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Database: UniProt
Entry: A0A2T4BYC0_TRILO
LinkDB: A0A2T4BYC0_TRILO
Original site: A0A2T4BYC0_TRILO 
ID   A0A2T4BYC0_TRILO        Unreviewed;       491 AA.
AC   A0A2T4BYC0;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=poly(A)-specific ribonuclease {ECO:0000256|ARBA:ARBA00012161};
DE            EC=3.1.13.4 {ECO:0000256|ARBA:ARBA00012161};
GN   ORFNames=M440DRAFT_1338128 {ECO:0000313|EMBL:PTB74226.1};
OS   Trichoderma longibrachiatum ATCC 18648.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=983965 {ECO:0000313|EMBL:PTB74226.1, ECO:0000313|Proteomes:UP000240760};
RN   [1] {ECO:0000313|EMBL:PTB74226.1, ECO:0000313|Proteomes:UP000240760}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 18648 {ECO:0000313|EMBL:PTB74226.1,
RC   ECO:0000313|Proteomes:UP000240760};
RG   DOE Joint Genome Institute;
RA   Aerts A., Atanasova L., Chenthamara K., Zhang J., Grujic M., Henrissat B.,
RA   Kuo A., Salamov A., Lipzen A., Labutti K., Barry K., Miao Y., Rahimi M.J.,
RA   Shen Q., Grigoriev I.V., Kubicek C.P., Druzhinina I.S.;
RT   "Multiple horizontal gene transfer events from other fungi enriched the
RT   ability of initially mycotrophic Trichoderma (Ascomycota) to feed on dead
RT   plant biomass.";
RL   Submitted (JUL-2016) 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}.
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DR   EMBL; KZ679136; PTB74226.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T4BYC0; -.
DR   STRING; 983965.A0A2T4BYC0; -.
DR   Proteomes; UP000240760; Unassembled WGS sequence.
DR   GO; GO:0030014; C:CCR4-NOT complex; IEA:InterPro.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:UP000240760};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT   REGION          1..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          426..468
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        431..468
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   491 AA;  53433 MW;  F0028E090111A9AF CRC64;
     MPPQLRAFGG GPGVGAPFHQ PGFPSHGQPQ GGPLGNQYLN ANAQLNPFTP NNINSFNAAA
     LNGAAGFPDT GFGSQSARMG FAHGPNAAAA ALQQPQQQHG GQVQHNALMD HPTMRTQQSN
     KGRIREVWKH NLEEEMAVLR DIIDKYPYVA MDTEFPGVVA RPMGGFRGKS DYHYQCLRTN
     VDMLKVIQIG ITLFNEDGET PPARPGPELG LSPATRRHIG QGPFPYSWQF NFKFSLKDDM
     YNEKSIESLQ QAGIDFNLLE RDGIDPHQFA SLLIPSGLVC FDNVRWISFH GGYDFGYLTK
     LLICTPLPND EVDFDHKMKL YFPKTYDVKH LMKYAIRLHN SGMLTPSDPG TAEILQKFEH
     KSGLENIAET LKIKRIGSAH QAGSDSLLTG KVFFQMRDRI FNGEIPDDHL GKVWGLGIPD
     IGLPMSMMGQ GGDQNGGQNG NTPSTPNTGP AHLATTPAQN HNTNGMPNMG PMTPGGGGGV
     FGNFAFGGNG R
//
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