ID L8WXG8_THACA Unreviewed; 607 AA.
AC L8WXG8;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Small ribosomal subunit protein uS2 {ECO:0000256|HAMAP-Rule:MF_03015};
GN Name=RPS0 {ECO:0000256|HAMAP-Rule:MF_03015};
GN ORFNames=AG1IA_03304 {ECO:0000313|EMBL:ELU42685.1};
OS Thanatephorus cucumeris (strain AG1-IA) (Rice sheath blight fungus)
OS (Rhizoctonia solani).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Cantharellales; Ceratobasidiaceae; Rhizoctonia; Rhizoctonia solani AG-1.
OX NCBI_TaxID=983506 {ECO:0000313|EMBL:ELU42685.1, ECO:0000313|Proteomes:UP000011668};
RN [1] {ECO:0000313|EMBL:ELU42685.1, ECO:0000313|Proteomes:UP000011668}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AG-1 IA {ECO:0000313|Proteomes:UP000011668};
RX PubMed=23361014; DOI=10.1038/ncomms2427;
RA Zheng A., Lin R., Xu L., Qin P., Tang C., Ai P., Zhang D., Liu Y., Sun Z.,
RA Feng H., Wang Y., Chen Y., Liang X., Fu R., Li Q., Zhang J., Yu X., Xie Z.,
RA Ding L., Guan P., Tang J., Liang Y., Wang S., Deng Q., Li S., Zhu J.,
RA Wang L., Liu H., Li P.;
RT "The evolution and pathogenic mechanisms of the rice sheath blight
RT pathogen.";
RL Nat. Commun. 4:1424-1424(2013).
CC -!- FUNCTION: Required for the assembly and/or stability of the 40S
CC ribosomal subunit. Required for the processing of the 20S rRNA-
CC precursor to mature 18S rRNA in a late step of the maturation of 40S
CC ribosomal subunits. {ECO:0000256|HAMAP-Rule:MF_03015}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PROSITE-ProRule:PRU00333};
CC -!- SUBUNIT: Component of the small ribosomal subunit. Mature ribosomes
CC consist of a small (40S) and a large (60S) subunit. The 40S subunit
CC contains about 33 different proteins and 1 molecule of RNA (18S). The
CC 60S subunit contains about 49 different proteins and 3 molecules of RNA
CC (25S, 5.8S and 5S). Interacts with RPS21. {ECO:0000256|HAMAP-
CC Rule:MF_03015}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_03015}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS2 family.
CC {ECO:0000256|ARBA:ARBA00006242, ECO:0000256|HAMAP-Rule:MF_03015,
CC ECO:0000256|RuleBase:RU003631}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ELU42685.1}.
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DR EMBL; AFRT01000772; ELU42685.1; -; Genomic_DNA.
DR AlphaFoldDB; L8WXG8; -.
DR STRING; 983506.L8WXG8; -.
DR HOGENOM; CLU_449910_0_0_1; -.
DR OMA; CHIAFVE; -.
DR Proteomes; UP000011668; Unassembled WGS sequence.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:UniProtKB-UniRule.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0000028; P:ribosomal small subunit assembly; IEA:UniProtKB-UniRule.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR CDD; cd01425; RPS2; 1.
DR Gene3D; 3.20.20.330; Homocysteine-binding-like domain; 1.
DR HAMAP; MF_03015; Ribosomal_S2_euk; 1.
DR InterPro; IPR003726; HCY_dom.
DR InterPro; IPR036589; HCY_dom_sf.
DR InterPro; IPR001865; Ribosomal_uS2.
DR InterPro; IPR018130; Ribosomal_uS2_CS.
DR InterPro; IPR027498; Ribosomal_uS2_euk.
DR InterPro; IPR005707; Ribosomal_uS2_euk/arc.
DR InterPro; IPR023591; Ribosomal_uS2_flav_dom_sf.
DR NCBIfam; TIGR01012; uS2_euk_arch; 1.
DR PANTHER; PTHR11489; 40S RIBOSOMAL PROTEIN SA; 1.
DR PANTHER; PTHR11489:SF9; 40S RIBOSOMAL PROTEIN SA; 1.
DR Pfam; PF00318; Ribosomal_S2; 2.
DR Pfam; PF02574; S-methyl_trans; 1.
DR PRINTS; PR00395; RIBOSOMALS2.
DR SUPFAM; SSF82282; Homocysteine S-methyltransferase; 1.
DR SUPFAM; SSF52313; Ribosomal protein S2; 1.
DR PROSITE; PS50970; HCY; 1.
DR PROSITE; PS00962; RIBOSOMAL_S2_1; 1.
DR PROSITE; PS00963; RIBOSOMAL_S2_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_03015};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00333};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|PROSITE-
KW ProRule:PRU00333}; Reference proteome {ECO:0000313|Proteomes:UP000011668};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274, ECO:0000256|HAMAP-
KW Rule:MF_03015};
KW Ribosomal protein {ECO:0000256|ARBA:ARBA00022980, ECO:0000256|HAMAP-
KW Rule:MF_03015};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PROSITE-
KW ProRule:PRU00333}; Zinc {ECO:0000256|PROSITE-ProRule:PRU00333}.
FT DOMAIN 9..393
FT /note="Hcy-binding"
FT /evidence="ECO:0000259|PROSITE:PS50970"
FT BINDING 270
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00333"
FT BINDING 378
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00333"
FT BINDING 379
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00333"
SQ SEQUENCE 607 AA; 66518 MW; 20BBDAE24BF31E91 CRC64;
MGEEGSKTTR LTSRFAREDI AFLDAGLGTT LEDVLHKNIS HPLWSAHLID TNPDAIVEAH
LAFLRAGSSV ILTATAGYTH DQASAITHKA IALAVRAREI YMNITSPDTL KPQVALSLGP
FGATLSPAAE FSGIYPPPYG PPQPVTFFTG EQALEDEQKA ENALLKFHLE RISMLASTKE
TWDAIDIIAF ETVPLLREAR AIRRAMTAFA SANPSLRIPP WWISFNFPDG VLPEQTSQGK
NYTAGDAVSA CFAQHQADST AIPDAFGINC TQVRYLHECV SLASDALQTV KQNPYSKSRP
SVLDPRNLPS KSGPTLVVYP NGGRIYDPNT MTWLPAASES SETKGLSESD AWAIGLVDVL
QGAVPEDSGW SGLLIGGCCK TEPEHHAMAS KYPAALNPTE EDIQLLLSAQ AHLGTKNCDK
QMEPYVWKRR RNGIGIHIIN IGKTWEKLVL AARIIAAIEN PSDVVAISAR PYGQRAVLKF
AANTGAQAIA GRFTPGNFTN YITRSFKEPR LIIVTDPRVD HQAIREASYV NIPVIALCDT
DAPLKFVDVA IPTNNKSKNS IGLIWWLLAR EVLRLRGTVP RTPDGWNVMV DMFFYRDPQE
EQEQENQ
//
