ID A0A0A2KFJ9_PENIT Unreviewed; 294 AA.
AC A0A0A2KFJ9;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=RNA exonuclease 4 {ECO:0000256|ARBA:ARBA00016937};
GN ORFNames=PITC_008090 {ECO:0000313|EMBL:KGO65693.1};
OS Penicillium italicum (Blue mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=40296 {ECO:0000313|EMBL:KGO65693.1, ECO:0000313|Proteomes:UP000030104};
RN [1] {ECO:0000313|EMBL:KGO65693.1, ECO:0000313|Proteomes:UP000030104}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHI-1 {ECO:0000313|EMBL:KGO65693.1,
RC ECO:0000313|Proteomes:UP000030104};
RX PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome, transcriptome, and functional analyses of Penicillium expansum
RT provide new insights into secondary metabolism and pathogenicity.";
RL Mol. Plant Microbe Interact. 28:232-248(2015).
CC -!- FUNCTION: Exoribonuclease involved in ribosome biosynthesis. Involved
CC in the processing of ITS1, the internal transcribed spacer localized
CC between the 18S and 5.8S rRNAs. {ECO:0000256|ARBA:ARBA00025599}.
CC -!- SIMILARITY: Belongs to the REXO4 family.
CC {ECO:0000256|ARBA:ARBA00010489}.
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:KGO65693.1}.
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DR EMBL; JQGA01001486; KGO65693.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A2KFJ9; -.
DR STRING; 40296.A0A0A2KFJ9; -.
DR HOGENOM; CLU_022453_2_1_1; -.
DR OMA; SQKEMRF; -.
DR OrthoDB; 5479236at2759; -.
DR PhylomeDB; A0A0A2KFJ9; -.
DR Proteomes; UP000030104; Unassembled WGS sequence.
DR GO; GO:0008408; F:3'-5' exonuclease activity; IEA:InterPro.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006364; P:rRNA processing; IEA:InterPro.
DR CDD; cd06144; REX4_like; 1.
DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR InterPro; IPR013520; Exonuclease_RNaseT/DNA_pol3.
DR InterPro; IPR037431; REX4_DEDDh_dom.
DR InterPro; IPR047021; REXO1/3/4-like.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR PANTHER; PTHR12801:SF45; RNA EXONUCLEASE 4; 1.
DR PANTHER; PTHR12801; RNA EXONUCLEASE REXO1 / RECO3 FAMILY MEMBER-RELATED; 1.
DR Pfam; PF00929; RNase_T; 1.
DR SMART; SM00479; EXOIII; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
PE 3: Inferred from homology;
KW Exonuclease {ECO:0000313|EMBL:KGO65693.1};
KW Hydrolase {ECO:0000313|EMBL:KGO65693.1};
KW Nuclease {ECO:0000313|EMBL:KGO65693.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000030104}.
FT DOMAIN 99..261
FT /note="Exonuclease"
FT /evidence="ECO:0000259|SMART:SM00479"
FT REGION 1..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 269..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..93
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 294 AA; 33233 MW; A964C10FC7E3B93E CRC64;
MDKTALSSNW KKLQATFKKD PTVKRKPSDL ESGDGIVKKR KLTEKQKPYN QDAKPTLKRK
RMSDKKETGD SADASAPKIE TSSRHKENEG RSSSAELGKY VAMDCEMVGV GPNPDNDSAL
ARVSVVNFNG DQIYDSYVRP KEMVTDWRTH VSGIAPKHMV EARTLEHVQK EIADIMKDRI
LVGHAVSNDL DALLLSHPKR DIRDTSKHAP YRRIAGGGSP RLKMLAEEFL GITIQEGAHS
SVEDARATMA LYRREKDAFE REHLKKWPAR MLADTREKGE GQKKKKKKKT TRKR
//
