ID H2ASB8_KAZAF Unreviewed; 95 AA.
AC H2ASB8;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=U6 snRNA-associated Sm-like protein LSm2 {ECO:0000256|PIRNR:PIRNR016394};
GN Name=KAFR0C02750 {ECO:0000313|EMBL:CCF57268.1};
GN ORFNames=KAFR_0C02750 {ECO:0000313|EMBL:CCF57268.1};
OS Kazachstania africana (strain ATCC 22294 / BCRC 22015 / CBS 2517 / CECT
OS 1963 / NBRC 1671 / NRRL Y-8276) (Yeast) (Kluyveromyces africanus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kazachstania.
OX NCBI_TaxID=1071382 {ECO:0000313|EMBL:CCF57268.1, ECO:0000313|Proteomes:UP000005220};
RN [1] {ECO:0000313|EMBL:CCF57268.1, ECO:0000313|Proteomes:UP000005220}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 22294 / BCRC 22015 / CBS 2517 / CECT 1963 / NBRC 1671 /
RC NRRL Y-8276 {ECO:0000313|Proteomes:UP000005220};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
CC -!- FUNCTION: Binds specifically to the 3'-terminal U-tract of U6 snRNA.
CC {ECO:0000256|PIRNR:PIRNR016394}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the snRNP Sm proteins family.
CC {ECO:0000256|ARBA:ARBA00006850, ECO:0000256|PIRNR:PIRNR016394}.
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DR EMBL; HE650823; CCF57268.1; -; Genomic_DNA.
DR RefSeq; XP_003956403.1; XM_003956354.1.
DR AlphaFoldDB; H2ASB8; -.
DR STRING; 1071382.H2ASB8; -.
DR GeneID; 13885187; -.
DR KEGG; kaf:KAFR_0C02750; -.
DR eggNOG; KOG3448; Eukaryota.
DR HOGENOM; CLU_130474_3_0_1; -.
DR InParanoid; H2ASB8; -.
DR OrthoDB; 101568at2759; -.
DR Proteomes; UP000005220; Chromosome 3.
DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IEA:UniProtKB-UniRule.
DR CDD; cd01725; LSm2; 1.
DR Gene3D; 2.30.30.100; -; 1.
DR InterPro; IPR010920; LSM_dom_sf.
DR InterPro; IPR047575; Sm.
DR InterPro; IPR001163; Sm_dom_euk/arc.
DR InterPro; IPR016654; U6_snRNA_Lsm2.
DR PANTHER; PTHR13829; SNRNP CORE PROTEIN FAMILY MEMBER; 1.
DR PANTHER; PTHR13829:SF2; U6 SNRNA-ASSOCIATED SM-LIKE PROTEIN LSM2; 1.
DR Pfam; PF01423; LSM; 1.
DR PIRSF; PIRSF016394; U6_snRNA_Lsm2; 1.
DR SMART; SM00651; Sm; 1.
DR SUPFAM; SSF50182; Sm-like ribonucleoproteins; 1.
DR PROSITE; PS52002; SM; 1.
PE 3: Inferred from homology;
KW mRNA processing {ECO:0000256|ARBA:ARBA00022664,
KW ECO:0000256|PIRNR:PIRNR016394};
KW mRNA splicing {ECO:0000256|ARBA:ARBA00023187,
KW ECO:0000256|PIRNR:PIRNR016394};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR016394};
KW Reference proteome {ECO:0000313|Proteomes:UP000005220};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274,
KW ECO:0000256|PIRNR:PIRNR016394};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PIRNR:PIRNR016394};
KW Spliceosome {ECO:0000256|ARBA:ARBA00022728, ECO:0000256|PIRNR:PIRNR016394}.
FT DOMAIN 2..76
FT /note="Sm"
FT /evidence="ECO:0000259|PROSITE:PS52002"
SQ SEQUENCE 95 AA; 11152 MW; 23227CE430878E8E CRC64;
MLFFSFFKTL VDQEVVVQLK NDIEIKGTLQ SVDQFLNLKL DNISCTDETK YPHLGSVRNM
FIRGSTVRYV YLNKNMVDKN LLQDATRREI MSEKK
//
