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VTS1_NEUCR
ID   VTS1_NEUCR              Reviewed;         620 AA.
AC   Q7RZQ3; U9W515;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-FEB-2014, sequence version 3.
DT   25-MAY-2022, entry version 92.
DE   RecName: Full=RNA-binding protein VTS1;
GN   Name=vts1; ORFNames=NCU00311;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
CC   -!- FUNCTION: RNA-binding protein involved in post-transcriptional
CC       regulation through transcript degradation.
CC       {ECO:0000250|UniProtKB:Q08831}.
CC   -!- SUBUNIT: Monomer. Binds to RNA. {ECO:0000250|UniProtKB:Q08831}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:Q08831}. Cytoplasm, P-body
CC       {ECO:0000250|UniProtKB:J9VVN9}.
CC   -!- SIMILARITY: Belongs to the VTS1 family. {ECO:0000305}.
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DR   EMBL; CM002238; ESA43334.1; -; Genomic_DNA.
DR   EMBL; CM002238; ESA43335.1; -; Genomic_DNA.
DR   RefSeq; XP_011393809.1; XM_011395507.1.
DR   RefSeq; XP_011393810.1; XM_011395508.1.
DR   AlphaFoldDB; Q7RZQ3; -.
DR   SMR; Q7RZQ3; -.
DR   STRING; 5141.EFNCRP00000000389; -.
DR   EnsemblFungi; ESA43334; ESA43334; NCU00311.
DR   EnsemblFungi; ESA43335; ESA43335; NCU00311.
DR   GeneID; 3873920; -.
DR   KEGG; ncr:NCU00311; -.
DR   VEuPathDB; FungiDB:NCU00311; -.
DR   HOGENOM; CLU_017632_0_0_1; -.
DR   InParanoid; Q7RZQ3; -.
DR   Proteomes; UP000001805; Chromosome 3, Linkage Group III.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0000932; C:P-body; IBA:GO_Central.
DR   GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0030371; F:translation repressor activity; IBA:GO_Central.
DR   GO; GO:0000289; P:nuclear-transcribed mRNA poly(A) tail shortening; IBA:GO_Central.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   CDD; cd09556; SAM_VTS1_fungal; 1.
DR   Gene3D; 1.10.150.50; -; 1.
DR   InterPro; IPR001660; SAM.
DR   InterPro; IPR013761; SAM/pointed_sf.
DR   InterPro; IPR037635; VTS1_SAM.
DR   Pfam; PF07647; SAM_2; 1.
DR   SMART; SM00454; SAM; 1.
DR   SUPFAM; SSF47769; SSF47769; 1.
DR   PROSITE; PS50105; SAM_DOMAIN; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Nucleotide-binding; Protein transport; Reference proteome;
KW   RNA-binding; Transport.
FT   CHAIN           1..620
FT                   /note="RNA-binding protein VTS1"
FT                   /id="PRO_0000081454"
FT   DOMAIN          553..614
FT                   /note="SAM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          189..211
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          231..317
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          398..423
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          527..555
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..29
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        231..296
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        404..423
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        527..546
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   620 AA;  66842 MW;  A642BC5C1E3670ED CRC64;
     MLNMSNIMSN RNSTPEASNV SSLRPPSSRA IGSNHGLRAS ADVAALTGAQ AAASRIRPSS
     DFYGQPQSGQ VQGNAELDPQ DKLAQQWIAD IDQYETTLEE MAAATLDQDF KDELSAIEQW
     FRVLSEAERT AALYALLQQT TQVQIRFFIQ VLQQMGKNHP MSGVLSPANF DKDPMSSRLS
     DAMGKLEVGS ARNSLARPSG GANKRHSGLD QTTINTMFPD AVAAIATEKA KFTQQTGNPP
     PSNRNSLVDN RNSLAAPTVS GPKDDINGQN PASPWGPSDT SRPKSSTGQT PMGQFVQPPP
     SAGGLRSPRP PQLSSNTNIQ STTLTAAEPQ LTELPLLSPY TSSGNWASMV NTPMVPTFGQ
     TQGNNADMVA NATAMKLAAL STVNNRFALD DARRYRRARS NDGAPGQSHA QHPLSPGPQG
     IPSTNVVMIN EHGQVLSHDH VLALQQQQQQ GLQQGLGGFG GHRSRPTSPG IAMPNYGSAL
     QFTSPQNNGF LSAYDGGAPG LINNGLVPMM GQFNLGGHHA EGYLSDHSEI NRGRSPRGRR
     GSSKPPEDPT DPTLLQDIPS WLRSLRLHKY TDNLKDMKWT DLIELDDKQL EERGVNALGA
     RRKMLKVFEQ VKEAKKEGKI
 
 
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