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Database: UniProt
Entry: A0A9Q0XZS0_9SAUR
LinkDB: A0A9Q0XZS0_9SAUR
Original site: A0A9Q0XZS0_9SAUR 
ID   A0A9Q0XZS0_9SAUR        Unreviewed;       564 AA.
AC   A0A9Q0XZS0;
DT   13-SEP-2023, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2023, sequence version 1.
DT   28-JAN-2026, entry version 11.
DE   RecName: Full=YTH domain-containing family protein {ECO:0000256|RuleBase:RU369095};
GN   ORFNames=JRQ81_014322 {ECO:0000313|EMBL:KAJ7332142.1};
OS   Phrynocephalus forsythii.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Iguania; Acrodonta; Agamidae; Agaminae; Phrynocephalus.
OX   NCBI_TaxID=171643 {ECO:0000313|EMBL:KAJ7332142.1, ECO:0000313|Proteomes:UP001142489};
RN   [1] {ECO:0000313|EMBL:KAJ7332142.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Muscle {ECO:0000313|EMBL:KAJ7332142.1};
RX   PubMed=36882113;
RA   Qi Y., Zhao W., Zhao Y., Niu C., Cao S., Zhang Y.;
RT   "Chromosome-level genome assembly of Phrynocephalus forsythii using third-
RT   generation DNA sequencing and Hi-C analysis.";
RL   DNA Res. 0:0-0(2023).
CC   -!- FUNCTION: Specifically recognizes and binds N6-methyladenosine (m6A)-
CC       containing RNAs, and regulates mRNA stability. M6A is a modification
CC       present at internal sites of mRNAs and some non-coding RNAs and plays a
CC       role in mRNA stability and processing. {ECO:0000256|RuleBase:RU369095}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, P-body
CC       {ECO:0000256|ARBA:ARBA00004201}. Cytoplasm, Stress granule
CC       {ECO:0000256|ARBA:ARBA00004210}.
CC   -!- SIMILARITY: Belongs to the YTHDF family.
CC       {ECO:0000256|RuleBase:RU369095}.
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:KAJ7332142.1}.
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DR   EMBL; JAPFRF010000005; KAJ7332142.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A9Q0XZS0; -.
DR   OrthoDB; 306690at2759; -.
DR   Proteomes; UP001142489; Unassembled WGS sequence.
DR   GO; GO:0010494; C:cytoplasmic stress granule; IEA:UniProtKB-SubCell.
DR   GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell.
DR   GO; GO:0003729; F:mRNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:1990247; F:N6-methyladenosine-containing RNA reader activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0061157; P:mRNA destabilization; IEA:UniProtKB-ARBA.
DR   CDD; cd21134; YTH; 1.
DR   FunFam; 3.10.590.10:FF:000001; YTH domain family 1, isoform CRA_a; 1.
DR   Gene3D; 3.10.590.10; ph1033 like domains; 1.
DR   InterPro; IPR007275; YTH_domain.
DR   InterPro; IPR045168; YTH_prot.
DR   PANTHER; PTHR12357:SF65; YTH DOMAIN-CONTAINING FAMILY PROTEIN 1; 1.
DR   PANTHER; PTHR12357; YTH YT521-B HOMOLOGY DOMAIN-CONTAINING; 1.
DR   Pfam; PF04146; YTH; 1.
DR   SUPFAM; SSF81995; beta-sandwich domain of Sec23/24; 1.
DR   PROSITE; PS50882; YTH; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Reference proteome {ECO:0000313|Proteomes:UP001142489};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|RuleBase:RU369095}.
FT   DOMAIN          394..528
FT                   /note="YTH"
FT                   /evidence="ECO:0000259|PROSITE:PS50882"
FT   REGION          1..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          239..368
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        24..33
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        39..50
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        306..330
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        351..362
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   564 AA;  61413 MW;  86AD2675B3B21FCD CRC64;
     MSATSVDPQR PKGQDNKVQN GSLHQKDAVH DNDFEPYLSG QSNQNNSYPS MTDPYLSSYY
     PPSIGFPYSL SEAPWSTGGD PPIPYLTTYG QLSNGDHHFM HDAVFGQPGG LGNNIYPHRF
     NFFPENPPFS AWGTSGSQGQ QTQNSAYGSS YSYPPSSLGG TIVDGQTGFH NDTLNKAPGM
     NSIEQGMVGL KIGGDVTASA VKAVGSVVNS AGMAGALSGN GGSSISLPVS KPTSWAAIAS
     KPAKPQPKMK TKSGPVVGAA LPPPPIKHNM DIGTWDNKGP AAKVPTPQQI PSPQSVPQPQ
     LIQPIPAQPP PLTQLPYQNP QPPPPPPPPQ NRWVAPRNRN AAFGQSGGTG HENNSPGTTP
     ANSIPAGESH PVLEKLKAAH SYNPKDFEWN LKNGRVFIIK SYSEDDIHRS IKYSIWCSTE
     HGNKRLDSAF RSMNSKGPVY LLFSVNGSGH FCGVAEMKSS VDYGTSAGVW SQDKWKGKFD
     VKWIFVKDVP NNQLRHIRLE NNDNKPVTNS RDTQEVPLEK AKQVLKIIAT YKHTTSIFDD
     FSHYEKRQEE EEVVRKERQN RNKQ
//
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