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Database: UniProt
Entry: F9X0B1_ZYMTI
LinkDB: F9X0B1_ZYMTI
Original site: F9X0B1_ZYMTI 
ID   F9X0B1_ZYMTI            Unreviewed;      1506 AA.
AC   F9X0B1;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   RecName: Full=Ribonuclease II/R domain-containing protein {ECO:0000259|SMART:SM00955};
GN   ORFNames=MYCGRDRAFT_107385 {ECO:0000313|EMBL:EGP91419.1};
OS   Zymoseptoria tritici (strain CBS 115943 / IPO323) (Speckled leaf blotch
OS   fungus) (Septoria tritici).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX   NCBI_TaxID=336722 {ECO:0000313|EMBL:EGP91419.1, ECO:0000313|Proteomes:UP000008062};
RN   [1] {ECO:0000313|EMBL:EGP91419.1, ECO:0000313|Proteomes:UP000008062}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 115943 / IPO323 {ECO:0000313|Proteomes:UP000008062};
RX   PubMed=21695235; DOI=10.1371/journal.pgen.1002070;
RA   Goodwin S.B., Ben M'barek S., Dhillon B., Wittenberg A.H.J., Crane C.F.,
RA   Hane J.K., Foster A.J., Van der Lee T.A.J., Grimwood J., Aerts A.,
RA   Antoniw J., Bailey A., Bluhm B., Bowler J., Bristow J., van der Burgt A.,
RA   Canto-Canche B., Churchill A.C.L., Conde-Ferraez L., Cools H.J.,
RA   Coutinho P.M., Csukai M., Dehal P., De Wit P., Donzelli B.,
RA   van de Geest H.C., van Ham R.C.H.J., Hammond-Kosack K.E., Henrissat B.,
RA   Kilian A., Kobayashi A.K., Koopmann E., Kourmpetis Y., Kuzniar A.,
RA   Lindquist E., Lombard V., Maliepaard C., Martins N., Mehrabi R.,
RA   Nap J.P.H., Ponomarenko A., Rudd J.J., Salamov A., Schmutz J.,
RA   Schouten H.J., Shapiro H., Stergiopoulos I., Torriani S.F.F., Tu H.,
RA   de Vries R.P., Waalwijk C., Ware S.B., Wiebenga A., Zwiers L.-H.,
RA   Oliver R.P., Grigoriev I.V., Kema G.H.J.;
RT   "Finished genome of the fungal wheat pathogen Mycosphaerella graminicola
RT   reveals dispensome structure, chromosome plasticity, and stealth
RT   pathogenesis.";
RL   PLoS Genet. 7:E1002070-E1002070(2011).
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DR   EMBL; CM001196; EGP91419.1; -; Genomic_DNA.
DR   RefSeq; XP_003856443.1; XM_003856395.1.
DR   STRING; 336722.F9X0B1; -.
DR   EnsemblFungi; Mycgr3T107385; Mycgr3P107385; Mycgr3G107385.
DR   GeneID; 13399153; -.
DR   KEGG; ztr:MYCGRDRAFT_107385; -.
DR   eggNOG; KOG2102; Eukaryota.
DR   HOGENOM; CLU_002333_0_3_1; -.
DR   InParanoid; F9X0B1; -.
DR   OMA; QIQATHQ; -.
DR   OrthoDB; 945235at2759; -.
DR   Proteomes; UP000008062; Chromosome 1.
DR   GO; GO:0005935; C:cellular bud neck; IEA:EnsemblFungi.
DR   GO; GO:0010494; C:cytoplasmic stress granule; IEA:EnsemblFungi.
DR   GO; GO:0005634; C:nucleus; IEA:EnsemblFungi.
DR   GO; GO:0000932; C:P-body; IEA:EnsemblFungi.
DR   GO; GO:0003730; F:mRNA 3'-UTR binding; IEA:EnsemblFungi.
DR   GO; GO:0048027; F:mRNA 5'-UTR binding; IEA:EnsemblFungi.
DR   GO; GO:0000900; F:mRNA regulatory element binding translation repressor activity; IEA:EnsemblFungi.
DR   GO; GO:0004540; F:RNA nuclease activity; IEA:InterPro.
DR   GO; GO:0008298; P:intracellular mRNA localization; IEA:EnsemblFungi.
DR   GO; GO:0060237; P:regulation of fungal-type cell wall organization; IEA:EnsemblFungi.
DR   GO; GO:1903450; P:regulation of G1 to G0 transition; IEA:EnsemblFungi.
DR   Gene3D; 2.40.50.690; -; 1.
DR   Gene3D; 2.40.50.700; -; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   InterPro; IPR041505; Dis3_CSD2.
DR   InterPro; IPR041093; Dis3l2_C.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR001900; RNase_II/R.
DR   PANTHER; PTHR23355:SF9; DIS3-LIKE EXONUCLEASE 2; 1.
DR   PANTHER; PTHR23355; RIBONUCLEASE; 1.
DR   Pfam; PF17877; Dis3l2_C_term; 1.
DR   Pfam; PF17849; OB_Dis3; 1.
DR   Pfam; PF00773; RNB; 1.
DR   SMART; SM00955; RNB; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 3.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000008062}.
FT   DOMAIN          894..1228
FT                   /note="Ribonuclease II/R"
FT                   /evidence="ECO:0000259|SMART:SM00955"
FT   REGION          250..312
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          335..502
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          646..706
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          750..784
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1337..1450
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        277..295
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        401..502
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        646..661
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        662..681
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        758..784
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1345..1375
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1388..1402
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1417..1450
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1506 AA;  165739 MW;  3D1E0281C1106BF8 CRC64;
     MHESTVDARP SRIRNLNDIR HLRTNSPERP TNRRRLRPSL HSPVTSIIFI TALTHSFPQH
     VAAADTPSFR NSSSSSVLRS LPTSLSLHTL HRNLHHRPAL PGLHVASPRQ LETAVYCIYS
     PTTTLHKKFV MDQQGQQTGP QGPNGRRLHI AHRRSPSEMT PLMMEQLALA QQIEMLQQQQ
     QQIAATHQQY VNMGMIPQQQ QLPNQFQQLQ GQMQNLNVGS NPAAFQFPQQ PQMGQQHLGI
     PMAGGMAQAS AHRRNQSAMP NMGMGPPPAP SSGASGSAFG DFGNFGQNRT ENNAPTRGRG
     GGAAGGGHAR RHSLALPEAK KAAELAEAKR KTSGFQFPIP GAAGAPPAPD NRAASPGSGE
     AGSAAGSATR GGVGGRGHGR SQSMAVGNNR GMGQLSRGGP TGFQFPPQQA TVDGGSNTSE
     LSRRGSQGHG RTGSRNFDGN WRNPNPNNTQ PPTDGQTTNM GNFHMNQHTS AQPFQPGHRQ
     RGSVGGQSIS SLQSFGNYQP QPQLMQLPQG QVLVQPAAMF GGQQLNALQL AQLQAYQQAG
     IQAPTLAQLT GQHNGPQIGM HQQQQQRKTL FTPYLPQATL PALLGDGQLV AGILRVNKKN
     RSDAYVTTTD LDADIFICGS KDRNRALEGD LVAVELLDVD EVWGQKREKE EKKKRKDVTD
     QRSGNMTAVN DATTQPESAS AAQEGGLRRR GSLKQRPTQK KNDDVEVEGQ SLLLMEEDEI
     NDEQKPLYAG HIVAVIERVA GQMFSGSLGL LRPSSQATKE KQEAERQARD GGNARHQERQ
     QDRPKIVWFK PTDKRVPLIA IPTEQAPRDF VDRHQDYANK IFVACIKRWP ITSLHPFGTL
     VEQLGEAGDL KVETDALLRD NNFGPDDFSE AVIKNVGFED WSIEKEGESA LEGRRDFREE
     QTFTIDPNGS KELDDAIHFK DLGDGNVEIG MHVTDIAHFV KANSLVDREA KKRGTGVYLT
     DRTVNMLPSK ITHDVCCLNP GEDRYTVSVV FKVDAASGRV SEEDTWVGKA IIKSSGKLSY
     EEVDAVINGS KESSLGEERS KQILMLHNIA QKLRRGRYNS EEEDIPPLRL FYQLDDENVP
     VERNIFDSSP AHEMIEELSH KTNAVVAQKI FAQLQDRALL RRQADPFPRR LQTFAERMAN
     IGYDMDISSS ASLQNSLFRI DDAEIRKGME TLIIKAMGRA KYVVPGKVPD PSLSHYALNL
     PLYTHFTNPS RRYADIIVHR QLEAALSNGA VEFSEDLESL NKTAETCNTK KDSAHAAQEQ
     SVHIESCRLM NRLSEEQGGD LISVGIVVCV YESAFDVLIP EYGFEKRVHC DQLPLKKAEF
     DKNKRLLELY WEKGVPSSAF VPDDERPQAK GHRPTHSFVA REATAKHREA QEAERKAMNT
     GSIDAQDVDA LFDDDDDDNA SEATDNAAGV ALNGDRATQS GPPSPSRNGA PPQRSKSDSR
     ALNNSAAPEA KLSNKDKYLG FFKLREENGH YIQDVKEMTR VPVLLRTDLT KSPPCLTIRS
     LNPYAL
//
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