ID   A0A165HI39_9APHY        Unreviewed;       886 AA.
AC   A0A165HI39;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=HRDC domain-containing protein {ECO:0000259|PROSITE:PS50967};
GN   ORFNames=LAESUDRAFT_733747 {ECO:0000313|EMBL:KZT11760.1};
OS   Laetiporus sulphureus 93-53.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Laetiporus.
OX   NCBI_TaxID=1314785 {ECO:0000313|EMBL:KZT11760.1, ECO:0000313|Proteomes:UP000076871};
RN   [1] {ECO:0000313|EMBL:KZT11760.1, ECO:0000313|Proteomes:UP000076871}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-53 {ECO:0000313|EMBL:KZT11760.1,
RC   ECO:0000313|Proteomes:UP000076871};
RX   PubMed=26659563; DOI=10.1093/molbev/msv337;
RA   Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA   Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA   Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA   Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT   "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT   Insights into the Origins of Lignocellulose Decay Capabilities.";
RL   Mol. Biol. Evol. 33:959-970(2016).
CC   -!- SIMILARITY: Belongs to the exosome component 10/RRP6 family.
CC       {ECO:0000256|ARBA:ARBA00043957}.
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DR   EMBL; KV427606; KZT11760.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A165HI39; -.
DR   STRING; 1314785.A0A165HI39; -.
DR   InParanoid; A0A165HI39; -.
DR   OrthoDB; 2880475at2759; -.
DR   Proteomes; UP000076871; 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   SUPFAM; SSF47819; HRDC-like; 1.
DR   SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR   PROSITE; PS50967; HRDC; 1.
PE   3: Inferred from homology;
KW   Exosome {ECO:0000256|ARBA:ARBA00022835};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076871};
KW   rRNA processing {ECO:0000256|ARBA:ARBA00022552}.
FT   DOMAIN          511..591
FT                   /note="HRDC"
FT                   /evidence="ECO:0000259|PROSITE:PS50967"
FT   REGION          128..148
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          428..449
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          834..886
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        428..448
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   886 AA;  96473 MW;  FCB00510B1EA99E2 CRC64;
     MAESSSSSPF TPASFNDYNN SLQTVALTAT KRGAQLPADI SFHRTIDRAF GRELDACSAR
     VLSLTNRLLA LAASVHGSNA KSKGKARLES AEDVLDDFRA LVVDPMDQLL ERADICLDEV
     LGRTKPPAIA VNPTPTTMQK KKAKIPPKGR LDPALQHASH LPKPQLRFAR KVDNSPHTIW
     QPTLQHKYHA QVPLGYNLND AIDVDMDGEG DELSVPSALH PYRYEITHTP YPSHMFAPAE
     PIAPASFDVT PFTWVDTPAH FSAMLERLRD AREIAVDLEY HSYRTFGGFV CLMQLSTREA
     DWVVDTLALR DDMEALNEVF TDPRIVKVLH GAESDIVWLQ QDFNLYIVNL FDTHHASKVL
     DFPRHNLATL LEMYCDFIAD KRYQLADWRI RPLPEEMLAY ARSDTHFLLF IFDNLRNALL
     DRGQSLSSSQ SCAETPSAST SLSGAPTTDP QALIREVLSR SETTALRVYA KEGYDAAGGT
     GPGGWDNLAR KWNKGALMAA AELEGVKDSV YAVQRAVYRC VHTWRDRVAR VEDESTRYVL
     ANHYLFVLAE QPPADMAALL RTLRSVPPVV QRRAKELLGA IRTAVASALA PSTSGSPPAI
     SGDAEFSSGI SALENTAIST ARVAEMPQSI ADDDAAVPSP PMLILSVVIG CCGEGSRKVR
     PAATNKASIA SASASSLFGA TLAPTSGRDS VKEEVRVSYS ATRSALFDER VTSISRTSET
     ARGSRFQEVV ARIHGTLVIA PTMPKLAAIP SKAGAEMVEA VEEAAGSAQI EGQAEIPFIP
     AAQRTSAKME TVDDTIVVVG QARAKKRKRA PPRTAAIEVE SFDYSTASNI LDEGFDGDAA
     EEAGTKKQKK KARQMKGAAG YQYGEFPAPP KALSQPKSGN QSRTFR
//