VTS1_ASPFU
ID VTS1_ASPFU Reviewed; 612 AA.
AC Q4WJS2;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 2.
DT 25-MAY-2022, entry version 93.
DE RecName: Full=RNA-binding protein vts1;
GN Name=vts1; ORFNames=AFUA_1G04990;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
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; AAHF01000007; EAL88210.2; -; Genomic_DNA.
DR RefSeq; XP_750248.2; XM_745155.2.
DR AlphaFoldDB; Q4WJS2; -.
DR SMR; Q4WJS2; -.
DR STRING; 746128.CADAFUBP00000527; -.
DR EnsemblFungi; EAL88210; EAL88210; AFUA_1G04990.
DR GeneID; 3507442; -.
DR KEGG; afm:AFUA_1G04990; -.
DR VEuPathDB; FungiDB:Afu1g04990; -.
DR eggNOG; KOG3791; Eukaryota.
DR HOGENOM; CLU_017632_0_0_1; -.
DR InParanoid; Q4WJS2; -.
DR OMA; ANFDKDP; -.
DR OrthoDB; 1052795at2759; -.
DR Proteomes; UP000002530; Chromosome 1.
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..612
FT /note="RNA-binding protein vts1"
FT /id="PRO_0000081447"
FT DOMAIN 541..602
FT /note="SAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT REGION 1..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 184..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 253..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 391..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 511..544
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 42..74
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 253..271
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..311
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..411
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 513..534
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 612 AA; 65610 MW; 8B55326BA8DECF25 CRC64;
MASHIIGNRN STPDASKSSL RPPSSSRNLG SHQLRASADM SGFPSPLSSR SIRPSSEVYY
SQQSQAQNNA EDPLDRAAQQ WLADIDQYET TLEEMAAATL DQDFKDELSA IEQWFRVLSE
AERTAALYAL LQQTTQVQIR FFIQVLQQMA KSHPMSGLLS PANFSEKDAM SNRLNDAMSK
LNIDSSRNSL GRPPPSPGAK RNSGLDSSTI NAMFPDAAAA IAKKKAEFTQ QTGNAPPSNR
NSAVYGDRSS LVAPTISAPD NTDNLGQPPA SPWAQRGNEP QPPIARPKSS SGQQPMGQFS
QASSGLRSPL PTQTATITAP EIEAPLLSPY NVGNASWASM TNTPMTATFG QQVHQPPNSQ
ADMVANATAM KLAALSTVNN RIALDDARKY RRARSNDGQG RSSNTNVNQT IQGGLASPGL
PGANHLVAGQ LLNAQQLAAL QAQQQAAMAG RRSRPTSPGI AMQGGALAAM GFTSPQNNGF
LAAYDPNNPL LGNGLGALGL SQFGLGGHEG YLSDHSEVTR GRSPRGRRGS SKPPEDPTDP
NLLKDIPSWL RSLRLHKYTD NLKDLKWTEL IELDDKALEE RGVNALGARN KMLKVFEQVK
EAKSEGKLDS IA
