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Database: UniProt
Entry: A0A2K5XRR3_MANLE
LinkDB: A0A2K5XRR3_MANLE
Original site: A0A2K5XRR3_MANLE 
ID   A0A2K5XRR3_MANLE        Unreviewed;       860 AA.
AC   A0A2K5XRR3;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   SubName: Full=Exosome component 10 {ECO:0000313|Ensembl:ENSMLEP00000005981.1};
GN   Name=EXOSC10 {ECO:0000313|Ensembl:ENSMLEP00000005981.1};
OS   Mandrillus leucophaeus (Drill) (Papio leucophaeus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Mandrillus.
OX   NCBI_TaxID=9568 {ECO:0000313|Ensembl:ENSMLEP00000005981.1, ECO:0000313|Proteomes:UP000233140};
RN   [1] {ECO:0000313|Ensembl:ENSMLEP00000005981.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC       {ECO:0000256|ARBA:ARBA00004604}.
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DR   AlphaFoldDB; A0A2K5XRR3; -.
DR   Ensembl; ENSMLET00000028060.1; ENSMLEP00000005981.1; ENSMLEG00000025160.1.
DR   GeneTree; ENSGT00390000015408; -.
DR   OMA; MNCKEFA; -.
DR   Proteomes; UP000233140; Unplaced.
DR   GO; GO:0000176; C:nuclear exosome (RNase complex); IEA:InterPro.
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   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   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Exosome {ECO:0000256|ARBA:ARBA00022835};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233140};
KW   rRNA processing {ECO:0000256|ARBA:ARBA00022552}.
FT   DOMAIN          503..583
FT                   /note="HRDC"
FT                   /evidence="ECO:0000259|PROSITE:PS50967"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          210..233
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          750..860
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          711..745
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        215..233
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        750..789
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        800..821
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   860 AA;  98214 MW;  5C85B0302D26B2D7 CRC64;
     MAPPSTREPR VQSATSATKP DGEMVLPGFP DADSFVKFAL GSVVAVTKAS GGLPQFGDEY
     DFYRSFPGFQ AFCETQGDRL LQCMSRVMQY HGCRSNIKDR SKVTELEDKF DLLVDANDVI
     LERVGILLDE ASGVNKNQQP VLPAGLQVPK TVVSSWNRKA AEYGKKAKSE TFRLLHAKNI
     IRPQLKFREK IDNSNTPFLP KIFIKPNAQK PLPQALSKER RERPQDRPED LDVPPALADF
     IHQQRTQQVE QDMFAHPYQY ELNHFTPPDS VFQKPQPQLY RPIEETPCHF ISSLDELVEL
     NEKLLNCQEF AVDLEHHSYR SFLGLTCLMQ ISTRTEDFII DTLELRSDMY ILNESLTDPA
     IVKVFHGADS DIEWLQKDFG LYVVNMFDTH QAARLLNLGR HSLDHLLKLY CNVDSNKQYQ
     LADWRIRPLP EEMLSYARDD THYLLYIYDK MRLELWERGN GQPVQLQVVW QRSRDICLKK
     FIKPIFTDES YLELYRKQKK HLNTQQLTAF QLLFAWRDKT ARREDESYGY VLPNHMMLKI
     AEELPKEPQG IIACCNPVPP LVRQQINEMH LLIQQAREMP LLKSEVAAGV KKSGPLPSAE
     RLENVLFGPH DCSHAPPDGY PIIPTNGSVP VQKQASLFPE EKEDNLLGTT CLIATAVITL
     FNEPSAEDNK KGPLTIAQKK AQNIMESFEN PFRMISNRWK LAQVQVQKDS KETVKKKAAE
     QTAAREQAKE ACKAAAEQAV SVRQQVALEN AAKKRERATS DPRTTEQKQE KKRLKISKKP
     KDLEPPEKEF TPYDYSQSDF KAFAGNSKSK AASQFDPNKQ TPSGKKCIAA KKIKQSVGNK
     SMSFPTGKSD RGFRYNWPQR
//
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