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Database: UniProt
Entry: Q0CHU1_ASPTN
LinkDB: Q0CHU1_ASPTN
Original site: Q0CHU1_ASPTN 
ID   Q0CHU1_ASPTN            Unreviewed;       510 AA.
AC   Q0CHU1;
DT   17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   17-OCT-2006, sequence version 1.
DT   22-FEB-2023, entry version 75.
DE   RecName: Full=RNA exonuclease 4 {ECO:0000256|ARBA:ARBA00016937};
GN   ORFNames=ATEG_06743 {ECO:0000313|EMBL:EAU33287.1};
OS   Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=341663 {ECO:0000313|EMBL:EAU33287.1, ECO:0000313|Proteomes:UP000007963};
RN   [1] {ECO:0000313|Proteomes:UP000007963}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIH 2624 / FGSC A1156 {ECO:0000313|Proteomes:UP000007963};
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA   Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA   Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA   Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA   Nierman W.C., Milne T., Madden K.;
RT   "Annotation of the Aspergillus terreus NIH2624 genome.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; CH476602; EAU33287.1; -; Genomic_DNA.
DR   RefSeq; XP_001215921.1; XM_001215921.1.
DR   AlphaFoldDB; Q0CHU1; -.
DR   STRING; 341663.Q0CHU1; -.
DR   EnsemblFungi; EAU33287; EAU33287; ATEG_06743.
DR   GeneID; 4322294; -.
DR   VEuPathDB; FungiDB:ATEG_06743; -.
DR   eggNOG; KOG2249; Eukaryota.
DR   HOGENOM; CLU_038378_1_0_1; -.
DR   OMA; HETMPAS; -.
DR   OrthoDB; 5479236at2759; -.
DR   Proteomes; UP000007963; Unassembled WGS sequence.
DR   GO; GO:0032299; C:ribonuclease H2 complex; IEA:InterPro.
DR   GO; GO:0008408; F:3'-5' exonuclease activity; IEA:InterPro.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0006401; P:RNA catabolic process; IEA:InterPro.
DR   GO; GO:0006364; P:rRNA processing; IEA:InterPro.
DR   CDD; cd06144; REX4_like; 1.
DR   CDD; cd09271; RNase_H2-C; 1.
DR   Gene3D; 2.40.128.680; -; 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; IPR013924; RNase_H2_suC.
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; PF08615; RNase_H2_suC; 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:EAU33287.1};
KW   Hydrolase {ECO:0000313|EMBL:EAU33287.1};
KW   Nuclease {ECO:0000313|EMBL:EAU33287.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007963}.
FT   DOMAIN          118..280
FT                   /note="Exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00479"
FT   REGION          1..109
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          292..323
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        13..79
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        80..97
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   510 AA;  57353 MW;  30E7353C0CD1F49A CRC64;
     MDLKNLSSNW KKLQETLKKE SVSTSTKRKT ADREPQNGAV KKRKTEALQG KTKYEQAREI
     KKRKRMSEVS SEDRGNGVQE TEVKSVSRKS STATLAVRAE PKTAKVNEGR SKTAELGKYV
     AMDCEMVGVG PNPDHDSALA RVSIVNFNGE QVYDSFVRPK EMVTDWRTHV SGILPRHMAE
     ARTLEQVQKE VAEIIDGRIL VGHALRNDLD ALLLSHPKRD IRDTSKYPPY RKVAGGGSPR
     LKVLASEFLG LDIQGGAHSS VEDAKATMLL YRRDKDGFER EHAKKWPVRV VVEKEKGDDQ
     KKKKKKKKKT RKRQDMVPTP LSNKLSTIEP PMIKLNYAHI AYFVISDNSF SNWTTAMFAL
     QRPSQSSDST CPDKCTPNIL PCRVHHDGPV NSVDRFWIPV PDEKDKALQT AHFRGRKLRG
     RHVAVPEGYQ GVVAALTERV IPSKPAENDD SAPEEPIKIL EQQSTFKEVV VWGHETMPAS
     DDPFVKGVEE WIKLAEAMHI QPSSEKQPST
//
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