ID A0A1X7S5L6_ZYMTR Unreviewed; 183 AA.
AC A0A1X7S5L6;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=U6 snRNA-associated Sm-like protein LSm4 {ECO:0000256|RuleBase:RU365049};
GN Name=LSM4 {ECO:0000256|RuleBase:RU365049};
GN ORFNames=ZT3D7_G9866 {ECO:0000313|EMBL:SMQ54711.1};
OS Zymoseptoria tritici ST99CH_3D7.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX NCBI_TaxID=1276538 {ECO:0000313|EMBL:SMQ54711.1, ECO:0000313|Proteomes:UP000215127};
RN [1] {ECO:0000313|EMBL:SMQ54711.1, ECO:0000313|Proteomes:UP000215127}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Binds specifically to the 3'-terminal U-tract of U6 snRNA.
CC {ECO:0000256|RuleBase:RU365049}.
CC -!- SUBUNIT: LSm subunits form a heteromer with a doughnut shape.
CC {ECO:0000256|RuleBase:RU365049}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|RuleBase:RU365049}.
CC -!- SIMILARITY: Belongs to the snRNP Sm proteins family.
CC {ECO:0000256|ARBA:ARBA00006850, ECO:0000256|RuleBase:RU365049}.
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DR EMBL; LT853701; SMQ54711.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X7S5L6; -.
DR STRING; 1276538.A0A1X7S5L6; -.
DR Proteomes; UP000215127; Chromosome 10.
DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-UniRule.
DR GO; GO:0097525; C:spliceosomal snRNP complex; IEA:UniProt.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IEA:InterPro.
DR GO; GO:0000956; P:nuclear-transcribed mRNA catabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd01723; LSm4; 1.
DR Gene3D; 2.30.30.100; -; 1.
DR InterPro; IPR034101; Lsm4.
DR InterPro; IPR027141; LSm4/Sm_D1/D3.
DR InterPro; IPR010920; LSM_dom_sf.
DR InterPro; IPR047575; Sm.
DR InterPro; IPR001163; Sm_dom_euk/arc.
DR PANTHER; PTHR23338; SMALL NUCLEAR RIBONUCLEOPROTEIN SM; 1.
DR PANTHER; PTHR23338:SF16; U6 SNRNA-ASSOCIATED SM-LIKE PROTEIN LSM4; 1.
DR Pfam; PF01423; LSM; 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|RuleBase:RU365049};
KW mRNA splicing {ECO:0000256|ARBA:ARBA00023187,
KW ECO:0000256|RuleBase:RU365049};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU365049};
KW Reference proteome {ECO:0000313|Proteomes:UP000215127};
KW Ribonucleoprotein {ECO:0000256|RuleBase:RU365049};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|RuleBase:RU365049};
KW Spliceosome {ECO:0000256|RuleBase:RU365049}.
FT DOMAIN 2..75
FT /note="Sm"
FT /evidence="ECO:0000259|PROSITE:PS52002"
FT REGION 81..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..113
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 183 AA; 20519 MW; 6545745FE77A0AD7 CRC64;
MLPLGLLTAA QGHPMLVELK TGETLNGHLV SCDTYMNIML KEVVQTSPDG DKFFRLPECY
VRGNNIKYLR VPDEVVDVVK DQQAAQQSQR GGRGGGEGVG EVAEEHGDTQ RRMDACMPRP
NVSKSARRPM PAQPSVTNAR TDRELMPRDW IWLRSAGGLW QNIQRGQTES THLAQKYTHT
FEM
//
