ID   ZCHC8_XENLA             Reviewed;         743 AA.
AC   Q6DD45;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=Zinc finger CCHC domain-containing protein 8;
DE   AltName: Full=TRAMP-like complex RNA-binding factor ZCCHC8;
GN   Name=zcchc8;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Scaffolding subunit of the trimeric nuclear exosome targeting
CC       (NEXT) complex that is involved in the surveillance and turnover of
CC       aberrant transcripts and non-coding RNAs. NEXT functions as an RNA
CC       exosome cofactor that directs a subset of non-coding short-lived RNAs
CC       for exosomal degradation. May be involved in pre-mRNA splicing. It is
CC       required for 3'-end maturation of telomerase RNA component (TERC), TERC
CC       3'-end targeting to the nuclear RNA exosome, and for telomerase
CC       function. {ECO:0000250|UniProtKB:Q6NZY4}.
CC   -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC       {ECO:0000250|UniProtKB:Q6NZY4}. Note=Excluded from nucleolus.
CC       {ECO:0000250|UniProtKB:Q6NZY4}.
CC   -!- SIMILARITY: Belongs to the ZCCHC8 family. {ECO:0000305}.
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DR   EMBL; BC077784; AAH77784.1; -; mRNA.
DR   RefSeq; NP_001086929.1; NM_001093460.1.
DR   AlphaFoldDB; Q6DD45; -.
DR   SMR; Q6DD45; -.
DR   GeneID; 446764; -.
DR   KEGG; xla:446764; -.
DR   CTD; 446764; -.
DR   Xenbase; XB-GENE-977405; zcchc8.L.
DR   Proteomes; UP000186698; Chromosome 1L.
DR   Bgee; 446764; Expressed in blastula and 19 other tissues.
DR   GO; GO:0005654; C:nucleoplasm; ISS:UniProtKB.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0034470; P:ncRNA processing; ISS:UniProtKB.
DR   InterPro; IPR006568; PSP_pro-rich.
DR   InterPro; IPR001878; Znf_CCHC.
DR   InterPro; IPR036875; Znf_CCHC_sf.
DR   Pfam; PF04046; PSP; 1.
DR   Pfam; PF00098; zf-CCHC; 1.
DR   SMART; SM00581; PSP; 1.
DR   SMART; SM00343; ZnF_C2HC; 1.
DR   SUPFAM; SSF57756; SSF57756; 1.
DR   PROSITE; PS50158; ZF_CCHC; 1.
PE   2: Evidence at transcript level;
KW   Coiled coil; Metal-binding; Nucleus; Reference proteome; Zinc; Zinc-finger.
FT   CHAIN           1..743
FT                   /note="Zinc finger CCHC domain-containing protein 8"
FT                   /id="PRO_0000150964"
FT   ZN_FING         213..230
FT                   /note="CCHC-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT   REGION          390..432
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          449..518
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          540..566
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          600..649
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          662..700
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          29..67
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        393..431
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        455..509
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        662..681
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   743 AA;  82944 MW;  A09876C016CCF491 CRC64;
     MAEVDFGDTE LFEQLDGDLP ASSVHVRFDS EGEANDVQEL VSQHEETINR LSAENQELKR
     RLSLLNRPSG LPVEDKLDGP LLQILFMNHI ISKQYHQEIE EFITSLFQKY EEHRKSNSEK
     TSFNIKPQPS SILLEENDDS DADTMKNIKQ AFSVVGSVQY FKNFCLDKLG QPLLNENPQL
     TEGWDIPKYQ QVFTQIVSLD GQEIQVKAKR PKPCCFNCGS EEHQMRDCPK PRDQAHINMK
     RKEFLDACGE AGNQNQQRYH AEEVEERFGK YKPGVISEEL QEALGIMDKN LPPFIYRMRE
     LGYPPGWLKE AELENSGLSL YDGKERLDAS DGEIEDRDTE AKKHVSYDVS KLVNYPGFNI
     SAPPDMFDEW QMFGSIPMQQ AHQKDIFANY LTDSFPPGSS NKSNKRSSCQ SSSSERKRQK
     TSGNHTVTSA VMDMDMESDE DMYHSRASKG YMFHPPLPPG SPSYGTPPPL PRGTPPSTPP
     NFIPPPPPTP TPPPLPKGTP PPTPNRDSPK VPPQVLDEDT WTLEELEEKQ RLLWAQLDNG
     ESTNSDCDAH TPITVSSVTS SPSRTELDIA TGRKAAPRQT AHELKSPCVI TKLFVAEPEE
     GGPLIPEEGG PLIPEEGGPL IPEEGGPLIP EEGGPLIPEE DSETNEDSNE CYVVEGNDIE
     VNKLSSKHEN ASEKNPSDED ATEEAACVEP SPKRSGVPDV SKFAEGITPF EYDNMSDSTG
     VYLRLRGLLK NSPRNVQKSK KQV