ID   F8MS02_NEUT8            Unreviewed;      1139 AA.
AC   F8MS02;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   RecName: Full=mRNA 3'-end-processing protein RNA14 {ECO:0000256|RuleBase:RU369035};
GN   ORFNames=NEUTE1DRAFT_85042 {ECO:0000313|EMBL:EGO54996.1};
OS   Neurospora tetrasperma (strain FGSC 2508 / ATCC MYA-4615 / P0657).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=510951 {ECO:0000313|EMBL:EGO54996.1};
RN   [1] {ECO:0000313|EMBL:EGO54996.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=FGSC 2508 {ECO:0000313|EMBL:EGO54996.1};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Ellison C.E., Stajich J.E., Jacobson D.J., Lindquist E., Lapidus A.,
RA   Foster B., Aerts A., Riley R., Grigoriev I.V., Taylor J.W.;
RT   "Massive changes in genome architecture accompany the transition to self-
RT   fertility in the filamentous fungus Neurospora tetrasperma.";
RL   Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Component of the cleavage factor IA (CFIA) complex, which is
CC       involved in the endonucleolytic cleavage during polyadenylation-
CC       dependent pre-mRNA 3'-end formation. {ECO:0000256|ARBA:ARBA00002863,
CC       ECO:0000256|RuleBase:RU369035}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU369035}.
CC       Cytoplasm {ECO:0000256|RuleBase:RU369035}. Note=Nucleus and/or
CC       cytoplasm. {ECO:0000256|RuleBase:RU369035}.
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DR   EMBL; GL891306; EGO54996.1; -; Genomic_DNA.
DR   RefSeq; XP_009852884.1; XM_009854582.1.
DR   AlphaFoldDB; F8MS02; -.
DR   GeneID; 20830784; -.
DR   KEGG; nte:NEUTE1DRAFT85042; -.
DR   VEuPathDB; FungiDB:NEUTE1DRAFT_85042; -.
DR   HOGENOM; CLU_007630_1_1_1; -.
DR   OrthoDB; 23291at2759; -.
DR   Proteomes; UP000008065; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0006378; P:mRNA polyadenylation; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.25.40.1040; -; 1.
DR   InterPro; IPR003107; HAT.
DR   InterPro; IPR045243; Rna14-like.
DR   InterPro; IPR008847; Suf.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   PANTHER; PTHR19980:SF0; CLEAVAGE STIMULATION FACTOR SUBUNIT 3; 1.
DR   PANTHER; PTHR19980; RNA CLEAVAGE STIMULATION FACTOR; 1.
DR   Pfam; PF05843; Suf; 1.
DR   Pfam; PF13428; TPR_14; 1.
DR   SMART; SM00386; HAT; 5.
DR   SUPFAM; SSF48452; TPR-like; 2.
PE   4: Predicted;
KW   Cytoplasm {ECO:0000256|RuleBase:RU369035};
KW   mRNA processing {ECO:0000256|RuleBase:RU369035};
KW   Nucleus {ECO:0000256|RuleBase:RU369035}.
FT   DOMAIN          670..1002
FT                   /note="Suppressor of forked"
FT                   /evidence="ECO:0000259|Pfam:PF05843"
FT   REGION          1..165
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          179..224
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          861..959
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1018..1139
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        51..65
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        179..215
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        902..923
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1110..1125
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1139 AA;  125473 MW;  5442875135F461DB CRC64;
     MSDDYDPTNI NAASWEEQED YGEADGSEQY GEAEGSEQQD IQHSSEHQEA EYSVESNPND
     LGDHPSQDGN TDDVGDDYDP ASVVTSSVPA PSAPAPQEDS KTAPQPAAPV AKKPRTAGGF
     LVGDSDDEDE DVAHKETGSG ASSSGGSAPA PAPASATAAP QSHSPALQTA TLTVQDNAGA
     TTFNAPPVPQ QVSHQSGATT AAVPTTPNSA APAVDPTPVT QPAPDRVAIY EDQIRDDPRG
     AMNAWLELMK EKRARNDIDG ARQVYERFLA IFPQAADIWV EYLDLELSLN NFPQAEGIFA
     KCLMTTPNVN LWTRYLDYIR RRNDLNDSTG QARQTVSQAY EFVIDNIGLD KDSGKIWAEY
     IQFIKFGPGT VGGSQWQDQQ KMDQLRKAYQ RAICVPISNV NTLWKEYDQF EMGLNKLTGR
     KYLSEKSPSY MSAKSANTAL EHITRGLNRT NLPRLPPAPG FDGDQEFMEQ VEIWKKWIAW
     EKSDPLDLKD DKDQPGLYQK RILYVYNQAL MALRFWPEMW VDAAQWCFDN NITTVENKVT
     KDGNANGVEF LIRGIEANPE SVLLAFKHAD HIESTYPIEE NDEAKIQRGE AVKAPYNKVL
     DTLYAMIKSL KEKEAAQIAK LQEMTAAQES KAGSDNEDGD GAADNIKKAP IEAIQKGYAA
     QTQLLSRMIS FVWIALIRAM RRVQGKGGLN VPLGGMRKAF HDARARGRLT SDVYAAVAQL
     EWTIYKDPAG GKIFDRGAKL FPEDENFTLE NIKYLHSRDD HTNARVLFET VVNRLTQKPE
     LVHKAKPLYQ YFHKYESQFG ELAQVTKLEK RMAELFPEDP KLAAFTARYA SDKFDPITAR
     IIVSPTTQLR PKNMIMPSIE QQQPQLPMSQ RDTPAAGFSP RPQGLKSPSA GPGAPFAPYA
     AKRPLDDRDY DDHPRKIARS EHDPFVRGAS PLKGAAGRRL DQQRRMGGTA GAYSGSGAGS
     QVAPIARDIT FLLSQIPRVE FYDSHRLNPS RMVSLLQNVK VPEYLDWKRE RERMQQMQGD
     GYGGYGGGGG GGYQGGGHAR NISQDYAYRE SPGPLGGRPL SPFTGGPGSR LASATAAYRQ
     APVGRPESSG SYEPPPAAQY GVPPPAQYDG GWAQQQQQQQ YGQPPAPQGY RYGNPPPPY
//