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Conserved domains on  [gi|158297031|ref|XP_317335|]
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AGAP008124-PA, partial [Anopheles gambiae str. PEST]

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 ...
84-402 1.14e-175

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: 492.21  E-value: 1.14e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158297031  84 FEGKVLGFVTPWNNHGYDVAKLWGPKFDYVSPVWLQILRKGPKkYEVAGVHDIDDGWVKDVKKAGSTInnRVIPRVLFDK 163
Cdd:cd02876    1 FQGPVLGYVTPWNSHGYDVAKKFAAKFTHVSPVWLQIKRKGNK-FVIEGTHDIDKGWIEEVRKANKNI--KILPRVLFEG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158297031 164 FTDRDFSQLLTYPEERTIVAKLLLATARKHRFDGLVLEVWSQLAARV---EDSYLIGLVEEICNTLTAASYDCILVIPPA 240
Cdd:cd02876   78 WSYQDLQSLLNDEQEREKLIKLLVTTAKKNHFDGIVLEVWSQLAAYGvpdKRKELIQLVIHLGETLHSANLKLILVIPPP 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158297031 241 RK--ETYDLFSRKHFEALEPSVTAFSLMTYDFSSVQRPGANAPLYWVRNAVQHVCPDGADrmreKRAKILVGLNMYGSDF 318
Cdd:cd02876  158 REkgNQNGLFTRKDFEKLAPHVDGFSLMTYDYSSPQRPGPNAPLSWVRSCLELLLPESGK----KRAKILLGLNFYGNDY 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158297031 319 TPNG-GQPIVAHEYLALLKHLKGHLTYDEHDVENFFEVKTSNGRHMVFYPTLFSIDERLKLARELGTGISIWELGQGLDY 397
Cdd:cd02876  234 TLPGgGGAITGSEYLKLLKSNKPKLQWDEKSAEHFFEYKNKGGKHAVFYPTLKSIQLRLDLAKELGTGISIWELGQGLDY 313

                 ....*
gi 158297031 398 FYDLF 402
Cdd:cd02876  314 FYDLL 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 ...
84-402 1.14e-175

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: 492.21  E-value: 1.14e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158297031  84 FEGKVLGFVTPWNNHGYDVAKLWGPKFDYVSPVWLQILRKGPKkYEVAGVHDIDDGWVKDVKKAGSTInnRVIPRVLFDK 163
Cdd:cd02876    1 FQGPVLGYVTPWNSHGYDVAKKFAAKFTHVSPVWLQIKRKGNK-FVIEGTHDIDKGWIEEVRKANKNI--KILPRVLFEG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158297031 164 FTDRDFSQLLTYPEERTIVAKLLLATARKHRFDGLVLEVWSQLAARV---EDSYLIGLVEEICNTLTAASYDCILVIPPA 240
Cdd:cd02876   78 WSYQDLQSLLNDEQEREKLIKLLVTTAKKNHFDGIVLEVWSQLAAYGvpdKRKELIQLVIHLGETLHSANLKLILVIPPP 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158297031 241 RK--ETYDLFSRKHFEALEPSVTAFSLMTYDFSSVQRPGANAPLYWVRNAVQHVCPDGADrmreKRAKILVGLNMYGSDF 318
Cdd:cd02876  158 REkgNQNGLFTRKDFEKLAPHVDGFSLMTYDYSSPQRPGPNAPLSWVRSCLELLLPESGK----KRAKILLGLNFYGNDY 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158297031 319 TPNG-GQPIVAHEYLALLKHLKGHLTYDEHDVENFFEVKTSNGRHMVFYPTLFSIDERLKLARELGTGISIWELGQGLDY 397
Cdd:cd02876  234 TLPGgGGAITGSEYLKLLKSNKPKLQWDEKSAEHFFEYKNKGGKHAVFYPTLKSIQLRLDLAKELGTGISIWELGQGLDY 313

                 ....*
gi 158297031 398 FYDLF 402
Cdd:cd02876  314 FYDLL 318
Glyco_18 smart00636
Glyco_18 domain;
87-393 7.49e-25

Glyco_18 domain;


Pssm-ID: 214753 [Multi-domain]  Cd Length: 334  Bit Score: 103.91  E-value: 7.49e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158297031    87 KVLGFVTPWNNHG--YDVAKLWGPKFDYVSPVWLQIlrKGPKKYEVAGVH-DID-DGWVKDVKKAGSTInnRVIPRVLFD 162
Cdd:smart00636   1 RVVGYFTNWGVYGrnFPVDDIPASKLTHIIYAFANI--DPDGTVTIGDEWaDIGnFGQLKALKKKNPGL--KVLLSIGGW 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158297031   163 KFTDRdFSQLLTYPEERTIVAKLLLATARKHRFDGLVLEvWSQLAARVED-SYLIGLVEEICNTLTAASYDC---ILVIP 238
Cdd:smart00636  77 TESDN-FSSMLSDPASRKKFIDSIVSFLKKYGFDGIDID-WEYPGGRGDDrENYTALLKELREALDKEGAEGkgyLLTIA 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158297031   239 PARKETYDLFSRKHFEALEPSVTAFSLMTYDFSSV--QRPGANAPLYWVRNAVQHVCPD-GADRMREKRA---KILVGLN 312
Cdd:smart00636 155 VPAGPDKIDKGYGDLPAIAKYLDFINLMTYDFHGAwsNPTGHNAPLYAGPGDPEKYNVDyAVKYYLCKGVppsKLVLGIP 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158297031   313 MYGSDFT----PNGGQPIVAH---------------EYLALLKHLKGHLTYDEhDVENFFEVKTSNGrHMVFYPTLFSID 373
Cdd:smart00636 235 FYGRGWTlvdgSNNGPGAPFTgpatggpgtweggvvDYREICKLLGATVVYDD-TAKAPYAYNPGTG-QWVSYDDPRSIK 312
                          330       340
                   ....*....|....*....|.
gi 158297031   374 ERLKLARELGT-GISIWELGQ 393
Cdd:smart00636 313 AKADYVKDKGLgGVMIWELDA 333
Glyco_hydro_18 pfam00704
Glycosyl hydrolases family 18;
169-393 4.42e-13

Glycosyl hydrolases family 18;


Pssm-ID: 425828 [Multi-domain]  Cd Length: 311  Bit Score: 69.41  E-value: 4.42e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158297031  169 FSQLLTYPEERTIVAKLLLATARKHRFDGLVLEvWSQLAARVED-SYLIGLVEEICNTLTAASYDCILVI---PPARKET 244
Cdd:pfam00704  79 FSLMASNPASRKKFADSIVSFLRKYGFDGIDID-WEYPGGNPEDkENYDLLLRELRAALDEAKGGKKYLLsaaVPASYPD 157
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158297031  245 YDLFSrkHFEALEPSVTAFSLMTYDFSS--VQRPGANAPLYW-----VRNAVQHVCPDGADrmrekRAKILVGLNMYGSD 317
Cdd:pfam00704 158 LDKGY--DLPKIAKYLDFINVMTYDFHGswDNVTGHHAPLYGggsynVDYAVKYYLKQGVP-----ASKLVLGVPFYGRS 230
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158297031  318 FT----PNGGQPIVAHEYLALLKHLKGHLT---YDEHDVENFfevkTSNGRHMVFYPTLFSIDERLKLARE--LGtGISI 388
Cdd:pfam00704 231 WTlvngSGNTWEDGVLAYKEICNLLKDNGAtvvWDDVAKAPY----VYDGDQFITYDDPRSIATKVDYVKAkgLG-GVMI 305

                  ....*
gi 158297031  389 WELGQ 393
Cdd:pfam00704 306 WSLDA 310
 
Name Accession Description Interval E-value
GH18_SI-CLP cd02876
Stabilin-1 interacting chitinase-like protein (SI-CLP) is a eukaryotic chitinase-like protein ...
84-402 1.14e-175

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: 492.21  E-value: 1.14e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158297031  84 FEGKVLGFVTPWNNHGYDVAKLWGPKFDYVSPVWLQILRKGPKkYEVAGVHDIDDGWVKDVKKAGSTInnRVIPRVLFDK 163
Cdd:cd02876    1 FQGPVLGYVTPWNSHGYDVAKKFAAKFTHVSPVWLQIKRKGNK-FVIEGTHDIDKGWIEEVRKANKNI--KILPRVLFEG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158297031 164 FTDRDFSQLLTYPEERTIVAKLLLATARKHRFDGLVLEVWSQLAARV---EDSYLIGLVEEICNTLTAASYDCILVIPPA 240
Cdd:cd02876   78 WSYQDLQSLLNDEQEREKLIKLLVTTAKKNHFDGIVLEVWSQLAAYGvpdKRKELIQLVIHLGETLHSANLKLILVIPPP 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158297031 241 RK--ETYDLFSRKHFEALEPSVTAFSLMTYDFSSVQRPGANAPLYWVRNAVQHVCPDGADrmreKRAKILVGLNMYGSDF 318
Cdd:cd02876  158 REkgNQNGLFTRKDFEKLAPHVDGFSLMTYDYSSPQRPGPNAPLSWVRSCLELLLPESGK----KRAKILLGLNFYGNDY 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158297031 319 TPNG-GQPIVAHEYLALLKHLKGHLTYDEHDVENFFEVKTSNGRHMVFYPTLFSIDERLKLARELGTGISIWELGQGLDY 397
Cdd:cd02876  234 TLPGgGGAITGSEYLKLLKSNKPKLQWDEKSAEHFFEYKNKGGKHAVFYPTLKSIQLRLDLAKELGTGISIWELGQGLDY 313

                 ....*
gi 158297031 398 FYDLF 402
Cdd:cd02876  314 FYDLL 318
Glyco_18 smart00636
Glyco_18 domain;
87-393 7.49e-25

Glyco_18 domain;


Pssm-ID: 214753 [Multi-domain]  Cd Length: 334  Bit Score: 103.91  E-value: 7.49e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158297031    87 KVLGFVTPWNNHG--YDVAKLWGPKFDYVSPVWLQIlrKGPKKYEVAGVH-DID-DGWVKDVKKAGSTInnRVIPRVLFD 162
Cdd:smart00636   1 RVVGYFTNWGVYGrnFPVDDIPASKLTHIIYAFANI--DPDGTVTIGDEWaDIGnFGQLKALKKKNPGL--KVLLSIGGW 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158297031   163 KFTDRdFSQLLTYPEERTIVAKLLLATARKHRFDGLVLEvWSQLAARVED-SYLIGLVEEICNTLTAASYDC---ILVIP 238
Cdd:smart00636  77 TESDN-FSSMLSDPASRKKFIDSIVSFLKKYGFDGIDID-WEYPGGRGDDrENYTALLKELREALDKEGAEGkgyLLTIA 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158297031   239 PARKETYDLFSRKHFEALEPSVTAFSLMTYDFSSV--QRPGANAPLYWVRNAVQHVCPD-GADRMREKRA---KILVGLN 312
Cdd:smart00636 155 VPAGPDKIDKGYGDLPAIAKYLDFINLMTYDFHGAwsNPTGHNAPLYAGPGDPEKYNVDyAVKYYLCKGVppsKLVLGIP 234
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158297031   313 MYGSDFT----PNGGQPIVAH---------------EYLALLKHLKGHLTYDEhDVENFFEVKTSNGrHMVFYPTLFSID 373
Cdd:smart00636 235 FYGRGWTlvdgSNNGPGAPFTgpatggpgtweggvvDYREICKLLGATVVYDD-TAKAPYAYNPGTG-QWVSYDDPRSIK 312
                          330       340
                   ....*....|....*....|.
gi 158297031   374 ERLKLARELGT-GISIWELGQ 393
Cdd:smart00636 313 AKADYVKDKGLgGVMIWELDA 333
GH18_CFLE_spore_hydrolase cd02874
Cortical fragment-lytic enzyme (CFLE) is a peptidoglycan hydrolase involved in bacterial ...
88-393 9.46e-19

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: 86.16  E-value: 9.46e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158297031  88 VLGFVTPWNNHGYDVAKLWGPKFDYVSPVWLQILRKGpkkyevaGVHDIDDGWVKDVKKagstiNNRVIPRVLFDKFTDR 167
Cdd:cd02874    4 VLGYYTPRNGSDYESLRANAPYLTYIAPFWYGVDADG-------TLTGLPDERLIEAAK-----RRGVKPLLVITNLTNG 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158297031 168 DFS-----QLLTYPEERTIVAKLLLATARKHRFDGLVL--EvwsqlAARVED-SYLIGLVEEICNTLTAASYdcIL---V 236
Cdd:cd02874   72 NFDselahAVLSNPEARQRLINNILALAKKYGYDGVNIdfE-----NVPPEDrEAYTQFLRELSDRLHPAGY--TLstaV 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158297031 237 IPPARKETYDLFSRKH-FEALEPSVTAFSLMTYDF---SSVqrPGANAPLYWVRN----AVQHVcpdgadrmreKRAKIL 308
Cdd:cd02874  145 VPKTSADQFGNWSGAYdYAAIGKIVDFVVLMTYDWhwrGGP--PGPVAPIGWVERvlqyAVTQI----------PREKIL 212
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158297031 309 VGLNMYGSDFT--PNGGQPIVAHEYLALLKHLKGH---LTYDE-HDVENFFEVKTSNGRHMVFYPTLFSIDERLKLAREL 382
Cdd:cd02874  213 LGIPLYGYDWTlpYKKGGKASTISPQQAINLAKRYgaeIQYDEeAQSPFFRYVDEQGRRHEVWFEDARSLQAKFELAKEY 292
                        330
                 ....*....|..
gi 158297031 383 G-TGISIWELGQ 393
Cdd:cd02874  293 GlRGVSYWRLGL 304
Glyco_hydro_18 pfam00704
Glycosyl hydrolases family 18;
169-393 4.42e-13

Glycosyl hydrolases family 18;


Pssm-ID: 425828 [Multi-domain]  Cd Length: 311  Bit Score: 69.41  E-value: 4.42e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158297031  169 FSQLLTYPEERTIVAKLLLATARKHRFDGLVLEvWSQLAARVED-SYLIGLVEEICNTLTAASYDCILVI---PPARKET 244
Cdd:pfam00704  79 FSLMASNPASRKKFADSIVSFLRKYGFDGIDID-WEYPGGNPEDkENYDLLLRELRAALDEAKGGKKYLLsaaVPASYPD 157
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158297031  245 YDLFSrkHFEALEPSVTAFSLMTYDFSS--VQRPGANAPLYW-----VRNAVQHVCPDGADrmrekRAKILVGLNMYGSD 317
Cdd:pfam00704 158 LDKGY--DLPKIAKYLDFINVMTYDFHGswDNVTGHHAPLYGggsynVDYAVKYYLKQGVP-----ASKLVLGVPFYGRS 230
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158297031  318 FT----PNGGQPIVAHEYLALLKHLKGHLT---YDEHDVENFfevkTSNGRHMVFYPTLFSIDERLKLARE--LGtGISI 388
Cdd:pfam00704 231 WTlvngSGNTWEDGVLAYKEICNLLKDNGAtvvWDDVAKAPY----VYDGDQFITYDDPRSIATKVDYVKAkgLG-GVMI 305

                  ....*
gi 158297031  389 WELGQ 393
Cdd:pfam00704 306 WSLDA 310
GH18_chitolectin_chitotriosidase cd02872
This conserved domain family includes a large number of catalytically inactive chitinase-like ...
169-319 1.16e-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: 47.17  E-value: 1.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158297031 169 FSQLLTYPEERTIVAKLLLATARKHRFDGLVLEvW---SQLAARVED-SYLIGLVEEICNT---------LTAAsydcIL 235
Cdd:cd02872   87 FSAMAASPENRKTFIKSAIAFLRKYGFDGLDLD-WeypGQRGGPPEDkENFVTLLKELREAfepeaprllLTAA----VS 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 158297031 236 VIPPARKETYDLfsrkhfEALEPSVTAFSLMTYDF--SSVQRPGANAPLYW------------VRNAVQHVCPDGADrmr 301
Cdd:cd02872  162 AGKETIDAAYDI------PEISKYLDFINVMTYDFhgSWEGVTGHNSPLYAgsadtgdqkylnVDYAIKYWLSKGAP--- 232
                        170
                 ....*....|....*...
gi 158297031 302 ekRAKILVGLNMYGSDFT 319
Cdd:cd02872  233 --PEKLVLGIPTYGRSFT 248
 
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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