|
Name |
Accession |
Description |
Interval |
E-value |
| ChiA |
COG3325 |
Chitinase, GH18 family [Carbohydrate transport and metabolism]; |
26-413 |
1.53e-120 |
|
Chitinase, GH18 family [Carbohydrate transport and metabolism];
Pssm-ID: 442554 [Multi-domain] Cd Length: 391 Bit Score: 355.76 E-value: 1.53e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520332475 26 VGYFNGGGdvTAGPGGDIDKLDVRQITHLNYSFGLIYNDEK-DETNAALKDPAHLHEIWLSPKVQADLQKLPALRKQNPD 104
Cdd:COG3325 22 VGYFTQWG--IYGRNYLVKDIPASKLTHINYAFANVDPDGKcSVGDAWAKPSVDGAADDWDQPLKGNFNQLKKLKAKNPN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520332475 105 LKVLLSVGGWG-ARGFSGAAASKETRKVFIQSAQEIVEKYGLDGIDLDWEFPVNGAWGLVASQPADRDNFTALLKELRAA 183
Cdd:COG3325 100 LKVLISIGGWTwSKGFSDAAATPASRAAFVDSCVDLLRKYNFDGIDIDWEYPGSGGAPGNVYRPEDKANFTALLKELRAQ 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520332475 184 F-------GTRKLVTIAVGANAESPKSWvDVKAIAPSLDYINLMTYDMAYGTQY---FNSNLYDSSHWPTvaaADKYSAD 253
Cdd:COG3325 180 LdalgaetGKHYLLTAAAPAGPDKLDGI-ELPKVAQYLDYVNVMTYDFHGAWSPttgHQAPLYDSPKDPE---AQGYSVD 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520332475 254 FVVNNYLAAGLKPSQMNLGIGFYGRVpkravepgidWTTADAQNNPVTQPYFGPQEVALFASlgydlskdtYVKYNDIVG 333
Cdd:COG3325 256 SAVQAYLAAGVPASKLVLGVPFYGRG----------WTGVTGGNNGLYQPATGPAPGTWEAG---------VNDYKDLKA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520332475 334 KLLNDPQkrFTEHWDDEAKVPWLSvqsaEGKPLFALSYENPRSVAIKADYIKAKGLAGAMFWEYGADDQN-QLARQLAES 412
Cdd:COG3325 317 LYLGSNG--YTRYWDDVAKAPYLY----NGDTGTFISYDDPRSIAAKADYVKDKGLGGVMFWELSGDTADgTLLNAIGEG 390
|
.
gi 2520332475 413 L 413
Cdd:COG3325 391 L 391
|
|
| GH18_chitinase |
cd06548 |
The GH18 (glycosyl hydrolases, family 18) type II chitinases hydrolyze chitin, an abundant ... |
25-400 |
1.69e-101 |
|
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: 304.55 E-value: 1.69e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520332475 25 SVGYFNGGGDVTAGPGGDiDKLDVRQITHLNYSFGLIYNDEKDETNAALKDPAHLH-----EIWLSPKVQADLQKLPALR 99
Cdd:cd06548 1 VVGYFTNWGIYGRNYFVT-DDIPADKLTHINYAFADIDGDGGVVTSDDEAADEAAQsvdggADTDDQPLKGNFGQLRKLK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520332475 100 KQNPDLKVLLSVGGWGAR-GFSGAAASKETRKVFIQSAQEIVEKYGLDGIDLDWEFPVNGAWGLVASQPADRDNFTALLK 178
Cdd:cd06548 80 QKNPHLKILLSIGGWTWSgGFSDAAATEASRAKFADSAVDFIRKYGFDGIDIDWEYPGSGGAPGNVARPEDKENFTLLLK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520332475 179 ELRAAF-------GTRKLVTIAVGANAESPKSwVDVKAIAPSLDYINLMTYDMAYG---TQYFNSNLYDSSHWPTvaaaD 248
Cdd:cd06548 160 ELREALdalgaetGRKYLLTIAAPAGPDKLDK-LEVAEIAKYLDFINLMTYDFHGAwsnTTGHHSNLYASPADPP----G 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520332475 249 KYSADFVVNNYLAAGLKPSQMNLGIGFYGRVpkravepgidWTTadaqnnpvtqpyfgpqevalfaslgydlskdtyvky 328
Cdd:cd06548 235 GYSVDAAVNYYLSAGVPPEKLVLGVPFYGRG----------WTG------------------------------------ 268
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2520332475 329 ndivgkllndpqkrFTEHWDDEAKVPWLsVQSAEGkplFALSYENPRSVAIKADYIKAKGLAGAMFWEYGAD 400
Cdd:cd06548 269 --------------YTRYWDEVAKAPYL-YNPSTK---TFISYDDPRSIKAKADYVKDKGLGGVMFWELSGD 322
|
|
| Glyco_18 |
smart00636 |
Glyco_18 domain; |
26-400 |
2.27e-85 |
|
Glyco_18 domain;
Pssm-ID: 214753 [Multi-domain] Cd Length: 334 Bit Score: 263.77 E-value: 2.27e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520332475 26 VGYFNGGGdvTAGPGGDIDKLDVRQITHLNYSFGLIYNDEKDEtnaaLKDPahlheiwlspkvQADLQK---LPALRKQN 102
Cdd:smart00636 3 VGYFTNWG--VYGRNFPVDDIPASKLTHIIYAFANIDPDGTVT----IGDE------------WADIGNfgqLKALKKKN 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520332475 103 PDLKVLLSVGGWGA-RGFSGAAASKETRKVFIQSAQEIVEKYGLDGIDLDWEFPVNGawglvasqPADRDNFTALLKELR 181
Cdd:smart00636 65 PGLKVLLSIGGWTEsDNFSSMLSDPASRKKFIDSIVSFLKKYGFDGIDIDWEYPGGR--------GDDRENYTALLKELR 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520332475 182 AAF------GTRKLVTIAVGANAES-PKSWVDVKAIAPSLDYINLMTYDMAYGTQYF---NSNLYDSSHWPTvaaadKYS 251
Cdd:smart00636 137 EALdkegaeGKGYLLTIAVPAGPDKiDKGYGDLPAIAKYLDFINLMTYDFHGAWSNPtghNAPLYAGPGDPE-----KYN 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520332475 252 ADFVVNNYLAAGLKPSQMNLGIGFYGRvpkravepgiDWTTADAQNNPVTQPYFGPqevalfASLGYDLSKDTYVKYNDI 331
Cdd:smart00636 212 VDYAVKYYLCKGVPPSKLVLGIPFYGR----------GWTLVDGSNNGPGAPFTGP------ATGGPGTWEGGVVDYREI 275
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2520332475 332 VGKLLndpqkrFTEHWDDEAKVPWLsvqSAEGKPLFaLSYENPRSVAIKADYIKAKGLAGAMFWEYGAD 400
Cdd:smart00636 276 CKLLG------ATVVYDDTAKAPYA---YNPGTGQW-VSYDDPRSIKAKADYVKDKGLGGVMIWELDAD 334
|
|
| GH18_chitolectin_chitotriosidase |
cd02872 |
This conserved domain family includes a large number of catalytically inactive chitinase-like ... |
52-401 |
1.04e-75 |
|
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: 239.77 E-value: 1.04e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520332475 52 THLNYSFGLIYNDekdetnaalkdpahLHEIWLSPKVQADL---QKLPALRKQNPDLKVLLSVGGW--GARGFSGAAASK 126
Cdd:cd02872 29 THIIYAFAGLNPD--------------GNIIILDEWNDIDLglyERFNALKEKNPNLKTLLAIGGWnfGSAKFSAMAASP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520332475 127 ETRKVFIQSAQEIVEKYGLDGIDLDWEFPvnGAWGlvaSQPADRDNFTALLKELRAAF---GTRKLVTIAVGANAESPKS 203
Cdd:cd02872 95 ENRKTFIKSAIAFLRKYGFDGLDLDWEYP--GQRG---GPPEDKENFVTLLKELREAFepeAPRLLLTAAVSAGKETIDA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520332475 204 WVDVKAIAPSLDYINLMTYD--MAYGTQY-FNSNLYDSSHwpTVAAADKYSADFVVNNYLAAGLKPSQMNLGIGFYGRvp 280
Cdd:cd02872 170 AYDIPEISKYLDFINVMTYDfhGSWEGVTgHNSPLYAGSA--DTGDQKYLNVDYAIKYWLSKGAPPEKLVLGIPTYGR-- 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520332475 281 kravepgiDWTTADAQNNPVTQPYFGPqevalfASLGydlskdTYVK------YNDIVGKLLNDpqkrFTEHWDDEAKVP 354
Cdd:cd02872 246 --------SFTLASPSNTGVGAPASGP------GTAG------PYTReagflaYYEICEFLKSG----WTVVWDDEQKVP 301
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 2520332475 355 -------WlsvqsaegkplfaLSYENPRSVAIKADYIKAKGLAGAMFWEYGADD 401
Cdd:cd02872 302 yaykgnqW-------------VGYDDEESIALKVQYLKSKGLGGAMVWSIDLDD 342
|
|
| Glyco_hydro_18 |
pfam00704 |
Glycosyl hydrolases family 18; |
26-400 |
8.58e-73 |
|
Glycosyl hydrolases family 18;
Pssm-ID: 425828 [Multi-domain] Cd Length: 311 Bit Score: 230.42 E-value: 8.58e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520332475 26 VGYFNGGGDVTAGPGGDIDKLdvrqiTHLNYSFGLIYNDEkdetnaalkdpahlHEIWLSPKVQADLQKLPALRKQ-NPD 104
Cdd:pfam00704 3 VGYYTSWGVYRNGNFLPSDKL-----THIIYAFANIDGSD--------------GTLFIGDWDLGNFEQLKKLKKQkNPG 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520332475 105 LKVLLSVGGWGA-RGFSGAAASKETRKVFIQSAQEIVEKYGLDGIDLDWEFPVngawglvaSQPADRDNFTALLKELRAA 183
Cdd:pfam00704 64 VKVLLSIGGWTDsTGFSLMASNPASRKKFADSIVSFLRKYGFDGIDIDWEYPG--------GNPEDKENYDLLLRELRAA 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520332475 184 F-----GTRKLVTIAVGANAESPKSWVDVKAIAPSLDYINLMTYDmaygtqYFNSNLYDSSHWPTVAAADKYSADFVVNN 258
Cdd:pfam00704 136 LdeakgGKKYLLSAAVPASYPDLDKGYDLPKIAKYLDFINVMTYD------FHGSWDNVTGHHAPLYGGGSYNVDYAVKY 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520332475 259 YLAAGLKPSQMNLGIGFYGRvpkravepgiDWTTADAQNNPvtqpyfgpqevalfaslgydlSKDTYVKYNDIVGKLLND 338
Cdd:pfam00704 210 YLKQGVPASKLVLGVPFYGR----------SWTLVNGSGNT---------------------WEDGVLAYKEICNLLKDN 258
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2520332475 339 PqkrFTEHWDDEAKVPWLsvqsaeGKPLFALSYENPRSVAIKADYIKAKGLAGAMFWEYGAD 400
Cdd:pfam00704 259 G---ATVVWDDVAKAPYV------YDGDQFITYDDPRSIATKVDYVKAKGLGGVMIWSLDAD 311
|
|
| GH18_chitinase-like |
cd00598 |
The GH18 (glycosyl hydrolase, family 18) type II chitinases hydrolyze chitin, an abundant ... |
26-224 |
4.99e-41 |
|
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: 144.44 E-value: 4.99e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520332475 26 VGYFNGGGDvtaGPGGDIDKLDVRQITHLNYSFGLIYNDEKDETnaalkdpahlheiWLSPKVQADLQKLPALRKQNPDL 105
Cdd:cd00598 2 ICYYDGWSS---GRGPDPTDIPLSLCTHIIYAFAEISSDGSLNL-------------FGDKSEEPLKGALEELASKKPGL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520332475 106 KVLLSVGGWGARGFSGAAASKETRKVFIQSAQEIVEKYGLDGIDLDWEFPvngawglVASQPADRDNFTALLKELRAAFG 185
Cdd:cd00598 66 KVLISIGGWTDSSPFTLASDPASRAAFANSLVSFLKTYGFDGVDIDWEYP-------GAADNSDRENFITLLRELRSALG 138
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2520332475 186 -TRKLVTIAVGANAESPKSWVDVKAIAPSLDYINLMTYDM 224
Cdd:cd00598 139 aANYLLTIAVPASYFDLGYAYDVPAIGDYVDFVNVMTYDL 178
|
|
| GH18_IDGF |
cd02873 |
The IDGF's (imaginal disc growth factors) are a family of growth factors identified in insects ... |
97-401 |
1.83e-36 |
|
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: 137.83 E-value: 1.83e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520332475 97 ALRKQNPDLKVLLSVGGWGARGFSGAA-------ASKETRKVFIQSAQEIVEKYGLDGIDLDWEFP------VNGAWGLV 163
Cdd:cd02873 67 SLKRKYPHLKVLLSVGGDRDTDEEGENekyllllESSESRNAFINSAHSLLKTYGFDGLDLAWQFPknkpkkVRGTFGSA 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520332475 164 ---------ASQPAD------RDNFTALLKELRAAFGTR-KLVTIAVGANAESpkSW-VDVKAIAPSLDYINLMTYDmaY 226
Cdd:cd02873 147 whsfkklftGDSVVDekaaehKEQFTALVRELKNALRPDgLLLTLTVLPHVNS--TWyFDVPAIANNVDFVNLATFD--F 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520332475 227 GTQYFNSNLYDSSHwPTVAAADK---YSADFVVNNYLAAGLKPSQMNLGIGFYGRVPKRAVEPGIdwttadaQNNPVTQP 303
Cdd:cd02873 223 LTPERNPEEADYTA-PIYELYERnphHNVDYQVKYWLNQGTPASKLNLGIATYGRAWKLTKDSGI-------TGVPPVLE 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520332475 304 YFGPQEVALFASLGYDLSkdtyvkYNDIVGKLLN---------------DPQKRFTEHwddeakvpwlSVQSAE--GKPL 366
Cdd:cd02873 295 TDGPGPAGPQTKTPGLLS------WPEICSKLPNpanlkgadaplrkvgDPTKRFGSY----------AYRPADenGEHG 358
|
330 340 350
....*....|....*....|....*....|....*
gi 2520332475 367 FALSYENPRSVAIKADYIKAKGLAGAMFWEYGADD 401
Cdd:cd02873 359 IWVSYEDPDTAANKAGYAKAKGLGGVALFDLSLDD 393
|
|
| GH18_plant_chitinase_class_V |
cd02879 |
The class V plant chitinases have a glycosyl hydrolase family 18 (GH18) domain, but lack the ... |
45-405 |
1.70e-32 |
|
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: 124.40 E-value: 1.70e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520332475 45 KLDVRQITHLNYSFGLIyndekdetnaalkDPAHlHEIWLSPKVQADLQKL-PALRKQNPDLKVLLSVGGWGARG--FSG 121
Cdd:cd02879 20 NIDSSLFTHLFYAFADL-------------DPST-YEVVISPSDESEFSTFtETVKRKNPSVKTLLSIGGGGSDSsaFAA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520332475 122 AAASKETRKVFIQSAQEIVEKYGLDGIDLDWEFPVNgawglvasqPADRDNFTALLKELRAAF-------GTRKLV-TIA 193
Cdd:cd02879 86 MASDPTARKAFINSSIKVARKYGFDGLDLDWEFPSS---------QVEMENFGKLLEEWRAAVkdearssGRPPLLlTAA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520332475 194 V---------GANAESPkswvdVKAIAPSLDYINLMTYDmAYGTQYFNSN-----LYDSshwptvaaADKYSADFVVNNY 259
Cdd:cd02879 157 VyfspilflsDDSVSYP-----IEAINKNLDWVNVMAYD-YYGSWESNTTgpaaaLYDP--------NSNVSTDYGIKSW 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520332475 260 LAAGLKPSQMNLGIGFYGRVpkravepgidWTtadaqnnpvtqpyfgpqevalfaslgydLSKDTYVKYNDIVGkllndp 339
Cdd:cd02879 223 IKAGVPAKKLVLGLPLYGRA----------WT----------------------------LYDTTTVSSYVYAG------ 258
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2520332475 340 qkrftehwddeakvpwlsvqsaegkpLFALSYENPRSVAIKADYIKAKGLAGAMFWEYGADDQNQL 405
Cdd:cd02879 259 --------------------------TTWIGYDDVQSIAVKVKYAKQKGLLGYFAWAVGYDDNNWL 298
|
|
| GH18_CFLE_spore_hydrolase |
cd02874 |
Cortical fragment-lytic enzyme (CFLE) is a peptidoglycan hydrolase involved in bacterial ... |
106-403 |
7.12e-22 |
|
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: 95.41 E-value: 7.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520332475 106 KVLLSVGGWGARGFSGAAASK-----ETRKVFIQSAQEIVEKYGLDGIDLDWEFpVNgawglvasqPADRDNFTALLKEL 180
Cdd:cd02874 60 KPLLVITNLTNGNFDSELAHAvlsnpEARQRLINNILALAKKYGYDGVNIDFEN-VP---------PEDREAYTQFLREL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520332475 181 RAAFGTRKL-VTIAVGAN--AESPKSWV---DVKAIAPSLDYINLMTYDMAYGTqyfnsnlydSSHWPtVAaadkySADF 254
Cdd:cd02874 130 SDRLHPAGYtLSTAVVPKtsADQFGNWSgayDYAAIGKIVDFVVLMTYDWHWRG---------GPPGP-VA-----PIGW 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520332475 255 V--VNNYLAAGLKPSQMNLGIGFYGRvpkravepgiDWTTADAQNNPVTqpYFGPQEValfaslgYDLSKdtyvKYNDIV 332
Cdd:cd02874 195 VerVLQYAVTQIPREKILLGIPLYGY----------DWTLPYKKGGKAS--TISPQQA-------INLAK----RYGAEI 251
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2520332475 333 GkllndpqkrftehWDDEAKVPWLSVQSAEGKpLFALSYENPRSVAIKADYIKAKGLAGAMFWEYGADDQN 403
Cdd:cd02874 252 Q-------------YDEEAQSPFFRYVDEQGR-RHEVWFEDARSLQAKFELAKEYGLRGVSYWRLGLEDPQ 308
|
|
| GH18_zymocin_alpha |
cd02878 |
Zymocin, alpha subunit. Zymocin is a heterotrimeric enzyme that inhibits yeast cell cycle ... |
24-223 |
3.05e-16 |
|
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: 79.28 E-value: 3.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520332475 24 MSVGYFNGGGDVTAGPGGDIDKLDVRQITHLNYSFGLIYNDekdetnaalkdpahlHEIWLSpKVQADLQKLPALRKqnp 103
Cdd:cd02878 1 KNIAYFEAYNLDRPCLNMDVTQIDTSKYTHIHFAFANITSD---------------FSVDVS-SVQEQFSDFKKLKG--- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520332475 104 dLKVLLSVGGWGargFSGAAAS---------KETRKVFIQSAQEIVEKYGLDGIDLDWEFPvnGAW---GLVASQPADRD 171
Cdd:cd02878 62 -VKKILSFGGWD---FSTSPSTyqifrdavkPANRDTFANNVVNFVNKYNLDGVDFDWEYP--GAPdipGIPAGDPDDGK 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2520332475 172 NFTALLKELRAAFGTRKLVTIAVganaesPKS-W----VDVKAIAPSLDYINLMTYD 223
Cdd:cd02878 136 NYLEFLKLLKSKLPSGKSLSIAA------PASyWylkgFPIKDMAKYVDYIVYMTYD 186
|
|
| GH18_3CO4_chitinase |
cd06545 |
The Bacteroides thetaiotaomicron protein represented by pdb structure 3CO4 is an ... |
26-277 |
7.44e-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: 65.17 E-value: 7.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520332475 26 VGYFNGGGDVTAgpggDIDKLDVRQITHLNYSFG-------LIYNDEKDETNAALKDpAHLHEIwlspkvqadlqklpal 98
Cdd:cd06545 2 VGYLPNYDDLNA----LSPTIDFSKLTHINLAFAnpdangtLNANPVRSELNSVVNA-AHAHNV---------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520332475 99 rkqnpdlKVLLSVGGWGARGFSGAAASKETRKVFIQSAQEIVEKYGLDGIDLDWEFPVNGAwglvasqpADRDNFTAllk 178
Cdd:cd06545 61 -------KILISLAGGSPPEFTAALNDPAKRKALVDKIINYVVSYNLDGIDVDLEGPDVTF--------GDYLVFIR--- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520332475 179 ELRAAFGTR-KLVTIAVGAN--AESPKSWVdvkaiaPSLDYINLMTYDmAYGTqyfnsnlydsshWPTVAAADKYSADFV 255
Cdd:cd06545 123 ALYAALKKEgKLLTAAVSSWngGAVSDSTL------AYFDFINIMSYD-ATGP------------WWGDNPGQHSSYDDA 183
|
250 260
....*....|....*....|....*.
gi 2520332475 256 VNN---YLAAGLKP-SQMNLGIGFYG 277
Cdd:cd06545 184 VNDlnyWNERGLASkDKLVLGLPFYG 209
|
|
| GH18_chitobiase |
cd02875 |
Chitobiase (also known as di-N-acetylchitobiase) is a lysosomal glycosidase that hydrolyzes ... |
129-395 |
6.99e-11 |
|
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: 63.22 E-value: 6.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520332475 129 RKVFIQSAQEIVEKYGLDGIDLDWEFPVNgawglvaSQPADRDNFTALLKELRAAFGTRKL---VTIAVganAESP---- 201
Cdd:cd02875 97 RTQWIQQKVELAKSQFMDGINIDIEQPIT-------KGSPEYYALTELVKETTKAFKKENPgyqISFDV---AWSPscid 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520332475 202 KSWVDVKAIAPSLDYINLMTYDMayGTQYFNSnlydsshwPTVAAADK-YS-ADFVVNNYLAAGLKPSQMNLGIGFYGRV 279
Cdd:cd02875 167 KRCYDYTGIADASDFLVVMDYDE--QSQIWGK--------ECIAGANSpYSqTLSGYNNFTKLGIDPKKLVMGLPWYGYD 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520332475 280 PKRAvepGIDWTTADAQNNPVtqPYfgpqevalfasLGYDLSK--DTYVKYNDIVgKLLNDPQKrfTEHWDDEAKVPWLS 357
Cdd:cd02875 237 YPCL---NGNLEDVVCTIPKV--PF-----------RGANCSDaaGRQIPYSEIM-KQINSSIG--GRLWDSEQKSPFYN 297
|
250 260 270
....*....|....*....|....*....|....*...
gi 2520332475 358 VQSAEGKPlFALSYENPRSVAIKADYIKAKGLAGAMFW 395
Cdd:cd02875 298 YKDKQGNL-HQVWYDNPQSLSIKVAYAKNLGLKGIGMW 334
|
|
| GH18_EndoS-like |
cd06542 |
Endo-beta-N-acetylglucosaminidases are bacterial chitinases that hydrolyze the chitin core of ... |
93-336 |
1.24e-10 |
|
Endo-beta-N-acetylglucosaminidases are bacterial chitinases that hydrolyze the chitin core of various asparagine (N)-linked glycans and glycoproteins. The endo-beta-N-acetylglucosaminidases have a glycosyl hydrolase family 18 (GH18) catalytic domain. Some members also have an additional C-terminal glycosyl hydrolase family 20 (GH20) domain while others have an N-terminal domain of unknown function (pfam08522). Members of this family include endo-beta-N-acetylglucosaminidase S (EndoS) from Streptococcus pyogenes, EndoF1, EndoF2, EndoF3, and EndoH from Flavobacterium meningosepticum, and EndoE from Enterococcus faecalis. EndoS is a secreted endoglycosidase from Streptococcus pyogenes that specifically hydrolyzes the glycan on human IgG between two core N-acetylglucosamine residues. EndoE is a secreted endoglycosidase, encoded by the ndoE gene in Enterococcus faecalis, that hydrolyzes the glycan on human RNase B.
Pssm-ID: 119359 Cd Length: 255 Bit Score: 61.63 E-value: 1.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520332475 93 QKLPALRKQNpdLKVLLSVGGWGARGFSGAAASKETRKVFiqsAQEI---VEKYGLDGIDLDWEFpvNGAWGLVASQPAD 169
Cdd:cd06542 55 TYIRPLQAKG--TKVLLSILGNHLGAGFANNLSDAAAKAY---AKAIvdtVDKYGLDGVDFDDEY--SGYGKNGTSQPSN 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520332475 170 rDNFTALLKELRAAFG-TRKLVTIAVGANAespkSWVDVKAIAPSLDYInlmtydmAYGTqyfnsnlYDSSHWPTVAAAD 248
Cdd:cd06542 128 -EAFVRLIKELRKYMGpTDKLLTIDGYGQA----LSNDGEEVSPYVDYV-------IYQY-------YGSSSSSTQRNWN 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520332475 249 KYSadfvvnnylaAGLKPSQMNLGIGFYGrvpkraVEPGIDWTTAD--AQNNPVTQPYFGpqevalfaSLGYDLSKDTYV 326
Cdd:cd06542 189 TNS----------PKIPPEKMVYTESFEE------ENGGNSGSSAEqyARWTPAKGGKGG--------IGTYALDRDYYR 244
|
250
....*....|
gi 2520332475 327 KYNDIVGKLL 336
Cdd:cd06542 245 PYDSAVSKAL 254
|
|
| Chi1 |
COG3469 |
Chitinase [Carbohydrate transport and metabolism]; |
106-273 |
4.64e-09 |
|
Chitinase [Carbohydrate transport and metabolism];
Pssm-ID: 442692 [Multi-domain] Cd Length: 534 Bit Score: 58.23 E-value: 4.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520332475 106 KVLLSVGGwgARG---FSGAAAsketRKVFIQSAQEIVEKYGLDGIDLDWEfpvNGAWGLVAS--QPADRDNFTALLKEL 180
Cdd:COG3469 290 KVLLSIGG--ANGtvqLNTAAA----ADNFVNSVIALIDEYGFDGLDIDLE---GGSNSLNAGdtDTPVITNLISALKQL 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520332475 181 RAAFGTRKLVTIA-------VGANAESPkSWVD----VKAIAPSLDYINlmtydmaygTQYFNS---NLYDSShwptvaA 246
Cdd:COG3469 361 KAKYGPGFVLTMApetpyvqGGYVAYGG-IWGAylpvILALRDILTLLH---------VQYYNSgsmLGLDGQ------V 424
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2520332475 247 ADKYSADFVV--------------NNYLAAGLKPSQMNLGI 273
Cdd:COG3469 425 YSQGTVDFLVamadmllegfpvagNSNGFPGLRPDQVAIGL 465
|
|
| GH18_narbonin |
cd06544 |
Narbonin is a plant 2S protein from the globulin fraction of narbon bean (Vicia narbonensis L.) ... |
47-228 |
3.85e-08 |
|
Narbonin is a plant 2S protein from the globulin fraction of narbon bean (Vicia narbonensis L.) cotyledons with unknown function. Narbonin has a glycosyl hydrolase family 18 (GH18) domain without the conserved catalytic residues and with no known enzymatic activity. Narbonin amounts to up to 3% of the total seed globulins of mature seeds and was thought to be a storage protein but was found to degrade too slowly during germination. This family also includes the VfNOD32 nodulin from Vicia faba.
Pssm-ID: 119361 Cd Length: 253 Bit Score: 53.91 E-value: 3.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520332475 47 DVRQITHLNYSFGLIYNDEKDETNAalKDPAHLHEIWLSPKVQADlqKLPALRKQNPDLKVLLSVGGWGArGFSGAAASK 126
Cdd:cd06544 17 DVPINPKVEFHFILSFAIDYDTESN--PTNGKFNPYWDTENLTPE--AVKSIKAQHPNVKVVISIGGRGV-QNNPTPFDP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520332475 127 ETRKVFIQSA----QEIVEKYGLDGIDLDWE-FpvngawglvasqPADRDNFT----ALLKELRAAfGTRKLVTIAVGAN 197
Cdd:cd06544 92 SNVDSWVSNAvsslTSIIQTYNLDGIDIDYEhF------------PADPDTFVecigQLITELKNN-GVIKVASIAPSED 158
|
170 180 190
....*....|....*....|....*....|.
gi 2520332475 198 AESPKSWVDVKAIAPSLDYINLMTYdmAYGT 228
Cdd:cd06544 159 AEQSHYLALYNAYGDYIDYVNYQFY--NYGV 187
|
|
| GH18_trifunctional |
cd06549 |
GH18 domain of an uncharacterized family of bacterial proteins, which share a common ... |
129-292 |
1.90e-07 |
|
GH18 domain of an uncharacterized family of bacterial proteins, which share a common three-domain architecture: an N-terminal glycosyl hydrolase family 18 (GH18) domain, a glycosyl transferase family 2 domain, and a C-terminal polysaccharide deacetylase domain.
Pssm-ID: 119366 [Multi-domain] Cd Length: 298 Bit Score: 52.41 E-value: 1.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520332475 129 RKVFIQSAQEIVEKYGLDGIDLDWE-FPVNgawglvasqpaDRDNFTALLKELRAAFGT-RKLVTIAVGANAEspksWVD 206
Cdd:cd06549 89 RAKFIANIAAYLERNQADGIVLDFEeLPAD-----------DLPKYVAFLSELRRRLPAqGKQLTVTVPADEA----DWN 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520332475 207 VKAIAPSLDYINLMTYDmaygtqyfnsnlydsSHWPTVAAADKYSADFVVNNYLAA--GLKPSQMNLGIGFYgrvpkrav 284
Cdd:cd06549 154 LKALARNADKLILMAYD---------------EHYQGGAPGPIASQDWFESNLAQAvkKLPPEKLIVALGSY-------- 210
|
....*...
gi 2520332475 285 epGIDWTT 292
Cdd:cd06549 211 --GYDWTK 216
|
|
| GH18_chitinase_D-like |
cd02871 |
GH18 domain of Chitinase D (ChiD). ChiD, a chitinase found in Bacillus circulans, hydrolyzes ... |
106-193 |
6.92e-06 |
|
GH18 domain of Chitinase D (ChiD). ChiD, a chitinase found in Bacillus circulans, hydrolyzes the 1,4-beta-linkages of N-acetylglucosamine in chitin and chitodextrins. The domain architecture of ChiD includes a catalytic glycosyl hydrolase family 18 (GH18) domain, a chitin-binding domain, and a fibronectin type III domain. The chitin-binding and fibronectin type III domains are located either N-terminal or C-terminal to the catalytic domain. This family includes exochitinase Chi36 from Bacillus cereus.
Pssm-ID: 119350 [Multi-domain] Cd Length: 312 Bit Score: 47.72 E-value: 6.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520332475 106 KVLLSVGGWGARGFSGAAASKEtrkVFIQSAQEIVEKYGLDGIDLDWEFpvngawGLVASQPADRD-NFTALLKELRAAF 184
Cdd:cd02871 75 KVLISIGGANGHVDLNHTAQED---NFVDSIVAIIKEYGFDGLDIDLES------GSNPLNATPVItNLISALKQLKDHY 145
|
....*....
gi 2520332475 185 GTRKLVTIA 193
Cdd:cd02871 146 GPNFILTMA 154
|
|
| GH18_CTS3_chitinase |
cd06546 |
GH18 domain of CTS3 (chitinase 3), an uncharacterized protein from the human fungal pathogen ... |
53-198 |
1.35e-05 |
|
GH18 domain of CTS3 (chitinase 3), an uncharacterized protein from the human fungal pathogen Coccidioides posadasii. CTS3 has a chitinase-like glycosyl hydrolase family 18 (GH18) domain; and has homologs in bacteria as well as fungi.
Pssm-ID: 119363 Cd Length: 256 Bit Score: 46.17 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520332475 53 HLNYSFGLIYNDEKDEtnaalkDPAHLhEIWlspkvqadlQKLPALRKQNpdLKVLLSVGGWGARGFSGAAASKETRKVF 132
Cdd:cd06546 39 HINDDGNIHLNDHPPD------HPRFT-TLW---------TELAILQSSG--VKVMGMLGGAAPGSFSRLDDDDEDFERY 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2520332475 133 IQSAQEIVEKYGLDGIDLDWEfpvngawglvasQPADRDNFTALLKELRAAFGTRKLVTIAVGANA 198
Cdd:cd06546 101 YGQLRDMIRRRGLDGLDLDVE------------EPMSLDGIIRLIDRLRSDFGPDFIITLAPVASA 154
|
|
| GH18_PF-ChiA-like |
cd06543 |
PF-ChiA is an uncharacterized chitinase found in the hyperthermophilic archaeon Pyrococcus ... |
90-248 |
2.67e-03 |
|
PF-ChiA is an uncharacterized chitinase found in the hyperthermophilic archaeon Pyrococcus furiosus with a glycosyl hydrolase family 18 (GH18) catalytic domain as well as a cellulose-binding domain. Members of this domain family are found not only in archaea but also in eukaryotes and prokaryotes. PF-ChiA exhibits hydrolytic activity toward both colloidal and crystalline (beta/alpha) chitins at high temperature.
Pssm-ID: 119360 Cd Length: 294 Bit Score: 39.58 E-value: 2.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520332475 90 ADLQKLPALRKQNPDLKVllSVGGWGARGFSGAAASKETrkvfIQSA-QEIVEKYGLDGIDLDWEfpvnGAWglVASQPA 168
Cdd:cd06543 55 WIKSDIAALRAAGGDVIV--SFGGASGTPLATSCTSADQ----LAAAyQKVIDAYGLTHLDFDIE----GGA--LTDTAA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520332475 169 DRDNFTAlLKELRAAFGTRKL-VTIAVGANAESPKSwVDV----KAIAPSLDYINLMTydMAYGTQYFNSNLYDSshwpT 243
Cdd:cd06543 123 IDRRAQA-LALLQKEYPDLKIsFTLPVLPTGLTPDG-LNVleaaAANGVDLDTVNIMT--MDYGSSAGSQDMGAA----A 194
|
....*
gi 2520332475 244 VAAAD 248
Cdd:cd06543 195 ISAAE 199
|
|
| GH18_SI-CLP |
cd02876 |
Stabilin-1 interacting chitinase-like protein (SI-CLP) is a eukaryotic chitinase-like protein ... |
97-223 |
3.48e-03 |
|
Stabilin-1 interacting chitinase-like protein (SI-CLP) is a eukaryotic chitinase-like protein of unknown function that interacts with the endocytic/sorting transmembrane receptor stabilin-1 and is secreted from the lysosome. SI-CLP has a glycosyl hydrolase family 18 (GH18) domain but lacks a chitin-binding domain. The catalytic amino acids of the GH18 domain are not conserved in SI-CLP, similar to the chitolectins YKL-39, YKL-40, and YM1/2. Human SI-CLP is sorted to late endosomes and secretory lysosomes in alternatively activated macrophages.
Pssm-ID: 119355 [Multi-domain] Cd Length: 318 Bit Score: 39.21 E-value: 3.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2520332475 97 ALRKQNPDLKVL--LSVGGWGARGFSGAAASKETRKVFIQSAQEIVEKYGLDGIDLDwefpvngAWG-LVAS-QPADRDN 172
Cdd:cd02876 59 EVRKANKNIKILprVLFEGWSYQDLQSLLNDEQEREKLIKLLVTTAKKNHFDGIVLE-------VWSqLAAYgVPDKRKE 131
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 2520332475 173 FTALLKELRAAFGTRKLVTIAVG---ANAESPKSWV---DVKAIAPSLDYINLMTYD 223
Cdd:cd02876 132 LIQLVIHLGETLHSANLKLILVIpppREKGNQNGLFtrkDFEKLAPHVDGFSLMTYD 188
|
|
| |
