MRT4_CHATD
ID MRT4_CHATD Reviewed; 270 AA.
AC G0S616;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 29-OCT-2014, sequence version 2.
DT 25-MAY-2022, entry version 36.
DE RecName: Full=Ribosome assembly factor mrt4 {ECO:0000250|UniProtKB:P33201};
DE AltName: Full=mRNA turnover protein 4 {ECO:0000250|UniProtKB:P33201};
GN ORFNames=CTHT_0025680 {ECO:0000312|EMBL:EGS20732.1};
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).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS), IDENTIFICATION OF FRAMESHIFT, AND
RP SEQUENCE REVISION TO 13; 139; 228 AND 259.
RX PubMed=24662372; DOI=10.1038/ncomms4491;
RA Leidig C., Thoms M., Holdermann I., Bradatsch B., Berninghausen O.,
RA Bange G., Sinning I., Hurt E., Beckmann R.;
RT "60S ribosome biogenesis requires rotation of the 5S ribonucleoprotein
RT particle.";
RL Nat. Commun. 5:3491-3491(2014).
CC -!- FUNCTION: Component of the ribosome assembly machinery. Nuclear paralog
CC of the ribosomal protein P0, it binds pre-60S subunits at an early
CC stage of assembly in the nucleolus, and is replaced by P0 in
CC cytoplasmic pre-60S subunits and mature 80S ribosomes.
CC {ECO:0000250|UniProtKB:P33201}.
CC -!- SUBUNIT: Associates with the pre-60S ribosomal particle.
CC {ECO:0000250|UniProtKB:P33201}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:P33201}. Cytoplasm
CC {ECO:0000250|UniProtKB:P33201}. Note=Shuttles between the nucleus and
CC the cytoplasm. {ECO:0000250|UniProtKB:P33201}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL10 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EGS20732.1; Type=Erroneous gene model prediction; Evidence={ECO:0000303|PubMed:24662372, ECO:0000305};
CC Sequence=EGS20732.1; Type=Frameshift; Evidence={ECO:0000303|PubMed:24662372, ECO:0000305};
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DR EMBL; GL988041; EGS20732.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_006693028.1; XM_006692965.1.
DR PDB; 4NWB; X-ray; 1.80 A; A=1-270.
DR PDBsum; 4NWB; -.
DR AlphaFoldDB; G0S616; -.
DR SMR; G0S616; -.
DR STRING; 759272.G0S616; -.
DR EnsemblFungi; EGS20732; EGS20732; CTHT_0025680.
DR GeneID; 18256606; -.
DR KEGG; cthr:CTHT_0025680; -.
DR HOGENOM; CLU_071690_3_0_1; -.
DR OrthoDB; 1181992at2759; -.
DR Proteomes; UP000008066; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0000027; P:ribosomal large subunit assembly; IEA:InterPro.
DR CDD; cd05796; Ribosomal_P0_like; 1.
DR Gene3D; 3.30.70.1730; -; 1.
DR Gene3D; 3.90.105.20; -; 1.
DR InterPro; IPR033867; Mrt4.
DR InterPro; IPR043141; Ribosomal_L10-like_sf.
DR InterPro; IPR001790; Ribosomal_L10P.
DR InterPro; IPR043164; RL10_insert_sf.
DR InterPro; IPR040637; RL10P_insert.
DR Pfam; PF00466; Ribosomal_L10; 1.
DR Pfam; PF17777; RL10P_insert; 1.
DR SUPFAM; SSF160369; SSF160369; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Nucleus; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein.
FT CHAIN 1..270
FT /note="Ribosome assembly factor mrt4"
FT /id="PRO_0000430590"
FT REGION 234..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..258
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 13
FT /note="T -> I (in Ref. 1; EGS20732)"
FT CONFLICT 139
FT /note="P -> T (in Ref. 1; EGS20732)"
FT CONFLICT 228
FT /note="S -> N (in Ref. 1; EGS20732)"
FT CONFLICT 259
FT /note="M -> I (in Ref. 1; EGS20732)"
FT HELIX 8..15
FT /evidence="ECO:0007829|PDB:4NWB"
FT HELIX 26..33
FT /evidence="ECO:0007829|PDB:4NWB"
FT HELIX 34..36
FT /evidence="ECO:0007829|PDB:4NWB"
FT STRAND 38..47
FT /evidence="ECO:0007829|PDB:4NWB"
FT HELIX 50..59
FT /evidence="ECO:0007829|PDB:4NWB"
FT TURN 60..62
FT /evidence="ECO:0007829|PDB:4NWB"
FT STRAND 63..66
FT /evidence="ECO:0007829|PDB:4NWB"
FT HELIX 70..77
FT /evidence="ECO:0007829|PDB:4NWB"
FT TURN 81..83
FT /evidence="ECO:0007829|PDB:4NWB"
FT HELIX 89..95
FT /evidence="ECO:0007829|PDB:4NWB"
FT STRAND 98..107
FT /evidence="ECO:0007829|PDB:4NWB"
FT HELIX 109..118
FT /evidence="ECO:0007829|PDB:4NWB"
FT STRAND 121..123
FT /evidence="ECO:0007829|PDB:4NWB"
FT STRAND 135..137
FT /evidence="ECO:0007829|PDB:4NWB"
FT STRAND 139..141
FT /evidence="ECO:0007829|PDB:4NWB"
FT TURN 144..147
FT /evidence="ECO:0007829|PDB:4NWB"
FT HELIX 151..153
FT /evidence="ECO:0007829|PDB:4NWB"
FT HELIX 159..161
FT /evidence="ECO:0007829|PDB:4NWB"
FT HELIX 162..167
FT /evidence="ECO:0007829|PDB:4NWB"
FT STRAND 172..175
FT /evidence="ECO:0007829|PDB:4NWB"
FT STRAND 178..181
FT /evidence="ECO:0007829|PDB:4NWB"
FT STRAND 192..195
FT /evidence="ECO:0007829|PDB:4NWB"
FT HELIX 203..211
FT /evidence="ECO:0007829|PDB:4NWB"
FT STRAND 217..228
FT /evidence="ECO:0007829|PDB:4NWB"
FT TURN 229..231
FT /evidence="ECO:0007829|PDB:4NWB"
FT STRAND 234..236
FT /evidence="ECO:0007829|PDB:4NWB"
FT HELIX 238..241
FT /evidence="ECO:0007829|PDB:4NWB"
SQ SEQUENCE 270 AA; 30480 MW; 2458BF4ED266B410 CRC64;
MPKSKRARVY HLTQVNKKGR EAKERLFSNI RETIPKYQHC FVFSVDNMRN NYLKDVRHEL
NDCRIFFGKT KLMARALGTT PEEEQADGLH RLTRYLTGTV GLLFTNRDPA DIESYFSNLS
QVDFARAGTV APRTVTVPPG IVYSTGGEVP PEHDVPVSHT LEPELRRLGM PVRMIKGKVC
LGDEKGEASE GYTICKEGEV LDSRQTRLLK LFSICLSEFK VSLLGYWSSA SGEVTELEAG
KTRPKREGNR RQAMNGDEMD EDQSSDEDSD