGLASPSVQEKIKELKERFGNkKKLIVGVDRLDYIKGIPQKLLAFERFLEEYPEWRGKVVLVQIAVPSRG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 311 KVGQYRVLKQEIDELVGRINGKYGTPEWVPISYFYRSLPFQTIVAFYLAADVALLTSMRDGMNLIAKEFVASRVDGKGVL 390
Cdd:pfam00982 321 DVEEYQNLRSQIEELVGRINGEFGTLDYTPVHFLHRPLDFDELIALYAVADVCLVTSLRDGMNLVAYEYVACQQGRKGVL 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 52548412 391 ILSEMAGAARELGE-ALVVNPNNKEEVAEALNEALRMPEEEQKSRNEEMQKRLSHYDVFHWGSGFIRS 457
Cdd:pfam00982 401 ILSEFAGAAQSLNDgAILVNPWDIDEVAEAINEALTMSEEERKKRHKKLYKYISKHDSQHWAESFLSD 468
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK14501 |
PRK14501 |
putative bifunctional trehalose-6-phosphate synthase/HAD hydrolase subfamily IIB; Provisional |
3-720 |
0e+00 |
|
putative bifunctional trehalose-6-phosphate synthase/HAD hydrolase subfamily IIB; Provisional
Pssm-ID: 184712 [Multi-domain] Cd Length: 726 Bit Score: 1116.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 3 RLLIISNRLPVSVERRKNELRFSSSVGGLATGLNALHQRYESVWVGWPGIAINR---EETDYVESKLSEFNCYPVFLSQG 79
Cdd:PRK14501 2 RLIIVSNRLPVTVVREDGGVELTPSVGGLATGLRSFHERGGGLWVGWPGLDLEEeseEQRARIEPRLEELGLVPVFLSAE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 80 EVEKYYYGFSNKTLWPLFHYFPQYAKYEHSEWSAYEHVNRKFCERVAEIAKPEDIIWIHDYHLMLLPGLIRERFPDATIG 159
Cdd:PRK14501 82 EVDRYYEGFCNSTLWPLFHYFPEYTEFEDRFWESYERVNQRFAEAIAAIARPGDVVWVHDYQLMLLPAMLRERLPDARIG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 160 FFLHIPFPSADLFRLIPWRRRILEGVLGADLIGFHTYDYAHNFLCSVLRLLGYEHEFGKLAIGDRIVQVDVHPMGVEVQK 239
Cdd:PRK14501 162 FFLHIPFPSFEVFRLLPWREEILEGLLGADLIGFHTYDYVRHFLSSVLRVLGYETELGEIRLGGRIVRVDAFPMGIDYDK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 240 FVRATSGRGIKREVARLRSRFKNCKIIFSMDRLDYTKGIPERLYAFEHFLETHPEWHEKVVFILKIAPSRTKVGQYRVLK 319
Cdd:PRK14501 242 FHNSAQDPEVQEEIRRLRQDLRGRKIILSIDRLDYTKGIPRRLLAFERFLEKNPEWRGKVRLVQVAVPSRTGVPQYQEMK 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 320 QEIDELVGRINGKYGTPEWVPISYFYRSLPFQTIVAFYLAADVALLTSMRDGMNLIAKEFVASRVDGKGVLILSEMAGAA 399
Cdd:PRK14501 322 REIDELVGRINGEFGTVDWTPIHYFYRSLPFEELVALYRAADVALVTPLRDGMNLVAKEYVASRTDGDGVLILSEMAGAA 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 400 RELGEALVVNPNNKEEVAEALNEALRMPEEEQKSRNEEMQKRLSHYDVFHWGSGFIRSVLETKRLQEELNMKKLSEKIRE 479
Cdd:PRK14501 402 AELAEALLVNPNDIEGIAAAIKRALEMPEEEQRERMQAMQERLRRYDVHKWASDFLDELREAAEKNKAFASKPITPAAAE 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 480 ELKNAYKAADKCLLLLDYDGTLVPFADKPERAKPDKELLYLFRALSEPPENTVVIISGRDKETLERWFGDTGVCLVAEHG 559
Cdd:PRK14501 482 EIIARYRAASRRLLLLDYDGTLVPFAPDPELAVPDKELRDLLRRLAADPNTDVAIISGRDRDTLERWFGDLPIHLVAEHG 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 560 VRLKEEEGEWKEIELLKEDWKEKIIPILDLFVDRAPGSFIEEKSFSLVWHYRKVDPELGELRAKELTDQLIDLTACTELQ 639
Cdd:PRK14501 562 AWSRAPGGEWQLLEPVATEWKDAVRPILEEFVDRTPGSFIEEKEASLAWHYRNADPELGEARANELILALSSLLSNAPLE 641
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 640 VMKGNKVVEVKDGRVNKGIAASHWLTKG-FGFILAVGDDLTDEDMFKVLPEGAYSVKIGFTPSKARFYLGSPKEVRALLD 718
Cdd:PRK14501 642 VLRGNKVVEVRPAGVNKGRAVRRLLEAGpYDFVLAIGDDTTDEDMFRALPETAITVKVGPGESRARYRLPSQREVRELLR 721
|
..
gi 52548412 719 EM 720
Cdd:PRK14501 722 RL 723
|
|
| OtsA |
COG0380 |
Trehalose-6-phosphate synthase, GT20 family [Carbohydrate transport and metabolism]; |
1-468 |
0e+00 |
|
Trehalose-6-phosphate synthase, GT20 family [Carbohydrate transport and metabolism];
Pssm-ID: 440149 Cd Length: 474 Bit Score: 715.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 1 MRRLLIISNRLPVSVERRKNELRFSSSVGGLATGLNALHQRYESVWVGWPGIAINREETDY----VESKLSEFNCYPVFL 76
Cdd:COG0380 1 GSRLVVVSNRLPVPHVREDGSIRVKRSAGGLVTALEPVLRRRGGLWVGWSGGDADREAVEEprgpVPPDLGGYTLAPVDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 77 SQGEVEKYYYGFSNKTLWPLFHYFPQYAKYEHSEWSAYEHVNRKFCERVAEIAKPEDIIWIHDYHLMLLPGLIRERFPDA 156
Cdd:COG0380 81 SAEEVDGYYEGFSNETLWPLFHYRLDLPEFDREDWEAYRRVNRRFAEALAEEAEPDDVVWVHDYHLLLVPAMLRELGPDA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 157 TIGFFLHIPFPSADLFRLIPWRRRILEGVLGADLIGFHTYDYAHNFLCSVLRLLGYE-HEFGKLAIGDRIVQVDVHPMGV 235
Cdd:COG0380 161 RIGFFLHIPFPPPEIFRILPWREEILEGLLGADLIGFQTPRDARNFLDCVRRLLGAEvDEGGTVRYGGRTVRVGAFPIGI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 236 EVQKFVRATSGRGIKREVARLRSRFKNCKIIFSMDRLDYTKGIPERLYAFEHFLETHPEWHEKVVFILKIAPSRTKVGQY 315
Cdd:COG0380 241 DVEEFAELARSPEVRARAERLREELGGRKLILGVDRLDYTKGIPERLRAFERLLERHPELRGKVTLLQIAVPSREDVPAY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 316 RVLKQEIDELVGRINGKYGTPEWVPISYFYRSLPFQTIVAFYLAADVALLTSMRDGMNLIAKEFVASRVDGKGVLILSEM 395
Cdd:COG0380 321 RELRREIEELVGRINGRFGTLDWTPIRYLNRSLPREELAALYRAADVALVTPLRDGMNLVAKEYVAAQPDDPGVLVLSEF 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 52548412 396 AGAARELGEALVVNPNNKEEVAEALNEALRMPEEEQKSRNEEMQKRLSHYDVFHWGSGFIRSVLETKRLQEEL 468
Cdd:COG0380 401 AGAAEELTEALLVNPYDIDGMAEAIHRALTMPLEERRRRMRALRERVRRYDVHRWADDFLDALAAVRAAASPL 473
|
|
| GT20_TPS |
cd03788 |
trehalose-6-phosphate synthase; Trehalose-6-Phosphate Synthase (TPS, EC 2.4.1.15) is a ... |
3-457 |
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: 683.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 3 RLLIISNRLPVSVERRK-NELRFSSSVGGLATGLNALHQRYESVWVGWPGIAINREETDYVESK--LSEFNCYPVFLSQG 79
Cdd:cd03788 1 RLIVVSNRLPVTLERDDdGEVEFRRSAGGLVTALKGLLKSTGGLWVGWPGIEADEEESDQVVSPelLEEYNVVPVFLSDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 80 EVEKYYYGFSNKTLWPLFHYFPQY--AKYEHSEWSAYEHVNRKFCERVAEIAKPEDIIWIHDYHLMLLPGLIRERFPDAT 157
Cdd:cd03788 81 DFEGYYNGFSNSVLWPLFHYLLPLpdGRFEREWWEAYVRVNQAFADAVVEVYRPGDLIWVHDYHLLLLPQMLRERLPDAR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 158 IGFFLHIPFPSADLFRLIPWRRRILEGVLGADLIGFHTYDYAHNFLCSVLRLLGYEHEF-GKLAIGDRIVQVDVHPMGVE 236
Cdd:cd03788 161 IGFFLHIPFPSSEIFRCLPWREEILRGLLGADLIGFQTFEYARHFLSCCSRLLGLETTSaGGVEYGGRRVRVGAFPIGID 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 237 VQKFVRATSGRGIKREVARLRSRFKNCKIIFSMDRLDYTKGIPERLYAFEHFLETHPEWHEKVVFILKIAPSRTKVGQYR 316
Cdd:cd03788 241 PDRFRRLAASPEVQERARELRERYKGKKLIVGVDRLDYTKGIPEKLLAFERFLERYPEWRGKVVLVQVAVPSRTDVEEYQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 317 VLKQEIDELVGRINGKYGTPEWVPISYFYRSLPFQTIVAFYLAADVALLTSMRDGMNLIAKEFVASRVDGKGVLILSEMA 396
Cdd:cd03788 321 ELRREVEELVGRINGRFGTLDWTPVVYLHQSLDREELLALYRAADVALVTSLRDGMNLVAKEYVACQRDNPGVLILSEFA 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 52548412 397 GAARELGEALVVNPNNKEEVAEALNEALRMPEEEQKSRNEEMQKRLSHYDVFHWGSGFIRS 457
Cdd:cd03788 401 GAASELDGAILVNPWDIEEVAEAINRALTMSPEERKERHQKLRKYVETHDVQAWANSFLDD 461
|
|
| trehalose_OtsA |
TIGR02400 |
alpha,alpha-trehalose-phosphate synthase [UDP-forming]; This enzyme catalyzes the key, ... |
3-457 |
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: 615.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 3 RLLIISNRLPVSVERRKNElrfsSSVGGLATGLNALHQRYESVWVGWPGIAINREETDYVESK--LSEFNCYPVFLSQGE 80
Cdd:TIGR02400 1 RLIVVSNRLPVPITRGGLE----PSAGGLAVALLGALKATGGVWFGWSGKTVEEDEGEPFLRTelEGKITLAPVFLSEED 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 81 VEKYYYGFSNKTLWPLFHYFPQYAKYEHSEWSAYEHVNRKFCERVAEIAKPEDIIWIHDYHLMLLPGLIRERFPDATIGF 160
Cdd:TIGR02400 77 VDGYYNGFSNSTLWPLFHYRPDLIRYDRKAWEAYRRVNRLFAEALAPLLQPGDIVWVHDYHLMLLPAMLRELGVQNKIGF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 161 FLHIPFPSADLFRLIPWRRRILEGVLGADLIGFHTYDYAHNFLCSVLRLLGYEHEFGKLAIGDRIVQVDVHPMGVEVQKF 240
Cdd:TIGR02400 157 FLHIPFPSSEIYRTLPWRRELLEGLLAYDLVGFQTYDDARNFLSAVSRELGLETLPNGVESGGRTVRVGAFPIGIDVDRF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 241 VRATSGRGIKREVARLRSRFKNCKIIFSMDRLDYTKGIPERLYAFEHFLETHPEWHEKVVFILKIAPSRTKVGQYRVLKQ 320
Cdd:TIGR02400 237 AEQAKKPSVQKRIAELRESLKGRKLIIGVDRLDYSKGLPERLLAFERFLEEHPEWRGKVVLVQIAVPSRGDVPEYQQLRR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 321 EIDELVGRINGKYGTPEWVPISYFYRSLPFQTIVAFYLAADVALLTSMRDGMNLIAKEFVASRVDGKGVLILSEMAGAAR 400
Cdd:TIGR02400 317 QVEELVGRINGRFGTLDWTPIRYLNRSYDREELMALYRAADVGLVTPLRDGMNLVAKEYVAAQDPKDGVLILSEFAGAAQ 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 52548412 401 ELGEALVVNPNNKEEVAEALNEALRMPEEEQKSRNEEMQKRLSHYDVFHWGSGFIRS 457
Cdd:TIGR02400 397 ELNGALLVNPYDIDGMADAIARALTMPLEEREERHRAMMDKLRKNDVQRWREDFLSD 453
|
|
| Glyco_transf_20 |
pfam00982 |
Glycosyltransferase family 20; Members of this family belong to glycosyl transferase family 20. ... |
3-457 |
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: 561.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 3 RLLIISNRLPVSVERR----KNELRFSSSVGGLATGLNALHQRYESVWVGWPGIAIN-REETDYVESKLSE-FNCYPVFL 76
Cdd:pfam00982 2 RLVVVSNRLPVTAVRDeedgKWEFSIKMSSGGLVSALNGLSAATEGVWVGWPGVPVDeSEPKDKVSQSLKEkFNCVPVFL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 77 SQGEVEKYYYGFSNKTLWPLFHYFP---QYAKYEHSEWSAYEHVNRKFCERVAEIAKPEDIIWIHDYHLMLLPGLIRERF 153
Cdd:pfam00982 82 SDELFDSYYNGFSNSILWPLFHYMIppnNEDAFDRSWWDAYVKVNKLFADKIVEVYKDGDLIWIHDYHLMLLPQMLRKRL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 154 PDATIGFFLHIPFPSADLFRLIPWRRRILEGVLGADLIGFHTYDYAHNFLCSVLRLLG--YEHEFGkLAIGDRIVQVDVH 231
Cdd:pfam00982 162 PDAKIGFFLHTPFPSSEIFRCLPVREEILEGLLGADLIGFHTYDYARHFLSCCSRLLGleTRSDGG-VEYGGRTVSVKAF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 232 PMGVEVQKFVRATSGRGIKREVARLRSRFKN-CKIIFSMDRLDYTKGIPERLYAFEHFLETHPEWHEKVVFILKIAPSRT 310
Cdd:pfam00982 241 PIGIDPGRIESGLASPSVQEKIKELKERFGNkKKLIVGVDRLDYIKGIPQKLLAFERFLEEYPEWRGKVVLVQIAVPSRG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 311 KVGQYRVLKQEIDELVGRINGKYGTPEWVPISYFYRSLPFQTIVAFYLAADVALLTSMRDGMNLIAKEFVASRVDGKGVL 390
Cdd:pfam00982 321 DVEEYQNLRSQIEELVGRINGEFGTLDYTPVHFLHRPLDFDELIALYAVADVCLVTSLRDGMNLVAYEYVACQQGRKGVL 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 52548412 391 ILSEMAGAARELGE-ALVVNPNNKEEVAEALNEALRMPEEEQKSRNEEMQKRLSHYDVFHWGSGFIRS 457
Cdd:pfam00982 401 ILSEFAGAAQSLNDgAILVNPWDIDEVAEAINEALTMSEEERKKRHKKLYKYISKHDSQHWAESFLSD 468
|
|
| PLN03063 |
PLN03063 |
alpha,alpha-trehalose-phosphate synthase (UDP-forming); Provisional |
3-720 |
4.03e-171 |
|
alpha,alpha-trehalose-phosphate synthase (UDP-forming); Provisional
Pssm-ID: 215555 [Multi-domain] Cd Length: 797 Bit Score: 510.95 E-value: 4.03e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 3 RLLIISNRLPVSVERR-KNELRFSSSVGGLATGLNALHQrYESVWVGWPGIAINRE-ETDYVESKLSEFNCYPVFLsQGE 80
Cdd:PLN03063 12 RLLVVANRLPVSAKRTgEDSWSLEMSPGGLVSALLGVKE-FETKWIGWPGVDVHDEiGKAALTESLAEKGCIPVFL-NEV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 81 VEKYYYGFSNKTLWPLFHYFPQYAKYEH-------SEWSAYEHVNRKFCERVAEIAKPEDIIWIHDYHLMLLPGLIRERF 153
Cdd:PLN03063 90 FDQYYNGYCNNILWPIFHYMGLPQEDRHdatrtfeSQYDAYKKANRMFLDVVKENYEEGDVVWCHDYHLMFLPQYLKEYN 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 154 PDATIGFFLHIPFPSADLFRLIPWRRRILEGVLGADLIGFHTYDYAHNFLCSVLRLLGYEHEFGKLAIGDRIVQVDVHPM 233
Cdd:PLN03063 170 NKMKVGWFLHTPFPSSEIYKTLPSRSELLRAVLTADLIGFHTYDFARHFLSACTRILGVEGTHEGVVDQGKVTRVAVFPI 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 234 GVEVQKFVRATSGRGIKREVARLRSRFKNCKIIFSMDRLDYTKGIPERLYAFEHFLETHPEWHEKVVFILKIAPSRTKVG 313
Cdd:PLN03063 250 GIDPERFINTCELPEVKQHMKELKRFFAGRKVILGVDRLDMIKGIPQKYLAFEKFLEENPEWRDKVMLVQIAVPTRNDVP 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 314 QYRVLKQEIDELVGRINGKYGTPEWVPISYFYRSLPFQTIVAFYLAADVALLTSMRDGMNLIAKEFVASRVDGKGVLILS 393
Cdd:PLN03063 330 EYQKLKSQVHELVGRINGRFGSVSSVPIHHLDCSVDFNYLCALYAITDVMLVTSLRDGMNLVSYEFVACQKAKKGVLVLS 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 394 EMAGAARELGE-ALVVNPNNKEEVAEALNEALRMPEEEQKSRNEEMQKRLSHYDVFHWGSGFIRSVLETKrLQEELNMKK 472
Cdd:PLN03063 410 EFAGAGQSLGAgALLVNPWNITEVSSAIKEALNMSDEERETRHRHNFQYVKTHSAQKWADDFMSELNDII-VEAELRTRN 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 473 LSEKIREE-LKNAYKAADKCLLLLDYDGTLV-PFADKPERAK--PDKELLYLFRALSEPPENTVVIISGRDKETLERWFG 548
Cdd:PLN03063 489 IPLELPEQdVIQQYSKSNNRLLILGFYGTLTePRNSQIKEMDlgLHPELKETLKALCSDPKTTVVVLSRSGKDILDKNFG 568
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 549 DTGVCLVAEHGVRLKEEEGEWKEIEL--LKEDWKEKIIPILDLFVDRAPGSFIEEKSFSLVWHYRKVDPELGELRAKELT 626
Cdd:PLN03063 569 EYNIWLAAENGMFLRHTSGEWVTTMPehMNLDWVDGVKNVFKYFTDRTPRSYVEKSETSLVWNYEYADVEFGRAQARDML 648
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 627 DQL-IDLTACTELQVMKGNKVVEVKDGRVNKGIAASHWL---------TKGFGFILAVGDDLT-DEDMF----------- 684
Cdd:PLN03063 649 QHLwAGPISNASVDVVRGQKSVEVHAIGVTKGAAIGRILgeivhnksmTTPIDFVFCSGYFLEkDEDVYtffepeilskk 728
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*
gi 52548412 685 -------------------KVLPEGAYSVKIGFTPSKARFYLGSPKEVRALLDEM 720
Cdd:PLN03063 729 kssssnysdsdkkvssnlvDLKGENYFSCAIGQARTKARYVLDSSNDVVSLLHKL 783
|
|
| PLN03064 |
PLN03064 |
alpha,alpha-trehalose-phosphate synthase (UDP-forming); Provisional |
2-714 |
8.10e-171 |
|
alpha,alpha-trehalose-phosphate synthase (UDP-forming); Provisional
Pssm-ID: 215556 [Multi-domain] Cd Length: 934 Bit Score: 514.35 E-value: 8.10e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 2 RRLLIISNRLPVSVERR-KNELRFSSSVGGLATGLNALHQrYESVWVGWPGIAINREETDYVESK-LSEFNCYPVFLSQG 79
Cdd:PLN03064 94 QRLLVVANRLPVSAVRRgEDSWSLEISAGGLVSALLGVKE-FEARWIGWAGVNVPDEVGQKALTKaLAEKRCIPVFLDEE 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 80 EVEKYYYGFSNKTLWPLFHY--FPQYAKYE-----HSEWSAYEHVNRKFCERVAEIAKPEDIIWIHDYHLMLLPGLIRER 152
Cdd:PLN03064 173 IVHQYYNGYCNNILWPLFHYlgLPQEDRLAttrsfQSQFAAYKKANQMFADVVNEHYEEGDVVWCHDYHLMFLPKCLKEY 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 153 FPDATIGFFLHIPFPSADLFRLIPWRRRILEGVLGADLIGFHTYDYAHNFLCSVLRLLGYEHEFGKLAIGDRIVQVDVHP 232
Cdd:PLN03064 253 NSNMKVGWFLHTPFPSSEIHRTLPSRSELLRSVLAADLVGFHTYDYARHFVSACTRILGLEGTPEGVEDQGRLTRVAAFP 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 233 MGVEVQKFVRATSGRGIKREVARLRSRFKNCKIIFSMDRLDYTKGIPERLYAFEHFLETHPEWHEKVVfILKIA-PSRTK 311
Cdd:PLN03064 333 IGIDSDRFIRALETPQVQQHIKELKERFAGRKVMLGVDRLDMIKGIPQKILAFEKFLEENPEWRDKVV-LLQIAvPTRTD 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 312 VGQYRVLKQEIDELVGRINGKYGTPEWVPISYFYRSLPFQTIVAFYLAADVALLTSMRDGMNLIAKEFVASRVDGKGVLI 391
Cdd:PLN03064 412 VPEYQKLTSQVHEIVGRINGRFGTLTAVPIHHLDRSLDFHALCALYAVTDVALVTSLRDGMNLVSYEFVACQDSKKGVLI 491
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 392 LSEMAGAARELGE-ALVVNPNNKEEVAEALNEALRMPEEEQKSRNEEMQKRLSHYDVFHWGSGFIrSVLETKRLQEELNM 470
Cdd:PLN03064 492 LSEFAGAAQSLGAgAILVNPWNITEVAASIAQALNMPEEEREKRHRHNFMHVTTHTAQEWAETFV-SELNDTVVEAQLRT 570
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 471 KKLSEKIREElkNA---YKAADKCLLLLDYDGTLVPFADKPERaKPDK----------ELLYLFRALSEPPENTVVIISG 537
Cdd:PLN03064 571 RQVPPQLPPE--DAiqrYLQSNNRLLILGFNATLTEPVDTPGR-RGDQikemelrlhpELKEPLRALCSDPKTTIVVLSG 647
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 538 RDKETLERWFGDTGVCLVAEHG--VRLKEEEGEWKEIELLKEDWKEKIIPILDLFVDRAPGSFIEEKSFSLVWHYRKVDP 615
Cdd:PLN03064 648 SDRSVLDENFGEFDMWLAAENGmfLRHTKGEWMTTMPEHLNMDWVDSVKHVFEYFTERTPRSHFETRETSLVWNYKYADV 727
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 616 ELGELRAKELTDQL----IDLTActeLQVMKGNKVVEVKDGRVNKG---------IAASHWLTKGFGFILAVGDDLT-DE 681
Cdd:PLN03064 728 EFGRLQARDMLQHLwtgpISNAA---VDVVQGSRSVEVRPVGVTKGaaidrilgeIVHSKSMTTPIDYVLCIGHFLGkDE 804
|
730 740 750
....*....|....*....|....*....|...
gi 52548412 682 DMFKVLPEGAYSVKIGFTPSKARFYLGSPKEVR 714
Cdd:PLN03064 805 DIYTFFEPELPSDSPAIARSRSPDGLKSSGDRR 837
|
|
| PLN02205 |
PLN02205 |
alpha,alpha-trehalose-phosphate synthase [UDP-forming] |
1-717 |
1.29e-153 |
|
alpha,alpha-trehalose-phosphate synthase [UDP-forming]
Pssm-ID: 177855 [Multi-domain] Cd Length: 854 Bit Score: 467.58 E-value: 1.29e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 1 MRRLLIISNRLPVSVERR---KNELRFS----SSVGGLATGLNalHQRYESVWVGWPGIAINREETDYVESKLSE-FNCY 72
Cdd:PLN02205 59 KDRIIIVANQLPIRAQRKsdgSKGWIFSwdenSLLLQLKDGLG--DDEIEVIYVGCLKEEIHLNEQEEVSQILLEtFKCV 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 73 PVFLSQGEVEKYYYGFSNKTLWPLFHYF----PQYA-KYEHSEWSAYEHVNRKFCERVAEIAKPED-IIWIHDYHLMLLP 146
Cdd:PLN02205 137 PTFLPPDLFTRYYHGFCKQQLWPLFHYMlplsPDLGgRFNRSLWQAYVSVNKIFADRIMEVINPEDdFVWIHDYHLMVLP 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 147 GLIRERFPDATIGFFLHIPFPSADLFRLIPWRRRILEGVLGADLIGFHTYDYAHNFLCSVLRLLGYEHEFGKLAIG---- 222
Cdd:PLN02205 217 TFLRKRFNRVKLGFFLHSPFPSSEIYKTLPIREELLRALLNSDLIGFHTFDYARHFLSCCSRMLGLSYESKRGYIGleyy 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 223 DRIVQVDVHPMGVEVQKFVRATSGRGIKREVARLRSRF--KNCKIIFSMDRLDYTKGIPERLYAFEHFLETHPEWHEKVV 300
Cdd:PLN02205 297 GRTVSIKILPVGIHMGQLQSVLSLPETEAKVKELIKQFcdQDRIMLLGVDDMDIFKGISLKLLAMEQLLMQHPEWQGKVV 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 301 FILKIAPSRTKVGQYRVLKQEIDELVGRINGKYGTPEWVPISYFYRSLPFQTIVAFYLAADVALLTSMRDGMNLIAKEFV 380
Cdd:PLN02205 377 LVQIANPARGKGKDVKEVQAETHSTVKRINETFGKPGYDPIVLIDAPLKFYERVAYYVVAECCLVTAVRDGMNLIPYEYI 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 381 ASR---------------VDGKGVLILSEMAGAARELGEALVVNPNNKEEVAEALNEALRMPEEEQKSRNEEMQKRLSHY 445
Cdd:PLN02205 457 ISRqgnekldkllglepsTPKKSMLVVSEFIGCSPSLSGAIRVNPWNIDAVADAMDSALEMAEPEKQLRHEKHYRYVSTH 536
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 446 DVFHWGSGFIRSVLETKR------------------LQEELNMKKLSekiREELKNAYKAADKCLLLLDYDGTLVPFADK 507
Cdd:PLN02205 537 DVGYWARSFLQDLERTCRdhsrrrcwgigfglsfrvVALDPNFRKLS---MEHIVSAYKRTTTRAILLDYDGTLMPQASI 613
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 508 PERakPDKELLYLFRALSEPPENTVVIISGRDKETLERWFGD-TGVCLVAEHG--VRLKEEEGEWKEIELLKEDWKEKII 584
Cdd:PLN02205 614 DKS--PSSKSIDILNTLCRDKNNMVFIVSARSRKTLADWFSPcEKLGIAAEHGyfLRLKRDVEWETCVPVADCSWKQIAE 691
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 585 PILDLFVDRAPGSFIEEKSFSLVWHYRKVDPELGELRAKELTDQLIDLTACTELQVMKGNKVVEVKDGRVNKGIAASHWL 664
Cdd:PLN02205 692 PVMQLYTETTDGSTIEDKETALVWCYEDADPDFGSCQAKELLDHLESVLANEPVTVKSGQNIVEVKPQGVSKGLVAKRLL 771
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 665 T----KGF--GFILAVGDDLTDEDMFKVL------PEGA-----YSVKIGFTPSKARFYLGSPKEVRALL 717
Cdd:PLN02205 772 SimqeRGMlpDFVLCIGDDRSDEDMFEVItssmagPSIApraevFACTVGQKPSKAKYYLDDTAEIVRLM 841
|
|
| gluc_glyc_Psyn |
TIGR02398 |
glucosylglycerol-phosphate synthase; Glucosylglycerol-phosphate synthase catalyzes the key ... |
25-464 |
3.55e-116 |
|
glucosylglycerol-phosphate synthase; Glucosylglycerol-phosphate synthase catalyzes the key step in the biosynthesis of the osmolyte glucosylglycerol. It is known in several cyanobacteria and in Pseudomonas anguilliseptica. The enzyme is closely related to the alpha,alpha-trehalose-phosphate synthase, likewise involved in osmolyte biosynthesis, of E. coli and many other bacteria. A close homolog from Xanthomonas campestris is excluded from this model and scores between trusted and noise.
Pssm-ID: 131451 Cd Length: 487 Bit Score: 358.44 E-value: 3.55e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 25 SSSVGGLATGLNALHQRYESVWVGWPGIAINREETDYVESKL---SEFNCYPVFLSQGEVEKYYYGFSNKTLWPLFHYFP 101
Cdd:TIGR02398 23 TSPNGIIPTLLSFFGDGRAGTWVAWAEHDENSGETFDSHMTVpaeYKLTAARIPLSKEQVDIFYHITSKEAFWPILHTFP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 102 QYAKYEHSEWSAYEHVNRKFCERVAEIAKPEDIIWIHDYHLMLLPGLIRERFPDATIGFFLHIPFPSADLFRLIPWRRRI 181
Cdd:TIGR02398 103 ERFQFREDDWQVFLKVNRAFAEAACLEAAEGATVWVHDYNLWLVPGYIRQLRPDLKIAFFHHTPFPSADVFNILPWREQI 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 182 LEGVLGADLIGFHTYDYAHNF---------------------LCSVLRLLGYEHEFGKLAIGDRIVQVDVHPMGVEVQKF 240
Cdd:TIGR02398 183 IGSLLCCDYIGFHIPRYVENFvdaarglmplqtvsrqnvdprFITVGTALGEERMTTALDTGNRVVKLGAHPVGTDPERI 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 241 VRATSGRGIKREVARLRSRFKNCKIIFSMDRLDYTKGIPERLYAFEHFLETHPEWHEKVVFILKIAPSRTKVGQYRVLKQ 320
Cdd:TIGR02398 263 RSALAAASIREMMERIRSELAGVKLILSAERVDYTKGILEKLNAYERLLERRPELLGKVTLVTACVPAASGMTIYDELQG 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 321 EIDELVGRINGKYGTPEWVPISYFYRSLPFQTIVAFYLAADVALLTSMRDGMNLIAKEFVASRVDGKGVLILSEMAGAAR 400
Cdd:TIGR02398 343 QIEQAVGRINGRFARIGWTPLQFFTRSLPYEEVSAWFAMADVMWITPLRDGLNLVAKEYVAAQGLLDGVLVLSEFAGAAV 422
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 52548412 401 ELGEALVVNPNNKEEVAEALNEALRMPEEEQKSRNEEMQKRLSHYDVFHWGSGFIRSVLETKRL 464
Cdd:TIGR02398 423 ELKGALLTNPYDPVRMDETIYVALAMPKAEQQARMREMFDAVNYYDVQRWADEFLAAVSPQAQL 486
|
|
| PRK10117 |
PRK10117 |
trehalose-6-phosphate synthase; Provisional |
1-472 |
5.91e-106 |
|
trehalose-6-phosphate synthase; Provisional
Pssm-ID: 182249 Cd Length: 474 Bit Score: 331.33 E-value: 5.91e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 1 MRRLLIISNRLPVSVERRknelrfsSSVGGLATG-LNALhQRYESVWVGWPGiAINREETDYveSKLSEFN-CYPVF-LS 77
Cdd:PRK10117 1 MSRLVVVSNRIAPPDEHK-------ASAGGLAVGiLGAL-KAAGGLWFGWSG-ETGNEDQPL--KKVKKGNiTWASFnLS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 78 QGEVEKYYYGFSNKTLWPLFHYFPQYAKYEHSEWSAYEHVNRKFCERVAEIAKPEDIIWIHDYHLMLLPGLIRERFPDAT 157
Cdd:PRK10117 70 EQDYDEYYNQFSNAVLWPAFHYRLDLVQFQRPAWEGYLRVNALLADKLLPLLKDDDIIWIHDYHLLPFASELRKRGVNNR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 158 IGFFLHIPFPSADLFRLIPWRRRILEGVLGADLIGFHTYDYAHNFLCSVLRLLGYEHEFGK--LAIGdRIVQVDVHPMGV 235
Cdd:PRK10117 150 IGFFLHIPFPTPEIFNALPPHDELLEQLCDYDLLGFQTENDRLAFLDCLSNLTRVTTRSGKshTAWG-KAFRTEVYPIGI 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 236 EVQKFVRATSGrGIKREVARLRSRFKNCKIIFSMDRLDYTKGIPERLYAFEHFLETHPEWHEKVVFIlKIAP-SRTKVGQ 314
Cdd:PRK10117 229 EPDEIAKQAAG-PLPPKLAQLKAELKNVQNIFSVERLDYSKGLPERFLAYEALLEKYPQHHGKIRYT-QIAPtSRGDVQA 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 315 YRVLKQEIDELVGRINGKYGTPEWVPISYFYRSLPFQTIVAFYLAADVALLTSMRDGMNLIAKEFVASR-VDGKGVLILS 393
Cdd:PRK10117 307 YQDIRHQLETEAGRINGKYGQLGWTPLYYLNQHFDRKLLMKIFRYSDVGLVTPLRDGMNLVAKEYVAAQdPANPGVLVLS 386
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 52548412 394 EMAGAARELGEALVVNPNNKEEVAEALNEALRMPEEEQKSRNEEMQKRLSHYDVFHWGSGFIRSVLETKRLQEELNMKK 472
Cdd:PRK10117 387 QFAGAANELTSALIVNPYDRDEVAAALDRALTMPLAERISRHAEMLDVIVKNDINHWQECFISDLKQIVPRSAESQQRD 465
|
|
| OtsB |
COG1877 |
Trehalose-6-phosphate phosphatase [Carbohydrate transport and metabolism]; |
488-720 |
3.08e-81 |
|
Trehalose-6-phosphate phosphatase [Carbohydrate transport and metabolism];
Pssm-ID: 441481 [Multi-domain] Cd Length: 242 Bit Score: 258.58 E-value: 3.08e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 488 ADKCLLLLDYDGTLVPFADKPERAKPDKELLYLFRALSEPPENTVVIISGRDKETLERWFGDTGVCLVAEHGV--RLKEE 565
Cdd:COG1877 1 APRLLLFLDFDGTLAPIVPDPDAARPPPELRELLRRLAARPGGAVAIVSGRDLADLDRLLGPLGLPLAGSHGAerRLPGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 566 EGEWKEIELLKEDWKEKIIPILDLFVDRAPGSFIEEKSFSLVWHYRKVDPELgelrAKELTDQLIDLTAC--TELQVMKG 643
Cdd:COG1877 81 EWEVLPLAAEAPEWLDALRAALEALAARTPGVLVEDKGASLALHYRQAPPEE----AEELRAALRELAARlgPGLEVLPG 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 52548412 644 NKVVEVKDGRVNKGIAASHWLTK-GFG-FILAVGDDLTDEDMFKVLPEGAYSVKIGFTPSKARFYLGSPKEVRALLDEM 720
Cdd:COG1877 157 KKVVELRPAGVDKGRAVRALLAElPFGrAPVFIGDDVTDEDAFAALPAGGLGIKVGSGPTAARYRLADPAEVRALLARL 235
|
|
| HAD_TPP |
cd01627 |
trehalose-phosphate phosphatase similar to Escherichia coli trehalose-6-phosphate phosphatase ... |
492-715 |
2.53e-66 |
|
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: 218.70 E-value: 2.53e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 492 LLLLDYDGTLVPFADKPERAKPDKELLYLFRALSEPPENTVVIISGRDKETLERWFGDTGVCLVAEHGVRLKEEEGEWKE 571
Cdd:cd01627 1 LLFLDYDGTLAPIVPDPDAAVPSPELLEALKKLAADPKNAVAIVSGRDLDDLDKWLGLPGIGLAGEHGAEIRLPGGGEWV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 572 IELLKED--WKEKIIPILDLFVDRAPGSFIEEKSFSLVWHYRKVDPElGELRAKELTDQLIDlTACTELQVMKGNKVVEV 649
Cdd:cd01627 81 TLAPKADleWKEEVEAIFKYFTERTPGSLVEDKGASLAWHYRNADPE-GARAALELALHLAS-DLLKALEVVPGKKVVEV 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 650 KDGRVNKGIAASHWLTKGFG---FILAVGDDLTDEDMFKVLPE-GAYSVKIGFTPSKARFYLGSPKEVRA 715
Cdd:cd01627 159 RPVGVNKGEAVERILGELPFagdFVLCAGDDVTDEDAFRALNGeGGFSVKVGEGPTAAKFRLDDPPDVVA 228
|
|
| Trehalose_PPase |
pfam02358 |
Trehalose-phosphatase; This family consist of trehalose-phosphatases EC:3.1.3.12 these enzyme ... |
494-710 |
5.63e-51 |
|
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: 177.53 E-value: 5.63e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 494 LLDYDGTLVPFADKPERAKPDKELLYLFRALSEPPENTVVIISGRDKETLERWFGDTGVCLVAEHG--VRLKEEEGEWKE 571
Cdd:pfam02358 1 FLDYDGTLSPIVSDPIAAVPSDRMLSALQDLASDPPNTVAIISGRSRQEEDLFVGVPNLGLAAEHGafVRLPGGGDWYNQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 572 IELLKEDWKEKIIPILDLFVDRAPGSFIEEKSFSLVWHYRKVDPELGELRAKELTDQLID-LTACTELQVMKGNKVVEVK 650
Cdd:pfam02358 81 AEVEDLPWKKEVAPILEYYTERTPGSYVENKKSALSWHYRNADDDFGSFQAKELAEHLESvLQDNPPLRVTQGKKVVEVR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 52548412 651 DGRVNKGIAAsHWLTKGFG-------FILAVGDDLTDEDMFKVL---PEGAYSVKIGFT-----PSKARFYLGSP 710
Cdd:pfam02358 161 PVGVSKGKAV-EFILEELGsagslpdFPLCIGDDRTDEDMFSVLrptKPSGVGIEVFAVsvgskPSSASYFLDDP 234
|
|
| T6PP |
TIGR00685 |
trehalose-phosphatase; Trehalose, a neutral disaccharide of two glucose residues, is an ... |
488-718 |
8.20e-35 |
|
trehalose-phosphatase; Trehalose, a neutral disaccharide of two glucose residues, is an important osmolyte for dessication and/or salt tolerance in a number of prokaryotic and eukaryotic species, including E. coli, Saccharomyces cerevisiae, and Arabidopsis thaliana. Many bacteria also utilize trehalose in the synthesis of trehalolipids, specialized cell wall constituents believed to be involved in the uptake of hydrophobic substances. Trehalose dimycolate (TDM, cord factor) and related substances are important constituents of the mycobacterial waxy coat and responsible for various clinically important immunological interactions with host organism. This enzyme, trehalose-phosphatase, removes a phosphate group in the final step of trehalose biosynthesis. The trehalose-phosphatase from Saccharomyces cerevisiae is fused to the synthase. At least 18 distinct sequences from Arabidopsis have been identified, roughly half of these are of the fungal type, with a fused synthase and half are like the bacterial members having only the phosphatase domain. It has been suggested that trehalose is being used in Arabidopsis as a regulatory molecule in development and possibly other processes. [Cellular processes, Adaptations to atypical conditions]
Pssm-ID: 273219 [Multi-domain] Cd Length: 244 Bit Score: 132.65 E-value: 8.20e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 488 ADKCLLLLDYDGTLVPFADKPERAKPDKELLYLFRALSEPPENTVVIISGRDKETLERWFGDTGVCLVAEHGVRLKEEEG 567
Cdd:TIGR00685 1 ARKRAFFFDYDGTLSEIVPDPDAAVVSDRLLTILQKLAARPHNAIWIISGRKFLEKWLGVKLPGLGLAGEHGCEMKDNGS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 568 EWKEIELLKED--WKEKIIPILDLFVDRaPGSFIEEKSFSLVWHYRK-VDPELGELRAKELTDQLIDLTActeLQVMKGN 644
Cdd:TIGR00685 81 CQDWVNLTEKIpsWKVRANELREEITTR-PGVFIERKGVALAWHYRQaPVPELARFRAKELKEKILSFTD---LEVMDGK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 645 KVVEVKDGRVNKG--IAASHWLTKGFGFI-LAVGDDLTDEDMFKVLPE-----GAYSVKIGfTPSK---ARFYLGSPKEV 713
Cdd:TIGR00685 157 AVVELKPRFVNKGeiVKRLLWHQPGSGISpVYLGDDITDEDAFRVVNNqwgnyGFYPVPIG-SGSKktvAKFHLTGPQQV 235
|
....*
gi 52548412 714 RALLD 718
Cdd:TIGR00685 236 LEFLG 240
|
|
| HAD-SF-IIB |
TIGR01484 |
HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid ... |
492-690 |
4.65e-18 |
|
HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The Class II subfamilies are characterized by a domain that is located between the second and third conserved catalytic motifs of the superfamily domain. The IIB subfamily is distinguished from the IIA subfamily (TIGR01460) by homology and the predicted secondary structure of this domain by PSI-PRED. The IIB subfamily's Class II domain has the following predicted structure: Helix-Sheet-Sheet-(Helix or Sheet)-Helix-Sheet-(variable)-Helix-Sheet-Sheet. The IIB subfamily consists of Trehalose-6-phosphatase (TIGR00685), plant and cyanobacterial Sucrose-phosphatase and a closely related group of bacterial and archaeal sequences, eukaryotic phosphomannomutase (pfam03332), a large subfamily ("Cof-like hydrolases", TIGR00099) containing many closely related bacterial sequences, a hypothetical equivalog containing the E. coli YedP protein, as well as two small clusters containing OMNI|TC0379 and OMNI|SA2196 whose relationship to the other groups is unclear. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 273651 [Multi-domain] Cd Length: 207 Bit Score: 83.20 E-value: 4.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 492 LLLLDYDGTLVPfadkPERAKPDKELLYLFRALSEPpENTVVIISGRDKETLERWFGDTGVC--LVAEHG-----VRLKE 564
Cdd:TIGR01484 1 LLFFDLDGTLLD----PNAHELSPETIEALERLREA-GVKVVIVTGRSLAEIKELLKQLNLPlpLIAENGalifyPGEIL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 565 EEGEWKEIELLKEDWKEKIIPILDLFVDRAPGSFIEEKSFSLVWHYrkVDPELGELRAKELTDQLiDLTACTELQV---M 641
Cdd:TIGR01484 76 YIEPSDVFEEILGIKFEEIGAELKSLSEHYVGTFIEDKAIAVAIHY--VGAELGQELDSKMRERL-EKIGRNDLELeaiY 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 52548412 642 KGNKVVEVKDGRVNKGIAASHWLTKGFG---FILAVGDDLTDEDMFKVLPEG 690
Cdd:TIGR01484 153 SGKTDLEVLPAGVNKGSALQALLQELNGkkdEILAFGDSGNDEEMFEVAGLA 204
|
|
| PLN02151 |
PLN02151 |
trehalose-phosphatase |
451-720 |
8.28e-17 |
|
trehalose-phosphatase
Pssm-ID: 177812 Cd Length: 354 Bit Score: 82.80 E-value: 8.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 451 GSGFIRSVLETKRLQEELNMKKLSEK------------IREELKNAYKAaDKCLLLLDYDGTLVPFADKPERAKPDKELL 518
Cdd:PLN02151 48 GGGLIRSWVDSMRACSPTRPKSFNKQscwikehpsalnMFEEILHKSEG-KQIVMFLDYDGTLSPIVDDPDRAFMSKKMR 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 519 YLFRALSE--PpentVVIISGRDKETLERWFGDTGVCLVAEHGVRLK----EEEGEWKEIELLKEDWKEkIIPILDLFVD 592
Cdd:PLN02151 127 NTVRKLAKcfP----TAIVSGRCREKVSSFVKLTELYYAGSHGMDIKgpeqGSKYKKENQSLLCQPATE-FLPVINEVYK 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 593 R-------APGSFIEEKSFSLVWHYRKVDpelgELRAKELTDQLID-LTACTELQVMKGNKVVEVKD-GRVNKGiAASHW 663
Cdd:PLN02151 202 KlvektksIPGAKVENNKFCASVHFRCVE----ENKWSDLANQVRSvLKNYPKLMLTQGRKVLEIRPiIKWDKG-KALEF 276
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 52548412 664 LTKGFG-------FILAVGDDLTDEDMFKVLPEGAYSVKIGFTP----SKARFYLGSPKEVRALLDEM 720
Cdd:PLN02151 277 LLESLGyanctdvFPIYIGDDRTDEDAFKILRDKKQGLGILVSKyakeTNASYSLQEPDEVMEFLERL 344
|
|
| PLN02580 |
PLN02580 |
trehalose-phosphatase |
484-717 |
4.78e-11 |
|
trehalose-phosphatase
Pssm-ID: 215317 [Multi-domain] Cd Length: 384 Bit Score: 65.22 E-value: 4.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 484 AYKAADKCLLLLDYDGTLVPFADKPERAKPDKELLYLFRALSE--PpentVVIISGRDKETLERWFGDTGVCLVAEHG-- 559
Cdd:PLN02580 113 NFAKGKKIALFLDYDGTLSPIVDDPDRALMSDAMRSAVKNVAKyfP----TAIISGRSRDKVYELVGLTELYYAGSHGmd 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 560 ----VRLKEEEGEWKEIELLKEDWKE--------KIIPILDLfVDRA--------PGSFIEEKSFSLVWHYRKVDPELGE 619
Cdd:PLN02580 189 imgpVRESVSNDHPNCIKSTDQQGKEvnlfqpasEFLPMIDE-VFRSlvestkdiKGAKVENHKFCVSVHYRNVDEKNWP 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 620 LRAKELTDQLIDLTactELQVMKGNKVVEVKDG-RVNKGIAAShWLTKGFGFI-------LAVGDDLTDEDMFKVLPEG- 690
Cdd:PLN02580 268 LVAQCVHDVLKKYP---RLRLTHGRKVLEVRPViDWNKGKAVE-FLLESLGLSncddvlpIYIGDDRTDEDAFKVLREGn 343
|
250 260 270
....*....|....*....|....*....|
gi 52548412 691 -AYSVKIGFTP--SKARFYLGSPKEVRALL 717
Cdd:PLN02580 344 rGYGILVSSVPkeSNAFYSLRDPSEVMEFL 373
|
|
| GT4_PimA-like |
cd03801 |
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ... |
123-446 |
6.26e-11 |
|
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: 64.87 E-value: 6.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 123 ERVAEIAKPEDIIWIHDYHLMLLpGLIRERFPDATIGFFLHiPFPSADLFRLIPWRRRILEGVL----GADLIGFHTydy 198
Cdd:cd03801 74 LRPLLRLRKFDVVHAHGLLAALL-AALLALLLGAPLVVTLH-GAEPGRLLLLLAAERRLLARAEallrRADAVIAVS--- 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 199 ahNFLCSVLRLLGyehefgklaiGDRIVQVDVHPMGVEVQKFvratsgrgiKREVARLRSRFKNCKIIFSMDRLDYTKGI 278
Cdd:cd03801 149 --EALRDELRALG----------GIPPEKIVVIPNGVDLERF---------SPPLRRKLGIPPDRPVLLFVGRLSPRKGV 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 279 PERLYAFEHFLETHPEWHekvvFILkiapsrtkVGQYRVLKQEIDELvgringKYGTPEWVpisYFYRSLPFQTIVAFYL 358
Cdd:cd03801 208 DLLLEALAKLLRRGPDVR----LVI--------VGGDGPLRAELEEL------ELGLGDRV---RFLGFVPDEELPALYA 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 359 AADVALLTSMRDGMNLIAKE-------FVASRVDGKGVLILSEMAGaarelgeaLVVNPNNKEEVAEALNEALRMPEEEQ 431
Cdd:cd03801 267 AADVFVLPSRYEGFGLVVLEamaaglpVVATDVGGLPEVVEDGEGG--------LVVPPDDVEALADALLRLLADPELRA 338
|
330
....*....|....*
gi 52548412 432 KSRNEEMQKRLSHYD 446
Cdd:cd03801 339 RLGRAARERVAERFS 353
|
|
| PLN03017 |
PLN03017 |
trehalose-phosphatase |
455-717 |
8.10e-11 |
|
trehalose-phosphatase
Pssm-ID: 178591 [Multi-domain] Cd Length: 366 Bit Score: 64.28 E-value: 8.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 455 IRSVLETKRLQEELN---MKKLS-----EKIREELKnaykaADKCLLLLDYDGTLVPFADKPERAKPDKELLYLFRALSE 526
Cdd:PLN03017 73 LKSLPSSISSQQQLNswiMQHPSalemfEQIMEASR-----GKQIVMFLDYDGTLSPIVDDPDKAFMSSKMRRTVKKLAK 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 527 --PpentVVIISGRDKETLERWFGDTGVCLVAEHGVRLKEEEGEWKEIELLKE--------DWKEKIIPILDLFVDRA-- 594
Cdd:PLN03017 148 cfP----TAIVTGRCIDKVYNFVKLAELYYAGSHGMDIKGPAKGFSRHKRVKQsllyqpanDYLPMIDEVYRQLLEKTks 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 595 -PGSFIEEKSFSLVWHYRKVDpelgELRAKELTDQLID-LTACTELQVMKGNKVVEVKDG-RVNKGIAASHWLTK-GFG- 669
Cdd:PLN03017 224 tPGAKVENHKFCASVHFRCVD----EKKWSELVLQVRSvLKNFPTLKLTQGRKVFEIRPMiEWDKGKALEFLLESlGFGn 299
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 52548412 670 ----FILAVGDDLTDEDMFKVLP---EGaYSVKIGFTP--SKARFYLGSPKEVRALL 717
Cdd:PLN03017 300 tnnvFPVYIGDDRTDEDAFKMLRdrgEG-FGILVSKFPkdTDASYSLQDPSEVMDFL 355
|
|
| PRK10187 |
PRK10187 |
trehalose-6-phosphate phosphatase; Provisional |
496-720 |
7.03e-09 |
|
trehalose-6-phosphate phosphatase; Provisional
Pssm-ID: 182291 [Multi-domain] Cd Length: 266 Bit Score: 57.44 E-value: 7.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 496 DYDGTLVPFADKPERAKPDKELLYLFRALSEPPENTVVIISGRDKETLERW-----FGDTGVclvaeHGVRLKEEEGEWK 570
Cdd:PRK10187 20 DLDGTLAEIKPHPDQVVVPDNILQGLQLLATANDGALALISGRSMVELDALakpyrFPLAGV-----HGAERRDINGKTH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 571 EIEL---LKEDWKEKIIPILDLFvdraPGSFIEEKSFSLVWHYRKvdpelgelrAKELTDQLIDL-----TACTELQVMK 642
Cdd:PRK10187 95 IVHLpdaIARDISVQLHTALAQL----PGAELEAKGMAFALHYRQ---------APQHEDALLALaqritQIWPQLALQP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 643 GNKVVEVKDGRVNKGIAASHWLTKGfGFI----LAVGDDLTDEDMFKVL-PEGAYSVKIGFTPSKARFYLGSPKEVRALL 717
Cdd:PRK10187 162 GKCVVEIKPRGTNKGEAIAAFMQEA-PFAgrtpVFVGDDLTDEAGFAVVnRLGGISVKVGTGATQASWRLAGVPDVWSWL 240
|
...
gi 52548412 718 DEM 720
Cdd:PRK10187 241 EMI 243
|
|
| Glycos_transf_1 |
pfam00534 |
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ... |
264-432 |
7.26e-07 |
|
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: 49.58 E-value: 7.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 264 KIIFSMDRLDYTKGIPERLYAFEHFLETHPEWheKVVFilkiapsrtkVGQyrvlKQEIDELVGRInGKYGTPEWVpisY 343
Cdd:pfam00534 3 KIILFVGRLEPEKGLDLLIKAFALLKEKNPNL--KLVI----------AGD----GEEEKRLKKLA-EKLGLGDNV---I 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 344 FYRSLPFQTIVAFYLAADVALLTSMRDGMNLIAKEFVASrvdgkGVLILSEMAGAAREL----GEALVVNPNNKEEVAEA 419
Cdd:pfam00534 63 FLGFVSDEDLPELLKIADVFVLPSRYEGFGIVLLEAMAC-----GLPVIASDVGGPPEVvkdgETGFLVKPNNAEALAEA 137
|
170
....*....|...
gi 52548412 420 LNEALRMPEEEQK 432
Cdd:pfam00534 138 IDKLLEDEELRER 150
|
|
| GT4_Bme6-like |
cd03821 |
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ... |
264-432 |
2.31e-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: 44.28 E-value: 2.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 264 KIIFSMDRLDYTKGIPERLYAFEHFLETHPEWHekvvfiLKIAPSRTkvGQYRVLKQEIDELVGRingkygtpewvPISY 343
Cdd:cd03821 205 RIILFLGRIHPKKGLDLLIRAARKLAEQGRDWH------LVIAGPDD--GAYPAFLQLQSSLGLG-----------DRVT 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 344 FYRSLPFQTIVAFYLAADVALLTSMRDGMNLIAKEFVASrvdGKGVLILSEMAGAA-RELGEALVVNPNNkEEVAEALNE 422
Cdd:cd03821 266 FTGPLYGEAKWALYASADLFVLPSYSENFGNVVAEALAC---GLPVVITDKCGLSElVEAGCGVVVDPNV-SSLAEALAE 341
|
170
....*....|
gi 52548412 423 ALRMPEEEQK 432
Cdd:cd03821 342 ALRDPADRKR 351
|
|
| RfaB |
COG0438 |
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ... |
353-446 |
2.46e-04 |
|
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440207 [Multi-domain] Cd Length: 123 Bit Score: 41.51 E-value: 2.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 353 IVAFYLAADVALLTSMRDGMNLIAKEFVASrvdgkGVLILSEMAGAARELGE----ALVVNPNNKEEVAEALNEALRMPE 428
Cdd:COG0438 14 LEALLAAADVFVLPSRSEGFGLVLLEAMAA-----GLPVIATDVGGLPEVIEdgetGLLVPPGDPEALAEAILRLLEDPE 88
|
90
....*....|....*...
gi 52548412 429 EEQKSRNEEMQKRLSHYD 446
Cdd:COG0438 89 LRRRLGEAARERAEERFS 106
|
|
| S6PP |
pfam05116 |
Sucrose-6F-phosphate phosphohydrolase; This family consists of Sucrose-6F-phosphate ... |
492-716 |
4.29e-03 |
|
Sucrose-6F-phosphate phosphohydrolase; This family consists of Sucrose-6F-phosphate phosphohydrolase proteins found in plants and cyanobacteria. Sucrose-6(F)-phosphate phosphohydrolase catalyzes the final step in the pathway of sucrose biosynthesis.
Pssm-ID: 428314 [Multi-domain] Cd Length: 246 Bit Score: 39.56 E-value: 4.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 492 LLLLDYDGTLVPfadkperakPDKELLYLFRALSEP--PENTVVIISGRD---------KETLER---WFGDTGVCLVAE 557
Cdd:pfam05116 4 LLVSDLDNTLVD---------GDNEALARLNQLLEAyrPDVGLVFATGRSldsakellkEKPLPTpdyLITSVGTEIYYG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 558 HGVRLkeeegEWKEIELLKEDW-KEKIIPILDLFVDRAPGSFIEEKSFSLVWHyrkVDPElgelRAKELTDQLIDLTACT 636
Cdd:pfam05116 75 PSLVP-----DQSWQEHLDYHWdRQAVVEALAKFPGLTLQPEEEQRPHKVSYF---LDPE----AAAAVLAELEQLLRKR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52548412 637 ELQV---MKGNKVVEVKDGRVNKGiAASHWLTKGFGF----ILAVGDDLTDEDMFKvlpEGAYSVKIG-FTPSKARFYLG 708
Cdd:pfam05116 143 GLDVkviYSSGRDLDILPLRASKG-EALRYLALKLGLplenTLVCGDSGNDEELFI---GGTRGVVVGnAQPELLQWYLE 218
|
....*...
gi 52548412 709 SPKEVRAL 716
Cdd:pfam05116 219 NARDNPRI 226
|
|
| |
