ID A0A194VFE4_9PEZI Unreviewed; 600 AA.
AC A0A194VFE4;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 03-MAY-2023, entry version 23.
DE RecName: Full=RNA-binding protein VTS1 {ECO:0000256|ARBA:ARBA00024136};
GN ORFNames=VP1G_09835 {ECO:0000313|EMBL:KUI62727.1};
OS Valsa mali var. pyri (nom. inval.).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Valsaceae; Valsa.
OX NCBI_TaxID=694573 {ECO:0000313|EMBL:KUI62727.1, ECO:0000313|Proteomes:UP000078576};
RN [1] {ECO:0000313|Proteomes:UP000078576}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SXYL134 {ECO:0000313|Proteomes:UP000078576};
RA Yin Z., Liu H., Gao X., Li Z., Song N., Ke X., Dai Q., Wu Y., Sun Y.,
RA Xu J.-R., Kang Z.K., Wang L., Huang L.;
RT "Genome Sequence of Valsa Canker Pathogens Uncovers a Specific Adaption of
RT Colonization on Woody Bark.";
RL Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBUNIT: Monomer. Binds to RNA. {ECO:0000256|ARBA:ARBA00024046}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, P-body
CC {ECO:0000256|ARBA:ARBA00004201}. Cytoplasm, cytosol
CC {ECO:0000256|ARBA:ARBA00004514}.
CC -!- SIMILARITY: Belongs to the VTS1 family.
CC {ECO:0000256|ARBA:ARBA00007325}.
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DR EMBL; KN714829; KUI62727.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A194VFE4; -.
DR STRING; 694573.A0A194VFE4; -.
DR OrthoDB; 1351201at2759; -.
DR Proteomes; UP000078576; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell.
DR GO; GO:0003729; F:mRNA binding; IEA:InterPro.
DR GO; GO:0043488; P:regulation of mRNA stability; IEA:InterPro.
DR CDD; cd09556; SAM_VTS1_fungal; 1.
DR Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR037635; VTS1_SAM.
DR PANTHER; PTHR12515:SF5; PROTEIN SMAUG; 1.
DR PANTHER; PTHR12515; STERILE ALPHA MOTIF DOMAIN CONTAINING PROTEIN 4-RELATED; 1.
DR Pfam; PF07647; SAM_2; 1.
DR SMART; SM00454; SAM; 1.
DR SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000078576};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT DOMAIN 532..593
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT REGION 1..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 186..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 250..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 499..533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..70
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..285
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..312
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 501..525
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 600 AA; 64526 MW; 12677F9C22060463 CRC64;
MSNIMSNRNS TPEAGNASSL RPPSSRAIGA GHQLRASADM ASFTGTPQSK QIRPNSDFYG
QSQHGQGQGT GELDPQDKLA QQWIADIDQY ETTLEEMAAA TLDQDFKDEL SAIEQWFRVL
SEAERTAALY ALLQQTTQVQ IRFFIQVLQQ MGKSHPMSGV LSPANFDKDP MSSRLSDAMG
KLSVDSARNS LTRAPSTSKR QSGLDTNTIN AMFPDAAAAI ATEKAKYTQS TGTAPPSNRN
STVDNRNSLV APTISAPDDS NGQNNSPWGT DQRPKSSTGQ APMGQFAQPP PSAGLRSPHP
QIQGSQQIKS QTITAGDKSV NDLPLLSPYG PSGGNWASMV NTPMVANFNH QQQGANQADM
VANATAMKLA ALSTVNNRFA LDDVRKYRRA RSNDAPGAPL SPNPQGMGMG SHLNIVMSNE
RGQVLTPEQM IAIQNQQLAG GDRSRPNSPG FAMHGGFQQM GAFASPQANG FLNPYSGASP
LLNNGMTLGM GGIPIGGHHE GYLSDHSDMN RGRSPRGRRG TSKPPEDPTD QTLLQDIPAW
LRSLRLHKYT DNLKDLKWNE LVELDDAALE ARGVNALGAR RKMLKVFDQV KEAKAAGKLP
//
