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Database: UniProt
Entry: A0A179G4F1_METCM
LinkDB: A0A179G4F1_METCM
Original site: A0A179G4F1_METCM 
ID   A0A179G4F1_METCM        Unreviewed;        98 AA.
AC   A0A179G4F1;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=U6 snRNA-associated Sm-like protein LSm2 {ECO:0000256|PIRNR:PIRNR016394};
GN   ORFNames=VFPPC_15089 {ECO:0000313|EMBL:OAQ72241.1};
OS   Pochonia chlamydosporia 170.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Pochonia.
OX   NCBI_TaxID=1380566 {ECO:0000313|EMBL:OAQ72241.1, ECO:0000313|Proteomes:UP000078397};
RN   [1] {ECO:0000313|EMBL:OAQ72241.1, ECO:0000313|Proteomes:UP000078397}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=170 {ECO:0000313|EMBL:OAQ72241.1};
RX   PubMed=27416025;
RA   Wang G., Liu Z., Lin R., Li E., Mao Z., Ling J., Yang Y., Yin W.B., Xie B.;
RT   "Biosynthesis of antibiotic leucinostatins in bio-control fungus
RT   Purpureocillium lilacinum and their inhibition on phytophthora revealed by
RT   genome mining.";
RL   PLoS Pathog. 12:E1005685-E1005685(2016).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OAQ72241.1}.
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DR   EMBL; LSBJ02000001; OAQ72241.1; -; Genomic_DNA.
DR   RefSeq; XP_018148324.1; XM_018292842.1.
DR   AlphaFoldDB; A0A179G4F1; -.
DR   STRING; 1380566.A0A179G4F1; -.
DR   GeneID; 28856836; -.
DR   KEGG; pchm:VFPPC_15089; -.
DR   OrthoDB; 101568at2759; -.
DR   Proteomes; UP000078397; Chromosome 1.
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:UP000078397};
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   98 AA;  11148 MW;  6B118ABD08696402 CRC64;
     MLFFSFFKTL IDHEVTVELK NDIQLKGTLK SVDQYLNIKL DDISVVEELK YPHLSSVKNV
     FIRGSVVRYV HLPAGSVDTQ LLEDATRREA AAQQAKAR
//
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