ID R1E996_BOTPV Unreviewed; 233 AA.
AC R1E996;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=H/ACA ribonucleoprotein complex subunit 2 {ECO:0000256|RuleBase:RU366039};
DE AltName: Full=Nucleolar protein family A member 2 {ECO:0000256|RuleBase:RU366039};
GN ORFNames=UCRNP2_8924 {ECO:0000313|EMBL:EOD44358.1};
OS Botryosphaeria parva (strain UCR-NP2) (Grapevine canker fungus)
OS (Neofusicoccum parvum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetes incertae sedis; Botryosphaeriales; Botryosphaeriaceae;
OC Neofusicoccum.
OX NCBI_TaxID=1287680 {ECO:0000313|EMBL:EOD44358.1, ECO:0000313|Proteomes:UP000013521};
RN [1] {ECO:0000313|Proteomes:UP000013521}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCR-NP2 {ECO:0000313|Proteomes:UP000013521};
RX PubMed=23766404; DOI=10.1128/genomea.00339-13;
RA Blanco-Ulate B., Rolshausen P., Cantu D.;
RT "Draft genome sequence of Neofusicoccum parvum isolate UCR-NP2, a fungal
RT vascular pathogen associated with grapevine cankers.";
RL Genome Announc. 1:E0033913-E0033913(2013).
CC -!- FUNCTION: Common component of the spliceosome and rRNA processing
CC machinery. {ECO:0000256|RuleBase:RU366039}.
CC -!- FUNCTION: Required for ribosome biogenesis. Part of a complex which
CC catalyzes pseudouridylation of rRNA. This involves the isomerization of
CC uridine such that the ribose is subsequently attached to C5, instead of
CC the normal N1. Pseudouridine ('psi') residues may serve to stabilize
CC the conformation of rRNAs. {ECO:0000256|RuleBase:RU366039}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000256|RuleBase:RU366039}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eL8 family.
CC {ECO:0000256|ARBA:ARBA00007337, ECO:0000256|RuleBase:RU366039}.
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DR EMBL; KB916735; EOD44358.1; -; Genomic_DNA.
DR RefSeq; XP_007588161.1; XM_007588099.1.
DR AlphaFoldDB; R1E996; -.
DR STRING; 1287680.R1E996; -.
DR KEGG; npa:UCRNP2_8924; -.
DR eggNOG; KOG3167; Eukaryota.
DR HOGENOM; CLU_084513_0_0_1; -.
DR OMA; HGIPYVY; -.
DR OrthoDB; 5481356at2759; -.
DR Proteomes; UP000013521; Unassembled WGS sequence.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0042254; P:ribosome biogenesis; IEA:InterPro.
DR Gene3D; 3.30.1330.30; -; 1.
DR InterPro; IPR002415; H/ACA_rnp_Nhp2-like.
DR InterPro; IPR029064; Ribosomal_eL30-like_sf.
DR InterPro; IPR004037; Ribosomal_eL8-like_CS.
DR InterPro; IPR004038; Ribosomal_eL8/eL30/eS12/Gad45.
DR PANTHER; PTHR11843; 40S RIBOSOMAL PROTEIN S12; 1.
DR PANTHER; PTHR11843:SF0; 40S RIBOSOMAL PROTEIN S12; 1.
DR Pfam; PF01248; Ribosomal_L7Ae; 1.
DR PRINTS; PR00883; NUCLEARHMG.
DR SUPFAM; SSF55315; L30e-like; 1.
DR PROSITE; PS01082; RIBOSOMAL_L7AE; 1.
PE 3: Inferred from homology;
KW Nucleus {ECO:0000256|RuleBase:RU366039};
KW Reference proteome {ECO:0000313|Proteomes:UP000013521};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274,
KW ECO:0000256|RuleBase:RU366039};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|RuleBase:RU366039}.
FT DOMAIN 97..200
FT /note="Ribosomal protein eL8/eL30/eS12/Gadd45"
FT /evidence="ECO:0000259|Pfam:PF01248"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..38
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 233 AA; 25026 MW; E304507ECE226EEF CRC64;
MAKDKVKEKK EKKEKRSETD GVKKSKKDKK EKKQSEHVTE ALLSSISDAS SGADVRTVVV
SKTAGESDDE AAAGLPVSAL NLVPFAVPLA DDKVTKKIFK TVKKAAKHKT LKRGVKEVVK
AVRKSSTNLP ASSLIDDPSA VVVIAADISP MDVISHIPVL CEEHNIPYIF VTSRAELGAA
GNTKRPTSVV MICKDRGSKK ASDDAKAEDE ADYKEAYDGV VKAVLKASKG VRR
//
