|
Name |
Accession |
Description |
Interval |
E-value |
| COG3459 |
COG3459 |
Cellobiose phosphorylase [Carbohydrate transport and metabolism]; |
2068-2858 |
0e+00 |
|
Cellobiose phosphorylase [Carbohydrate transport and metabolism];
Pssm-ID: 442682 [Multi-domain] Cd Length: 794 Bit Score: 1321.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545295835 2068 NGYGGFSQDGREYQIVlreNALTPAPWSNILANSRFGSVISEAGQAYTWYENAHEYRLTPWENDPVSDRSGEAFYLRDEE 2147
Cdd:COG3459 1 NGYGGFDDDGREYVIT---GPDTPAPWINVLANPDFGFLVSETGGGYSWYKNSRENRLTRWRNDPVSDPPGEYFYLRDEE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545295835 2148 SGECWSPTALPVRG-HGDYLTRHGFGYSVFAHRESGIDSELTVLVAEEEPVKLVLLTLSNSSGRTRQLSVTGYVEWTLGE 2226
Cdd:COG3459 78 TGDYWSPTWQPVRKpLDEYECRHGFGYTRFEHEYNGIESELTYFVPLDDPVEIWRLKLTNTSDRPRRLSVTSYVEWVLGN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545295835 2227 TRTRSAPHIVT-HVARTPGGCGVL-ANNFYGDNGGGRTAFFAVSGNGCSLTGDRREFIGRNGSLHAPSAMKLQKLSGKTG 2304
Cdd:COG3459 158 ARDDTANFQVTlSTGEVDPEGGAIlARNPYNERFNGRVAFFAVSEPVSSFTGDREEFLGRYGSLANPAALERGKLSNSVG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545295835 2305 AGLDPCGAVQSAVTLIDGDQRTFIFILGAEENDVCAQETLARYMNEDTVRQELNRIHNHWHNVLDKIVVNTPDTSVNLLV 2384
Cdd:COG3459 238 AGLDPCAALQVDIELAPGEEKELVFLLGQGENKEEARALIARYRDPDAVDAALAEVKAYWDELLGAVQVETPDPALDLMV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545295835 2385 NGWLLYQTVACRLMARSGYYQSGGAFGFRDQLQDTLALNHAAPDRMREQIILCASRQFIEGDVQHWWHPPHGNGVRTRCS 2464
Cdd:COG3459 318 NGWLLYQTLACRLWARSAFYQSGGAYGFRDQLQDSMALVHARPELAREQILLAASRQFPEGDVQHWWHPPTGRGVRTRFS 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545295835 2465 DDYLWLPLAVCHYVETTGDMDALEIRIPYLEGCPLQPGEESVYDTPVISGTEETLWLHCVKAIHYGL-RFGEHGLPLMGA 2543
Cdd:COG3459 398 DDLLWLPYAVAAYIKETGDFSILDEVVPFLDGPPLPPGEEDAYDLPTVSGEEATLYEHCKRAIDFSLnRLGPHGLPLIGR 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545295835 2544 GDWNDGMNRVGIEGKGESVWLGFFLYDILQRFAALADRRLDESVAAMCRSQALRLQSNLEAHAWDGEWYRRGYFDDGTPL 2623
Cdd:COG3459 478 GDWNDGMNLVGEGGKGESVWLAWFLYYALKEFAPLAEARGDEERAERYRAEAEELREAIEKHAWDGEWYRRAYFDDGTPL 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545295835 2624 GSKTSQDCRIDAIAQSWSVLSGAASPGRCAKAMQALDKHLVDNEGGLIKLLTPPFDGHGPNPGYIQGYLPGVRENGGQYT 2703
Cdd:COG3459 558 GSKENEECKIDLIAQSWAVLSGAADPERARKAMDSVDKYLVTEYGGLILLLTPPFDKYDPDPGYIKGYPPGVRENGGQYT 637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545295835 2704 HGAIWAVMAFARMGNAERAWQLWSMLNPVNHTLNaglVGIYKAEPYVMSADVYSVAPHTGRAGWSWYTGSAGWAWRLLTE 2783
Cdd:COG3459 638 HAAPWAIMAEALLGDGDRAYELYSMINPINHNDE---ADRYKVEPYVYAADVYGVDPHFGRGGWSWYTGSAGWMYRAATE 714
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 545295835 2784 ELLGIKRSGTDFSVHARFPDEWSSFSMAYQYGDSHYQISVSRGDA----EYCVTLDGVLLPDDRIPLKDDGQNHTVEII 2858
Cdd:COG3459 715 YILGIRPEGDGLRIDPCIPSDWPGFSVTRRFRGAVYHITVKNPDGvskgVKSITVDGKPIEGNLIPLVDDGKEHEVEVV 793
|
|
| GH94N_ChvB_NdvB_2_like |
cd11753 |
Second GH94N domain of cyclic beta 1-2 glucan synthetase and similar domains; The glycoside ... |
1525-1860 |
4.78e-166 |
|
Second GH94N domain of cyclic beta 1-2 glucan synthetase and similar domains; The glycoside hydrolase family 94 (previously known as glycosyltransferase family 36) includes cyclic beta 1-2 glucan synthetase (EC:2.4.1.20) or ChvB (encoded by the chromosomal chvB virulence gene). This second of two tandemly repeated GH94-N-terminal-like domains has not been characterized functionally. Some beta 1-2 glucan synthetases are annotated as NdvB (nodule development B) gene products, glycosyltransferases required for the synthesis of cyclic beta-(1,2)-glucans, which play a role in interactions between bacteria and plants.
Pssm-ID: 213069 [Multi-domain] Cd Length: 336 Bit Score: 515.53 E-value: 4.78e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545295835 1525 MTERFMSSTVFRSASLLLQERVPDAVDLYSPRRHFESHEGRV-KPVRYEPRIFYSVDTPAPDIQLLSNGHYHLMLTAGGG 1603
Cdd:cd11753 1 MQRRFHADPRIQAAELLLQERIPREVPIITPRLEELSRPAKKeEEAPEPVRRFTTPDTALPEVHLLSNGRYSVMLTASGS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545295835 1604 GYSRWNDIALTRWRSDTTRDNWGAFCYIRDTQTGDVWSNTWQPTGyTSGQDEEVLFTDAGAEFRRSFGGLSLKTQVVISP 1683
Cdd:cd11753 81 GYSRWNDLAVTRWREDATRDNWGSFIYLRDVDSGKVWSATYQPTR-DPPDEYEVVFSEDRAEFRRRDGGIETTTEVVVSP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545295835 1684 EDDVELRRLTLIHRGRKPRSLELTTYAEVVLAPDASDLAHPAFSNLFIQTELAPERDAILCHRRPCSPDEPAPCLFHMMV 1763
Cdd:cd11753 160 EDDAEIRRVTLTNLSRRPRELEVTSYAEVVLAPPAADEAHPAFSKLFVQTEFLPEQGALLATRRPRSPDEPPPWAAHFVA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545295835 1764 VHGDNRHNVSFETDRARFIGRGRNPANAQAIEAGGMLGNTSGSVLDPILAIRNAIILQPGQPVTIDIIYGISETRQQSLA 1843
Cdd:cd11753 240 VEGEAVGPLQYETDRARFIGRGRSLANPAAMDDGAPLSGTVGAVLDPIFSLRRRVRLPPGETARVTFVTGVADSREEALE 319
|
330
....*....|....*..
gi 545295835 1844 LLEKYRDYPIADRVFEL 1860
Cdd:cd11753 320 LADKYRDPSAVERAFEL 336
|
|
| GH94N_ChvB_NdvB_1_like |
cd11756 |
First GH94N domain of cyclic beta 1-2 glucan synthetase and similar domains; The glycoside ... |
2067-2347 |
6.92e-144 |
|
First GH94N domain of cyclic beta 1-2 glucan synthetase and similar domains; The glycoside hydrolase family 94 (previously known as glycosyltransferase family 36) includes cyclic beta 1-2 glucan synthetase (EC:2.4.1.20) or ChvB (encoded by the chromosomal chvB virulence gene). This first of two tandemly repeated GH94-N-terminal-like domains has not been characterized functionally. Some beta 1-2 glucan synthetases are annotated as NdvB (nodule development B) gene products, glycosyltransferases required for the synthesis of cyclic beta-(1,2)-glucans, which play a role in interactions between bacteria and plants.
Pssm-ID: 213072 [Multi-domain] Cd Length: 284 Bit Score: 449.65 E-value: 6.92e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545295835 2067 FNGYGGFSQDGREYQIVLRENALTPAPWSNILANSRFGSVISEAGQAYTWYENAHEYRLTPWENDPVSDRSGEAFYLRDE 2146
Cdd:cd11756 5 FNGYGGFSPDGREYVIVLGPGKRTPAPWINVIANPGFGFLVSESGSGYTWAENSRENRLTPWSNDPVSDPPGEALYLRDE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545295835 2147 ESGECWSPTALPVRGHGDYLTRHGFGYSVFAHRESGIDSELTVLVAEEEPVKLVLLTLSNSSGRTRQLSVTGYVEWTLGE 2226
Cdd:cd11756 85 ETGEVWSPTPLPIRGGGPYRVRHGFGYSRFEHRSHGIEQELTVFVPRDDPVKISRLRLRNTSGRPRRLSVTYYAEWVLGV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545295835 2227 TRTRSAPHIVTHVARTPGgcGVLANNFYGDNGGGRTAFFAVSGNGCSLTGDRREFIGRNGSLHAPSAMKLQKLSGKTGAG 2306
Cdd:cd11756 165 NREKTAPHIVTEYDEETG--ALLARNPYNEDFGGRVAFLAVSGGPRSFTGDRREFIGRNGSLANPAALKRGRLSGRTGAG 242
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 545295835 2307 LDPCGAVQSAVTLIDGDQRTFIFILGAEENDVCAQETLARY 2347
Cdd:cd11756 243 LDPCAALQVDLELAPGEEKEIVFLLGEADDAEEARALIRRY 283
|
|
| Glyco_hydro_36 |
pfam17167 |
Glycosyl hydrolase 36 superfamily, catalytic domain; This is the catalytic region of the ... |
2363-2789 |
2.19e-136 |
|
Glycosyl hydrolase 36 superfamily, catalytic domain; This is the catalytic region of the superfamily of enzymes referred to as GH36. UniProtKB:Q76IQ9 is a chitobiose phosphorylase that catalyzes the reversible phosphorolysis of chitobiose into alpha-GlcNAc-1-phosphate and GlcNAc with inversion of the anomeric configuration. The full-length enzyme comprises a beta sandwich domain and an (alpha/alpha)(6) barrel domain. The alpha-helical barrel component of the domain, this family, is the catalytic region.
Pssm-ID: 465366 Cd Length: 425 Bit Score: 434.24 E-value: 2.19e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545295835 2363 HWHNVLDKIVVNTPDTSVNLLVNGWLLYQTVACRLMARSG-YYQSGGA--FGFRDQLQDTLALNHAAPDRMREQIILCAS 2439
Cdd:pfam17167 1 YWDSRLEKFQVKTPDESLDTMINIWNLYQCEICFVWSRFAsFIESGGRtgYGFRDTAQDIIGVPHMNPEMTRKRILDLAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545295835 2440 RQFIEGDVQHWWHPPHgNGVRTRCSDDYLWLPLAVcHYVETTGDM---DALEIrIPYLEGCPLQPGEESVYD--TPVISG 2514
Cdd:pfam17167 81 GQFKAGYGLHLFDPDW-DDIKPSKSPTVLPTPYDN-DKIHGIGDTcsdDHLWL-VPTIEAYVKETGDFSFLDevIPYSDG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545295835 2515 TEETLWLHCVKAIHYGLRF-GEHGLPLMGAGDWNDGMNRvgieGKGESVWLGFFLYDILQRFAALADRRLDESVAAMCRS 2593
Cdd:pfam17167 158 KKATVYEHLKKAIDFSLEYlGQHGIPLGGRADWNDCLNL----GGGESVFVSFLLYLALQEFIEIAKFKGDDEDAEWYEK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545295835 2594 QALRLQSNLEAHAWDGEWYRRGYFDDGTPLGSKTSQDCRIDAIAQSWSVLSGAASPGRCAKAMQALDKHLvDNEGGLIkL 2673
Cdd:pfam17167 234 MADKVREAIEKYAWDGEWYIRAYTKDGDKIGSKQNEEGKIHLESQSWAVLSGIGKDERAKKAMDSVEKYL-FTEYGLH-L 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545295835 2674 LTPPFDGHGPNPGYIQGYLPGVRENGGQYTHGAIWAVMAFARMGNAERAWQLWSMLNPVNHTlnaGLVGIYKAEPYVMSA 2753
Cdd:pfam17167 312 NQPPFSTPNLDIGFITRYYPGVKENGGIFCHPNPWVIVAETKLGRGDRAMKLYDAINPANQN---DIIETRKAEPYVYAQ 388
|
410 420 430
....*....|....*....|....*....|....*..
gi 545295835 2754 DVYSV-APHTGRAGWSWYTGSAGWAWRLLTEELLGIK 2789
Cdd:pfam17167 389 FVMGKdHPDHGRANHPWLTGTAGWAYVAITEGILGLR 425
|
|
| Glyco_transf_36 |
pfam06165 |
Glycosyltransferase family 36; The glycosyltransferase family 36 includes cellobiose ... |
1582-1833 |
7.57e-94 |
|
Glycosyltransferase family 36; The glycosyltransferase family 36 includes cellobiose phosphorylase (EC:2.4.1.20), cellodextrin phosphorylase (EC:2.4.1.49), chitobiose phosphorylase (EC:2.4.1.-). Many members of this family contain two copies of this domain.
Pssm-ID: 461842 [Multi-domain] Cd Length: 247 Bit Score: 304.41 E-value: 7.57e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545295835 1582 PAPDIQLLSNGHYHLMLTAGGGGYSRWNDIA---LTRWRSDTTRDNWGAFCYIRDTQTGDVWSNTWQPTGytSGQDEEVL 1658
Cdd:pfam06165 1 PAPWINVLSNGDYGVLISNTGGGYSWYKNSRenrLTRWRNDPVRDPPGEYIYIRDEESGEVWSPTWQPVR--KPLDYEVR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545295835 1659 FTDAGAEFRRSFGGLSLKTQVVISPEDDVELRRLTLIHRGRKPRSLELTTYAEVVLAPDASDLAHPAFSNLFIQTELAPE 1738
Cdd:pfam06165 79 HGLGYTRFEREDGGIETELTVFVPPEDPVEIRRLTLTNTSDRERRLSVTSYVEWVLGNAAADLAHPAFSRLFSQTEIVTE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545295835 1739 RDAILCHRRPCSPDEPAPCLFHMMVVHGDnrhnvSFETDRARFIGRGRNPANAQAIEAgGMLGNTSGSVLDPILAIRNAI 1818
Cdd:pfam06165 159 LGAILAARNPRSEEFRNRYAFHAVSGPVD-----SYETDREEFIGRGGSLANPAALER-GPLSNSVGAGLDPCAALQVRI 232
|
250
....*....|....*
gi 545295835 1819 ILQPGQPVTIDIIYG 1833
Cdd:pfam06165 233 ELAPGETKEVVFILG 247
|
|
| COG3459 |
COG3459 |
Cellobiose phosphorylase [Carbohydrate transport and metabolism]; |
1580-1859 |
1.77e-44 |
|
Cellobiose phosphorylase [Carbohydrate transport and metabolism];
Pssm-ID: 442682 [Multi-domain] Cd Length: 794 Bit Score: 176.10 E-value: 1.77e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545295835 1580 DTPAPDIQLLSNGHYHLMLTAGGGGYSRWNDIA---LTRWRSDTTRDNWGAFCYIRDTQTGDVWSNTWQPT--------- 1647
Cdd:COG3459 19 DTPAPWINVLANPDFGFLVSETGGGYSWYKNSRenrLTRWRNDPVSDPPGEYFYLRDEETGDYWSPTWQPVrkpldeyec 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545295835 1648 ----GYTSgqdeevlftdagaeFRRSFGGLSLKTQVVISPEDDVELRRLTLIHRGRKPRSLELTTYAEVVLAPDASDLAH 1723
Cdd:COG3459 99 rhgfGYTR--------------FEHEYNGIESELTYFVPLDDPVEIWRLKLTNTSDRPRRLSVTSYVEWVLGNARDDTAN 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545295835 1724 paFSNLFIQTELAPERDAILcHRRPCSPDEPAPCLFhmMVVHGDNRhnvSFETDRARFIGRGRNPANAQAIEAGGmLGNT 1803
Cdd:COG3459 165 --FQVTLSTGEVDPEGGAIL-ARNPYNERFNGRVAF--FAVSEPVS---SFTGDREEFLGRYGSLANPAALERGK-LSNS 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 545295835 1804 SGSVLDPILAIRNAIILQPGQPVTIDIIYGISETRQQSLALLEKYRDYPIADRVFE 1859
Cdd:COG3459 236 VGAGLDPCAALQVDIELAPGEEKELVFLLGQGENKEEARALIARYRDPDAVDAALA 291
|
|
| CBM_X |
smart01068 |
Putative carbohydrate binding domain; |
2068-2133 |
3.11e-21 |
|
Putative carbohydrate binding domain;
Pssm-ID: 215008 [Multi-domain] Cd Length: 62 Bit Score: 89.17 E-value: 3.11e-21
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 545295835 2068 NGYGGFSQDGREYQIVLReNALTPAPWSNILANSRFGSVISEAGQAYT-WYENAheyrLTPWENDPV 2133
Cdd:smart01068 1 NGLGGFDDDGREYVRTLD-GPDTPAPWINVLSNGRYGVMVSASGSGYSrWADNS----LTRWRNDPV 62
|
|
| Glycoamylase |
pfam10091 |
Putative glucoamylase; The structure of UniProt:Q5LIB7 has an alpha/alpha toroid fold and is ... |
1319-1512 |
1.35e-19 |
|
Putative glucoamylase; The structure of UniProt:Q5LIB7 has an alpha/alpha toroid fold and is similar structurally to a number of glucoamylases. Most of these structural homologs are glucoamylases, involved in breaking down complex sugars (e.g. starch). The biologically relevant state is likely to be monomeric. The putative active site is located at the centre of the toroid with a well defined large cavity.
Pssm-ID: 431045 Cd Length: 218 Bit Score: 90.12 E-value: 1.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545295835 1319 SHYDLLPSEIRLTSFLAIA--TNQLPLKSWYALGRLF----TTIDNETALMSWSGSMFEYLMPNLVMPTWP-----GSLL 1387
Cdd:pfam10091 1 NYPWDGYNEALILYILAAGspTHPVPPEVYHNWARAFrrdwGNYGGELLLYSWGGPLFWHQYSHAWLDFRGirdayGIDY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545295835 1388 DEMSQSAVMRQIHWGKE-------RGVP-WGVSESGYHAfdvqhnyQYQAFGVPGlglrRGLADDMVVAPYATLLALMVS 1459
Cdd:pfam10091 81 FENSRRATLAQREYCIRnpkkfkgYGEDcWGLTASDSPG-------GYSARGPPY----GNLSDDGTISPTAALSSLPFA 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 545295835 1460 PQRACENL--FRMQKNGARGEYGFYEALDYTPSRlatgqlYAVVQSWMAHHQGMA 1512
Cdd:pfam10091 150 PEIALPALryLYELGDQLYGRYGFYDAFNPTFND------GWYSKDYLGIDQGPI 198
|
|
| CBM_X |
smart01068 |
Putative carbohydrate binding domain; |
1574-1621 |
9.92e-19 |
|
Putative carbohydrate binding domain;
Pssm-ID: 215008 [Multi-domain] Cd Length: 62 Bit Score: 82.24 E-value: 9.92e-19
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 545295835 1574 RIFYSVDTPAPDIQLLSNGHYHLMLTAGGGGYSRWNDIALTRWRSDTT 1621
Cdd:smart01068 15 RTLDGPDTPAPWINVLSNGRYGVMVSASGSGYSRWADNSLTRWRNDPV 62
|
|
| HomoserineK_II |
cd05153 |
Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a ... |
136-212 |
2.69e-03 |
|
Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a subset of bacteria, which have a Protein Kinase fold. These proteins do not bear any similarity to the GHMP family homoserine kinases present in most bacteria and eukaryotes. Homoserine kinase catalyzes the transfer of the gamma-phosphoryl group from ATP to L-homoserine producing L-homoserine phosphate, an intermediate in the production of the amino acids threonine, methionine, and isoleucine. The Type II homoserine kinase subfamily is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K).
Pssm-ID: 270702 [Multi-domain] Cd Length: 300 Bit Score: 42.63 E-value: 2.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545295835 136 PRIYHIASEAVAH---GDGRWDVASLTSYLTAYQKVTPLTLGEVWALPGMLRLALienLRRISMEVIKAQRDRNLADTWI 212
Cdd:cd05153 211 PLLYDLAIALNDWcfdDDGKLDPERAKALLAGYQSVRPLTEEEKAALPLLLRAAA---LRFWLSRLYDFHLPREGALVTP 287
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COG3459 |
COG3459 |
Cellobiose phosphorylase [Carbohydrate transport and metabolism]; |
2068-2858 |
0e+00 |
|
Cellobiose phosphorylase [Carbohydrate transport and metabolism];
Pssm-ID: 442682 [Multi-domain] Cd Length: 794 Bit Score: 1321.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545295835 2068 NGYGGFSQDGREYQIVlreNALTPAPWSNILANSRFGSVISEAGQAYTWYENAHEYRLTPWENDPVSDRSGEAFYLRDEE 2147
Cdd:COG3459 1 NGYGGFDDDGREYVIT---GPDTPAPWINVLANPDFGFLVSETGGGYSWYKNSRENRLTRWRNDPVSDPPGEYFYLRDEE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545295835 2148 SGECWSPTALPVRG-HGDYLTRHGFGYSVFAHRESGIDSELTVLVAEEEPVKLVLLTLSNSSGRTRQLSVTGYVEWTLGE 2226
Cdd:COG3459 78 TGDYWSPTWQPVRKpLDEYECRHGFGYTRFEHEYNGIESELTYFVPLDDPVEIWRLKLTNTSDRPRRLSVTSYVEWVLGN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545295835 2227 TRTRSAPHIVT-HVARTPGGCGVL-ANNFYGDNGGGRTAFFAVSGNGCSLTGDRREFIGRNGSLHAPSAMKLQKLSGKTG 2304
Cdd:COG3459 158 ARDDTANFQVTlSTGEVDPEGGAIlARNPYNERFNGRVAFFAVSEPVSSFTGDREEFLGRYGSLANPAALERGKLSNSVG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545295835 2305 AGLDPCGAVQSAVTLIDGDQRTFIFILGAEENDVCAQETLARYMNEDTVRQELNRIHNHWHNVLDKIVVNTPDTSVNLLV 2384
Cdd:COG3459 238 AGLDPCAALQVDIELAPGEEKELVFLLGQGENKEEARALIARYRDPDAVDAALAEVKAYWDELLGAVQVETPDPALDLMV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545295835 2385 NGWLLYQTVACRLMARSGYYQSGGAFGFRDQLQDTLALNHAAPDRMREQIILCASRQFIEGDVQHWWHPPHGNGVRTRCS 2464
Cdd:COG3459 318 NGWLLYQTLACRLWARSAFYQSGGAYGFRDQLQDSMALVHARPELAREQILLAASRQFPEGDVQHWWHPPTGRGVRTRFS 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545295835 2465 DDYLWLPLAVCHYVETTGDMDALEIRIPYLEGCPLQPGEESVYDTPVISGTEETLWLHCVKAIHYGL-RFGEHGLPLMGA 2543
Cdd:COG3459 398 DDLLWLPYAVAAYIKETGDFSILDEVVPFLDGPPLPPGEEDAYDLPTVSGEEATLYEHCKRAIDFSLnRLGPHGLPLIGR 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545295835 2544 GDWNDGMNRVGIEGKGESVWLGFFLYDILQRFAALADRRLDESVAAMCRSQALRLQSNLEAHAWDGEWYRRGYFDDGTPL 2623
Cdd:COG3459 478 GDWNDGMNLVGEGGKGESVWLAWFLYYALKEFAPLAEARGDEERAERYRAEAEELREAIEKHAWDGEWYRRAYFDDGTPL 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545295835 2624 GSKTSQDCRIDAIAQSWSVLSGAASPGRCAKAMQALDKHLVDNEGGLIKLLTPPFDGHGPNPGYIQGYLPGVRENGGQYT 2703
Cdd:COG3459 558 GSKENEECKIDLIAQSWAVLSGAADPERARKAMDSVDKYLVTEYGGLILLLTPPFDKYDPDPGYIKGYPPGVRENGGQYT 637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545295835 2704 HGAIWAVMAFARMGNAERAWQLWSMLNPVNHTLNaglVGIYKAEPYVMSADVYSVAPHTGRAGWSWYTGSAGWAWRLLTE 2783
Cdd:COG3459 638 HAAPWAIMAEALLGDGDRAYELYSMINPINHNDE---ADRYKVEPYVYAADVYGVDPHFGRGGWSWYTGSAGWMYRAATE 714
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 545295835 2784 ELLGIKRSGTDFSVHARFPDEWSSFSMAYQYGDSHYQISVSRGDA----EYCVTLDGVLLPDDRIPLKDDGQNHTVEII 2858
Cdd:COG3459 715 YILGIRPEGDGLRIDPCIPSDWPGFSVTRRFRGAVYHITVKNPDGvskgVKSITVDGKPIEGNLIPLVDDGKEHEVEVV 793
|
|
| GH94N_ChvB_NdvB_2_like |
cd11753 |
Second GH94N domain of cyclic beta 1-2 glucan synthetase and similar domains; The glycoside ... |
1525-1860 |
4.78e-166 |
|
Second GH94N domain of cyclic beta 1-2 glucan synthetase and similar domains; The glycoside hydrolase family 94 (previously known as glycosyltransferase family 36) includes cyclic beta 1-2 glucan synthetase (EC:2.4.1.20) or ChvB (encoded by the chromosomal chvB virulence gene). This second of two tandemly repeated GH94-N-terminal-like domains has not been characterized functionally. Some beta 1-2 glucan synthetases are annotated as NdvB (nodule development B) gene products, glycosyltransferases required for the synthesis of cyclic beta-(1,2)-glucans, which play a role in interactions between bacteria and plants.
Pssm-ID: 213069 [Multi-domain] Cd Length: 336 Bit Score: 515.53 E-value: 4.78e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545295835 1525 MTERFMSSTVFRSASLLLQERVPDAVDLYSPRRHFESHEGRV-KPVRYEPRIFYSVDTPAPDIQLLSNGHYHLMLTAGGG 1603
Cdd:cd11753 1 MQRRFHADPRIQAAELLLQERIPREVPIITPRLEELSRPAKKeEEAPEPVRRFTTPDTALPEVHLLSNGRYSVMLTASGS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545295835 1604 GYSRWNDIALTRWRSDTTRDNWGAFCYIRDTQTGDVWSNTWQPTGyTSGQDEEVLFTDAGAEFRRSFGGLSLKTQVVISP 1683
Cdd:cd11753 81 GYSRWNDLAVTRWREDATRDNWGSFIYLRDVDSGKVWSATYQPTR-DPPDEYEVVFSEDRAEFRRRDGGIETTTEVVVSP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545295835 1684 EDDVELRRLTLIHRGRKPRSLELTTYAEVVLAPDASDLAHPAFSNLFIQTELAPERDAILCHRRPCSPDEPAPCLFHMMV 1763
Cdd:cd11753 160 EDDAEIRRVTLTNLSRRPRELEVTSYAEVVLAPPAADEAHPAFSKLFVQTEFLPEQGALLATRRPRSPDEPPPWAAHFVA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545295835 1764 VHGDNRHNVSFETDRARFIGRGRNPANAQAIEAGGMLGNTSGSVLDPILAIRNAIILQPGQPVTIDIIYGISETRQQSLA 1843
Cdd:cd11753 240 VEGEAVGPLQYETDRARFIGRGRSLANPAAMDDGAPLSGTVGAVLDPIFSLRRRVRLPPGETARVTFVTGVADSREEALE 319
|
330
....*....|....*..
gi 545295835 1844 LLEKYRDYPIADRVFEL 1860
Cdd:cd11753 320 LADKYRDPSAVERAFEL 336
|
|
| GH94N_ChvB_NdvB_1_like |
cd11756 |
First GH94N domain of cyclic beta 1-2 glucan synthetase and similar domains; The glycoside ... |
2067-2347 |
6.92e-144 |
|
First GH94N domain of cyclic beta 1-2 glucan synthetase and similar domains; The glycoside hydrolase family 94 (previously known as glycosyltransferase family 36) includes cyclic beta 1-2 glucan synthetase (EC:2.4.1.20) or ChvB (encoded by the chromosomal chvB virulence gene). This first of two tandemly repeated GH94-N-terminal-like domains has not been characterized functionally. Some beta 1-2 glucan synthetases are annotated as NdvB (nodule development B) gene products, glycosyltransferases required for the synthesis of cyclic beta-(1,2)-glucans, which play a role in interactions between bacteria and plants.
Pssm-ID: 213072 [Multi-domain] Cd Length: 284 Bit Score: 449.65 E-value: 6.92e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545295835 2067 FNGYGGFSQDGREYQIVLRENALTPAPWSNILANSRFGSVISEAGQAYTWYENAHEYRLTPWENDPVSDRSGEAFYLRDE 2146
Cdd:cd11756 5 FNGYGGFSPDGREYVIVLGPGKRTPAPWINVIANPGFGFLVSESGSGYTWAENSRENRLTPWSNDPVSDPPGEALYLRDE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545295835 2147 ESGECWSPTALPVRGHGDYLTRHGFGYSVFAHRESGIDSELTVLVAEEEPVKLVLLTLSNSSGRTRQLSVTGYVEWTLGE 2226
Cdd:cd11756 85 ETGEVWSPTPLPIRGGGPYRVRHGFGYSRFEHRSHGIEQELTVFVPRDDPVKISRLRLRNTSGRPRRLSVTYYAEWVLGV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545295835 2227 TRTRSAPHIVTHVARTPGgcGVLANNFYGDNGGGRTAFFAVSGNGCSLTGDRREFIGRNGSLHAPSAMKLQKLSGKTGAG 2306
Cdd:cd11756 165 NREKTAPHIVTEYDEETG--ALLARNPYNEDFGGRVAFLAVSGGPRSFTGDRREFIGRNGSLANPAALKRGRLSGRTGAG 242
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 545295835 2307 LDPCGAVQSAVTLIDGDQRTFIFILGAEENDVCAQETLARY 2347
Cdd:cd11756 243 LDPCAALQVDLELAPGEEKEIVFLLGEADDAEEARALIRRY 283
|
|
| Glyco_hydro_36 |
pfam17167 |
Glycosyl hydrolase 36 superfamily, catalytic domain; This is the catalytic region of the ... |
2363-2789 |
2.19e-136 |
|
Glycosyl hydrolase 36 superfamily, catalytic domain; This is the catalytic region of the superfamily of enzymes referred to as GH36. UniProtKB:Q76IQ9 is a chitobiose phosphorylase that catalyzes the reversible phosphorolysis of chitobiose into alpha-GlcNAc-1-phosphate and GlcNAc with inversion of the anomeric configuration. The full-length enzyme comprises a beta sandwich domain and an (alpha/alpha)(6) barrel domain. The alpha-helical barrel component of the domain, this family, is the catalytic region.
Pssm-ID: 465366 Cd Length: 425 Bit Score: 434.24 E-value: 2.19e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545295835 2363 HWHNVLDKIVVNTPDTSVNLLVNGWLLYQTVACRLMARSG-YYQSGGA--FGFRDQLQDTLALNHAAPDRMREQIILCAS 2439
Cdd:pfam17167 1 YWDSRLEKFQVKTPDESLDTMINIWNLYQCEICFVWSRFAsFIESGGRtgYGFRDTAQDIIGVPHMNPEMTRKRILDLAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545295835 2440 RQFIEGDVQHWWHPPHgNGVRTRCSDDYLWLPLAVcHYVETTGDM---DALEIrIPYLEGCPLQPGEESVYD--TPVISG 2514
Cdd:pfam17167 81 GQFKAGYGLHLFDPDW-DDIKPSKSPTVLPTPYDN-DKIHGIGDTcsdDHLWL-VPTIEAYVKETGDFSFLDevIPYSDG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545295835 2515 TEETLWLHCVKAIHYGLRF-GEHGLPLMGAGDWNDGMNRvgieGKGESVWLGFFLYDILQRFAALADRRLDESVAAMCRS 2593
Cdd:pfam17167 158 KKATVYEHLKKAIDFSLEYlGQHGIPLGGRADWNDCLNL----GGGESVFVSFLLYLALQEFIEIAKFKGDDEDAEWYEK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545295835 2594 QALRLQSNLEAHAWDGEWYRRGYFDDGTPLGSKTSQDCRIDAIAQSWSVLSGAASPGRCAKAMQALDKHLvDNEGGLIkL 2673
Cdd:pfam17167 234 MADKVREAIEKYAWDGEWYIRAYTKDGDKIGSKQNEEGKIHLESQSWAVLSGIGKDERAKKAMDSVEKYL-FTEYGLH-L 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545295835 2674 LTPPFDGHGPNPGYIQGYLPGVRENGGQYTHGAIWAVMAFARMGNAERAWQLWSMLNPVNHTlnaGLVGIYKAEPYVMSA 2753
Cdd:pfam17167 312 NQPPFSTPNLDIGFITRYYPGVKENGGIFCHPNPWVIVAETKLGRGDRAMKLYDAINPANQN---DIIETRKAEPYVYAQ 388
|
410 420 430
....*....|....*....|....*....|....*..
gi 545295835 2754 DVYSV-APHTGRAGWSWYTGSAGWAWRLLTEELLGIK 2789
Cdd:pfam17167 389 FVMGKdHPDHGRANHPWLTGTAGWAYVAITEGILGLR 425
|
|
| Glyco_transf_36 |
pfam06165 |
Glycosyltransferase family 36; The glycosyltransferase family 36 includes cellobiose ... |
2091-2332 |
1.53e-100 |
|
Glycosyltransferase family 36; The glycosyltransferase family 36 includes cellobiose phosphorylase (EC:2.4.1.20), cellodextrin phosphorylase (EC:2.4.1.49), chitobiose phosphorylase (EC:2.4.1.-). Many members of this family contain two copies of this domain.
Pssm-ID: 461842 [Multi-domain] Cd Length: 247 Bit Score: 323.67 E-value: 1.53e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545295835 2091 PAPWSNILANSRFGSVISEAGQAYTWYENAHEYRLTPWENDPVSDRSGEAFYLRDEESGECWSPTALPVRGHGDYLTRHG 2170
Cdd:pfam06165 1 PAPWINVLSNGDYGVLISNTGGGYSWYKNSRENRLTRWRNDPVRDPPGEYIYIRDEESGEVWSPTWQPVRKPLDYEVRHG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545295835 2171 FGYSVFAHRESGIDSELTVLVAEEEPVKLVLLTLSNSSGRTRQLSVTGYVEWTLGETRTRSA-----PHIVTHVARTPGG 2245
Cdd:pfam06165 81 LGYTRFEREDGGIETELTVFVPPEDPVEIRRLTLTNTSDRERRLSVTSYVEWVLGNAAADLAhpafsRLFSQTEIVTELG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545295835 2246 CGVLANNFYGDNGGGRTAFFAVSGNGCSLTGDRREFIGRNGSLHAPSAMKLQKLSGKTGAGLDPCGAVQSAVTLIDGDQR 2325
Cdd:pfam06165 161 AILAARNPRSEEFRNRYAFHAVSGPVDSYETDREEFIGRGGSLANPAALERGPLSNSVGAGLDPCAALQVRIELAPGETK 240
|
....*..
gi 545295835 2326 TFIFILG 2332
Cdd:pfam06165 241 EVVFILG 247
|
|
| Glyco_transf_36 |
pfam06165 |
Glycosyltransferase family 36; The glycosyltransferase family 36 includes cellobiose ... |
1582-1833 |
7.57e-94 |
|
Glycosyltransferase family 36; The glycosyltransferase family 36 includes cellobiose phosphorylase (EC:2.4.1.20), cellodextrin phosphorylase (EC:2.4.1.49), chitobiose phosphorylase (EC:2.4.1.-). Many members of this family contain two copies of this domain.
Pssm-ID: 461842 [Multi-domain] Cd Length: 247 Bit Score: 304.41 E-value: 7.57e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545295835 1582 PAPDIQLLSNGHYHLMLTAGGGGYSRWNDIA---LTRWRSDTTRDNWGAFCYIRDTQTGDVWSNTWQPTGytSGQDEEVL 1658
Cdd:pfam06165 1 PAPWINVLSNGDYGVLISNTGGGYSWYKNSRenrLTRWRNDPVRDPPGEYIYIRDEESGEVWSPTWQPVR--KPLDYEVR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545295835 1659 FTDAGAEFRRSFGGLSLKTQVVISPEDDVELRRLTLIHRGRKPRSLELTTYAEVVLAPDASDLAHPAFSNLFIQTELAPE 1738
Cdd:pfam06165 79 HGLGYTRFEREDGGIETELTVFVPPEDPVEIRRLTLTNTSDRERRLSVTSYVEWVLGNAAADLAHPAFSRLFSQTEIVTE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545295835 1739 RDAILCHRRPCSPDEPAPCLFHMMVVHGDnrhnvSFETDRARFIGRGRNPANAQAIEAgGMLGNTSGSVLDPILAIRNAI 1818
Cdd:pfam06165 159 LGAILAARNPRSEEFRNRYAFHAVSGPVD-----SYETDREEFIGRGGSLANPAALER-GPLSNSVGAGLDPCAALQVRI 232
|
250
....*....|....*
gi 545295835 1819 ILQPGQPVTIDIIYG 1833
Cdd:pfam06165 233 ELAPGETKEVVFILG 247
|
|
| GH94N_ChBP_like |
cd11755 |
N-terminal domain of chitobiose phosphorylase (ChBP) and similar proteins; The glycoside ... |
2070-2357 |
1.74e-51 |
|
N-terminal domain of chitobiose phosphorylase (ChBP) and similar proteins; The glycoside hydrolase family 94 (previously known as glycosyltransferase family 36) includes chitobiose phosphorylase (EC:2.4.1.-). This N-terminal domain is involved in oligomerization and may play a role in catalysis, but it is separate from the catalytic domain [an (alpha/alpha)(6) barrel]. Chitobiose phosphorylase catalyzes the reversible phosphate dependent hydrolysis of chitobiose [(GlcNAc)2] into alpha-GlcNAc-1-phosphate and GlcNAc. In some organisms, ChBP may be involved in the production of GlcNac-6-phosphate in intracellular pathways.
Pssm-ID: 213071 [Multi-domain] Cd Length: 300 Bit Score: 184.75 E-value: 1.74e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545295835 2070 YGGFSQDGREYQIvlrENALTPAPWSNILANSRFGSVISEAGQAYTWYENAHEYRLTPWE-NDPVSDRSGEAFYLRDEES 2148
Cdd:cd11755 3 YGYFDDENREYVI---TRPDTPTPWTNYLGSGEYGAIISNNAGGYSFYKSPANGRITRFRfNSVPMDRPGRYVYLRDNES 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545295835 2149 GECWSPTALPVrghGD------YLTRHGFGYSVFAHRESGIDSELTVLVAEEEPVKLVLLTLSNSSGRTRQLSVTGYVE- 2221
Cdd:cd11755 80 GDYWSASWQPV---GKpldeykYECRHGTGYTTIESEYKGIAAETTYFVPLDQDYEIWDVKITNTSSRKRKLSVFSYAEf 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545295835 2222 --------------WTLGETRTRSAPHIVTHVARTpggcgvlaNNFYGDNGGGRTAFFAVSGNGC-SLTGDRREFIGRNG 2286
Cdd:cd11755 157 sfhwnaeqdqqnlqYSLYISRTSYKDGIIEYDNYY--------NLDDDPNGDERYRFFTSAGAEVdGFDGSRDRFIGPYR 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 545295835 2287 SLHAPSAMKLQKLSGKTGAGLDPCGAVQSAVTLIDGDQRTFIFILGAEENDVcAQETLARYMNEDTVRQEL 2357
Cdd:cd11755 229 SESNPIAVERGKCSNSLATGGNHCGALQSDITLAPGEEKEIIFILGVGNREE-GRAIRAKYSDPEAVDAEF 298
|
|
| COG3459 |
COG3459 |
Cellobiose phosphorylase [Carbohydrate transport and metabolism]; |
1580-1859 |
1.77e-44 |
|
Cellobiose phosphorylase [Carbohydrate transport and metabolism];
Pssm-ID: 442682 [Multi-domain] Cd Length: 794 Bit Score: 176.10 E-value: 1.77e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545295835 1580 DTPAPDIQLLSNGHYHLMLTAGGGGYSRWNDIA---LTRWRSDTTRDNWGAFCYIRDTQTGDVWSNTWQPT--------- 1647
Cdd:COG3459 19 DTPAPWINVLANPDFGFLVSETGGGYSWYKNSRenrLTRWRNDPVSDPPGEYFYLRDEETGDYWSPTWQPVrkpldeyec 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545295835 1648 ----GYTSgqdeevlftdagaeFRRSFGGLSLKTQVVISPEDDVELRRLTLIHRGRKPRSLELTTYAEVVLAPDASDLAH 1723
Cdd:COG3459 99 rhgfGYTR--------------FEHEYNGIESELTYFVPLDDPVEIWRLKLTNTSDRPRRLSVTSYVEWVLGNARDDTAN 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545295835 1724 paFSNLFIQTELAPERDAILcHRRPCSPDEPAPCLFhmMVVHGDNRhnvSFETDRARFIGRGRNPANAQAIEAGGmLGNT 1803
Cdd:COG3459 165 --FQVTLSTGEVDPEGGAIL-ARNPYNERFNGRVAF--FAVSEPVS---SFTGDREEFLGRYGSLANPAALERGK-LSNS 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 545295835 1804 SGSVLDPILAIRNAIILQPGQPVTIDIIYGISETRQQSLALLEKYRDYPIADRVFE 1859
Cdd:COG3459 236 VGAGLDPCAALQVDIELAPGEEKELVFLLGQGENKEEARALIARYRDPDAVDAALA 291
|
|
| GH94N_like_4 |
cd11751 |
Glycoside hydrolase family 94 N-terminal-like domain of uncharacterized function; The ... |
2131-2336 |
1.40e-43 |
|
Glycoside hydrolase family 94 N-terminal-like domain of uncharacterized function; The glycoside hydrolase family 94 (previously known as glycosyltransferase family 36) includes cellobiose phosphorylase (EC:2.4.1.20), cellodextrin phosphorylase (EC:2.4.1.49), chitobiose phosphorylase (EC:2.4.1.-), amongst other members. Their N-terminal domain is involved in oligomerization and may play a role in catalysis, but it is separate from the catalytic domain [an (alpha/alpha)(6) barrel]. The GH64N domain, as represented by this model, is found near the N-terminus of GH94 members and related proteins with uncharacterized specificities.
Pssm-ID: 213067 Cd Length: 223 Bit Score: 159.45 E-value: 1.40e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545295835 2131 DPVSDRSGEAFYLRDEESGECWSPTALPVRGHG-DYLTRHGFGYSVFAHRESGIDSELTVLVAEEEPVKLVLLTLSNSSG 2209
Cdd:cd11751 2 DLIKDNWGKYFYIRDDDTGEVWSATYKPLKTEPeDYECVHGIGYSEFTSEYNGIRSSLTVFVPKDDPVEIWSLTLRNTSD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545295835 2210 RTRQLSVTGYVEWTLG--------------ETRTRSAPHIVT---HVARTPGGCGVLANNFYgdnggGRTAFFAVSGNGC 2272
Cdd:cd11751 82 RERRLSVFSYFEWELGgfpdehrefhklfiETSFDRELNGIYarkYLWGFPDEKGRHNNRNW-----PYVAFHAASEPVV 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 545295835 2273 SLTGDRREFIGRNGSLHAPSAMKLQKLSGKTGAGLDPCGAVQSAVTLIDGDQRTFIFILGAEEN 2336
Cdd:cd11751 157 SYDGDKESFIGMYGSEENPDAVAMGGLSNSVGRFEDAIGVLQHEVTLEPGEEKTIHFTLGAAES 220
|
|
| GH94N_ChvB_NdvB_1_like |
cd11756 |
First GH94N domain of cyclic beta 1-2 glucan synthetase and similar domains; The glycoside ... |
1581-1849 |
1.91e-35 |
|
First GH94N domain of cyclic beta 1-2 glucan synthetase and similar domains; The glycoside hydrolase family 94 (previously known as glycosyltransferase family 36) includes cyclic beta 1-2 glucan synthetase (EC:2.4.1.20) or ChvB (encoded by the chromosomal chvB virulence gene). This first of two tandemly repeated GH94-N-terminal-like domains has not been characterized functionally. Some beta 1-2 glucan synthetases are annotated as NdvB (nodule development B) gene products, glycosyltransferases required for the synthesis of cyclic beta-(1,2)-glucans, which play a role in interactions between bacteria and plants.
Pssm-ID: 213072 [Multi-domain] Cd Length: 284 Bit Score: 138.02 E-value: 1.91e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545295835 1581 TPAPDIQLLSNGHYHLMLTAGGGGY-----SRWNdiALTRWRSDTTRDNWGAFCYIRDTQTGDVWSNTWQP--------- 1646
Cdd:cd11756 28 TPAPWINVIANPGFGFLVSESGSGYtwaenSREN--RLTPWSNDPVSDPPGEALYLRDEETGEVWSPTPLPirgggpyrv 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545295835 1647 ---TGYTSgqdeevlftdagaeFRRSFGGLSLKTQVVISPEDDVELRRLTLIHRGRKPRSLELTTYAEVVLApdasdlAH 1723
Cdd:cd11756 106 rhgFGYSR--------------FEHRSHGIEQELTVFVPRDDPVKISRLRLRNTSGRPRRLSVTYYAEWVLG------VN 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545295835 1724 PAFSNLFIQTELAPERDAILChRRPCSPDEPAPCLFhmMVVHGdnrHNVSFETDRARFIGRGRNPANAQAIEAGGmLGNT 1803
Cdd:cd11756 166 REKTAPHIVTEYDEETGALLA-RNPYNEDFGGRVAF--LAVSG---GPRSFTGDRREFIGRNGSLANPAALKRGR-LSGR 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 545295835 1804 SGSVLDPILAIRNAIILQPGQPVTIDIIYGISETRQQSLALLEKYR 1849
Cdd:cd11756 239 TGAGLDPCAALQVDLELAPGEEKEIVFLLGEADDAEEARALIRRYR 284
|
|
| GH94N_CBP_like |
cd11754 |
N-terminal domain of cellobiose phosphorylase (CBP) and similar proteins; The glycoside ... |
2070-2357 |
6.95e-34 |
|
N-terminal domain of cellobiose phosphorylase (CBP) and similar proteins; The glycoside hydrolase family 94 (previously known as glycosyltransferase family 36) includes cellobiose phosphorylase (EC:2.4.1.20) or cellobiose:phosphate alpha-D-glucosyltransferase, or CepA. This N-terminal domain is involved in oligomerization and may play a role in catalysis, but it is separate from the catalytic domain [an (alpha/alpha)(6) barrel]. Cellobiose phosphorylase participates in the degradation of cellulose, it catalyzes the phosphate dependent hydrolysis of cellobiose into alpha-D-glucose-1-phosphate and D-glucose, a reversible reaction.
Pssm-ID: 213070 [Multi-domain] Cd Length: 303 Bit Score: 133.90 E-value: 6.95e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545295835 2070 YGGFSQDGREYQIvlrENALTPAPWSNILANSRFGSVISEAGQAYTWYENAHEYRLTPWE--NDPVsDRSGEAFYLRDee 2147
Cdd:cd11754 3 YGHFDDENREYVI---TTPDTPLPWINYLGSEDFFSLISNTAGGYSFYKDARLRRLTRYRynNVPL-DNGGRYFYIKD-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545295835 2148 SGECWSPTALPVRGHGD-YLTRHGFGYSVFAHRESGIDSELTVLVAEEEPVKLVLLTLSNSSGRTRQLSVTGYVEWTL-- 2224
Cdd:cd11754 77 GGTVWNPGWKPVKTPLDsYECRHGLGYTRITGEKNGIEAEVLYFVPLGENAEIWRLTLTNTSDSPKKLKLFSFVEFCLwn 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545295835 2225 --------------GETRTRSAP--HIVTHVARtpggcgvlaNNFYgdngggrtAFFAVSGNGCSLTGDRREFIGRNGSL 2288
Cdd:cd11754 157 alddmtnfqrnlstGEVEVEGSViyHKTEYRER---------RNHY--------AFFAVNAPIDGFDTDRDAFLGLYNGF 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545295835 2289 HAPSAMKLQKLSGKTGAGLDPCGAVQSAVTLIDGDQRTFIFILGAEEND-------------VCAQETLARYMNEDTVRQ 2355
Cdd:cd11754 220 DEPQAVLEGKSTNSVAHGWSPIGSHHVELTLAPGESKELIFVLGYVENPddekwespgvinkKPAKELIERFATPEAVDA 299
|
..
gi 545295835 2356 EL 2357
Cdd:cd11754 300 AF 301
|
|
| GH94N_ChvB_NdvB_2_like |
cd11753 |
Second GH94N domain of cyclic beta 1-2 glucan synthetase and similar domains; The glycoside ... |
2087-2333 |
5.82e-32 |
|
Second GH94N domain of cyclic beta 1-2 glucan synthetase and similar domains; The glycoside hydrolase family 94 (previously known as glycosyltransferase family 36) includes cyclic beta 1-2 glucan synthetase (EC:2.4.1.20) or ChvB (encoded by the chromosomal chvB virulence gene). This second of two tandemly repeated GH94-N-terminal-like domains has not been characterized functionally. Some beta 1-2 glucan synthetases are annotated as NdvB (nodule development B) gene products, glycosyltransferases required for the synthesis of cyclic beta-(1,2)-glucans, which play a role in interactions between bacteria and plants.
Pssm-ID: 213069 [Multi-domain] Cd Length: 336 Bit Score: 129.56 E-value: 5.82e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545295835 2087 NALTPAPWSNILANSRFGSVISEAGQAYTWYENAHEYRltpWENDPVSDRSGEAFYLRDEESGECWSPTALPVRGHGD-Y 2165
Cdd:cd11753 55 TPDTALPEVHLLSNGRYSVMLTASGSGYSRWNDLAVTR---WREDATRDNWGSFIYLRDVDSGKVWSATYQPTRDPPDeY 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545295835 2166 LTRHGFGYSVFAHRESGIDSELTVLVAEEEPVKLVLLTLSNSSGRTRQLSVTGYVEWTLGE--------------TRTRS 2231
Cdd:cd11753 132 EVVFSEDRAEFRRRDGGIETTTEVVVSPEDDAEIRRVTLTNLSRRPRELEVTSYAEVVLAPpaadeahpafsklfVQTEF 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545295835 2232 APH----IVTHVARTPGGCGVLANNFYGDNGGGRTAFfavsgngcSLTGDRREFIGRNGSLHAPSAMKL-QKLSGKTGAG 2306
Cdd:cd11753 212 LPEqgalLATRRPRSPDEPPPWAAHFVAVEGEAVGPL--------QYETDRARFIGRGRSLANPAAMDDgAPLSGTVGAV 283
|
250 260
....*....|....*....|....*..
gi 545295835 2307 LDPCGAVQSAVTLIDGDQRTFIFILGA 2333
Cdd:cd11753 284 LDPIFSLRRRVRLPPGETARVTFVTGV 310
|
|
| GH94N_like_4 |
cd11751 |
Glycoside hydrolase family 94 N-terminal-like domain of uncharacterized function; The ... |
1619-1840 |
5.54e-31 |
|
Glycoside hydrolase family 94 N-terminal-like domain of uncharacterized function; The glycoside hydrolase family 94 (previously known as glycosyltransferase family 36) includes cellobiose phosphorylase (EC:2.4.1.20), cellodextrin phosphorylase (EC:2.4.1.49), chitobiose phosphorylase (EC:2.4.1.-), amongst other members. Their N-terminal domain is involved in oligomerization and may play a role in catalysis, but it is separate from the catalytic domain [an (alpha/alpha)(6) barrel]. The GH64N domain, as represented by this model, is found near the N-terminus of GH94 members and related proteins with uncharacterized specificities.
Pssm-ID: 213067 Cd Length: 223 Bit Score: 122.86 E-value: 5.54e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545295835 1619 DTTRDNWGAFCYIRDTQTGDVWSNTWQPTGyTSGQDEEVLFTDAGAEFRRSFGGLSLKTQVVISPEDDVELRRLTLIHRG 1698
Cdd:cd11751 2 DLIKDNWGKYFYIRDDDTGEVWSATYKPLK-TEPEDYECVHGIGYSEFTSEYNGIRSSLTVFVPKDDPVEIWSLTLRNTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545295835 1699 RKPRSLELTTYAEVVL--APDasdlAHPAFSNLFIQTELAPERDAILCHRR-PCSPDEPAP--CLFHMMVV-HGDNRHNV 1772
Cdd:cd11751 81 DRERRLSVFSYFEWELggFPD----EHREFHKLFIETSFDRELNGIYARKYlWGFPDEKGRhnNRNWPYVAfHAASEPVV 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 545295835 1773 SFETDRARFIGRGRNPANAQAIEAGGmLGNTSGSVLDPILAIRNAIILQPGQPVTIDIIYGISETRQQ 1840
Cdd:cd11751 157 SYDGDKESFIGMYGSEENPDAVAMGG-LSNSVGRFEDAIGVLQHEVTLEPGEEKTIHFTLGAAESGEE 223
|
|
| GH94N_like |
cd11746 |
N-terminal domain of glycoside hydrolase family 94 and related domains; The glycoside ... |
2141-2332 |
1.38e-28 |
|
N-terminal domain of glycoside hydrolase family 94 and related domains; The glycoside hydrolase family 94 (previously known as glycosyltransferase family 36) includes cellobiose phosphorylase (EC:2.4.1.20), cellodextrin phosphorylase (EC:2.4.1.49), chitobiose phosphorylase (EC:2.4.1.-), amongst other members. Their N-terminal domain is involved in oligomerization and may play a role in catalysis, but it is separate from the catalytic domain [an (alpha/alpha)(6) barrel]. This GH64N domain also occurs in tandem repeat arrangements (not at the N-terminus) in cyclic beta 1-2 glucan synthetase and related proteins, and as a standalone domain in distantly related proteins of unknown function.
Pssm-ID: 213062 Cd Length: 179 Bit Score: 114.53 E-value: 1.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545295835 2141 FYLRDEESGECWSPTALPVRGHGDYLTRHgFGYSVFAHRESGIDSELTVLVAEEEPVKLVLLTLSNSSGRTRQLSVTGYV 2220
Cdd:cd11746 1 FYFYLSDDGDKWSLGWQPVRREAEHYEVR-LGYVTFENEYNGIEAETTIFVPPDDPGEIQRVKLTNTGDRPRELTLFPYF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545295835 2221 EWTLGetrtrSAPHIVThvARTPGGCGVLANNFYGDNGGGRTAFFAVSGNGCSLTGDRRefigrnGSLHAPSAMKLQKLS 2300
Cdd:cd11746 80 EWCLP-----DALFQGT--SYDPEGGAVNCTTYYSYNIGARPAFYATSFKPDDFDGDGG------RTLANPLAVVAGQLS 146
|
170 180 190
....*....|....*....|....*....|..
gi 545295835 2301 GKTGAGLDPCGAVQSAVTLIDGDQRTFIFILG 2332
Cdd:cd11746 147 NTVGRVEDPIAALAIRFALEPGESKRYTFALG 178
|
|
| GH94N_ChBP_like |
cd11755 |
N-terminal domain of chitobiose phosphorylase (ChBP) and similar proteins; The glycoside ... |
1580-1859 |
6.02e-26 |
|
N-terminal domain of chitobiose phosphorylase (ChBP) and similar proteins; The glycoside hydrolase family 94 (previously known as glycosyltransferase family 36) includes chitobiose phosphorylase (EC:2.4.1.-). This N-terminal domain is involved in oligomerization and may play a role in catalysis, but it is separate from the catalytic domain [an (alpha/alpha)(6) barrel]. Chitobiose phosphorylase catalyzes the reversible phosphate dependent hydrolysis of chitobiose [(GlcNAc)2] into alpha-GlcNAc-1-phosphate and GlcNAc. In some organisms, ChBP may be involved in the production of GlcNac-6-phosphate in intracellular pathways.
Pssm-ID: 213071 [Multi-domain] Cd Length: 300 Bit Score: 110.79 E-value: 6.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545295835 1580 DTPAPDIQLLSNGHYHLMLTAGGGGYSRWNDIA---LTRWRSD-TTRDNWGAFCYIRDTQTGDVWSNTWQP--------- 1646
Cdd:cd11755 19 DTPTPWTNYLGSGEYGAIISNNAGGYSFYKSPAngrITRFRFNsVPMDRPGRYVYLRDNESGDYWSASWQPvgkpldeyk 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545295835 1647 ------TGYTSgqdeevlftdagaeFRRSFGGLSLKTQVVISPEDDVELRRLTLIHRGRKPRSLELTTYAEVVLAPDAS- 1719
Cdd:cd11755 99 yecrhgTGYTT--------------IESEYKGIAAETTYFVPLDQDYEIWDVKITNTSSRKRKLSVFSYAEFSFHWNAEq 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545295835 1720 DLAHPAFSnLFI-QTELapeRDAILCHRRPCSPDEPAP--CLFHMMVVHGDNRhnVSFETDRARFIGRGRNPANAQAIEA 1796
Cdd:cd11755 165 DQQNLQYS-LYIsRTSY---KDGIIEYDNYYNLDDDPNgdERYRFFTSAGAEV--DGFDGSRDRFIGPYRSESNPIAVER 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 545295835 1797 gGMLGNTSGSVLDPILAIRNAIILQPGQPVTIDIIYGIsETRQQSLALLEKYRDYPIADRVFE 1859
Cdd:cd11755 239 -GKCSNSLATGGNHCGALQSDITLAPGEEKEIIFILGV-GNREEGRAIRAKYSDPEAVDAEFE 299
|
|
| CBM_X |
smart01068 |
Putative carbohydrate binding domain; |
2068-2133 |
3.11e-21 |
|
Putative carbohydrate binding domain;
Pssm-ID: 215008 [Multi-domain] Cd Length: 62 Bit Score: 89.17 E-value: 3.11e-21
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 545295835 2068 NGYGGFSQDGREYQIVLReNALTPAPWSNILANSRFGSVISEAGQAYT-WYENAheyrLTPWENDPV 2133
Cdd:smart01068 1 NGLGGFDDDGREYVRTLD-GPDTPAPWINVLSNGRYGVMVSASGSGYSrWADNS----LTRWRNDPV 62
|
|
| Glycoamylase |
pfam10091 |
Putative glucoamylase; The structure of UniProt:Q5LIB7 has an alpha/alpha toroid fold and is ... |
1319-1512 |
1.35e-19 |
|
Putative glucoamylase; The structure of UniProt:Q5LIB7 has an alpha/alpha toroid fold and is similar structurally to a number of glucoamylases. Most of these structural homologs are glucoamylases, involved in breaking down complex sugars (e.g. starch). The biologically relevant state is likely to be monomeric. The putative active site is located at the centre of the toroid with a well defined large cavity.
Pssm-ID: 431045 Cd Length: 218 Bit Score: 90.12 E-value: 1.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545295835 1319 SHYDLLPSEIRLTSFLAIA--TNQLPLKSWYALGRLF----TTIDNETALMSWSGSMFEYLMPNLVMPTWP-----GSLL 1387
Cdd:pfam10091 1 NYPWDGYNEALILYILAAGspTHPVPPEVYHNWARAFrrdwGNYGGELLLYSWGGPLFWHQYSHAWLDFRGirdayGIDY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545295835 1388 DEMSQSAVMRQIHWGKE-------RGVP-WGVSESGYHAfdvqhnyQYQAFGVPGlglrRGLADDMVVAPYATLLALMVS 1459
Cdd:pfam10091 81 FENSRRATLAQREYCIRnpkkfkgYGEDcWGLTASDSPG-------GYSARGPPY----GNLSDDGTISPTAALSSLPFA 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 545295835 1460 PQRACENL--FRMQKNGARGEYGFYEALDYTPSRlatgqlYAVVQSWMAHHQGMA 1512
Cdd:pfam10091 150 PEIALPALryLYELGDQLYGRYGFYDAFNPTFND------GWYSKDYLGIDQGPI 198
|
|
| CBM_X |
smart01068 |
Putative carbohydrate binding domain; |
1574-1621 |
9.92e-19 |
|
Putative carbohydrate binding domain;
Pssm-ID: 215008 [Multi-domain] Cd Length: 62 Bit Score: 82.24 E-value: 9.92e-19
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 545295835 1574 RIFYSVDTPAPDIQLLSNGHYHLMLTAGGGGYSRWNDIALTRWRSDTT 1621
Cdd:smart01068 15 RTLDGPDTPAPWINVLSNGRYGVMVSASGSGYSRWADNSLTRWRNDPV 62
|
|
| GH94N_like |
cd11746 |
N-terminal domain of glycoside hydrolase family 94 and related domains; The glycoside ... |
1630-1834 |
2.78e-17 |
|
N-terminal domain of glycoside hydrolase family 94 and related domains; The glycoside hydrolase family 94 (previously known as glycosyltransferase family 36) includes cellobiose phosphorylase (EC:2.4.1.20), cellodextrin phosphorylase (EC:2.4.1.49), chitobiose phosphorylase (EC:2.4.1.-), amongst other members. Their N-terminal domain is involved in oligomerization and may play a role in catalysis, but it is separate from the catalytic domain [an (alpha/alpha)(6) barrel]. This GH64N domain also occurs in tandem repeat arrangements (not at the N-terminus) in cyclic beta 1-2 glucan synthetase and related proteins, and as a standalone domain in distantly related proteins of unknown function.
Pssm-ID: 213062 Cd Length: 179 Bit Score: 82.17 E-value: 2.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545295835 1630 YIRDTQTGDVWSNTWQPTGytSGQDEEVLFTDAgAEFRRSFGGLSLKTQVVISPEDDVELRRLTLIHRGRKPRSLELTTY 1709
Cdd:cd11746 2 YFYLSDDGDKWSLGWQPVR--REAEHYEVRLGY-VTFENEYNGIEAETTIFVPPDDPGEIQRVKLTNTGDRPRELTLFPY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545295835 1710 AEVVLapdasdlahpaFSNLFIQTELAPERDAILCHRRPCSPDEPAPcLFHmmvvhgdnrhnvSFETDRARFIGRGRNP- 1788
Cdd:cd11746 79 FEWCL-----------PDALFQGTSYDPEGGAVNCTTYYSYNIGARP-AFY------------ATSFKPDDFDGDGGRTl 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 545295835 1789 ANAQAIEAgGMLGNTSGSVLDPILAIRNAIILQPGQPVTIDIIYGI 1834
Cdd:cd11746 135 ANPLAVVA-GQLSNTVGRVEDPIAALAIRFALEPGESKRYTFALGI 179
|
|
| GH94N_CBP_like |
cd11754 |
N-terminal domain of cellobiose phosphorylase (CBP) and similar proteins; The glycoside ... |
1580-1824 |
1.76e-16 |
|
N-terminal domain of cellobiose phosphorylase (CBP) and similar proteins; The glycoside hydrolase family 94 (previously known as glycosyltransferase family 36) includes cellobiose phosphorylase (EC:2.4.1.20) or cellobiose:phosphate alpha-D-glucosyltransferase, or CepA. This N-terminal domain is involved in oligomerization and may play a role in catalysis, but it is separate from the catalytic domain [an (alpha/alpha)(6) barrel]. Cellobiose phosphorylase participates in the degradation of cellulose, it catalyzes the phosphate dependent hydrolysis of cellobiose into alpha-D-glucose-1-phosphate and D-glucose, a reversible reaction.
Pssm-ID: 213070 [Multi-domain] Cd Length: 303 Bit Score: 83.06 E-value: 1.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545295835 1580 DTPAPDIQLLSNGHYHLMLTAGGGGYSRWNDIAL---TRWR-SDTTRDNWGAFCYIRDTqtGDVWSNTWQPT-------- 1647
Cdd:cd11754 19 DTPLPWINYLGSEDFFSLISNTAGGYSFYKDARLrrlTRYRyNNVPLDNGGRYFYIKDG--GTVWNPGWKPVktpldsye 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545295835 1648 -----GYTSgqdeevlftdagaeFRRSFGGLSLKTQVVISPEDDVELRRLTLIHRGRKPRSLELTTYAEVVLApDASDLA 1722
Cdd:cd11754 97 crhglGYTR--------------ITGEKNGIEAEVLYFVPLGENAEIWRLTLTNTSDSPKKLKLFSFVEFCLW-NALDDM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545295835 1723 HPAFSNLFI-QTELAperDAILCH------RRPcspdepapclfHMMVVHGDNRHNvSFETDRARFIGRGRNPANAQAIE 1795
Cdd:cd11754 162 TNFQRNLSTgEVEVE---GSVIYHkteyreRRN-----------HYAFFAVNAPID-GFDTDRDAFLGLYNGFDEPQAVL 226
|
250 260 270
....*....|....*....|....*....|..
gi 545295835 1796 AggmlGNTSGSVLD---PILAIRNAIILQPGQ 1824
Cdd:cd11754 227 E----GKSTNSVAHgwsPIGSHHVELTLAPGE 254
|
|
| GH94N_like_3 |
cd11750 |
Glycoside hydrolase family 94 N-terminal-like domain of uncharacterized function; The ... |
2070-2336 |
2.33e-12 |
|
Glycoside hydrolase family 94 N-terminal-like domain of uncharacterized function; The glycoside hydrolase family 94 (previously known as glycosyltransferase family 36) includes cellobiose phosphorylase (EC:2.4.1.20), cellodextrin phosphorylase (EC:2.4.1.49), chitobiose phosphorylase (EC:2.4.1.-), amongst other members. Their N-terminal domain is involved in oligomerization and may play a role in catalysis, but it is separate from the catalytic domain [an (alpha/alpha)(6) barrel]. The GH64N domain, as represented by this model, is found at the N-terminus of GH94 members with uncharacterized specificities.
Pssm-ID: 213066 [Multi-domain] Cd Length: 282 Bit Score: 70.20 E-value: 2.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545295835 2070 YGGFSQDGREYQIVlreNALTPAPWSNILANSRFGSVISEAGQAYTWYENAHEYRLTPW-ENDPVSDRSGEAFYLR--DE 2146
Cdd:cd11750 1 YGYFDDANKEYVIT---TPKTPIKWINYVGTLDFGGFVDHTGGSLVCKGDPALNRITKYiAQLPSSDFKGSTIYIRvkDG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545295835 2147 ESGECWSPTALPVRGHGD-YLTRHGFGYSVFAHRESGIDSELTVLVAEEEPVKLVLLTLSNSSGRTRQLSVTGYVEWTLG 2225
Cdd:cd11750 78 DNYKIFSPFYVPTLDKYDkYECHVGLGYSRIIAEAYGIRTEITIFVPEGDQVLLQDIKVTNIRDKPVEVDVIPVVEYTHF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545295835 2226 E-----TRTRSAPHIVTHVA-RTPGGCGVLANNFYGdNGGGRTAFFAVSGNGCSLTGDRREFIGRN--GSLHAPSAMKLQ 2297
Cdd:cd11750 158 DalkqlTNADWVPQTMTSKAhQEENGHTVLEQYAFM-KRDYAVNYFTSNRPVSSFEGDRRSFLGQNeyGTWANPLSLQND 236
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 545295835 2298 KLSGKTGAGLDPCGAVQSAVTLID-GDQRTFIFILGAEEN 2336
Cdd:cd11750 237 ELSNYECLRGDNIGALMHHLGWLApGETKRVITQLGQEES 276
|
|
| GH94N_NdvB_like |
cd11748 |
Glycoside hydrolase family 94 N-terminal-like domain of NdvB-like proteins; The glycoside ... |
2138-2350 |
2.04e-11 |
|
Glycoside hydrolase family 94 N-terminal-like domain of NdvB-like proteins; The glycoside hydrolase family 94 (previously known as glycosyltransferase family 36) includes cellobiose phosphorylase (EC:2.4.1.20), cellodextrin phosphorylase (EC:2.4.1.49), chitobiose phosphorylase (EC:2.4.1.-), amongst other members. Their N-terminal domain is involved in oligomerization and may play a role in catalysis, but it is separate from the catalytic domain [an (alpha/alpha)(6) barrel)]. The GH64N domain, as represented by this model, is found at the N-terminus of largely uncharacterized proteins, some members from Xanthomonas campestris and related organisms are annotated as NdvB (nodule development B) gene products, glycosyltransferases required for the synthesis of cyclic beta-(1,2)-glucans, which play a role in interactions between bacteria and plants.
Pssm-ID: 213064 [Multi-domain] Cd Length: 294 Bit Score: 67.73 E-value: 2.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545295835 2138 GEAFYLRDEESGECWSPTALPVRGHGDyltrhGFGYSVFAH------RESGIDSELTVLVAEEEPVKLVLLTLSNSSGRT 2211
Cdd:cd11748 75 GRFFYVKDEDTGELFSAPYEPVRRPPD-----SFAFSVGKNdirwvvEQDGLEVELTLSLPVDDPAELWEVKVRNLSDRA 149
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545295835 2212 RQLSVT-----GYVEW---------TLGETRTRSaphiVTHVARtpggcgvLANNFYGDNGGGRTaFFAVSGNGCSLTGD 2277
Cdd:cd11748 150 RKLSLYpyfpvGYMSWmnqsarydeGLNAIVASS----VTPYQK-------VEDYFKNKDLKDKT-FLLADRKPDSWEAR 217
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 545295835 2278 RREFIGRnGSLHAPSAMKLQKLSGKTGAGLDPCGAVQSAVTLIDGDQRTFIFILGAEENDVCAQETLARYMNE 2350
Cdd:cd11748 218 QEAFEGE-GGLHNPSALQAPTLANGDARYETPAAVMQYRLTLDPGETEQYRFVFGPAKDEAEIAQLRARYLGA 289
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| HomoserineK_II |
cd05153 |
Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a ... |
136-212 |
2.69e-03 |
|
Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a subset of bacteria, which have a Protein Kinase fold. These proteins do not bear any similarity to the GHMP family homoserine kinases present in most bacteria and eukaryotes. Homoserine kinase catalyzes the transfer of the gamma-phosphoryl group from ATP to L-homoserine producing L-homoserine phosphate, an intermediate in the production of the amino acids threonine, methionine, and isoleucine. The Type II homoserine kinase subfamily is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K).
Pssm-ID: 270702 [Multi-domain] Cd Length: 300 Bit Score: 42.63 E-value: 2.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545295835 136 PRIYHIASEAVAH---GDGRWDVASLTSYLTAYQKVTPLTLGEVWALPGMLRLALienLRRISMEVIKAQRDRNLADTWI 212
Cdd:cd05153 211 PLLYDLAIALNDWcfdDDGKLDPERAKALLAGYQSVRPLTEEEKAALPLLLRAAA---LRFWLSRLYDFHLPREGALVTP 287
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