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Conserved domains on  [gi|2217284321|ref|XP_047283442|]
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chitinase domain-containing protein 1 isoform X11 [Homo sapiens]

Protein Classification

glycoside hydrolase family 18 protein( domain architecture ID 248)

glycoside hydrolase family 18 protein such as chitinase, which catalyzes the random endo-hydrolysis of the 1,4-beta-linkages of N-acetylglucosamine in chitin and chitodextrins

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
GH18_chitinase-like super family cl10447
The GH18 (glycosyl hydrolase, family 18) type II chitinases hydrolyze chitin, an abundant ...
77-288 1.30e-115

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.


The actual alignment was detected with superfamily member cd02876:

Pssm-ID: 471972 [Multi-domain]  Cd Length: 318  Bit Score: 335.43  E-value: 1.30e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217284321  77 FAGDVLGYVTPWNSHGYDVTKVFGSKFTQISPVWLQLKRRGReMFEVTGLHDVDQGWMRAVRKHAKGLHIVPRLLFEDWT 156
Cdd:cd02876     1 FQGPVLGYVTPWNSHGYDVAKKFAAKFTHVSPVWLQIKRKGN-KFVIEGTHDIDKGWIEEVRKANKNIKILPRVLFEGWS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217284321 157 YDDFRNVLDSEDEIEELSKTVVQVAKNQHFDGFVVEVWNQLLS----QKRV----------------------------- 203
Cdd:cd02876    80 YQDLQSLLNDEQEREKLIKLLVTTAKKNHFDGIVLEVWSQLAAygvpDKRKeliqlvihlgetlhsanlklilvipppre 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217284321 204 -TDQLGMFTHKEFEQLAPVLDGFSLMTYDYSTAHQPGPNAPLSWVRACVQVLDPKS-KWRSKILLGLNFYGMDYATSkDA 281
Cdd:cd02876   160 kGNQNGLFTRKDFEKLAPHVDGFSLMTYDYSSPQRPGPNAPLSWVRSCLELLLPESgKKRAKILLGLNFYGNDYTLP-GG 238

                  ....*..
gi 2217284321 282 REPVVGA 288
Cdd:cd02876   239 GGAITGS 245
 
Name Accession Description Interval E-value
GH18_SI-CLP cd02876
Stabilin-1 interacting chitinase-like protein (SI-CLP) is a eukaryotic chitinase-like protein ...
77-288 1.30e-115

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: 335.43  E-value: 1.30e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217284321  77 FAGDVLGYVTPWNSHGYDVTKVFGSKFTQISPVWLQLKRRGReMFEVTGLHDVDQGWMRAVRKHAKGLHIVPRLLFEDWT 156
Cdd:cd02876     1 FQGPVLGYVTPWNSHGYDVAKKFAAKFTHVSPVWLQIKRKGN-KFVIEGTHDIDKGWIEEVRKANKNIKILPRVLFEGWS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217284321 157 YDDFRNVLDSEDEIEELSKTVVQVAKNQHFDGFVVEVWNQLLS----QKRV----------------------------- 203
Cdd:cd02876    80 YQDLQSLLNDEQEREKLIKLLVTTAKKNHFDGIVLEVWSQLAAygvpDKRKeliqlvihlgetlhsanlklilvipppre 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217284321 204 -TDQLGMFTHKEFEQLAPVLDGFSLMTYDYSTAHQPGPNAPLSWVRACVQVLDPKS-KWRSKILLGLNFYGMDYATSkDA 281
Cdd:cd02876   160 kGNQNGLFTRKDFEKLAPHVDGFSLMTYDYSSPQRPGPNAPLSWVRSCLELLLPESgKKRAKILLGLNFYGNDYTLP-GG 238

                  ....*..
gi 2217284321 282 REPVVGA 288
Cdd:cd02876   239 GGAITGS 245
Glyco_18 smart00636
Glyco_18 domain;
81-281 2.19e-25

Glyco_18 domain;


Pssm-ID: 214753 [Multi-domain]  Cd Length: 334  Bit Score: 103.14  E-value: 2.19e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217284321   81 VLGYVTPWNSHG--YDVTKVFGSKFTQISPVWLQLKRRGrEMFEVTGLHDVDQ-GWMRAVRKHAKGLHIVprLLFEDWTY 157
Cdd:smart00636   2 VVGYFTNWGVYGrnFPVDDIPASKLTHIIYAFANIDPDG-TVTIGDEWADIGNfGQLKALKKKNPGLKVL--LSIGGWTE 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217284321  158 DD-FRNVLDSEDEIEELSKTVVQVAKNQHFDG--------------------FVVEVWNQLLSQKRVTDQL--------- 207
Cdd:smart00636  79 SDnFSSMLSDPASRKKFIDSIVSFLKKYGFDGididweypggrgddrenytaLLKELREALDKEGAEGKGYlltiavpag 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217284321  208 ---GMFTHKEFEQLAPVLDGFSLMTYDYSTA--HQPGPNAPLSW---------VRACVQVLDPKSKWRSKILLGLNFYGM 273
Cdd:smart00636 159 pdkIDKGYGDLPAIAKYLDFINLMTYDFHGAwsNPTGHNAPLYAgpgdpekynVDYAVKYYLCKGVPPSKLVLGIPFYGR 238

                   ....*...
gi 2217284321  274 DYATSKDA 281
Cdd:smart00636 239 GWTLVDGS 246
Glyco_hydro_18 pfam00704
Glycosyl hydrolases family 18;
214-281 1.19e-05

Glycosyl hydrolases family 18;


Pssm-ID: 425828 [Multi-domain]  Cd Length: 311  Bit Score: 45.91  E-value: 1.19e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217284321 214 EFEQLAPVLDGFSLMTYDYSTA--HQPGPNAPLSW-----VRACVQVLDPKSKWRSKILLGLNFYGMDYATSKDA 281
Cdd:pfam00704 163 DLPKIAKYLDFINVMTYDFHGSwdNVTGHHAPLYGggsynVDYAVKYYLKQGVPASKLVLGVPFYGRSWTLVNGS 237
ChiA COG3325
Chitinase, GH18 family [Carbohydrate transport and metabolism];
214-272 7.04e-05

Chitinase, GH18 family [Carbohydrate transport and metabolism];


Pssm-ID: 442554 [Multi-domain]  Cd Length: 391  Bit Score: 43.75  E-value: 7.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217284321 214 EFEQLAPVLDGFSLMTYDYSTA--HQPGPNAPL-------------------SWVRACVQvldpkskwRSKILLGLNFYG 272
Cdd:COG3325   208 ELPKVAQYLDYVNVMTYDFHGAwsPTTGHQAPLydspkdpeaqgysvdsavqAYLAAGVP--------ASKLVLGVPFYG 279
 
Name Accession Description Interval E-value
GH18_SI-CLP cd02876
Stabilin-1 interacting chitinase-like protein (SI-CLP) is a eukaryotic chitinase-like protein ...
77-288 1.30e-115

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: 335.43  E-value: 1.30e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217284321  77 FAGDVLGYVTPWNSHGYDVTKVFGSKFTQISPVWLQLKRRGReMFEVTGLHDVDQGWMRAVRKHAKGLHIVPRLLFEDWT 156
Cdd:cd02876     1 FQGPVLGYVTPWNSHGYDVAKKFAAKFTHVSPVWLQIKRKGN-KFVIEGTHDIDKGWIEEVRKANKNIKILPRVLFEGWS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217284321 157 YDDFRNVLDSEDEIEELSKTVVQVAKNQHFDGFVVEVWNQLLS----QKRV----------------------------- 203
Cdd:cd02876    80 YQDLQSLLNDEQEREKLIKLLVTTAKKNHFDGIVLEVWSQLAAygvpDKRKeliqlvihlgetlhsanlklilvipppre 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217284321 204 -TDQLGMFTHKEFEQLAPVLDGFSLMTYDYSTAHQPGPNAPLSWVRACVQVLDPKS-KWRSKILLGLNFYGMDYATSkDA 281
Cdd:cd02876   160 kGNQNGLFTRKDFEKLAPHVDGFSLMTYDYSSPQRPGPNAPLSWVRSCLELLLPESgKKRAKILLGLNFYGNDYTLP-GG 238

                  ....*..
gi 2217284321 282 REPVVGA 288
Cdd:cd02876   239 GGAITGS 245
Glyco_18 smart00636
Glyco_18 domain;
81-281 2.19e-25

Glyco_18 domain;


Pssm-ID: 214753 [Multi-domain]  Cd Length: 334  Bit Score: 103.14  E-value: 2.19e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217284321   81 VLGYVTPWNSHG--YDVTKVFGSKFTQISPVWLQLKRRGrEMFEVTGLHDVDQ-GWMRAVRKHAKGLHIVprLLFEDWTY 157
Cdd:smart00636   2 VVGYFTNWGVYGrnFPVDDIPASKLTHIIYAFANIDPDG-TVTIGDEWADIGNfGQLKALKKKNPGLKVL--LSIGGWTE 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217284321  158 DD-FRNVLDSEDEIEELSKTVVQVAKNQHFDG--------------------FVVEVWNQLLSQKRVTDQL--------- 207
Cdd:smart00636  79 SDnFSSMLSDPASRKKFIDSIVSFLKKYGFDGididweypggrgddrenytaLLKELREALDKEGAEGKGYlltiavpag 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217284321  208 ---GMFTHKEFEQLAPVLDGFSLMTYDYSTA--HQPGPNAPLSW---------VRACVQVLDPKSKWRSKILLGLNFYGM 273
Cdd:smart00636 159 pdkIDKGYGDLPAIAKYLDFINLMTYDFHGAwsNPTGHNAPLYAgpgdpekynVDYAVKYYLCKGVPPSKLVLGIPFYGR 238

                   ....*...
gi 2217284321  274 DYATSKDA 281
Cdd:smart00636 239 GWTLVDGS 246
GH18_chitinase-like cd00598
The GH18 (glycosyl hydrolase, family 18) type II chitinases hydrolyze chitin, an abundant ...
81-231 4.27e-18

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: 80.88  E-value: 4.27e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217284321  81 VLGYVTPWNSH-GYDVTKVFGSKFTQISPVWLQLKRRGREMFEVTGLHDVDQGWMRAVRKHAKGLHIVPRllFEDWTYDD 159
Cdd:cd00598     1 VICYYDGWSSGrGPDPTDIPLSLCTHIIYAFAEISSDGSLNLFGDKSEEPLKGALEELASKKPGLKVLIS--IGGWTDSS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217284321 160 FRNVLDSEDEIEELSKTVVQVAKNQHFDGFVVEVWNQLLS-----------QKRVTDQLGM----FTH------------ 212
Cdd:cd00598    79 PFTLASDPASRAAFANSLVSFLKTYGFDGVDIDWEYPGAAdnsdrenfitlLRELRSALGAanylLTIavpasyfdlgya 158
                         170
                  ....*....|....*....
gi 2217284321 213 KEFEQLAPVLDGFSLMTYD 231
Cdd:cd00598   159 YDVPAIGDYVDFVNVMTYD 177
GH18_CFLE_spore_hydrolase cd02874
Cortical fragment-lytic enzyme (CFLE) is a peptidoglycan hydrolase involved in bacterial ...
81-293 2.57e-14

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: 71.91  E-value: 2.57e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217284321  81 VLGYVTPWNSHGYDVTKVFGSKFTQISPVWLQLKRRGremfEVTGLHDvdqgwMRAVrKHAKGLHIVPRLLFEDWTYDDF 160
Cdd:cd02874     4 VLGYYTPRNGSDYESLRANAPYLTYIAPFWYGVDADG----TLTGLPD-----ERLI-EAAKRRGVKPLLVITNLTNGNF 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217284321 161 -----RNVLDSEDEIEELSKTVVQVAKNQHFDGFVV----------EVWNQLLSQ------------------KRVTDQL 207
Cdd:cd02874    74 dselaHAVLSNPEARQRLINNILALAKKYGYDGVNIdfenvppedrEAYTQFLRElsdrlhpagytlstavvpKTSADQF 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217284321 208 GMF--THkEFEQLAPVLDGFSLMTYDYSTAH-QPGPNAPLSWVRacvQVLD------PkskwRSKILLGLNFYGMDYATS 278
Cdd:cd02874   154 GNWsgAY-DYAAIGKIVDFVVLMTYDWHWRGgPPGPVAPIGWVE---RVLQyavtqiP----REKILLGIPLYGYDWTLP 225
                         250
                  ....*....|....*
gi 2217284321 279 KDAREPVVGASVHGA 293
Cdd:cd02874   226 YKKGGKASTISPQQA 240
Glyco_hydro_18 pfam00704
Glycosyl hydrolases family 18;
214-281 1.19e-05

Glycosyl hydrolases family 18;


Pssm-ID: 425828 [Multi-domain]  Cd Length: 311  Bit Score: 45.91  E-value: 1.19e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217284321 214 EFEQLAPVLDGFSLMTYDYSTA--HQPGPNAPLSW-----VRACVQVLDPKSKWRSKILLGLNFYGMDYATSKDA 281
Cdd:pfam00704 163 DLPKIAKYLDFINVMTYDFHGSwdNVTGHHAPLYGggsynVDYAVKYYLKQGVPASKLVLGVPFYGRSWTLVNGS 237
GH18_chitolectin_chitotriosidase cd02872
This conserved domain family includes a large number of catalytically inactive chitinase-like ...
214-293 3.14e-05

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: 44.86  E-value: 3.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217284321 214 EFEQLAPVLDGFSLMTYDY--STAHQPGPNAPLSW------------VRACVQVLDPKSKWRSKILLGLNFYGMDYATSk 279
Cdd:cd02872   172 DIPEISKYLDFINVMTYDFhgSWEGVTGHNSPLYAgsadtgdqkylnVDYAIKYWLSKGAPPEKLVLGIPTYGRSFTLA- 250
                          90
                  ....*....|....
gi 2217284321 280 DAREPVVGASVHGA 293
Cdd:cd02872   251 SPSNTGVGAPASGP 264
ChiA COG3325
Chitinase, GH18 family [Carbohydrate transport and metabolism];
214-272 7.04e-05

Chitinase, GH18 family [Carbohydrate transport and metabolism];


Pssm-ID: 442554 [Multi-domain]  Cd Length: 391  Bit Score: 43.75  E-value: 7.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217284321 214 EFEQLAPVLDGFSLMTYDYSTA--HQPGPNAPL-------------------SWVRACVQvldpkskwRSKILLGLNFYG 272
Cdd:COG3325   208 ELPKVAQYLDYVNVMTYDFHGAwsPTTGHQAPLydspkdpeaqgysvdsavqAYLAAGVP--------ASKLVLGVPFYG 279
GH18_chitinase cd06548
The GH18 (glycosyl hydrolases, family 18) type II chitinases hydrolyze chitin, an abundant ...
212-272 6.59e-03

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: 37.61  E-value: 6.59e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217284321 212 HKEFEQLAPVLDGFSLMTYDYS------TAHQ----PGPNAPLS------WVRACVQVLDPKskwrSKILLGLNFYG 272
Cdd:cd06548   191 KLEVAEIAKYLDFINLMTYDFHgawsntTGHHsnlyASPADPPGgysvdaAVNYYLSAGVPP----EKLVLGVPFYG 263
 
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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