|
Name |
Accession |
Description |
Interval |
E-value |
| PRK14501 |
PRK14501 |
putative bifunctional trehalose-6-phosphate synthase/HAD hydrolase subfamily IIB; Provisional |
20-766 |
0e+00 |
|
putative bifunctional trehalose-6-phosphate synthase/HAD hydrolase subfamily IIB; Provisional
Pssm-ID: 184712 [Multi-domain] Cd Length: 726 Bit Score: 641.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 20 LIVVSNRLPFVLIRDPKTDELERraSAGGLVTAVCPVVIKGSGLWVGWSGIHLkdpnEAIPESNPNDQTPTagLKSEQVV 99
Cdd:PRK14501 3 LIIVSNRLPVTVVREDGGVELTP--SVGGLATGLRSFHERGGGLWVGWPGLDL----EEESEEQRARIEPR--LEELGLV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 100 SVNIDSKIFDSYYNGCCNKIFWPLFHSMPGRANFGGEHWHDYVTVNKHFA---VRTIEAlekclaknqGSeksppIVWIH 176
Cdd:PRK14501 75 PVFLSAEEVDRYYEGFCNSTLWPLFHYFPEYTEFEDRFWESYERVNQRFAeaiAAIARP---------GD-----VVWVH 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 177 DYHLMLAANWVREHAEEKnlpcRLAFFLHIPFPPWDIFRLLPWSDEILQGMLGCDLVGFHIQDYCLNFVDCCQRNLGCRV 256
Cdd:PRK14501 141 DYQLMLLPAMLRERLPDA----RIGFFLHIPFPSFEVFRLLPWREEILEGLLGADLIGFHTYDYVRHFLSSVLRVLGYET 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 257 DRNNllVEHGGRTVRVRPLPIGIPYERFVNLATTaPKV--------LKTSKMQIILGVDRLDYTKGLVHRLMAFEALLLK 328
Cdd:PRK14501 217 ELGE--IRLGGRIVRVDAFPMGIDYDKFHNSAQD-PEVqeeirrlrQDLRGRKIILSIDRLDYTKGIPRRLLAFERFLEK 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 329 YPQHKEKVSLLQISVPSRTDVKEYRELKEEVDQLVGRINGRFTTANWAPIRYIYDYVSQDELAALYRDAAVCLVTPLRDG 408
Cdd:PRK14501 294 NPEWRGKVRLVQVAVPSRTGVPQYQEMKREIDELVGRINGEFGTVDWTPIHYFYRSLPFEELVALYRAADVALVTPLRDG 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 409 MNLVAKEFVACQINEvPGVLVISPFAGAGEMMHEALLCNPYEVNEAAEVIHRALTMPEDERVLRMARLRRREAECDVSHW 488
Cdd:PRK14501 374 MNLVAKEYVASRTDG-DGVLILSEMAGAAAELAEALLVNPNDIEGIAAAIKRALEMPEEEQRERMQAMQERLRRYDVHKW 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 489 MRCFLKAVGALEMDDVgTTIMQPVSVDDFDDYLLKYIGYNHKLaLLLDYDGTLAPIAPHPDLATLSPEIKNVLYKLSNHS 568
Cdd:PRK14501 453 ASDFLDELREAAEKNK-AFASKPITPAAAEEIIARYRAASRRL-LLLDYDGTLVPFAPDPELAVPDKELRDLLRRLAADP 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 569 DVYVAVISGRNVDNVKKMVGIEGITYAGNHGLEILHPDGSkFVHPMPMEYEKKVSdLLKALQDSVCR-DGAWVENKGALL 647
Cdd:PRK14501 531 NTDVAIISGRDRDTLERWFGDLPIHLVAEHGAWSRAPGGE-WQLLEPVATEWKDA-VRPILEEFVDRtPGSFIEEKEASL 608
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 648 TFHYRET-PN--HLRGA-MVDKARSLIEKYGFKATEAHCALEARPPVqWNKGRASIYILrtsfgvdwnERIK---IIYVG 720
Cdd:PRK14501 609 AWHYRNAdPElgEARANeLILALSSLLSNAPLEVLRGNKVVEVRPAG-VNKGRAVRRLL---------EAGPydfVLAIG 678
|
730 740 750 760
....*....|....*....|....*....|....*....|....*.
gi 19920676 721 DDLTDEDAMVALKGMARTFRVTSSdivKTAADHRLPSTDSVYTLLK 766
Cdd:PRK14501 679 DDTTDEDMFRALPETAITVKVGPG---ESRARYRLPSQREVRELLR 721
|
|
| OtsA |
COG0380 |
Trehalose-6-phosphate synthase, GT20 family [Carbohydrate transport and metabolism]; |
17-500 |
0e+00 |
|
Trehalose-6-phosphate synthase, GT20 family [Carbohydrate transport and metabolism];
Pssm-ID: 440149 Cd Length: 474 Bit Score: 627.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 17 KASLIVVSNRLPFVLIRDPktDELERRASAGGLVTAVCPVVIKGSGLWVGWSGIHLKDPneaipESNPNDQTPTAGLKSE 96
Cdd:COG0380 1 GSRLVVVSNRLPVPHVRED--GSIRVKRSAGGLVTALEPVLRRRGGLWVGWSGGDADRE-----AVEEPRGPVPPDLGGY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 97 QVVSVNIDSKIFDSYYNGCCNKIFWPLFHSMPGRANFGGEHWHDYVTVNKHFAvrtiEALEKCLAKNqgsekspPIVWIH 176
Cdd:COG0380 74 TLAPVDLSAEEVDGYYEGFSNETLWPLFHYRLDLPEFDREDWEAYRRVNRRFA----EALAEEAEPD-------DVVWVH 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 177 DYHLMLAANWVREHaeeknLP-CRLAFFLHIPFPPWDIFRLLPWSDEILQGMLGCDLVGFHIQDYCLNFVDCCQRNLGCR 255
Cdd:COG0380 143 DYHLLLVPAMLREL-----GPdARIGFFLHIPFPPPEIFRILPWREEILEGLLGADLIGFQTPRDARNFLDCVRRLLGAE 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 256 VDRNNLlVEHGGRTVRVRPLPIGIPYERFVNLATTAPKVLKTSKM-------QIILGVDRLDYTKGLVHRLMAFEALLLK 328
Cdd:COG0380 218 VDEGGT-VRYGGRTVRVGAFPIGIDVEEFAELARSPEVRARAERLreelggrKLILGVDRLDYTKGIPERLRAFERLLER 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 329 YPQHKEKVSLLQISVPSRTDVKEYRELKEEVDQLVGRINGRFTTANWAPIRYIYDYVSQDELAALYRDAAVCLVTPLRDG 408
Cdd:COG0380 297 HPELRGKVTLLQIAVPSREDVPAYRELRREIEELVGRINGRFGTLDWTPIRYLNRSLPREELAALYRAADVALVTPLRDG 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 409 MNLVAKEFVACQINEvPGVLVISPFAGAGEMMHEALLCNPYEVNEAAEVIHRALTMPEDERVLRMARLRRREAECDVSHW 488
Cdd:COG0380 377 MNLVAKEYVAAQPDD-PGVLVLSEFAGAAEELTEALLVNPYDIDGMAEAIHRALTMPLEERRRRMRALRERVRRYDVHRW 455
|
490
....*....|..
gi 19920676 489 MRCFLKAVGALE 500
Cdd:COG0380 456 ADDFLDALAAVR 467
|
|
| GT20_TPS |
cd03788 |
trehalose-6-phosphate synthase; Trehalose-6-Phosphate Synthase (TPS, EC 2.4.1.15) is a ... |
19-495 |
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: 616.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 19 SLIVVSNRLPFVLIRDPKTdELERRASAGGLVTAVCPVVIKGSGLWVGWSGIHLKDPNEAipesnpnDQTPTAGLKSEQV 98
Cdd:cd03788 1 RLIVVSNRLPVTLERDDDG-EVEFRRSAGGLVTALKGLLKSTGGLWVGWPGIEADEEESD-------QVVSPELLEEYNV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 99 VSVNIDSKIFDSYYNGCCNKIFWPLFHSMPGR--ANFGGEHWHDYVTVNKHFAVRTIEALEKclaknqgseksPPIVWIH 176
Cdd:cd03788 73 VPVFLSDEDFEGYYNGFSNSVLWPLFHYLLPLpdGRFEREWWEAYVRVNQAFADAVVEVYRP-----------GDLIWVH 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 177 DYHLMLAANWVREhaeeKNLPCRLAFFLHIPFPPWDIFRLLPWSDEILQGMLGCDLVGFHIQDYCLNFVDCCQRNLGCRV 256
Cdd:cd03788 142 DYHLLLLPQMLRE----RLPDARIGFFLHIPFPSSEIFRCLPWREEILRGLLGADLIGFQTFEYARHFLSCCSRLLGLET 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 257 DRNNLlVEHGGRTVRVRPLPIGIPYERFVNLATTAPKVLKTSK-------MQIILGVDRLDYTKGLVHRLMAFEALLLKY 329
Cdd:cd03788 218 TSAGG-VEYGGRRVRVGAFPIGIDPDRFRRLAASPEVQERARElrerykgKKLIVGVDRLDYTKGIPEKLLAFERFLERY 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 330 PQHKEKVSLLQISVPSRTDVKEYRELKEEVDQLVGRINGRFTTANWAPIRYIYDYVSQDELAALYRDAAVCLVTPLRDGM 409
Cdd:cd03788 297 PEWRGKVVLVQVAVPSRTDVEEYQELRREVEELVGRINGRFGTLDWTPVVYLHQSLDREELLALYRAADVALVTSLRDGM 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 410 NLVAKEFVACQiNEVPGVLVISPFAGAGEMMHEALLCNPYEVNEAAEVIHRALTMPEDERVLRMARLRRREAECDVSHWM 489
Cdd:cd03788 377 NLVAKEYVACQ-RDNPGVLILSEFAGAASELDGAILVNPWDIEEVAEAINRALTMSPEERKERHQKLRKYVETHDVQAWA 455
|
....*.
gi 19920676 490 RCFLKA 495
Cdd:cd03788 456 NSFLDD 461
|
|
| trehalose_OtsA |
TIGR02400 |
alpha,alpha-trehalose-phosphate synthase [UDP-forming]; This enzyme catalyzes the key, ... |
20-495 |
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: 529.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 20 LIVVSNRLPFVLIRDpktdelERRASAGGLVTAVCPVVIKGSGLWVGWSGihlkdpnEAIPESNPNDQTPTAGLKSEQVV 99
Cdd:TIGR02400 2 LIVVSNRLPVPITRG------GLEPSAGGLAVALLGALKATGGVWFGWSG-------KTVEEDEGEPFLRTELEGKITLA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 100 SVNIDSKIFDSYYNGCCNKIFWPLFHSMPGRANFGGEHWHDYVTVNKHFAvrtiEALEKCLAKNQgseksppIVWIHDYH 179
Cdd:TIGR02400 69 PVFLSEEDVDGYYNGFSNSTLWPLFHYRPDLIRYDRKAWEAYRRVNRLFA----EALAPLLQPGD-------IVWVHDYH 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 180 LMLAANWVREhaeeKNLPCRLAFFLHIPFPPWDIFRLLPWSDEILQGMLGCDLVGFHIQDYCLNFVDCCQRNLGCRVDRN 259
Cdd:TIGR02400 138 LMLLPAMLRE----LGVQNKIGFFLHIPFPSSEIYRTLPWRRELLEGLLAYDLVGFQTYDDARNFLSAVSRELGLETLPN 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 260 NllVEHGGRTVRVRPLPIGIPYERFVNLA---TTAPKVLKTSKM----QIILGVDRLDYTKGLVHRLMAFEALLLKYPQH 332
Cdd:TIGR02400 214 G--VESGGRTVRVGAFPIGIDVDRFAEQAkkpSVQKRIAELRESlkgrKLIIGVDRLDYSKGLPERLLAFERFLEEHPEW 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 333 KEKVSLLQISVPSRTDVKEYRELKEEVDQLVGRINGRFTTANWAPIRYIYDYVSQDELAALYRDAAVCLVTPLRDGMNLV 412
Cdd:TIGR02400 292 RGKVVLVQIAVPSRGDVPEYQQLRRQVEELVGRINGRFGTLDWTPIRYLNRSYDREELMALYRAADVGLVTPLRDGMNLV 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 413 AKEFVACQiNEVPGVLVISPFAGAGEMMHEALLCNPYEVNEAAEVIHRALTMPEDERVLRMARLRRREAECDVSHWMRCF 492
Cdd:TIGR02400 372 AKEYVAAQ-DPKDGVLILSEFAGAAQELNGALLVNPYDIDGMADAIARALTMPLEEREERHRAMMDKLRKNDVQRWREDF 450
|
...
gi 19920676 493 LKA 495
Cdd:TIGR02400 451 LSD 453
|
|
| Glyco_transf_20 |
pfam00982 |
Glycosyltransferase family 20; Members of this family belong to glycosyl transferase family 20. ... |
19-494 |
2.78e-165 |
|
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: 487.17 E-value: 2.78e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 19 SLIVVSNRLPFVLIRDPKTDELERR--ASAGGLVTAVCPVVIKGSGLWVGWSGIHlkdpneaIPESNPNDQTpTAGLKSE 96
Cdd:pfam00982 2 RLVVVSNRLPVTAVRDEEDGKWEFSikMSSGGLVSALNGLSAATEGVWVGWPGVP-------VDESEPKDKV-SQSLKEK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 97 -QVVSVNIDSKIFDSYYNGCCNKIFWPLFHSMPGRAN---FGGEHWHDYVTVNKHFAVRTIEALEKclaknqGSeksppI 172
Cdd:pfam00982 74 fNCVPVFLSDELFDSYYNGFSNSILWPLFHYMIPPNNedaFDRSWWDAYVKVNKLFADKIVEVYKD------GD-----L 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 173 VWIHDYHLMLAANWVREhaeeKNLPCRLAFFLHIPFPPWDIFRLLPWSDEILQGMLGCDLVGFHIQDYCLNFVDCCQRNL 252
Cdd:pfam00982 143 IWIHDYHLMLLPQMLRK----RLPDAKIGFFLHTPFPSSEIFRCLPVREEILEGLLGADLIGFHTYDYARHFLSCCSRLL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 253 GCRVdRNNLLVEHGGRTVRVRPLPIGIPYERF---VNLATTAPKV--LKT---SKMQIILGVDRLDYTKGLVHRLMAFEA 324
Cdd:pfam00982 219 GLET-RSDGGVEYGGRTVSVKAFPIGIDPGRIesgLASPSVQEKIkeLKErfgNKKKLIVGVDRLDYIKGIPQKLLAFER 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 325 LLLKYPQHKEKVSLLQISVPSRTDVKEYRELKEEVDQLVGRINGRFTTANWAPIRYIYDYVSQDELAALYRDAAVCLVTP 404
Cdd:pfam00982 298 FLEEYPEWRGKVVLVQIAVPSRGDVEEYQNLRSQIEELVGRINGEFGTLDYTPVHFLHRPLDFDELIALYAVADVCLVTS 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 405 LRDGMNLVAKEFVACQiNEVPGVLVISPFAGAGEMMHE-ALLCNPYEVNEAAEVIHRALTMPEDERVLRMARLRRREAEC 483
Cdd:pfam00982 378 LRDGMNLVAYEYVACQ-QGRKGVLILSEFAGAAQSLNDgAILVNPWDIDEVAEAINEALTMSEEERKKRHKKLYKYISKH 456
|
490
....*....|.
gi 19920676 484 DVSHWMRCFLK 494
Cdd:pfam00982 457 DSQHWAESFLS 467
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK14501 |
PRK14501 |
putative bifunctional trehalose-6-phosphate synthase/HAD hydrolase subfamily IIB; Provisional |
20-766 |
0e+00 |
|
putative bifunctional trehalose-6-phosphate synthase/HAD hydrolase subfamily IIB; Provisional
Pssm-ID: 184712 [Multi-domain] Cd Length: 726 Bit Score: 641.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 20 LIVVSNRLPFVLIRDPKTDELERraSAGGLVTAVCPVVIKGSGLWVGWSGIHLkdpnEAIPESNPNDQTPTagLKSEQVV 99
Cdd:PRK14501 3 LIIVSNRLPVTVVREDGGVELTP--SVGGLATGLRSFHERGGGLWVGWPGLDL----EEESEEQRARIEPR--LEELGLV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 100 SVNIDSKIFDSYYNGCCNKIFWPLFHSMPGRANFGGEHWHDYVTVNKHFA---VRTIEAlekclaknqGSeksppIVWIH 176
Cdd:PRK14501 75 PVFLSAEEVDRYYEGFCNSTLWPLFHYFPEYTEFEDRFWESYERVNQRFAeaiAAIARP---------GD-----VVWVH 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 177 DYHLMLAANWVREHAEEKnlpcRLAFFLHIPFPPWDIFRLLPWSDEILQGMLGCDLVGFHIQDYCLNFVDCCQRNLGCRV 256
Cdd:PRK14501 141 DYQLMLLPAMLRERLPDA----RIGFFLHIPFPSFEVFRLLPWREEILEGLLGADLIGFHTYDYVRHFLSSVLRVLGYET 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 257 DRNNllVEHGGRTVRVRPLPIGIPYERFVNLATTaPKV--------LKTSKMQIILGVDRLDYTKGLVHRLMAFEALLLK 328
Cdd:PRK14501 217 ELGE--IRLGGRIVRVDAFPMGIDYDKFHNSAQD-PEVqeeirrlrQDLRGRKIILSIDRLDYTKGIPRRLLAFERFLEK 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 329 YPQHKEKVSLLQISVPSRTDVKEYRELKEEVDQLVGRINGRFTTANWAPIRYIYDYVSQDELAALYRDAAVCLVTPLRDG 408
Cdd:PRK14501 294 NPEWRGKVRLVQVAVPSRTGVPQYQEMKREIDELVGRINGEFGTVDWTPIHYFYRSLPFEELVALYRAADVALVTPLRDG 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 409 MNLVAKEFVACQINEvPGVLVISPFAGAGEMMHEALLCNPYEVNEAAEVIHRALTMPEDERVLRMARLRRREAECDVSHW 488
Cdd:PRK14501 374 MNLVAKEYVASRTDG-DGVLILSEMAGAAAELAEALLVNPNDIEGIAAAIKRALEMPEEEQRERMQAMQERLRRYDVHKW 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 489 MRCFLKAVGALEMDDVgTTIMQPVSVDDFDDYLLKYIGYNHKLaLLLDYDGTLAPIAPHPDLATLSPEIKNVLYKLSNHS 568
Cdd:PRK14501 453 ASDFLDELREAAEKNK-AFASKPITPAAAEEIIARYRAASRRL-LLLDYDGTLVPFAPDPELAVPDKELRDLLRRLAADP 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 569 DVYVAVISGRNVDNVKKMVGIEGITYAGNHGLEILHPDGSkFVHPMPMEYEKKVSdLLKALQDSVCR-DGAWVENKGALL 647
Cdd:PRK14501 531 NTDVAIISGRDRDTLERWFGDLPIHLVAEHGAWSRAPGGE-WQLLEPVATEWKDA-VRPILEEFVDRtPGSFIEEKEASL 608
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 648 TFHYRET-PN--HLRGA-MVDKARSLIEKYGFKATEAHCALEARPPVqWNKGRASIYILrtsfgvdwnERIK---IIYVG 720
Cdd:PRK14501 609 AWHYRNAdPElgEARANeLILALSSLLSNAPLEVLRGNKVVEVRPAG-VNKGRAVRRLL---------EAGPydfVLAIG 678
|
730 740 750 760
....*....|....*....|....*....|....*....|....*.
gi 19920676 721 DDLTDEDAMVALKGMARTFRVTSSdivKTAADHRLPSTDSVYTLLK 766
Cdd:PRK14501 679 DDTTDEDMFRALPETAITVKVGPG---ESRARYRLPSQREVRELLR 721
|
|
| OtsA |
COG0380 |
Trehalose-6-phosphate synthase, GT20 family [Carbohydrate transport and metabolism]; |
17-500 |
0e+00 |
|
Trehalose-6-phosphate synthase, GT20 family [Carbohydrate transport and metabolism];
Pssm-ID: 440149 Cd Length: 474 Bit Score: 627.53 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 17 KASLIVVSNRLPFVLIRDPktDELERRASAGGLVTAVCPVVIKGSGLWVGWSGIHLKDPneaipESNPNDQTPTAGLKSE 96
Cdd:COG0380 1 GSRLVVVSNRLPVPHVRED--GSIRVKRSAGGLVTALEPVLRRRGGLWVGWSGGDADRE-----AVEEPRGPVPPDLGGY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 97 QVVSVNIDSKIFDSYYNGCCNKIFWPLFHSMPGRANFGGEHWHDYVTVNKHFAvrtiEALEKCLAKNqgsekspPIVWIH 176
Cdd:COG0380 74 TLAPVDLSAEEVDGYYEGFSNETLWPLFHYRLDLPEFDREDWEAYRRVNRRFA----EALAEEAEPD-------DVVWVH 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 177 DYHLMLAANWVREHaeeknLP-CRLAFFLHIPFPPWDIFRLLPWSDEILQGMLGCDLVGFHIQDYCLNFVDCCQRNLGCR 255
Cdd:COG0380 143 DYHLLLVPAMLREL-----GPdARIGFFLHIPFPPPEIFRILPWREEILEGLLGADLIGFQTPRDARNFLDCVRRLLGAE 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 256 VDRNNLlVEHGGRTVRVRPLPIGIPYERFVNLATTAPKVLKTSKM-------QIILGVDRLDYTKGLVHRLMAFEALLLK 328
Cdd:COG0380 218 VDEGGT-VRYGGRTVRVGAFPIGIDVEEFAELARSPEVRARAERLreelggrKLILGVDRLDYTKGIPERLRAFERLLER 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 329 YPQHKEKVSLLQISVPSRTDVKEYRELKEEVDQLVGRINGRFTTANWAPIRYIYDYVSQDELAALYRDAAVCLVTPLRDG 408
Cdd:COG0380 297 HPELRGKVTLLQIAVPSREDVPAYRELRREIEELVGRINGRFGTLDWTPIRYLNRSLPREELAALYRAADVALVTPLRDG 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 409 MNLVAKEFVACQINEvPGVLVISPFAGAGEMMHEALLCNPYEVNEAAEVIHRALTMPEDERVLRMARLRRREAECDVSHW 488
Cdd:COG0380 377 MNLVAKEYVAAQPDD-PGVLVLSEFAGAAEELTEALLVNPYDIDGMAEAIHRALTMPLEERRRRMRALRERVRRYDVHRW 455
|
490
....*....|..
gi 19920676 489 MRCFLKAVGALE 500
Cdd:COG0380 456 ADDFLDALAAVR 467
|
|
| GT20_TPS |
cd03788 |
trehalose-6-phosphate synthase; Trehalose-6-Phosphate Synthase (TPS, EC 2.4.1.15) is a ... |
19-495 |
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: 616.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 19 SLIVVSNRLPFVLIRDPKTdELERRASAGGLVTAVCPVVIKGSGLWVGWSGIHLKDPNEAipesnpnDQTPTAGLKSEQV 98
Cdd:cd03788 1 RLIVVSNRLPVTLERDDDG-EVEFRRSAGGLVTALKGLLKSTGGLWVGWPGIEADEEESD-------QVVSPELLEEYNV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 99 VSVNIDSKIFDSYYNGCCNKIFWPLFHSMPGR--ANFGGEHWHDYVTVNKHFAVRTIEALEKclaknqgseksPPIVWIH 176
Cdd:cd03788 73 VPVFLSDEDFEGYYNGFSNSVLWPLFHYLLPLpdGRFEREWWEAYVRVNQAFADAVVEVYRP-----------GDLIWVH 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 177 DYHLMLAANWVREhaeeKNLPCRLAFFLHIPFPPWDIFRLLPWSDEILQGMLGCDLVGFHIQDYCLNFVDCCQRNLGCRV 256
Cdd:cd03788 142 DYHLLLLPQMLRE----RLPDARIGFFLHIPFPSSEIFRCLPWREEILRGLLGADLIGFQTFEYARHFLSCCSRLLGLET 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 257 DRNNLlVEHGGRTVRVRPLPIGIPYERFVNLATTAPKVLKTSK-------MQIILGVDRLDYTKGLVHRLMAFEALLLKY 329
Cdd:cd03788 218 TSAGG-VEYGGRRVRVGAFPIGIDPDRFRRLAASPEVQERARElrerykgKKLIVGVDRLDYTKGIPEKLLAFERFLERY 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 330 PQHKEKVSLLQISVPSRTDVKEYRELKEEVDQLVGRINGRFTTANWAPIRYIYDYVSQDELAALYRDAAVCLVTPLRDGM 409
Cdd:cd03788 297 PEWRGKVVLVQVAVPSRTDVEEYQELRREVEELVGRINGRFGTLDWTPVVYLHQSLDREELLALYRAADVALVTSLRDGM 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 410 NLVAKEFVACQiNEVPGVLVISPFAGAGEMMHEALLCNPYEVNEAAEVIHRALTMPEDERVLRMARLRRREAECDVSHWM 489
Cdd:cd03788 377 NLVAKEYVACQ-RDNPGVLILSEFAGAASELDGAILVNPWDIEEVAEAINRALTMSPEERKERHQKLRKYVETHDVQAWA 455
|
....*.
gi 19920676 490 RCFLKA 495
Cdd:cd03788 456 NSFLDD 461
|
|
| trehalose_OtsA |
TIGR02400 |
alpha,alpha-trehalose-phosphate synthase [UDP-forming]; This enzyme catalyzes the key, ... |
20-495 |
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: 529.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 20 LIVVSNRLPFVLIRDpktdelERRASAGGLVTAVCPVVIKGSGLWVGWSGihlkdpnEAIPESNPNDQTPTAGLKSEQVV 99
Cdd:TIGR02400 2 LIVVSNRLPVPITRG------GLEPSAGGLAVALLGALKATGGVWFGWSG-------KTVEEDEGEPFLRTELEGKITLA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 100 SVNIDSKIFDSYYNGCCNKIFWPLFHSMPGRANFGGEHWHDYVTVNKHFAvrtiEALEKCLAKNQgseksppIVWIHDYH 179
Cdd:TIGR02400 69 PVFLSEEDVDGYYNGFSNSTLWPLFHYRPDLIRYDRKAWEAYRRVNRLFA----EALAPLLQPGD-------IVWVHDYH 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 180 LMLAANWVREhaeeKNLPCRLAFFLHIPFPPWDIFRLLPWSDEILQGMLGCDLVGFHIQDYCLNFVDCCQRNLGCRVDRN 259
Cdd:TIGR02400 138 LMLLPAMLRE----LGVQNKIGFFLHIPFPSSEIYRTLPWRRELLEGLLAYDLVGFQTYDDARNFLSAVSRELGLETLPN 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 260 NllVEHGGRTVRVRPLPIGIPYERFVNLA---TTAPKVLKTSKM----QIILGVDRLDYTKGLVHRLMAFEALLLKYPQH 332
Cdd:TIGR02400 214 G--VESGGRTVRVGAFPIGIDVDRFAEQAkkpSVQKRIAELRESlkgrKLIIGVDRLDYSKGLPERLLAFERFLEEHPEW 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 333 KEKVSLLQISVPSRTDVKEYRELKEEVDQLVGRINGRFTTANWAPIRYIYDYVSQDELAALYRDAAVCLVTPLRDGMNLV 412
Cdd:TIGR02400 292 RGKVVLVQIAVPSRGDVPEYQQLRRQVEELVGRINGRFGTLDWTPIRYLNRSYDREELMALYRAADVGLVTPLRDGMNLV 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 413 AKEFVACQiNEVPGVLVISPFAGAGEMMHEALLCNPYEVNEAAEVIHRALTMPEDERVLRMARLRRREAECDVSHWMRCF 492
Cdd:TIGR02400 372 AKEYVAAQ-DPKDGVLILSEFAGAAQELNGALLVNPYDIDGMADAIARALTMPLEEREERHRAMMDKLRKNDVQRWREDF 450
|
...
gi 19920676 493 LKA 495
Cdd:TIGR02400 451 LSD 453
|
|
| Glyco_transf_20 |
pfam00982 |
Glycosyltransferase family 20; Members of this family belong to glycosyl transferase family 20. ... |
19-494 |
2.78e-165 |
|
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: 487.17 E-value: 2.78e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 19 SLIVVSNRLPFVLIRDPKTDELERR--ASAGGLVTAVCPVVIKGSGLWVGWSGIHlkdpneaIPESNPNDQTpTAGLKSE 96
Cdd:pfam00982 2 RLVVVSNRLPVTAVRDEEDGKWEFSikMSSGGLVSALNGLSAATEGVWVGWPGVP-------VDESEPKDKV-SQSLKEK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 97 -QVVSVNIDSKIFDSYYNGCCNKIFWPLFHSMPGRAN---FGGEHWHDYVTVNKHFAVRTIEALEKclaknqGSeksppI 172
Cdd:pfam00982 74 fNCVPVFLSDELFDSYYNGFSNSILWPLFHYMIPPNNedaFDRSWWDAYVKVNKLFADKIVEVYKD------GD-----L 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 173 VWIHDYHLMLAANWVREhaeeKNLPCRLAFFLHIPFPPWDIFRLLPWSDEILQGMLGCDLVGFHIQDYCLNFVDCCQRNL 252
Cdd:pfam00982 143 IWIHDYHLMLLPQMLRK----RLPDAKIGFFLHTPFPSSEIFRCLPVREEILEGLLGADLIGFHTYDYARHFLSCCSRLL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 253 GCRVdRNNLLVEHGGRTVRVRPLPIGIPYERF---VNLATTAPKV--LKT---SKMQIILGVDRLDYTKGLVHRLMAFEA 324
Cdd:pfam00982 219 GLET-RSDGGVEYGGRTVSVKAFPIGIDPGRIesgLASPSVQEKIkeLKErfgNKKKLIVGVDRLDYIKGIPQKLLAFER 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 325 LLLKYPQHKEKVSLLQISVPSRTDVKEYRELKEEVDQLVGRINGRFTTANWAPIRYIYDYVSQDELAALYRDAAVCLVTP 404
Cdd:pfam00982 298 FLEEYPEWRGKVVLVQIAVPSRGDVEEYQNLRSQIEELVGRINGEFGTLDYTPVHFLHRPLDFDELIALYAVADVCLVTS 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 405 LRDGMNLVAKEFVACQiNEVPGVLVISPFAGAGEMMHE-ALLCNPYEVNEAAEVIHRALTMPEDERVLRMARLRRREAEC 483
Cdd:pfam00982 378 LRDGMNLVAYEYVACQ-QGRKGVLILSEFAGAAQSLNDgAILVNPWDIDEVAEAINEALTMSEEERKKRHKKLYKYISKH 456
|
490
....*....|.
gi 19920676 484 DVSHWMRCFLK 494
Cdd:pfam00982 457 DSQHWAESFLS 467
|
|
| PLN03064 |
PLN03064 |
alpha,alpha-trehalose-phosphate synthase (UDP-forming); Provisional |
12-615 |
1.12e-109 |
|
alpha,alpha-trehalose-phosphate synthase (UDP-forming); Provisional
Pssm-ID: 215556 [Multi-domain] Cd Length: 934 Bit Score: 357.18 E-value: 1.12e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 12 GEPSTKASLIVVSNRLPFVLIRDPKTD-ELErrASAGGLVTAVCPVViKGSGLWVGWSGIHLKDpneaipesNPNDQTPT 90
Cdd:PLN03064 88 GRRPLRQRLLVVANRLPVSAVRRGEDSwSLE--ISAGGLVSALLGVK-EFEARWIGWAGVNVPD--------EVGQKALT 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 91 AGLKSEQVVSVNIDSKIFDSYYNGCCNKIFWPLFHSMPGRA--------NFGGEhWHDYVTVNKHFAVRTIEALEKclak 162
Cdd:PLN03064 157 KALAEKRCIPVFLDEEIVHQYYNGYCNNILWPLFHYLGLPQedrlattrSFQSQ-FAAYKKANQMFADVVNEHYEE---- 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 163 nqGSeksppIVWIHDYHLMLAANWVREHaeekNLPCRLAFFLHIPFPPWDIFRLLPWSDEILQGMLGCDLVGFHIQDYCL 242
Cdd:PLN03064 232 --GD-----VVWCHDYHLMFLPKCLKEY----NSNMKVGWFLHTPFPSSEIHRTLPSRSELLRSVLAADLVGFHTYDYAR 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 243 NFVDCCQRNLGCRVDRNNllVEHGGRTVRVRPLPIGIPYERFVNlATTAPKV------LKT--SKMQIILGVDRLDYTKG 314
Cdd:PLN03064 301 HFVSACTRILGLEGTPEG--VEDQGRLTRVAAFPIGIDSDRFIR-ALETPQVqqhikeLKErfAGRKVMLGVDRLDMIKG 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 315 LVHRLMAFEALLLKYPQHKEKVSLLQISVPSRTDVKEYRELKEEVDQLVGRINGRFTTANWAPIRYIYDYVSQDELAALY 394
Cdd:PLN03064 378 IPQKILAFEKFLEENPEWRDKVVLLQIAVPTRTDVPEYQKLTSQVHEIVGRINGRFGTLTAVPIHHLDRSLDFHALCALY 457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 395 RDAAVCLVTPLRDGMNLVAKEFVACQiNEVPGVLVISPFAGAGEMMHE-ALLCNPYEVNEAAEVIHRALTMPEDERVLRm 473
Cdd:PLN03064 458 AVTDVALVTSLRDGMNLVSYEFVACQ-DSKKGVLILSEFAGAAQSLGAgAILVNPWNITEVAASIAQALNMPEEEREKR- 535
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 474 arlRRREAECDVSH----WMRCFLKavgalEMDDvgtTIMQ--------PVSVDDfDDYLLKYIGYNHKLaLLLDYDGTL 541
Cdd:PLN03064 536 ---HRHNFMHVTTHtaqeWAETFVS-----ELND---TVVEaqlrtrqvPPQLPP-EDAIQRYLQSNNRL-LILGFNATL 602
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 542 APIAPHPDL---------ATLSPEIKNVLYKLSNHSDVYVAVISGRNVDNVKKMVGIEGITYAGNHGLEILHPDGsKFVH 612
Cdd:PLN03064 603 TEPVDTPGRrgdqikemeLRLHPELKEPLRALCSDPKTTIVVLSGSDRSVLDENFGEFDMWLAAENGMFLRHTKG-EWMT 681
|
...
gi 19920676 613 PMP 615
Cdd:PLN03064 682 TMP 684
|
|
| PLN03063 |
PLN03063 |
alpha,alpha-trehalose-phosphate synthase (UDP-forming); Provisional |
20-652 |
1.63e-109 |
|
alpha,alpha-trehalose-phosphate synthase (UDP-forming); Provisional
Pssm-ID: 215555 [Multi-domain] Cd Length: 797 Bit Score: 353.02 E-value: 1.63e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 20 LIVVSNRLPFVLIRDPKtDELERRASAGGLVTAVCPVVIKGSGlWVGWSGIHLKDPNEAipesnpndQTPTAGLKSEQVV 99
Cdd:PLN03063 13 LLVVANRLPVSAKRTGE-DSWSLEMSPGGLVSALLGVKEFETK-WIGWPGVDVHDEIGK--------AALTESLAEKGCI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 100 SVNIDSkIFDSYYNGCCNKIFWPLFHSMpgraNFGGEHWHD-----------YVTVNKHFAVRTIEALEkclaknQGSek 168
Cdd:PLN03063 83 PVFLNE-VFDQYYNGYCNNILWPIFHYM----GLPQEDRHDatrtfesqydaYKKANRMFLDVVKENYE------EGD-- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 169 sppIVWIHDYHLMLAANWVREHaeekNLPCRLAFFLHIPFPPWDIFRLLPWSDEILQGMLGCDLVGFHIQDYCLNFVDCC 248
Cdd:PLN03063 150 ---VVWCHDYHLMFLPQYLKEY----NNKMKVGWFLHTPFPSSEIYKTLPSRSELLRAVLTADLIGFHTYDFARHFLSAC 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 249 QRNLGcrVDRNNLLVEHGGRTVRVRPLPIGIPYERFVNLATTAPKVLKTSKMQ-------IILGVDRLDYTKGLVHRLMA 321
Cdd:PLN03063 223 TRILG--VEGTHEGVVDQGKVTRVAVFPIGIDPERFINTCELPEVKQHMKELKrffagrkVILGVDRLDMIKGIPQKYLA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 322 FEALLLKYPQHKEKVSLLQISVPSRTDVKEYRELKEEVDQLVGRINGRFTTANWAPIRYIYDYVSQDELAALYRDAAVCL 401
Cdd:PLN03063 301 FEKFLEENPEWRDKVMLVQIAVPTRNDVPEYQKLKSQVHELVGRINGRFGSVSSVPIHHLDCSVDFNYLCALYAITDVML 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 402 VTPLRDGMNLVAKEFVACQINEvPGVLVISPFAGAGEMMHE-ALLCNPYEVNEAAEVIHRALTMPEDERVLR----MARL 476
Cdd:PLN03063 381 VTSLRDGMNLVSYEFVACQKAK-KGVLVLSEFAGAGQSLGAgALLVNPWNITEVSSAIKEALNMSDEERETRhrhnFQYV 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 477 RRREAECDVSHWMRCFLKAVGALEMDDVGTTIMQPVsvddfDDYLLKYIGYNHKLaLLLDYDGTLApiAPHPDLAT---- 552
Cdd:PLN03063 460 KTHSAQKWADDFMSELNDIIVEAELRTRNIPLELPE-----QDVIQQYSKSNNRL-LILGFYGTLT--EPRNSQIKemdl 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 553 -LSPEIKNVLYKLSNHSDVYVAVISGRNVDNVKKMVGIEGITYAGNHGLEILHPDGsKFVHPMP----MEYEKKVSDLLK 627
Cdd:PLN03063 532 gLHPELKETLKALCSDPKTTVVVLSRSGKDILDKNFGEYNIWLAAENGMFLRHTSG-EWVTTMPehmnLDWVDGVKNVFK 610
|
650 660
....*....|....*....|....*
gi 19920676 628 ALQDSVCRdgAWVENKGALLTFHYR 652
Cdd:PLN03063 611 YFTDRTPR--SYVEKSETSLVWNYE 633
|
|
| PRK10117 |
PRK10117 |
trehalose-6-phosphate synthase; Provisional |
20-494 |
1.92e-98 |
|
trehalose-6-phosphate synthase; Provisional
Pssm-ID: 182249 Cd Length: 474 Bit Score: 314.00 E-value: 1.92e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 20 LIVVSNRlpfvlIRDPKtdelERRASAGGLVTAVCPVVIKGSGLWVGWSGihlkdpneaipeSNPNDQTPTAGLKSEQV- 98
Cdd:PRK10117 4 LVVVSNR-----IAPPD----EHKASAGGLAVGILGALKAAGGLWFGWSG------------ETGNEDQPLKKVKKGNIt 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 99 -VSVNIDSKIFDSYYNGCCNKIFWPLFHSMPGRANFGGEHWHDYVTVNKHFAVRTIEALekclaknqgseKSPPIVWIHD 177
Cdd:PRK10117 63 wASFNLSEQDYDEYYNQFSNAVLWPAFHYRLDLVQFQRPAWEGYLRVNALLADKLLPLL-----------KDDDIIWIHD 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 178 YHLMLAANWVREhaeeKNLPCRLAFFLHIPFPPWDIFRLLPWSDEILQGMLGCDLVGFHIQDYCLNFVDCC--QRNLGCR 255
Cdd:PRK10117 132 YHLLPFASELRK----RGVNNRIGFFLHIPFPTPEIFNALPPHDELLEQLCDYDLLGFQTENDRLAFLDCLsnLTRVTTR 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 256 VDRNNllvEHGGRTVRVRPLPIGIPYERFVNLATTA--PKVLKTSK----MQIILGVDRLDYTKGLVHRLMAFEALLLKY 329
Cdd:PRK10117 208 SGKSH---TAWGKAFRTEVYPIGIEPDEIAKQAAGPlpPKLAQLKAelknVQNIFSVERLDYSKGLPERFLAYEALLEKY 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 330 PQHKEKVSLLQISVPSRTDVKEYRELKEEVDQLVGRINGRFTTANWAPIRYIYDYVSQDELAALYRDAAVCLVTPLRDGM 409
Cdd:PRK10117 285 PQHHGKIRYTQIAPTSRGDVQAYQDIRHQLETEAGRINGKYGQLGWTPLYYLNQHFDRKLLMKIFRYSDVGLVTPLRDGM 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 410 NLVAKEFVACQINEVPGVLVISPFAGAGEMMHEALLCNPYEVNEAAEVIHRALTMPEDERVLRMARLRRREAECDVSHWM 489
Cdd:PRK10117 365 NLVAKEYVAAQDPANPGVLVLSQFAGAANELTSALIVNPYDRDEVAAALDRALTMPLAERISRHAEMLDVIVKNDINHWQ 444
|
....*
gi 19920676 490 RCFLK 494
Cdd:PRK10117 445 ECFIS 449
|
|
| PLN02205 |
PLN02205 |
alpha,alpha-trehalose-phosphate synthase [UDP-forming] |
2-727 |
3.83e-81 |
|
alpha,alpha-trehalose-phosphate synthase [UDP-forming]
Pssm-ID: 177855 [Multi-domain] Cd Length: 854 Bit Score: 278.06 E-value: 3.83e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 2 PDTEIIVTNAGEPSTKASLIVVSNRLPfvlIRdpktdeLERRASagglvtavcpvvikGSGLWV-GWSG----IHLKDP- 75
Cdd:PLN02205 44 PSESVCSDPSSSSVPKDRIIIVANQLP---IR------AQRKSD--------------GSKGWIfSWDEnsllLQLKDGl 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 76 -NEAIP---------ESNPNDQTPTAG--LKSEQVVSVNIDSKIFDSYYNGCCNKIFWPLFHSM-PGRANFGGEH----W 138
Cdd:PLN02205 101 gDDEIEviyvgclkeEIHLNEQEEVSQilLETFKCVPTFLPPDLFTRYYHGFCKQQLWPLFHYMlPLSPDLGGRFnrslW 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 139 HDYVTVNKHFAVRTIEALEKclaknqgsekSPPIVWIHDYHLMLAANWVREHAEEknlpCRLAFFLHIPFPPWDIFRLLP 218
Cdd:PLN02205 181 QAYVSVNKIFADRIMEVINP----------EDDFVWIHDYHLMVLPTFLRKRFNR----VKLGFFLHSPFPSSEIYKTLP 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 219 WSDEILQGMLGCDLVGFHIQDYCLNFVDCCQRNLGCRVD--RNNLLVEHGGRTVRVRPLPIGI---PYERFVNLATTAPK 293
Cdd:PLN02205 247 IREELLRALLNSDLIGFHTFDYARHFLSCCSRMLGLSYEskRGYIGLEYYGRTVSIKILPVGIhmgQLQSVLSLPETEAK 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 294 VLKTSKM------QIILGVDRLDYTKGLVHRLMAFEALLLKYPQHKEKVSLLQISVPSRTDVKEYRELKEEVDQLVGRIN 367
Cdd:PLN02205 327 VKELIKQfcdqdrIMLLGVDDMDIFKGISLKLLAMEQLLMQHPEWQGKVVLVQIANPARGKGKDVKEVQAETHSTVKRIN 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 368 GRFTTANWAPIRYIYDYVSQDELAALYRDAAVCLVTPLRDGMNLVAKEFVAC-----QINEVPG---------VLVISPF 433
Cdd:PLN02205 407 ETFGKPGYDPIVLIDAPLKFYERVAYYVVAECCLVTAVRDGMNLIPYEYIISrqgneKLDKLLGlepstpkksMLVVSEF 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 434 AGAGEMMHEALLCNPYEVNEAAEVIHRALTMPEDERVLRMARLRRREAECDVSHWMRCFLKAVGALEMDD-------VGT 506
Cdd:PLN02205 487 IGCSPSLSGAIRVNPWNIDAVADAMDSALEMAEPEKQLRHEKHYRYVSTHDVGYWARSFLQDLERTCRDHsrrrcwgIGF 566
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 507 TI-MQPVSVD-DFDDYLLKYIGYNHK----LALLLDYDGTLAP---IAPHPdlatlSPEIKNVLYKLSNHSDVYVAVISG 577
Cdd:PLN02205 567 GLsFRVVALDpNFRKLSMEHIVSAYKrtttRAILLDYDGTLMPqasIDKSP-----SSKSIDILNTLCRDKNNMVFIVSA 641
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 578 RNVDNVKKMVG-IEGITYAGNHGLeilhpdgskFVHPM-PMEYEKKVSDL---LKALQDSVCR------DGAWVENKGAL 646
Cdd:PLN02205 642 RSRKTLADWFSpCEKLGIAAEHGY---------FLRLKrDVEWETCVPVAdcsWKQIAEPVMQlytettDGSTIEDKETA 712
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 647 LTFHYRETPNHLRGA----MVDKARSLIEKYGFKATEAHCALEARPPvQWNKGRASIYILRTsfgVDWNERIK--IIYVG 720
Cdd:PLN02205 713 LVWCYEDADPDFGSCqakeLLDHLESVLANEPVTVKSGQNIVEVKPQ-GVSKGLVAKRLLSI---MQERGMLPdfVLCIG 788
|
....*..
gi 19920676 721 DDLTDED 727
Cdd:PLN02205 789 DDRSDED 795
|
|
| HAD_TPP |
cd01627 |
trehalose-phosphate phosphatase similar to Escherichia coli trehalose-6-phosphate phosphatase ... |
532-761 |
1.01e-69 |
|
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: 229.10 E-value: 1.01e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 532 ALLLDYDGTLAPIAPHPDLATLSPEIKNVLYKLSNHSDVYVAVISGRNVDNVKKMVGIEGITYAGNHGLEILHPDGSKFV 611
Cdd:cd01627 1 LLFLDYDGTLAPIVPDPDAAVPSPELLEALKKLAADPKNAVAIVSGRDLDDLDKWLGLPGIGLAGEHGAEIRLPGGGEWV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 612 HPMPMEYEKKVSDLLKALQDSVCR-DGAWVENKGALLTFHYRETPNHLRGAMVDKARSLIEKYG--FKATEAHCALEARp 688
Cdd:cd01627 81 TLAPKADLEWKEEVEAIFKYFTERtPGSLVEDKGASLAWHYRNADPEGARAALELALHLASDLLkaLEVVPGKKVVEVR- 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19920676 689 PVQWNKGRASIYILRTSFGvdwnERIKIIYVGDDLTDEDAMVALKG-MARTFRVTSSDivkTAADHRLPSTDSV 761
Cdd:cd01627 160 PVGVNKGEAVERILGELPF----AGDFVLCAGDDVTDEDAFRALNGeGGFSVKVGEGP---TAAKFRLDDPPDV 226
|
|
| OtsB |
COG1877 |
Trehalose-6-phosphate phosphatase [Carbohydrate transport and metabolism]; |
530-767 |
9.54e-66 |
|
Trehalose-6-phosphate phosphatase [Carbohydrate transport and metabolism];
Pssm-ID: 441481 [Multi-domain] Cd Length: 242 Bit Score: 218.91 E-value: 9.54e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 530 KLALLLDYDGTLAPIAPHPDLATLSPEIKNVLYKLSNHSDVYVAVISGRNVDNVKKMVGIEGITYAGNHGLEILHPDGSK 609
Cdd:COG1877 3 RLLLFLDFDGTLAPIVPDPDAARPPPELRELLRRLAARPGGAVAIVSGRDLADLDRLLGPLGLPLAGSHGAERRLPGGEW 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 610 FVHPMPMEYEKKVSDLLKALQDSVCR-DGAWVENKGALLTFHYRETPNHLRGAMVDKARSLIEKYG--FKATEAHCALEA 686
Cdd:COG1877 83 EVLPLAAEAPEWLDALRAALEALAARtPGVLVEDKGASLALHYRQAPPEEAEELRAALRELAARLGpgLEVLPGKKVVEL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 687 RPPvQWNKGRASIYIL-RTSFGVdwneriKIIYVGDDLTDEDAMVALKGMARTFRVTSSDivkTAADHRLPSTDSVYTLL 765
Cdd:COG1877 163 RPA-GVDKGRAVRALLaELPFGR------APVFIGDDVTDEDAFAALPAGGLGIKVGSGP---TAARYRLADPAEVRALL 232
|
..
gi 19920676 766 KW 767
Cdd:COG1877 233 AR 234
|
|
| Trehalose_PPase |
pfam02358 |
Trehalose-phosphatase; This family consist of trehalose-phosphatases EC:3.1.3.12 these enzyme ... |
534-758 |
9.28e-39 |
|
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: 144.01 E-value: 9.28e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 534 LLDYDGTLAPIAPHPDLATLSPEIKNVLYKLSNHSDVYVAVISGRNVDNVKKMVGIEGITYAGNHGLEILHPDGSKFVH- 612
Cdd:pfam02358 1 FLDYDGTLSPIVSDPIAAVPSDRMLSALQDLASDPPNTVAIISGRSRQEEDLFVGVPNLGLAAEHGAFVRLPGGGDWYNq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 613 --PMPMEYEKKVSDLlkaLQDSVCR-DGAWVENKGALLTFHYRETPNHLRGAMVDKA-----RSLIEKYGFKATEAHCAL 684
Cdd:pfam02358 81 aeVEDLPWKKEVAPI---LEYYTERtPGSYVENKKSALSWHYRNADDDFGSFQAKELaehleSVLQDNPPLRVTQGKKVV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19920676 685 EARPPVQWnKGRASIYILRTSfGVDWNERIKIIYVGDDLTDEDAMVALK-----GMARTFRVTSSDIVKTAADHRLPST 758
Cdd:pfam02358 158 EVRPVGVS-KGKAVEFILEEL-GSAGSLPDFPLCIGDDRTDEDMFSVLRptkpsGVGIEVFAVSVGSKPSSASYFLDDP 234
|
|
| T6PP |
TIGR00685 |
trehalose-phosphatase; Trehalose, a neutral disaccharide of two glucose residues, is an ... |
530-770 |
1.28e-36 |
|
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: 138.04 E-value: 1.28e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 530 KLALLLDYDGTLAPIAPHPDLATLSPEIKNVLYKLSNHSDVYVAVISGRNVDNVKKMVGIEGITYAGNHGLEiLHPDGSK 609
Cdd:TIGR00685 3 KRAFFFDYDGTLSEIVPDPDAAVVSDRLLTILQKLAARPHNAIWIISGRKFLEKWLGVKLPGLGLAGEHGCE-MKDNGSC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 610 FVHPMPMEYEKKVSDLLKALQDSVC-RDGAWVENKGALLTFHYRETPNHLRGAM--VDKARSLIEKYGFKATEAHCALEA 686
Cdd:TIGR00685 82 QDWVNLTEKIPSWKVRANELREEITtRPGVFIERKGVALAWHYRQAPVPELARFraKELKEKILSFTDLEVMDGKAVVEL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 687 RPPvQWNKGRASIYILRTSFGVDWNErikiIYVGDDLTDEDAMVALKGMARTFRVTSSDIV----KTAADHRLPSTDSVY 762
Cdd:TIGR00685 162 KPR-FVNKGEIVKRLLWHQPGSGISP----VYLGDDITDEDAFRVVNNQWGNYGFYPVPIGsgskKTVAKFHLTGPQQVL 236
|
....*...
gi 19920676 763 TLLKWVER 770
Cdd:TIGR00685 237 EFLGLLVG 244
|
|
| PLN02151 |
PLN02151 |
trehalose-phosphatase |
510-766 |
1.15e-31 |
|
trehalose-phosphatase
Pssm-ID: 177812 Cd Length: 354 Bit Score: 127.10 E-value: 1.15e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 510 QPVSVDDFDDYLLKYIGynHKLALLLDYDGTLAPIAPHPDLATLSPEIKNVLYKLSNHsdVYVAVISGRNVDNVKKMVGI 589
Cdd:PLN02151 80 HPSALNMFEEILHKSEG--KQIVMFLDYDGTLSPIVDDPDRAFMSKKMRNTVRKLAKC--FPTAIVSGRCREKVSSFVKL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 590 EGITYAGNHGLEILHPD-GSKfvhpmpmeYEKKVSDLL----------------KALQDSVCRDGAWVENKGALLTFHYR 652
Cdd:PLN02151 156 TELYYAGSHGMDIKGPEqGSK--------YKKENQSLLcqpateflpvinevykKLVEKTKSIPGAKVENNKFCASVHFR 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 653 ETPNHLRGAMVDKARSLIEKY-GFKATEAHCALEARPPVQWNKGRASIYILRtSFGVDWNERIKIIYVGDDLTDEDAMVA 731
Cdd:PLN02151 228 CVEENKWSDLANQVRSVLKNYpKLMLTQGRKVLEIRPIIKWDKGKALEFLLE-SLGYANCTDVFPIYIGDDRTDEDAFKI 306
|
250 260 270
....*....|....*....|....*....|....*.
gi 19920676 732 LKGMARTFRVTSSDIVK-TAADHRLPSTDSVYTLLK 766
Cdd:PLN02151 307 LRDKKQGLGILVSKYAKeTNASYSLQEPDEVMEFLE 342
|
|
| PLN02580 |
PLN02580 |
trehalose-phosphatase |
528-764 |
4.92e-28 |
|
trehalose-phosphatase
Pssm-ID: 215317 [Multi-domain] Cd Length: 384 Bit Score: 116.83 E-value: 4.92e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 528 NHKLALLLDYDGTLAPIAPHPDLATLSPEIKNVLYKLSNHsdVYVAVISGRNVDNVKKMVGIEGITYAGNHGLEILHPDG 607
Cdd:PLN02580 117 GKKIALFLDYDGTLSPIVDDPDRALMSDAMRSAVKNVAKY--FPTAIISGRSRDKVYELVGLTELYYAGSHGMDIMGPVR 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 608 SKFV--HPMPMEYEKKVSDLLKALQ---------DSVCR---------DGAWVENKGALLTFHYRETPNHLRGAMVDKAR 667
Cdd:PLN02580 195 ESVSndHPNCIKSTDQQGKEVNLFQpaseflpmiDEVFRslvestkdiKGAKVENHKFCVSVHYRNVDEKNWPLVAQCVH 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 668 SLIEKYG-FKATEAHCALEARPPVQWNKGRASIYILRtSFGVDWNERIKIIYVGDDLTDEDAMVALKGMARTFRVTSSDI 746
Cdd:PLN02580 275 DVLKKYPrLRLTHGRKVLEVRPVIDWNKGKAVEFLLE-SLGLSNCDDVLPIYIGDDRTDEDAFKVLREGNRGYGILVSSV 353
|
250
....*....|....*...
gi 19920676 747 VKtaadhrlpSTDSVYTL 764
Cdd:PLN02580 354 PK--------ESNAFYSL 363
|
|
| PLN03017 |
PLN03017 |
trehalose-phosphatase |
508-775 |
1.39e-27 |
|
trehalose-phosphatase
Pssm-ID: 178591 [Multi-domain] Cd Length: 366 Bit Score: 115.12 E-value: 1.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 508 IMQ-PVSVDDFDDYLLKYIGynHKLALLLDYDGTLAPIAPHPDLATLSPEIKNVLYKLSNHsdVYVAVISGRNVDNVKKM 586
Cdd:PLN03017 90 IMQhPSALEMFEQIMEASRG--KQIVMFLDYDGTLSPIVDDPDKAFMSSKMRRTVKKLAKC--FPTAIVTGRCIDKVYNF 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 587 VGIEGITYAGNHGLEILHP---------DGSKFVHPMPMEYEKKVSDLLKAL-QDSVCRDGAWVENKGALLTFHYRETPN 656
Cdd:PLN03017 166 VKLAELYYAGSHGMDIKGPakgfsrhkrVKQSLLYQPANDYLPMIDEVYRQLlEKTKSTPGAKVENHKFCASVHFRCVDE 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 657 HLRGAMVDKARSLIEKY-GFKATEAHCALEARPPVQWNKGRASIYILRtSFGVDWNERIKIIYVGDDLTDEDAMVALKGM 735
Cdd:PLN03017 246 KKWSELVLQVRSVLKNFpTLKLTQGRKVFEIRPMIEWDKGKALEFLLE-SLGFGNTNNVFPVYIGDDRTDEDAFKMLRDR 324
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 19920676 736 ARTFRVTSSDIVKtaadhrlpSTDSVYTLLKWVE-RHFMGR 775
Cdd:PLN03017 325 GEGFGILVSKFPK--------DTDASYSLQDPSEvMDFLAR 357
|
|
| PRK10187 |
PRK10187 |
trehalose-6-phosphate phosphatase; Provisional |
530-769 |
1.88e-19 |
|
trehalose-6-phosphate phosphatase; Provisional
Pssm-ID: 182291 [Multi-domain] Cd Length: 266 Bit Score: 89.03 E-value: 1.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 530 KLALLLDYDGTLAPIAPHPDLATLSPEIKNVLYKLSNHSDVYVAVISGRNVDNVKKMVGIEGITYAGNHGLEILHPDGSK 609
Cdd:PRK10187 14 NYAWFFDLDGTLAEIKPHPDQVVVPDNILQGLQLLATANDGALALISGRSMVELDALAKPYRFPLAGVHGAERRDINGKT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 610 FVHPMPMEYEKKVSDLLK-ALQDsvcRDGAWVENKGALLTFHYRETPNHlRGAMVDKARSLIEKYGFKATE-AHCALEAR 687
Cdd:PRK10187 94 HIVHLPDAIARDISVQLHtALAQ---LPGAELEAKGMAFALHYRQAPQH-EDALLALAQRITQIWPQLALQpGKCVVEIK 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 688 PPVQwNKGRA-SIYILRTSFGvdwnERIKiIYVGDDLTDE---DAMVALKGMarTFRVTSSDivkTAADHRLPSTDSVYT 763
Cdd:PRK10187 170 PRGT-NKGEAiAAFMQEAPFA----GRTP-VFVGDDLTDEagfAVVNRLGGI--SVKVGTGA---TQASWRLAGVPDVWS 238
|
....*.
gi 19920676 764 llkWVE 769
Cdd:PRK10187 239 ---WLE 241
|
|
| HAD-SF-IIB |
TIGR01484 |
HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid ... |
532-732 |
7.13e-17 |
|
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: 80.12 E-value: 7.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 532 ALLLDYDGTLAPiaphPDLATLSPEIKNVLYKLSNhSDVYVAVISGRNVDNVKKMVGIEG--ITYAGNHGLEILHPDGSK 609
Cdd:TIGR01484 1 LLFFDLDGTLLD----PNAHELSPETIEALERLRE-AGVKVVIVTGRSLAEIKELLKQLNlpLPLIAENGALIFYPGEIL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 610 FVHP--MPMEYE----KKVSDLLKALqdSVCRDGAWVENKGALLTFHYRETPNHLrgAMVDKARSLIEKYGFKATEAHCA 683
Cdd:TIGR01484 76 YIEPsdVFEEILgikfEEIGAELKSL--SEHYVGTFIEDKAIAVAIHYVGAELGQ--ELDSKMRERLEKIGRNDLELEAI 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 19920676 684 LEARP-----PVQWNKGRASIYILRTSFGvdwnERIKIIYVGDDLTDEDAMVAL 732
Cdd:TIGR01484 152 YSGKTdlevlPAGVNKGSALQALLQELNG----KKDEILAFGDSGNDEEMFEVA 201
|
|
| GT4_PimA-like |
cd03801 |
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ... |
128-494 |
8.48e-10 |
|
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: 61.40 E-value: 8.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 128 PGRANFGGEHWHDYVTVNKHFAVRTIEALEKCLAKNQGSEKSPPIVWIHdYHLMLAANWVREHAEEKNLPCRLAFFLHIP 207
Cdd:cd03801 39 PADPGEPPEELEDGVIVPLLPSLAALLRARRLLRELRPLLRLRKFDVVH-AHGLLAALLAALLALLLGAPLVVTLHGAEP 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 208 FPPWDIFR-LLPWSDEILQGMLGCDLVGFHiqdyclnfvdccqrnlgCRVDRNNLLVEHGGRTVRVRPLPIGIPYERFVN 286
Cdd:cd03801 118 GRLLLLLAaERRLLARAEALLRRADAVIAV-----------------SEALRDELRALGGIPPEKIVVIPNGVDLERFSP 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 287 LATTAPKVLKTSKMQIILGvdRLDYTKGLVHRLMAFEALLLKYPQhkekVSLLqISVPSRTDVKEYRELKEEVDQLVgri 366
Cdd:cd03801 181 PLRRKLGIPPDRPVLLFVG--RLSPRKGVDLLLEALAKLLRRGPD----VRLV-IVGGDGPLRAELEELELGLGDRV--- 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 367 ngRFTtanwapiryiyDYVSQDELAALYRDAAVCLVTPLRDGMNLVAKEFVACqinevpGVLVI-SPFAGAGEMMHE--- 442
Cdd:cd03801 251 --RFL-----------GFVPDEELPALYAAADVFVLPSRYEGFGLVVLEAMAA------GLPVVaTDVGGLPEVVEDgeg 311
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 19920676 443 ALLCNPYEVNEAAEVIHRALTMPEDERVLRMARLRRREAECDVSHWMRCFLK 494
Cdd:cd03801 312 GLVVPPDDVEALADALLRLLADPELRARLGRAARERVAERFSWERVAERLLD 363
|
|
| GT4_sucrose_synthase |
cd03800 |
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ... |
302-478 |
5.69e-06 |
|
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: 49.55 E-value: 5.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 302 IILGVDRLDYTKGLVHRLMAFEALllkyPQHKEKVSLLQISVPSRTDVKEYRELKEEVDQLVGRINgrfttanwapiRY- 380
Cdd:cd03800 222 VVLALGRLDPRKGIDTLVRAFAQL----PELRELANLVLVGGPSDDPLSMDREELAELAEELGLID-----------RVr 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 381 IYDYVSQDELAALYRDAAVCLVTPLRDGMNLVAKEFVACqinevpGVLVI-SPFAGAGEMM---HEALLCNPYEVNEAAE 456
Cdd:cd03800 287 FPGRVSRDDLPELYRAADVFVVPSLYEPFGLTAIEAMAC------GTPVVaTAVGGLQDIVrdgRTGLLVDPHDPEALAA 360
|
170 180
....*....|....*....|..
gi 19920676 457 VIHRALTMPEDERVLRMARLRR 478
Cdd:cd03800 361 ALRRLLDDPALWQRLSRAGLER 382
|
|
| RfaB |
COG0438 |
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ... |
390-499 |
1.76e-05 |
|
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440207 [Multi-domain] Cd Length: 123 Bit Score: 44.98 E-value: 1.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 390 LAALYRDAAVCLVTPLRDGMNLVAKEFVACqinevpGVLVI-SPFAGAGEMMHE---ALLCNPYEVNEAAEVIHRALTMP 465
Cdd:COG0438 14 LEALLAAADVFVLPSRSEGFGLVLLEAMAA------GLPVIaTDVGGLPEVIEDgetGLLVPPGDPEALAEAILRLLEDP 87
|
90 100 110
....*....|....*....|....*....|....
gi 19920676 466 EDERVLRMARLRRREAECDVSHWMRCFLKAVGAL 499
Cdd:COG0438 88 ELRRRLGEAARERAEERFSWEAIAERLLALYEEL 121
|
|
| GT4_MtfB-like |
cd03809 |
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ... |
351-482 |
8.02e-05 |
|
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. MtfB (mannosyltransferase B) in E. coli has been shown to direct the growth of the O9-specific polysaccharide chain. It transfers two mannoses into the position 3 of the previously synthesized polysaccharide.
Pssm-ID: 340838 [Multi-domain] Cd Length: 362 Bit Score: 45.82 E-value: 8.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 351 EYRELKEEVDQLVGRINGRFTtanwapiryiyDYVSQDELAALYRDAAvCLVTP-LRDGMNLVAKEFVACQineVPgVLV 429
Cdd:cd03809 235 EDEELLDLVKKLGLGGRVRFL-----------GYVSDEDLPALYRGAR-AFVFPsLYEGFGLPVLEAMACG---TP-VIA 298
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 19920676 430 --ISPFAG-AGEMmheALLCNPYEVNEAAEVIHRALTmpEDERVLRMARLRRREAE 482
Cdd:cd03809 299 snISVLPEvAGDA---ALYFDPLDPESIADAILRLLE--DPSLREELIRKGLERAK 349
|
|
| Cof |
COG0561 |
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ... |
532-630 |
4.71e-04 |
|
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport and metabolism, General function prediction only];
Pssm-ID: 440327 [Multi-domain] Cd Length: 192 Bit Score: 42.04 E-value: 4.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 532 ALLLDYDGTLApiapHPDlATLSPEIKNVLYKLSNHsDVYVAVISGRNVDNVKKMV---GIEG--ITYAGNhglEILHPD 606
Cdd:COG0561 4 LIALDLDGTLL----NDD-GEISPRTKEALRRLREK-GIKVVIATGRPLRSALPLLeelGLDDplITSNGA---LIYDPD 74
|
90 100
....*....|....*....|....*
gi 19920676 607 GSK-FVHPMPMEYEKKVSDLLKALQ 630
Cdd:COG0561 75 GEVlYERPLDPEDVREILELLREHG 99
|
|
| Glycos_transf_1 |
pfam00534 |
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ... |
302-472 |
1.00e-03 |
|
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: 40.34 E-value: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 302 IILGVDRLDYTKGLVHRLMAFEALLLKYPQhkekVSLLQISvpsrtDVKEYRELKEEVDQLVGRINGRFTTanwapiryi 381
Cdd:pfam00534 4 IILFVGRLEPEKGLDLLIKAFALLKEKNPN----LKLVIAG-----DGEEEKRLKKLAEKLGLGDNVIFLG--------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19920676 382 ydYVSQDELAALYRDAAVCLVTPLRDGMNLVAKEFVACqinevpGVLVI-SPFAGAGEMM---HEALLCNPYEVNEAAEV 457
Cdd:pfam00534 66 --FVSDEDLPELLKIADVFVLPSRYEGFGIVLLEAMAC------GLPVIaSDVGGPPEVVkdgETGFLVKPNNAEALAEA 137
|
170
....*....|....*
gi 19920676 458 IHRALTMPEDERVLR 472
Cdd:pfam00534 138 IDKLLEDEELRERLG 152
|
|
| |
