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Database: UniProt
Entry: A0A0F0IAU9_ASPPU
LinkDB: A0A0F0IAU9_ASPPU
Original site: A0A0F0IAU9_ASPPU 
ID   A0A0F0IAU9_ASPPU        Unreviewed;       488 AA.
AC   A0A0F0IAU9;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=poly(A)-specific ribonuclease {ECO:0000256|ARBA:ARBA00012161};
DE            EC=3.1.13.4 {ECO:0000256|ARBA:ARBA00012161};
GN   ORFNames=P875_00138364 {ECO:0000313|EMBL:KJK64236.1};
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:KJK64236.1, ECO:0000313|Proteomes:UP000033540};
RN   [1] {ECO:0000313|EMBL:KJK64236.1, 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   -!- CATALYTIC ACTIVITY:
CC       Reaction=Exonucleolytic cleavage of poly(A) to 5'-AMP.; EC=3.1.13.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00001663};
CC   -!- SIMILARITY: Belongs to the CAF1 family.
CC       {ECO:0000256|ARBA:ARBA00008372}.
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:KJK64236.1}.
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DR   EMBL; JZEE01000518; KJK64236.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F0IAU9; -.
DR   STRING; 1403190.A0A0F0IAU9; -.
DR   Proteomes; UP000033540; Unassembled WGS sequence.
DR   GO; GO:0030014; C:CCR4-NOT complex; IEA:InterPro.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0004535; F:poly(A)-specific ribonuclease activity; IEA:UniProtKB-EC.
DR   GO; GO:0006402; P:mRNA catabolic process; IEA:UniProt.
DR   Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR   InterPro; IPR039637; CNOT7/CNOT8/Pop2.
DR   InterPro; IPR006941; RNase_CAF1.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   PANTHER; PTHR10797; CCR4-NOT TRANSCRIPTION COMPLEX SUBUNIT; 1.
DR   PANTHER; PTHR10797:SF0; CCR4-NOT TRANSCRIPTION COMPLEX SUBUNIT 7; 1.
DR   Pfam; PF04857; CAF1; 2.
DR   SUPFAM; SSF53098; Ribonuclease H-like; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000033540};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT   REGION          21..64
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        21..47
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   488 AA;  52477 MW;  84480349CFD8DFC1 CRC64;
     MPPPVGRYGP TGLSAPYTHL QQAHLQQQQQ QPQHHPAHAQ SANTALPPPS LGGHPGFAAG
     NPNTNINPFT LSGTGIANGM SVAGFGGAAD AGGTGLASHA AQLGFARGAQ MQQQQLHQTH
     DGRLALEAKA GAVKTRIRDV WKHNLAQEMA VLRQLVEKYP YISMDTEFPG IVARPIGAFT
     NKADYHYQTL RCNVDLLKMI QLGITLFSAE GEVPPPNATD VNGQPLGNSL VPAPCTWQFN
     FRFSLEDDMY AQESTAMLAK AGIDFSMHDK NGIDPFEFGA LLISSGLVLL DDVHWVSFHS
     GYDFGYLMKI MLCKPLPENE EEFHKLLNIF FPSLYDIKYL MKHAGRNQAV NDTPLTPAAA
     QILTNLGQKS GLQDIADELG VKRVGIAHQA GSDSLVTGEI YWKMRQLVFN GNIDESKYSG
     QIWGLNGQMP ALLYQMPHQT PNLNGATIYS AAGTPSTPNA GTPQHQGLGA LTPGAVGGVL
     GQFQVGKA
//
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