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Database: UniProt
Entry: Q4V6F2_DROME
LinkDB: Q4V6F2_DROME
Original site: Q4V6F2_DROME 
ID   Q4V6F2_DROME            Unreviewed;        81 AA.
AC   Q4V6F2;
DT   05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2005, sequence version 1.
DT   24-JAN-2024, entry version 57.
DE   RecName: Full=U6 snRNA-associated Sm-like protein LSm1 {ECO:0000256|RuleBase:RU365047};
DE   Flags: Fragment;
GN   Name=CG4279 {ECO:0000313|EMBL:AAY54770.1};
GN   Synonyms=LSM1 {ECO:0000256|RuleBase:RU365047};
OS   Drosophila melanogaster (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7227 {ECO:0000313|EMBL:AAY54770.1};
RN   [1] {ECO:0000313|EMBL:AAY54770.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Stapleton M., Carlson J., Chavez C., Frise E., George R., Pacleb J.,
RA   Park S., Wan K., Yu C., Celniker S.;
RL   Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Probably involved with other LSm subunits in the general
CC       process of degradation of mRNAs. {ECO:0000256|RuleBase:RU365047}.
CC   -!- SUBUNIT: LSm subunits form a heteromer with a donut shape.
CC       {ECO:0000256|RuleBase:RU365047}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU365047}.
CC       Cytoplasm, P-body {ECO:0000256|RuleBase:RU365047}.
CC   -!- SIMILARITY: Belongs to the snRNP Sm proteins family.
CC       {ECO:0000256|RuleBase:RU365047}.
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DR   EMBL; BT022354; AAY54770.1; -; mRNA.
DR   AlphaFoldDB; Q4V6F2; -.
DR   PeptideAtlas; Q4V6F2; -.
DR   VEuPathDB; VectorBase:FBgn0261067; -.
DR   ExpressionAtlas; Q4V6F2; baseline and differential.
DR   GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell.
DR   GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
DR   GO; GO:0000339; F:RNA cap binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-UniRule.
DR   GO; GO:0000956; P:nuclear-transcribed mRNA catabolic process; IEA:InterPro.
DR   CDD; cd01728; LSm1; 1.
DR   Gene3D; 2.30.30.100; -; 1.
DR   InterPro; IPR034104; Lsm1.
DR   InterPro; IPR010920; LSM_dom_sf.
DR   InterPro; IPR044642; PTHR15588.
DR   InterPro; IPR001163; Sm_dom_euk/arc.
DR   PANTHER; PTHR15588; LSM1; 1.
DR   PANTHER; PTHR15588:SF8; U6 SNRNA-ASSOCIATED SM-LIKE PROTEIN LSM1; 1.
DR   Pfam; PF01423; LSM; 1.
DR   SMART; SM00651; Sm; 1.
DR   SUPFAM; SSF50182; Sm-like ribonucleoproteins; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm {ECO:0000256|RuleBase:RU365047};
KW   mRNA processing {ECO:0000256|RuleBase:RU365047};
KW   Ribonucleoprotein {ECO:0000256|RuleBase:RU365047};
KW   RNA-binding {ECO:0000256|RuleBase:RU365047}.
FT   DOMAIN          13..68
FT                   /note="Sm"
FT                   /evidence="ECO:0000259|SMART:SM00651"
FT   REGION          59..81
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        67..81
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AAY54770.1"
SQ   SEQUENCE   81 AA;  9138 MW;  68CA163F17702C4B CRC64;
     GTRDDLNPLA GTAHLLEEVD KKLMVLLRDG RTLIGYLRSV DQFANLVLQR TIERIHVGRR
     HSSRSLHHSR GECGATGRNR P
//
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