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Database: UniProt
Entry: A0A1X7REB7_ZYMTR
LinkDB: A0A1X7REB7_ZYMTR
Original site: A0A1X7REB7_ZYMTR 
ID   A0A1X7REB7_ZYMTR        Unreviewed;      1375 AA.
AC   A0A1X7REB7;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=RRM domain-containing protein {ECO:0000259|PROSITE:PS50102};
GN   ORFNames=ZT3D7_G715 {ECO:0000313|EMBL:SMQ45571.1};
OS   Zymoseptoria tritici ST99CH_3D7.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX   NCBI_TaxID=1276538 {ECO:0000313|EMBL:SMQ45571.1, ECO:0000313|Proteomes:UP000215127};
RN   [1] {ECO:0000313|EMBL:SMQ45571.1, ECO:0000313|Proteomes:UP000215127}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; LT853692; SMQ45571.1; -; Genomic_DNA.
DR   STRING; 1276538.A0A1X7REB7; -.
DR   Proteomes; UP000215127; Chromosome 1.
DR   GO; GO:0005634; C:nucleus; IEA:UniProt.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR   CDD; cd12296; RRM1_Prp24; 1.
DR   CDD; cd12299; RRM4_Prp24; 1.
DR   CDD; cd00590; RRM_SF; 1.
DR   Gene3D; 3.30.70.330; -; 4.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 2.
DR   InterPro; IPR003107; HAT.
DR   InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR   InterPro; IPR034397; Prp24_RRM1.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR000504; RRM_dom.
DR   InterPro; IPR031766; RRM_occluded.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   PANTHER; PTHR10352; EUKARYOTIC TRANSLATION INITIATION FACTOR 3 SUBUNIT G; 1.
DR   PANTHER; PTHR10352:SF0; EUKARYOTIC TRANSLATION INITIATION FACTOR 3 SUBUNIT G; 1.
DR   Pfam; PF00076; RRM_1; 3.
DR   Pfam; PF16842; RRM_occluded; 1.
DR   SMART; SM00386; HAT; 4.
DR   SMART; SM00360; RRM; 4.
DR   SUPFAM; SSF54928; RNA-binding domain, RBD; 3.
DR   SUPFAM; SSF48452; TPR-like; 1.
DR   PROSITE; PS50102; RRM; 4.
PE   4: Predicted;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Reference proteome {ECO:0000313|Proteomes:UP000215127};
KW   RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00176}.
FT   DOMAIN          897..972
FT                   /note="RRM"
FT                   /evidence="ECO:0000259|PROSITE:PS50102"
FT   DOMAIN          973..1051
FT                   /note="RRM"
FT                   /evidence="ECO:0000259|PROSITE:PS50102"
FT   DOMAIN          1065..1142
FT                   /note="RRM"
FT                   /evidence="ECO:0000259|PROSITE:PS50102"
FT   DOMAIN          1199..1279
FT                   /note="RRM"
FT                   /evidence="ECO:0000259|PROSITE:PS50102"
FT   REGION          1..245
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          845..893
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1161..1192
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1320..1375
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..36
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        60..88
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        89..125
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        126..145
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        152..225
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        851..893
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1353..1375
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1375 AA;  152678 MW;  742B730BFBFE4337 CRC64;
     MDINALLSPD DGSSSSAKGE GAPSSSVSPQ KSRSSRVRRP SGGKRTASGL SHEVSRSPDR
     RPLSTTPQQQ QQQQQALHQH HQQGQPHPHR PSYPQPPPPP AGHPPHRPAN VADFRPPPPT
     SNPAADPAPR HQTNSTTSQQ NYLDPSRPLI AHRPSSTPSM ETLADLASIQ QRQQTTRTYS
     ANSVSTLRGL DAPSQQRPPL HSHTSGTPPI SRGISRQSLA DLTMAEAPSQ TPPPRDFKSS
     DLSEDESRTV SDLLNYLAEN SYAYEQHVQL INLLHKGFLS HAHPFAASPD TATPSAPSSY
     ALLNEMRQAR EAMDTRFAVG EAIWADWLAD EALLANTSDE RIAMTELCQK AVQDEPASVI
     LWMMFVDWVT SNYAACHDLE GAENSTWTSD DKEMCRELFT WEMVVGILEQ AIAATKWRID
     KSHLLWNRYA QMVQDQFPSN PTEADVKSLH SLFLDRLQVP HAAWDETRQT YWPIVSRFEG
     DAYEAVFEQV NKMAQPAQKA MKVREQHEFK LERAVQSGEP LQVHRELEKY LKSERFQHNK
     PGLFDYDLRC GLYERALLYE PTNTEWWLDY VDFVVTSPAA ATQSLLPLIE RATRHCPWSG
     ELWARRILQA DSERKSRDEI ESTKHRATNA GLLDIGGMEE LVRMLQEWCS YLRRHAFRAG
     NAEDDIDTAE VGITMALEDV QQAGVKIYGK DFKGDPLWRL EQIQLKFYTQ GRRFDEARSL
     FQKLAKTVGH SYEFWKHYYN WELTMWGFNR FRDPQRFETD DNGPNDATAV VQEALRQRNV
     ESPERILQLY LDHFRLHESG SRLHAALVEG REYANRLAAT KAKQAEEAAR VAAQQQQYYA
     ETMEATAEVS APGGEKRKRD DDTLTNGDSH KKSKTDAAAT RVSEEPTTHV KRDREHNTIT
     VKNLPLDVQE AEIKKFFKDC GNTPSVNILR DEENNASSAT VEFETHEDVL AAKTRDGKAF
     EGREINISSG VQNTLYVTNY PAEWEESNIR DLLKSYGEII SIRLPSLKYN NRRRFCYVQF
     LHPDMAKAAE AAMDGTKLDA AHTILAKISN PDRKKARSGA LEEGRELFVK NLDRDAPEDD
     LKKLFEPYGK LEKFNLLRLM NNKLTGSGFF TYSSAAEANA AIEALHNKPF HGRILNVALA
     TPKGGAAPID RAKAEDVIIK RTGGTSATPE PNGARRDSDV SMHSAPPAEN HSAAEIRARK
     VAIFNLPDTV NDARITSAME KFGPISKIQL RREKDGAIVE FVDSNHAFHV RQGVDLHSLG
     EGVTSGDVGD LLAIKKPKKA AAAPGGAGGA TSLAFVPPAA ARAAAGRGGR RGGLGFKRGG
     AGGFGGAAAG PKSDSVAAEG STTGGKKSNA DFRSMLEASK KPDEAANKEA STEEE
//
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