SIGNALING PROTEIN / SAM / STERILE ALPHA MOTIF / HELICAL / PROTEIN-PROTEIN INTERACTION DOMAIN / GROWTH ARREST
Function / homology
Function and homology information
osmosensory signaling pathway via Sho1 osmosensor / signal transduction involved in filamentous growth / SAM domain binding / pheromone-dependent signal transduction involved in conjugation with cellular fusion / protein kinase regulator activity / p38MAPK cascade / regulation of cell cycle / cell cycle / cytoplasm Similarity search - Function
Mass: 9897.152 Da / Num. of mol.: 1 / Fragment: SAM DOMAIN, RESIDUES 27-108 Source method: isolated from a genetically manipulated source Source: (gene. exp.) SACCHAROMYCES CEREVISIAE (brewer's yeast) Plasmid: PGEX-2T / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21 / References: UniProt: P25344
Compound details
INVOLVED IN GROWTH ARREST DURING CONJUGATION. MAY INTERACT WITH THE G PROTEIN ALPHA SUBUNIT.
Sequence details
THE FIRST THREE RESIDUES IN THE DBREF RECORDS SHOWN ORIGINATE FROM THE EXPRESSION SYSTEM, AND ARE ...THE FIRST THREE RESIDUES IN THE DBREF RECORDS SHOWN ORIGINATE FROM THE EXPRESSION SYSTEM, AND ARE THEREFORE, MAPPED TO THEMSELVES RATHER THAN A SWISSPROT DATABASE CROSS-REFERENCE.
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Experimental details
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Experiment
Experiment
Method: SOLUTION NMR
NMR experiment
Conditions-ID
Experiment-ID
Solution-ID
Type
1
1
1
HSQC
1
2
1
15N-SEPARATED NOESY
1
3
1
HNCA
1
4
1
HN(CO)CA
1
5
1
CBCA(CO)NH
1
6
1
HN(CA)CB
1
7
1
H(CC)(CO)NH
1
8
1
(H)CC(CO)NH
1
9
1
(H)CCH-TOCSY
1
10
1
13C-SEPARATED NOESY
NMR details
Text: THE STRUCURE WAS DETERMINED USING 15N-LABELLED AND 13C,15N-LABELLED PROTEINS
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