GenomeNet

Database: UniProt
Entry: A0A401L137_ASPAW
LinkDB: A0A401L137_ASPAW
Original site: A0A401L137_ASPAW 
ID   A0A401L137_ASPAW        Unreviewed;       782 AA.
AC   A0A401L137;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Exosome complex exonuclease rrp6 {ECO:0000313|EMBL:GCB25172.1};
GN   ORFNames=AAWM_08057 {ECO:0000313|EMBL:GCB25172.1};
OS   Aspergillus awamori (Black koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=105351 {ECO:0000313|EMBL:GCB25172.1, ECO:0000313|Proteomes:UP000286921};
RN   [1] {ECO:0000313|EMBL:GCB25172.1, ECO:0000313|Proteomes:UP000286921}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IFM 58123 {ECO:0000313|EMBL:GCB25172.1,
RC   ECO:0000313|Proteomes:UP000286921};
RA   Kusuya Y., Shimizu M., Takahashi H., Yaguchi T.;
RT   "Aspergillus awamori IFM 58123T.";
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the exosome component 10/RRP6 family.
CC       {ECO:0000256|ARBA:ARBA00043957}.
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:GCB25172.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BDHI01000021; GCB25172.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A401L137; -.
DR   STRING; 105351.A0A401L137; -.
DR   Proteomes; UP000286921; Unassembled WGS sequence.
DR   GO; GO:0000176; C:nuclear exosome (RNase complex); IEA:InterPro.
DR   GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR   GO; GO:0000175; F:3'-5'-RNA exonuclease activity; IEA:InterPro.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0000467; P:exonucleolytic trimming to generate mature 3'-end of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IEA:InterPro.
DR   CDD; cd06147; Rrp6p_like_exo; 1.
DR   Gene3D; 1.10.150.80; HRDC domain; 1.
DR   Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR   InterPro; IPR002562; 3'-5'_exonuclease_dom.
DR   InterPro; IPR012588; Exosome-assoc_fac_Rrp6_N.
DR   InterPro; IPR010997; HRDC-like_sf.
DR   InterPro; IPR002121; HRDC_dom.
DR   InterPro; IPR044876; HRDC_dom_sf.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   InterPro; IPR045092; Rrp6-like.
DR   InterPro; IPR049559; Rrp6p-like_exo.
DR   PANTHER; PTHR12124:SF47; EXOSOME COMPONENT 10; 1.
DR   PANTHER; PTHR12124; POLYMYOSITIS/SCLERODERMA AUTOANTIGEN-RELATED; 1.
DR   Pfam; PF01612; DNA_pol_A_exo1; 1.
DR   Pfam; PF00570; HRDC; 1.
DR   Pfam; PF08066; PMC2NT; 1.
DR   SMART; SM00474; 35EXOc; 1.
DR   SMART; SM00341; HRDC; 1.
DR   SUPFAM; SSF47819; HRDC-like; 1.
DR   SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR   PROSITE; PS50967; HRDC; 1.
PE   3: Inferred from homology;
KW   Exonuclease {ECO:0000313|EMBL:GCB25172.1};
KW   Exosome {ECO:0000256|ARBA:ARBA00022835};
KW   Hydrolase {ECO:0000313|EMBL:GCB25172.1};
KW   Nuclease {ECO:0000313|EMBL:GCB25172.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000286921};
KW   rRNA processing {ECO:0000256|ARBA:ARBA00022552}.
FT   DOMAIN          450..530
FT                   /note="HRDC"
FT                   /evidence="ECO:0000259|PROSITE:PS50967"
FT   REGION          542..568
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          607..782
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        637..667
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        668..685
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        687..716
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        734..748
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   782 AA;  87144 MW;  8EA51E7306CF486E CRC64;
     MDSTADFGSL QQRVQSSLMQ VTRTAGQLSA EDLDFHRTSN AEVSDSLDEQ SNRLLSLTSS
     ILKAATAGTD VSAPTLDEED SLEDNWRGVV DVIDALLEKA DACLDEFTGV IKKLSPSQQD
     QAAAAAAKAS KKQPAKFPTI YDYGPSKIPK PQLLFERKAD NTDTAPFKPL LKTKPHAVVP
     LKDSLKLSDS AVGYVNPYEK EIRAAKFPTS SYSVSPPVDY QPWESTKATF VDTLEGVKEM
     LEELKAAKEI AIDLEHHDVH SYQGLVSLMQ ISTRDKDWVV DTLKPWREEL QVLNEVFTDP
     NILKVLHGSS MDIIWLQRDL GLYVVGMFDT YHAACALNYP KRSLKFLLQK FVNFEADKRY
     QMADWRIRPI PEGMFDYARS DTHYLLHIYD HIRNELVENS LPDNNLIDYV LEQSKKEALQ
     VYERPVYDAA TGQGPGGWYD LLSRNSVVVN REQFAVFKAV HQWRDEVARE EDEGVQCVFP
     KHVLFRVAHT MPLDLGTLFR TLSPVTPIVQ NRAVDLLEVI KKAKDEGADG PEWRDVYVKP
     TRGTPAAPAT QPVDVPSPTP ADEANLPTVS RYEVSQFWGS VLESQEPPTV PAYSAVASAE
     ALRLSLPLPP MPKTVSEARE KLAPAQPQTP KPATSAPAAK EEKKEDENKY FTVKEMGGPR
     KRKAAPAETA EQSQSASSEF DTTDASSSLD TEDKPSKKQR RKEKKDKSAA QSETAAKEDG
     EEEEEEAPFN YESAASVFNA NPKATSGLPS RRRYNPYAKV LDAPSGVRKQ KRETAGKAFT
     FR
//
DBGET integrated database retrieval system