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VTS1_EMENI
ID   VTS1_EMENI              Reviewed;         611 AA.
AC   Q5BGC4; C8VTI0;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=RNA-binding protein vts1;
GN   Name=vts1; ORFNames=AN0406;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS   M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA   Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA   Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA   Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA   Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA   Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA   Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA   Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA   Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA   Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA   Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA   Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA   Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA   van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA   Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA   Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA   Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA   Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA   Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA   van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA   Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA   Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT   effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
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; AACD01000007; EAA66505.1; -; Genomic_DNA.
DR   EMBL; BN001308; CBF89550.1; -; Genomic_DNA.
DR   RefSeq; XP_658010.1; XM_652918.1.
DR   AlphaFoldDB; Q5BGC4; -.
DR   SMR; Q5BGC4; -.
DR   STRING; 162425.CADANIAP00002293; -.
DR   EnsemblFungi; CBF89550; CBF89550; ANIA_00406.
DR   EnsemblFungi; EAA66505; EAA66505; AN0406.2.
DR   GeneID; 2876181; -.
DR   KEGG; ani:AN0406.2; -.
DR   eggNOG; KOG3791; Eukaryota.
DR   HOGENOM; CLU_017632_0_0_1; -.
DR   InParanoid; Q5BGC4; -.
DR   OMA; ANFDKDP; -.
DR   OrthoDB; 1052795at2759; -.
DR   Proteomes; UP000000560; Chromosome VIII.
DR   Proteomes; UP000005890; Unassembled WGS sequence.
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..611
FT                   /note="RNA-binding protein vts1"
FT                   /id="PRO_0000081451"
FT   DOMAIN          539..600
FT                   /note="SAM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT   REGION          1..49
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          185..211
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          227..246
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          257..318
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          393..416
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          509..542
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..35
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        229..246
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        257..276
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        288..318
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        399..416
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        511..532
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   611 AA;  65439 MW;  6199CC695761D850 CRC64;
     MASHIIGNRN STPEASKSSL RPPSSSRNLA THQLRASADM SGFPSPLSSR SIRPASEVYF
     NQQAQTPGNA EDPLDRAAQQ WLADIDQYET TLEEMAAATL DQDFKDELSA IEQWFRVLSE
     AERTAALYAL LQQTTQVQIR FFIQVLQQMA KSHPMSGLLS PANFGEKGID AMSNRLNDAM
     SKLNVDSSRN SLGRPPPSPG AKRNSGLDSS TINAMFPDAA AAIAKKKAEF TQQTGNAPPS
     NRNSAVFNER TSFVAPTISA PDNSADNLSQ PPVSPWAQRG ASEPQPPIAR PKSSSGQQPM
     GQFNQSGLRS PLPTSQTATI PAPEIEAPLL SPYNVNASWA SMTNTPMTAT FGSQLGAPHQ
     QGSDMVANAT AMKLAALSTV NNRIALDDAR KYRRARSNDG QGKNASNNTG AQSIQGGLAS
     PGLPVAGQLL NAQQFAALQA QQQAAMAGHR SRPTSPGIAM QGGALGPMGF TSPQNNGFLT
     AYDPNNPLIG NGLGALGMGQ FGLSGHEGYL SDHSEINRGR SPRGRRGSSK PPEDPTDPNL
     LKDIPSWLRS LRLHKYTDNL KDLKWTELIE LNDKQLEERG VNALGARNKM LKVFEQVKEA
     KAEGKLDNAT A
 
 
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