ID V2XSI8_MONRO Unreviewed; 339 AA.
AC V2XSI8;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=poly(A)-specific ribonuclease {ECO:0000256|ARBA:ARBA00012161};
DE EC=3.1.13.4 {ECO:0000256|ARBA:ARBA00012161};
GN ORFNames=Moror_12428 {ECO:0000313|EMBL:ESK95816.1};
OS Moniliophthora roreri (strain MCA 2997) (Cocoa frosty pod rot fungus)
OS (Crinipellis roreri).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX NCBI_TaxID=1381753 {ECO:0000313|EMBL:ESK95816.1, ECO:0000313|Proteomes:UP000017559};
RN [1] {ECO:0000313|EMBL:ESK95816.1, ECO:0000313|Proteomes:UP000017559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 2997 {ECO:0000313|EMBL:ESK95816.1,
RC ECO:0000313|Proteomes:UP000017559};
RX PubMed=24571091; DOI=10.1186/1471-2164-15-164;
RA Meinhardt L.W., Costa G.G.L., Thomazella D.P.T., Teixeira P.J.P.L.,
RA Carazzolle M.F., Schuster S.C., Carlson J.E., Guiltinan M.J.,
RA Mieczkowski P., Farmer A., Ramaraj T., Crozier J., Davis R.E., Shao J.,
RA Melnick R.L., Pereira G.A.G., Bailey B.A.;
RT "Genome and secretome analysis of the hemibiotrophic fungal pathogen,
RT Moniliophthora roreri, which causes frosty pod rot disease of cacao:
RT mechanisms of the biotrophic and necrotrophic phases.";
RL BMC Genomics 15:164-164(2014).
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:ESK95816.1}.
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DR EMBL; AWSO01000061; ESK95816.1; -; Genomic_DNA.
DR RefSeq; XP_007844903.1; XM_007846712.1.
DR AlphaFoldDB; V2XSI8; -.
DR STRING; 1381753.V2XSI8; -.
DR KEGG; mrr:Moror_12428; -.
DR HOGENOM; CLU_027974_0_2_1; -.
DR OrthoDB; 341493at2759; -.
DR Proteomes; UP000017559; 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; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000017559};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT REGION 268..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 339 AA; 37892 MW; C2D9561642A929EC CRC64;
MQSQARIREV WGPNLQEELR LLRDVIETHP YVALDTEFPG VVARPIGNFK TQSEYHYQTM
RCNVDLLKII QVGITLSDED GNYSTEGSTW QFNFRFNVND DMAAPESIDL LQKSGIDFAR
HEEMGILPND FAELLITSGM VLTKEITWIS FHSGYDFGYF LRLLTGESLP PTEDGFFEVL
RQWFPINYDV RYLMREVNPS ANKGLLQDFA EELGVLRVGS SHQAGSDSLL ISGAFFKIRE
LYYRDGIDVK SLSGKLFGLG QTTNGLTDSA GRGSATIAER EDRTTTRELH NQTPGPQNQT
VAIGLQLQAG NPIQIPPTQY GPMGANGPPY LRTSLVGGR
//
