ID   A0A0F4GRB6_9PEZI        Unreviewed;      1016 AA.
AC   A0A0F4GRB6;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   22-FEB-2023, entry version 30.
DE   RecName: Full=mRNA 3'-end-processing protein RNA14 {ECO:0000256|RuleBase:RU369035};
GN   ORFNames=TI39_contig392g00024 {ECO:0000313|EMBL:KJX98755.1};
OS   Zymoseptoria brevis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX   NCBI_TaxID=1047168 {ECO:0000313|EMBL:KJX98755.1, ECO:0000313|Proteomes:UP000033647};
RN   [1] {ECO:0000313|EMBL:KJX98755.1, ECO:0000313|Proteomes:UP000033647}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Zb18110 {ECO:0000313|EMBL:KJX98755.1,
RC   ECO:0000313|Proteomes:UP000033647};
RA   Grandaubert J., Bhattacharyya A., Stukenbrock E.H.;
RT   "RNA-seq based gene annotation and comparative genomics of four
RT   Zymoseptoria species reveal species-specific pathogenicity related genes
RT   and transposable element activity.";
RL   Submitted (MAR-2015) 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}.
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:KJX98755.1}.
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DR   EMBL; LAFY01000384; KJX98755.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F4GRB6; -.
DR   STRING; 1047168.A0A0F4GRB6; -.
DR   OrthoDB; 23291at2759; -.
DR   Proteomes; UP000033647; 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; -; 2.
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   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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033647}.
FT   DOMAIN          667..1000
FT                   /note="Suppressor of forked"
FT                   /evidence="ECO:0000259|Pfam:PF05843"
FT   REGION          1..162
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          611..643
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          858..888
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        19..33
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        34..53
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        127..162
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        629..643
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        859..878
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1016 AA;  113601 MW;  3CF247E4A1ADE482 CRC64;
     MAEEYDPLDP PTFDPADESD DAEQQKYESG ADAADDAADD AADEDDDYDP SSFNYGEDTE
     QSEAAEPDQT LKEPPAQIEQ PRKPQQTVAG FIVEESDDEQ EESVAAPPQI NGGSDAEEHD
     AETNIEAQDV SLRSAPQDTA TSSTSLNGST TIPVPASTPS LPVSTLQTSV ADLGKDVLTP
     VESAAPTPQA QADTKAPAVS LPTTQLNGSM PAAQMRLPHD KVGQLEDRIK DDPKGDTDAW
     LSLIKHYYDK TQYQGARDVY KRFLAVFPTA VSMWVKYIQM ENELDERDNV VHILGESVMT
     VPSVELWKLY LDHVRRALPL INDAGGKNRT EITKAFDVTL DNVGIDPDAG ILWREYIDFV
     RDGPGMVGGQ DWQDLQKVDQ LRKAYQRATK LPHSESVKLW KEYENFEMGL HKATGRKHVQ
     EQSPHYMQAR TARMQLEQKL EGLDRRSIPV LPPLYGCAGE DEFGNQVEKW RSWIEWEKNE
     DPLVFKGTED DAWRRRVLYA YKQATLFLCF YPPIWFEAAS WCFSQGIDSF TIEGEQFLDK
     GMATNPESVL LAMSKADRVE SSLETGNTEE ILIRNGDKLD VPYEQVHTAL YAFRGRLKEK
     DDKTIAQINA HFASLSPEEE PTTVQEDDDD DQPSNKPKTR AEQLKAAIDS VKQASAAHMD
     LLKRTISYVW VAKMRAFRRV QGQGKPPKKG DTTSKVVKGF RGIFADARPR GQLSSDVYIA
     SALLEWRCYK DPSAIKIFER GMKLFPLDEV FILEYVKHLI ALSDITNARV VFESTIPKIV
     NAADLSLEQK REKCRPLIAY MHDYESKYGD LAQIHKIEKR MSELYPEEPE ISRFSHRFSL
     PDFDAMHVQL VLSPTQARPR AFEPQQQAPQ QAPANSIEHM HNSPRGAAPE ILLGPNGPYV
     ASPKRPLEDS DNEQPQRKFM RGESPLKGAA GLRMQSKAGA TSGGGFATKT FVPNSVSVPS
     GPPPLPPMIE YVLRLMPAAR DYNQARFDAV KIAYLVASTD VDSAKAAFSR GNLQRR
//