|
Name |
Accession |
Description |
Interval |
E-value |
| ChiA |
COG3325 |
Chitinase, GH18 family [Carbohydrate transport and metabolism]; |
285-698 |
4.32e-176 |
|
Chitinase, GH18 family [Carbohydrate transport and metabolism];
Pssm-ID: 442554 [Multi-domain] Cd Length: 391 Bit Score: 507.53 E-value: 4.32e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565447 285 ATTLAGDGGTTGKRVIGYFTQWGIYGRNYRVKNIDssgsAARLTHINYAFGNVR-NNRCEVGitqpsdpnsgaggDAFAD 363
Cdd:COG3325 7 SDTAAAATATSGKRVVGYFTQWGIYGRNYLVKDIP----ASKLTHINYAFANVDpDGKCSVG-------------DAWAK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565447 364 ytkafsaaESVSGSADTWDQPLRGNWNQLKQLKAKYPGMKVLISLGGWTWSRGFSSAAR-PENRQAFVASCIDAYIKGNl 442
Cdd:COG3325 70 --------PSVDGAADDWDQPLKGNFNQLKKLKAKNPNLKVLISIGGWTWSKGFSDAAAtPASRAAFVDSCVDLLRKYN- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565447 443 pvtdgaggagaalgvFDGIDVDWEYPVACGIEC--GKPEDNANFTALMAEFRRQLDAV----RPGLLLTVAVGAGIDKIR 516
Cdd:COG3325 141 ---------------FDGIDIDWEYPGSGGAPGnvYRPEDKANFTALLKELRAQLDALgaetGKHYLLTAAAPAGPDKLD 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565447 517 VTDPAAYHPYLDYINVMTYDFHGAWDAKTNHQSALFDSPNDPSTGDqklYNSNDAIEAFISRGVPAAKLNLGIGYYGRGW 596
Cdd:COG3325 206 GIELPKVAQYLDYVNVMTYDFHGAWSPTTGHQAPLYDSPKDPEAQG---YSVDSAVQAYLAAGVPASKLVLGVPFYGRGW 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565447 597 TGVANANNGLYQTATGAAPGTYEAGIEDWKVLKNLA-----WPSYTDNTAGATWIYNGS--TLWSFDTPANITRKMGYVK 669
Cdd:COG3325 283 TGVTGGNNGLYQPATGPAPGTWEAGVNDYKDLKALYlgsngYTRYWDDVAKAPYLYNGDtgTFISYDDPRSIAAKADYVK 362
|
410 420
....*....|....*....|....*....
gi 896565447 670 TQGLGGAFVWEFSGDDAQGTLTKAVSDGL 698
Cdd:COG3325 363 DKGLGGVMFWELSGDTADGTLLNAIGEGL 391
|
|
| GH18_chitinase |
cd06548 |
The GH18 (glycosyl hydrolases, family 18) type II chitinases hydrolyze chitin, an abundant ... |
299-684 |
4.33e-129 |
|
The GH18 (glycosyl hydrolases, family 18) type II chitinases hydrolyze chitin, an abundant polymer of N-acetylglucosamine and have been identified in bacteria, fungi, insects, plants, viruses, and protozoan parasites. The structure of this domain is an eight-stranded alpha/beta barrel with a pronounced active-site cleft at the C-terminal end of the beta-barrel.
Pssm-ID: 119365 [Multi-domain] Cd Length: 322 Bit Score: 384.67 E-value: 4.33e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565447 299 VIGYFTQWGIYGRNYRVKNidsSGSAARLTHINYAFGNVRNNRCEVgitqpsdpnsgaggdaFADYTKAFSAAESVSGSA 378
Cdd:cd06548 1 VVGYFTNWGIYGRNYFVTD---DIPADKLTHINYAFADIDGDGGVV----------------TSDDEAADEAAQSVDGGA 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565447 379 DTWDQPLRGNWNQLKQLKAKYPGMKVLISLGGWTWSRGFSSAAR-PENRQAFVASCIDAYIKGNlpvtdgaggagaalgv 457
Cdd:cd06548 62 DTDDQPLKGNFGQLRKLKQKNPHLKILLSIGGWTWSGGFSDAAAtEASRAKFADSAVDFIRKYG---------------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565447 458 FDGIDVDWEYPVACG--IECGKPEDNANFTALMAEFRRQLDAV----RPGLLLTVAVGAGIDKIRVTDPAAYHPYLDYIN 531
Cdd:cd06548 126 FDGIDIDWEYPGSGGapGNVARPEDKENFTLLLKELREALDALgaetGRKYLLTIAAPAGPDKLDKLEVAEIAKYLDFIN 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565447 532 VMTYDFHGAWDAKTNHQSALFDSPNDPSTGdqklYNSNDAIEAFISRGVPAAKLNLGIGYYGRGWTGvanannglyqtat 611
Cdd:cd06548 206 LMTYDFHGAWSNTTGHHSNLYASPADPPGG----YSVDAAVNYYLSAGVPPEKLVLGVPFYGRGWTG------------- 268
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 896565447 612 gaapgtyeagiedwkvlknlaWPSYTDNTAGATWIYNGST--LWSFDTPANITRKMGYVKTQGLGGAFVWEFSGD 684
Cdd:cd06548 269 ---------------------YTRYWDEVAKAPYLYNPSTktFISYDDPRSIKAKADYVKDKGLGGVMFWELSGD 322
|
|
| Glyco_18 |
smart00636 |
Glyco_18 domain; |
298-684 |
3.41e-115 |
|
Glyco_18 domain;
Pssm-ID: 214753 [Multi-domain] Cd Length: 334 Bit Score: 349.67 E-value: 3.41e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565447 298 RVIGYFTQWGIYGRNYRVKNIDSSGsaarLTHINYAFGNVRNNrcevgitqpsdpNSGAGGDAFADYtkafsaaesvsgs 377
Cdd:smart00636 1 RVVGYFTNWGVYGRNFPVDDIPASK----LTHIIYAFANIDPD------------GTVTIGDEWADI------------- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565447 378 adtwdqplrGNWNQLKQLKAKYPGMKVLISLGGWTWSRGFSSAAR-PENRQAFVASCIDAYIKGNlpvtdgaggagaalg 456
Cdd:smart00636 52 ---------GNFGQLKALKKKNPGLKVLLSIGGWTESDNFSSMLSdPASRKKFIDSIVSFLKKYG--------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565447 457 vFDGIDVDWEYPVACGiecgkpEDNANFTALMAEFRRQLD---AVRPGLLLTVAVGAGIDKIRVTDP--AAYHPYLDYIN 531
Cdd:smart00636 108 -FDGIDIDWEYPGGRG------DDRENYTALLKELREALDkegAEGKGYLLTIAVPAGPDKIDKGYGdlPAIAKYLDFIN 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565447 532 VMTYDFHGAWDAKTNHQSALFDSPNDPstgdqKLYNSNDAIEAFISRGVPAAKLNLGIGYYGRGWTGVANANNGLYQTAT 611
Cdd:smart00636 181 LMTYDFHGAWSNPTGHNAPLYAGPGDP-----EKYNVDYAVKYYLCKGVPPSKLVLGIPFYGRGWTLVDGSNNGPGAPFT 255
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 896565447 612 GAA---PGTYEAGIEDWKVL-KNLAWPSYTDNTAGATWIYNGST--LWSFDTPANITRKMGYVKTQGLGGAFVWEFSGD 684
Cdd:smart00636 256 GPAtggPGTWEGGVVDYREIcKLLGATVVYDDTAKAPYAYNPGTgqWVSYDDPRSIKAKADYVKDKGLGGVMIWELDAD 334
|
|
| Glyco_hydro_18 |
pfam00704 |
Glycosyl hydrolases family 18; |
298-684 |
4.66e-95 |
|
Glycosyl hydrolases family 18;
Pssm-ID: 425828 [Multi-domain] Cd Length: 311 Bit Score: 296.67 E-value: 4.66e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565447 298 RVIGYFTQWGIYGRNyrvKNIDSSGsaarLTHINYAFGNVRNNRCEVGITQPSDpnsgaggdafadytkafsaaesvsgs 377
Cdd:pfam00704 1 RIVGYYTSWGVYRNG---NFLPSDK----LTHIIYAFANIDGSDGTLFIGDWDL-------------------------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565447 378 adtwdqplrGNWNQLKQLK-AKYPGMKVLISLGGWTWSRGFSSAAR-PENRQAFVASCIDAYIKGNlpvtdgaggagaal 455
Cdd:pfam00704 48 ---------GNFEQLKKLKkQKNPGVKVLLSIGGWTDSTGFSLMASnPASRKKFADSIVSFLRKYG-------------- 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565447 456 gvFDGIDVDWEYPVacgiecGKPEDNANFTALMAEFRRQLDAV--RPGLLLTVAVGAGIDKIRV-TDPAAYHPYLDYINV 532
Cdd:pfam00704 105 --FDGIDIDWEYPG------GNPEDKENYDLLLRELRAALDEAkgGKKYLLSAAVPASYPDLDKgYDLPKIAKYLDFINV 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565447 533 MTYDFHGAWDAKTNHQSALFDSPNdpstgdqklYNSNDAIEAFISRGVPAAKLNLGIGYYGRGWTGVANANNglyqtatg 612
Cdd:pfam00704 177 MTYDFHGSWDNVTGHHAPLYGGGS---------YNVDYAVKYYLKQGVPASKLVLGVPFYGRSWTLVNGSGN-------- 239
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 896565447 613 aapgTYEAGIEDWKVLKNLA----WPSYTDNTAGATWIYNGSTLWSFDTPANITRKMGYVKTQGLGGAFVWEFSGD 684
Cdd:pfam00704 240 ----TWEDGVLAYKEICNLLkdngATVVWDDVAKAPYVYDGDQFITYDDPRSIATKVDYVKAKGLGGVMIWSLDAD 311
|
|
| Big_7 |
pfam17957 |
Bacterial Ig domain; This entry represents a bacterial ig-like domain that is found in ... |
105-171 |
8.04e-18 |
|
Bacterial Ig domain; This entry represents a bacterial ig-like domain that is found in glycosyl hydrolase enzymes.
Pssm-ID: 436171 [Multi-domain] Cd Length: 67 Bit Score: 78.03 E-value: 8.04e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 896565447 105 VSLTSPANGATFSaGSTVNVTANASDpDGSVAKVEFFRDGSTLGVATSAPYAASW--ANASAGSHTLRA 171
Cdd:pfam17957 1 VSITSPANGATVS-GGTVTISATASD-DGGVSKVEFYVDGTLVGTDTSAPYSFTWttTALANGTHTITV 67
|
|
| FN3 |
COG3401 |
Fibronectin type 3 domain [General function prediction only]; |
75-287 |
8.36e-14 |
|
Fibronectin type 3 domain [General function prediction only];
Pssm-ID: 442628 [Multi-domain] Cd Length: 603 Bit Score: 74.65 E-value: 8.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565447 75 WNAPPDHPAGAPYYTNLGACDGSGSNQPPVVSLTSPANGATFSAGSTVNVTANASDPDGSVAKVEFFRDGSTLGVATSAP 154
Cdd:COG3401 115 DEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTSTTLVD 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565447 155 YAASWANASAGSHTLRAVATDNNNATTSTATititvnaAGGDTTAPSVPGGLAVGTRTANSIALSWSPSTDntggSGVAG 234
Cdd:COG3401 195 GGGDIEPGTTYYYRVAATDTGGESAPSNEVS-------VTTPTTPPSAPTGLTATADTPGSVTLSWDPVTE----SDATG 263
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 896565447 235 YDVYRNGS------LVGSPSSASYIDGGLTASTTYRYRVRARDNAGNASAQGTEISATT 287
Cdd:COG3401 264 YRVYRSNSgdgpftKVATVTTTSYTDTGLTNGTTYYYRVTAVDAAGNESAPSNVVSVTT 322
|
|
| FN3 |
smart00060 |
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ... |
200-274 |
1.43e-10 |
|
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.
Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 58.01 E-value: 1.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565447 200 PSVPGGLAVGTRTANSIALSWSPSTDNTGGSGVAGYDVYRNGS------LVGSPSSASYIDGGLTASTTYRYRVRARDNA 273
Cdd:smart00060 1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEgsewkeVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGA 80
|
.
gi 896565447 274 G 274
Cdd:smart00060 81 G 81
|
|
| FN3 |
cd00063 |
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ... |
200-287 |
3.50e-10 |
|
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.
Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 57.12 E-value: 3.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565447 200 PSVPGGLAVGTRTANSIALSWSPSTDNtgGSGVAGYDVYRNGSL--------VGSPSSASYIDGGLTASTTYRYRVRARd 271
Cdd:cd00063 1 PSPPTNLRVTDVTSTSVTLSWTPPEDD--GGPITGYVVEYREKGsgdwkeveVTPGSETSYTLTGLKPGTEYEFRVRAV- 77
|
90
....*....|....*.
gi 896565447 272 NAGNASAQGTEISATT 287
Cdd:cd00063 78 NGGGESPPSESVTVTT 93
|
|
| ChiA1_BD |
cd12214 |
chitin-binding domain of Chi A1-like proteins; This group contains proteins related to the ... |
49-88 |
1.13e-06 |
|
chitin-binding domain of Chi A1-like proteins; This group contains proteins related to the chitin binding domain of chitinase A1 (ChiA1) of Bacillus circulans WL-12. Glycosidase ChiA1 hydrolyzes chitin and is comprised of several domains: the C-terminal chitin binding domain, an N-terminal and catalytic domain, and 2 fibronectin type III-like domains. Chitinases function in invertebrates in the degradation of old exoskeletons, in fungi to utilize chitin in cell walls, and in bacteria which use chitin as an energy source. Bacillus circulans WL-12 ChiA1 facilitates invasion of fungal cell walls. The ChiAi chitin binding domain is required for the specific recognition of insoluble chitin. although topologically and structurally related, ChiA1 lacks the characteristic aromatic residues of Erwinia chrysanthemi endoglucanase Z (CBD(EGZ)).
Pssm-ID: 213177 [Multi-domain] Cd Length: 45 Bit Score: 45.79 E-value: 1.13e-06
10 20 30 40
....*....|....*....|....*....|....*....|
gi 896565447 49 WDQAKIYRAGDTLQKGGVLYRANQDIWNAPPDHPAGAPYY 88
Cdd:cd12214 2 WAAGTTYKAGDIVTYNGKLYRCLQAHTSLAGWEPPAVPAL 41
|
|
| fn3 |
pfam00041 |
Fibronectin type III domain; |
201-275 |
2.40e-06 |
|
Fibronectin type III domain;
Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 45.87 E-value: 2.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565447 201 SVPGGLAVGTRTANSIALSWSPSTDntGGSGVAGYDV-YRNGSLVG-------SPSSASYIDGGLTASTTYRYRVRARDN 272
Cdd:pfam00041 1 SAPSNLTVTDVTSTSLTVSWTPPPD--GNGPITGYEVeYRPKNSGEpwneitvPGTTTSVTLTGLKPGTEYEVRVQAVNG 78
|
...
gi 896565447 273 AGN 275
Cdd:pfam00041 79 GGE 81
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| ChiA |
COG3325 |
Chitinase, GH18 family [Carbohydrate transport and metabolism]; |
285-698 |
4.32e-176 |
|
Chitinase, GH18 family [Carbohydrate transport and metabolism];
Pssm-ID: 442554 [Multi-domain] Cd Length: 391 Bit Score: 507.53 E-value: 4.32e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565447 285 ATTLAGDGGTTGKRVIGYFTQWGIYGRNYRVKNIDssgsAARLTHINYAFGNVR-NNRCEVGitqpsdpnsgaggDAFAD 363
Cdd:COG3325 7 SDTAAAATATSGKRVVGYFTQWGIYGRNYLVKDIP----ASKLTHINYAFANVDpDGKCSVG-------------DAWAK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565447 364 ytkafsaaESVSGSADTWDQPLRGNWNQLKQLKAKYPGMKVLISLGGWTWSRGFSSAAR-PENRQAFVASCIDAYIKGNl 442
Cdd:COG3325 70 --------PSVDGAADDWDQPLKGNFNQLKKLKAKNPNLKVLISIGGWTWSKGFSDAAAtPASRAAFVDSCVDLLRKYN- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565447 443 pvtdgaggagaalgvFDGIDVDWEYPVACGIEC--GKPEDNANFTALMAEFRRQLDAV----RPGLLLTVAVGAGIDKIR 516
Cdd:COG3325 141 ---------------FDGIDIDWEYPGSGGAPGnvYRPEDKANFTALLKELRAQLDALgaetGKHYLLTAAAPAGPDKLD 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565447 517 VTDPAAYHPYLDYINVMTYDFHGAWDAKTNHQSALFDSPNDPSTGDqklYNSNDAIEAFISRGVPAAKLNLGIGYYGRGW 596
Cdd:COG3325 206 GIELPKVAQYLDYVNVMTYDFHGAWSPTTGHQAPLYDSPKDPEAQG---YSVDSAVQAYLAAGVPASKLVLGVPFYGRGW 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565447 597 TGVANANNGLYQTATGAAPGTYEAGIEDWKVLKNLA-----WPSYTDNTAGATWIYNGS--TLWSFDTPANITRKMGYVK 669
Cdd:COG3325 283 TGVTGGNNGLYQPATGPAPGTWEAGVNDYKDLKALYlgsngYTRYWDDVAKAPYLYNGDtgTFISYDDPRSIAAKADYVK 362
|
410 420
....*....|....*....|....*....
gi 896565447 670 TQGLGGAFVWEFSGDDAQGTLTKAVSDGL 698
Cdd:COG3325 363 DKGLGGVMFWELSGDTADGTLLNAIGEGL 391
|
|
| GH18_chitinase |
cd06548 |
The GH18 (glycosyl hydrolases, family 18) type II chitinases hydrolyze chitin, an abundant ... |
299-684 |
4.33e-129 |
|
The GH18 (glycosyl hydrolases, family 18) type II chitinases hydrolyze chitin, an abundant polymer of N-acetylglucosamine and have been identified in bacteria, fungi, insects, plants, viruses, and protozoan parasites. The structure of this domain is an eight-stranded alpha/beta barrel with a pronounced active-site cleft at the C-terminal end of the beta-barrel.
Pssm-ID: 119365 [Multi-domain] Cd Length: 322 Bit Score: 384.67 E-value: 4.33e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565447 299 VIGYFTQWGIYGRNYRVKNidsSGSAARLTHINYAFGNVRNNRCEVgitqpsdpnsgaggdaFADYTKAFSAAESVSGSA 378
Cdd:cd06548 1 VVGYFTNWGIYGRNYFVTD---DIPADKLTHINYAFADIDGDGGVV----------------TSDDEAADEAAQSVDGGA 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565447 379 DTWDQPLRGNWNQLKQLKAKYPGMKVLISLGGWTWSRGFSSAAR-PENRQAFVASCIDAYIKGNlpvtdgaggagaalgv 457
Cdd:cd06548 62 DTDDQPLKGNFGQLRKLKQKNPHLKILLSIGGWTWSGGFSDAAAtEASRAKFADSAVDFIRKYG---------------- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565447 458 FDGIDVDWEYPVACG--IECGKPEDNANFTALMAEFRRQLDAV----RPGLLLTVAVGAGIDKIRVTDPAAYHPYLDYIN 531
Cdd:cd06548 126 FDGIDIDWEYPGSGGapGNVARPEDKENFTLLLKELREALDALgaetGRKYLLTIAAPAGPDKLDKLEVAEIAKYLDFIN 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565447 532 VMTYDFHGAWDAKTNHQSALFDSPNDPSTGdqklYNSNDAIEAFISRGVPAAKLNLGIGYYGRGWTGvanannglyqtat 611
Cdd:cd06548 206 LMTYDFHGAWSNTTGHHSNLYASPADPPGG----YSVDAAVNYYLSAGVPPEKLVLGVPFYGRGWTG------------- 268
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 896565447 612 gaapgtyeagiedwkvlknlaWPSYTDNTAGATWIYNGST--LWSFDTPANITRKMGYVKTQGLGGAFVWEFSGD 684
Cdd:cd06548 269 ---------------------YTRYWDEVAKAPYLYNPSTktFISYDDPRSIKAKADYVKDKGLGGVMFWELSGD 322
|
|
| Glyco_18 |
smart00636 |
Glyco_18 domain; |
298-684 |
3.41e-115 |
|
Glyco_18 domain;
Pssm-ID: 214753 [Multi-domain] Cd Length: 334 Bit Score: 349.67 E-value: 3.41e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565447 298 RVIGYFTQWGIYGRNYRVKNIDSSGsaarLTHINYAFGNVRNNrcevgitqpsdpNSGAGGDAFADYtkafsaaesvsgs 377
Cdd:smart00636 1 RVVGYFTNWGVYGRNFPVDDIPASK----LTHIIYAFANIDPD------------GTVTIGDEWADI------------- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565447 378 adtwdqplrGNWNQLKQLKAKYPGMKVLISLGGWTWSRGFSSAAR-PENRQAFVASCIDAYIKGNlpvtdgaggagaalg 456
Cdd:smart00636 52 ---------GNFGQLKALKKKNPGLKVLLSIGGWTESDNFSSMLSdPASRKKFIDSIVSFLKKYG--------------- 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565447 457 vFDGIDVDWEYPVACGiecgkpEDNANFTALMAEFRRQLD---AVRPGLLLTVAVGAGIDKIRVTDP--AAYHPYLDYIN 531
Cdd:smart00636 108 -FDGIDIDWEYPGGRG------DDRENYTALLKELREALDkegAEGKGYLLTIAVPAGPDKIDKGYGdlPAIAKYLDFIN 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565447 532 VMTYDFHGAWDAKTNHQSALFDSPNDPstgdqKLYNSNDAIEAFISRGVPAAKLNLGIGYYGRGWTGVANANNGLYQTAT 611
Cdd:smart00636 181 LMTYDFHGAWSNPTGHNAPLYAGPGDP-----EKYNVDYAVKYYLCKGVPPSKLVLGIPFYGRGWTLVDGSNNGPGAPFT 255
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 896565447 612 GAA---PGTYEAGIEDWKVL-KNLAWPSYTDNTAGATWIYNGST--LWSFDTPANITRKMGYVKTQGLGGAFVWEFSGD 684
Cdd:smart00636 256 GPAtggPGTWEGGVVDYREIcKLLGATVVYDDTAKAPYAYNPGTgqWVSYDDPRSIKAKADYVKDKGLGGVMIWELDAD 334
|
|
| Glyco_hydro_18 |
pfam00704 |
Glycosyl hydrolases family 18; |
298-684 |
4.66e-95 |
|
Glycosyl hydrolases family 18;
Pssm-ID: 425828 [Multi-domain] Cd Length: 311 Bit Score: 296.67 E-value: 4.66e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565447 298 RVIGYFTQWGIYGRNyrvKNIDSSGsaarLTHINYAFGNVRNNRCEVGITQPSDpnsgaggdafadytkafsaaesvsgs 377
Cdd:pfam00704 1 RIVGYYTSWGVYRNG---NFLPSDK----LTHIIYAFANIDGSDGTLFIGDWDL-------------------------- 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565447 378 adtwdqplrGNWNQLKQLK-AKYPGMKVLISLGGWTWSRGFSSAAR-PENRQAFVASCIDAYIKGNlpvtdgaggagaal 455
Cdd:pfam00704 48 ---------GNFEQLKKLKkQKNPGVKVLLSIGGWTDSTGFSLMASnPASRKKFADSIVSFLRKYG-------------- 104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565447 456 gvFDGIDVDWEYPVacgiecGKPEDNANFTALMAEFRRQLDAV--RPGLLLTVAVGAGIDKIRV-TDPAAYHPYLDYINV 532
Cdd:pfam00704 105 --FDGIDIDWEYPG------GNPEDKENYDLLLRELRAALDEAkgGKKYLLSAAVPASYPDLDKgYDLPKIAKYLDFINV 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565447 533 MTYDFHGAWDAKTNHQSALFDSPNdpstgdqklYNSNDAIEAFISRGVPAAKLNLGIGYYGRGWTGVANANNglyqtatg 612
Cdd:pfam00704 177 MTYDFHGSWDNVTGHHAPLYGGGS---------YNVDYAVKYYLKQGVPASKLVLGVPFYGRSWTLVNGSGN-------- 239
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 896565447 613 aapgTYEAGIEDWKVLKNLA----WPSYTDNTAGATWIYNGSTLWSFDTPANITRKMGYVKTQGLGGAFVWEFSGD 684
Cdd:pfam00704 240 ----TWEDGVLAYKEICNLLkdngATVVWDDVAKAPYVYDGDQFITYDDPRSIATKVDYVKAKGLGGVMIWSLDAD 311
|
|
| GH18_chitolectin_chitotriosidase |
cd02872 |
This conserved domain family includes a large number of catalytically inactive chitinase-like ... |
299-698 |
5.35e-81 |
|
This conserved domain family includes a large number of catalytically inactive chitinase-like lectins (chitolectins) including YKL-39, YKL-40 (HCGP39), YM1, oviductin, and AMCase (acidic mammalian chitinase), as well as catalytically active chitotriosidases. The conserved domain is an eight-stranded alpha/beta barrel fold belonging to the family 18 glycosyl hydrolases. The fold has a pronounced active-site cleft at the C-terminal end of the beta-barrel. The chitolectins lack a key active site glutamate (the proton donor required for hydrolytic activity) but retain highly conserved residues involved in oligosaccharide binding. Chitotriosidase is a chitinolytic enzyme expressed in maturing macrophages, which suggests that it plays a part in antimicrobial defense. Chitotriosidase hydrolyzes chitotriose, as well as colloidal chitin to yield chitobiose and is therefore considered an exochitinase. Chitotriosidase occurs in two major forms, the large form being converted to the small form by either RNA or post-translational processing. Although the small form, containing the chitinase domain alone, is sufficient for the chitinolytic activity, the additional C-terminal chitin-binding domain of the large form plays a role in processing colloidal chitin. The chitotriosidase gene is nonessential in humans, as about 35% of the population are heterozygous and 6% homozygous for an inactivated form of the gene. HCGP39 is a 39-kDa human cartilage glycoprotein thought to play a role in connective tissue remodeling and defense against pathogens.
Pssm-ID: 119351 [Multi-domain] Cd Length: 362 Bit Score: 261.72 E-value: 5.35e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565447 299 VIGYFTQWGIYgRN----YRVKNIDssgsaARL-THINYAFGNVRNnrcevgitqpsdpnsgaggdafaDYTKAfsaaes 373
Cdd:cd02872 1 VVCYFTNWAQY-RPgngkFVPENID-----PFLcTHIIYAFAGLNP-----------------------DGNII------ 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565447 374 vsgSADTWDQPLRGNWNQLKQLKAKYPGMKVLISLGGWTW-SRGFSS-AARPENRQAFVASCIDAYIKGNlpvtdgagga 451
Cdd:cd02872 46 ---ILDEWNDIDLGLYERFNALKEKNPNLKTLLAIGGWNFgSAKFSAmAASPENRKTFIKSAIAFLRKYG---------- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565447 452 gaalgvFDGIDVDWEYPVACGiecGKPEDNANFTALMAEFRRQLDAVRPGLLLTVAVGAGIDKIRvtdpAAYH-----PY 526
Cdd:cd02872 113 ------FDGLDLDWEYPGQRG---GPPEDKENFVTLLKELREAFEPEAPRLLLTAAVSAGKETID----AAYDipeisKY 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565447 527 LDYINVMTYDFHGAWDAKTNHQSALFDSPNDpsTGDQKLYNSNDAIEAFISRGVPAAKLNLGIGYYGRGWTGVANANNGL 606
Cdd:cd02872 180 LDFINVMTYDFHGSWEGVTGHNSPLYAGSAD--TGDQKYLNVDYAIKYWLSKGAPPEKLVLGIPTYGRSFTLASPSNTGV 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565447 607 YQTATGAA-PGTY--EAGI----EDWKVLKNlAWPSYTDNTAGATWIYNGSTLWSFDTPANITRKMGYVKTQGLGGAFVW 679
Cdd:cd02872 258 GAPASGPGtAGPYtrEAGFlayyEICEFLKS-GWTVVWDDEQKVPYAYKGNQWVGYDDEESIALKVQYLKSKGLGGAMVW 336
|
410 420
....*....|....*....|....*.
gi 896565447 680 EFSGDDAQGT-------LTKAVSDGL 698
Cdd:cd02872 337 SIDLDDFRGTcgqgkypLLNAINRAL 362
|
|
| GH18_plant_chitinase_class_V |
cd02879 |
The class V plant chitinases have a glycosyl hydrolase family 18 (GH18) domain, but lack the ... |
317-690 |
1.59e-39 |
|
The class V plant chitinases have a glycosyl hydrolase family 18 (GH18) domain, but lack the chitin-binding domain present in other GH18 enzymes. The GH18 domain of the class V chitinases has endochitinase activity in some cases and no catalytic activity in others. Included in this family is a lectin found in black locust (Robinia pseudoacacia) bark, which binds chitin but lacks chitinase activity. Also included is a chitinase-related receptor-like kinase (CHRK1) from tobacco (Nicotiana tabacum), with an N-terminal GH18 domain and a C-terminal kinase domain, which is thought to be part of a plant signaling pathway. The GH18 domain of CHRK1 is expressed extracellularly where it binds chitin but lacks chitinase activity.
Pssm-ID: 119358 [Multi-domain] Cd Length: 299 Bit Score: 147.51 E-value: 1.59e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565447 317 NIDSSgsaaRLTHINYAFGNVRNNRCEVGITQPSDPnsgaggdAFADYTKAFsaaesvsgsadtwdqplrgnwnqlkqlK 396
Cdd:cd02879 20 NIDSS----LFTHLFYAFADLDPSTYEVVISPSDES-------EFSTFTETV---------------------------K 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565447 397 AKYPGMKVLISLGGWTWSRG-FSS-AARPENRQAFVASCID-AYIKGnlpvtdgaggagaalgvFDGIDVDWEYPvacgi 473
Cdd:cd02879 62 RKNPSVKTLLSIGGGGSDSSaFAAmASDPTARKAFINSSIKvARKYG-----------------FDGLDLDWEFP----- 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565447 474 ecGKPEDNANFTALMAEFRR--QLDAV---RPGLLLTVAVGAGIDKIRVTDPAAYH-----PYLDYINVMTYDFHGAWDA 543
Cdd:cd02879 120 --SSQVEMENFGKLLEEWRAavKDEARssgRPPLLLTAAVYFSPILFLSDDSVSYPieainKNLDWVNVMAYDYYGSWES 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565447 544 KTN-HQSALFDSPNDPSTgdqklynsNDAIEAFISRGVPAAKLNLGIGYYGRGWTgvananngLYQTATGaapGTYeagi 622
Cdd:cd02879 198 NTTgPAAALYDPNSNVST--------DYGIKSWIKAGVPAKKLVLGLPLYGRAWT--------LYDTTTV---SSY---- 254
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 896565447 623 edwkvlknlawpsytdNTAGATWIyngstlwSFDTPANITRKMGYVKTQGLGGAFVWEFSGDDAQGTL 690
Cdd:cd02879 255 ----------------VYAGTTWI-------GYDDVQSIAVKVKYAKQKGLLGYFAWAVGYDDNNWLS 299
|
|
| GH18_chitinase-like |
cd00598 |
The GH18 (glycosyl hydrolase, family 18) type II chitinases hydrolyze chitin, an abundant ... |
299-536 |
8.08e-32 |
|
The GH18 (glycosyl hydrolase, family 18) type II chitinases hydrolyze chitin, an abundant polymer of beta-1,4-linked N-acetylglucosamine (GlcNAc) which is a major component of the cell wall of fungi and the exoskeleton of arthropods. Chitinases have been identified in viruses, bacteria, fungi, protozoan parasites, insects, and plants. The structure of the GH18 domain is an eight-stranded beta/alpha barrel with a pronounced active-site cleft at the C-terminal end of the beta-barrel. The GH18 family includes chitotriosidase, chitobiase, hevamine, zymocin-alpha, narbonin, SI-CLP (stabilin-1 interacting chitinase-like protein), IDGF (imaginal disc growth factor), CFLE (cortical fragment-lytic enzyme) spore hydrolase, the type III and type V plant chitinases, the endo-beta-N-acetylglucosaminidases, and the chitolectins. The GH85 (glycosyl hydrolase, family 85) ENGases (endo-beta-N-acetylglucosaminidases) are closely related to the GH18 chitinases and are included in this alignment model.
Pssm-ID: 119349 [Multi-domain] Cd Length: 210 Bit Score: 122.87 E-value: 8.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565447 299 VIGYFTQWGIYGRNYrVKNIDSSGsaarLTHINYAFgnvrnnrcevgitqpSDPNSGAGGDAFADytkafsaaesvsgsa 378
Cdd:cd00598 1 VICYYDGWSSGRGPD-PTDIPLSL----CTHIIYAF---------------AEISSDGSLNLFGD--------------- 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565447 379 dTWDQPLrgnWNQLKQLKAKYPGMKVLISLGGWTWSRGFSSAARPENRQAFVASCIDAYIKGNlpvtdgaggagaalgvF 458
Cdd:cd00598 46 -KSEEPL---KGALEELASKKPGLKVLISIGGWTDSSPFTLASDPASRAAFANSLVSFLKTYG----------------F 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565447 459 DGIDVDWEYPVACGIecgkpEDNANFTALMAEFRRQLDAvrPGLLLTVAVGAGIDKIrvtDPAAYHP----YLDYINVMT 534
Cdd:cd00598 106 DGVDIDWEYPGAADN-----SDRENFITLLRELRSALGA--ANYLLTIAVPASYFDL---GYAYDVPaigdYVDFVNVMT 175
|
..
gi 896565447 535 YD 536
Cdd:cd00598 176 YD 177
|
|
| GH18_zymocin_alpha |
cd02878 |
Zymocin, alpha subunit. Zymocin is a heterotrimeric enzyme that inhibits yeast cell cycle ... |
300-679 |
1.96e-25 |
|
Zymocin, alpha subunit. Zymocin is a heterotrimeric enzyme that inhibits yeast cell cycle progression. The zymocin alpha subunit has a chitinase activity that is essential for holoenzyme action from the cell exterior while the gamma subunit contains the intracellular toxin responsible for G1 phase cell cycle arrest. The zymocin alpha and beta subunits are thought to act from the cell's exterior by docking to the cell wall-associated chitin, thus mediating gamma-toxin translocation. The alpha subunit has an eight-stranded TIM barrel fold similar to that of family 18 glycosyl hydrolases such as hevamine, chitolectin, and chitobiase.
Pssm-ID: 119357 [Multi-domain] Cd Length: 345 Bit Score: 108.17 E-value: 1.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565447 300 IGYFTQWGiYGR---NYRVKNIDSSGsaarLTHINYAFGNVrnnrcevgitqpsdpnsgaggdafadyTKAFSaaesVSg 376
Cdd:cd02878 3 IAYFEAYN-LDRpclNMDVTQIDTSK----YTHIHFAFANI---------------------------TSDFS----VD- 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565447 377 sadtwDQPLRGNWNQLKQLKakypGMKVLISLGGWTWSRG------FSSAARPENRQAFVASCIDAYIKGNLpvtdgagg 450
Cdd:cd02878 46 -----VSSVQEQFSDFKKLK----GVKKILSFGGWDFSTSpstyqiFRDAVKPANRDTFANNVVNFVNKYNL-------- 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565447 451 agaalgvfDGIDVDWEYPVAC---GIECGKPEDNANFTALMAEFRRQLdavRPGLLLTVAVgagidkirvtdPAAY---- 523
Cdd:cd02878 109 --------DGVDFDWEYPGAPdipGIPAGDPDDGKNYLEFLKLLKSKL---PSGKSLSIAA-----------PASYwylk 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565447 524 -------HPYLDYINVMTYDFHGAWDAktNHQSALFDSPNDPSTGDQ-KLYNSNDAIEAFISRGVPAAKLNLGIGYYGR- 594
Cdd:cd02878 167 gfpikdmAKYVDYIVYMTYDLHGQWDY--GNKWASPGCPAGNCLRSHvNKTETLDALSMITKAGVPSNKVVVGVASYGRs 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565447 595 ----------------GWTGVANANNGlyqTATGAAPGTYEAGIEDWKVLKNLAWpsYTDNTAGATWIYNGSTLWSFDTP 658
Cdd:cd02878 245 fkmadpgctgpgctftGPGSGAEAGRC---TCTAGYGAISEIEIIDISKSKNKRW--YDTDSDSDILVYDDDQWVAYMSP 319
|
410 420
....*....|....*....|.
gi 896565447 659 ANITRKMGYVKTQGLGGAFVW 679
Cdd:cd02878 320 ATKAARIEWYKGLNFGGTSDW 340
|
|
| GH18_IDGF |
cd02873 |
The IDGF's (imaginal disc growth factors) are a family of growth factors identified in insects ... |
386-692 |
2.48e-25 |
|
The IDGF's (imaginal disc growth factors) are a family of growth factors identified in insects that include at least five members, some of which are encoded by genes in a tight cluster. The IDGF's have an eight-stranded alpha/beta barrel fold and are related to the glycosyl hydrolase family 18 (GH18) chitinases, but they have an amino acid substitution known to abolish chitinase catalytic activity. IDGFs may have evolved from chitinases to gain new functions as growth factors, interacting with cell surface glycoproteins involved in growth-promoting processes.
Pssm-ID: 119352 [Multi-domain] Cd Length: 413 Bit Score: 108.94 E-value: 2.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565447 386 RGNWNQLKQLKAKYPGMKVLISLGG-WTWSRGFSSA------ARPENRQAFVASCIDAyIKGNlpvtdgaggagaalgVF 458
Cdd:cd02873 59 KSHYRAITSLKRKYPHLKVLLSVGGdRDTDEEGENEkyllllESSESRNAFINSAHSL-LKTY---------------GF 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565447 459 DGIDVDWEYPVAcgiecgKP-----------------------------EDNANFTALMAEFRRQLdavRP-GLLLTVAV 508
Cdd:cd02873 123 DGLDLAWQFPKN------KPkkvrgtfgsawhsfkklftgdsvvdekaaEHKEQFTALVRELKNAL---RPdGLLLTLTV 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565447 509 GAGIDKIRVTDPAAYHPYLDYINVMTYDFHgawDAKTNHQSALFDSPNDPSTGDQKLYNSNDAIEAFISRGVPAAKLNLG 588
Cdd:cd02873 194 LPHVNSTWYFDVPAIANNVDFVNLATFDFL---TPERNPEEADYTAPIYELYERNPHHNVDYQVKYWLNQGTPASKLNLG 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565447 589 IGYYGRGWTgvANANNGL-----YQTATGAAP-GTY--EAGIEDW---------------------------KVLKNLAW 633
Cdd:cd02873 271 IATYGRAWK--LTKDSGItgvppVLETDGPGPaGPQtkTPGLLSWpeicsklpnpanlkgadaplrkvgdptKRFGSYAY 348
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 896565447 634 PSYTDNTAGATWIyngstlwSFDTPANITRKMGYVKTQGLGGAFVWEFSGDDAQGTLTK 692
Cdd:cd02873 349 RPADENGEHGIWV-------SYEDPDTAANKAGYAKAKGLGGVALFDLSLDDFRGQCTG 400
|
|
| Big_7 |
pfam17957 |
Bacterial Ig domain; This entry represents a bacterial ig-like domain that is found in ... |
105-171 |
8.04e-18 |
|
Bacterial Ig domain; This entry represents a bacterial ig-like domain that is found in glycosyl hydrolase enzymes.
Pssm-ID: 436171 [Multi-domain] Cd Length: 67 Bit Score: 78.03 E-value: 8.04e-18
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 896565447 105 VSLTSPANGATFSaGSTVNVTANASDpDGSVAKVEFFRDGSTLGVATSAPYAASW--ANASAGSHTLRA 171
Cdd:pfam17957 1 VSITSPANGATVS-GGTVTISATASD-DGGVSKVEFYVDGTLVGTDTSAPYSFTWttTALANGTHTITV 67
|
|
| FN3 |
COG3401 |
Fibronectin type 3 domain [General function prediction only]; |
75-287 |
8.36e-14 |
|
Fibronectin type 3 domain [General function prediction only];
Pssm-ID: 442628 [Multi-domain] Cd Length: 603 Bit Score: 74.65 E-value: 8.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565447 75 WNAPPDHPAGAPYYTNLGACDGSGSNQPPVVSLTSPANGATFSAGSTVNVTANASDPDGSVAKVEFFRDGSTLGVATSAP 154
Cdd:COG3401 115 DEVPSPAVGTATTATAVAGGAATAGTYALGAGLYGVDGANASGTTASSVAGAGVVVSPDTSATAAVATTSLTVTSTTLVD 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565447 155 YAASWANASAGSHTLRAVATDNNNATTSTATititvnaAGGDTTAPSVPGGLAVGTRTANSIALSWSPSTDntggSGVAG 234
Cdd:COG3401 195 GGGDIEPGTTYYYRVAATDTGGESAPSNEVS-------VTTPTTPPSAPTGLTATADTPGSVTLSWDPVTE----SDATG 263
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 896565447 235 YDVYRNGS------LVGSPSSASYIDGGLTASTTYRYRVRARDNAGNASAQGTEISATT 287
Cdd:COG3401 264 YRVYRSNSgdgpftKVATVTTTSYTDTGLTNGTTYYYRVTAVDAAGNESAPSNVVSVTT 322
|
|
| FN3 |
COG3401 |
Fibronectin type 3 domain [General function prediction only]; |
196-414 |
2.17e-13 |
|
Fibronectin type 3 domain [General function prediction only];
Pssm-ID: 442628 [Multi-domain] Cd Length: 603 Bit Score: 73.50 E-value: 2.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565447 196 DTTAPSVPGGLAVGTRTANSIALSWSPSTDNtggsGVAGYDVYRNGSLVGS-------PSSASYIDGGLTASTTYRYRVR 268
Cdd:COG3401 323 DLTPPAAPSGLTATAVGSSSITLSWTASSDA----DVTGYNVYRSTSGGGTytkiaetVTTTSYTDTGLTPGTTYYYKVT 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565447 269 ARDNAGNASAQGTEISATTLAGDGGTTGKRVI---GYFTQWGIYGRNYRVKNIDSSGSAARLTHINYAFGNVRNNRCEVG 345
Cdd:COG3401 399 AVDAAGNESAPSEEVSATTASAASGESLTASVdavPLTDVAGATAAASAASNPGVSAAVLADGGDTGNAVPFTTTSSTVT 478
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 896565447 346 IT--------QPSDPNSGAGGDAFADYTKAFSAAESVSGSADTWDQPLRGNWNQLKQLKAKYPGMKVLISLGGWTWS 414
Cdd:COG3401 479 ATttdtttanLSVTTGSLVGGSGASSVTNSVSVIGASAAAAVGGAPDGTPNVTGASPVTVGASTGDVLITDLVSLTT 555
|
|
| Chi1 |
COG3469 |
Chitinase [Carbohydrate transport and metabolism]; |
75-507 |
1.59e-12 |
|
Chitinase [Carbohydrate transport and metabolism];
Pssm-ID: 442692 [Multi-domain] Cd Length: 534 Bit Score: 70.55 E-value: 1.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565447 75 WNAPPDHPAGAPYYTNLGACDGSGSNQPPVVSLTSPANGATFSAGSTVNVTANASDPDGSVAKVEFFRDGSTLGVATSAP 154
Cdd:COG3469 2 SSVSTAASPTAGGASATAVTLLGAAATAASVTLTAATATTVVSTTGSVVVAASGSAGSGTGTTAASSTAATSSTTSTTAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565447 155 YAASWANASAGSHTLRAVATDNNNAttstatititvNAAGGDTTAPSVPGGLAVGTRTANSIALSWSPSTDNTGGSGVAG 234
Cdd:COG3469 82 ATAAAAAATSTSATLVATSTASGAN-----------TGTSTVTTTSTGAGSVTSTTSSTAGSTTTSGASATSSAGSTTTT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565447 235 YDVYRNGSLVGSPSSASYIDGGLTASTTYRYRVRARD-NAGNASAQGTEISATTL-AGDGGTTGKRVIGYFTQWGIYGRN 312
Cdd:COG3469 151 TTVSGTETATGGTTTTSTTTTTTSASTTPSATTTATAtTASGATTPSATTTATTTgPPTPGLPKHVLVGYWHNFDNGSGY 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565447 313 YRVKNIDSSGSAarlthINYAFG-NVRNNRCEVGITQpsDPNSGAGGDAFADYTKAfsaaesvsgsadtwdqplrgnwnQ 391
Cdd:COG3469 231 IRLSDVPDKYDV-----INVAFAePTGATNGTVTFTL--DPGSSSPGGYTDAQFKA-----------------------D 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565447 392 LKQLKAKypGMKVLISLGGWTWSRGFSSAArpeNRQAFVASC---IDAYikgnlpvtdgaggagaalgVFDGIDVDWEYp 468
Cdd:COG3469 281 IAALQAQ--GKKVLLSIGGANGTVQLNTAA---AADNFVNSVialIDEY-------------------GFDGLDIDLEG- 335
|
410 420 430
....*....|....*....|....*....|....*....
gi 896565447 469 vACGIECGKPEDNANFTALMAEFRRQLDAVRPGLLLTVA 507
Cdd:COG3469 336 -GSNSLNAGDTDTPVITNLISALKQLKAKYGPGFVLTMA 373
|
|
| GH18_3CO4_chitinase |
cd06545 |
The Bacteroides thetaiotaomicron protein represented by pdb structure 3CO4 is an ... |
299-597 |
2.08e-12 |
|
The Bacteroides thetaiotaomicron protein represented by pdb structure 3CO4 is an uncharacterized bacterial member of the family 18 glycosyl hydrolases with homologs found in Flavobacterium, Stigmatella, and Pseudomonas.
Pssm-ID: 119362 [Multi-domain] Cd Length: 253 Bit Score: 67.86 E-value: 2.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565447 299 VIGYFTQWgiYGRNYRVKNIDSSgsaaRLTHINYAFGNVRNNrcevgitqpsdpnsgaggdafadytKAFSAAESVSGSA 378
Cdd:cd06545 1 VVGYLPNY--DDLNALSPTIDFS----KLTHINLAFANPDAN-------------------------GTLNANPVRSELN 49
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565447 379 DtwdqplrgnwnqlKQLKAKYPGMKVLISLGGWTWSRGFSSAARPENRQAFVASCIDAYIKGNLpvtdgaggagaalgvf 458
Cdd:cd06545 50 S-------------VVNAAHAHNVKILISLAGGSPPEFTAALNDPAKRKALVDKIINYVVSYNL---------------- 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565447 459 DGIDVDWEYPVACGIecgkpednaNFTALMAEFRRQLDAvrPGLLLTVAVGAGIdkiRVTDPAAYHPYLDYINVMTYDFH 538
Cdd:cd06545 101 DGIDVDLEGPDVTFG---------DYLVFIRALYAALKK--EGKLLTAAVSSWN---GGAVSDSTLAYFDFINIMSYDAT 166
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565447 539 GAWDAktnhqsalfDSPNDPSTGDQklynSNDAIEAFISRGV-PAAKLNLGIGYYGRGWT 597
Cdd:cd06545 167 GPWWG---------DNPGQHSSYDD----AVNDLNYWNERGLaSKDKLVLGLPFYGYGFY 213
|
|
| COG3979 |
COG3979 |
Chitodextrinase [Carbohydrate transport and metabolism]; |
198-384 |
2.21e-11 |
|
Chitodextrinase [Carbohydrate transport and metabolism];
Pssm-ID: 443178 [Multi-domain] Cd Length: 369 Bit Score: 65.95 E-value: 2.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565447 198 TAPSVPGGLAVGTRTANSIALSWSPSTDNTggsGVAGYDVYRNGSLVGSPSS-ASYIDGGLTASTTYRYRVRARDNAGNA 276
Cdd:COG3979 1 QAPTAPTGLTASNVTSSSVSLSWDASTDNV---GVTGYDVYRGGDQVATVTGlTAWTVTGLTPGTEYTFTVGACDAAGNV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565447 277 SAQ-----GTEISATTLAGDGGTTGKRVIGYFTQWGIYGRNYRVKNIDSSGSAARLTHINYAFGNVRNNRCEVGITQPSD 351
Cdd:COG3979 78 SAAsgtstAMFGGSSTTLGSAEGVADTSGNLAASGAFFGVTTPPTPSSTLVVDGTTTVNAAATANGGTGGSGGTTTIITT 157
|
170 180 190
....*....|....*....|....*....|...
gi 896565447 352 PNSGAGGDAFADYTKAFSAAESVSGSADTWDQP 384
Cdd:COG3979 158 GVEGGGGSKTAQSLNAITAAGTAALNGGVVGGA 190
|
|
| FN3 |
smart00060 |
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ... |
200-274 |
1.43e-10 |
|
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.
Pssm-ID: 214495 [Multi-domain] Cd Length: 83 Bit Score: 58.01 E-value: 1.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565447 200 PSVPGGLAVGTRTANSIALSWSPSTDNTGGSGVAGYDVYRNGS------LVGSPSSASYIDGGLTASTTYRYRVRARDNA 273
Cdd:smart00060 1 PSPPSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEgsewkeVNVTPSSTSYTLTGLKPGTEYEFRVRAVNGA 80
|
.
gi 896565447 274 G 274
Cdd:smart00060 81 G 81
|
|
| FN3 |
cd00063 |
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ... |
200-287 |
3.50e-10 |
|
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.
Pssm-ID: 238020 [Multi-domain] Cd Length: 93 Bit Score: 57.12 E-value: 3.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565447 200 PSVPGGLAVGTRTANSIALSWSPSTDNtgGSGVAGYDVYRNGSL--------VGSPSSASYIDGGLTASTTYRYRVRARd 271
Cdd:cd00063 1 PSPPTNLRVTDVTSTSVTLSWTPPEDD--GGPITGYVVEYREKGsgdwkeveVTPGSETSYTLTGLKPGTEYEFRVRAV- 77
|
90
....*....|....*.
gi 896565447 272 NAGNASAQGTEISATT 287
Cdd:cd00063 78 NGGGESPPSESVTVTT 93
|
|
| GH18_CFLE_spore_hydrolase |
cd02874 |
Cortical fragment-lytic enzyme (CFLE) is a peptidoglycan hydrolase involved in bacterial ... |
458-679 |
1.47e-09 |
|
Cortical fragment-lytic enzyme (CFLE) is a peptidoglycan hydrolase involved in bacterial endospore germination. CFLE is expressed as an inactive preprotein (called SleB) in the forespore compartment of sporulating cells. SleB translocates across the forespore inner membrane and is deposited as a mature enzyme in the cortex layer of the spore. As part of a sensory mechanism capable of initiating germination, CFLE degrades a spore-specific peptidoglycan constituent called muramic-acid delta-lactam that comprises the outer cortex. CFLE has a C-terminal glycosyl hydrolase family 18 (GH18) catalytic domain as well as two N-terminal LysM peptidoglycan-binding domains. In addition to SleB, this family includes YaaH, YdhD, and YvbX from Bacillus subtilis.
Pssm-ID: 119353 [Multi-domain] Cd Length: 313 Bit Score: 59.97 E-value: 1.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565447 458 FDGIDVDWEYpVAcgiecgkPEDNANFTALMAEFRRQLDAvrPGLLLTVAVGA---GIDKIRVTDP---AAYHPYLDYIN 531
Cdd:cd02874 104 YDGVNIDFEN-VP-------PEDREAYTQFLRELSDRLHP--AGYTLSTAVVPktsADQFGNWSGAydyAAIGKIVDFVV 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565447 532 VMTYDFHGAWdakTNHQSAlfdSPNDPstgdqklynSNDAIEAFISRgVPAAKLNLGIGYYGRGWTgvananNGLYQTAT 611
Cdd:cd02874 174 LMTYDWHWRG---GPPGPV---APIGW---------VERVLQYAVTQ-IPREKILLGIPLYGYDWT------LPYKKGGK 231
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 896565447 612 GAAPGTYEAgiEDWKVLKNlAWPSYTDNTAGATWIY---NGST--LWsFDTPANITRKMGYVKTQGLGGAFVW 679
Cdd:cd02874 232 ASTISPQQA--INLAKRYG-AEIQYDEEAQSPFFRYvdeQGRRheVW-FEDARSLQAKFELAKEYGLRGVSYW 300
|
|
| COG4733 |
COG4733 |
Phage-related protein, tail protein J [Mobilome: prophages, transposons]; |
101-291 |
2.65e-08 |
|
Phage-related protein, tail protein J [Mobilome: prophages, transposons];
Pssm-ID: 443767 [Multi-domain] Cd Length: 978 Bit Score: 57.26 E-value: 2.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565447 101 QPPVVSLTSpANGATFSAGSTVNVTANAS---DPDGSVAKVEFFRDGSTL-GVATSAPYAASWANASAGSHTLRAVATDN 176
Cdd:COG4733 530 QWPPVNVTT-SESLSVVAQGTAVTTLTVSwdaPAGAVAYEVEWRRDDGNWvSVPRTSGTSFEVPGIYAGDYEVRVRAINA 608
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565447 177 NNATTSTATITITVnaAGGDTTAPSVPGGLAVgTRTANSIALSWSPSTDntggSGVAGYDVYR-------NGSLVGSP-S 248
Cdd:COG4733 609 LGVSSAWAASSETT--VTGKTAPPPAPTGLTA-TGGLGGITLSWSFPVD----ADTLRTEIRYsttgdwaSATVAQALyP 681
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 896565447 249 SASYIDGGLTASTTYRYRVRARDNAGNASAQGTEISATTLAGD 291
Cdd:COG4733 682 GNTYTLAGLKAGQTYYYRARAVDRSGNVSAWWVSGQASADAAG 724
|
|
| GH18_chitobiase |
cd02875 |
Chitobiase (also known as di-N-acetylchitobiase) is a lysosomal glycosidase that hydrolyzes ... |
459-698 |
4.54e-07 |
|
Chitobiase (also known as di-N-acetylchitobiase) is a lysosomal glycosidase that hydrolyzes the reducing-end N-acetylglucosamine from the chitobiose core of oligosaccharides during the ordered degradation of asparagine-linked glycoproteins in eukaryotes. Chitobiase can only do so if the asparagine that joins the oligosaccharide to protein is previously removed by a glycosylasparaginase. Chitobiase is therefore the final step in the lysosomal degradation of the protein/carbohydrate linkage component of asparagine-linked glycoproteins. The catalytic domain of chitobiase is an eight-stranded alpha/beta barrel fold similar to that of other family 18 glycosyl hydrolases such as hevamine and chitotriosidase.
Pssm-ID: 119354 [Multi-domain] Cd Length: 358 Bit Score: 52.43 E-value: 4.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565447 459 DGIDVDWEYPvacgIECGKPEDNAnFTALMAEFRRQLDAVRPGLLLTVAVG---AGIDKiRVTDPAAYHPYLDYINVMTY 535
Cdd:cd02875 114 DGINIDIEQP----ITKGSPEYYA-LTELVKETTKAFKKENPGYQISFDVAwspSCIDK-RCYDYTGIADASDFLVVMDY 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565447 536 DFHGawDAKTNHQSALFDSPNDpstgdqklyNSNDAIEAFISRGVPAAKLNLGIGYYGRGWTGVananNGLYQTATG--- 612
Cdd:cd02875 188 DEQS--QIWGKECIAGANSPYS---------QTLSGYNNFTKLGIDPKKLVMGLPWYGYDYPCL----NGNLEDVVCtip 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565447 613 -----AAPGTYEAGIE-DW-KVLKNLawpsyTDNTAGATW-------IYNGS-------TLWsFDTPANITRKMGYVKTQ 671
Cdd:cd02875 253 kvpfrGANCSDAAGRQiPYsEIMKQI-----NSSIGGRLWdseqkspFYNYKdkqgnlhQVW-YDNPQSLSIKVAYAKNL 326
|
250 260 270
....*....|....*....|....*....|..
gi 896565447 672 GLGGAFVW-----EFSGDDAQGTLTKAVSDGL 698
Cdd:cd02875 327 GLKGIGMWngdllDYSGLPIAEKQTEDMWNAL 358
|
|
| ChiA1_BD |
cd12214 |
chitin-binding domain of Chi A1-like proteins; This group contains proteins related to the ... |
49-88 |
1.13e-06 |
|
chitin-binding domain of Chi A1-like proteins; This group contains proteins related to the chitin binding domain of chitinase A1 (ChiA1) of Bacillus circulans WL-12. Glycosidase ChiA1 hydrolyzes chitin and is comprised of several domains: the C-terminal chitin binding domain, an N-terminal and catalytic domain, and 2 fibronectin type III-like domains. Chitinases function in invertebrates in the degradation of old exoskeletons, in fungi to utilize chitin in cell walls, and in bacteria which use chitin as an energy source. Bacillus circulans WL-12 ChiA1 facilitates invasion of fungal cell walls. The ChiAi chitin binding domain is required for the specific recognition of insoluble chitin. although topologically and structurally related, ChiA1 lacks the characteristic aromatic residues of Erwinia chrysanthemi endoglucanase Z (CBD(EGZ)).
Pssm-ID: 213177 [Multi-domain] Cd Length: 45 Bit Score: 45.79 E-value: 1.13e-06
10 20 30 40
....*....|....*....|....*....|....*....|
gi 896565447 49 WDQAKIYRAGDTLQKGGVLYRANQDIWNAPPDHPAGAPYY 88
Cdd:cd12214 2 WAAGTTYKAGDIVTYNGKLYRCLQAHTSLAGWEPPAVPAL 41
|
|
| fn3 |
pfam00041 |
Fibronectin type III domain; |
201-275 |
2.40e-06 |
|
Fibronectin type III domain;
Pssm-ID: 394996 [Multi-domain] Cd Length: 85 Bit Score: 45.87 E-value: 2.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565447 201 SVPGGLAVGTRTANSIALSWSPSTDntGGSGVAGYDV-YRNGSLVG-------SPSSASYIDGGLTASTTYRYRVRARDN 272
Cdd:pfam00041 1 SAPSNLTVTDVTSTSLTVSWTPPPD--GNGPITGYEVeYRPKNSGEpwneitvPGTTTSVTLTGLKPGTEYEVRVQAVNG 78
|
...
gi 896565447 273 AGN 275
Cdd:pfam00041 79 GGE 81
|
|
| Chi1 |
COG3469 |
Chitinase [Carbohydrate transport and metabolism]; |
40-209 |
8.49e-05 |
|
Chitinase [Carbohydrate transport and metabolism];
Pssm-ID: 442692 [Multi-domain] Cd Length: 534 Bit Score: 45.90 E-value: 8.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565447 40 AASCAGVAQWDQAKIYRAGDTLQKGGVLYRANQDIWNAPPDHPAGAPYYTNLGACDGSGSNQPPVVSLTSPANGATFSAG 119
Cdd:COG3469 58 GSGTGTTAASSTAATSSTTSTTATATAAAAAATSTSATLVATSTASGANTGTSTVTTTSTGAGSVTSTTSSTAGSTTTSG 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 896565447 120 STVNVTANASDPDGSVAKVEFFRDGSTLGVATSAPYAASWANASAGSHTlravatdnNNATTSTATITITVNAAGGDTTA 199
Cdd:COG3469 138 ASATSSAGSTTTTTTVSGTETATGGTTTTSTTTTTTSASTTPSATTTAT--------ATTASGATTPSATTTATTTGPPT 209
|
170
....*....|
gi 896565447 200 PSVPGGLAVG 209
Cdd:COG3469 210 PGLPKHVLVG 219
|
|
| |
