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Conserved domains on  [gi|1958665823|ref|XP_038944412|]
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protein Aster-C isoform X3 [Rattus norvegicus]

Protein Classification

GRAM and VASt domain-containing protein( domain architecture ID 10987411)

GRAM and VASt domain-containing protein, with similarity to Saccharomyces cerevisiae membrane-anchored lipid-binding protein YSP2

CATH:  2.30.29.30
Gene Ontology:  GO:0016020
PubMed:  11050430|18201690|24965341
SCOP:  4000903

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
VASt pfam16016
VAD1 Analog of StAR-related lipid transfer domain; The VASt (VAD1 Analog of StAR-related lipid ...
 319-466 4.47e-46

VAD1 Analog of StAR-related lipid transfer domain; The VASt (VAD1 Analog of StAR-related lipid transfer) domain is conserved across eukaryotes and is structurally related to Bet v1-like domains, including START lipid-binding domains. The 190-amino acid VASt domain is predominantly associated with lipid binding domains such as GRAM pfam02893, C2 and PH domains. The VASt domain is likely to have a function in binding large hydrophobic ligands and may be specific for sterol. The predicted structure of the VASt domain is a two-layer sandwich alpha beta fold, also called 'helix grip fold', containing three alpha helices (alpha1 to 3), six beta-sheets (beta1 to 6) and two loops (omega1 and 2) numbered from N to C terminus. Some proteins known to contain a VASt domain are : Plant vascular associated death1 (VAD1), a regulator of programmed cell death (PCD) harboring a GRAM putative lipid-binding domain. Yeast SNF1 Interacting Protein 3 (SIP3), may be involved in sterol transfer between intracellular membranes. Yeast Suicide Protein 1 (YSP1), a mitochondrial protein specifically required for the mitochondrial thread-grain transition, de-energization, and the cell death. May be involved in sterol transfer between intracellular membranes. Yeast Suicide Protein 2 (YSP2), a mitochondrial membrane protein involved in mitochondrial fragmentation and may be involved in sterol transfer between intracellular membranes.It is also found in human GramD1a-c.


:

Pssm-ID: 464975  Cd Length: 147  Bit Score: 160.08  E-value: 4.47e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665823 319 LYINRVFHISAERMFELLFT-SSHFMQRFTNSRNIIDVVSTPWTVESGGDQLRTMTYTIVLSNPLTGKCTAATEKQTLYK 397
Cdd:pfam16016   1 VLLDEVFPISVGKLFELLFGdDSSFLQKFLEERGDTDISVGPWEPDEEGGLTREISYTKPLNGSIGPKQTKCTETQTILL 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958665823 398 ESREAQFYlVDSEVLTHDVPYHDYFYTLNRYCIVRSAKQRCRLRVSTDLKYRKQPWglIKSLIEKNSWS 466
Cdd:pfam16016  81 EHDDLEVY-VVTTTKTPDVPYGDSFSVETRYCITWGSNNSTRLQVSTGVEWTKSSW--LKGKIEKGAID 146
PH-like super family cl17171
Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like ...
 101-162 3.26e-29

Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like and IRS-like PTB domains, the ran-binding domain, the EVH1 domain, a domain in neurobeachin and the third domain of FERM. All of these domains have a PH fold, but lack significant sequence similarity. They are generally involved in targeting to protein to the appropriate cellular location or interacting with a binding partner. This domain family possesses multiple functions including the ability to bind inositol phosphates and to other proteins.


The actual alignment was detected with superfamily member cd13220:

Pssm-ID: 473070  Cd Length: 94  Bit Score: 111.06  E-value: 3.26e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665823 101 DSEKLIADYACALQRDILLQGRLYLSENWLCFYSNIFRWETT--------------------------------FFFTSF 148
Cdd:cd13220     1 EDERLIDDFSCALQRDILLQGRLYISENHLCFYSNIFGWETKlvipfkditsiekkktalifpnaieittkgekYFFTSF 80

                          90
                  ....*....|....
gi 1958665823 149 GARDRSYLSIFRLW 162
Cdd:cd13220    81 LSRDSAYKLLTRVW 94
 
Name Accession Description Interval E-value
VASt pfam16016
VAD1 Analog of StAR-related lipid transfer domain; The VASt (VAD1 Analog of StAR-related lipid ...
 319-466 4.47e-46

VAD1 Analog of StAR-related lipid transfer domain; The VASt (VAD1 Analog of StAR-related lipid transfer) domain is conserved across eukaryotes and is structurally related to Bet v1-like domains, including START lipid-binding domains. The 190-amino acid VASt domain is predominantly associated with lipid binding domains such as GRAM pfam02893, C2 and PH domains. The VASt domain is likely to have a function in binding large hydrophobic ligands and may be specific for sterol. The predicted structure of the VASt domain is a two-layer sandwich alpha beta fold, also called 'helix grip fold', containing three alpha helices (alpha1 to 3), six beta-sheets (beta1 to 6) and two loops (omega1 and 2) numbered from N to C terminus. Some proteins known to contain a VASt domain are : Plant vascular associated death1 (VAD1), a regulator of programmed cell death (PCD) harboring a GRAM putative lipid-binding domain. Yeast SNF1 Interacting Protein 3 (SIP3), may be involved in sterol transfer between intracellular membranes. Yeast Suicide Protein 1 (YSP1), a mitochondrial protein specifically required for the mitochondrial thread-grain transition, de-energization, and the cell death. May be involved in sterol transfer between intracellular membranes. Yeast Suicide Protein 2 (YSP2), a mitochondrial membrane protein involved in mitochondrial fragmentation and may be involved in sterol transfer between intracellular membranes.It is also found in human GramD1a-c.


Pssm-ID: 464975  Cd Length: 147  Bit Score: 160.08  E-value: 4.47e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665823 319 LYINRVFHISAERMFELLFT-SSHFMQRFTNSRNIIDVVSTPWTVESGGDQLRTMTYTIVLSNPLTGKCTAATEKQTLYK 397
Cdd:pfam16016   1 VLLDEVFPISVGKLFELLFGdDSSFLQKFLEERGDTDISVGPWEPDEEGGLTREISYTKPLNGSIGPKQTKCTETQTILL 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958665823 398 ESREAQFYlVDSEVLTHDVPYHDYFYTLNRYCIVRSAKQRCRLRVSTDLKYRKQPWglIKSLIEKNSWS 466
Cdd:pfam16016  81 EHDDLEVY-VVTTTKTPDVPYGDSFSVETRYCITWGSNNSTRLQVSTGVEWTKSSW--LKGKIEKGAID 146
PH-GRAM_GRAMDC cd13220
GRAM domain-containing protein (GRAMDC) Pleckstrin Homology-Glucosyltransferases, Rab-like ...
 101-162 3.26e-29

GRAM domain-containing protein (GRAMDC) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain; The GRAMDC proteins are membrane proteins. Nothing is known about its function. Members include: GRAMDC1A, GRAMDC1B, GRAMDC1C, GRAMDC2, GRAMDC3, GRAMDC4, and GRAMDC-like proteins. All of the members, except for GRAMDC4 are included in this hierarchy. Each contains a single PH-GRAM domain at their N-terminus. The GRAM domain is found in glucosyltransferases, myotubularins and other putative membrane-associated proteins. The GRAM domain is part of a larger motif with a pleckstrin homology (PH) domain fold.


Pssm-ID: 275406  Cd Length: 94  Bit Score: 111.06  E-value: 3.26e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665823 101 DSEKLIADYACALQRDILLQGRLYLSENWLCFYSNIFRWETT--------------------------------FFFTSF 148
Cdd:cd13220     1 EDERLIDDFSCALQRDILLQGRLYISENHLCFYSNIFGWETKlvipfkditsiekkktalifpnaieittkgekYFFTSF 80

                          90
                  ....*....|....
gi 1958665823 149 GARDRSYLSIFRLW 162
Cdd:cd13220    81 LSRDSAYKLLTRVW 94
GRAM smart00568
domain in glucosyltransferases, myotubularins and other putative membrane-associated proteins;
99-145 4.29e-17

domain in glucosyltransferases, myotubularins and other putative membrane-associated proteins;


Pssm-ID: 214725 [Multi-domain]  Cd Length: 60  Bit Score: 75.71  E-value: 4.29e-17
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1958665823   99 LPDSEKLIADYACALQRDILLQGRLYLSENWLCFYSNIFRWETTFFF 145
Cdd:smart00568   2 LPEEEKLIADYSCYLSRTGPVQGRLYISNYRLCFRSNLPGKLTKVVI 48
GRAM pfam02893
GRAM domain; The GRAM domain is found in in glucosyltransferases, myotubularins and other ...
 94-167 6.60e-15

GRAM domain; The GRAM domain is found in in glucosyltransferases, myotubularins and other putative membrane-associated proteins. Note the alignment is lacking the last two beta strands and alpha helix.


Pssm-ID: 397160  Cd Length: 112  Bit Score: 71.24  E-value: 6.60e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665823  94 QQFTHLPDSEKLIADYACALQRD-ILLQGRLYLSENWLCFYSNIFRWETTFF---------------------------- 144
Cdd:pfam02893   4 RKKFKLPPEERLIASYSCYLNRDgGPVQGRLYLTNYRLCFRSLPKGWSTKVViplvdieeieklkgganlfpngiqvetg 83

                          90       100
                  ....*....|....*....|....*....
gi 1958665823 145 ------FTSFGARDRSYLSIFRLWQNVLL 167
Cdd:pfam02893  84 sndkfsFAGFVTRDEAIEFILALLKNAHP 112
 
Name Accession Description Interval E-value
VASt pfam16016
VAD1 Analog of StAR-related lipid transfer domain; The VASt (VAD1 Analog of StAR-related lipid ...
 319-466 4.47e-46

VAD1 Analog of StAR-related lipid transfer domain; The VASt (VAD1 Analog of StAR-related lipid transfer) domain is conserved across eukaryotes and is structurally related to Bet v1-like domains, including START lipid-binding domains. The 190-amino acid VASt domain is predominantly associated with lipid binding domains such as GRAM pfam02893, C2 and PH domains. The VASt domain is likely to have a function in binding large hydrophobic ligands and may be specific for sterol. The predicted structure of the VASt domain is a two-layer sandwich alpha beta fold, also called 'helix grip fold', containing three alpha helices (alpha1 to 3), six beta-sheets (beta1 to 6) and two loops (omega1 and 2) numbered from N to C terminus. Some proteins known to contain a VASt domain are : Plant vascular associated death1 (VAD1), a regulator of programmed cell death (PCD) harboring a GRAM putative lipid-binding domain. Yeast SNF1 Interacting Protein 3 (SIP3), may be involved in sterol transfer between intracellular membranes. Yeast Suicide Protein 1 (YSP1), a mitochondrial protein specifically required for the mitochondrial thread-grain transition, de-energization, and the cell death. May be involved in sterol transfer between intracellular membranes. Yeast Suicide Protein 2 (YSP2), a mitochondrial membrane protein involved in mitochondrial fragmentation and may be involved in sterol transfer between intracellular membranes.It is also found in human GramD1a-c.


Pssm-ID: 464975  Cd Length: 147  Bit Score: 160.08  E-value: 4.47e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665823 319 LYINRVFHISAERMFELLFT-SSHFMQRFTNSRNIIDVVSTPWTVESGGDQLRTMTYTIVLSNPLTGKCTAATEKQTLYK 397
Cdd:pfam16016   1 VLLDEVFPISVGKLFELLFGdDSSFLQKFLEERGDTDISVGPWEPDEEGGLTREISYTKPLNGSIGPKQTKCTETQTILL 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958665823 398 ESREAQFYlVDSEVLTHDVPYHDYFYTLNRYCIVRSAKQRCRLRVSTDLKYRKQPWglIKSLIEKNSWS 466
Cdd:pfam16016  81 EHDDLEVY-VVTTTKTPDVPYGDSFSVETRYCITWGSNNSTRLQVSTGVEWTKSSW--LKGKIEKGAID 146
PH-GRAM_GRAMDC cd13220
GRAM domain-containing protein (GRAMDC) Pleckstrin Homology-Glucosyltransferases, Rab-like ...
 101-162 3.26e-29

GRAM domain-containing protein (GRAMDC) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain; The GRAMDC proteins are membrane proteins. Nothing is known about its function. Members include: GRAMDC1A, GRAMDC1B, GRAMDC1C, GRAMDC2, GRAMDC3, GRAMDC4, and GRAMDC-like proteins. All of the members, except for GRAMDC4 are included in this hierarchy. Each contains a single PH-GRAM domain at their N-terminus. The GRAM domain is found in glucosyltransferases, myotubularins and other putative membrane-associated proteins. The GRAM domain is part of a larger motif with a pleckstrin homology (PH) domain fold.


Pssm-ID: 275406  Cd Length: 94  Bit Score: 111.06  E-value: 3.26e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665823 101 DSEKLIADYACALQRDILLQGRLYLSENWLCFYSNIFRWETT--------------------------------FFFTSF 148
Cdd:cd13220     1 EDERLIDDFSCALQRDILLQGRLYISENHLCFYSNIFGWETKlvipfkditsiekkktalifpnaieittkgekYFFTSF 80

                          90
                  ....*....|....
gi 1958665823 149 GARDRSYLSIFRLW 162
Cdd:cd13220    81 LSRDSAYKLLTRVW 94
GRAM smart00568
domain in glucosyltransferases, myotubularins and other putative membrane-associated proteins;
99-145 4.29e-17

domain in glucosyltransferases, myotubularins and other putative membrane-associated proteins;


Pssm-ID: 214725 [Multi-domain]  Cd Length: 60  Bit Score: 75.71  E-value: 4.29e-17
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1958665823   99 LPDSEKLIADYACALQRDILLQGRLYLSENWLCFYSNIFRWETTFFF 145
Cdd:smart00568   2 LPEEEKLIADYSCYLSRTGPVQGRLYISNYRLCFRSNLPGKLTKVVI 48
GRAM pfam02893
GRAM domain; The GRAM domain is found in in glucosyltransferases, myotubularins and other ...
 94-167 6.60e-15

GRAM domain; The GRAM domain is found in in glucosyltransferases, myotubularins and other putative membrane-associated proteins. Note the alignment is lacking the last two beta strands and alpha helix.


Pssm-ID: 397160  Cd Length: 112  Bit Score: 71.24  E-value: 6.60e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958665823  94 QQFTHLPDSEKLIADYACALQRD-ILLQGRLYLSENWLCFYSNIFRWETTFF---------------------------- 144
Cdd:pfam02893   4 RKKFKLPPEERLIASYSCYLNRDgGPVQGRLYLTNYRLCFRSLPKGWSTKVViplvdieeieklkgganlfpngiqvetg 83

                          90       100
                  ....*....|....*....|....*....
gi 1958665823 145 ------FTSFGARDRSYLSIFRLWQNVLL 167
Cdd:pfam02893  84 sndkfsFAGFVTRDEAIEFILALLKNAHP 112
PH-GRAM_C2-GRAM cd13219
C2 and GRAM domain-containing protein Pleckstrin Homology-Glucosyltransferases, Rab-like ...
 103-145 3.19e-12

C2 and GRAM domain-containing protein Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain; C2GRAM contains two N-terminal C2 domains followed by a single PH-GRAM domain. Since it contains both of these domains it is assumed that this gene cross-links both calcium and phosphoinositide signaling pathways. In general he C2 domain is involved in binding phospholipids in a calcium dependent manner or calcium independent manner. The GRAM domain is found in glucosyltransferases, myotubularins and other putative membrane-associated proteins. The GRAM domain is part of a larger motif with a pleckstrin homology (PH) domain fold.


Pssm-ID: 270039 [Multi-domain]  Cd Length: 111  Bit Score: 63.64  E-value: 3.19e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1958665823 103 EKLIADYACALQRDILLQGRLYLSENWLCFYSNIFRWETTFFF 145
Cdd:cd13219     2 EFLINDFSCALKRKFLYQGRMFLSARHIGFHSNVFGKKTKFVF 44
PH-GRAM2_AGT26 cd13216
Autophagy-related protein 26/Sterol 3-beta-glucosyltransferase Pleckstrin homology (PH) domain, ...
 102-134 3.03e-06

Autophagy-related protein 26/Sterol 3-beta-glucosyltransferase Pleckstrin homology (PH) domain, repeat 2; ATG26 (also called UGT51/UDP-glycosyltransferase 51), a member of the glycosyltransferase 28 family, resulting in the biosynthesis of sterol glucoside. ATG26 in decane metabolism and autophagy. There are 32 known autophagy-related (ATG) proteins, 17 are components of the core autophagic machinery essential for all autophagy-related pathways and 15 are the additional components required only for certain pathways or species. The core autophagic machinery includes 1) the ATG9 cycling system (ATG1, ATG2, ATG9, ATG13, ATG18, and ATG27), 2) the phosphatidylinositol 3-kinase complex (ATG6/VPS30, ATG14, VPS15, and ATG34), and 3) the ubiquitin-like protein system (ATG3, ATG4, ATG5, ATG7, ATG8, ATG10, ATG12, and ATG16). Less is known about how the core machinery is adapted or modulated with additional components to accommodate the nonselective sequestration of bulk cytosol (autophagosome formation) or selective sequestration of specific cargos (Cvt vesicle, pexophagosome, or bacteria-containing autophagosome formation). The pexophagosome-specific additions include the ATG30-ATG11-ATG17 receptor-adaptors complex, the coiled-coil protein ATG25, and the sterol glucosyltransferase ATG26. ATG26 is necessary for the degradation of medium peroxisomes. It contains 2 GRAM domains and a single PH domain. PH domains are only found in eukaryotes. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. PH domains also have diverse functions. They are often involved in targeting proteins to the plasma membrane, but few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 275403  Cd Length: 93  Bit Score: 45.65  E-value: 3.03e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1958665823 102 SEKLIADYACALQRDILLQGRLYLSENWLCFYS 134
Cdd:cd13216     1 TEKLIASYYCYLIRVLPVYGKLYVSNNYLCFRS 33
PH-GRAM cd10570
Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins ...
 103-145 3.46e-04

Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain; Myotubularin-related proteins are a subfamily of protein tyrosine phosphatases (PTPs) that dephosphorylate D3-phosphorylated inositol lipids. Mutations in this family cause the human neuromuscular disorders myotubular myopathy and type 4B Charcot-Marie-Tooth syndrome. 6 of the 13 MTMRs (MTMRs 5, 9-13) contain naturally occurring substitutions of residues required for catalysis by PTP family enzymes. Although these proteins are predicted to be enzymatically inactive, they are thought to function as antagonists of endogenous phosphatase activity or interaction modules. Most MTMRs contain a N-terminal PH-GRAM domain, a Rac-induced recruitment domain (RID) domain, a PTP domain (which may be active or inactive), a SET-interaction domain, and a C-terminal coiled-coil region. In addition some members contain DENN domain N-terminal to the PH-GRAM domain and FYVE, PDZ, and PH domains C-terminal to the coiled-coil region. The GRAM domain, found in myotubularins, glucosyltransferases, and other putative membrane-associated proteins, is part of a larger motif with a pleckstrin homology (PH) domain fold.


Pssm-ID: 275393  Cd Length: 94  Bit Score: 40.06  E-value: 3.46e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1958665823 103 EKLIADYACAL-QRDILLQGRLYLSENWLCFYSNIFRWETTFFF 145
Cdd:cd10570     2 EKLGVRFCCALrPRKLPLEGTLYLSTYRLIFSSKADGDETKLVI 45
PH-GRAM1_TCB1D8_TCB1D9_family cd13217
TCB1D8 and TCB1D9 family Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators ...
 103-142 1.67e-03

TCB1D8 and TCB1D9 family Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain, repeat 1; TBC1D8, TBC1D8B, TBC1D9 and TBC1D9B may act as a GTPase-activating proteins for Rab family protein(s). They all contain an N-terminal PH-GRAM domain and a C-terminal Rab-GTPase-TBC (Tre-2, BUB2p, and Cdc16p) domain. This cd contains the first repeat of the PH-GRAM domain. The GRAM domain is found in glucosyltransferases, myotubularins and other putative membrane-associated proteins. The GRAM domain is part of a larger motif with a pleckstrin homology (PH) domain fold.


Pssm-ID: 275404  Cd Length: 99  Bit Score: 38.19  E-value: 1.67e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1958665823 103 EKLIADYACALQRD-ILLQGRLYLSENWLCFYSNIFRWETT 142
Cdd:cd13217     2 EKLVTYYSCSYWKGrVPRQGWLYLSINHLCFYSFLLGSESK 42
PH-GRAM1_TCB1D9_TCB1D9B cd13351
TBC1 domain family members 9 and 9B (TBC1D9 and TBC1D9B) Pleckstrin ...
 103-141 1.94e-03

TBC1 domain family members 9 and 9B (TBC1D9 and TBC1D9B) Pleckstrin Homology-Glucosyltransferases, Rab-like GTPase activators and Myotubularins (PH-GRAM) domain, repeat 1; TBC1D9 and TCB1D9B may act as a GTPase-activating proteins for Rab family protein(s). TBC1D9 and TCB1D9B contain two N-terminal PH-GRAM domain and a C-terminal Rab-GTPase-TBC (Tre-2, BUB2p, and Cdc16p) domain. This cd contains the first repeat of the PH-GRAM domain. The GRAM domain is found in glucosyltransferases, myotubularins and other putative membrane-associated proteins. The GRAM domain is part of a larger motif with a pleckstrin homology (PH) domain fold.


Pssm-ID: 275420  Cd Length: 99  Bit Score: 38.14  E-value: 1.94e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1958665823 103 EKLIADYACAL-QRDILLQGRLYLSENWLCFYSNIFRWET 141
Cdd:cd13351     2 EKLVNYYSCSYwKGRVPRQGWLYLSVNHLCFYSFLLGKEA 41
 
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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