ID V2X5A0_MONRO Unreviewed; 175 AA.
AC V2X5A0;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE RecName: Full=Sm protein B {ECO:0000256|ARBA:ARBA00041355};
GN ORFNames=Moror_10875 {ECO:0000313|EMBL:ESK87961.1};
OS Moniliophthora roreri (strain MCA 2997) (Cocoa frosty pod rot fungus)
OS (Crinipellis roreri).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX NCBI_TaxID=1381753 {ECO:0000313|EMBL:ESK87961.1, ECO:0000313|Proteomes:UP000017559};
RN [1] {ECO:0000313|EMBL:ESK87961.1, ECO:0000313|Proteomes:UP000017559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 2997 {ECO:0000313|EMBL:ESK87961.1,
RC ECO:0000313|Proteomes:UP000017559};
RX PubMed=24571091; DOI=10.1186/1471-2164-15-164;
RA Meinhardt L.W., Costa G.G.L., Thomazella D.P.T., Teixeira P.J.P.L.,
RA Carazzolle M.F., Schuster S.C., Carlson J.E., Guiltinan M.J.,
RA Mieczkowski P., Farmer A., Ramaraj T., Crozier J., Davis R.E., Shao J.,
RA Melnick R.L., Pereira G.A.G., Bailey B.A.;
RT "Genome and secretome analysis of the hemibiotrophic fungal pathogen,
RT Moniliophthora roreri, which causes frosty pod rot disease of cacao:
RT mechanisms of the biotrophic and necrotrophic phases.";
RL BMC Genomics 15:164-164(2014).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the snRNP SmB/SmN family.
CC {ECO:0000256|ARBA:ARBA00009123}.
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:ESK87961.1}.
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DR EMBL; AWSO01000718; ESK87961.1; -; Genomic_DNA.
DR RefSeq; XP_007852741.1; XM_007854550.1.
DR AlphaFoldDB; V2X5A0; -.
DR STRING; 1381753.V2X5A0; -.
DR KEGG; mrr:Moror_10875; -.
DR HOGENOM; CLU_076902_1_1_1; -.
DR OrthoDB; 5475294at2759; -.
DR Proteomes; UP000017559; Unassembled WGS sequence.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR CDD; cd01717; Sm_B; 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 PANTHER; PTHR10701:SF0; SMALL NUCLEAR RIBONUCLEOPROTEIN-ASSOCIATED PROTEIN B; 1.
DR PANTHER; PTHR10701; SMALL NUCLEAR RIBONUCLEOPROTEIN-ASSOCIATED PROTEIN B AND N; 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 Reference proteome {ECO:0000313|Proteomes:UP000017559};
KW Ribonucleoprotein {ECO:0000313|EMBL:ESK87961.1}.
FT DOMAIN 6..93
FT /note="Sm"
FT /evidence="ECO:0000259|PROSITE:PS52002"
FT REGION 122..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..175
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 175 AA; 18542 MW; C5E15809415BD378 CRC64;
MPPPKSKGGK MLGLINWRLK VTINDGRSLV GQMLAFDRHM NLVLADCEEF RRVRPKKKPG
DESTPPEQEM KRTLGLVILR GETVVSLSVE GPPPVVDDDK KNVLPIGPGR GMPAGRGMGM
MPPGGVPPAG QPGMPFPPGM PGPPPGFRPP GFPPGMPFPP PPGFSGPPPG FQPPQ
//