ID   REI1_CHATD              Reviewed;         537 AA.
AC   G0S920;
DT   11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT   11-DEC-2013, sequence version 2.
DT   03-AUG-2022, entry version 39.
DE   RecName: Full=Cytoplasmic 60S subunit biogenesis factor REI1 homolog;
DE   AltName: Full=pre-60S factor REI1 homolog;
GN   ORFNames=CTHT_0044240;
OS   Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX   NCBI_TaxID=759272;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 1495 / CBS 144.50 / IMI 039719;
RX   PubMed=21784248; DOI=10.1016/j.cell.2011.06.039;
RA   Amlacher S., Sarges P., Flemming D., van Noort V., Kunze R., Devos D.P.,
RA   Arumugam M., Bork P., Hurt E.;
RT   "Insight into structure and assembly of the nuclear pore complex by
RT   utilizing the genome of a eukaryotic thermophile.";
RL   Cell 146:277-289(2011).
CC   -!- FUNCTION: Pre-60S-associated factor involved in the cytoplasmic
CC       maturation of the 60S subunit. Involved in the dissociation and
CC       recycling of other late pre-60S factors before newly synthesized large
CC       ribosomal subunits enter translation (By similarity).
CC       {ECO:0000250|UniProtKB:P38344}.
CC   -!- SUBUNIT: Associates with nascent pre-60S particles that have not yet
CC       entered the translating pool, and is released from mature 60S subunits.
CC       {ECO:0000250|UniProtKB:P38344}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P38344}.
CC   -!- SIMILARITY: Belongs to the REI1 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EGS19931.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; GL988043; EGS19931.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; XP_006694816.1; XM_006694753.1.
DR   AlphaFoldDB; G0S920; -.
DR   STRING; 759272.G0S920; -.
DR   EnsemblFungi; EGS19931; EGS19931; CTHT_0044240.
DR   GeneID; 18258462; -.
DR   KEGG; cthr:CTHT_0044240; -.
DR   eggNOG; KOG2785; Eukaryota.
DR   HOGENOM; CLU_018787_1_2_1; -.
DR   OrthoDB; 1383726at2759; -.
DR   Proteomes; UP000008066; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-KW.
DR   InterPro; IPR003604; Matrin/U1-like-C_Znf_C2H2.
DR   InterPro; IPR041661; ZN622/Rei1/Reh1_Znf-C2H2.
DR   InterPro; IPR040025; Znf622/Rei1/Reh1.
DR   InterPro; IPR022755; Znf_C2H2_jaz.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR13182; PTHR13182; 1.
DR   Pfam; PF12756; zf-C2H2_2; 1.
DR   Pfam; PF12171; zf-C2H2_jaz; 1.
DR   SMART; SM00355; ZnF_C2H2; 4.
DR   SMART; SM00451; ZnF_U1; 2.
DR   SUPFAM; SSF57667; SSF57667; 3.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 2.
PE   3: Inferred from homology;
KW   Cytoplasm; Metal-binding; Reference proteome; Repeat; Ribosome biogenesis;
KW   Zinc; Zinc-finger.
FT   CHAIN           1..537
FT                   /note="Cytoplasmic 60S subunit biogenesis factor REI1
FT                   homolog"
FT                   /id="PRO_0000424593"
FT   ZN_FING         18..42
FT                   /note="C2H2-type 1"
FT   ZN_FING         83..107
FT                   /note="C2H2-type 2"
FT   ZN_FING         260..284
FT                   /note="C2H2-type 3"
FT   REGION          101..151
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          163..204
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          312..361
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          382..401
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        180..204
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        322..340
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        341..359
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   537 AA;  61196 MW;  2BB080182EFFA13F CRC64;
     MATIAGSRAP TEVPSHPYTC NTCQVAFRNS ELQRGHMRSD WHRYNLKRRV ASLPPISSEV
     FTEKVLQARA ATTAQADKAG FEKTCEVCQK TYYSENSFRN HLSSTKHKSK AAAAARRPAN
     NKVDDDVSSM SFSLGEPARA DSVVDSEAEE EFSEVVEGIK NASIHDTASP IKRPSAPQPA
     VEEQSKTDAQ MEETPTTTPK PEALTPSATT CVFCNYESPT PQLNASHMER IHGMFIPEKQ
     YLVDLEGLLK HLWEKVFRYN ECLTCGKMKV NVFAIQTHMR DKSHYHIPYT TEEEQLEIGE
     FYDFRSTYSD GDWETEEEDK GEEDGGVRLG AKRESKVVDE NGDEVMEDEE GWETDSDASS
     LDTDDLHAVP AEGHYHQYER LGKHPHHSRE NKKAHREADG IHAPSKRTHA VYYDEYELHL
     PSGKSVGHRS LARYYRQNLY HYPTPEERAE RLAIEAAERE NRMDVDGEEP ERGRTRTRAL
     VPRDIKGLGV TTMSDPRVRG IVQKGKKEEW KNRDSKWWMH SQVAIKEKAK HPSTYLR