|
Name |
Accession |
Description |
Interval |
E-value |
| GalB |
NF041463 |
beta-galactosidase GalB; |
75-916 |
0e+00 |
|
beta-galactosidase GalB;
Pssm-ID: 469351 [Multi-domain] Cd Length: 799 Bit Score: 649.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 75 VNFDSAWKFAMGELPGASERNYDDSSWKTLNLPHDFSLKQDYTQSGEAESGYKLG-----GIGWYRKTFSVNETIAKGRV 149
Cdd:NF041463 4 ISINDGWRFHKGDPAGAADADFDDSGWEQVTLPHDWAIAGPFYKGGPAEVGGGMGrlpswGVAWYRKKLDIPASDAGKSI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 150 YLKFDGSYMETEVFVNGHSLGVHPNGYTSFTFDVTKYLKVGEENTIAIKVTNKIPSSRWYSGSGIYRSLQLVFTPAVHLA 229
Cdd:NF041463 84 FLDIDGAMSYAMVWLNGQLVGGWPYGYNSWRLDLTPYLKPGGENQLAIRLDNPPESSRWYPGGGLYRNVWLTKTNPVHVA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 230 DNGIVMKTPDLSQTAqsgtgSQVHVTAKVYNQSGNASQIRVKSILYERKEDGSLGQKAAESELSQPVDVKSGEQVPVNQQ 309
Cdd:NF041463 164 QWGTFVTTPEVSADS-----ATVDLAVTVDNDSAADADVEVSTEIYALDADGKRTGKAVARFAPASLTVAAGESATVSGS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 310 FSIVKPKLWSP---DNPTLYVLRTELYQNGQKIQTVDQETGFRYTSFNSETGFSLNGQTMKLKGVSMHHDQGALGSAAYY 386
Cdd:NF041463 239 LTIANPRLWGPpptQTPNRYVAVTTVYQGGKVVDRYETPFGIRSLRFDPDRGVLVNGEHIRLQGVNQHHDLGALGAAFNV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 387 NAIERQVSILKRMGVNAIRVTHNPASRALKDIANRMGMLLIDEAFDGWRDYKngNTYDYTRFFdkkignsveglsnvesP 466
Cdd:NF041463 319 RAAERQLEILREMGCNAIRMAHNPPAPELLELTDRMGFLVVDEIFDSWERKK--TPLDFHLIF----------------P 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 467 DqtWAEYHIKQMVRSGINDPSIIMWSTGNEVTE-GTSKASAgtypQLIAQLINWIDQVDGTRPATLGDNYLKNrdttsvG 545
Cdd:NF041463 381 D--WHEQDLRAMIRRDRNHPSVIMWSIGNEVGEqYTGEAGA----AIARRLHDIVKEEDPTRPTTASMNYAKP------D 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 546 MAnaltnnkLQGVV---GYNY--ANGR---------------QYDKGHELNPNWFIYGSETASSINSRGVYNVKNQEQRS 605
Cdd:NF041463 449 MP-------FPAVMdviSLNYqgEGIRdapayeglkgirtppLYPAFHAKFPDKVILSSETASALSSRGEYLFPVTPGIS 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 606 ------------DKQLSSYDQSKVGWGHLASEAWYDVIKRDFVAGEFVWTGFDYLGEPTPWngigsgsvgtWPApKSSYF 673
Cdd:NF041463 522 apvrdgrggdpvTHQVSAYELYAADFGSSADKVFAAQDQHPYVAGEFVWTGWDYLGEPTPY----------YSS-RSSYS 590
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 674 GIVDTAGFPKDSYYFYQSQWNQKVKTLHVLPG-TWNEslikKEGGKVEVAVYSNAAKVKLVhVSDKGvetdLGTKaftkv 752
Cdd:NF041463 591 GIIDLAGFPKDRFYLYQSRWRPELPMAHILPHwNWPG----REGQVTPVHVFTSGDEAELF-LNGKS----LGRK----- 656
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 753 tTKAGHSYQiykgndkqaaehknlyLTW-KVPYKKGYLRAIAYDeNGKVInkteGRKEVKMAGKATKLAAKLE-SKVDSK 830
Cdd:NF041463 657 -KKGPYEYR----------------LRWdDVVYEPGELKVVAYK-NGKPW----AEDTVKTAGAAAKLQLTADrATIAAD 714
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 831 VTDhsLAYVGVDVQDAKGNLVTDANNKVEFSVSGPAKLVGVDNGNAVDHQSYQDTNRKAFSGKVLAIVKMT-GKSGTVTV 909
Cdd:NF041463 715 GKD--LSFVTVRVTDKDGLLVPRADNRLRFSIEGPGEIVATDNGDPTDLEPFPSPERNAFNGLALAIVRAKpGQAGKITV 792
|
....*..
gi 2461862307 910 TAKSKGL 916
Cdd:NF041463 793 TAESDGL 799
|
|
| GalA |
NF041462 |
beta-galactosidase GalA; |
78-923 |
0e+00 |
|
beta-galactosidase GalA;
Pssm-ID: 469350 [Multi-domain] Cd Length: 757 Bit Score: 620.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 78 DSAWKFAMGELP----------------------GASERNYDDSSWKTLNLPHDFSLKQDYTQSGEAESGYKLGGIGWYR 135
Cdd:NF041462 1 DFGWRFHLGDIAdpakdfhfgtdqytfakagnawGAAAPDFDDSDWRSVDLPHDWAVELPFVPDANASHGYKPRGIGWYR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 136 KTFSVNETIAKGRVYLKFDGSYMETEVFVNGHSLGVHPNGYTSFTFDVTKYLKVGEENTIAIKVTNKIPSSRWYSGSGIY 215
Cdd:NF041462 81 RTFDLPASDRGKRIELEFDGVFRNATVWVNGSVVGRNWSGYTSFRIDITDFLRYGDENVIAVRVDATAGEGWWYEGAGIY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 216 RSLQLVFTPAVHLADNGIVMKtpdlsqTAQSGTGSQVHVTAKVYNQSGNASQIRVKSILYERKedgslGQKAAESElSQP 295
Cdd:NF041462 161 RHVWLVKTDPVHIATDGVFVR------PRLDGGRATVPVETTLANEGDAAATVRVESTLLDPD-----GRVVATAE-SAP 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 296 VDVKSGEQVPVNQQFSIVKPKLWSPDNPTLYVLRTELYQNGQKIQTVDQETGFRYTSFNSETGFSLNGQTMKLKGVSMHH 375
Cdd:NF041462 229 LSVAALETATVTQTLPVANPALWSVETPYLYTLVTTVLVDGKVVDEVVTPFGFRTIRFDADKGFFLNGKPVKLKGVCNHQ 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 376 DQGALGSAAYYNAIERQVSILKRMGVNAIRVTHNPASRALKDIANRMGMLLIDEafdgwrdykngntydyTRFFdkkiGN 455
Cdd:NF041462 309 DHAGVGVAVPDALQEWRLRRLKEMGCNAYRTSHNPPTPELLDACDRLGMLVMDE----------------NRLF----NS 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 456 SVEGLSNVESpdqtwaeyhikqMVRSGINDPSIIMWSTGNEvtEGTSKASAGTypQLIAQLINWIDQVDGTRPATLGdny 535
Cdd:NF041462 369 SPEYLAQLEW------------MVRRDRNHPSIILWSVGNE--EPMQGTEQGA--RIVRRMVALVKRLDPTRPVTAA--- 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 536 lKNRDTTSVGMANALTnnklqgVVGYNYANGrQYDKGHELNPNWFIYGSETASSINSRGVYnvknqeqRSDKQ---LSSY 612
Cdd:NF041462 430 -MNGGFFGEGVSDVVD------VVGFNYRTG-NYDKFHAAHPNKPIIGSETASAVSTRGEY-------ATDKAkhvVSSY 494
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 613 DQSKVGWGHLASEAWYDVIKRDFVAGEFVWTGFDYLGEPTPWNgigsgsvgtWPApKSSYFGIVDTAGFPKDSYYFYQSQ 692
Cdd:NF041462 495 DTEAPSWGSTAEEWWKFIAERPFLAGGFVWTGFDYRGEPTPYE---------WPS-VSSQFGIMDLCGFPKDAYYYYRAW 564
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 693 WnQKVKTLHVLPgTWNESLikKEGGKVEVAVYSNAAKVKLVhVSDKgvetDLGtkaftkvttkaghsyqiykgndKQAAE 772
Cdd:NF041462 565 W-RDEPVLHLFP-HWNWPG--KEGQPIKVWVYSNADEVELF-LNGK----SLG----------------------RQKVD 613
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 773 HkNLYLTWKVPYKKGYLRAIAYdENGKVINKTegrkEVKMAGKATKLaaKLESKVDSKVTDHS-LAYVGVDVQDAKGNLV 851
Cdd:NF041462 614 R-NGHLEWSVPYAPGRLEARGY-RGGKVVLTE----VVETTGAPAAL--RLTPDRTVLAADGEdVAVVTVEAVDAKGRHV 685
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2461862307 852 TDANNKVEFSVSGPAKLVGVDNGNAVDHQSYQDTNRKAFSGKVLAIVKMTGKSGTVTVTAKSKGLTTSTVTF 923
Cdd:NF041462 686 PTADNLVRFSVSGPGRIIGVGNGDPNSHEPDKAPQRSLFNGLAQVIVQSTKGAGAITLTATAEGLKPATLVI 757
|
|
| LacZ |
COG3250 |
Beta-galactosidase/beta-glucuronidase [Carbohydrate transport and metabolism]; |
81-806 |
1.44e-129 |
|
Beta-galactosidase/beta-glucuronidase [Carbohydrate transport and metabolism];
Pssm-ID: 442481 [Multi-domain] Cd Length: 638 Bit Score: 422.63 E-value: 1.44e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 81 WKFAMGELPGASERNYDDSSWKTLNLPHDFSLKQDYTQSGEAESGYKLGGIGWYRKTFSVNETIAKGRVYLKFDGSYMET 160
Cdd:COG3250 3 WKFRLGDAPEGAKPDFDDSGWDPITVPGDWELDLYGLPDPFVGPWYLYNGVGWYRRTFTVPASWKGKRVFLHFEGVDTAA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 161 EVFVNGHSLGVHPNGYTSFTFDVTKYLKVGEeNTIAIKVTN-----KIPSSRWYSGSGIYRSLQLVFTPAVHLADNGIvm 235
Cdd:COG3250 83 EVWVNGKKVGYHEGGFTPFEFDITDYLKPGE-NVLAVRVDNpsdgsYLEGQDWWRTSGIYRDVWLEATPKVHIEDVFV-- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 236 kTPDLSqtAQSGTgsqVHVTAKVYNQSGNASQIRVKsiLYERKedgslGQKAAESElsQPVDVKSGEQVPVNQQFSIVKP 315
Cdd:COG3250 160 -TPDLD--DGSAT---LTVEVELENESDAGVTVEVT--LLDAD-----GKVVATAT--AKVTLAAGEENTVTLTLTVPNP 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 316 KLWSPDNPTLYVLRTELYQNGQKIQTVDQETGFRYTSFNSETGFSLNGQTMKLKGVSMHHDQGALGSAAYYNAIERQVSI 395
Cdd:COG3250 225 KLWSPEDPNLYTLVVTLKDDGKVVDTVSTRFGFRTIEIDGDGGFLLNGKPVFLKGVNRHEDWPDDGRAVTDEAMRRDLEL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 396 LKRMGVNAIRVTHNPASRALKDIANRMGMLLIDEAFDGWRDykngnTYDYTRFFDKkignsveglsnvespdqtWAEYHI 475
Cdd:COG3250 305 MKEAGFNAVRTSHYPEDPEFYDLCDELGLLVWDEAPFEWHG-----MLGDDPEFLE------------------AVEAEL 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 476 KQMVRSGINDPSIIMWSTGNEVTEGTSkasagtypqlIAQLINWIDQVDGTRPatlgdnylknrdttsvgmanaltnnkl 555
Cdd:COG3250 362 REMVRRDRNHPSIILWSGGNESGGGPN----------FAALYEWVKELDPTRP--------------------------- 404
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 556 qgvvgynyangrqydkghelnpnwFIYGSETASSI-NS-RGVYNVKNQEQRSdkQLSSYDQskvgwghlasEAWYDVIKR 633
Cdd:COG3250 405 ------------------------VRFLSEYGHAMpNSlGGGYHQPSDFEEY--QALQALE----------EYWEAFRRR 448
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 634 DFVAGEFVWTGFDYLGEPTPWNGigsgsvgtwpapKSSYFGIVD-TAGFPKDSYYFYQSQWNQKV---KTLHVLPGTWNE 709
Cdd:COG3250 449 PRLAGGFIWQLNDYWPEPRDNDG------------NFCSWGLVDyYDRTPKPAYYEVKSAWQPVLvsdGMLHILLPHWND 516
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 710 slikkegGKVEVAVYSNAAKVKLVHVSDKGVETDLGTKAFTKVTTKAGHSYQIYKGNDKQAAEHKNLYLTWKVPYKKGYL 789
Cdd:COG3250 517 -------GKEGELPYSSTVADLYTPYVRPQENGNRTDVRWLTLTNGKGKGLLVSGVPLLSGSALAYLTEDLLAAKEEGLL 589
|
730
....*....|....*..
gi 2461862307 790 RAIAYDENGKVINKTEG 806
Cdd:COG3250 590 LAADLTTLLLDLADLGG 606
|
|
| GH20_DspB_LnbB-like |
cd06564 |
Glycosyl hydrolase family 20 (GH20) catalytic domain of dispersin B (DspB), lacto-N-biosidase ... |
1600-1938 |
3.14e-92 |
|
Glycosyl hydrolase family 20 (GH20) catalytic domain of dispersin B (DspB), lacto-N-biosidase (LnbB) and related proteins. Dispersin B is a soluble beta-N-acetylglucosamidase found in bacteria that hydrolyzes the beta-1,6-linkages of PGA (poly-beta-(1,6)-N-acetylglucosamine), a major component of the extracellular polysaccharide matrix. Lacto-N-biosidase hydrolyzes lacto-N-biose (LNB) type I oligosaccharides at the nonreducing terminus to produce lacto-N-biose as part of the GNB/LNB (galacto-N-biose/lacto-N-biose I) degradation pathway. The lacto-N-biosidase from Bifidobacterium bifidum has this GH20 domain, a carbohydrate binding module 32, and a bacterial immunoglobulin-like domain 2, as well as a YSIRK signal peptide and a G5 membrane anchor at the N and C termini, respectively. The GH20 hexosaminidases are thought to act via a catalytic mechanism in which the catalytic nucleophile is not provided by solvent or the enzyme, but by the substrate itself.
Pssm-ID: 119334 Cd Length: 326 Bit Score: 302.67 E-value: 3.14e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 1600 MKAISLDAGRKYFSAAQIKEIIDEASKRGYTHLHLLLgNDALRFLLNDMTLKVNGKTYSSDEVKAaivhGTDAYYKDPHG 1679
Cdd:cd06564 2 VRGFMLDVGRKYYSMDFLKDIIKTMSWYKMNDLQLHL-NDNLIFNLDDMSTTVNNATYASDDVKS----GNNYYNLTAND 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 1680 NHLTQAEMDDILQYAKTKNIALIPAINSPGHMDAILDAMEQLGIKDarfsYNGKKSKRTIDLNNSDAVHFTKALIKKYAE 1759
Cdd:cd06564 77 GYYTKEEFKELIAYAKDRGVNIIPEIDSPGHSLAFTKAMPELGLKN----PFSKYDKDTLDISNPEAVKFVKALFDEYLD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 1760 YFSNKVEIFNIGLDEYANDvskesgfgllqrTGNYPKFINYVNELAKIVKDLHLKPMAFNDGFYYNNDKSSgaFDSDIII 1839
Cdd:cd06564 153 GFNPKSDTVHIGADEYAGD------------AGYAEAFRAYVNDLAKYVKDKGKTPRVWGDGIYYKGDTTV--LSKDVII 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 1840 SYWTAGWsgytvASSKYLSEKGHKILNTNDAWYYVLGRETKHSGWYNLEQGLNGMDKTPLDSVPKSEGAKIP-ILGSMIA 1918
Cdd:cd06564 219 NYWSYGW-----ADPKELLNKGYKIINTNDGYLYIVPGAGYYGDYLNTEDIYNNWTPNKFGGTNATLPEGDPqILGGMFA 293
|
330 340
....*....|....*....|.
gi 2461862307 1919 AWADEPRRAFN-KENFIRWID 1938
Cdd:cd06564 294 IWNDDSDAGISeVDIYDRIFP 314
|
|
| ebgA |
PRK10340 |
cryptic beta-D-galactosidase subunit alpha; Reviewed |
132-496 |
6.20e-41 |
|
cryptic beta-D-galactosidase subunit alpha; Reviewed
Pssm-ID: 236673 [Multi-domain] Cd Length: 1021 Bit Score: 166.00 E-value: 6.20e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 132 GWYRKTFSVNETIAKGRVYLKFDGSYMETEVFVNGHSLGVHPNGYTSFTFDVTKYLKVGEeNTIAIKVTNKIPSS----- 206
Cdd:PRK10340 111 GAYQRTFTLSDGWQGKQTIIKFDGVETYFEVYVNGQYVGFSKGSRLTAEFDISAMVKTGD-NLLCVRVMQWADSTyledq 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 207 -RWYSgSGIYRSLQLVFTPAVHLADngIVMKTpDLSQTAQSGTGSqvhVTAKVYNQSGNASQIRVKSILYerkeDGslGQ 285
Cdd:PRK10340 190 dMWWL-AGIFRDVYLVGKPLTHIND--FTVRT-DFDEDYCDATLS---CEVVLENLAASPVVTTLEYTLF----DG--ER 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 286 KAAESELSQpvdVKSGEQVPVNQQFSIVKPKLWSPDNPTLYVLRTELYQ-NGQKIQTVDQETGFRYTSFNSETgFSLNGQ 364
Cdd:PRK10340 257 VVHSSAIDH---LAIEKLTSASFAFTVEQPQQWSAESPYLYHLVMTLKDaNGNVLEVVPQRVGFRDIKVRDGL-FWINNR 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 365 TMKLKGVSMHHDQGALGSAAYYNAIERQVSILKRMGVNAIRVTHNPASRALKDIANRMGMLLIDEA------FDgwrdyk 438
Cdd:PRK10340 333 YVKLHGVNRHDNDHRKGRAVGMDRVEKDIQLMKQHNINSVRTAHYPNDPRFYELCDIYGLFVMAETdveshgFA------ 406
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2461862307 439 ngNTYDYTRFFDkkignsveglsnvespDQTWAEYHIKQMVR---SGINDPSIIMWSTGNE 496
Cdd:PRK10340 407 --NVGDISRITD----------------DPQWEKVYVDRIVRhihAQKNHPSIIIWSLGNE 449
|
|
| Glyco_hydro2_C5 |
pfam18565 |
Glycoside hydrolase family 2 C-terminal domain 5; Domain 5 is found in dimeric ... |
836-922 |
2.96e-36 |
|
Glycoside hydrolase family 2 C-terminal domain 5; Domain 5 is found in dimeric beta-D-galactosidase from Paracoccus sp. 32d, which contributes to stabilization of the functional dimer. It is suggested that the location of this domain 5, may be one of the factors responsible for the creation of a functional dimer and cold-adaptation of this enzyme.
Pssm-ID: 436582 Cd Length: 103 Bit Score: 133.35 E-value: 2.96e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 836 LAYVGVDVQDAKGNLVTDANNKVEFSVSGPAKLVGVDNGNAVDHQSYQDTNRKAFSGKVLAIVKMTGKSGTVTVTAKSKG 915
Cdd:pfam18565 17 LAFVTVEVVDKNGNLVPNADNLVTFSVEGPGELVGVDNGDPTSLESFQSNERKAFNGKALAIVRSTGEAGTITLTASAEG 96
|
....*..
gi 2461862307 916 LTTSTVT 922
Cdd:pfam18565 97 LKSATVT 103
|
|
| Glyco_hydro_20 |
pfam00728 |
Glycosyl hydrolase family 20, catalytic domain; This domain has a TIM barrel fold. |
1605-1921 |
7.09e-16 |
|
Glycosyl hydrolase family 20, catalytic domain; This domain has a TIM barrel fold.
Pssm-ID: 425840 Cd Length: 344 Bit Score: 81.58 E-value: 7.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 1605 LDAGRKYFSAAQIKEIIDE--ASKRGYTHLHLLlgndalrfllNDMTLKVNGKTYSsdevkaaIVHGTDAYYKD-----P 1677
Cdd:pfam00728 8 LDVARHFLPVDDIKRTIDAmaAYKLNVLHWHLT----------DDQGWRLEIKKYP-------KLTEKGAYRPSdldgtP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 1678 HGNHLTQAEMDDILQYAKTKNIALIPAINSPGHMDAILDAMEQLGIKDARFS----YNGKKSKRTIDLNNSDAVHFTKAL 1753
Cdd:pfam00728 71 YGGFYTQEDIREIVAYAAARGIRVIPEIDMPGHARAALAAYPELGCGCGADSpwvsVQWGPPEGQLNPGNEKTYTFLDNV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 1754 IKKYAEYFSNkvEIFNIGLDEYANDVSKESGF--GLLQRTG-----NYPKFinYVNELAKIVKDLHLKPMAFNDGFYYNN 1826
Cdd:pfam00728 151 FDEVADLFPS--DYIHIGGDEVPKGCWEKSPEcqARMKEEGlkslhELQQY--FIKRASKIVSSKGRRLIGWDEILDGGV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 1827 DKSsgafDSDIIISYWTaGWSGYTVAsskyLSEKGHK-ILNTNDAWY--YVLGRETKHSGWY-----NLEQGLNGmdkTP 1898
Cdd:pfam00728 227 PLL----PKNTTVQSWR-GGDEAAQK----AAKQGYDvIMSPGDFLYldCGQGGNPTEEPYYwggfvPLEDVYNW---DP 294
|
330 340
....*....|....*....|...
gi 2461862307 1899 LDSVPKSEGAKIPILGSMIAAWA 1921
Cdd:pfam00728 295 VPDTWNDPEQAKHVLGGQANLWT 317
|
|
| Chb |
COG3525 |
N-acetyl-beta-hexosaminidase [Carbohydrate transport and metabolism]; |
1605-1873 |
2.60e-13 |
|
N-acetyl-beta-hexosaminidase [Carbohydrate transport and metabolism];
Pssm-ID: 442747 [Multi-domain] Cd Length: 578 Bit Score: 75.28 E-value: 2.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 1605 LDAGRKYFSAAQIKEIIDEAS--KRGYTHLHLllgndalrfllndmtlkvngktysSD------EVKA------------ 1664
Cdd:COG3525 164 LDVARHFFPKEFVKRLIDLMAlyKLNVFHWHL------------------------TDdqgwriEIKKypeltevgawrg 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 1665 --AIVHGTDAYYKDPHGNHLTQAEMDDILQYAKTKNIALIPAINSPGHMDAILDAMEQLGIKDARFSYNGKK--SKRTID 1740
Cdd:COG3525 220 htLIGHDPQPFDGKPYGGFYTQEDIREIVAYAAARGITVIPEIDMPGHARAAIAAYPELGCTGKPYSVRSVWgvFDNVLN 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 1741 LNNSDAVHFTKALIKKYAEYF-SnkvEIFNIGLDEYANDVSKESGF--------GL-----LQrtgNYpkFInyvNELAK 1806
Cdd:COG3525 300 PGKESTYTFLEDVLDEVAALFpS---PYIHIGGDEVPKGQWEKSPAcqalmkelGLkdeheLQ---SY--FI---RRVEK 368
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2461862307 1807 IVKDLHLKPMAFNDGfyynndkSSGAFDSDIIISYWTAGWSGYTVAsskylsEKGHKILNTNDAWYY 1873
Cdd:COG3525 369 ILASKGRKMIGWDEI-------LEGGLAPNATVMSWRGEDGGIEAA------KAGHDVVMSPGSYLY 422
|
|
| F5_F8_type_C |
pfam00754 |
F5/8 type C domain; This domain is also known as the discoidin (DS) domain family. |
1365-1489 |
3.73e-12 |
|
F5/8 type C domain; This domain is also known as the discoidin (DS) domain family.
Pssm-ID: 459925 [Multi-domain] Cd Length: 127 Bit Score: 65.55 E-value: 3.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 1365 SVQPGAENAVENANDFNVDSMWHSdwaGTSARNLWATFDTGKIRTINGLAYLERMDKIqNGKIIDYEIYASKNNKDWFKV 1444
Cdd:pfam00754 5 SSSYSGEGPAAAALDGDPNTAWSA---WSGDDPQWIQVDLGKPKKITGVVTQGRQDGS-NGYVTSYKIEYSLDGENWTTV 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2461862307 1445 AKGRFA---DVEKWQEASF-TPVKARYLKLVGVKtlSDNSKKFISASEL 1489
Cdd:pfam00754 81 KDEKIPgnnDNNTPVTNTFdPPIKARYVRIVPTS--WNGGNGIALRAEL 127
|
|
| FA58C |
cd00057 |
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ... |
1358-1471 |
3.35e-09 |
|
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached carbohydrate-binding domain, present in eukaryotes and assumed to have horizontally transferred to eubacterial genomes.
Pssm-ID: 238014 [Multi-domain] Cd Length: 143 Bit Score: 57.36 E-value: 3.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 1358 DITLSAGSVQpGAENAVENAnDFNVDSMWHSDWagtSARNLWATFDTGKIRTINGLAYLERMDKIQNGKIIDYEIYASKN 1437
Cdd:cd00057 11 DDQITASSSY-SSGWEASRA-RLNSDNAWTPAV---NDPPQWLQVDLGKTRRVTGIQTQGRKGGGSSEWVTSYKVQYSLD 85
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2461862307 1438 NKDW--------FKVAKGrFADVEKWQEASF-TPVKARYLKLV 1471
Cdd:cd00057 86 GETWttykdkgeEKVFTG-NSDGSTPVTNDFpPPIVARYIRIL 127
|
|
| Big_4 |
pfam07532 |
Bacterial Ig-like domain (group 4); This family consists of bacterial domains with an Ig-like ... |
1016-1073 |
2.26e-04 |
|
Bacterial Ig-like domain (group 4); This family consists of bacterial domains with an Ig-like fold. Members of this family are found in a variety of bacterial surface proteins.
Pssm-ID: 400079 [Multi-domain] Cd Length: 59 Bit Score: 41.15 E-value: 2.26e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2461862307 1016 KNISTAVEKGRVPDLPKYVQAYVKSGNllSAQFPVTWKIPTSSIFDKVGTVTIKGVAD 1073
Cdd:pfam07532 2 ENIEVTVAQGESYTLPTTVTATYSDGS--VKEVPVTWDLTPNVDTSKPGTYTVEGTVE 57
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| GalB |
NF041463 |
beta-galactosidase GalB; |
75-916 |
0e+00 |
|
beta-galactosidase GalB;
Pssm-ID: 469351 [Multi-domain] Cd Length: 799 Bit Score: 649.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 75 VNFDSAWKFAMGELPGASERNYDDSSWKTLNLPHDFSLKQDYTQSGEAESGYKLG-----GIGWYRKTFSVNETIAKGRV 149
Cdd:NF041463 4 ISINDGWRFHKGDPAGAADADFDDSGWEQVTLPHDWAIAGPFYKGGPAEVGGGMGrlpswGVAWYRKKLDIPASDAGKSI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 150 YLKFDGSYMETEVFVNGHSLGVHPNGYTSFTFDVTKYLKVGEENTIAIKVTNKIPSSRWYSGSGIYRSLQLVFTPAVHLA 229
Cdd:NF041463 84 FLDIDGAMSYAMVWLNGQLVGGWPYGYNSWRLDLTPYLKPGGENQLAIRLDNPPESSRWYPGGGLYRNVWLTKTNPVHVA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 230 DNGIVMKTPDLSQTAqsgtgSQVHVTAKVYNQSGNASQIRVKSILYERKEDGSLGQKAAESELSQPVDVKSGEQVPVNQQ 309
Cdd:NF041463 164 QWGTFVTTPEVSADS-----ATVDLAVTVDNDSAADADVEVSTEIYALDADGKRTGKAVARFAPASLTVAAGESATVSGS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 310 FSIVKPKLWSP---DNPTLYVLRTELYQNGQKIQTVDQETGFRYTSFNSETGFSLNGQTMKLKGVSMHHDQGALGSAAYY 386
Cdd:NF041463 239 LTIANPRLWGPpptQTPNRYVAVTTVYQGGKVVDRYETPFGIRSLRFDPDRGVLVNGEHIRLQGVNQHHDLGALGAAFNV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 387 NAIERQVSILKRMGVNAIRVTHNPASRALKDIANRMGMLLIDEAFDGWRDYKngNTYDYTRFFdkkignsveglsnvesP 466
Cdd:NF041463 319 RAAERQLEILREMGCNAIRMAHNPPAPELLELTDRMGFLVVDEIFDSWERKK--TPLDFHLIF----------------P 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 467 DqtWAEYHIKQMVRSGINDPSIIMWSTGNEVTE-GTSKASAgtypQLIAQLINWIDQVDGTRPATLGDNYLKNrdttsvG 545
Cdd:NF041463 381 D--WHEQDLRAMIRRDRNHPSVIMWSIGNEVGEqYTGEAGA----AIARRLHDIVKEEDPTRPTTASMNYAKP------D 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 546 MAnaltnnkLQGVV---GYNY--ANGR---------------QYDKGHELNPNWFIYGSETASSINSRGVYNVKNQEQRS 605
Cdd:NF041463 449 MP-------FPAVMdviSLNYqgEGIRdapayeglkgirtppLYPAFHAKFPDKVILSSETASALSSRGEYLFPVTPGIS 521
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 606 ------------DKQLSSYDQSKVGWGHLASEAWYDVIKRDFVAGEFVWTGFDYLGEPTPWngigsgsvgtWPApKSSYF 673
Cdd:NF041463 522 apvrdgrggdpvTHQVSAYELYAADFGSSADKVFAAQDQHPYVAGEFVWTGWDYLGEPTPY----------YSS-RSSYS 590
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 674 GIVDTAGFPKDSYYFYQSQWNQKVKTLHVLPG-TWNEslikKEGGKVEVAVYSNAAKVKLVhVSDKGvetdLGTKaftkv 752
Cdd:NF041463 591 GIIDLAGFPKDRFYLYQSRWRPELPMAHILPHwNWPG----REGQVTPVHVFTSGDEAELF-LNGKS----LGRK----- 656
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 753 tTKAGHSYQiykgndkqaaehknlyLTW-KVPYKKGYLRAIAYDeNGKVInkteGRKEVKMAGKATKLAAKLE-SKVDSK 830
Cdd:NF041463 657 -KKGPYEYR----------------LRWdDVVYEPGELKVVAYK-NGKPW----AEDTVKTAGAAAKLQLTADrATIAAD 714
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 831 VTDhsLAYVGVDVQDAKGNLVTDANNKVEFSVSGPAKLVGVDNGNAVDHQSYQDTNRKAFSGKVLAIVKMT-GKSGTVTV 909
Cdd:NF041463 715 GKD--LSFVTVRVTDKDGLLVPRADNRLRFSIEGPGEIVATDNGDPTDLEPFPSPERNAFNGLALAIVRAKpGQAGKITV 792
|
....*..
gi 2461862307 910 TAKSKGL 916
Cdd:NF041463 793 TAESDGL 799
|
|
| GalA |
NF041462 |
beta-galactosidase GalA; |
78-923 |
0e+00 |
|
beta-galactosidase GalA;
Pssm-ID: 469350 [Multi-domain] Cd Length: 757 Bit Score: 620.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 78 DSAWKFAMGELP----------------------GASERNYDDSSWKTLNLPHDFSLKQDYTQSGEAESGYKLGGIGWYR 135
Cdd:NF041462 1 DFGWRFHLGDIAdpakdfhfgtdqytfakagnawGAAAPDFDDSDWRSVDLPHDWAVELPFVPDANASHGYKPRGIGWYR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 136 KTFSVNETIAKGRVYLKFDGSYMETEVFVNGHSLGVHPNGYTSFTFDVTKYLKVGEENTIAIKVTNKIPSSRWYSGSGIY 215
Cdd:NF041462 81 RTFDLPASDRGKRIELEFDGVFRNATVWVNGSVVGRNWSGYTSFRIDITDFLRYGDENVIAVRVDATAGEGWWYEGAGIY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 216 RSLQLVFTPAVHLADNGIVMKtpdlsqTAQSGTGSQVHVTAKVYNQSGNASQIRVKSILYERKedgslGQKAAESElSQP 295
Cdd:NF041462 161 RHVWLVKTDPVHIATDGVFVR------PRLDGGRATVPVETTLANEGDAAATVRVESTLLDPD-----GRVVATAE-SAP 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 296 VDVKSGEQVPVNQQFSIVKPKLWSPDNPTLYVLRTELYQNGQKIQTVDQETGFRYTSFNSETGFSLNGQTMKLKGVSMHH 375
Cdd:NF041462 229 LSVAALETATVTQTLPVANPALWSVETPYLYTLVTTVLVDGKVVDEVVTPFGFRTIRFDADKGFFLNGKPVKLKGVCNHQ 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 376 DQGALGSAAYYNAIERQVSILKRMGVNAIRVTHNPASRALKDIANRMGMLLIDEafdgwrdykngntydyTRFFdkkiGN 455
Cdd:NF041462 309 DHAGVGVAVPDALQEWRLRRLKEMGCNAYRTSHNPPTPELLDACDRLGMLVMDE----------------NRLF----NS 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 456 SVEGLSNVESpdqtwaeyhikqMVRSGINDPSIIMWSTGNEvtEGTSKASAGTypQLIAQLINWIDQVDGTRPATLGdny 535
Cdd:NF041462 369 SPEYLAQLEW------------MVRRDRNHPSIILWSVGNE--EPMQGTEQGA--RIVRRMVALVKRLDPTRPVTAA--- 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 536 lKNRDTTSVGMANALTnnklqgVVGYNYANGrQYDKGHELNPNWFIYGSETASSINSRGVYnvknqeqRSDKQ---LSSY 612
Cdd:NF041462 430 -MNGGFFGEGVSDVVD------VVGFNYRTG-NYDKFHAAHPNKPIIGSETASAVSTRGEY-------ATDKAkhvVSSY 494
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 613 DQSKVGWGHLASEAWYDVIKRDFVAGEFVWTGFDYLGEPTPWNgigsgsvgtWPApKSSYFGIVDTAGFPKDSYYFYQSQ 692
Cdd:NF041462 495 DTEAPSWGSTAEEWWKFIAERPFLAGGFVWTGFDYRGEPTPYE---------WPS-VSSQFGIMDLCGFPKDAYYYYRAW 564
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 693 WnQKVKTLHVLPgTWNESLikKEGGKVEVAVYSNAAKVKLVhVSDKgvetDLGtkaftkvttkaghsyqiykgndKQAAE 772
Cdd:NF041462 565 W-RDEPVLHLFP-HWNWPG--KEGQPIKVWVYSNADEVELF-LNGK----SLG----------------------RQKVD 613
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 773 HkNLYLTWKVPYKKGYLRAIAYdENGKVINKTegrkEVKMAGKATKLaaKLESKVDSKVTDHS-LAYVGVDVQDAKGNLV 851
Cdd:NF041462 614 R-NGHLEWSVPYAPGRLEARGY-RGGKVVLTE----VVETTGAPAAL--RLTPDRTVLAADGEdVAVVTVEAVDAKGRHV 685
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2461862307 852 TDANNKVEFSVSGPAKLVGVDNGNAVDHQSYQDTNRKAFSGKVLAIVKMTGKSGTVTVTAKSKGLTTSTVTF 923
Cdd:NF041462 686 PTADNLVRFSVSGPGRIIGVGNGDPNSHEPDKAPQRSLFNGLAQVIVQSTKGAGAITLTATAEGLKPATLVI 757
|
|
| LacZ |
COG3250 |
Beta-galactosidase/beta-glucuronidase [Carbohydrate transport and metabolism]; |
81-806 |
1.44e-129 |
|
Beta-galactosidase/beta-glucuronidase [Carbohydrate transport and metabolism];
Pssm-ID: 442481 [Multi-domain] Cd Length: 638 Bit Score: 422.63 E-value: 1.44e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 81 WKFAMGELPGASERNYDDSSWKTLNLPHDFSLKQDYTQSGEAESGYKLGGIGWYRKTFSVNETIAKGRVYLKFDGSYMET 160
Cdd:COG3250 3 WKFRLGDAPEGAKPDFDDSGWDPITVPGDWELDLYGLPDPFVGPWYLYNGVGWYRRTFTVPASWKGKRVFLHFEGVDTAA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 161 EVFVNGHSLGVHPNGYTSFTFDVTKYLKVGEeNTIAIKVTN-----KIPSSRWYSGSGIYRSLQLVFTPAVHLADNGIvm 235
Cdd:COG3250 83 EVWVNGKKVGYHEGGFTPFEFDITDYLKPGE-NVLAVRVDNpsdgsYLEGQDWWRTSGIYRDVWLEATPKVHIEDVFV-- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 236 kTPDLSqtAQSGTgsqVHVTAKVYNQSGNASQIRVKsiLYERKedgslGQKAAESElsQPVDVKSGEQVPVNQQFSIVKP 315
Cdd:COG3250 160 -TPDLD--DGSAT---LTVEVELENESDAGVTVEVT--LLDAD-----GKVVATAT--AKVTLAAGEENTVTLTLTVPNP 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 316 KLWSPDNPTLYVLRTELYQNGQKIQTVDQETGFRYTSFNSETGFSLNGQTMKLKGVSMHHDQGALGSAAYYNAIERQVSI 395
Cdd:COG3250 225 KLWSPEDPNLYTLVVTLKDDGKVVDTVSTRFGFRTIEIDGDGGFLLNGKPVFLKGVNRHEDWPDDGRAVTDEAMRRDLEL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 396 LKRMGVNAIRVTHNPASRALKDIANRMGMLLIDEAFDGWRDykngnTYDYTRFFDKkignsveglsnvespdqtWAEYHI 475
Cdd:COG3250 305 MKEAGFNAVRTSHYPEDPEFYDLCDELGLLVWDEAPFEWHG-----MLGDDPEFLE------------------AVEAEL 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 476 KQMVRSGINDPSIIMWSTGNEVTEGTSkasagtypqlIAQLINWIDQVDGTRPatlgdnylknrdttsvgmanaltnnkl 555
Cdd:COG3250 362 REMVRRDRNHPSIILWSGGNESGGGPN----------FAALYEWVKELDPTRP--------------------------- 404
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 556 qgvvgynyangrqydkghelnpnwFIYGSETASSI-NS-RGVYNVKNQEQRSdkQLSSYDQskvgwghlasEAWYDVIKR 633
Cdd:COG3250 405 ------------------------VRFLSEYGHAMpNSlGGGYHQPSDFEEY--QALQALE----------EYWEAFRRR 448
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 634 DFVAGEFVWTGFDYLGEPTPWNGigsgsvgtwpapKSSYFGIVD-TAGFPKDSYYFYQSQWNQKV---KTLHVLPGTWNE 709
Cdd:COG3250 449 PRLAGGFIWQLNDYWPEPRDNDG------------NFCSWGLVDyYDRTPKPAYYEVKSAWQPVLvsdGMLHILLPHWND 516
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 710 slikkegGKVEVAVYSNAAKVKLVHVSDKGVETDLGTKAFTKVTTKAGHSYQIYKGNDKQAAEHKNLYLTWKVPYKKGYL 789
Cdd:COG3250 517 -------GKEGELPYSSTVADLYTPYVRPQENGNRTDVRWLTLTNGKGKGLLVSGVPLLSGSALAYLTEDLLAAKEEGLL 589
|
730
....*....|....*..
gi 2461862307 790 RAIAYDENGKVINKTEG 806
Cdd:COG3250 590 LAADLTTLLLDLADLGG 606
|
|
| GH20_DspB_LnbB-like |
cd06564 |
Glycosyl hydrolase family 20 (GH20) catalytic domain of dispersin B (DspB), lacto-N-biosidase ... |
1600-1938 |
3.14e-92 |
|
Glycosyl hydrolase family 20 (GH20) catalytic domain of dispersin B (DspB), lacto-N-biosidase (LnbB) and related proteins. Dispersin B is a soluble beta-N-acetylglucosamidase found in bacteria that hydrolyzes the beta-1,6-linkages of PGA (poly-beta-(1,6)-N-acetylglucosamine), a major component of the extracellular polysaccharide matrix. Lacto-N-biosidase hydrolyzes lacto-N-biose (LNB) type I oligosaccharides at the nonreducing terminus to produce lacto-N-biose as part of the GNB/LNB (galacto-N-biose/lacto-N-biose I) degradation pathway. The lacto-N-biosidase from Bifidobacterium bifidum has this GH20 domain, a carbohydrate binding module 32, and a bacterial immunoglobulin-like domain 2, as well as a YSIRK signal peptide and a G5 membrane anchor at the N and C termini, respectively. The GH20 hexosaminidases are thought to act via a catalytic mechanism in which the catalytic nucleophile is not provided by solvent or the enzyme, but by the substrate itself.
Pssm-ID: 119334 Cd Length: 326 Bit Score: 302.67 E-value: 3.14e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 1600 MKAISLDAGRKYFSAAQIKEIIDEASKRGYTHLHLLLgNDALRFLLNDMTLKVNGKTYSSDEVKAaivhGTDAYYKDPHG 1679
Cdd:cd06564 2 VRGFMLDVGRKYYSMDFLKDIIKTMSWYKMNDLQLHL-NDNLIFNLDDMSTTVNNATYASDDVKS----GNNYYNLTAND 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 1680 NHLTQAEMDDILQYAKTKNIALIPAINSPGHMDAILDAMEQLGIKDarfsYNGKKSKRTIDLNNSDAVHFTKALIKKYAE 1759
Cdd:cd06564 77 GYYTKEEFKELIAYAKDRGVNIIPEIDSPGHSLAFTKAMPELGLKN----PFSKYDKDTLDISNPEAVKFVKALFDEYLD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 1760 YFSNKVEIFNIGLDEYANDvskesgfgllqrTGNYPKFINYVNELAKIVKDLHLKPMAFNDGFYYNNDKSSgaFDSDIII 1839
Cdd:cd06564 153 GFNPKSDTVHIGADEYAGD------------AGYAEAFRAYVNDLAKYVKDKGKTPRVWGDGIYYKGDTTV--LSKDVII 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 1840 SYWTAGWsgytvASSKYLSEKGHKILNTNDAWYYVLGRETKHSGWYNLEQGLNGMDKTPLDSVPKSEGAKIP-ILGSMIA 1918
Cdd:cd06564 219 NYWSYGW-----ADPKELLNKGYKIINTNDGYLYIVPGAGYYGDYLNTEDIYNNWTPNKFGGTNATLPEGDPqILGGMFA 293
|
330 340
....*....|....*....|.
gi 2461862307 1919 AWADEPRRAFN-KENFIRWID 1938
Cdd:cd06564 294 IWNDDSDAGISeVDIYDRIFP 314
|
|
| ebgA |
PRK10340 |
cryptic beta-D-galactosidase subunit alpha; Reviewed |
132-496 |
6.20e-41 |
|
cryptic beta-D-galactosidase subunit alpha; Reviewed
Pssm-ID: 236673 [Multi-domain] Cd Length: 1021 Bit Score: 166.00 E-value: 6.20e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 132 GWYRKTFSVNETIAKGRVYLKFDGSYMETEVFVNGHSLGVHPNGYTSFTFDVTKYLKVGEeNTIAIKVTNKIPSS----- 206
Cdd:PRK10340 111 GAYQRTFTLSDGWQGKQTIIKFDGVETYFEVYVNGQYVGFSKGSRLTAEFDISAMVKTGD-NLLCVRVMQWADSTyledq 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 207 -RWYSgSGIYRSLQLVFTPAVHLADngIVMKTpDLSQTAQSGTGSqvhVTAKVYNQSGNASQIRVKSILYerkeDGslGQ 285
Cdd:PRK10340 190 dMWWL-AGIFRDVYLVGKPLTHIND--FTVRT-DFDEDYCDATLS---CEVVLENLAASPVVTTLEYTLF----DG--ER 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 286 KAAESELSQpvdVKSGEQVPVNQQFSIVKPKLWSPDNPTLYVLRTELYQ-NGQKIQTVDQETGFRYTSFNSETgFSLNGQ 364
Cdd:PRK10340 257 VVHSSAIDH---LAIEKLTSASFAFTVEQPQQWSAESPYLYHLVMTLKDaNGNVLEVVPQRVGFRDIKVRDGL-FWINNR 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 365 TMKLKGVSMHHDQGALGSAAYYNAIERQVSILKRMGVNAIRVTHNPASRALKDIANRMGMLLIDEA------FDgwrdyk 438
Cdd:PRK10340 333 YVKLHGVNRHDNDHRKGRAVGMDRVEKDIQLMKQHNINSVRTAHYPNDPRFYELCDIYGLFVMAETdveshgFA------ 406
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2461862307 439 ngNTYDYTRFFDkkignsveglsnvespDQTWAEYHIKQMVR---SGINDPSIIMWSTGNE 496
Cdd:PRK10340 407 --NVGDISRITD----------------DPQWEKVYVDRIVRhihAQKNHPSIIIWSLGNE 449
|
|
| Glyco_hydro2_C5 |
pfam18565 |
Glycoside hydrolase family 2 C-terminal domain 5; Domain 5 is found in dimeric ... |
836-922 |
2.96e-36 |
|
Glycoside hydrolase family 2 C-terminal domain 5; Domain 5 is found in dimeric beta-D-galactosidase from Paracoccus sp. 32d, which contributes to stabilization of the functional dimer. It is suggested that the location of this domain 5, may be one of the factors responsible for the creation of a functional dimer and cold-adaptation of this enzyme.
Pssm-ID: 436582 Cd Length: 103 Bit Score: 133.35 E-value: 2.96e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 836 LAYVGVDVQDAKGNLVTDANNKVEFSVSGPAKLVGVDNGNAVDHQSYQDTNRKAFSGKVLAIVKMTGKSGTVTVTAKSKG 915
Cdd:pfam18565 17 LAFVTVEVVDKNGNLVPNADNLVTFSVEGPGELVGVDNGDPTSLESFQSNERKAFNGKALAIVRSTGEAGTITLTASAEG 96
|
....*..
gi 2461862307 916 LTTSTVT 922
Cdd:pfam18565 97 LKSATVT 103
|
|
| PRK10150 |
PRK10150 |
beta-D-glucuronidase; Provisional |
70-544 |
8.02e-35 |
|
beta-D-glucuronidase; Provisional
Pssm-ID: 236657 [Multi-domain] Cd Length: 604 Bit Score: 143.22 E-value: 8.02e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 70 KTDKTVNFDSAWKFAMGElpgasERNYDDSSWKTLNLPHDFSLK-----QDYTQSGEaesgyKLGGIG--WYRKTFSVNE 142
Cdd:PRK10150 8 KTREIKDLSGLWAFKLDR-----ENCGIDQRWWESALPESRAMAvpgsfNDQFADAD-----IRNYVGdvWYQREVFIPK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 143 TIAKGRVYLKFDGSYMETEVFVNGHSLGVHPNGYTSFTFDVTKYLKVGEENTIAIKVTNK-----IPSSR---------- 207
Cdd:PRK10150 78 GWAGQRIVLRFGSVTHYAKVWVNGQEVMEHKGGYTPFEADITPYVYAGKSVRITVCVNNElnwqtLPPGNviedgngkkk 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 208 ------WYSGSGIYRSLQLVFTPAVHLADNGIvmkTPDLSQTAQSGTgsqVHVTAKVynqSGNASQIRVkSILYERkedg 281
Cdd:PRK10150 158 qkynfdFFNYAGIHRPVMLYTTPKTHIDDITV---VTELAQDLNHAS---VDWSVET---NGDVDSVSV-TLRDAD---- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 282 slGQKAAESElsqpvdVKSGeqvpvnqQFSIVKPKLWSPDNPTLYVLRTELYQNGQKIQTVDQETGFRyTSFNSETGFSL 361
Cdd:PRK10150 224 --GQVVATGQ------GTSG-------TLQVVNPHLWQPGEGYLYTLCVELAKSGTECDTYPLRFGIR-SVAVKGGQFLI 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 362 NGQTMKLKGVSMHHDQGALGSAAYYNAIERQVSILKRMGVNAIRVTHNPASRALKDIANRMGMLLIDEAFDGWRDYKNGN 441
Cdd:PRK10150 288 NGKPFYFKGFGKHEDADIRGKGLDEVLNVHDHNLMKWIGANSFRTSHYPYSEEMLDLADRHGIVVIDETPAVGLNLSFGA 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 442 TYDYTRffDKKIGNSVEGLSnvespDQTwAEYH---IKQMVRSGINDPSIIMWSTGNEvtEGTSKASAGTYpqlIAQLIN 518
Cdd:PRK10150 368 GLEAGN--KPKETYSEEAVN-----GET-QQAHlqaIRELIARDKNHPSVVMWSIANE--PASREQGAREY---FAPLAE 434
|
490 500
....*....|....*....|....*.
gi 2461862307 519 WIDQVDGTRPATLGDNYLKNRDTTSV 544
Cdd:PRK10150 435 LTRKLDPTRPVTCVNVMFATPDTDTV 460
|
|
| Glyco_hydro_2_N |
pfam02837 |
Glycosyl hydrolases family 2, sugar binding domain; This family contains beta-galactosidase, ... |
78-224 |
2.91e-29 |
|
Glycosyl hydrolases family 2, sugar binding domain; This family contains beta-galactosidase, beta-mannosidase and beta-glucuronidase activities and has a jelly-roll fold. The domain binds the sugar moiety during the sugar-hydrolysis reaction.
Pssm-ID: 397120 [Multi-domain] Cd Length: 169 Bit Score: 115.80 E-value: 2.91e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 78 DSAWKFAMGELP-GASER--NYDDSSWKTLNLPHDFSLKQDYTQSGEA---ESGY--KLGGIGWYRKTFSVNETIAKGRV 149
Cdd:pfam02837 5 NGEWAFALFDAPcGAPQSwwESALQESRTIAVPSSWNDQPIYTNVEYPidfADPFipTYNGTGWYQRTFFIPSKWAGQRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 150 YLKFDGSYMETEVFVNGHSLGVHPNGYTSFTFDVTKYLKVGeENTIAIKVTNKIPS-----------SRWYSGSGIYRSL 218
Cdd:pfam02837 85 RLRFDGVTHYGEVWVNGQWVGEHQGGYTPFEFDLTPYVIAG-KNRIAVKVLNWSDG*yiedqngkyfHDFWNYSGIYRDV 163
|
....*.
gi 2461862307 219 QLVFTP 224
Cdd:pfam02837 164 SLLTTP 169
|
|
| lacZ |
PRK09525 |
beta-galactosidase; |
132-528 |
1.30e-24 |
|
beta-galactosidase;
Pssm-ID: 236548 [Multi-domain] Cd Length: 1027 Bit Score: 112.72 E-value: 1.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 132 GWYRKTFSVNET-IAKGRVYLKFDGSYMETEVFVNGHSLGVHPNGYTSFTFDVTKYLKVGEeNTIAIKVTnkipssRWYS 210
Cdd:PRK09525 122 GCYSLTFTVDESwLQSGQTRIIFDGVNSAFHLWCNGRWVGYSQDSRLPAEFDLSPFLRAGE-NRLAVMVL------RWSD 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 211 G-----------SGIYRSLQLVFTPAVHLADNGIvmkTPDLSQTAQSGTgsqVHVTAKVYNQSGNASQIRVKsiLYerke 279
Cdd:PRK09525 195 GsyledqdmwrmSGIFRDVSLLHKPTTQLSDFHI---TTELDDDFRRAV---LEVEAQVNGELRDELRVTVQ--LW---- 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 280 DGslGQKAAESEL---SQPVDVKSGEQVPVNQQFSIVKPKLWSPDNPTLYVLRTELYQN-GQKIQTVDQETGFRYTSFns 355
Cdd:PRK09525 263 DG--ETLVASGTApfgTEIIDERGAYADRVTLRLNVENPKLWSAETPNLYRAVVSLLDAdGTLIEAEAYDVGFRKVEI-- 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 356 ETG-FSLNGQTMKLKGVSMHHDQGALGSAAYYNAIERQVSILKRMGVNAIRVTHNPASRALKDIANRMGMLLIDEAfdgw 434
Cdd:PRK09525 339 ENGlLKLNGKPLLIRGVNRHEHHPEHGQVMDEETMVQDILLMKQHNFNAVRCSHYPNHPLWYELCDRYGLYVVDEA---- 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 435 rdykNGNTYDYT---RffdkkignsvegLSNvespDQTWAEYH---IKQMVRSGINDPSIIMWSTGNEVTEGTSKASagt 508
Cdd:PRK09525 415 ----NIETHGMVpmnR------------LSD----DPRWLPAMserVTRMVQRDRNHPSIIIWSLGNESGHGANHDA--- 471
|
410 420
....*....|....*....|
gi 2461862307 509 ypqliaqLINWIDQVDGTRP 528
Cdd:PRK09525 472 -------LYRWIKSNDPSRP 484
|
|
| GH20_hexosaminidase |
cd02742 |
Beta-N-acetylhexosaminidases of glycosyl hydrolase family 20 (GH20) catalyze the removal of ... |
1602-1873 |
1.39e-21 |
|
Beta-N-acetylhexosaminidases of glycosyl hydrolase family 20 (GH20) catalyze the removal of beta-1,4-linked N-acetyl-D-hexosamine residues from the non-reducing ends of N-acetyl-beta-D-hexosaminides including N-acetylglucosides and N-acetylgalactosides. These enzymes are broadly distributed in microorganisms, plants and animals, and play roles in various key physiological and pathological processes. These processes include cell structural integrity, energy storage, cellular signaling, fertilization, pathogen defense, viral penetration, the development of carcinomas, inflammatory events and lysosomal storage disorders. The GH20 enzymes include the eukaryotic beta-N-acetylhexosaminidases A and B, the bacterial chitobiases, dispersin B, and lacto-N-biosidase. The GH20 hexosaminidases are thought to act via a catalytic mechanism in which the catalytic nucleophile is not provided by the solvent or the enzyme, but by the substrate itself.
Pssm-ID: 119331 [Multi-domain] Cd Length: 303 Bit Score: 97.50 E-value: 1.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 1602 AISLDAGRKYFSAAQIKEIIDEASKRGYTHLHLLLGND-ALRF------LLNDMTLKVNGKTYSsdevkaaivhgtdAYY 1674
Cdd:cd02742 3 GIMLDVSRHFLSVESIKRTIDVLARYKINTFHWHLTDDqAWRIeskkfpELAEKGGQINPRSPG-------------GFY 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 1675 kdphgnhlTQAEMDDILQYAKTKNIALIPAINSPGHMDAILDAMEQLgIKDARFSYNGKKSKRTIDLNNSDAVHFTKALI 1754
Cdd:cd02742 70 --------TYAQLKDIIEYAAARGIEVIPEIDMPGHSTAFVKSFPKL-LTECYAGLKLRDVFDPLDPTLPKGYDFLDDLF 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 1755 KKYAEYFSnkVEIFNIGLDEYANDVSKEsgfgllqrtgnyPKFINYVNELAKIVKDLHLKPMAFNDGFYYNNdkssgAFD 1834
Cdd:cd02742 141 GEIAELFP--DRYLHIGGDEAHFKQDRK------------HLMSQFIQRVLDIVKKKGKKVIVWQDGFDKKM-----KLK 201
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2461862307 1835 SDIIISYwtagWSGYTVASSKYLSE---KGHKILNTNDAWYY 1873
Cdd:cd02742 202 EDVIVQY----WDYDGDKYNVELPEaaaKGFPVILSNGYYLD 239
|
|
| Glyco_hydro_2_C |
pfam02836 |
Glycosyl hydrolases family 2, TIM barrel domain; This family contains beta-galactosidase, ... |
359-673 |
1.39e-17 |
|
Glycosyl hydrolases family 2, TIM barrel domain; This family contains beta-galactosidase, beta-mannosidase and beta-glucuronidase activities.
Pssm-ID: 397119 [Multi-domain] Cd Length: 302 Bit Score: 85.96 E-value: 1.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 359 FSLNGQTMKLKGVSMHHDQGALGSAAYYNAIERQVSILKRMGVNAIRVTHNPASRALKDIANRMGMLLIDEAfdgwrdyk 438
Cdd:pfam02836 8 FLINGKPFYFRGVNRHEDHDRRGRGFDMDLMVKDIQLMKQNNINAVRTSHYPNHPEWYQLCDEYGIYVIDEA-------- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 439 NGNTYDYTRFFdkkigNSVEGLSNVESPDQTWAEYH---IKQMVRSGINDPSIIMWSTGNEvtegtskASAGTYpqlIAQ 515
Cdd:pfam02836 80 NLETHGLWQKF-----GEIEPSYSELTDNPEWLPAHlerAEELVQRDKNHPSVIIWSLGNE-------SGAGEN---IAA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 516 LINWIDQVDGTRPAT----LGDNYLKnrDTTSVGMANALTNNKLQGVVGYNYANGrqydKGHELNPnwFI---YGSETas 588
Cdd:pfam02836 145 MYAATKSLDPTRPVHyegvGIDPEVD--DIILDIYSRMYEDYGHPEVIEKYLEDW----YKKPQKP--IIiceYGHAM-- 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 589 sINSRGVYnvknqeQRSDKQLSSYDQSKVGWghlaSEAWYDV--IKRD-FVAGEFVWTGFDYLGEPTPWNGIGSGSVGTW 665
Cdd:pfam02836 215 -GNSPGGL------QEYQDLFYKYPEYQGGF----IWDWHDQgiQKRDpNVGGEWYWYGGDFGDRPSDYRFCGNGLFFAD 283
|
....*...
gi 2461862307 666 PAPKSSYF 673
Cdd:pfam02836 284 RTPKPALF 291
|
|
| Glyco_hydro_20 |
pfam00728 |
Glycosyl hydrolase family 20, catalytic domain; This domain has a TIM barrel fold. |
1605-1921 |
7.09e-16 |
|
Glycosyl hydrolase family 20, catalytic domain; This domain has a TIM barrel fold.
Pssm-ID: 425840 Cd Length: 344 Bit Score: 81.58 E-value: 7.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 1605 LDAGRKYFSAAQIKEIIDE--ASKRGYTHLHLLlgndalrfllNDMTLKVNGKTYSsdevkaaIVHGTDAYYKD-----P 1677
Cdd:pfam00728 8 LDVARHFLPVDDIKRTIDAmaAYKLNVLHWHLT----------DDQGWRLEIKKYP-------KLTEKGAYRPSdldgtP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 1678 HGNHLTQAEMDDILQYAKTKNIALIPAINSPGHMDAILDAMEQLGIKDARFS----YNGKKSKRTIDLNNSDAVHFTKAL 1753
Cdd:pfam00728 71 YGGFYTQEDIREIVAYAAARGIRVIPEIDMPGHARAALAAYPELGCGCGADSpwvsVQWGPPEGQLNPGNEKTYTFLDNV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 1754 IKKYAEYFSNkvEIFNIGLDEYANDVSKESGF--GLLQRTG-----NYPKFinYVNELAKIVKDLHLKPMAFNDGFYYNN 1826
Cdd:pfam00728 151 FDEVADLFPS--DYIHIGGDEVPKGCWEKSPEcqARMKEEGlkslhELQQY--FIKRASKIVSSKGRRLIGWDEILDGGV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 1827 DKSsgafDSDIIISYWTaGWSGYTVAsskyLSEKGHK-ILNTNDAWY--YVLGRETKHSGWY-----NLEQGLNGmdkTP 1898
Cdd:pfam00728 227 PLL----PKNTTVQSWR-GGDEAAQK----AAKQGYDvIMSPGDFLYldCGQGGNPTEEPYYwggfvPLEDVYNW---DP 294
|
330 340
....*....|....*....|...
gi 2461862307 1899 LDSVPKSEGAKIPILGSMIAAWA 1921
Cdd:pfam00728 295 VPDTWNDPEQAKHVLGGQANLWT 317
|
|
| Chb |
COG3525 |
N-acetyl-beta-hexosaminidase [Carbohydrate transport and metabolism]; |
1605-1873 |
2.60e-13 |
|
N-acetyl-beta-hexosaminidase [Carbohydrate transport and metabolism];
Pssm-ID: 442747 [Multi-domain] Cd Length: 578 Bit Score: 75.28 E-value: 2.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 1605 LDAGRKYFSAAQIKEIIDEAS--KRGYTHLHLllgndalrfllndmtlkvngktysSD------EVKA------------ 1664
Cdd:COG3525 164 LDVARHFFPKEFVKRLIDLMAlyKLNVFHWHL------------------------TDdqgwriEIKKypeltevgawrg 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 1665 --AIVHGTDAYYKDPHGNHLTQAEMDDILQYAKTKNIALIPAINSPGHMDAILDAMEQLGIKDARFSYNGKK--SKRTID 1740
Cdd:COG3525 220 htLIGHDPQPFDGKPYGGFYTQEDIREIVAYAAARGITVIPEIDMPGHARAAIAAYPELGCTGKPYSVRSVWgvFDNVLN 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 1741 LNNSDAVHFTKALIKKYAEYF-SnkvEIFNIGLDEYANDVSKESGF--------GL-----LQrtgNYpkFInyvNELAK 1806
Cdd:COG3525 300 PGKESTYTFLEDVLDEVAALFpS---PYIHIGGDEVPKGQWEKSPAcqalmkelGLkdeheLQ---SY--FI---RRVEK 368
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2461862307 1807 IVKDLHLKPMAFNDGfyynndkSSGAFDSDIIISYWTAGWSGYTVAsskylsEKGHKILNTNDAWYY 1873
Cdd:COG3525 369 ILASKGRKMIGWDEI-------LEGGLAPNATVMSWRGEDGGIEAA------KAGHDVVMSPGSYLY 422
|
|
| GH20_GcnA-like |
cd06565 |
Glycosyl hydrolase family 20 (GH20) catalytic domain of N-acetyl-beta-D-glucosaminidase (GcnA, ... |
1680-1842 |
8.89e-13 |
|
Glycosyl hydrolase family 20 (GH20) catalytic domain of N-acetyl-beta-D-glucosaminidase (GcnA, also known as BhsA) and related proteins. GcnA is an exoglucosidase which cleaves N-acetyl-beta-D-galactosamine (NAG) and N-acetyl-beta-D-galactosamine residues from 4-methylumbelliferylated (4MU) substrates, as well as cleaving NAG from chito-oligosaccharides (i.e. NAG polymers). In contrast, sulfated forms of the substrate are unable to be cleaved and act instead as mild competitive inhibitors. Additionally, the enzyme is known to be poisoned by several first-row transition metals as well as by mercury. GcnA forms a homodimer with subunits comprised of three domains, an N-terminal zincin-like domain, this central catalytic GH20 domain, and a C-terminal alpha helical domain. The GH20 hexosaminidases are thought to act via a catalytic mechanism in which the catalytic nucleophile is not provided by solvent or the enzyme, but by the substrate itself.
Pssm-ID: 119335 Cd Length: 301 Bit Score: 71.47 E-value: 8.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 1680 NHLTQAEMDDILQYAKTKNIALIPAINSPGHMDAILDAMEQLGIKDARFSYNgkkskrTIDLNNSDAVHFTKALIKKYAE 1759
Cdd:cd06565 55 GAYTKEEIREIDDYAAELGIEVIPLIQTLGHLEFILKHPEFRHLREVDDPPQ------TLCPGEPKTYDFIEEMIRQVLE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 1760 YF-SNKV-----EIFNIGLDEYANDVSKESGFGLlqrtgnypkFINYVNELAKIVKDLHLKPMAFND---GFYYNNDKSS 1830
Cdd:cd06565 129 LHpSKYIhigmdEAYDLGRGRSLRKHGNLGRGEL---------YLEHLKKVLKIIKKRGPKPMMWDDmlrKLSIEPEALS 199
|
170
....*....|..
gi 2461862307 1831 GaFDSDIIISYW 1842
Cdd:cd06565 200 G-LPKLVTPVVW 210
|
|
| F5_F8_type_C |
pfam00754 |
F5/8 type C domain; This domain is also known as the discoidin (DS) domain family. |
1365-1489 |
3.73e-12 |
|
F5/8 type C domain; This domain is also known as the discoidin (DS) domain family.
Pssm-ID: 459925 [Multi-domain] Cd Length: 127 Bit Score: 65.55 E-value: 3.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 1365 SVQPGAENAVENANDFNVDSMWHSdwaGTSARNLWATFDTGKIRTINGLAYLERMDKIqNGKIIDYEIYASKNNKDWFKV 1444
Cdd:pfam00754 5 SSSYSGEGPAAAALDGDPNTAWSA---WSGDDPQWIQVDLGKPKKITGVVTQGRQDGS-NGYVTSYKIEYSLDGENWTTV 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2461862307 1445 AKGRFA---DVEKWQEASF-TPVKARYLKLVGVKtlSDNSKKFISASEL 1489
Cdd:pfam00754 81 KDEKIPgnnDNNTPVTNTFdPPIKARYVRIVPTS--WNGGNGIALRAEL 127
|
|
| GH20_chitobiase-like |
cd06563 |
The chitobiase of Serratia marcescens is a beta-N-1,4-acetylhexosaminidase with a glycosyl ... |
1605-1921 |
6.95e-12 |
|
The chitobiase of Serratia marcescens is a beta-N-1,4-acetylhexosaminidase with a glycosyl hydrolase family 20 (GH20) domain that hydrolyzes the beta-1,4-glycosidic linkages in oligomers derived from chitin. Chitin is degraded by a two step process: i) a chitinase hydrolyzes the chitin to oligosaccharides and disaccharides such as di-N-acetyl-D-glucosamine and chitobiose, ii) chitobiase then further degrades these oligomers into monomers. This GH20 domain family includes an N-acetylglucosamidase (GlcNAcase A) from Pseudoalteromonas piscicida and an N-acetylhexosaminidase (SpHex) from Streptomyces plicatus. SpHex lacks the C-terminal PKD (polycystic kidney disease I)-like domain found in the chitobiases. The GH20 hexosaminidases are thought to act via a catalytic mechanism in which the catalytic nucleophile is not provided by solvent or the enzyme, but by the substrate itself.
Pssm-ID: 119333 Cd Length: 357 Bit Score: 69.53 E-value: 6.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 1605 LDAGRKYFSAAQIKEIIDEAS--KRGYTHLHL--------------LLgndalrfllndmTLKvnGKTYSSDEVKAAIVH 1668
Cdd:cd06563 8 LDVSRHFFPVDEVKRFIDLMAlyKLNVFHWHLtddqgwrieikkypKL------------TEV--GAWRGPTEIGLPQGG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 1669 GTDayykDPHGNHLTQAEMDDILQYAKTKNIALIPAINSPGHMDAILDAMEQLGIKDARFSY--NGKKSKRTIDLNNSDA 1746
Cdd:cd06563 74 GDG----TPYGGFYTQEEIREIVAYAAERGITVIPEIDMPGHALAALAAYPELGCTGGPGSVvsVQGVVSNVLCPGKPET 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 1747 VHFTKALIKKYAEYFSNkvEIFNIGLDEYANDVSKESGF--GLLQRTG--NYPKFINY-VNELAKIVKDLHLKPMAFNDG 1821
Cdd:cd06563 150 YTFLEDVLDEVAELFPS--PYIHIGGDEVPKGQWEKSPAcqARMKEEGlkDEHELQSYfIKRVEKILASKGKKMIGWDEI 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 1822 FYynndkssGAFDSDIIISYWTaGWSGyTVASSKylseKGHKILNTNDAWYYVLGRETKHSGWYNLEQGLNGMDKT---- 1897
Cdd:cd06563 228 LE-------GGLPPNATVMSWR-GEDG-GIKAAK----QGYDVIMSPGQYLYLDYAQSKGPDEPASWAGFNTLEKVysfe 294
|
330 340
....*....|....*....|....
gi 2461862307 1898 PLDSVPKSEGAKIpILGSMIAAWA 1921
Cdd:cd06563 295 PVPGGLTPEQAKR-ILGVQANLWT 317
|
|
| GH20_HexA_HexB-like |
cd06562 |
Beta-N-acetylhexosaminidases catalyze the removal of beta-1,4-linked N-acetyl-D-hexosamine ... |
1603-1872 |
2.98e-11 |
|
Beta-N-acetylhexosaminidases catalyze the removal of beta-1,4-linked N-acetyl-D-hexosamine residues from the non-reducing ends of N-acetyl-beta-D-hexosaminides including N-acetylglucosides and N-acetylgalactosides. The hexA and hexB genes encode the alpha- and beta-subunits of the two major beta-N-acetylhexosaminidase isoenzymes, N-acetyl-beta-D-hexosaminidase A (HexA) and beta-N-acetylhexosaminidase B (HexB). Both the alpha and the beta catalytic subunits have a TIM-barrel fold and belong to the glycosyl hydrolase family 20 (GH20). The HexA enzyme is a heterodimer containing one alpha and one beta subunit while the HexB enzyme is a homodimer containing two beta-subunits. Hexosaminidase mutations cause an inability to properly hydrolyze certain sphingolipids which accumulate in lysosomes within the brain, resulting in the lipid storage disorders Tay-Sachs and Sandhoff. Mutations in the alpha subunit cause in a deficiency in the HexA enzyme and result in Tay-Sachs, mutations in the beta-subunit cause in a deficiency in both HexA and HexB enzymes and result in Sandhoff disease. In both disorders GM(2) gangliosides accumulate in lysosomes. The GH20 hexosaminidases are thought to act via a catalytic mechanism in which the catalytic nucleophile is not provided by solvent or the enzyme, but by the substrate itself.
Pssm-ID: 119332 [Multi-domain] Cd Length: 348 Bit Score: 67.24 E-value: 2.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 1603 ISLDAGRKYFSAAQIKEIID--EASKRGYTHLHLLlgnDALRFLLN-----DMTLKvnGKtYSSDEVkaaivhgtdayYk 1675
Cdd:cd06562 6 LLLDTSRHFLSVDSIKRTIDamAYNKLNVLHWHIT---DSQSFPLEspsypELSKK--GA-YSPSEV-----------Y- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 1676 dphgnhlTQAEMDDILQYAKTKNIALIPAINSPGHMDAILDAMEQLGIKDARFSYNGKKSKRT--IDLNNSDAVHFTKAL 1753
Cdd:cd06562 68 -------TPEDVKEIVEYARLRGIRVIPEIDTPGHTGSWGQGYPELLTGCYAVWRKYCPEPPCgqLNPTNPKTYDFLKTL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 1754 IKKYAEYFSNKVeiFNIGLDE-----YANDVS-----KESGFGLLQRTGNYpkfinYVNELAKIVKDLHLKPMAFNDGFY 1823
Cdd:cd06562 141 FKEVSELFPDKY--FHLGGDEvnfncWNSNPEiqkfmKKNNGTDYSDLESY-----FIQRALDIVRSLGKTPIVWEEVFD 213
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2461862307 1824 YNNDKSsgafDSDIIISYWTagwSGYTVassKYLSEKGHK-ILNTNDAWY 1872
Cdd:cd06562 214 NGVYLL----PKDTIVQVWG---GSDEL---KNVLAAGYKvILSSYDFWY 253
|
|
| GH20_SpHex_like |
cd06568 |
A subgroup of the Glycosyl hydrolase family 20 (GH20) catalytic domain found in proteins ... |
1604-1842 |
3.50e-11 |
|
A subgroup of the Glycosyl hydrolase family 20 (GH20) catalytic domain found in proteins similar to the N-acetylhexosaminidase from Streptomyces plicatus (SpHex). SpHex catalyzes the hydrolysis of N-acetyl-beta-hexosaminides. An Asp residue within the active site plays a critical role in substrate-assisted catalysis by orienting the 2-acetamido group and stabilizing the transition state. The GH20 hexosaminidases are thought to act via a catalytic mechanism in which the catalytic nucleophile is not provided by solvent or the enzyme, but by the substrate itself. Proteins belonging to this subgroup lack the C-terminal PKD (polycystic kidney disease I)-like domain found in the chitobiases.
Pssm-ID: 119336 Cd Length: 329 Bit Score: 66.97 E-value: 3.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 1604 SLDAGRKYFSAAQIKEIIDEASKRGYTHLHLLLGND-ALRFLL-NDMTLKVNGKTYSSDEvkaaivhGTDAYYkdphgnh 1681
Cdd:cd06568 7 MLDVARHFFTVAEVKRYIDLLALYKLNVLHLHLTDDqGWRIEIkSWPKLTEIGGSTEVGG-------GPGGYY------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 1682 lTQAEMDDILQYAKTKNIALIPAINSPGHMDAILDAMEQL-GIKDARFSYNGKKSK-RTIDLNNSDAVHFTKALIKKYAE 1759
Cdd:cd06568 73 -TQEDYKDIVAYAAERHITVVPEIDMPGHTNAALAAYPELnCDGKAKPLYTGIEVGfSSLDVDKPTTYEFVDDVFRELAA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 1760 YFSNkvEIFNIGLDEyANDVSKEsgfgllqrtgnypKFINYVNELAKIVKDLHLKPMAFndgfyynNDKSSGAFDSDIII 1839
Cdd:cd06568 152 LTPG--PYIHIGGDE-AHSTPHD-------------DYAYFVNRVRAIVAKYGKTPVGW-------QEIARADLPAGTVA 208
|
...
gi 2461862307 1840 SYW 1842
Cdd:cd06568 209 QYW 211
|
|
| Glyco_hydro_2 |
pfam00703 |
Glycosyl hydrolases family 2; This family contains beta-galactosidase, beta-mannosidase and ... |
226-349 |
3.56e-11 |
|
Glycosyl hydrolases family 2; This family contains beta-galactosidase, beta-mannosidase and beta-glucuronidase activities.
Pssm-ID: 395572 [Multi-domain] Cd Length: 106 Bit Score: 61.72 E-value: 3.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 226 VHLADNGIvmkTPDLSQTAqsgtGSQVHVTAKVYNQSGNASQIRVKSILYERKEDGslgQKAAESELSQPVDVKsgeqvp 305
Cdd:pfam00703 1 VHIEDVFI---TPDLDDDK----TAKVTVEVELENDGDASVEVTLETEIKDADGKT---VAAAAKVLVLGAGET------ 64
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2461862307 306 vnQQFSIVKPKLWSPDNPTLYVLRTELYQNGQKIQTVDQETGFR 349
Cdd:pfam00703 65 --TELEVKNPKLWSPETPNLYTLTVELDKDGKVIDEVSTRFGFR 106
|
|
| FA58C |
cd00057 |
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached ... |
1358-1471 |
3.35e-09 |
|
Coagulation factor 5/8 C-terminal domain, discoidin domain; Cell surface-attached carbohydrate-binding domain, present in eukaryotes and assumed to have horizontally transferred to eubacterial genomes.
Pssm-ID: 238014 [Multi-domain] Cd Length: 143 Bit Score: 57.36 E-value: 3.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 1358 DITLSAGSVQpGAENAVENAnDFNVDSMWHSDWagtSARNLWATFDTGKIRTINGLAYLERMDKIQNGKIIDYEIYASKN 1437
Cdd:cd00057 11 DDQITASSSY-SSGWEASRA-RLNSDNAWTPAV---NDPPQWLQVDLGKTRRVTGIQTQGRKGGGSSEWVTSYKVQYSLD 85
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2461862307 1438 NKDW--------FKVAKGrFADVEKWQEASF-TPVKARYLKLV 1471
Cdd:cd00057 86 GETWttykdkgeEKVFTG-NSDGSTPVTNDFpPPIVARYIRIL 127
|
|
| GH20_chitobiase-like_1 |
cd06570 |
A functionally uncharacterized subgroup of the Glycosyl hydrolase family 20 (GH20) catalytic ... |
1601-1774 |
1.74e-08 |
|
A functionally uncharacterized subgroup of the Glycosyl hydrolase family 20 (GH20) catalytic domain found in proteins similar to the chitobiase of Serratia marcescens, a beta-N-1,4-acetylhexosaminidase that hydrolyzes the beta-1,4-glycosidic linkages in oligomers derived from chitin. Chitin is degraded by a two step process: i) a chitinase hydrolyzes the chitin to oligosaccharides and disaccharides such as di-N-acetyl-D-glucosamine and chitobiose, ii) chitobiase then further degrades these oligomers into monomers. This subgroup lacks the C-terminal PKD (polycystic kidney disease I)-like domain found in the chitobiases. The GH20 hexosaminidases are thought to act via a catalytic mechanism in which the catalytic nucleophile is not provided by solvent or the enzyme, but by the substrate itself.
Pssm-ID: 119338 Cd Length: 311 Bit Score: 58.58 E-value: 1.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 1601 KAISLDAGRKYFSAAQIKEIID--EASKRGYTHLHLLlgndalrfllNDMTLKVNGKTYSSDEVKAAivhgtdayykdpH 1678
Cdd:cd06570 4 RGLLIDVSRHFIPVAVIKRQLDamASVKLNVFHWHLT----------DDQGFRIESKKYPKLQQKAS------------D 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 1679 GNHLTQAEMDDILQYAKTKNIALIPAINSPGHMDAILDAMEQLGIKDARFSYNGKKS--KRTIDLNNSDAVHFTKALIKK 1756
Cdd:cd06570 62 GLYYTQEQIREVVAYARDRGIRVVPEIDVPGHASAIAVAYPELASGPGPYVIERGWGvfEPLLDPTNEETYTFLDNLFGE 141
|
170
....*....|....*...
gi 2461862307 1757 YAEYFSNkvEIFNIGLDE 1774
Cdd:cd06570 142 MAELFPD--EYFHIGGDE 157
|
|
| GH20_Sm-chitobiase-like |
cd06569 |
The chitobiase of Serratia marcescens is a beta-N-1,4-acetylhexosaminidase with a glycosyl ... |
1675-1873 |
2.95e-07 |
|
The chitobiase of Serratia marcescens is a beta-N-1,4-acetylhexosaminidase with a glycosyl hydrolase family 20 (GH20) domain that hydrolyzes the beta-1,4-glycosidic linkages in oligomers derived from chitin. Chitin is degraded by a two step process: i) a chitinase hydrolyzes the chitin to oligosaccharides and disaccharides such as di-N-acetyl-D-glucosamine and chitobiose, ii) chitobiase then further degrades these oligomers into monomers. The GH20 hexosaminidases are thought to act via a catalytic mechanism in which the catalytic nucleophile is not provided by solvent or the enzyme, but by the substrate itself.
Pssm-ID: 119337 Cd Length: 445 Bit Score: 55.38 E-value: 2.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 1675 KDPHGN-HLTQAEMDDILQYAKTKNIALIPAINSPGHMDAILDAMEqlgikdARFSY---NGKKSK----RTIDLNNSDA 1746
Cdd:cd06569 86 TNNSGSgYYSRADYIEILKYAKARHIEVIPEIDMPGHARAAIKAME------ARYRKlmaAGKPAEaeeyRLSDPADTSQ 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 1747 V----HFTKALIK-----KYAeyFSNKV--EI-------------FNIGLDEYANdVSKESGFGLLQRTGNYPKFINYVN 1802
Cdd:cd06569 160 YlsvqFYTDNVINpcmpsTYR--FVDKVidEIarmhqeagqplttIHFGGDEVPE-GAWGGSPACKAQLFAKEGSVKDVE 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 1803 EL--------AKIVKDLHLKPMAFNDGFYYNNDK-SSGAFDSDIIISYWtaGWSGYTVASSKY-LSEKGHKILNTNDAWY 1872
Cdd:cd06569 237 DLkdyffervSKILKAHGITLAGWEDGLLGKDTTnVDGFATPYVWNNVW--GWGYWGGEDRAYkLANKGYDVVLSNATNL 314
|
.
gi 2461862307 1873 Y 1873
Cdd:cd06569 315 Y 315
|
|
| DUF4982 |
pfam16355 |
Domain of unknown function (DUF4982); This family is found in the C-terminal of ... |
716-801 |
2.17e-06 |
|
Domain of unknown function (DUF4982); This family is found in the C-terminal of uncharacterized proteins and beta-galactosidases around 680 residues in length from various Bacteroides species. The function of this protein is unknown.
Pssm-ID: 465102 Cd Length: 62 Bit Score: 46.70 E-value: 2.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2461862307 716 GGKVEVAVYSNAAKVKLVhVSDKgvetDLGTKaftkvttkaghsyqiykgndkQAAEHKNLYLTWKVPYKKGYLRAIAYd 795
Cdd:pfam16355 1 GQPIPVEVYSNADEVELF-LNGK----SLGRK---------------------KKKDGRDYRLRWDVPYEPGELKAVAY- 53
|
....*.
gi 2461862307 796 ENGKVI 801
Cdd:pfam16355 54 KNGKEV 59
|
|
| Big_4 |
pfam07532 |
Bacterial Ig-like domain (group 4); This family consists of bacterial domains with an Ig-like ... |
1016-1073 |
2.26e-04 |
|
Bacterial Ig-like domain (group 4); This family consists of bacterial domains with an Ig-like fold. Members of this family are found in a variety of bacterial surface proteins.
Pssm-ID: 400079 [Multi-domain] Cd Length: 59 Bit Score: 41.15 E-value: 2.26e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2461862307 1016 KNISTAVEKGRVPDLPKYVQAYVKSGNllSAQFPVTWKIPTSSIFDKVGTVTIKGVAD 1073
Cdd:pfam07532 2 ENIEVTVAQGESYTLPTTVTATYSDGS--VKEVPVTWDLTPNVDTSKPGTYTVEGTVE 57
|
|
| |
