ID A0A2J6QCC9_9HELO Unreviewed; 222 AA.
AC A0A2J6QCC9;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=NA56DRAFT_687430 {ECO:0000313|EMBL:PMD23919.1};
OS Hyaloscypha hepaticicola.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Hyaloscyphaceae; Hyaloscypha.
OX NCBI_TaxID=2082293 {ECO:0000313|EMBL:PMD23919.1, ECO:0000313|Proteomes:UP000235672};
RN [1] {ECO:0000313|EMBL:PMD23919.1, ECO:0000313|Proteomes:UP000235672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 7357 {ECO:0000313|EMBL:PMD23919.1,
RC ECO:0000313|Proteomes:UP000235672};
RG DOE Joint Genome Institute;
RA Martino E., Morin E., Grelet G., Kuo A., Kohler A., Daghino S., Barry K.,
RA Choi C., Cichocki N., Clum A., Copeland A., Hainaut M., Haridas S.,
RA Labutti K., Lindquist E., Lipzen A., Khouja H.-R., Murat C., Ohm R.,
RA Olson A., Spatafora J., Veneault-Fourrey C., Henrissat B., Grigoriev I.,
RA Martin F., Perotto S.;
RT "A degradative enzymes factory behind the ericoid mycorrhizal symbiosis.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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; KZ613474; PMD23919.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2J6QCC9; -.
DR STRING; 1745343.A0A2J6QCC9; -.
DR OrthoDB; 5481356at2759; -.
DR Proteomes; UP000235672; 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:UP000235672};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274,
KW ECO:0000256|RuleBase:RU366039};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|RuleBase:RU366039}.
FT DOMAIN 92..185
FT /note="Ribosomal protein eL8/eL30/eS12/Gadd45"
FT /evidence="ECO:0000259|Pfam:PF01248"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..36
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 222 AA; 24137 MW; 1BCC469490B8C555 CRC64;
MAKEKSEKRD RKEKKEKRSE ADGVKKSKKD KKPKLNGDNV AAAFEEVTKA EEPVVETTAV
VIKESSGEVL LKPVGALVPF ANPLADEKVT KKVLKSVKKA AKNKTLKRGV KEVVKALRKS
PQGAANTAIP GVVVLAADIS PMDVISHIPV LCEDHNVPYI FVTSRAELGA AGNTKRPTSV
VMVSESRVGA KKAEKIEGDE EFAEVYKDLV KVVEKESRNV RI
//
