ID   B4KQL6_DROMO            Unreviewed;        79 AA.
AC   B4KQL6;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   02-SEP-2026, entry version 80.
DE   RecName: Full=U6 snRNA-associated Sm-like protein LSm6 {ECO:0000256|ARBA:ARBA00014768};
GN   Name=Dmoj\GI19714 {ECO:0000313|EMBL:EDW08185.1};
GN   ORFNames=Dmoj_GI19714 {ECO:0000313|EMBL:EDW08185.1};
OS   Drosophila mojavensis (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Altocrustacea; Allotriocarida;
OC   Hexapoda; Insecta; Pterygota; Neoptera; Eumetabola; Endopterygota;
OC   Aparaglossata; Panorpida; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila.
OX   NCBI_TaxID=7230 {ECO:0000313|EMBL:EDW08185.1, ECO:0000313|Proteomes:UP000009192};
RN   [1] {ECO:0000313|EMBL:EDW08185.1, ECO:0000313|Proteomes:UP000009192}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 15081-1352.22 {ECO:0000313|Proteomes:UP000009192};
RX   PubMed=17994087; DOI=10.1038/nature06341;
RG   Drosophila 12 Genomes Consortium;
RA   Clark A.G., Eisen M.B., Smith D.R., Bergman C.M., Oliver B., Markow T.A.,
RA   Kaufman T.C., Kellis M., Gelbart W., Iyer V.N., Pollard D.A., Sackton T.B.,
RA   Larracuente A.M., Singh N.D., Abad J.P., Abt D.N., Adryan B., Aguade M.,
RA   Akashi H., Anderson W.W., Aquadro C.F., Ardell D.H., Arguello R.,
RA   Artieri C.G., Barbash D.A., Barker D., Barsanti P., Batterham P.,
RA   Batzoglou S., Begun D., Bhutkar A., Blanco E., Bosak S.A., Bradley R.K.,
RA   Brand A.D., Brent M.R., Brooks A.N., Brown R.H., Butlin R.K., Caggese C.,
RA   Calvi B.R., Bernardo de Carvalho A., Caspi A., Castrezana S.,
RA   Celniker S.E., Chang J.L., Chapple C., Chatterji S., Chinwalla A.,
RA   Civetta A., Clifton S.W., Comeron J.M., Costello J.C., Coyne J.A., Daub J.,
RA   David R.G., Delcher A.L., Delehaunty K., Do C.B., Ebling H., Edwards K.,
RA   Eickbush T., Evans J.D., Filipski A., Findeiss S., Freyhult E., Fulton L.,
RA   Fulton R., Garcia A.C., Gardiner A., Garfield D.A., Garvin B.E., Gibson G.,
RA   Gilbert D., Gnerre S., Godfrey J., Good R., Gotea V., Gravely B.,
RA   Greenberg A.J., Griffiths-Jones S., Gross S., Guigo R., Gustafson E.A.,
RA   Haerty W., Hahn M.W., Halligan D.L., Halpern A.L., Halter G.M., Han M.V.,
RA   Heger A., Hillier L., Hinrichs A.S., Holmes I., Hoskins R.A., Hubisz M.J.,
RA   Hultmark D., Huntley M.A., Jaffe D.B., Jagadeeshan S., Jeck W.R.,
RA   Johnson J., Jones C.D., Jordan W.C., Karpen G.H., Kataoka E.,
RA   Keightley P.D., Kheradpour P., Kirkness E.F., Koerich L.B., Kristiansen K.,
RA   Kudrna D., Kulathinal R.J., Kumar S., Kwok R., Lander E., Langley C.H.,
RA   Lapoint R., Lazzaro B.P., Lee S.J., Levesque L., Li R., Lin C.F., Lin M.F.,
RA   Lindblad-Toh K., Llopart A., Long M., Low L., Lozovsky E., Lu J., Luo M.,
RA   Machado C.A., Makalowski W., Marzo M., Matsuda M., Matzkin L.,
RA   McAllister B., McBride C.S., McKernan B., McKernan K., Mendez-Lago M.,
RA   Minx P., Mollenhauer M.U., Montooth K., Mount S.M., Mu X., Myers E.,
RA   Negre B., Newfeld S., Nielsen R., Noor M.A., O'Grady P., Pachter L.,
RA   Papaceit M., Parisi M.J., Parisi M., Parts L., Pedersen J.S., Pesole G.,
RA   Phillippy A.M., Ponting C.P., Pop M., Porcelli D., Powell J.R.,
RA   Prohaska S., Pruitt K., Puig M., Quesneville H., Ram K.R., Rand D.,
RA   Rasmussen M.D., Reed L.K., Reenan R., Reily A., Remington K.A.,
RA   Rieger T.T., Ritchie M.G., Robin C., Rogers Y.H., Rohde C., Rozas J.,
RA   Rubenfield M.J., Ruiz A., Russo S., Salzberg S.L., Sanchez-Gracia A.,
RA   Saranga D.J., Sato H., Schaeffer S.W., Schatz M.C., Schlenke T.,
RA   Schwartz R., Segarra C., Singh R.S., Sirot L., Sirota M., Sisneros N.B.,
RA   Smith C.D., Smith T.F., Spieth J., Stage D.E., Stark A., Stephan W.,
RA   Strausberg R.L., Strempel S., Sturgill D., Sutton G., Sutton G.G., Tao W.,
RA   Teichmann S., Tobari Y.N., Tomimura Y., Tsolas J.M., Valente V.L.,
RA   Venter E., Venter J.C., Vicario S., Vieira F.G., Vilella A.J.,
RA   Villasante A., Walenz B., Wang J., Wasserman M., Watts T., Wilson D.,
RA   Wilson R.K., Wing R.A., Wolfner M.F., Wong A., Wong G.K., Wu C.I., Wu G.,
RA   Yamamoto D., Yang H.P., Yang S.P., Yorke J.A., Yoshida K., Zdobnov E.,
RA   Zhang P., Zhang Y., Zimin A.V., Baldwin J., Abdouelleil A., Abdulkadir J.,
RA   Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., An P.,
RA   Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., Barry A.,
RA   Bayul T., Berlin A., Bessette D., Bloom T., Blye J., Boguslavskiy L.,
RA   Bonnet C., Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S.,
RA   Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., Costello M.,
RA   D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., Dhargay N., Dooley K.,
RA   Dooley E., Doricent M., Dorje P., Dorjee K., Dupes A., Elong R., Falk J.,
RA   Farina A., Faro S., Ferguson D., Fisher S., Foley C.D., Franke A.,
RA   Friedrich D., Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T.,
RA   Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B.,
RA   Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L.,
RA   Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D.,
RA   Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., LeVine R.,
RA   Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y.,
RA   Lubonja R., Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C.,
RA   McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O.,
RA   Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., Mulrain L.,
RA   Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., Nicol R., Norbu C.,
RA   Norbu N., Novod N., O'Neill B., Osman S., Markiewicz E., Oyono O.L.,
RA   Patti C., Phunkhang P., Pierre F., Priest M., Raghuraman S., Rege F.,
RA   Reyes R., Rise C., Rogov P., Ross K., Ryan E., Settipalli S., Shea T.,
RA   Sherpa N., Shi L., Shih D., Sparrow T., Spaulding J., Stalker J.,
RA   Stange-Thomann N., Stavropoulos S., Stone C., Strader C., Tesfaye S.,
RA   Thomson T., Thoulutsang Y., Thoulutsang D., Topham K., Topping I.,
RA   Tsamla T., Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M.,
RA   Wilkinson J., Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D.,
RA   Zimmer A., Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J.,
RA   Chin C., Gnerre S., Grabherr M., Kleber M., Mauceli E., MacCallum I.;
RT   "Evolution of genes and genomes on the Drosophila phylogeny.";
RL   Nature 450:203-218(2007).
CC   -!- FUNCTION: Plays a role in pre-mRNA splicing as a core component of the
CC       spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins
CC       (snRNPs), the building blocks of the spliceosome.
CC       {ECO:0000256|PIRNR:PIRNR006609}.
CC   -!- FUNCTION: Plays a role in pre-mRNA splicing as component of the U4/U6-
CC       U5 tri-snRNP complex that is involved in spliceosome assembly, and as
CC       component of the precatalytic spliceosome (spliceosome B complex). The
CC       heptameric LSM2-8 complex binds specifically to the 3'-terminal U-tract
CC       of U6 snRNA. Component of LSm protein complexes, which are involved in
CC       RNA processing and may function in a chaperone-like manner,
CC       facilitating the efficient association of RNA processing factors with
CC       their substrates. Component of the cytoplasmic LSM1-LSM7 complex, which
CC       is thought to be involved in mRNA degradation by activating the
CC       decapping step in the 5'-to-3' mRNA decay pathway.
CC       {ECO:0000256|ARBA:ARBA00054795}.
CC   -!- SUBUNIT: Component of the precatalytic spliceosome (spliceosome B
CC       complex). Component of the U4/U6-U5 tri-snRNP complex, a building block
CC       of the precatalytic spliceosome (spliceosome B complex). The U4/U6-U5
CC       tri-snRNP complex is composed of the U4, U6 and U5 snRNAs and at least
CC       PRPF3, PRPF4, PRPF6, PRPF8, PRPF31, SNRNP200, TXNL4A, SNRNP40, SNRPB,
CC       SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF, SNRPG, DDX23, CD2BP2, PPIH,
CC       SNU13, EFTUD2, SART1 and USP39, plus LSM2, LSM3, LSM4, LSM5, LSM6, LSM7
CC       and LSM8. LSM2, LSM3, LSM4, LSM5, LSM6, LSM7 and LSM8 form a
CC       heptameric, ring-shaped subcomplex (the LSM2-8 complex) that is part of
CC       the U4/U6-U5 tri-snRNP complex and the precatalytic spliceosome.
CC       Component of the heptameric LSM1-LSM7 complex, which consists of LSM1,
CC       LSM2, LSM3, LSM4, LSM5, LSM6 and LSM7. {ECO:0000256|ARBA:ARBA00065816}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC       Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR006609}.
CC   -!- SIMILARITY: Belongs to the snRNP Sm proteins family. SmF/LSm6
CC       subfamily. {ECO:0000256|ARBA:ARBA00007927,
CC       ECO:0000256|PIRNR:PIRNR006609}.
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DR   EMBL; CH933808; EDW08185.1; -; Genomic_DNA.
DR   AlphaFoldDB; B4KQL6; -.
DR   FunCoup; B4KQL6; 1753.
DR   KEGG; dmo:Dmoj_GI19714; -.
DR   eggNOG; KOG1783; Eukaryota.
DR   HOGENOM; CLU_076902_7_4_1; -.
DR   InParanoid; B4KQL6; -.
DR   OMA; EQTVEYV; -.
DR   OrthoDB; 268799at2759; -.
DR   PhylomeDB; B4KQL6; -.
DR   Proteomes; UP000009192; Unassembled WGS sequence.
DR   GO; GO:0120115; C:Lsm2-8 complex; IEA:UniProtKB-ARBA.
DR   GO; GO:0005730; C:nucleolus; IEA:TreeGrafter.
DR   GO; GO:0000932; C:P-body; IEA:TreeGrafter.
DR   GO; GO:0005732; C:sno(s)RNA-containing ribonucleoprotein complex; IEA:TreeGrafter.
DR   GO; GO:0046540; C:U4/U6 x U5 tri-snRNP complex; IEA:TreeGrafter.
DR   GO; GO:0005688; C:U6 snRNP; IEA:TreeGrafter.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0030490; P:maturation of SSU-rRNA; IEA:TreeGrafter.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; IEA:InterPro.
DR   CDD; cd01726; LSm6; 1.
DR   FunFam; 2.30.30.100:FF:000010; U6 snRNA-associated Sm-like protein LSm6; 1.
DR   Gene3D; 2.30.30.100; -; 1.
DR   InterPro; IPR016487; Lsm6/sSmF.
DR   InterPro; IPR010920; LSM_dom_sf.
DR   InterPro; IPR047575; Sm.
DR   InterPro; IPR001163; Sm_dom_euk/arc.
DR   PANTHER; PTHR11021; SMALL NUCLEAR RIBONUCLEOPROTEIN F SNRNP-F; 1.
DR   PANTHER; PTHR11021:SF1; U6 SNRNA-ASSOCIATED SM-LIKE PROTEIN LSM6; 1.
DR   Pfam; PF01423; LSM; 1.
DR   PIRSF; PIRSF006609; snRNP_SmF; 1.
DR   SMART; SM00651; Sm; 1.
DR   SUPFAM; SSF50182; Sm-like ribonucleoproteins; 1.
DR   PROSITE; PS52002; SM; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   mRNA processing {ECO:0000256|ARBA:ARBA00022664,
KW   ECO:0000256|PIRNR:PIRNR006609};
KW   mRNA splicing {ECO:0000256|ARBA:ARBA00023187,
KW   ECO:0000256|PIRNR:PIRNR006609};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR006609};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009192};
KW   Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274,
KW   ECO:0000256|PIRNR:PIRNR006609};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PIRNR:PIRNR006609};
KW   rRNA processing {ECO:0000256|ARBA:ARBA00022552};
KW   Spliceosome {ECO:0000256|ARBA:ARBA00022728, ECO:0000256|PIRNR:PIRNR006609};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694}.
FT   DOMAIN          6..78
FT                   /note="Sm"
FT                   /evidence="ECO:0000259|PROSITE:PS52002"
SQ   SEQUENCE   79 AA;  8977 MW;  0480FB6D33AB9A3B CRC64;
     MSRKEALSQF INQIHGRPVA VKLNNGVDYR GVLACLDGYM NIALDQTEEY VNGQLKNKYG
     DAFIRGNNVL YISTQKRRV
//