|
Name |
Accession |
Description |
Interval |
E-value |
| COG3459 |
COG3459 |
Cellobiose phosphorylase [Carbohydrate transport and metabolism]; |
2067-2870 |
0e+00 |
|
Cellobiose phosphorylase [Carbohydrate transport and metabolism];
Pssm-ID: 442682 [Multi-domain] Cd Length: 794 Bit Score: 1362.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 2067 NGLGGFTPDGREYVITldpGQSTPAPWVNVIASPYIGTVVSESGSAYTWVENAHEFRLTTWHNDPLSDSSGEALYIRDEE 2146
Cdd:COG3459 1 NGYGGFDDDGREYVIT---GPDTPAPWINVLANPDFGFLVSETGGGYSWYKNSRENRLTRWRNDPVSDPPGEYFYLRDEE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 2147 TGAFWSPTPLPARGRSG-YVCRHGFGYSVFEHYEAGISSELFTYVAMDAPVKFAVVKLRNHSRRPRRLSLTGYWELVLGE 2225
Cdd:COG3459 78 TGDYWSPTWQPVRKPLDeYECRHGFGYTRFEHEYNGIESELTYFVPLDDPVEIWRLKLTNTSDRPRRLSVTSYVEWVLGN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 2226 WRHSNLMNIVT----ETDLHSGALFARNAYGRECANRVFFLQVSEVERTVTGNRTEFIGRNGSLSSPAAMRRKGLSGRKG 2301
Cdd:COG3459 158 ARDDTANFQVTlstgEVDPEGGAILARNPYNERFNGRVAFFAVSEPVSSFTGDREEFLGRYGSLANPAALERGKLSNSVG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 2302 AGLDPCAAIQTQIELADGQEREIVFVFGAARSTDEAQHLIQRFGGSVGAREALEAVWGHWNRTLGAVHVETPDPALDVLT 2381
Cdd:COG3459 238 AGLDPCAALQVDIELAPGEEKELVFLLGQGENKEEARALIARYRDPDAVDAALAEVKAYWDELLGAVQVETPDPALDLMV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 2382 NGWLVYQTLSCRLWGRSGYYQSGGAYGFRDQLQDTMALIHAAPWLAREQLIRCAERQFLQGDVQHWWHPPNGQGVRTHFS 2461
Cdd:COG3459 318 NGWLLYQTLACRLWARSAFYQSGGAYGFRDQLQDSMALVHARPELAREQILLAASRQFPEGDVQHWWHPPTGRGVRTRFS 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 2462 DDYLWLPYATCRYVLATGDTGVLDESVHFLEGRELNPGEEAYYDQPQRSHEVASLYEHCVRSIKHGL-RFGGHQLPLMGC 2540
Cdd:COG3459 398 DDLLWLPYAVAAYIKETGDFSILDEVVPFLDGPPLPPGEEDAYDLPTVSGEEATLYEHCKRAIDFSLnRLGPHGLPLIGR 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 2541 GDWNDGMNLVGRDGKGESVWLAWFLYENLQLFTGLARARNDEAFAEVCTRQASLLRSNIEASAWDGSWYRRAYFDDGTPL 2620
Cdd:COG3459 478 GDWNDGMNLVGEGGKGESVWLAWFLYYALKEFAPLAEARGDEERAERYRAEAEELREAIEKHAWDGEWYRRAYFDDGTPL 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 2621 GSSENDECQIDSISQSWAVISGGGDAMRARQAMAAVDKRLVRRDMQLIQLFAPPFDKSDLEPGYIKGYVPGVRENGGQYT 2700
Cdd:COG3459 558 GSKENEECKIDLIAQSWAVLSGAADPERARKAMDSVDKYLVTEYGGLILLLTPPFDKYDPDPGYIKGYPPGVRENGGQYT 637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 2701 HAAIWTTMAFAMMGDRERAWELYAMLNPINHGsrpEEIERYTVEPYVMCADIYGAPPHTSRGGWTWYTGAAGWMYRLTVE 2780
Cdd:COG3459 638 HAAPWAIMAEALLGDGDRAYELYSMINPINHN---DEADRYKVEPYVYAADVYGVDPHFGRGGWSWYTGSAGWMYRAATE 714
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 2781 TLLGLQLEVDHLRIAPCIPAHWASYKIHYRYRETFYHITVKRVGEQSEHVIRVTVDGAVVNGACvdgtgrpqgmIPLMDD 2860
Cdd:COG3459 715 YILGIRPEGDGLRIDPCIPSDWPGFSVTRRFRGAVYHITVKNPDGVSKGVKSITVDGKPIEGNL----------IPLVDD 784
|
810
....*....|
gi 1099334132 2861 RREHHVEVDL 2870
Cdd:COG3459 785 GKEHEVEVVL 794
|
|
| GH94N_ChvB_NdvB_2_like |
cd11753 |
Second GH94N domain of cyclic beta 1-2 glucan synthetase and similar domains; The glycoside ... |
1523-1862 |
0e+00 |
|
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: 560.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 1523 MQRRFMSAPLVRATELLLQERVPKKGATLHPHAAEVNATARlPVAEAGAIMRVFTDPNTPTPEVHLLSNGRYHVMATNAG 1602
Cdd:cd11753 1 MQRRFHADPRIQAAELLLQERIPREVPIITPRLEELSRPAK-KEEEAPEPVRRFTTPDTALPEVHLLSNGRYSVMLTASG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 1603 GGYSRWRDLAVTRWREDATSDCWGTFIYLRDRDTGRYWSTAYQPTLRKADHYEAIFVQARAEYRRRDQSIEAHTEIGVSP 1682
Cdd:cd11753 80 SGYSRWNDLAVTRWREDATRDNWGSFIYLRDVDSGKVWSATYQPTRDPPDEYEVVFSEDRAEFRRRDGGIETTTEVVVSP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 1683 EDDVEIRRVTLTNLASRTRQIEVTSYAEVVFAPLNADLAHRTFSNLFVQTEILSDRQAILCTRRPRTPGEQVPWMFHLLA 1762
Cdd:cd11753 160 EDDAEIRRVTLTNLSRRPRELEVTSYAEVVLAPPAADEAHPAFSKLFVQTEFLPEQGALLATRRPRSPDEPPPWAAHFVA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 1763 APGAIADEPSYETDRAKFIGRGRTAVNPVVLDsPGSPltLSNTDGSVLDPIVAIRCSIILSADESATVQIISGVAETREA 1842
Cdd:cd11753 240 VEGEAVGPLQYETDRARFIGRGRSLANPAAMD-DGAP--LSGTVGAVLDPIFSLRRRVRLPPGETARVTFVTGVADSREE 316
|
330 340
....*....|....*....|
gi 1099334132 1843 ALALLDKYCDRHFVERAFEM 1862
Cdd:cd11753 317 ALELADKYRDPSAVERAFEL 336
|
|
| GH94N_ChvB_NdvB_1_like |
cd11756 |
First GH94N domain of cyclic beta 1-2 glucan synthetase and similar domains; The glycoside ... |
2062-2344 |
1.75e-159 |
|
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: 494.33 E-value: 1.75e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 2062 ERIFYNGLGGFTPDGREYVITLDPGQSTPAPWVNVIASPYIGTVVSESGSAYTWVENAHEFRLTTWHNDPLSDSSGEALY 2141
Cdd:cd11756 1 DLQFFNGYGGFSPDGREYVIVLGPGKRTPAPWINVIANPGFGFLVSESGSGYTWAENSRENRLTPWSNDPVSDPPGEALY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 2142 IRDEETGAFWSPTPLPARGRSGYVCRHGFGYSVFEHYEAGISSELFTYVAMDAPVKFAVVKLRNHSRRPRRLSLTGYWEL 2221
Cdd:cd11756 81 LRDEETGEVWSPTPLPIRGGGPYRVRHGFGYSRFEHRSHGIEQELTVFVPRDDPVKISRLRLRNTSGRPRRLSVTYYAEW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 2222 VLGEWRHSNLMNIVTETDLHSGALFARNAYGRECANRVFFLQVSEVERTVTGNRTEFIGRNGSLSSPAAMRRKGLSGRKG 2301
Cdd:cd11756 161 VLGVNREKTAPHIVTEYDEETGALLARNPYNEDFGGRVAFLAVSGGPRSFTGDRREFIGRNGSLANPAALKRGRLSGRTG 240
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1099334132 2302 AGLDPCAAIQTQIELADGQEREIVFVFGAARSTDEAQHLIQRF 2344
Cdd:cd11756 241 AGLDPCAALQVDLELAPGEEKEIVFLLGEADDAEEARALIRRY 283
|
|
| Glyco_hydro_36 |
pfam17167 |
Glycosyl hydrolase 36 superfamily, catalytic domain; This is the catalytic region of the ... |
2360-2786 |
2.05e-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: 2.05e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 2360 HWNRTLGAVHVETPDPALDVLTNGWLVYQTLSCRLWGRSG-YYQSGGA--YGFRDQLQDTMALIHAAPWLAREQLIRCAE 2436
Cdd:pfam17167 1 YWDSRLEKFQVKTPDESLDTMINIWNLYQCEICFVWSRFAsFIESGGRtgYGFRDTAQDIIGVPHMNPEMTRKRILDLAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 2437 RQFLQGDVQHWWHP----------------PNG----QGVRTHFSDDYLWLPYATCRYVLATGDTGVLDESVHFLEGREl 2496
Cdd:pfam17167 81 GQFKAGYGLHLFDPdwddikpsksptvlptPYDndkiHGIGDTCSDDHLWLVPTIEAYVKETGDFSFLDEVIPYSDGKK- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 2497 npgeeayydqpqrshevASLYEHCVRSIKHGLRFGG-HQLPLMGCGDWNDGMNLvgrdGKGESVWLAWFLYENLQLFTGL 2575
Cdd:pfam17167 160 -----------------ATVYEHLKKAIDFSLEYLGqHGIPLGGRADWNDCLNL----GGGESVFVSFLLYLALQEFIEI 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 2576 ARARNDEAFAEVCTRQASLLRSNIEASAWDGSWYRRAYFDDGTPLGSSENDECQIDSISQSWAVISGGGDAMRARQAMAA 2655
Cdd:pfam17167 219 AKFKGDDEDAEWYEKMADKVREAIEKYAWDGEWYIRAYTKDGDKIGSKQNEEGKIHLESQSWAVLSGIGKDERAKKAMDS 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 2656 VDKRLV-RRDMQLIQlfaPPFDKSDLEPGYIKGYVPGVRENGGQYTHAAIWTTMAFAMMGDRERAWELYAMLNPINHGsr 2734
Cdd:pfam17167 299 VEKYLFtEYGLHLNQ---PPFSTPNLDIGFITRYYPGVKENGGIFCHPNPWVIVAETKLGRGDRAMKLYDAINPANQN-- 373
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1099334132 2735 pEEIERYTVEPYVMCADIYGA-PPHTSRGGWTWYTGAAGWMYRLTVETLLGLQ 2786
Cdd:pfam17167 374 -DIIETRKAEPYVYAQFVMGKdHPDHGRANHPWLTGTAGWAYVAITEGILGLR 425
|
|
| Glyco_transf_36 |
pfam06165 |
Glycosyltransferase family 36; The glycosyltransferase family 36 includes cellobiose ... |
1582-1835 |
3.83e-104 |
|
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: 334.07 E-value: 3.83e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 1582 PTPEVHLLSNGRYHVMATNAGGGYSRWRDLA---VTRWREDATSDCWGTFIYLRDRDTGRYWSTAYQPTlRKADHYEAIF 1658
Cdd:pfam06165 1 PAPWINVLSNGDYGVLISNTGGGYSWYKNSRenrLTRWRNDPVRDPPGEYIYIRDEESGEVWSPTWQPV-RKPLDYEVRH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 1659 VQARAEYRRRDQSIEAHTEIGVSPEDDVEIRRVTLTNLASRTRQIEVTSYAEVVFAPLNADLAHRTFSNLFVQTEILSDR 1738
Cdd:pfam06165 80 GLGYTRFEREDGGIETELTVFVPPEDPVEIRRLTLTNTSDRERRLSVTSYVEWVLGNAAADLAHPAFSRLFSQTEIVTEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 1739 QAILCTRRPRTPGEQVPWMFHLLAAPgaiadEPSYETDRAKFIGRGRTAVNPVVLDSPgsplTLSNTDGSVLDPIVAIRC 1818
Cdd:pfam06165 160 GAILAARNPRSEEFRNRYAFHAVSGP-----VDSYETDREEFIGRGGSLANPAALERG----PLSNSVGAGLDPCAALQV 230
|
250
....*....|....*..
gi 1099334132 1819 SIILSADESATVQIISG 1835
Cdd:pfam06165 231 RIELAPGETKEVVFILG 247
|
|
| COG3459 |
COG3459 |
Cellobiose phosphorylase [Carbohydrate transport and metabolism]; |
1575-1861 |
2.18e-49 |
|
Cellobiose phosphorylase [Carbohydrate transport and metabolism];
Pssm-ID: 442682 [Multi-domain] Cd Length: 794 Bit Score: 191.12 E-value: 2.18e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 1575 VFTDPNTPTPEVHLLSNGRYHVMATNAGGGYSrW----RDLAVTRWREDATSDCWGTFIYLRDRDTGRYWSTAYQPTLRK 1650
Cdd:COG3459 14 VITGPDTPAPWINVLANPDFGFLVSETGGGYS-WyknsRENRLTRWRNDPVSDPPGEYFYLRDEETGDYWSPTWQPVRKP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 1651 ADHYEA-------IFvqaraEYRRRDqsIEAHTEIGVSPEDDVEIRRVTLTNLASRTRQIEVTSYAEVVFAplNADLAHR 1723
Cdd:COG3459 93 LDEYECrhgfgytRF-----EHEYNG--IESELTYFVPLDDPVEIWRLKLTNTSDRPRRLSVTSYVEWVLG--NARDDTA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 1724 TFSNLFVQTEILSDRQAILCTRRPRT-PGEQVPWMfhllaapGAIADEPSYETDRAKFIGRGRTAVNPVVLDSPgsplTL 1802
Cdd:COG3459 164 NFQVTLSTGEVDPEGGAILARNPYNErFNGRVAFF-------AVSEPVSSFTGDREEFLGRYGSLANPAALERG----KL 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1099334132 1803 SNTDGSVLDPIVAIRCSIILSADESATVQIISGVAETREAALALLDKYCDRHFVERAFE 1861
Cdd:COG3459 233 SNSVGAGLDPCAALQVDIELAPGEEKELVFLLGQGENKEEARALIARYRDPDAVDAALA 291
|
|
| Glycoamylase |
pfam10091 |
Putative glucoamylase; The structure of UniProt:Q5LIB7 has an alpha/alpha toroid fold and is ... |
1319-1531 |
7.67e-25 |
|
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: 105.14 E-value: 7.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 1319 YDLLASEARLASFLLIAQGQVP-----QKHWF-ALGRQLTSHGGEMSLISWSGSMFEYLMPQLIM-----PSFVNTLLEQ 1387
Cdd:pfam10091 3 PWDGYNEALILYILAAGSPTHPvppevYHNWArAFRRDWGNYGGELLLYSWGGPLFWHQYSHAWLdfrgiRDAYGIDYFE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 1388 TCKAAVSRQIEYGRQRAVPW-GISESCYNATDMHHVYQYRAFGVPGlgfkRGLGDDLVVAPYASALALTVMPREACRNLQ 1466
Cdd:pfam10091 83 NSRRATLAQREYCIRNPKKFkGYGEDCWGLTASDSPGGYSARGPPY----GNLSDDGTISPTAALSSLPFAPEIALPALR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1099334132 1467 ALAAKG--FLGVYGFYEAVDYTPSRvplgknHAIVRTFMAHHQGMSLLAFEHaLLNRPMQRRFMSAP 1531
Cdd:pfam10091 159 YLYELGdqLYGRYGFYDAFNPTFND------GWYSKDYLGIDQGPILLMIEN-YRTGLLWKLFMSHP 218
|
|
| CBM_X |
smart01068 |
Putative carbohydrate binding domain; |
1573-1621 |
1.71e-23 |
|
Putative carbohydrate binding domain;
Pssm-ID: 215008 [Multi-domain] Cd Length: 62 Bit Score: 95.72 E-value: 1.71e-23
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1099334132 1573 MRVFTDPNTPTPEVHLLSNGRYHVMATNAGGGYSRWRDLAVTRWREDAT 1621
Cdd:smart01068 14 VRTLDGPDTPAPWINVLSNGRYGVMVSASGSGYSRWADNSLTRWRNDPV 62
|
|
| CBM_X |
smart01068 |
Putative carbohydrate binding domain; |
2067-2131 |
5.20e-20 |
|
Putative carbohydrate binding domain;
Pssm-ID: 215008 [Multi-domain] Cd Length: 62 Bit Score: 85.71 E-value: 5.20e-20
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1099334132 2067 NGLGGFTPDGREYVITLDpGQSTPAPWVNVIASPYIGTVVSESGSAYT-WVENAhefrLTTWHNDP 2131
Cdd:smart01068 1 NGLGGFDDDGREYVRTLD-GPDTPAPWINVLSNGRYGVMVSASGSGYSrWADNS----LTRWRNDP 61
|
|
| HomoserineK_II |
cd05153 |
Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a ... |
107-204 |
9.38e-05 |
|
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: 47.25 E-value: 9.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 107 PRIYDLA---LELISHMDGRVDSDNATQFVTAYQTAEPLKLGELWAFPIMLQLALlenLRRVALRIARRREERDVAITWa 183
Cdd:cd05153 211 PLLYDLAialNDWCFDDDGKLDPERAKALLAGYQSVRPLTEEEKAALPLLLRAAA---LRFWLSRLYDFHLPREGALVT- 286
|
90 100
....*....|....*....|.
gi 1099334132 184 drmlataEKEPKKLIQLLADF 204
Cdd:cd05153 287 -------PKDPDEFLRRLRQR 300
|
|
| COG5368 |
COG5368 |
Endo-beta-1,2-glucanase, glucoamylase superfamily [Carbohydrate transport and metabolism]; |
999-1114 |
1.88e-03 |
|
Endo-beta-1,2-glucanase, glucoamylase superfamily [Carbohydrate transport and metabolism];
Pssm-ID: 444138 [Multi-domain] Cd Length: 422 Bit Score: 43.63 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 999 RRTWRFFADFVGPQdNWLPPDNFQEYPAPASASRTSptniGMSLLANLAAYDFGYISAGEFLRLTGNTLATME-KLERYR 1077
Cdd:COG5368 34 RQTFRYFWEGANPV-SGLARDRSPSDDGDVASIAGT----GFGLMAIIVGVERGWITREEAVERTLKTLRFLEnKADRFH 108
|
90 100 110
....*....|....*....|....*....|....*..
gi 1099334132 1078 GHFYNWYDTRTLRPLHPRYVSSVDSGNLAGSLLTLQA 1114
Cdd:COG5368 109 GFFYHFLDGETGKRAWDDEGSLVDTAFLLQGLLTARE 145
|
|
| DUF3131 |
pfam11329 |
Protein of unknown function (DUF3131); This bacterial family of proteins has no known function. |
998-1105 |
2.24e-03 |
|
Protein of unknown function (DUF3131); This bacterial family of proteins has no known function.
Pssm-ID: 431818 Cd Length: 367 Bit Score: 43.02 E-value: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 998 ARRTWRFFadfvgpQDNWLP----PDNFQEYPApasasrTSPTNIGMSLLANLAAYDFGYISAGEFLRLTGNTLATMEKL 1073
Cdd:pfam11329 3 ARAAWSYF------ERNYQPatglVNSVDGYPS------TTLWDQGSYLAALVAARSLGLIPAAEFDQRLRKFLGTLAKL 70
|
90 100 110
....*....|....*....|....*....|...
gi 1099334132 1074 ERYRGHFYN-WYDTRTLRPlhpryvssVDSGNL 1105
Cdd:pfam11329 71 PLFDGELPNkVYNTRTLQM--------VDYGNN 95
|
|
| SrkA |
COG2334 |
Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal ... |
107-192 |
9.56e-03 |
|
Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal transduction mechanisms]; Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist is part of the Pathway/BioSystem: Threonine biosynthesis
Pssm-ID: 441905 [Multi-domain] Cd Length: 297 Bit Score: 40.68 E-value: 9.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 107 PRIYDLALELISHMDGRVDSDNATQFVTAYQTAEPLKLGELWAFPIMLQLALLenlrRVALRIARRREERDVAI-TWADR 185
Cdd:COG2334 211 PRLYDLAIALNGWADGPLDPARLAALLEGYRAVRPLTEAELAALPPLLRLRAL----RFLAWRLRRVRAKDPAFeRYLRR 286
|
....*..
gi 1099334132 186 MLATAEK 192
Cdd:COG2334 287 QIALAWA 293
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COG3459 |
COG3459 |
Cellobiose phosphorylase [Carbohydrate transport and metabolism]; |
2067-2870 |
0e+00 |
|
Cellobiose phosphorylase [Carbohydrate transport and metabolism];
Pssm-ID: 442682 [Multi-domain] Cd Length: 794 Bit Score: 1362.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 2067 NGLGGFTPDGREYVITldpGQSTPAPWVNVIASPYIGTVVSESGSAYTWVENAHEFRLTTWHNDPLSDSSGEALYIRDEE 2146
Cdd:COG3459 1 NGYGGFDDDGREYVIT---GPDTPAPWINVLANPDFGFLVSETGGGYSWYKNSRENRLTRWRNDPVSDPPGEYFYLRDEE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 2147 TGAFWSPTPLPARGRSG-YVCRHGFGYSVFEHYEAGISSELFTYVAMDAPVKFAVVKLRNHSRRPRRLSLTGYWELVLGE 2225
Cdd:COG3459 78 TGDYWSPTWQPVRKPLDeYECRHGFGYTRFEHEYNGIESELTYFVPLDDPVEIWRLKLTNTSDRPRRLSVTSYVEWVLGN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 2226 WRHSNLMNIVT----ETDLHSGALFARNAYGRECANRVFFLQVSEVERTVTGNRTEFIGRNGSLSSPAAMRRKGLSGRKG 2301
Cdd:COG3459 158 ARDDTANFQVTlstgEVDPEGGAILARNPYNERFNGRVAFFAVSEPVSSFTGDREEFLGRYGSLANPAALERGKLSNSVG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 2302 AGLDPCAAIQTQIELADGQEREIVFVFGAARSTDEAQHLIQRFGGSVGAREALEAVWGHWNRTLGAVHVETPDPALDVLT 2381
Cdd:COG3459 238 AGLDPCAALQVDIELAPGEEKELVFLLGQGENKEEARALIARYRDPDAVDAALAEVKAYWDELLGAVQVETPDPALDLMV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 2382 NGWLVYQTLSCRLWGRSGYYQSGGAYGFRDQLQDTMALIHAAPWLAREQLIRCAERQFLQGDVQHWWHPPNGQGVRTHFS 2461
Cdd:COG3459 318 NGWLLYQTLACRLWARSAFYQSGGAYGFRDQLQDSMALVHARPELAREQILLAASRQFPEGDVQHWWHPPTGRGVRTRFS 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 2462 DDYLWLPYATCRYVLATGDTGVLDESVHFLEGRELNPGEEAYYDQPQRSHEVASLYEHCVRSIKHGL-RFGGHQLPLMGC 2540
Cdd:COG3459 398 DDLLWLPYAVAAYIKETGDFSILDEVVPFLDGPPLPPGEEDAYDLPTVSGEEATLYEHCKRAIDFSLnRLGPHGLPLIGR 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 2541 GDWNDGMNLVGRDGKGESVWLAWFLYENLQLFTGLARARNDEAFAEVCTRQASLLRSNIEASAWDGSWYRRAYFDDGTPL 2620
Cdd:COG3459 478 GDWNDGMNLVGEGGKGESVWLAWFLYYALKEFAPLAEARGDEERAERYRAEAEELREAIEKHAWDGEWYRRAYFDDGTPL 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 2621 GSSENDECQIDSISQSWAVISGGGDAMRARQAMAAVDKRLVRRDMQLIQLFAPPFDKSDLEPGYIKGYVPGVRENGGQYT 2700
Cdd:COG3459 558 GSKENEECKIDLIAQSWAVLSGAADPERARKAMDSVDKYLVTEYGGLILLLTPPFDKYDPDPGYIKGYPPGVRENGGQYT 637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 2701 HAAIWTTMAFAMMGDRERAWELYAMLNPINHGsrpEEIERYTVEPYVMCADIYGAPPHTSRGGWTWYTGAAGWMYRLTVE 2780
Cdd:COG3459 638 HAAPWAIMAEALLGDGDRAYELYSMINPINHN---DEADRYKVEPYVYAADVYGVDPHFGRGGWSWYTGSAGWMYRAATE 714
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 2781 TLLGLQLEVDHLRIAPCIPAHWASYKIHYRYRETFYHITVKRVGEQSEHVIRVTVDGAVVNGACvdgtgrpqgmIPLMDD 2860
Cdd:COG3459 715 YILGIRPEGDGLRIDPCIPSDWPGFSVTRRFRGAVYHITVKNPDGVSKGVKSITVDGKPIEGNL----------IPLVDD 784
|
810
....*....|
gi 1099334132 2861 RREHHVEVDL 2870
Cdd:COG3459 785 GKEHEVEVVL 794
|
|
| GH94N_ChvB_NdvB_2_like |
cd11753 |
Second GH94N domain of cyclic beta 1-2 glucan synthetase and similar domains; The glycoside ... |
1523-1862 |
0e+00 |
|
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: 560.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 1523 MQRRFMSAPLVRATELLLQERVPKKGATLHPHAAEVNATARlPVAEAGAIMRVFTDPNTPTPEVHLLSNGRYHVMATNAG 1602
Cdd:cd11753 1 MQRRFHADPRIQAAELLLQERIPREVPIITPRLEELSRPAK-KEEEAPEPVRRFTTPDTALPEVHLLSNGRYSVMLTASG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 1603 GGYSRWRDLAVTRWREDATSDCWGTFIYLRDRDTGRYWSTAYQPTLRKADHYEAIFVQARAEYRRRDQSIEAHTEIGVSP 1682
Cdd:cd11753 80 SGYSRWNDLAVTRWREDATRDNWGSFIYLRDVDSGKVWSATYQPTRDPPDEYEVVFSEDRAEFRRRDGGIETTTEVVVSP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 1683 EDDVEIRRVTLTNLASRTRQIEVTSYAEVVFAPLNADLAHRTFSNLFVQTEILSDRQAILCTRRPRTPGEQVPWMFHLLA 1762
Cdd:cd11753 160 EDDAEIRRVTLTNLSRRPRELEVTSYAEVVLAPPAADEAHPAFSKLFVQTEFLPEQGALLATRRPRSPDEPPPWAAHFVA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 1763 APGAIADEPSYETDRAKFIGRGRTAVNPVVLDsPGSPltLSNTDGSVLDPIVAIRCSIILSADESATVQIISGVAETREA 1842
Cdd:cd11753 240 VEGEAVGPLQYETDRARFIGRGRSLANPAAMD-DGAP--LSGTVGAVLDPIFSLRRRVRLPPGETARVTFVTGVADSREE 316
|
330 340
....*....|....*....|
gi 1099334132 1843 ALALLDKYCDRHFVERAFEM 1862
Cdd:cd11753 317 ALELADKYRDPSAVERAFEL 336
|
|
| GH94N_ChvB_NdvB_1_like |
cd11756 |
First GH94N domain of cyclic beta 1-2 glucan synthetase and similar domains; The glycoside ... |
2062-2344 |
1.75e-159 |
|
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: 494.33 E-value: 1.75e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 2062 ERIFYNGLGGFTPDGREYVITLDPGQSTPAPWVNVIASPYIGTVVSESGSAYTWVENAHEFRLTTWHNDPLSDSSGEALY 2141
Cdd:cd11756 1 DLQFFNGYGGFSPDGREYVIVLGPGKRTPAPWINVIANPGFGFLVSESGSGYTWAENSRENRLTPWSNDPVSDPPGEALY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 2142 IRDEETGAFWSPTPLPARGRSGYVCRHGFGYSVFEHYEAGISSELFTYVAMDAPVKFAVVKLRNHSRRPRRLSLTGYWEL 2221
Cdd:cd11756 81 LRDEETGEVWSPTPLPIRGGGPYRVRHGFGYSRFEHRSHGIEQELTVFVPRDDPVKISRLRLRNTSGRPRRLSVTYYAEW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 2222 VLGEWRHSNLMNIVTETDLHSGALFARNAYGRECANRVFFLQVSEVERTVTGNRTEFIGRNGSLSSPAAMRRKGLSGRKG 2301
Cdd:cd11756 161 VLGVNREKTAPHIVTEYDEETGALLARNPYNEDFGGRVAFLAVSGGPRSFTGDRREFIGRNGSLANPAALKRGRLSGRTG 240
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1099334132 2302 AGLDPCAAIQTQIELADGQEREIVFVFGAARSTDEAQHLIQRF 2344
Cdd:cd11756 241 AGLDPCAALQVDLELAPGEEKEIVFLLGEADDAEEARALIRRY 283
|
|
| Glyco_hydro_36 |
pfam17167 |
Glycosyl hydrolase 36 superfamily, catalytic domain; This is the catalytic region of the ... |
2360-2786 |
2.05e-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: 2.05e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 2360 HWNRTLGAVHVETPDPALDVLTNGWLVYQTLSCRLWGRSG-YYQSGGA--YGFRDQLQDTMALIHAAPWLAREQLIRCAE 2436
Cdd:pfam17167 1 YWDSRLEKFQVKTPDESLDTMINIWNLYQCEICFVWSRFAsFIESGGRtgYGFRDTAQDIIGVPHMNPEMTRKRILDLAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 2437 RQFLQGDVQHWWHP----------------PNG----QGVRTHFSDDYLWLPYATCRYVLATGDTGVLDESVHFLEGREl 2496
Cdd:pfam17167 81 GQFKAGYGLHLFDPdwddikpsksptvlptPYDndkiHGIGDTCSDDHLWLVPTIEAYVKETGDFSFLDEVIPYSDGKK- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 2497 npgeeayydqpqrshevASLYEHCVRSIKHGLRFGG-HQLPLMGCGDWNDGMNLvgrdGKGESVWLAWFLYENLQLFTGL 2575
Cdd:pfam17167 160 -----------------ATVYEHLKKAIDFSLEYLGqHGIPLGGRADWNDCLNL----GGGESVFVSFLLYLALQEFIEI 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 2576 ARARNDEAFAEVCTRQASLLRSNIEASAWDGSWYRRAYFDDGTPLGSSENDECQIDSISQSWAVISGGGDAMRARQAMAA 2655
Cdd:pfam17167 219 AKFKGDDEDAEWYEKMADKVREAIEKYAWDGEWYIRAYTKDGDKIGSKQNEEGKIHLESQSWAVLSGIGKDERAKKAMDS 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 2656 VDKRLV-RRDMQLIQlfaPPFDKSDLEPGYIKGYVPGVRENGGQYTHAAIWTTMAFAMMGDRERAWELYAMLNPINHGsr 2734
Cdd:pfam17167 299 VEKYLFtEYGLHLNQ---PPFSTPNLDIGFITRYYPGVKENGGIFCHPNPWVIVAETKLGRGDRAMKLYDAINPANQN-- 373
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1099334132 2735 pEEIERYTVEPYVMCADIYGA-PPHTSRGGWTWYTGAAGWMYRLTVETLLGLQ 2786
Cdd:pfam17167 374 -DIIETRKAEPYVYAQFVMGKdHPDHGRANHPWLTGTAGWAYVAITEGILGLR 425
|
|
| Glyco_transf_36 |
pfam06165 |
Glycosyltransferase family 36; The glycosyltransferase family 36 includes cellobiose ... |
1582-1835 |
3.83e-104 |
|
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: 334.07 E-value: 3.83e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 1582 PTPEVHLLSNGRYHVMATNAGGGYSRWRDLA---VTRWREDATSDCWGTFIYLRDRDTGRYWSTAYQPTlRKADHYEAIF 1658
Cdd:pfam06165 1 PAPWINVLSNGDYGVLISNTGGGYSWYKNSRenrLTRWRNDPVRDPPGEYIYIRDEESGEVWSPTWQPV-RKPLDYEVRH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 1659 VQARAEYRRRDQSIEAHTEIGVSPEDDVEIRRVTLTNLASRTRQIEVTSYAEVVFAPLNADLAHRTFSNLFVQTEILSDR 1738
Cdd:pfam06165 80 GLGYTRFEREDGGIETELTVFVPPEDPVEIRRLTLTNTSDRERRLSVTSYVEWVLGNAAADLAHPAFSRLFSQTEIVTEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 1739 QAILCTRRPRTPGEQVPWMFHLLAAPgaiadEPSYETDRAKFIGRGRTAVNPVVLDSPgsplTLSNTDGSVLDPIVAIRC 1818
Cdd:pfam06165 160 GAILAARNPRSEEFRNRYAFHAVSGP-----VDSYETDREEFIGRGGSLANPAALERG----PLSNSVGAGLDPCAALQV 230
|
250
....*....|....*..
gi 1099334132 1819 SIILSADESATVQIISG 1835
Cdd:pfam06165 231 RIELAPGETKEVVFILG 247
|
|
| Glyco_transf_36 |
pfam06165 |
Glycosyltransferase family 36; The glycosyltransferase family 36 includes cellobiose ... |
2090-2329 |
5.58e-99 |
|
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: 319.05 E-value: 5.58e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 2090 PAPWVNVIASPYIGTVVSESGSAYTWVENAHEFRLTTWHNDPLSDSSGEALYIRDEETGAFWSPTPLPARGRSGYVCRHG 2169
Cdd:pfam06165 1 PAPWINVLSNGDYGVLISNTGGGYSWYKNSRENRLTRWRNDPVRDPPGEYIYIRDEESGEVWSPTWQPVRKPLDYEVRHG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 2170 FGYSVFEHYEAGISSELFTYVAMDAPVKFAVVKLRNHSRRPRRLSLTGYWELVLG----------EWRHSNLMNIVTETD 2239
Cdd:pfam06165 81 LGYTRFEREDGGIETELTVFVPPEDPVEIRRLTLTNTSDRERRLSVTSYVEWVLGnaaadlahpaFSRLFSQTEIVTELG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 2240 lhsGALFARNAYGRECANRVFFLQVSEVERTVTGNRTEFIGRNGSLSSPAAMRRKGLSGRKGAGLDPCAAIQTQIELADG 2319
Cdd:pfam06165 161 ---AILAARNPRSEEFRNRYAFHAVSGPVDSYETDREEFIGRGGSLANPAALERGPLSNSVGAGLDPCAALQVRIELAPG 237
|
250
....*....|
gi 1099334132 2320 QEREIVFVFG 2329
Cdd:pfam06165 238 ETKEVVFILG 247
|
|
| COG3459 |
COG3459 |
Cellobiose phosphorylase [Carbohydrate transport and metabolism]; |
1575-1861 |
2.18e-49 |
|
Cellobiose phosphorylase [Carbohydrate transport and metabolism];
Pssm-ID: 442682 [Multi-domain] Cd Length: 794 Bit Score: 191.12 E-value: 2.18e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 1575 VFTDPNTPTPEVHLLSNGRYHVMATNAGGGYSrW----RDLAVTRWREDATSDCWGTFIYLRDRDTGRYWSTAYQPTLRK 1650
Cdd:COG3459 14 VITGPDTPAPWINVLANPDFGFLVSETGGGYS-WyknsRENRLTRWRNDPVSDPPGEYFYLRDEETGDYWSPTWQPVRKP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 1651 ADHYEA-------IFvqaraEYRRRDqsIEAHTEIGVSPEDDVEIRRVTLTNLASRTRQIEVTSYAEVVFAplNADLAHR 1723
Cdd:COG3459 93 LDEYECrhgfgytRF-----EHEYNG--IESELTYFVPLDDPVEIWRLKLTNTSDRPRRLSVTSYVEWVLG--NARDDTA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 1724 TFSNLFVQTEILSDRQAILCTRRPRT-PGEQVPWMfhllaapGAIADEPSYETDRAKFIGRGRTAVNPVVLDSPgsplTL 1802
Cdd:COG3459 164 NFQVTLSTGEVDPEGGAILARNPYNErFNGRVAFF-------AVSEPVSSFTGDREEFLGRYGSLANPAALERG----KL 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1099334132 1803 SNTDGSVLDPIVAIRCSIILSADESATVQIISGVAETREAALALLDKYCDRHFVERAFE 1861
Cdd:COG3459 233 SNSVGAGLDPCAALQVDIELAPGEEKELVFLLGQGENKEEARALIARYRDPDAVDAALA 291
|
|
| GH94N_ChBP_like |
cd11755 |
N-terminal domain of chitobiose phosphorylase (ChBP) and similar proteins; The glycoside ... |
2070-2345 |
2.79e-47 |
|
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: 172.80 E-value: 2.79e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 2070 GGFTPDGREYVITlDPgqSTPAPWVNVIASPYIGTVVSESGSAYTWVENAHEFRLTTW-HNDPLSDSSGEALYIRDEETG 2148
Cdd:cd11755 4 GYFDDENREYVIT-RP--DTPTPWTNYLGSGEYGAIISNNAGGYSFYKSPANGRITRFrFNSVPMDRPGRYVYLRDNESG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 2149 AFWSPTPLPArGRS----GYVCRHGFGYSVFEHYEAGISSELFTYVAMDAPVKFAVVKLRNHSRRPRRLSLTGYWELVLg 2224
Cdd:cd11755 81 DYWSASWQPV-GKPldeyKYECRHGTGYTTIESEYKGIAAETTYFVPLDQDYEIWDVKITNTSSRKRKLSVFSYAEFSF- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 2225 EWRHSN-LMNI-----VTETDLHSGALFARNAYGRE------CANRVFFLQVSEVErTVTGNRTEFIGRNGSLSSPAAMR 2292
Cdd:cd11755 159 HWNAEQdQQNLqyslyISRTSYKDGIIEYDNYYNLDddpngdERYRFFTSAGAEVD-GFDGSRDRFIGPYRSESNPIAVE 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1099334132 2293 RKGLSGRKGAGLDPCAAIQTQIELADGQEREIVFVFGaARSTDEAQHLIQRFG 2345
Cdd:cd11755 238 RGKCSNSLATGGNHCGALQSDITLAPGEEKEIIFILG-VGNREEGRAIRAKYS 289
|
|
| GH94N_like_4 |
cd11751 |
Glycoside hydrolase family 94 N-terminal-like domain of uncharacterized function; The ... |
2130-2336 |
5.71e-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: 157.53 E-value: 5.71e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 2130 DPLSDSSGEALYIRDEETGAFWSPT--PLPARGRSgYVCRHGFGYSVFEHYEAGISSELFTYVAMDAPVKFAVVKLRNHS 2207
Cdd:cd11751 2 DLIKDNWGKYFYIRDDDTGEVWSATykPLKTEPED-YECVHGIGYSEFTSEYNGIRSSLTVFVPKDDPVEIWSLTLRNTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 2208 RRPRRLSLTGYWELVLG---EWRHSNLMN-IVTETDLHSGALFAR-------NAYGReCANR----VFFLQVSEVERTVT 2272
Cdd:cd11751 81 DRERRLSVFSYFEWELGgfpDEHREFHKLfIETSFDRELNGIYARkylwgfpDEKGR-HNNRnwpyVAFHAASEPVVSYD 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1099334132 2273 GNRTEFIGRNGSLSSPAAMRRKGLSGRKGAGLDPCAAIQTQIELADGQEREIVFVFGAARSTDE 2336
Cdd:cd11751 160 GDKESFIGMYGSEENPDAVAMGGLSNSVGRFEDAIGVLQHEVTLEPGEEKTIHFTLGAAESGEE 223
|
|
| GH94N_ChBP_like |
cd11755 |
N-terminal domain of chitobiose phosphorylase (ChBP) and similar proteins; The glycoside ... |
1575-1861 |
1.94e-38 |
|
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: 147.00 E-value: 1.94e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 1575 VFTDPNTPTPEVHLLSNGRYHVMATNAGGGYSRWRDLA---VTRWREDATS-DCWGTFIYLRDRDTGRYWSTAYQPTLRK 1650
Cdd:cd11755 14 VITRPDTPTPWTNYLGSGEYGAIISNNAGGYSFYKSPAngrITRFRFNSVPmDRPGRYVYLRDNESGDYWSASWQPVGKP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 1651 ADHYEAifvQAR---------AEYRrrdqSIEAHTEIGVSPEDDVEIRRVTLTNLASRTRQIEVTSYAEVVFAP-LNADL 1720
Cdd:cd11755 94 LDEYKY---ECRhgtgyttieSEYK----GIAAETTYFVPLDQDYEIWDVKITNTSSRKRKLSVFSYAEFSFHWnAEQDQ 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 1721 AH----RTFSNLFVQTEILsdrQAILCTRRPRTPGEQvpWMFHLLAAPGAIADepSYETDRAKFIGRGRTAVNPVVLDSP 1796
Cdd:cd11755 167 QNlqysLYISRTSYKDGII---EYDNYYNLDDDPNGD--ERYRFFTSAGAEVD--GFDGSRDRFIGPYRSESNPIAVERG 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1099334132 1797 GspltLSNTDGSVLDPIVAIRCSIILSADESATVQIISGVaETREAALALLDKYCDRHFVERAFE 1861
Cdd:cd11755 240 K----CSNSLATGGNHCGALQSDITLAPGEEKEIIFILGV-GNREEGRAIRAKYSDPEAVDAEFE 299
|
|
| GH94N_ChvB_NdvB_2_like |
cd11753 |
Second GH94N domain of cyclic beta 1-2 glucan synthetase and similar domains; The glycoside ... |
2038-2344 |
2.44e-34 |
|
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: 136.50 E-value: 2.44e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 2038 ERVPGRLEPLQQPAAEPANPLSARERIfynglggfTPDGREYvitldPGQSTPAPWVNVIASPYIGTVVSESGSAYTWVE 2117
Cdd:cd11753 20 ERIPREVPIITPRLEELSRPAKKEEEA--------PEPVRRF-----TTPDTALPEVHLLSNGRYSVMLTASGSGYSRWN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 2118 NAHefrLTTWHNDPLSDSSGEALYIRDEETGAFWSPTPLPARGRSG-YVCRHGFGYSVFEHYEAGISSELFTYVAMDAPV 2196
Cdd:cd11753 87 DLA---VTRWREDATRDNWGSFIYLRDVDSGKVWSATYQPTRDPPDeYEVVFSEDRAEFRRRDGGIETTTEVVVSPEDDA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 2197 KFAVVKLRNHSRRPRRLSLTGYWELVLGEWR----H---SNLMnIVTETDLHSGALFARnaygR----ECANRVFFLQVS 2265
Cdd:cd11753 164 EIRRVTLTNLSRRPRELEVTSYAEVVLAPPAadeaHpafSKLF-VQTEFLPEQGALLAT----RrprsPDEPPPWAAHFV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 2266 EVERTVTG------NRTEFIGRNGSLSSPAAM-RRKGLSGRKGAGLDPCAAIQTQIELADGQEREIVFVFGAARSTDEAQ 2338
Cdd:cd11753 239 AVEGEAVGplqyetDRARFIGRGRSLANPAAMdDGAPLSGTVGAVLDPIFSLRRRVRLPPGETARVTFVTGVADSREEAL 318
|
....*.
gi 1099334132 2339 HLIQRF 2344
Cdd:cd11753 319 ELADKY 324
|
|
| GH94N_ChvB_NdvB_1_like |
cd11756 |
First GH94N domain of cyclic beta 1-2 glucan synthetase and similar domains; The glycoside ... |
1580-1850 |
5.34e-34 |
|
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: 133.78 E-value: 5.34e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 1580 NTPTPEVHLLSNGRYHVMATNAGGGYSrW----RDLAVTRWREDATSDCWGTFIYLRDRDTGRYWSTAYQPtLRKADHYE 1655
Cdd:cd11756 27 RTPAPWINVIANPGFGFLVSESGSGYT-WaensRENRLTPWSNDPVSDPPGEALYLRDEETGEVWSPTPLP-IRGGGPYR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 1656 AIFVQARAEYRRRDQSIEAHTEIGVSPEDDVEIRRVTLTNLASRTRQIEVTSYAEVVFAplnadlAHRTFSNLFVQTEIL 1735
Cdd:cd11756 105 VRHGFGYSRFEHRSHGIEQELTVFVPRDDPVKISRLRLRNTSGRPRRLSVTYYAEWVLG------VNREKTAPHIVTEYD 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 1736 SDRQAILCtRRPRTPGeqvpwmFhllaaPGAIA------DEPSYETDRAKFIGRGRTAVNPVVLDSpgspLTLSNTDGSV 1809
Cdd:cd11756 179 EETGALLA-RNPYNED------F-----GGRVAflavsgGPRSFTGDRREFIGRNGSLANPAALKR----GRLSGRTGAG 242
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1099334132 1810 LDPIVAIRCSIILSADESATVQIISGVAETREAALALLDKY 1850
Cdd:cd11756 243 LDPCAALQVDLELAPGEEKEIVFLLGEADDAEEARALIRRY 283
|
|
| GH94N_like_4 |
cd11751 |
Glycoside hydrolase family 94 N-terminal-like domain of uncharacterized function; The ... |
1623-1841 |
6.21e-32 |
|
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: 125.94 E-value: 6.21e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 1623 DCWGTFIYLRDRDTGRYWSTAYQPTLRKADHYEAIFVQARAEYRRRDQSIEAHTEIGVSPEDDVEIRRVTLTNLASRTRQ 1702
Cdd:cd11751 6 DNWGKYFYIRDDDTGEVWSATYKPLKTEPEDYECVHGIGYSEFTSEYNGIRSSLTVFVPKDDPVEIWSLTLRNTSDRERR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 1703 IEVTSYAEVVFAplNADLAHRTFSNLFVQTEILSDRQAILCTRR-PRTPGEQVPW--------MFHLlaapgaiADEP-- 1771
Cdd:cd11751 86 LSVFSYFEWELG--GFPDEHREFHKLFIETSFDRELNGIYARKYlWGFPDEKGRHnnrnwpyvAFHA-------ASEPvv 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 1772 SYETDRAKFIGRGRTAVNPVVLDSPGspltLSNTDGSVLDPIVAIRCSIILSADESATVQIISGVAETRE 1841
Cdd:cd11751 157 SYDGDKESFIGMYGSEENPDAVAMGG----LSNSVGRFEDAIGVLQHEVTLEPGEEKTIHFTLGAAESGE 222
|
|
| GH94N_CBP_like |
cd11754 |
N-terminal domain of cellobiose phosphorylase (CBP) and similar proteins; The glycoside ... |
2070-2344 |
8.44e-30 |
|
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: 121.96 E-value: 8.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 2070 GGFTPDGREYVITlDPgqSTPAPWVNviaspYIGT-----VVSESGSAYTWVENAHEFRLTT--WHNDPLsDSSGEALYI 2142
Cdd:cd11754 4 GHFDDENREYVIT-TP--DTPLPWIN-----YLGSedffsLISNTAGGYSFYKDARLRRLTRyrYNNVPL-DNGGRYFYI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 2143 RDEETgaFWSPTPLPARGR-SGYVCRHGFGYSVFEHYEAGISSELFTYVAMDAPVKFAVVKLRNHSRRPRRLSLTGYWEL 2221
Cdd:cd11754 75 KDGGT--VWNPGWKPVKTPlDSYECRHGLGYTRITGEKNGIEAEVLYFVPLGENAEIWRLTLTNTSDSPKKLKLFSFVEF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 2222 VLgeWRHSNLM-----NIVT-ETDLHSGALFARNAYgRECANRVFFLQVSeveRTVTG---NRTEFIGRNGSLSSPAAMR 2292
Cdd:cd11754 153 CL--WNALDDMtnfqrNLSTgEVEVEGSVIYHKTEY-RERRNHYAFFAVN---APIDGfdtDRDAFLGLYNGFDEPQAVL 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1099334132 2293 RKGLSGRKGAGLDPCAAIQTQIELADGQEREIVFVFGAARSTDE-------------AQHLIQRF 2344
Cdd:cd11754 227 EGKSTNSVAHGWSPIGSHHVELTLAPGESKELIFVLGYVENPDDekwespgvinkkpAKELIERF 291
|
|
| Glycoamylase |
pfam10091 |
Putative glucoamylase; The structure of UniProt:Q5LIB7 has an alpha/alpha toroid fold and is ... |
1319-1531 |
7.67e-25 |
|
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: 105.14 E-value: 7.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 1319 YDLLASEARLASFLLIAQGQVP-----QKHWF-ALGRQLTSHGGEMSLISWSGSMFEYLMPQLIM-----PSFVNTLLEQ 1387
Cdd:pfam10091 3 PWDGYNEALILYILAAGSPTHPvppevYHNWArAFRRDWGNYGGELLLYSWGGPLFWHQYSHAWLdfrgiRDAYGIDYFE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 1388 TCKAAVSRQIEYGRQRAVPW-GISESCYNATDMHHVYQYRAFGVPGlgfkRGLGDDLVVAPYASALALTVMPREACRNLQ 1466
Cdd:pfam10091 83 NSRRATLAQREYCIRNPKKFkGYGEDCWGLTASDSPGGYSARGPPY----GNLSDDGTISPTAALSSLPFAPEIALPALR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1099334132 1467 ALAAKG--FLGVYGFYEAVDYTPSRvplgknHAIVRTFMAHHQGMSLLAFEHaLLNRPMQRRFMSAP 1531
Cdd:pfam10091 159 YLYELGdqLYGRYGFYDAFNPTFND------GWYSKDYLGIDQGPILLMIEN-YRTGLLWKLFMSHP 218
|
|
| CBM_X |
smart01068 |
Putative carbohydrate binding domain; |
1573-1621 |
1.71e-23 |
|
Putative carbohydrate binding domain;
Pssm-ID: 215008 [Multi-domain] Cd Length: 62 Bit Score: 95.72 E-value: 1.71e-23
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1099334132 1573 MRVFTDPNTPTPEVHLLSNGRYHVMATNAGGGYSRWRDLAVTRWREDAT 1621
Cdd:smart01068 14 VRTLDGPDTPAPWINVLSNGRYGVMVSASGSGYSRWADNSLTRWRNDPV 62
|
|
| GH94N_like |
cd11746 |
N-terminal domain of glycoside hydrolase family 94 and related domains; The glycoside ... |
1629-1836 |
4.06e-22 |
|
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: 96.04 E-value: 4.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 1629 IYLRDRDTGRYWSTAYQPTLRKADHYEAIFVQARAEyrRRDQSIEAHTEIGVSPEDDVEIRRVTLTNLASRTRQIEVTSY 1708
Cdd:cd11746 1 FYFYLSDDGDKWSLGWQPVRREAEHYEVRLGYVTFE--NEYNGIEAETTIFVPPDDPGEIQRVKLTNTGDRPRELTLFPY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 1709 AEVVFaplnadlahrtFSNLFVQTEILSDRQAILCTRRPRTP-GEQVpwmfhllaapgaiadePSYETDR--AKFIGRGR 1785
Cdd:cd11746 79 FEWCL-----------PDALFQGTSYDPEGGAVNCTTYYSYNiGARP----------------AFYATSFkpDDFDGDGG 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1099334132 1786 TAV-NPVVLDSpgspLTLSNTDGSVLDPIVAIRCSIILSADESATVQIISGV 1836
Cdd:cd11746 132 RTLaNPLAVVA----GQLSNTVGRVEDPIAALAIRFALEPGESKRYTFALGI 179
|
|
| GH94N_CBP_like |
cd11754 |
N-terminal domain of cellobiose phosphorylase (CBP) and similar proteins; The glycoside ... |
1575-1861 |
1.38e-20 |
|
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: 95.00 E-value: 1.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 1575 VFTDPNTPTPEVHLLSNGRYHVMATNAGGGYSRWRD---LAVTRWR-EDATSDCWGTFIYLRDRDTgrYWSTAYQPTLRK 1650
Cdd:cd11754 14 VITTPDTPLPWINYLGSEDFFSLISNTAGGYSFYKDarlRRLTRYRyNNVPLDNGGRYFYIKDGGT--VWNPGWKPVKTP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 1651 ADHYEA-------IFVQARaeyrrrdQSIEAHTEIGVSPEDDVEIRRVTLTNLASRTRQIEVTSYAEvvFAPLNA--DLA 1721
Cdd:cd11754 92 LDSYECrhglgytRITGEK-------NGIEAEVLYFVPLGENAEIWRLTLTNTSDSPKKLKLFSFVE--FCLWNAldDMT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 1722 H--RTFSN---------LFVQTEIlsdRQailctRRPRtpgeqvpwmFHLLAAPGAIAdepSYETDRAKFIGRGRTAVNP 1790
Cdd:cd11754 163 NfqRNLSTgevevegsvIYHKTEY---RE-----RRNH---------YAFFAVNAPID---GFDTDRDAFLGLYNGFDEP 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 1791 -VVLDspGSPltlSNTDGSVLDPIVAIRCSIILSADESATVQIISGVAE-------------TREAALALLDKYCDRHFV 1856
Cdd:cd11754 223 qAVLE--GKS---TNSVAHGWSPIGSHHVELTLAPGESKELIFVLGYVEnpddekwespgviNKKPAKELIERFATPEAV 297
|
....*
gi 1099334132 1857 ERAFE 1861
Cdd:cd11754 298 DAAFA 302
|
|
| CBM_X |
smart01068 |
Putative carbohydrate binding domain; |
2067-2131 |
5.20e-20 |
|
Putative carbohydrate binding domain;
Pssm-ID: 215008 [Multi-domain] Cd Length: 62 Bit Score: 85.71 E-value: 5.20e-20
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1099334132 2067 NGLGGFTPDGREYVITLDpGQSTPAPWVNVIASPYIGTVVSESGSAYT-WVENAhefrLTTWHNDP 2131
Cdd:smart01068 1 NGLGGFDDDGREYVRTLD-GPDTPAPWINVLSNGRYGVMVSASGSGYSrWADNS----LTRWRNDP 61
|
|
| GH94N_like |
cd11746 |
N-terminal domain of glycoside hydrolase family 94 and related domains; The glycoside ... |
2141-2329 |
1.19e-18 |
|
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: 86.02 E-value: 1.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 2141 YIRDEETGAFWSPTPLPARGR--SGYVCRHgfgYSVFEHYEAGISSELFTYVAMDAPVKFAVVKLRNHSRRPRRLSLTGY 2218
Cdd:cd11746 2 YFYLSDDGDKWSLGWQPVRREaeHYEVRLG---YVTFENEYNGIEAETTIFVPPDDPGEIQRVKLTNTGDRPRELTLFPY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 2219 WelvlgEWRHSNLMNIVTETDLHSGALFARNAYGRECANRVFFLqvseverTVTGNRTEFIGRNG-SLSSPAAMRRKGLS 2297
Cdd:cd11746 79 F-----EWCLPDALFQGTSYDPEGGAVNCTTYYSYNIGARPAFY-------ATSFKPDDFDGDGGrTLANPLAVVAGQLS 146
|
170 180 190
....*....|....*....|....*....|..
gi 1099334132 2298 GRKGAGLDPCAAIQTQIELADGQEREIVFVFG 2329
Cdd:cd11746 147 NTVGRVEDPIAALAIRFALEPGESKRYTFALG 178
|
|
| GH94N_NdvB_like |
cd11748 |
Glycoside hydrolase family 94 N-terminal-like domain of NdvB-like proteins; The glycoside ... |
2137-2344 |
2.22e-14 |
|
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: 76.59 E-value: 2.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 2137 GEALYIRDEETGAFWS----PTPLPARGRSGYVCRHGFGYSVFEHyeaGISSELFTYVAMDAPVKFAVVKLRNHSRRPRR 2212
Cdd:cd11748 75 GRFFYVKDEDTGELFSapyePVRRPPDSFAFSVGKNDIRWVVEQD---GLEVELTLSLPVDDPAELWEVKVRNLSDRARK 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 2213 LSLTGY-------WELVLGEWRHsNLMNIVTE--TDLHSGALFARNAYGRECanrVFFLQvsevERTVTG---NRTEFIG 2280
Cdd:cd11748 152 LSLYPYfpvgymsWMNQSARYDE-GLNAIVASsvTPYQKVEDYFKNKDLKDK---TFLLA----DRKPDSweaRQEAFEG 223
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1099334132 2281 RnGSLSSPAAMRRKGLSGRKGAGLDPCAAIQTQIELADGQEREIVFVFGAARSTDEAQHLIQRF 2344
Cdd:cd11748 224 E-GGLHNPSALQAPTLANGDARYETPAAVMQYRLTLDPGETEQYRFVFGPAKDEAEIAQLRARY 286
|
|
| GH94N_like_3 |
cd11750 |
Glycoside hydrolase family 94 N-terminal-like domain of uncharacterized function; The ... |
2070-2338 |
4.56e-10 |
|
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: 63.27 E-value: 4.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 2070 GGFTPDGREYVITlDPgqSTPAPWVNVIASPYIGTVVSESGSAYTWVENAHEFRLTTWHND-PLSDSSGEALYIR--DEE 2146
Cdd:cd11750 2 GYFDDANKEYVIT-TP--KTPIKWINYVGTLDFGGFVDHTGGSLVCKGDPALNRITKYIAQlPSSDFKGSTIYIRvkDGD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 2147 TGAFWSPTPLPARGR-SGYVCRHGFGYSVFEHYEAGISSELFTYVAMDAPVKFAVVKLRNHSRRPRRLSLtgyweLVLGE 2225
Cdd:cd11750 79 NYKIFSPFYVPTLDKyDKYECHVGLGYSRIIAEAYGIRTEITIFVPEGDQVLLQDIKVTNIRDKPVEVDV-----IPVVE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 2226 WRHSNLMNIVTETD-----LHSGALFARNAYG--RECAnrvfFLQVSEVERTVTGN---------RTEFIGRN--GSLSS 2287
Cdd:cd11750 154 YTHFDALKQLTNADwvpqtMTSKAHQEENGHTvlEQYA----FMKRDYAVNYFTSNrpvssfegdRRSFLGQNeyGTWAN 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1099334132 2288 PAAMRRKGLSGRKGAGLDPCAAIQTQI-ELADGQEREIVFVFGAARSTDEAQ 2338
Cdd:cd11750 230 PLSLQNDELSNYECLRGDNIGALMHHLgWLAPGETKRVITQLGQEESLKAAQ 281
|
|
| GH94N_NdvB_like |
cd11748 |
Glycoside hydrolase family 94 N-terminal-like domain of NdvB-like proteins; The glycoside ... |
1626-1861 |
1.38e-09 |
|
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: 61.95 E-value: 1.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 1626 GTFIYLRDRDTGRYWSTAYQPTLRKADHYEAIFVQARAEYRRRDQSIEAHTEIGVSPEDDVEIRRVTLTNLASRTRQIEV 1705
Cdd:cd11748 75 GRFFYVKDEDTGELFSAPYEPVRRPPDSFAFSVGKNDIRWVVEQDGLEVELTLSLPVDDPAELWEVKVRNLSDRARKLSL 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 1706 TSYAEVVFAplnadlahrtfSNLFVQTEILSDRQAILCtrRPRTPGEQVPWMF---HLLAAPGAIADEP--SYETDRAKF 1780
Cdd:cd11748 155 YPYFPVGYM-----------SWMNQSARYDEGLNAIVA--SSVTPYQKVEDYFknkDLKDKTFLLADRKpdSWEARQEAF 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 1781 IGRGRTAvNPVVLDSPgsplTLSNTDGSVLDPIVAIRCSIILSADESATVQIISGVAETrEAALALLDkycDRHFVERAF 1860
Cdd:cd11748 222 EGEGGLH-NPSALQAP----TLANGDARYETPAAVMQYRLTLDPGETEQYRFVFGPAKD-EAEIAQLR---ARYLGAEGF 292
|
.
gi 1099334132 1861 E 1861
Cdd:cd11748 293 E 293
|
|
| HomoserineK_II |
cd05153 |
Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a ... |
107-204 |
9.38e-05 |
|
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: 47.25 E-value: 9.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 107 PRIYDLA---LELISHMDGRVDSDNATQFVTAYQTAEPLKLGELWAFPIMLQLALlenLRRVALRIARRREERDVAITWa 183
Cdd:cd05153 211 PLLYDLAialNDWCFDDDGKLDPERAKALLAGYQSVRPLTEEEKAALPLLLRAAA---LRFWLSRLYDFHLPREGALVT- 286
|
90 100
....*....|....*....|.
gi 1099334132 184 drmlataEKEPKKLIQLLADF 204
Cdd:cd05153 287 -------PKDPDEFLRRLRQR 300
|
|
| COG5368 |
COG5368 |
Endo-beta-1,2-glucanase, glucoamylase superfamily [Carbohydrate transport and metabolism]; |
999-1114 |
1.88e-03 |
|
Endo-beta-1,2-glucanase, glucoamylase superfamily [Carbohydrate transport and metabolism];
Pssm-ID: 444138 [Multi-domain] Cd Length: 422 Bit Score: 43.63 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 999 RRTWRFFADFVGPQdNWLPPDNFQEYPAPASASRTSptniGMSLLANLAAYDFGYISAGEFLRLTGNTLATME-KLERYR 1077
Cdd:COG5368 34 RQTFRYFWEGANPV-SGLARDRSPSDDGDVASIAGT----GFGLMAIIVGVERGWITREEAVERTLKTLRFLEnKADRFH 108
|
90 100 110
....*....|....*....|....*....|....*..
gi 1099334132 1078 GHFYNWYDTRTLRPLHPRYVSSVDSGNLAGSLLTLQA 1114
Cdd:COG5368 109 GFFYHFLDGETGKRAWDDEGSLVDTAFLLQGLLTARE 145
|
|
| DUF3131 |
pfam11329 |
Protein of unknown function (DUF3131); This bacterial family of proteins has no known function. |
998-1105 |
2.24e-03 |
|
Protein of unknown function (DUF3131); This bacterial family of proteins has no known function.
Pssm-ID: 431818 Cd Length: 367 Bit Score: 43.02 E-value: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 998 ARRTWRFFadfvgpQDNWLP----PDNFQEYPApasasrTSPTNIGMSLLANLAAYDFGYISAGEFLRLTGNTLATMEKL 1073
Cdd:pfam11329 3 ARAAWSYF------ERNYQPatglVNSVDGYPS------TTLWDQGSYLAALVAARSLGLIPAAEFDQRLRKFLGTLAKL 70
|
90 100 110
....*....|....*....|....*....|...
gi 1099334132 1074 ERYRGHFYN-WYDTRTLRPlhpryvssVDSGNL 1105
Cdd:pfam11329 71 PLFDGELPNkVYNTRTLQM--------VDYGNN 95
|
|
| SrkA |
COG2334 |
Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal ... |
107-192 |
9.56e-03 |
|
Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal transduction mechanisms]; Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist is part of the Pathway/BioSystem: Threonine biosynthesis
Pssm-ID: 441905 [Multi-domain] Cd Length: 297 Bit Score: 40.68 E-value: 9.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1099334132 107 PRIYDLALELISHMDGRVDSDNATQFVTAYQTAEPLKLGELWAFPIMLQLALLenlrRVALRIARRREERDVAI-TWADR 185
Cdd:COG2334 211 PRLYDLAIALNGWADGPLDPARLAALLEGYRAVRPLTEAELAALPPLLRLRAL----RFLAWRLRRVRAKDPAFeRYLRR 286
|
....*..
gi 1099334132 186 MLATAEK 192
Cdd:COG2334 287 QIALAWA 293
|
|
| |
