ID A0A0F0IE46_ASPPU Unreviewed; 1014 AA.
AC A0A0F0IE46;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 22-FEB-2023, entry version 26.
DE RecName: Full=mRNA 3'-end-processing protein RNA14 {ECO:0000256|RuleBase:RU369035};
GN ORFNames=P875_00010764 {ECO:0000313|EMBL:KJK64992.1};
OS Aspergillus parasiticus (strain ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1403190 {ECO:0000313|EMBL:KJK64992.1, ECO:0000313|Proteomes:UP000033540};
RN [1] {ECO:0000313|EMBL:KJK64992.1, ECO:0000313|Proteomes:UP000033540}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 56775 / NRRL 5862 / SRRC 143 / SU-1
RC {ECO:0000313|Proteomes:UP000033540};
RA Yu J., Fedorova N., Yin Y., Losada L., Zafar N., Taujale R., Ehrlich K.C.,
RA Bhatnagar D., Cleveland T.E., Bennett J.W., Nierman W.C.;
RT "Draft genome sequence of Aspergillus parasiticus SU-1.";
RL Submitted (FEB-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:KJK64992.1}.
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DR EMBL; JZEE01000377; KJK64992.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F0IE46; -.
DR STRING; 1403190.A0A0F0IE46; -.
DR Proteomes; UP000033540; 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 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:UP000033540}.
FT DOMAIN 686..990
FT /note="Suppressor of forked"
FT /evidence="ECO:0000259|Pfam:PF05843"
FT REGION 1..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 222..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 632..663
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 851..951
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..65
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..80
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..117
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..172
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 186..209
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..240
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 856..890
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 896..917
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 918..949
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1014 AA; 113610 MW; 9F6858CF7DD2E955 CRC64;
MAEDDAEKAF FQAQAMNADS VDYKAVEDQG ASSDSDDYDP SKTLQDQYSA SIPDSKPSEI
APSSASPSDP TPPTQSIPPE TDPSQPADSA YPSQTPSRAD SQASASAPAS GTSVPLKTRT
IGGFVVEDED EDDAGDADYE PPAVLGVEDM NTISMNVPQQ PISGNANEDT PTPDVSMDGA
VQASADAKNF PNSSYTPASA AASKSDTPAL LSQDMYNSRT LQSENMQDSA AATPVPDSPS
TSKGRLPHDR VGILEDRIQE DPRGDIPAWL ELINEHRNRN RIDSAREVYE RFLTAFPFSA
EQWVAYATME SELNELYRLE QIFNRTLLTI PDVQLWTVYL DYVRRRNPLT TDTTGQSRRI
ISSAYDLALQ YVGVDKDSGS IWTDYVQFIR SGPGNVGGSG WQDQQKMDLL RKAYQKAICV
PTQAVNNLWK EYDQFEMGLN KLTGRKFLQE QSPAYMTARS SYTELQNITR DLNRTTLPRL
PPVLGSDGDI EFGQQVDIWK RWIKWEKGDP LVLKEEDQAA FKARVIYVYK QALMALRFLP
EIWFEAAEFC FLNDMENEGN EFLKNGIEAN PESCLLAFKR ADRLEITSES EQDPIKRGAK
VREPYDKLLN ALYDLIAKAR TRESQDVARL EETFAKINPD TQPSKTDDDD DDQSDSKARE
SMKNAQIEAL RNAHAIQIGI LSKTVSFAWI ALMRAMRRIQ GKGKPGEMPG SRQVFADARK
RGRITSDVYI ASALIEYHCY KDPAATKIFE RGAKLFPEDE NFALEYLKHL IDINDVINAR
AVFEMTVRKL ASNPENVHKT KPIFAFLHEY ESRYGDLVQV INLENRMREL FPEDPTLEQF
AHRYSSPAFD PTVVRPIISP SQTRPKTAFP TEQPVSRHGT PSSRYPDASV TNSPKRPLED
FDDDMNRPRK FMRADSPLKT TQRRQLDPPK RTQQVISSQT GSQFRSQGSP APLPRDIVYL
LSIIPSASAY NAGRFSPEKL VDLIRRIDMP TSISQIPLPP SVRGLGFPGA YRPQ
//
