ID I2GYC3_TETBL Unreviewed; 517 AA.
AC I2GYC3;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=Nucleolar protein 58 {ECO:0000256|ARBA:ARBA00020379};
GN Name=TBLA0B02830 {ECO:0000313|EMBL:CCH59125.1};
GN ORFNames=TBLA_0B02830 {ECO:0000313|EMBL:CCH59125.1};
OS Tetrapisispora blattae (strain ATCC 34711 / CBS 6284 / DSM 70876 / NBRC
OS 10599 / NRRL Y-10934 / UCD 77-7) (Yeast) (Kluyveromyces blattae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Tetrapisispora.
OX NCBI_TaxID=1071380 {ECO:0000313|EMBL:CCH59125.1, ECO:0000313|Proteomes:UP000002866};
RN [1] {ECO:0000313|EMBL:CCH59125.1, ECO:0000313|Proteomes:UP000002866}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 34711 / CBS 6284 / DSM 70876 / NBRC 10599 / NRRL Y-10934 /
RC UCD 77-7 {ECO:0000313|Proteomes:UP000002866};
RX PubMed=22123960; DOI=10.1073/pnas.1112808108;
RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P.,
RA Wolfe K.H.;
RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching
RT accidents.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
CC -!- FUNCTION: Required for pre-18S rRNA processing. May bind microtubules.
CC {ECO:0000256|ARBA:ARBA00024837}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000256|ARBA:ARBA00004604}.
CC -!- SIMILARITY: Belongs to the NOP5/NOP56 family.
CC {ECO:0000256|ARBA:ARBA00009211}.
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DR EMBL; HE806317; CCH59125.1; -; Genomic_DNA.
DR RefSeq; XP_004178644.1; XM_004178596.1.
DR AlphaFoldDB; I2GYC3; -.
DR STRING; 1071380.I2GYC3; -.
DR GeneID; 14493934; -.
DR KEGG; tbl:TBLA_0B02830; -.
DR eggNOG; KOG2572; Eukaryota.
DR HOGENOM; CLU_015495_5_2_1; -.
DR InParanoid; I2GYC3; -.
DR OMA; KGKMARI; -.
DR OrthoDB; 5489581at2759; -.
DR Proteomes; UP000002866; Chromosome 2.
DR GO; GO:0031428; C:box C/D RNP complex; IEA:InterPro.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0032040; C:small-subunit processome; IEA:InterPro.
DR GO; GO:0030515; F:snoRNA binding; IEA:InterPro.
DR GO; GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-KW.
DR Gene3D; 1.10.287.4070; -; 1.
DR Gene3D; 1.10.246.90; Nop domain; 1.
DR InterPro; IPR045056; Nop56/Nop58.
DR InterPro; IPR012974; NOP58/56_N.
DR InterPro; IPR042239; Nop_C.
DR InterPro; IPR002687; Nop_dom.
DR InterPro; IPR036070; Nop_dom_sf.
DR InterPro; IPR012976; NOSIC.
DR PANTHER; PTHR10894; NUCLEOLAR PROTEIN 5 NUCLEOLAR PROTEIN NOP5 NOP58; 1.
DR PANTHER; PTHR10894:SF1; NUCLEOLAR PROTEIN 58; 1.
DR Pfam; PF01798; Nop; 1.
DR Pfam; PF08156; NOP5NT; 1.
DR SMART; SM00931; NOSIC; 1.
DR SUPFAM; SSF89124; Nop domain; 1.
DR PROSITE; PS51358; NOP; 1.
PE 3: Inferred from homology;
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000002866};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274}.
FT DOMAIN 283..403
FT /note="Nop"
FT /evidence="ECO:0000259|PROSITE:PS51358"
FT REGION 428..517
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 449..504
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 517 AA; 57779 MW; F50172C2992B4D03 CRC64;
MSYVLTETPA GYALLKASDK KIYKSSSLLQ DLDTTDKVLK EFKIAAFSKF NSAANALEES
TAIIEGKVSP QLEKLLDEIK KDKKTTLIVS ETKLANAINK LGLNLNIVSD AVTLDIYRAV
KEYLPDLLPG LSDSDLNKMS LGLAHSIGRH KLKFSADKVD VMIIQAIALL DDLDKELNTY
AMRCKEWYGW HFPELAKIVT DSVAYARLIL TMGIRSKASE TDMSEILPEE IEERVKTAAE
VSMGTEITPT DLDNIKALAE QIVEFASYRE QLSNYLSSRM KAIAPNLTQL VGELVGARLI
AHSGSLISLA KSPASTIQIL GAEKALFRAL KTKHDTPKYG LLYHASLVGQ ATGKNKGKIA
RVLAAKAAVS LRYDALAEDR DDAGDVGLEA RTKVENRLSQ LEGRDLRTTP KVVREAKKVE
ITEARAYNAD ADTIPAAEAD SDDESEDESE EKKEKKDKKR KRDEDEDEEK EEKKKSKKEK
KEKKEKKEKK EKKDKKEKKD KKEKKDKKDK KSKKEKK
//
