NLE1_CHATD
ID NLE1_CHATD Reviewed; 517 AA.
AC G0SC29;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 29-OCT-2014, sequence version 2.
DT 25-MAY-2022, entry version 47.
DE RecName: Full=Ribosome assembly protein 4 {ECO:0000250|UniProtKB:P25382};
DE AltName: Full=Notchless protein homolog 1 {ECO:0000250|UniProtKB:Q9VPR4};
DE AltName: Full=Ribosome biogenesis factor RSA4 {ECO:0000250|UniProtKB:Q9VPR4};
GN ORFNames=CTHT_0055700 {ECO:0000312|EMBL:EGS18955.1};
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) OF 33-517.
RX PubMed=25404745; DOI=10.1083/jcb.201408111;
RA Bassler J., Paternoga H., Holdermann I., Thoms M., Granneman S.,
RA Barrio-Garcia C., Nyarko A., Lee W., Stier G., Clark S.A., Schraivogel D.,
RA Kallas M., Beckmann R., Tollervey D., Barbar E., Sinning I., Hurt E.;
RT "A network of assembly factors is involved in remodeling rRNA elements
RT during preribosome maturation.";
RL J. Cell Biol. 207:481-498(2014).
RN [3]
RP ERRATUM OF PUBMED:25404745.
RX PubMed=26150393; DOI=10.1083/jcb.20140811106112015c;
RA Bassler J., Paternoga H., Holdermann I., Thoms M., Granneman S.,
RA Barrio-Garcia C., Nyarko A., Lee W., Stier G., Clark S.A., Schraivogel D.,
RA Kallas M., Beckmann R., Tollervey D., Barbar E., Sinning I., Hurt E.;
RL J. Cell Biol. 210:169-170(2015).
CC -!- FUNCTION: Involved in ribosome biogenesis. Required for processing and
CC efficient intra-nuclear transport of pre-60S ribosomal subunits.
CC Interacts with the AAA-ATPase Midasin, which is essential for the ATP-
CC dependent dissociation of a group of nonribosomal factors from the pre-
CC 60S particle. {ECO:0000250|UniProtKB:P25382}.
CC -!- SUBUNIT: Associates with the pre-60S ribosomal particle. Interacts (via
CC WD repeats) with uL18. Interacts (via UBL domain) with MDN1 (via
CC VWFA/MIDAS domain). Interacts (via WD repeats) with NSA2.
CC {ECO:0000250|UniProtKB:P25382}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:P25382}.
CC -!- SIMILARITY: Belongs to the NLE1/RSA4 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EGS18955.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; GL988045; EGS18955.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_006695900.1; XM_006695837.1.
DR PDB; 4WJS; X-ray; 1.80 A; A=33-517.
DR PDB; 6QTA; X-ray; 1.89 A; B=30-128.
DR PDBsum; 4WJS; -.
DR PDBsum; 6QTA; -.
DR AlphaFoldDB; G0SC29; -.
DR SMR; G0SC29; -.
DR STRING; 759272.G0SC29; -.
DR EnsemblFungi; EGS18955; EGS18955; CTHT_0055700.
DR GeneID; 18259608; -.
DR KEGG; cthr:CTHT_0055700; -.
DR eggNOG; KOG0271; Eukaryota.
DR HOGENOM; CLU_000288_57_16_1; -.
DR OrthoDB; 723347at2759; -.
DR Proteomes; UP000008066; Unassembled WGS sequence.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0110136; P:protein-RNA complex remodeling; IEA:EnsemblFungi.
DR GO; GO:0000027; P:ribosomal large subunit assembly; IEA:EnsemblFungi.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF00400; WD40; 7.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 8.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 4.
DR PROSITE; PS50082; WD_REPEATS_2; 7.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Nucleus; Reference proteome; Repeat; Ribosome biogenesis;
KW WD repeat.
FT CHAIN 1..517
FT /note="Ribosome assembly protein 4"
FT /id="PRO_0000430589"
FT REPEAT 144..184
FT /note="WD 1"
FT /evidence="ECO:0000255"
FT REPEAT 187..226
FT /note="WD 2"
FT /evidence="ECO:0000255"
FT REPEAT 230..277
FT /note="WD 3"
FT /evidence="ECO:0000255"
FT REPEAT 278..316
FT /note="WD 4"
FT /evidence="ECO:0000255"
FT REPEAT 351..397
FT /note="WD 5"
FT /evidence="ECO:0000255"
FT REPEAT 402..441
FT /note="WD 6"
FT /evidence="ECO:0000255"
FT REPEAT 444..483
FT /note="WD 7"
FT /evidence="ECO:0000255"
FT REPEAT 486..517
FT /note="WD 8"
FT /evidence="ECO:0000255"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 34..128
FT /note="Ubiquitin-like (UBL) domain"
FT /evidence="ECO:0000305|PubMed:25404745"
FT TURN 30..32
FT /evidence="ECO:0007829|PDB:6QTA"
FT STRAND 36..42
FT /evidence="ECO:0007829|PDB:4WJS"
FT STRAND 53..56
FT /evidence="ECO:0007829|PDB:4WJS"
FT HELIX 57..59
FT /evidence="ECO:0007829|PDB:4WJS"
FT HELIX 62..72
FT /evidence="ECO:0007829|PDB:4WJS"
FT HELIX 77..79
FT /evidence="ECO:0007829|PDB:4WJS"
FT STRAND 83..88
FT /evidence="ECO:0007829|PDB:4WJS"
FT HELIX 103..109
FT /evidence="ECO:0007829|PDB:4WJS"
FT HELIX 115..117
FT /evidence="ECO:0007829|PDB:6QTA"
FT STRAND 123..126
FT /evidence="ECO:0007829|PDB:4WJS"
FT STRAND 137..142
FT /evidence="ECO:0007829|PDB:4WJS"
FT STRAND 149..154
FT /evidence="ECO:0007829|PDB:4WJS"
FT STRAND 161..166
FT /evidence="ECO:0007829|PDB:4WJS"
FT STRAND 171..175
FT /evidence="ECO:0007829|PDB:4WJS"
FT TURN 176..179
FT /evidence="ECO:0007829|PDB:4WJS"
FT STRAND 180..185
FT /evidence="ECO:0007829|PDB:4WJS"
FT STRAND 192..197
FT /evidence="ECO:0007829|PDB:4WJS"
FT STRAND 204..208
FT /evidence="ECO:0007829|PDB:4WJS"
FT STRAND 213..216
FT /evidence="ECO:0007829|PDB:4WJS"
FT TURN 218..220
FT /evidence="ECO:0007829|PDB:4WJS"
FT STRAND 235..240
FT /evidence="ECO:0007829|PDB:4WJS"
FT HELIX 243..245
FT /evidence="ECO:0007829|PDB:4WJS"
FT STRAND 252..257
FT /evidence="ECO:0007829|PDB:4WJS"
FT STRAND 262..266
FT /evidence="ECO:0007829|PDB:4WJS"
FT TURN 267..270
FT /evidence="ECO:0007829|PDB:4WJS"
FT STRAND 271..276
FT /evidence="ECO:0007829|PDB:4WJS"
FT STRAND 283..288
FT /evidence="ECO:0007829|PDB:4WJS"
FT STRAND 292..298
FT /evidence="ECO:0007829|PDB:4WJS"
FT STRAND 303..307
FT /evidence="ECO:0007829|PDB:4WJS"
FT TURN 308..311
FT /evidence="ECO:0007829|PDB:4WJS"
FT STRAND 312..317
FT /evidence="ECO:0007829|PDB:4WJS"
FT STRAND 324..329
FT /evidence="ECO:0007829|PDB:4WJS"
FT HELIX 332..336
FT /evidence="ECO:0007829|PDB:4WJS"
FT TURN 337..339
FT /evidence="ECO:0007829|PDB:4WJS"
FT HELIX 350..365
FT /evidence="ECO:0007829|PDB:4WJS"
FT STRAND 375..379
FT /evidence="ECO:0007829|PDB:4WJS"
FT STRAND 384..387
FT /evidence="ECO:0007829|PDB:4WJS"
FT HELIX 389..392
FT /evidence="ECO:0007829|PDB:4WJS"
FT STRAND 397..400
FT /evidence="ECO:0007829|PDB:4WJS"
FT STRAND 407..412
FT /evidence="ECO:0007829|PDB:4WJS"
FT STRAND 416..423
FT /evidence="ECO:0007829|PDB:4WJS"
FT STRAND 428..432
FT /evidence="ECO:0007829|PDB:4WJS"
FT TURN 433..435
FT /evidence="ECO:0007829|PDB:4WJS"
FT STRAND 438..442
FT /evidence="ECO:0007829|PDB:4WJS"
FT STRAND 449..454
FT /evidence="ECO:0007829|PDB:4WJS"
FT STRAND 458..465
FT /evidence="ECO:0007829|PDB:4WJS"
FT STRAND 470..474
FT /evidence="ECO:0007829|PDB:4WJS"
FT TURN 475..478
FT /evidence="ECO:0007829|PDB:4WJS"
FT STRAND 479..484
FT /evidence="ECO:0007829|PDB:4WJS"
FT STRAND 491..496
FT /evidence="ECO:0007829|PDB:4WJS"
FT STRAND 500..507
FT /evidence="ECO:0007829|PDB:4WJS"
FT STRAND 512..516
FT /evidence="ECO:0007829|PDB:4WJS"
SQ SEQUENCE 517 AA; 57549 MW; AC226E54F6B35E68 CRC64;
MATLAPPPSK RQRREEIQRT QTQQDVTPLV ATDLGSFKAN FIDSDGNQMT DVVEINFADA
TEKNISNLLN TLLGRDREEF TPYRFRIHIP GKDLIIDQYP NDLLSLLQKH GVTNPFETTI
TLSAEPQAIF KVHAVSRLAH RIPGHGQPIL SCQFSPVSSS RLATGSGDNT ARIWDTDSGT
PKFTLKGHTG WVLGVSWSPD GKYLATCSMD TTVRVWDPES GKQVNQEFRG HAKWVLALAW
QPYHLWRDGT ARLASASKDC TVRIWLVNTG RTEHVLSGHK GSVSCVKWGG TDLIYTGSHD
RSVRVWDAVK GTLVHNFTAH GHWVNHIALS SDHVLRTAYH DHTKEVPGTE EERRAKAKER
FEKAAKIKGK VAERLVSASD DFTMYLWDPT NNGSKPVARL LGHQNKVNHV QFSPDGTLIA
SAGWDNSTKL WNARDGKFIK NLRGHVAPVY QCAWSADSRL VVTGSKDCTL KVWNVRTGKL
AMDLPGHEDE VYAVDWAADG ELVASGGKDK AVRTWRN
