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Database: UniProt
Entry: A0A0F8VUE0_9EURO
LinkDB: A0A0F8VUE0_9EURO
Original site: A0A0F8VUE0_9EURO 
ID   A0A0F8VUE0_9EURO        Unreviewed;      1021 AA.
AC   A0A0F8VUE0;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=mRNA 3'-end-processing protein RNA14 {ECO:0000256|RuleBase:RU369035};
GN   ORFNames=ARAM_003500 {ECO:0000313|EMBL:KKK26866.1};
OS   Aspergillus rambellii.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=308745 {ECO:0000313|EMBL:KKK26866.1, ECO:0000313|Proteomes:UP000034291};
RN   [1] {ECO:0000313|EMBL:KKK26866.1, ECO:0000313|Proteomes:UP000034291}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SRRC1468 {ECO:0000313|EMBL:KKK26866.1,
RC   ECO:0000313|Proteomes:UP000034291};
RA   Moore G.G., Beltz S.B., Mack B.M.;
RT   "Draft Genome Sequences of Two Closely-Related Aflatoxigenic Aspergillus
RT   Species Obtained from the Cote d'Ivoire.";
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:KKK26866.1}.
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DR   EMBL; JZBS01000210; KKK26866.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F8VUE0; -.
DR   STRING; 308745.A0A0F8VUE0; -.
DR   OrthoDB; 23291at2759; -.
DR   Proteomes; UP000034291; 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; 6.
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:UP000034291}.
FT   DOMAIN          684..988
FT                   /note="Suppressor of forked"
FT                   /evidence="ECO:0000259|Pfam:PF05843"
FT   REGION          1..248
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          630..661
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          850..869
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          874..947
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        37..61
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        62..122
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        157..240
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        853..869
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        874..891
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        894..915
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        919..947
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1021 AA;  114836 MW;  22985C4F2D81FB76 CRC64;
     MAEDDAEQAF FQAQAMNADS GDYNGVDEDQ DAYSSDSDEY DPSKTLHDQY SAPEEDFKPS
     ENVSSDSPVS DAQPQTQTSP PQESDPSQQA GNAFPSQTPS PPESQASMSV PVLGTSVQPK
     TRTIGGFVVE DEDEDDTGDA DYEPPGVLGV EDVNTIPSQP IRGNAIEATS TPDVSLDEAV
     QDSASAKNVP NSSLPSVPVA SKNDGSMSLG QNMYNSRTLQ PENAQDSATA TPTPDSPSTS
     RGRLPHDRIG ILEDRIQEDP RGDIPAWLEL INEHRSRNRI DSCRDVYERF LKVFPFSAEA
     WVAYASMESE LNELFRLEQI FNRTLLTIPA VQLWTVYLDY VRRRNPLTTD TTGQARRIIS
     SAYDLAFKYI GVDKDSGSIW TDYVQFIRSG PGNAGGSGWQ DQQKMDLLRK AYQKAICVPM
     QAVNTLWKEY DQFEMGLNKL TGRKFLQEQS PAYMTARSSF TELQNITRDL VRTTLPRLPP
     VPGSEGDVEF MQQVEIWKRW IKWEKGDPLV LKEEDLAAFK SRVIYVYKQA LMALRFLPEI
     WFEAAEFCFL NDMETEGNDF LKNGIDANPE SCLLAFKRAD RLEITSESEQ DPIKRGAKVR
     EPYDRLLDAL YDLIAKARTR ENQDVARLEE TFAKFNPEKQ QTRNDDDDDN QSESKARESV
     KNAQIEAVRN AHAIQIGILS KTISFSWIGL MRAMRRIQGK GKPGEMPGSR QIFADARKKG
     RITSDVYIAS ALIEYHCYKD PAATKIFERG AKLFPDDENF ALEYLKHLID INDVINARAV
     FEMTVRKLAS NPENVQKTKP IFAFLHEYES RYGDLIQVIN LENRMRELFP DDPTLEQFSH
     RFAAPSFDPT AIRPIISPSQ TRPKSAYPQE QIISRHGTPT SRYQEASVTN SPKRPLEDFD
     DDITRPRKFV RAESPLKTAQ RRQIDQQKRT QPMTGTQTGS QYRSQGSAAP LPRDIVYLLS
     IIPPASTYTA GRFSPEKMVD LIRRIDMPTS ISQIPLPQSA RGLGTGQTTI GGQTFSGTYR
     S
//
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