ID A0A177C451_9PLEO Unreviewed; 1032 AA.
AC A0A177C451;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 28-JUN-2023, entry version 27.
DE RecName: Full=mRNA 3'-end-processing protein RNA14 {ECO:0000256|RuleBase:RU369035};
GN ORFNames=CC84DRAFT_1166368 {ECO:0000313|EMBL:OAG02524.1};
OS Paraphaeosphaeria sporulosa.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Massarineae; Didymosphaeriaceae;
OC Paraphaeosphaeria.
OX NCBI_TaxID=1460663 {ECO:0000313|EMBL:OAG02524.1, ECO:0000313|Proteomes:UP000077069};
RN [1] {ECO:0000313|EMBL:OAG02524.1, ECO:0000313|Proteomes:UP000077069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AP3s5-JAC2a {ECO:0000313|EMBL:OAG02524.1,
RC ECO:0000313|Proteomes:UP000077069};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) 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; KV441555; OAG02524.1; -; Genomic_DNA.
DR RefSeq; XP_018032889.1; XM_018178943.1.
DR AlphaFoldDB; A0A177C451; -.
DR STRING; 1460663.A0A177C451; -.
DR GeneID; 28762429; -.
DR InParanoid; A0A177C451; -.
DR OrthoDB; 23291at2759; -.
DR Proteomes; UP000077069; 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; 4.
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:UP000077069}.
FT DOMAIN 677..997
FT /note="Suppressor of forked"
FT /evidence="ECO:0000259|Pfam:PF05843"
FT REGION 1..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 181..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 617..657
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 874..926
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..44
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..161
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 887..901
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 911..925
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1032 AA; 113707 MW; 79435EC631E3D17A CRC64;
MADADAEMAF LEAQKQEYDP AADFSLAPEQ AEQDEEEEYD PDNAFGNPPE ETRSASAQSV
AMADSATNTP QPADEGALRA PPADTPAAPT PQKQPRTKGG FVDESEDDED EVSVAKPKAG
SALLNASGVS ESPQRSVTLS PNNTHAPQAM SSISAQDQPV PGVQSPPVAV PNVVSSLASA
TVPNGGTPVP DATKTGSSDP LKAAPAPASA STTTLPASLP RPRLPQDTVG RLEDRVAEDP
RGDIEAWLGL IDDHRKRHKV DEARGVFERF FQVFPSAAEI WVQYVNMETE LENFAQVEQI
FGRSIQNTPS LLLFSSYIDY VRRRYPLEEG DNRKIIVQAY EFVLPHVGID INAGKLWTDY
IEILKSGPGN LGGSGWQDMQ KMDILRKAYQ RAIAVPTNAT MEIWRDYDRF EMNLNKVQGR
KHLQEKSASY MTARSAVTVA ENITRSVHRT TLPKLPPAPG FDGAEDFTKQ VQAWKNWIEW
EKSDPLEIRD EDRETYNKRV LYIYKNALAA LRFWPEMWFD AAEWSLQNNL SDEGNTFLQG
GMEANPESCL LAFKRSNQLE LRTDFEEGDA GIIAKAKVVR EPLDTVLNTL YDLINKVKKR
EERSIAMAKE HFNAQLAAEE AARAGSEKGS DVEDDDDDEN SAAARRQRER QAGFDAQLQG
ITTSTNAEIH VLKKTLTYAW IALMRAMRRV QGKGGAKDTN IPGFRGVFGE ARKRGKLLSD
AYVASALIEH HCYQDVAAGK IFERGMKLFP DDEVFALEYV KHLVKLNDAT NARAVFETVV
TRLCQKPENI ARTKPLFVFF HDYESQFGEL AQITKLEQRM ATLFPEDPQL LRFASRFKSP
TFDPTAVRPI ISPRTQMRPA MPSNIMPTVE EPVQAAPPVP APQPERLQSP ATFNSPRLGH
LLPATNSPKR PLEDADNDQP RKMIRGESPL KGAAGRRLDA ARRNNAVGGG NTPVAGPTPL
PKGVNFLLGI IPPAHTYQAT RFRPEAMVNL LRGITLPLPG NAAASAGPPA AHIGAQLQNI
QARYGGVQPG YQ
//
