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Conserved domains on  [gi|25150970|ref|NP_508185|]
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Chitinase domain-containing protein 1 [Caenorhabditis elegans]

Protein Classification

GH18_SI-CLP domain-containing protein( domain architecture ID 10120846)

GH18_SI-CLP domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
GH18_SI-CLP cd02876
Stabilin-1 interacting chitinase-like protein (SI-CLP) is a eukaryotic chitinase-like protein ...
57-370 3.10e-144

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: 411.32  E-value: 3.10e-144
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150970  57 EGLTQLAYITPWNRHGYELAEKTAHKLTHVSPVWFQAKAFSengklDGCKIEGTHEINRDWIEKLREKNENIAIVPRILF 136
Cdd:cd02876   1 FQGPVLGYVTPWNSHGYDVAKKFAAKFTHVSPVWLQIKRKG-----NKFVIEGTHDIDKGWIEEVRKANKNIKILPRVLF 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150970 137 DGWSAQEMKNLLMDAKVARHCFEDIANFYSRNQFEGAVVELYMQALISVqsleVKEFIIESIQDLSRQMKKLH---MQVI 213
Cdd:cd02876  76 EGWSYQDLQSLLNDEQEREKLIKLLVTTAKKNHFDGIVLEVWSQLAAYG----VPDKRKELIQLVIHLGETLHsanLKLI 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150970 214 LTVPAPLEWNNQPnNLVTPDDFKKITAVSDFVQIMTYDYRG-NKPAGVAPYDWFESCIFYLGG-----GHKTLAGLNFYG 287
Cdd:cd02876 152 LVIPPPREKGNQN-GLFTRKDFEKLAPHVDGFSLMTYDYSSpQRPGPNAPLSWVRSCLELLLPesgkkRAKILLGLNFYG 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150970 288 YEFSK-GNVEAITADRYLTLLKSEKSKLEFDEKSMEHRVKTSNS----IAYFPSLTSLELRINMAHRYDVGIAIWDYGQG 362
Cdd:cd02876 231 NDYTLpGGGGAITGSEYLKLLKSNKPKLQWDEKSAEHFFEYKNKggkhAVFYPTLKSIQLRLDLAKELGTGISIWELGQG 310

                ....*...
gi 25150970 363 LDYFTNLL 370
Cdd:cd02876 311 LDYFYDLL 318
 
Name Accession Description Interval E-value
GH18_SI-CLP cd02876
Stabilin-1 interacting chitinase-like protein (SI-CLP) is a eukaryotic chitinase-like protein ...
57-370 3.10e-144

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: 411.32  E-value: 3.10e-144
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150970  57 EGLTQLAYITPWNRHGYELAEKTAHKLTHVSPVWFQAKAFSengklDGCKIEGTHEINRDWIEKLREKNENIAIVPRILF 136
Cdd:cd02876   1 FQGPVLGYVTPWNSHGYDVAKKFAAKFTHVSPVWLQIKRKG-----NKFVIEGTHDIDKGWIEEVRKANKNIKILPRVLF 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150970 137 DGWSAQEMKNLLMDAKVARHCFEDIANFYSRNQFEGAVVELYMQALISVqsleVKEFIIESIQDLSRQMKKLH---MQVI 213
Cdd:cd02876  76 EGWSYQDLQSLLNDEQEREKLIKLLVTTAKKNHFDGIVLEVWSQLAAYG----VPDKRKELIQLVIHLGETLHsanLKLI 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150970 214 LTVPAPLEWNNQPnNLVTPDDFKKITAVSDFVQIMTYDYRG-NKPAGVAPYDWFESCIFYLGG-----GHKTLAGLNFYG 287
Cdd:cd02876 152 LVIPPPREKGNQN-GLFTRKDFEKLAPHVDGFSLMTYDYSSpQRPGPNAPLSWVRSCLELLLPesgkkRAKILLGLNFYG 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150970 288 YEFSK-GNVEAITADRYLTLLKSEKSKLEFDEKSMEHRVKTSNS----IAYFPSLTSLELRINMAHRYDVGIAIWDYGQG 362
Cdd:cd02876 231 NDYTLpGGGGAITGSEYLKLLKSNKPKLQWDEKSAEHFFEYKNKggkhAVFYPTLKSIQLRLDLAKELGTGISIWELGQG 310

                ....*...
gi 25150970 363 LDYFTNLL 370
Cdd:cd02876 311 LDYFYDLL 318
Glyco_hydro_18 pfam00704
Glycosyl hydrolases family 18;
63-361 1.14e-04

Glycosyl hydrolases family 18;


Pssm-ID: 425828 [Multi-domain]  Cd Length: 311  Bit Score: 43.60  E-value: 1.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150970    63 AYITPWNRHGyELAEKTAHKLTHVspVWFQAKAFSENGKLdgcKIEGTHEINRDWIEKLR-EKNENIAIVPRIlfDGWSA 141
Cdd:pfam00704   4 GYYTSWGVYR-NGNFLPSDKLTHI--IYAFANIDGSDGTL---FIGDWDLGNFEQLKKLKkQKNPGVKVLLSI--GGWTD 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150970   142 QEMKNLLMDAKVARHCFED-IANFYSRNQFEGavVELYMQAliSVQSLEVKEFIIESIQDLSRQMKKL--HMQVILT--V 216
Cdd:pfam00704  76 STGFSLMASNPASRKKFADsIVSFLRKYGFDG--IDIDWEY--PGGNPEDKENYDLLLRELRAALDEAkgGKKYLLSaaV 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150970   217 PAPlewnnqPNNLVTPDDFKKITAVSDFVQIMTYDYRG--NKPAG-VAP-YDWFESCI-----FYLGGG---HKTLAGLN 284
Cdd:pfam00704 152 PAS------YPDLDKGYDLPKIAKYLDFINVMTYDFHGswDNVTGhHAPlYGGGSYNVdyavkYYLKQGvpaSKLVLGVP 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150970   285 FYGYEFSKGNVEAITADR-------YLTLLKSEKSKLEFDEKSMEHRVKTSNSIAYFPSLTSLELRINMAHRYDV-GIAI 356
Cdd:pfam00704 226 FYGRSWTLVNGSGNTWEDgvlaykeICNLLKDNGATVVWDDVAKAPYVYDGDQFITYDDPRSIATKVDYVKAKGLgGVMI 305

                  ....*
gi 25150970   357 WDYGQ 361
Cdd:pfam00704 306 WSLDA 310
Glyco_18 smart00636
Glyco_18 domain;
62-290 1.93e-04

Glyco_18 domain;


Pssm-ID: 214753 [Multi-domain]  Cd Length: 334  Bit Score: 43.05  E-value: 1.93e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150970     62 LAYITPWNRHG--YELAEKTAHKLTHVSPVWFQAKAFSENGKLDGCKIEGtheiNRDWIEKLREKNENIAIVPRIlfDGW 139
Cdd:smart00636   3 VGYFTNWGVYGrnFPVDDIPASKLTHIIYAFANIDPDGTVTIGDEWADIG----NFGQLKALKKKNPGLKVLLSI--GGW 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150970    140 SA-QEMKNLLMDAKVARHCFEDIANFYSRNQFEGavVEL---YmqaliSVQSLEVKEFIIESIQDLSRQMKKL-----HM 210
Cdd:smart00636  77 TEsDNFSSMLSDPASRKKFIDSIVSFLKKYGFDG--IDIdweY-----PGGRGDDRENYTALLKELREALDKEgaegkGY 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150970    211 QVILTVPAplewnNQPNNLVTPDDFKKITAVSDFVQIMTYDYRG--NKPAG-VAPYDW---------FESCI-FYLGGG- 276
Cdd:smart00636 150 LLTIAVPA-----GPDKIDKGYGDLPAIAKYLDFINLMTYDFHGawSNPTGhNAPLYAgpgdpekynVDYAVkYYLCKGv 224
                          250
                   ....*....|....*.
gi 25150970    277 --HKTLAGLNFYGYEF 290
Cdd:smart00636 225 ppSKLVLGIPFYGRGW 240
 
Name Accession Description Interval E-value
GH18_SI-CLP cd02876
Stabilin-1 interacting chitinase-like protein (SI-CLP) is a eukaryotic chitinase-like protein ...
57-370 3.10e-144

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: 411.32  E-value: 3.10e-144
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150970  57 EGLTQLAYITPWNRHGYELAEKTAHKLTHVSPVWFQAKAFSengklDGCKIEGTHEINRDWIEKLREKNENIAIVPRILF 136
Cdd:cd02876   1 FQGPVLGYVTPWNSHGYDVAKKFAAKFTHVSPVWLQIKRKG-----NKFVIEGTHDIDKGWIEEVRKANKNIKILPRVLF 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150970 137 DGWSAQEMKNLLMDAKVARHCFEDIANFYSRNQFEGAVVELYMQALISVqsleVKEFIIESIQDLSRQMKKLH---MQVI 213
Cdd:cd02876  76 EGWSYQDLQSLLNDEQEREKLIKLLVTTAKKNHFDGIVLEVWSQLAAYG----VPDKRKELIQLVIHLGETLHsanLKLI 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150970 214 LTVPAPLEWNNQPnNLVTPDDFKKITAVSDFVQIMTYDYRG-NKPAGVAPYDWFESCIFYLGG-----GHKTLAGLNFYG 287
Cdd:cd02876 152 LVIPPPREKGNQN-GLFTRKDFEKLAPHVDGFSLMTYDYSSpQRPGPNAPLSWVRSCLELLLPesgkkRAKILLGLNFYG 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150970 288 YEFSK-GNVEAITADRYLTLLKSEKSKLEFDEKSMEHRVKTSNS----IAYFPSLTSLELRINMAHRYDVGIAIWDYGQG 362
Cdd:cd02876 231 NDYTLpGGGGAITGSEYLKLLKSNKPKLQWDEKSAEHFFEYKNKggkhAVFYPTLKSIQLRLDLAKELGTGISIWELGQG 310

                ....*...
gi 25150970 363 LDYFTNLL 370
Cdd:cd02876 311 LDYFYDLL 318
GH18_CFLE_spore_hydrolase cd02874
Cortical fragment-lytic enzyme (CFLE) is a peptidoglycan hydrolase involved in bacterial ...
62-361 2.78e-20

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: 90.02  E-value: 2.78e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150970  62 LAYITPWNRHGYELAEKTAHKLTHVSPVWFQakaFSENGKLDGckiegthEINRDWIEKLREKN-ENIAIVPRILFDGWS 140
Cdd:cd02874   5 LGYYTPRNGSDYESLRANAPYLTYIAPFWYG---VDADGTLTG-------LPDERLIEAAKRRGvKPLLVITNLTNGNFD 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150970 141 AQEMKNLLMDAKVARHCFEDIANFYSRNQFEGAVVELymqalisvqslevkEFIieSIQD------LSRQMKK-LHMQ-- 211
Cdd:cd02874  75 SELAHAVLSNPEARQRLINNILALAKKYGYDGVNIDF--------------ENV--PPEDreaytqFLRELSDrLHPAgy 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150970 212 VILTVPAPLEWNNQPNNLVTPDDFKKITAVSDFVQIMTYD--YRGNKPAGVAPYDWFESCIFYLGGG---HKTLAGLNFY 286
Cdd:cd02874 139 TLSTAVVPKTSADQFGNWSGAYDYAAIGKIVDFVVLMTYDwhWRGGPPGPVAPIGWVERVLQYAVTQiprEKILLGIPLY 218
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150970 287 GYEFSKGNVEAITAdRYLT------LLKSEKSKLEFDEKS------------MEHRVktsnsiaYFPSLTSLELRINMAH 348
Cdd:cd02874 219 GYDWTLPYKKGGKA-STISpqqainLAKRYGAEIQYDEEAqspffryvdeqgRRHEV-------WFEDARSLQAKFELAK 290
                       330
                ....*....|....
gi 25150970 349 RYDV-GIAIWDYGQ 361
Cdd:cd02874 291 EYGLrGVSYWRLGL 304
GH18_trifunctional cd06549
GH18 domain of an uncharacterized family of bacterial proteins, which share a common ...
60-361 8.40e-14

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: 71.29  E-value: 8.40e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150970  60 TQLAYITPWNRHGYELAEKTAHKLTHVSPVWFQAKAfsENGKLDGCKIEGTHEInrdwIEKLREKNENIAIVPRILFDGW 139
Cdd:cd06549   1 IALAFYTPWDDASFASLKRHAPRLDWLVPEWLNLTG--PEGRIDVFVDPQGVAI----IAAAKAHPKVLPLVQNISGGAW 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150970 140 SAQEMKNLLMDAKvARHCFED-IANFYSRNQFEGAVVELymqALISVQSLEvkeFIIESIQDLSRQMKKLHMQVILTVPA 218
Cdd:cd06549  75 DGKNIARLLADPS-ARAKFIAnIAAYLERNQADGIVLDF---EELPADDLP---KYVAFLSELRRRLPAQGKQLTVTVPA 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150970 219 PLEWNNQPNNLvtpddfkkitAVSDFVQIMTYD--YRGNKPAGVAPYDWFESCIFYLGGG---HKTLAGLNFYGYEFSK- 292
Cdd:cd06549 148 DEADWNLKALA----------RNADKLILMAYDehYQGGAPGPIASQDWFESNLAQAVKKlppEKLIVALGSYGYDWTKg 217
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 25150970 293 GNVEAITADRYLTLLKSEKSKLEFDEKSME--HRVKTSNSIA---YFPSLTSLELRINMAHRYDV-GIAIWDYGQ 361
Cdd:cd06549 218 GNTKAISSEAAWLLAAHASAAVKFDDKASNatYFFYDDEGVShevWMLDAVTLFNQLKAVQRLGPaGVALWRLGS 292
GH18_chitinase-like cd00598
The GH18 (glycosyl hydrolase, family 18) type II chitinases hydrolyze chitin, an abundant ...
63-251 7.51e-08

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: 52.38  E-value: 7.51e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150970  63 AYITPWNRHGYELAEKT-AHKLTHVSPVWFQAKAFsENGKLDGCKIEgthEINRDWIEKLREKNENIAIVPRIlfDGWSA 141
Cdd:cd00598   3 CYYDGWSSGRGPDPTDIpLSLCTHIIYAFAEISSD-GSLNLFGDKSE---EPLKGALEELASKKPGLKVLISI--GGWTD 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150970 142 QEMKNLLMDAKVARHCFEDIANFYSRNQFEGavVELYMQALISVQSLEvKEFIIESIQDLSRQMKKLHMQVILTVPAPle 221
Cdd:cd00598  77 SSPFTLASDPASRAAFANSLVSFLKTYGFDG--VDIDWEYPGAADNSD-RENFITLLRELRSALGAANYLLTIAVPAS-- 151
                       170       180       190
                ....*....|....*....|....*....|
gi 25150970 222 wnnqPNNLVTPDDFKKITAVSDFVQIMTYD 251
Cdd:cd00598 152 ----YFDLGYAYDVPAIGDYVDFVNVMTYD 177
Glyco_hydro_18 pfam00704
Glycosyl hydrolases family 18;
63-361 1.14e-04

Glycosyl hydrolases family 18;


Pssm-ID: 425828 [Multi-domain]  Cd Length: 311  Bit Score: 43.60  E-value: 1.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150970    63 AYITPWNRHGyELAEKTAHKLTHVspVWFQAKAFSENGKLdgcKIEGTHEINRDWIEKLR-EKNENIAIVPRIlfDGWSA 141
Cdd:pfam00704   4 GYYTSWGVYR-NGNFLPSDKLTHI--IYAFANIDGSDGTL---FIGDWDLGNFEQLKKLKkQKNPGVKVLLSI--GGWTD 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150970   142 QEMKNLLMDAKVARHCFED-IANFYSRNQFEGavVELYMQAliSVQSLEVKEFIIESIQDLSRQMKKL--HMQVILT--V 216
Cdd:pfam00704  76 STGFSLMASNPASRKKFADsIVSFLRKYGFDG--IDIDWEY--PGGNPEDKENYDLLLRELRAALDEAkgGKKYLLSaaV 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150970   217 PAPlewnnqPNNLVTPDDFKKITAVSDFVQIMTYDYRG--NKPAG-VAP-YDWFESCI-----FYLGGG---HKTLAGLN 284
Cdd:pfam00704 152 PAS------YPDLDKGYDLPKIAKYLDFINVMTYDFHGswDNVTGhHAPlYGGGSYNVdyavkYYLKQGvpaSKLVLGVP 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150970   285 FYGYEFSKGNVEAITADR-------YLTLLKSEKSKLEFDEKSMEHRVKTSNSIAYFPSLTSLELRINMAHRYDV-GIAI 356
Cdd:pfam00704 226 FYGRSWTLVNGSGNTWEDgvlaykeICNLLKDNGATVVWDDVAKAPYVYDGDQFITYDDPRSIATKVDYVKAKGLgGVMI 305

                  ....*
gi 25150970   357 WDYGQ 361
Cdd:pfam00704 306 WSLDA 310
Glyco_18 smart00636
Glyco_18 domain;
62-290 1.93e-04

Glyco_18 domain;


Pssm-ID: 214753 [Multi-domain]  Cd Length: 334  Bit Score: 43.05  E-value: 1.93e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150970     62 LAYITPWNRHG--YELAEKTAHKLTHVSPVWFQAKAFSENGKLDGCKIEGtheiNRDWIEKLREKNENIAIVPRIlfDGW 139
Cdd:smart00636   3 VGYFTNWGVYGrnFPVDDIPASKLTHIIYAFANIDPDGTVTIGDEWADIG----NFGQLKALKKKNPGLKVLLSI--GGW 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150970    140 SA-QEMKNLLMDAKVARHCFEDIANFYSRNQFEGavVEL---YmqaliSVQSLEVKEFIIESIQDLSRQMKKL-----HM 210
Cdd:smart00636  77 TEsDNFSSMLSDPASRKKFIDSIVSFLKKYGFDG--IDIdweY-----PGGRGDDRENYTALLKELREALDKEgaegkGY 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150970    211 QVILTVPAplewnNQPNNLVTPDDFKKITAVSDFVQIMTYDYRG--NKPAG-VAPYDW---------FESCI-FYLGGG- 276
Cdd:smart00636 150 LLTIAVPA-----GPDKIDKGYGDLPAIAKYLDFINLMTYDFHGawSNPTGhNAPLYAgpgdpekynVDYAVkYYLCKGv 224
                          250
                   ....*....|....*.
gi 25150970    277 --HKTLAGLNFYGYEF 290
Cdd:smart00636 225 ppSKLVLGIPFYGRGW 240
GH18_3CO4_chitinase cd06545
The Bacteroides thetaiotaomicron protein represented by pdb structure 3CO4 is an ...
82-291 7.97e-04

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: 40.51  E-value: 7.97e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150970  82 KLTHVSpvwfqaKAFsENGKLDGCKIEGTheiNRDWIEKLREKNENIAIVPRILFDGWSAQEMKNLLMDAKVARHCFEDI 161
Cdd:cd06545  22 KLTHIN------LAF-ANPDANGTLNANP---VRSELNSVVNAAHAHNVKILISLAGGSPPEFTAALNDPAKRKALVDKI 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25150970 162 ANFYSRNQFEGAVVELYMQAlISVQSLEVkeFIIESIQDLSRQMKklhmqvILTVPAPLEWNNQPNNlvtpddfkKITAV 241
Cdd:cd06545  92 INYVVSYNLDGIDVDLEGPD-VTFGDYLV--FIRALYAALKKEGK------LLTAAVSSWNGGAVSD--------STLAY 154
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 25150970 242 SDFVQIMTYD----YRGNKPAGVAPYDWFESCIFY-----LGGGHKTLAGLNFYGYEFS 291
Cdd:cd06545 155 FDFINIMSYDatgpWWGDNPGQHSSYDDAVNDLNYwnergLASKDKLVLGLPFYGYGFY 213
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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