|
Name |
Accession |
Description |
Interval |
E-value |
| COG3459 |
COG3459 |
Cellobiose phosphorylase [Carbohydrate transport and metabolism]; |
1-810 |
0e+00 |
|
Cellobiose phosphorylase [Carbohydrate transport and metabolism];
Pssm-ID: 442682 [Multi-domain] Cd Length: 794 Bit Score: 1164.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526256126 1 MKYGFFDDANQEYVIHTPQTPYPWINYLGNERFFGLISNTGGGYAFYRDARLRRLTRYRYNNIpVDNGGRYFYIYDD--G 78
Cdd:COG3459 1 NGYGGFDDDGREYVITGPDTPAPWINVLANPDFGFLVSETGGGYSWYKNSRENRLTRWRNDPV-SDPPGEYFYLRDEetG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526256126 79 DYWTPGWMPVKRELEQYECRHGLGYTSIMGERRGIRATQLAFVPLSFDGEVHQVKLQNTSLQTKKIKLFSFVEFCLWNAY 158
Cdd:COG3459 80 DYWSPTWQPVRKPLDEYECRHGFGYTRFEHEYNGIESELTYFVPLDDPVEIWRLKLTNTSDRPRRLSVTSYVEWVLGNAR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526256126 159 DDMTNFQRNLNTGEVEIQDSVIYHKTEYRERRN-HYAFFDANRPLAGYDTDCEAFLGLYNGLDQPQTITAGQASNSIASG 237
Cdd:COG3459 160 DDTANFQVTLSTGEVDPEGGAILARNPYNERFNgRVAFFAVSEPVSSFTGDREEFLGRYGSLANPAALERGKLSNSVGAG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526256126 238 WSPIGSHCIEITLEPGEETSCNFVLGYVENPEEekwespgiinkkrAHAMIAQFADETDVERALSELRSYWNDLLSKYTL 317
Cdd:COG3459 240 LDPCAALQVDIELAPGEEKELVFLLGQGENKEE-------------ARALIARYRDPDAVDAALAEVKAYWDELLGAVQV 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526256126 318 QSHDDKLNRMVNIWNPYQCMVTFNLSRSAsYFESGigRGMGFRDSNQDLLGFVHQIPERARERIIDIASTQFENGGAYHQ 397
Cdd:COG3459 307 ETPDPALDLMVNGWLLYQTLACRLWARSA-FYQSG--GAYGFRDQLQDSMALVHARPELAREQILLAASRQFPEGDVQHW 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526256126 398 YQPLTKKGNHevgGGFNDDPLWLIVGTSAYIKETGDFGILDEQVPFD----------------GNVDRAASLFEHLKRSF 461
Cdd:COG3459 384 WHPPTGRGVR---TRFSDDLLWLPYAVAAYIKETGDFSILDEVVPFLdgpplppgeedaydlpTVSGEEATLYEHCKRAI 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526256126 462 YHVVDNLGPHGLPLIGRADWNDCLNLNCFsatpdesyqttqnlEGRiAESVFIAGLFVYTGPDFIELCKRRGLNEEAATA 541
Cdd:COG3459 461 DFSLNRLGPHGLPLIGRGDWNDGMNLVGE--------------GGK-GESVWLAWFLYYALKEFAPLAEARGDEERAERY 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526256126 542 QAHVDRMRTATLEHGFDGEWFLRAYDHYGNKIGSKDCEEGQIFIEPQGFCVMAGIGVKEgLAHKALDSTRDRLETPYG-- 619
Cdd:COG3459 526 RAEAEELREAIEKHAWDGEWYRRAYFDDGTPLGSKENEECKIDLIAQSWAVLSGAADPE-RARKAMDSVDKYLVTEYGgl 604
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526256126 620 IVLQHPPYSRYYMNLGEISSYPPGYKENAGIFCHNNPWIMMAEAVIGRGDRAFELYSKIAPAYLEDISDIHRTEPYVYAQ 699
Cdd:COG3459 605 ILLLTPPFDKYDPDPGYIKGYPPGVRENGGQYTHAAPWAIMAEALLGDGDRAYELYSMINPINHNDEADRYKVEPYVYAA 684
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526256126 700 MIAGKDaVREGEAKNSWLTGTAAWNFIAITQSILGIQPEWDGLRIDPCIPKSWGEFTVTRVFRGDTYVIHITNPQHVSKG 779
Cdd:COG3459 685 DVYGVD-PHFGRGGWSWYTGSAGWMYRAATEYILGIRPEGDGLRIDPCIPSDWPGFSVTRRFRGAVYHITVKNPDGVSKG 763
|
810 820 830
....*....|....*....|....*....|.
gi 1526256126 780 VATVTVDGTVLTNNILPVAGDGTIHQVKVLL 810
Cdd:COG3459 764 VKSITVDGKPIEGNLIPLVDDGKEHEVEVVL 794
|
|
| Glyco_hydro_36 |
pfam17167 |
Glycosyl hydrolase 36 superfamily, catalytic domain; This is the catalytic region of the ... |
307-736 |
0e+00 |
|
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: 589.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526256126 307 YWNDLLSKYTLQSHDDKLNRMVNIWNPYQCMVTFNLSRSASYFESGIGRGMGFRDSNQDLLGFVHQIPERARERIIDIAS 386
Cdd:pfam17167 1 YWDSRLEKFQVKTPDESLDTMINIWNLYQCEICFVWSRFASFIESGGRTGYGFRDTAQDIIGVPHMNPEMTRKRILDLAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526256126 387 TQFENGGAYHQYQPL--------------TKKGNHEVGG---GFNDDPLWLIVGTSAYIKETGDFGILDEQVPFDGNvdR 449
Cdd:pfam17167 81 GQFKAGYGLHLFDPDwddikpsksptvlpTPYDNDKIHGigdTCSDDHLWLVPTIEAYVKETGDFSFLDEVIPYSDG--K 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526256126 450 AASLFEHLKRSFYHVVDNLGPHGLPLIGRADWNDCLNLNCfsatpdesyqttqnlegriAESVFIAGLFVYTGPDFIELC 529
Cdd:pfam17167 159 KATVYEHLKKAIDFSLEYLGQHGIPLGGRADWNDCLNLGG-------------------GESVFVSFLLYLALQEFIEIA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526256126 530 KRRGLNEEAATAQAHVDRMRTATLEHGFDGEWFLRAYDHYGNKIGSKDCEEGQIFIEPQGFCVMAGIGvKEGLAHKALDS 609
Cdd:pfam17167 220 KFKGDDEDAEWYEKMADKVREAIEKYAWDGEWYIRAYTKDGDKIGSKQNEEGKIHLESQSWAVLSGIG-KDERAKKAMDS 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526256126 610 TRDRLETPYGIVLQHPPYSRYYMNLGEISSYPPGYKENAGIFCHNNPWIMMAEAVIGRGDRAFELYSKIAPAYLEDISDI 689
Cdd:pfam17167 299 VEKYLFTEYGLHLNQPPFSTPNLDIGFITRYYPGVKENGGIFCHPNPWVIVAETKLGRGDRAMKLYDAINPANQNDIIET 378
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1526256126 690 HRTEPYVYAQMIAGKDAVREGEAKNSWLTGTAAWNFIAITQSILGIQ 736
Cdd:pfam17167 379 RKAEPYVYAQFVMGKDHPDHGRANHPWLTGTAGWAYVAITEGILGLR 425
|
|
| GH94N_CBP_like |
cd11754 |
N-terminal domain of cellobiose phosphorylase (CBP) and similar proteins; The glycoside ... |
1-303 |
0e+00 |
|
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: 581.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526256126 1 MKYGFFDDANQEYVIHTPQTPYPWINYLGNERFFGLISNTGGGYAFYRDARLRRLTRYRYNNIPVDNGGRYFYIYDDGDY 80
Cdd:cd11754 1 MKYGHFDDENREYVITTPDTPLPWINYLGSEDFFSLISNTAGGYSFYKDARLRRLTRYRYNNVPLDNGGRYFYIKDGGTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526256126 81 WTPGWMPVKRELEQYECRHGLGYTSIMGERRGIRATQLAFVPLSFDGEVHQVKLQNTSLQTKKIKLFSFVEFCLWNAYDD 160
Cdd:cd11754 81 WNPGWKPVKTPLDSYECRHGLGYTRITGEKNGIEAEVLYFVPLGENAEIWRLTLTNTSDSPKKLKLFSFVEFCLWNALDD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526256126 161 MTNFQRNLNTGEVEIQDSVIYHKTEYRERRNHYAFFDANRPLAGYDTDCEAFLGLYNGLDQPQTITAGQASNSIASGWSP 240
Cdd:cd11754 161 MTNFQRNLSTGEVEVEGSVIYHKTEYRERRNHYAFFAVNAPIDGFDTDRDAFLGLYNGFDEPQAVLEGKSTNSVAHGWSP 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1526256126 241 IGSHCIEITLEPGEETSCNFVLGYVENPEEEKWESPGIINKKRAHAMIAQFADETDVERALSE 303
Cdd:cd11754 241 IGSHHVELTLAPGESKELIFVLGYVENPDDEKWESPGVINKKPAKELIERFATPEAVDAAFAE 303
|
|
| CBM_X |
smart01068 |
Putative carbohydrate binding domain; |
1-49 |
1.87e-15 |
|
Putative carbohydrate binding domain;
Pssm-ID: 215008 [Multi-domain] Cd Length: 62 Bit Score: 71.07 E-value: 1.87e-15
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1526256126 1 MKYGFFDDANQEYVIH--TPQTPYPWINYLGNERFFGLISNTGGGYAFYRD 49
Cdd:smart01068 1 NGLGGFDDDGREYVRTldGPDTPAPWINVLSNGRYGVMVSASGSGYSRWAD 51
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| COG3459 |
COG3459 |
Cellobiose phosphorylase [Carbohydrate transport and metabolism]; |
1-810 |
0e+00 |
|
Cellobiose phosphorylase [Carbohydrate transport and metabolism];
Pssm-ID: 442682 [Multi-domain] Cd Length: 794 Bit Score: 1164.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526256126 1 MKYGFFDDANQEYVIHTPQTPYPWINYLGNERFFGLISNTGGGYAFYRDARLRRLTRYRYNNIpVDNGGRYFYIYDD--G 78
Cdd:COG3459 1 NGYGGFDDDGREYVITGPDTPAPWINVLANPDFGFLVSETGGGYSWYKNSRENRLTRWRNDPV-SDPPGEYFYLRDEetG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526256126 79 DYWTPGWMPVKRELEQYECRHGLGYTSIMGERRGIRATQLAFVPLSFDGEVHQVKLQNTSLQTKKIKLFSFVEFCLWNAY 158
Cdd:COG3459 80 DYWSPTWQPVRKPLDEYECRHGFGYTRFEHEYNGIESELTYFVPLDDPVEIWRLKLTNTSDRPRRLSVTSYVEWVLGNAR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526256126 159 DDMTNFQRNLNTGEVEIQDSVIYHKTEYRERRN-HYAFFDANRPLAGYDTDCEAFLGLYNGLDQPQTITAGQASNSIASG 237
Cdd:COG3459 160 DDTANFQVTLSTGEVDPEGGAILARNPYNERFNgRVAFFAVSEPVSSFTGDREEFLGRYGSLANPAALERGKLSNSVGAG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526256126 238 WSPIGSHCIEITLEPGEETSCNFVLGYVENPEEekwespgiinkkrAHAMIAQFADETDVERALSELRSYWNDLLSKYTL 317
Cdd:COG3459 240 LDPCAALQVDIELAPGEEKELVFLLGQGENKEE-------------ARALIARYRDPDAVDAALAEVKAYWDELLGAVQV 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526256126 318 QSHDDKLNRMVNIWNPYQCMVTFNLSRSAsYFESGigRGMGFRDSNQDLLGFVHQIPERARERIIDIASTQFENGGAYHQ 397
Cdd:COG3459 307 ETPDPALDLMVNGWLLYQTLACRLWARSA-FYQSG--GAYGFRDQLQDSMALVHARPELAREQILLAASRQFPEGDVQHW 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526256126 398 YQPLTKKGNHevgGGFNDDPLWLIVGTSAYIKETGDFGILDEQVPFD----------------GNVDRAASLFEHLKRSF 461
Cdd:COG3459 384 WHPPTGRGVR---TRFSDDLLWLPYAVAAYIKETGDFSILDEVVPFLdgpplppgeedaydlpTVSGEEATLYEHCKRAI 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526256126 462 YHVVDNLGPHGLPLIGRADWNDCLNLNCFsatpdesyqttqnlEGRiAESVFIAGLFVYTGPDFIELCKRRGLNEEAATA 541
Cdd:COG3459 461 DFSLNRLGPHGLPLIGRGDWNDGMNLVGE--------------GGK-GESVWLAWFLYYALKEFAPLAEARGDEERAERY 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526256126 542 QAHVDRMRTATLEHGFDGEWFLRAYDHYGNKIGSKDCEEGQIFIEPQGFCVMAGIGVKEgLAHKALDSTRDRLETPYG-- 619
Cdd:COG3459 526 RAEAEELREAIEKHAWDGEWYRRAYFDDGTPLGSKENEECKIDLIAQSWAVLSGAADPE-RARKAMDSVDKYLVTEYGgl 604
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526256126 620 IVLQHPPYSRYYMNLGEISSYPPGYKENAGIFCHNNPWIMMAEAVIGRGDRAFELYSKIAPAYLEDISDIHRTEPYVYAQ 699
Cdd:COG3459 605 ILLLTPPFDKYDPDPGYIKGYPPGVRENGGQYTHAAPWAIMAEALLGDGDRAYELYSMINPINHNDEADRYKVEPYVYAA 684
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526256126 700 MIAGKDaVREGEAKNSWLTGTAAWNFIAITQSILGIQPEWDGLRIDPCIPKSWGEFTVTRVFRGDTYVIHITNPQHVSKG 779
Cdd:COG3459 685 DVYGVD-PHFGRGGWSWYTGSAGWMYRAATEYILGIRPEGDGLRIDPCIPSDWPGFSVTRRFRGAVYHITVKNPDGVSKG 763
|
810 820 830
....*....|....*....|....*....|.
gi 1526256126 780 VATVTVDGTVLTNNILPVAGDGTIHQVKVLL 810
Cdd:COG3459 764 VKSITVDGKPIEGNLIPLVDDGKEHEVEVVL 794
|
|
| Glyco_hydro_36 |
pfam17167 |
Glycosyl hydrolase 36 superfamily, catalytic domain; This is the catalytic region of the ... |
307-736 |
0e+00 |
|
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: 589.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526256126 307 YWNDLLSKYTLQSHDDKLNRMVNIWNPYQCMVTFNLSRSASYFESGIGRGMGFRDSNQDLLGFVHQIPERARERIIDIAS 386
Cdd:pfam17167 1 YWDSRLEKFQVKTPDESLDTMINIWNLYQCEICFVWSRFASFIESGGRTGYGFRDTAQDIIGVPHMNPEMTRKRILDLAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526256126 387 TQFENGGAYHQYQPL--------------TKKGNHEVGG---GFNDDPLWLIVGTSAYIKETGDFGILDEQVPFDGNvdR 449
Cdd:pfam17167 81 GQFKAGYGLHLFDPDwddikpsksptvlpTPYDNDKIHGigdTCSDDHLWLVPTIEAYVKETGDFSFLDEVIPYSDG--K 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526256126 450 AASLFEHLKRSFYHVVDNLGPHGLPLIGRADWNDCLNLNCfsatpdesyqttqnlegriAESVFIAGLFVYTGPDFIELC 529
Cdd:pfam17167 159 KATVYEHLKKAIDFSLEYLGQHGIPLGGRADWNDCLNLGG-------------------GESVFVSFLLYLALQEFIEIA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526256126 530 KRRGLNEEAATAQAHVDRMRTATLEHGFDGEWFLRAYDHYGNKIGSKDCEEGQIFIEPQGFCVMAGIGvKEGLAHKALDS 609
Cdd:pfam17167 220 KFKGDDEDAEWYEKMADKVREAIEKYAWDGEWYIRAYTKDGDKIGSKQNEEGKIHLESQSWAVLSGIG-KDERAKKAMDS 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526256126 610 TRDRLETPYGIVLQHPPYSRYYMNLGEISSYPPGYKENAGIFCHNNPWIMMAEAVIGRGDRAFELYSKIAPAYLEDISDI 689
Cdd:pfam17167 299 VEKYLFTEYGLHLNQPPFSTPNLDIGFITRYYPGVKENGGIFCHPNPWVIVAETKLGRGDRAMKLYDAINPANQNDIIET 378
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1526256126 690 HRTEPYVYAQMIAGKDAVREGEAKNSWLTGTAAWNFIAITQSILGIQ 736
Cdd:pfam17167 379 RKAEPYVYAQFVMGKDHPDHGRANHPWLTGTAGWAYVAITEGILGLR 425
|
|
| GH94N_CBP_like |
cd11754 |
N-terminal domain of cellobiose phosphorylase (CBP) and similar proteins; The glycoside ... |
1-303 |
0e+00 |
|
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: 581.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526256126 1 MKYGFFDDANQEYVIHTPQTPYPWINYLGNERFFGLISNTGGGYAFYRDARLRRLTRYRYNNIPVDNGGRYFYIYDDGDY 80
Cdd:cd11754 1 MKYGHFDDENREYVITTPDTPLPWINYLGSEDFFSLISNTAGGYSFYKDARLRRLTRYRYNNVPLDNGGRYFYIKDGGTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526256126 81 WTPGWMPVKRELEQYECRHGLGYTSIMGERRGIRATQLAFVPLSFDGEVHQVKLQNTSLQTKKIKLFSFVEFCLWNAYDD 160
Cdd:cd11754 81 WNPGWKPVKTPLDSYECRHGLGYTRITGEKNGIEAEVLYFVPLGENAEIWRLTLTNTSDSPKKLKLFSFVEFCLWNALDD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526256126 161 MTNFQRNLNTGEVEIQDSVIYHKTEYRERRNHYAFFDANRPLAGYDTDCEAFLGLYNGLDQPQTITAGQASNSIASGWSP 240
Cdd:cd11754 161 MTNFQRNLSTGEVEVEGSVIYHKTEYRERRNHYAFFAVNAPIDGFDTDRDAFLGLYNGFDEPQAVLEGKSTNSVAHGWSP 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1526256126 241 IGSHCIEITLEPGEETSCNFVLGYVENPEEEKWESPGIINKKRAHAMIAQFADETDVERALSE 303
Cdd:cd11754 241 IGSHHVELTLAPGESKELIFVLGYVENPDDEKWESPGVINKKPAKELIERFATPEAVDAAFAE 303
|
|
| GH94N_ChBP_like |
cd11755 |
N-terminal domain of chitobiose phosphorylase (ChBP) and similar proteins; The glycoside ... |
1-303 |
2.09e-92 |
|
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: 292.22 E-value: 2.09e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526256126 1 MKYGFFDDANQEYVIHTPQTPYPWINYLGNERFFGLISNTGGGYAFYRDARLRRLTRYRYNNIPVDNGGRYFYIYD--DG 78
Cdd:cd11755 1 MKYGYFDDENREYVITRPDTPTPWTNYLGSGEYGAIISNNAGGYSFYKSPANGRITRFRFNSVPMDRPGRYVYLRDneSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526256126 79 DYWTPGWMPVKRELEQ--YECRHGLGYTSIMGERRGIRATQLAFVPLSFDGEVHQVKLQNTSLQTKKIKLFSFVEFCL-W 155
Cdd:cd11755 81 DYWSASWQPVGKPLDEykYECRHGTGYTTIESEYKGIAAETTYFVPLDQDYEIWDVKITNTSSRKRKLSVFSYAEFSFhW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526256126 156 NAYDDMTNFQRNLNTGEVEIQDSVIYHKTEYRERRNH-----YAFFD-ANRPLAGYDTDCEAFLGLYNGLDQPQTITAGQ 229
Cdd:cd11755 161 NAEQDQQNLQYSLYISRTSYKDGIIEYDNYYNLDDDPngderYRFFTsAGAEVDGFDGSRDRFIGPYRSESNPIAVERGK 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1526256126 230 ASNSIASGWSPIGSHCIEITLEPGEETSCNFVLGYVenpeeekwespgiiNKKRAHAMIAQFADETDVERALSE 303
Cdd:cd11755 241 CSNSLATGGNHCGALQSDITLAPGEEKEIIFILGVG--------------NREEGRAIRAKYSDPEAVDAEFEA 300
|
|
| Glyco_transf_36 |
pfam06165 |
Glycosyltransferase family 36; The glycosyltransferase family 36 includes cellobiose ... |
21-263 |
2.47e-92 |
|
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: 289.78 E-value: 2.47e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526256126 21 PYPWINYLGNERFFGLISNTGGGYAFYRDARLRRLTRYRyNNIPVDNGGRYFYIYDD--GDYWTPGWMPVKRELEqYECR 98
Cdd:pfam06165 1 PAPWINVLSNGDYGVLISNTGGGYSWYKNSRENRLTRWR-NDPVRDPPGEYIYIRDEesGEVWSPTWQPVRKPLD-YEVR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526256126 99 HGLGYTSIMGERRGIRATQLAFVPLSFDGEVHQVKLQNTSLQTKKIKLFSFVEFCLWNAYDDMTN--FQRNLNTGEVEI- 175
Cdd:pfam06165 79 HGLGYTRFEREDGGIETELTVFVPPEDPVEIRRLTLTNTSDRERRLSVTSYVEWVLGNAAADLAHpaFSRLFSQTEIVTe 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526256126 176 QDSVIYHKTEY-RERRNHYAFFDANRPLAGYDTDCEAFLGLYNGLDQPQTITAGQASNSIASGWSPIGSHCIEITLEPGE 254
Cdd:pfam06165 159 LGAILAARNPRsEEFRNRYAFHAVSGPVDSYETDREEFIGRGGSLANPAALERGPLSNSVGAGLDPCAALQVRIELAPGE 238
|
....*....
gi 1526256126 255 ETSCNFVLG 263
Cdd:pfam06165 239 TKEVVFILG 247
|
|
| GH94N_like_4 |
cd11751 |
Glycoside hydrolase family 94 N-terminal-like domain of uncharacterized function; The ... |
66-270 |
1.51e-48 |
|
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: 171.01 E-value: 1.51e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526256126 66 DNGGRYFYIYDD--GDYWTPGWMPVKRELEQYECRHGLGYTSIMGERRGIRATQLAFVPLSFDGEVHQVKLQNTSLQTKK 143
Cdd:cd11751 6 DNWGKYFYIRDDdtGEVWSATYKPLKTEPEDYECVHGIGYSEFTSEYNGIRSSLTVFVPKDDPVEIWSLTLRNTSDRERR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526256126 144 IKLFSFVEFCLWNAYDD---------MTNFQRNLNTGEVEiqdsvIYHKTEYRERRNHY-------AFFDANRPLAGYDT 207
Cdd:cd11751 86 LSVFSYFEWELGGFPDEhrefhklfiETSFDRELNGIYAR-----KYLWGFPDEKGRHNnrnwpyvAFHAASEPVVSYDG 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1526256126 208 DCEAFLGLYNGLDQPQTITAGQASNSIASGWSPIGSHCIEITLEPGEETSCNFVLGYVENPEE 270
Cdd:cd11751 161 DKESFIGMYGSEENPDAVAMGGLSNSVGRFEDAIGVLQHEVTLEPGEEKTIHFTLGAAESGEE 223
|
|
| GH94N_like |
cd11746 |
N-terminal domain of glycoside hydrolase family 94 and related domains; The glycoside ... |
70-264 |
1.16e-38 |
|
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: 141.87 E-value: 1.16e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526256126 70 RYFYIYDDGDYWTPGWMPVKRELEQYECRhgLGYTSIMGERRGIRATQLAFVPLSFDGEVHQVKLQNTSLQTKKIKLFSF 149
Cdd:cd11746 1 FYFYLSDDGDKWSLGWQPVRREAEHYEVR--LGYVTFENEYNGIEAETTIFVPPDDPGEIQRVKLTNTGDRPRELTLFPY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526256126 150 VEFCLWNAYddmtnfqrnLNTGEVEIQDSVIYHKTEYRE-RRNHYAFFDANRPLAGYDTDCEaflglyNGLDQPQTITAG 228
Cdd:cd11746 79 FEWCLPDAL---------FQGTSYDPEGGAVNCTTYYSYnIGARPAFYATSFKPDDFDGDGG------RTLANPLAVVAG 143
|
170 180 190
....*....|....*....|....*....|....*.
gi 1526256126 229 QASNSIASGWSPIGSHCIEITLEPGEETSCNFVLGY 264
Cdd:cd11746 144 QLSNTVGRVEDPIAALAIRFALEPGESKRYTFALGI 179
|
|
| GH94N_ChvB_NdvB_1_like |
cd11756 |
First GH94N domain of cyclic beta 1-2 glucan synthetase and similar domains; The glycoside ... |
3-270 |
4.03e-37 |
|
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: 140.72 E-value: 4.03e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526256126 3 YGFFDDANQEYVIHTPQ---TPYPWINYLGNERFFGLISNTGGGYAFYRdarlrrltryryN----------NIPV-DNG 68
Cdd:cd11756 8 YGGFSPDGREYVIVLGPgkrTPAPWINVIANPGFGFLVSESGSGYTWAE------------NsrenrltpwsNDPVsDPP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526256126 69 GRYFYIYDD--GDYWTPGWMPVkRELEQYECRHGLGYTSIMGERRGIRATQLAFVPLsfDGEVH--QVKLQNTSLQTKKI 144
Cdd:cd11756 76 GEALYLRDEetGEVWSPTPLPI-RGGGPYRVRHGFGYSRFEHRSHGIEQELTVFVPR--DDPVKisRLRLRNTSGRPRRL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526256126 145 KLFSFVEFCLWNAYDDMTNFqrnLNTGEVEIQDSVIYHKTEYRERRNHYAFFDANRPLAGYDTDCEAFLGLYNGLDQPQT 224
Cdd:cd11756 153 SVTYYAEWVLGVNREKTAPH---IVTEYDEETGALLARNPYNEDFGGRVAFLAVSGGPRSFTGDRREFIGRNGSLANPAA 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1526256126 225 ITAGQASNSIASGWSPIGSHCIEITLEPGEETSCNFVLGYVENPEE 270
Cdd:cd11756 230 LKRGRLSGRTGAGLDPCAALQVDLELAPGEEKEIVFLLGEADDAEE 275
|
|
| GH94N_like_3 |
cd11750 |
Glycoside hydrolase family 94 N-terminal-like domain of uncharacterized function; The ... |
3-272 |
1.43e-27 |
|
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: 113.34 E-value: 1.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526256126 3 YGFFDDANQEYVIHTPQTPYPWINYLGNERFFGLISNTGGGYAFYRDARLRRLTRYRYNNIPVDNGGRYFYIY--DDGDY 80
Cdd:cd11750 1 YGYFDDANKEYVITTPKTPIKWINYVGTLDFGGFVDHTGGSLVCKGDPALNRITKYIAQLPSSDFKGSTIYIRvkDGDNY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526256126 81 --WTPGWMPVKRELEQYECRHGLGYTSIMGERRGIRATQLAFVPLSFDGEVHQVKLQNTSLQTKKIKLFSFVEFCLWNAY 158
Cdd:cd11750 81 kiFSPFYVPTLDKYDKYECHVGLGYSRIIAEAYGIRTEITIFVPEGDQVLLQDIKVTNIRDKPVEVDVIPVVEYTHFDAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526256126 159 DDMTNF----QRNLNTGEVEIQDSVIYHKTEYRERRNHYAFFDANRPLAGYDTDCEAFLGL--YNGLDQPQTITAGQASN 232
Cdd:cd11750 161 KQLTNAdwvpQTMTSKAHQEENGHTVLEQYAFMKRDYAVNYFTSNRPVSSFEGDRRSFLGQneYGTWANPLSLQNDELSN 240
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1526256126 233 SIASGWSPIGSHCIEI-TLEPGEETSCNFVLGYVENPEEEK 272
Cdd:cd11750 241 YECLRGDNIGALMHHLgWLAPGETKRVITQLGQEESLKAAQ 281
|
|
| GH94N_ChvB_NdvB_2_like |
cd11753 |
Second GH94N domain of cyclic beta 1-2 glucan synthetase and similar domains; The glycoside ... |
14-301 |
1.26e-15 |
|
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: 79.10 E-value: 1.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526256126 14 VIHTPQTPYPWINYLGNERFFGLISNTGGGYAFYRDarlrrltryrynnIPV---------DNGGRYFYIYD--DGDYWT 82
Cdd:cd11753 52 RFTTPDTALPEVHLLSNGRYSVMLTASGSGYSRWND-------------LAVtrwredatrDNWGSFIYLRDvdSGKVWS 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526256126 83 PGWMPVKRELEQYECRHGLGYTSIMGERRGIRATQLAFVPLSFDGEVHQVKLQNTSLQTKKIKLFSFVEFCLWNAYDDMT 162
Cdd:cd11753 119 ATYQPTRDPPDEYEVVFSEDRAEFRRRDGGIETTTEVVVSPEDDAEIRRVTLTNLSRRPRELEVTSYAEVVLAPPAADEA 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526256126 163 N--FQrNL--NTGEVEIQDSVIYHkteyRERRNH-----YAFF------DANRPLaGYDTDCEAFLGLYNGLDQPQTITA 227
Cdd:cd11753 199 HpaFS-KLfvQTEFLPEQGALLAT----RRPRSPdepppWAAHfvavegEAVGPL-QYETDRARFIGRGRSLANPAAMDD 272
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1526256126 228 GQA-SNSIASGWSPIGSHCIEITLEPGEETSCNFVLGYVENPEEekwespgiinkkrAHAMIAQFADETDVERAL 301
Cdd:cd11753 273 GAPlSGTVGAVLDPIFSLRRRVRLPPGETARVTFVTGVADSREE-------------ALELADKYRDPSAVERAF 334
|
|
| CBM_X |
smart01068 |
Putative carbohydrate binding domain; |
1-49 |
1.87e-15 |
|
Putative carbohydrate binding domain;
Pssm-ID: 215008 [Multi-domain] Cd Length: 62 Bit Score: 71.07 E-value: 1.87e-15
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1526256126 1 MKYGFFDDANQEYVIH--TPQTPYPWINYLGNERFFGLISNTGGGYAFYRD 49
Cdd:smart01068 1 NGLGGFDDDGREYVRTldGPDTPAPWINVLSNGRYGVMVSASGSGYSRWAD 51
|
|
| GH94N_NdvB_like |
cd11748 |
Glycoside hydrolase family 94 N-terminal-like domain of NdvB-like proteins; The glycoside ... |
69-270 |
4.08e-07 |
|
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: 52.32 E-value: 4.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526256126 69 GRYFYIYDD--GDYWTPGWMPVKRELEQYECRHGLGYTSIMGERRGIRATQLAFVPLSFDGEVHQVKLQNTSLQTKKIKL 146
Cdd:cd11748 75 GRFFYVKDEdtGELFSAPYEPVRRPPDSFAFSVGKNDIRWVVEQDGLEVELTLSLPVDDPAELWEVKVRNLSDRARKLSL 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1526256126 147 FSF--VEFCLW----NAYDDmtnfqrNLNTgevEIQDSVI-YHKTEYRERRNHY---AFFDANRPLAGYDTDCEAFLGLy 216
Cdd:cd11748 155 YPYfpVGYMSWmnqsARYDE------GLNA---IVASSVTpYQKVEDYFKNKDLkdkTFLLADRKPDSWEARQEAFEGE- 224
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1526256126 217 NGLDQPQTITAGQASNSIASGWSPIGSHCIEITLEPGEETSCNFVLGYVENPEE 270
Cdd:cd11748 225 GGLHNPSALQAPTLANGDARYETPAAVMQYRLTLDPGETEQYRFVFGPAKDEAE 278
|
|
| |
