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Conserved domains on  [gi|315932708|gb|ADU55784|]
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HSP25.5 [Citrullus lanatus]

Protein Classification

HSP20 family small heat-shock protein( domain architecture ID 10439842)

HSP20 family small heat-shock protein (sHsp) such as tomato chloroplast small heat shock protein HSP21 which is protecting photosystem II from oxidative stress and promoting color changes during fruit maturation.

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HSP20 pfam00011
Hsp20/alpha crystallin family; Not only do small heat-shock-proteins occur in eukaryotes and ...
 125-227 1.65e-30

Hsp20/alpha crystallin family; Not only do small heat-shock-proteins occur in eukaryotes and prokaryotes but they have also now been shown to occur in cyanobacterial phages as well as their bacterial hosts.


:

Pssm-ID: 459629  Cd Length: 100  Bit Score: 108.47  E-value: 1.65e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315932708  125 DIEEHENEIRMRFDMPGLSKEHVKVSVEDHFLIIKGGHETETtntSSNDDGWSTRNASAYHTRLQLPEGIDTDNIKAQLT 204
Cdd:pfam00011   1 DIKEDEDAFEVRLDVPGFKPEELKVKVEDNRLLVKGEHEEEK---EDDHGLRSERSYGSFSRKFTLPENADPDKVKASLK 77

                          90       100
                  ....*....|....*....|...
gi 315932708  205 NGVLYITLPKIKVQRKVMDIEIQ 227
Cdd:pfam00011  78 DGVLTVTVPKLEPEPKERRIQIQ 100
 
Name Accession Description Interval E-value
HSP20 pfam00011
Hsp20/alpha crystallin family; Not only do small heat-shock-proteins occur in eukaryotes and ...
 125-227 1.65e-30

Hsp20/alpha crystallin family; Not only do small heat-shock-proteins occur in eukaryotes and prokaryotes but they have also now been shown to occur in cyanobacterial phages as well as their bacterial hosts.


Pssm-ID: 459629  Cd Length: 100  Bit Score: 108.47  E-value: 1.65e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315932708  125 DIEEHENEIRMRFDMPGLSKEHVKVSVEDHFLIIKGGHETETtntSSNDDGWSTRNASAYHTRLQLPEGIDTDNIKAQLT 204
Cdd:pfam00011   1 DIKEDEDAFEVRLDVPGFKPEELKVKVEDNRLLVKGEHEEEK---EDDHGLRSERSYGSFSRKFTLPENADPDKVKASLK 77

                          90       100
                  ....*....|....*....|...
gi 315932708  205 NGVLYITLPKIKVQRKVMDIEIQ 227
Cdd:pfam00011  78 DGVLTVTVPKLEPEPKERRIQIQ 100
ACD_sHsps-like cd06464
Alpha-crystallin domain (ACD) of alpha-crystallin-type small(s) heat shock proteins (Hsps). ...
 125-214 5.88e-25

Alpha-crystallin domain (ACD) of alpha-crystallin-type small(s) heat shock proteins (Hsps). sHsps are small stress induced proteins with monomeric masses between 12 -43 kDa, whose common feature is the Alpha-crystallin domain (ACD). sHsps are generally active as large oligomers consisting of multiple subunits, and are believed to be ATP-independent chaperones that prevent aggregation and are important in refolding in combination with other Hsps.


Pssm-ID: 107221  Cd Length: 88  Bit Score: 93.77  E-value: 5.88e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315932708 125 DIEEHENEIRMRFDMPGLSKEHVKVSVEDHFLIIKGGHETETTNTssNDDGWSTRNASAYHTRLQLPEGIDTDNIKAQLT 204
Cdd:cd06464    1 DVYETDDAYVVEADLPGFKKEDIKVEVEDGVLTISGEREEEEEEE--ENYLRRERSYGSFSRSFRLPEDVDPDKIKASLE 78

                         90
                 ....*....|
gi 315932708 205 NGVLYITLPK 214
Cdd:cd06464   79 NGVLTITLPK 88
IbpA COG0071
Small heat shock protein IbpA, HSP20 family [Posttranslational modification, protein turnover, ...
 125-227 1.79e-22

Small heat shock protein IbpA, HSP20 family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 439841  Cd Length: 105  Bit Score: 87.90  E-value: 1.79e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315932708 125 DIEEHENEIRMRFDMPGLSKEHVKVSVEDHFLIIKGGHETETTNtssNDDGW--STRNASAYHTRLQLPEGIDTDNIKAQ 202
Cdd:COG0071    3 DIEETDDAYVITADLPGVDKEDIDVTVEGNVLTISGERKEEEEE---EGENYlrRERRYGSFERSFTLPDDVDVDKIEAS 79

                         90       100
                 ....*....|....*....|....*
gi 315932708 203 LTNGVLYITLPKiKVQRKVMDIEIQ 227
Cdd:COG0071   80 YENGVLTITLPK-AEEAKPRKIEIK 103
PRK10743 PRK10743
heat shock chaperone IbpA;
100-215 1.24e-06

heat shock chaperone IbpA;


Pssm-ID: 182691  Cd Length: 137  Bit Score: 46.34  E-value: 1.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315932708 100 DRLFDdavMMRPGWRWSRGEVrAPWDIE-EHENEIRMRFDMPGLSKEHVKVSVEDHFLIIKGGHETETTNTSSNDDGWST 178
Cdd:PRK10743  17 DRLFN---LLENNQSQSNGGY-PPYNVElVDENHYRIAIAVAGFAESELEITAQDNLLVVKGAHADEQKERTYLYQGIAE 92

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 315932708 179 RNasaYHTRLQLPEGIdtdNIK-AQLTNGVLYITLPKI 215
Cdd:PRK10743  93 RN---FERKFQLAENI---HVRgANLVNGLLYIDLERV 124
 
Name Accession Description Interval E-value
HSP20 pfam00011
Hsp20/alpha crystallin family; Not only do small heat-shock-proteins occur in eukaryotes and ...
 125-227 1.65e-30

Hsp20/alpha crystallin family; Not only do small heat-shock-proteins occur in eukaryotes and prokaryotes but they have also now been shown to occur in cyanobacterial phages as well as their bacterial hosts.


Pssm-ID: 459629  Cd Length: 100  Bit Score: 108.47  E-value: 1.65e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315932708  125 DIEEHENEIRMRFDMPGLSKEHVKVSVEDHFLIIKGGHETETtntSSNDDGWSTRNASAYHTRLQLPEGIDTDNIKAQLT 204
Cdd:pfam00011   1 DIKEDEDAFEVRLDVPGFKPEELKVKVEDNRLLVKGEHEEEK---EDDHGLRSERSYGSFSRKFTLPENADPDKVKASLK 77

                          90       100
                  ....*....|....*....|...
gi 315932708  205 NGVLYITLPKIKVQRKVMDIEIQ 227
Cdd:pfam00011  78 DGVLTVTVPKLEPEPKERRIQIQ 100
ACD_sHsps-like cd06464
Alpha-crystallin domain (ACD) of alpha-crystallin-type small(s) heat shock proteins (Hsps). ...
 125-214 5.88e-25

Alpha-crystallin domain (ACD) of alpha-crystallin-type small(s) heat shock proteins (Hsps). sHsps are small stress induced proteins with monomeric masses between 12 -43 kDa, whose common feature is the Alpha-crystallin domain (ACD). sHsps are generally active as large oligomers consisting of multiple subunits, and are believed to be ATP-independent chaperones that prevent aggregation and are important in refolding in combination with other Hsps.


Pssm-ID: 107221  Cd Length: 88  Bit Score: 93.77  E-value: 5.88e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315932708 125 DIEEHENEIRMRFDMPGLSKEHVKVSVEDHFLIIKGGHETETTNTssNDDGWSTRNASAYHTRLQLPEGIDTDNIKAQLT 204
Cdd:cd06464    1 DVYETDDAYVVEADLPGFKKEDIKVEVEDGVLTISGEREEEEEEE--ENYLRRERSYGSFSRSFRLPEDVDPDKIKASLE 78

                         90
                 ....*....|
gi 315932708 205 NGVLYITLPK 214
Cdd:cd06464   79 NGVLTITLPK 88
IbpA COG0071
Small heat shock protein IbpA, HSP20 family [Posttranslational modification, protein turnover, ...
 125-227 1.79e-22

Small heat shock protein IbpA, HSP20 family [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 439841  Cd Length: 105  Bit Score: 87.90  E-value: 1.79e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315932708 125 DIEEHENEIRMRFDMPGLSKEHVKVSVEDHFLIIKGGHETETTNtssNDDGW--STRNASAYHTRLQLPEGIDTDNIKAQ 202
Cdd:COG0071    3 DIEETDDAYVITADLPGVDKEDIDVTVEGNVLTISGERKEEEEE---EGENYlrRERRYGSFERSFTLPDDVDVDKIEAS 79

                         90       100
                 ....*....|....*....|....*
gi 315932708 203 LTNGVLYITLPKiKVQRKVMDIEIQ 227
Cdd:COG0071   80 YENGVLTITLPK-AEEAKPRKIEIK 103
ACD_sHsps_p23-like cd00298
This domain family includes the alpha-crystallin domain (ACD) of alpha-crystallin-type small ...
 126-214 9.11e-20

This domain family includes the alpha-crystallin domain (ACD) of alpha-crystallin-type small heat shock proteins (sHsps) and a similar domain found in p23-like proteins. sHsps are small stress induced proteins with monomeric masses between 12 -43 kDa, whose common feature is this ACD. sHsps are generally active as large oligomers consisting of multiple subunits, and are believed to be ATP-independent chaperones that prevent aggregation and are important in refolding in combination with other Hsps. p23 is a cochaperone of the Hsp90 chaperoning pathway. It binds Hsp90 and participates in the folding of a number of Hsp90 clients including the progesterone receptor. p23 also has a passive chaperoning activity. p23 in addition may act as the cytosolic prostaglandin E2 synthase. Included in this family is the p23-like C-terminal CHORD-SGT1 (CS) domain of suppressor of G2 allele of Skp1 (Sgt1) and the p23-like domains of human butyrate-induced transcript 1 (hB-ind1), NUD (nuclear distribution) C, Melusin, and NAD(P)H cytochrome b5 (NCB5) oxidoreductase (OR).


Pssm-ID: 107219  Cd Length: 80  Bit Score: 79.94  E-value: 9.11e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315932708 126 IEEHENEIRMRFDMPGLSKEHVKVSVEDHFLIIKGGHETETTntssnddgwSTRNASAYHTRLQLPEGIDTDNIKAQLTN 205
Cdd:cd00298    1 WYQTDDEVVVTVDLPGVKKEDIKVEVEDNVLTISGKREEEEE---------RERSYGEFERSFELPEDVDPEKSKASLEN 71


                 ....*....
gi 315932708 206 GVLYITLPK 214
Cdd:cd00298   72 GVLEITLPK 80
ACD_LpsHSP_like cd06471
Group of bacterial proteins containing an alpha crystallin domain (ACD) similar to ...
 125-214 1.77e-13

Group of bacterial proteins containing an alpha crystallin domain (ACD) similar to Lactobacillus plantarum (Lp) small heat shock proteins (sHsp) HSP 18.5, HSP 18.55 and HSP 19.3. sHsps are molecular chaperones that suppress protein aggregation and protect against cell stress, and are generally active as large oligomers consisting of multiple subunits. Transcription of the genes encoding Lp HSP 18.5, 18.55 and 19.3 is regulated by a variety of stresses including heat, cold and ethanol. Early growing L. plantarum cells contain elevated levels of these mRNAs which rapidly fall of as the cells enter stationary phase. Also belonging to this group is Bifidobacterium breve (Bb) HSP20 and Oenococcus oenis (syn. Leuconostoc oenos) (Oo) HSP18. Transcription of the gene encoding BbHSP20 is strongly induced following heat or osmotic shock, and that of the gene encoding OoHSP18 following heat, ethanol or acid shock. OoHSP18 is peripherally associated with the cytoplasmic membrane.


Pssm-ID: 107228  Cd Length: 93  Bit Score: 64.04  E-value: 1.77e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315932708 125 DIEEHENEIRMRFDMPGLSKEHVKVSVEDHFLIIKGGHEtETTNTSSNDDGW--STRNASAYHTRLQLPeGIDTDNIKAQ 202
Cdd:cd06471    4 DIKETDDEYIVEADLPGFKKEDIKLDYKDGYLTISAKRD-ESKDEKDKKGNYirRERYYGSFSRSFYLP-NVDEEEIKAK 81

                         90
                 ....*....|..
gi 315932708 203 LTNGVLYITLPK 214
Cdd:cd06471   82 YENGVLKITLPK 93
ACD_ScHsp26_like cd06472
Alpha crystallin domain (ACD) found in Saccharomyces cerevisiae (Sc) small heat shock protein ...
 138-214 7.61e-13

Alpha crystallin domain (ACD) found in Saccharomyces cerevisiae (Sc) small heat shock protein (Hsp)26 and similar proteins. sHsps are molecular chaperones that suppress protein aggregation and protect against cell stress, and are generally active as large oligomers consisting of multiple subunits. ScHsp26 is temperature-regulated, it switches from an inactive to a chaperone-active form upon elevation in temperature. It associates into large 24-mers storage forms which upon heat shock disassociate into dimers. These dimers initiate the interaction with non-native substrate proteins and re-assemble into large globular assemblies having one monomer of substrate bound per dimer. This group also contains Arabidopsis thaliana (Ath) Hsp15.7, a peroxisomal matrix protein which can complement the morphological phenotype of S. cerevisiae mutants deficient in Hsps26. AthHsp15.7 is minimally expressed under normal conditions and is strongly induced by heat and oxidative stress. Also belonging to this group is wheat HSP16.9 which differs in quaternary structure from the shell-type particles of ScHsp26, it assembles as a dodecameric double disc, with each disc organized as a trimer of dimers.


Pssm-ID: 107229  Cd Length: 92  Bit Score: 62.32  E-value: 7.61e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315932708 138 DMPGLSKEHVKVSVED-HFLIIKGghETETTNTSSNDDgWST--RNASAYHTRLQLPEGIDTDNIKAQLTNGVLYITLPK 214
Cdd:cd06472   16 DVPGVKKEDVKVEVEDgRVLRISG--ERKKEEEKKGDD-WHRveRSSGRFVRRFRLPENADADEVKAFLENGVLTVTVPK 92
metazoan_ACD cd06526
Alpha-crystallin domain (ACD) of metazoan alpha-crystallin-type small(s) heat shock proteins ...
 125-214 7.80e-10

Alpha-crystallin domain (ACD) of metazoan alpha-crystallin-type small(s) heat shock proteins (Hsps). sHsps are small stress induced proteins with monomeric masses between 12 -43 kDa, whose common feature is the Alpha-crystallin domain (ACD). sHsps are generally active as large oligomers consisting of multiple subunits, and are believed to be ATP-independent chaperones that prevent aggregation and are important in refolding in combination with other Hsps.


Pssm-ID: 107247  Cd Length: 83  Bit Score: 53.68  E-value: 7.80e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315932708 125 DIEEHENEIRMRFDMPGLSKEHVKVSVEDHFLIIKGGHETETTntssnDDGWSTRNasaYHTRLQLPEGIDTDNIKAQLT 204
Cdd:cd06526    1 VVNDDDEKFQVTLDVKGFKPEELKVKVSDNKLVVEGKHEERED-----EHGYVSRE---FTRRYQLPEGVDPDSVTSSLS 72

                         90
                 ....*....|.
gi 315932708 205 -NGVLYITLPK 214
Cdd:cd06526   73 sDGVLTIEAPK 83
PRK10743 PRK10743
heat shock chaperone IbpA;
100-215 1.24e-06

heat shock chaperone IbpA;


Pssm-ID: 182691  Cd Length: 137  Bit Score: 46.34  E-value: 1.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315932708 100 DRLFDdavMMRPGWRWSRGEVrAPWDIE-EHENEIRMRFDMPGLSKEHVKVSVEDHFLIIKGGHETETTNTSSNDDGWST 178
Cdd:PRK10743  17 DRLFN---LLENNQSQSNGGY-PPYNVElVDENHYRIAIAVAGFAESELEITAQDNLLVVKGAHADEQKERTYLYQGIAE 92

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 315932708 179 RNasaYHTRLQLPEGIdtdNIK-AQLTNGVLYITLPKI 215
Cdd:PRK10743  93 RN---FERKFQLAENI---HVRgANLVNGLLYIDLERV 124
ACD_IbpA-B_like cd06470
Alpha-crystallin domain (ACD) found in Escherichia coli inclusion body-associated proteins ...
 123-212 2.33e-03

Alpha-crystallin domain (ACD) found in Escherichia coli inclusion body-associated proteins IbpA and IbpB, and similar proteins. IbpA and IbpB are 16 kDa small heat shock proteins (sHsps). sHsps are molecular chaperones that suppress protein aggregation and protect against cell stress, and are generally active as large oligomers consisting of multiple subunits. IbpA and IbpB are produced during high-level production of various heterologous proteins, specifically human prorenin, renin and bovine insulin-like growth factor 2 (bIGF-2), and are strongly associated with inclusion bodies containing these heterologous proteins. IbpA and IbpB work as an integrated system to stabilize thermally aggregated proteins in a disaggregation competent state. The chaperone activity of IbpB is also significantly elevated as the temperature increases from normal to heat shock. The high temperature results in the disassociation of 2-3-MDa IbpB oligomers into smaller approximately 600-kDa structures. This elevated activity seen under heat shock conditions is retained for an extended period of time after the temperature is returned to normal. IbpA also forms multimers.


Pssm-ID: 107227  Cd Length: 90  Bit Score: 35.97  E-value: 2.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315932708 123 PWDIEEH-ENEIRMRFDMPGLSKEHVKVSVEDHFLIIKGGHETETTNTSSN-DDGWSTRNASayhTRLQLPEGIDTDNik 200
Cdd:cd06470    2 PYNIEKTgENNYRITLAVAGFSEDDLEIEVENNQLTVTGKKADEENEEREYlHRGIAKRAFE---RSFNLADHVKVKG-- 76

                         90
                 ....*....|..
gi 315932708 201 AQLTNGVLYITL 212
Cdd:cd06470   77 AELENGLLTIDL 88
ACD_alphaA-crystallin_HspB4 cd06497
Alpha-crystallin domain found in the small heat shock protein (sHsp) alphaA-crystallin (HspB4, ...
 125-214 2.90e-03

Alpha-crystallin domain found in the small heat shock protein (sHsp) alphaA-crystallin (HspB4, 20kDa). sHsps are molecular chaperones that suppress protein aggregation and protect against cell stress, and are generally active as large oligomers consisting of multiple subunits. Alpha crystallin, an abundant protein in the mammalian lens, is a large (700 kDa) heteropolymer composed of HspB4 and HspB5, generally in a molar ratio of HspB4:HspB5 of 3:1. Only trace amounts of HspB4 are found in tissues other than the lens. HspB5 does not belong to this group. Mutations inHspB4 have been associated with Autosomal Dominant Congenital Cataract (ADCC). The chaperone-like functions of HspB4 are considered important for maintaining lens transparency and preventing cataract.


Pssm-ID: 107245  Cd Length: 86  Bit Score: 35.74  E-value: 2.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315932708 125 DIEEHENEIRMRFDMPGLSKEHVKVSVEDHFLIIKGGHetettNTSSNDDGWSTRNasaYHTRLQLPEGIDTDNIKAQLT 204
Cdd:cd06497    4 EVRSDRDKFTIYLDVKHFSPEDLTVKVLDDYVEIHGKH-----SERQDDHGYISRE---FHRRYRLPSNVDQSAITCSLS 75

                         90
                 ....*....|.
gi 315932708 205 -NGVLYITLPK 214
Cdd:cd06497   76 aDGMLTFSGPK 86
ACD_HspB4-5-6 cd06478
Alpha-crystallin domain found in alphaA-crystallin (HspB4), alphaB-crystallin (HspB5), and the ...
 138-214 3.44e-03

Alpha-crystallin domain found in alphaA-crystallin (HspB4), alphaB-crystallin (HspB5), and the small heat shock protein (sHsp) HspB6, also known as Hsp20. sHsps are molecular chaperones that suppress protein aggregation and protect against cell stress, and are generally active as large oligomers consisting of multiple subunits. Alpha crystallin, an abundant protein in the mammalian lens, is a large (700 kDa) heteropolymer composed of HspB4 and HspB5, generally in a molar ratio of HspB4:HspB5 of 3:1. Only trace amounts of HspB4 are found in tissues other than the lens. HspB5 on the other hand is also expressed constitutively in other tissues including brain, heart, and type I and type IIa skeletal muscle fibers, and in several cancers including gliomas, renal cell carcinomas, basal-like and metaplastic breast carcinomas, and head and neck cancer. HspB5's functions include effects on the apoptotic pathway and on metastasis. Phosphorylation of HspB5 reduces its oligomerization and anti-apoptotic activities. HspB5 is protective in demyelinating disease such as multiple sclerosis (MS), being a negative regulator of inflammation. In early active MS lesions it is the most abundant gene transcript and an autoantigen, the immune response against it would disrupt its function and worsen inflammation and demyelination. Given as therapy for ongoing demyelinating disease it may counteract this effect. It is an autoantigen in the pathogenesis of various other inflammatory disorders including Lens-associated uveitis (LAU), and Behcet's disease. Mutations in HspB5 have been associated with diseases including dominant cataract and desmin-related myopathy. Mutations in HspB4 have been associated with Autosomal Dominant Congenital Cataract (ADCC). HspB6 (Hsp20) is ubiquitous and is involved in diverse functions including regulation of glucose transport and contraction of smooth muscle, in platelet aggregation, in cardioprotection, and in the prevention of apoptosis. It interacts with the universal scaffolding and adaptor protein 14-3-3, and also with the proapoptotic protein Bax.


Pssm-ID: 107233  Cd Length: 83  Bit Score: 35.50  E-value: 3.44e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 315932708 138 DMPGLSKEHVKVSVEDHFLIIKGGHETEttntsSNDDGWSTRNasaYHTRLQLPEGIDTDNIKAQLT-NGVLYITLPK 214
Cdd:cd06478   14 DVKHFSPEELSVKVLGDFVEIHGKHEER-----QDEHGFISRE---FHRRYRLPPGVDPAAITSSLSaDGVLTISGPR 83
 
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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