ID A0A0D7AAH0_9AGAR Unreviewed; 217 AA.
AC A0A0D7AAH0;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 08-NOV-2023, entry version 31.
DE SubName: Full=Ribosomal protein S5 domain 2-like protein {ECO:0000313|EMBL:KIY47394.1};
GN ORFNames=FISHEDRAFT_66107 {ECO:0000313|EMBL:KIY47394.1};
OS Fistulina hepatica ATCC 64428.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Fistulinaceae; Fistulina.
OX NCBI_TaxID=1128425 {ECO:0000313|EMBL:KIY47394.1, ECO:0000313|Proteomes:UP000054144};
RN [1] {ECO:0000313|EMBL:KIY47394.1, ECO:0000313|Proteomes:UP000054144}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 64428 {ECO:0000313|EMBL:KIY47394.1,
RC ECO:0000313|Proteomes:UP000054144};
RX PubMed=25683379; DOI=10.1016/j.fgb.2015.02.002;
RA Floudas D., Held B.W., Riley R., Nagy L.G., Koehler G., Ransdell A.S.,
RA Younus H., Chow J., Chiniquy J., Lipzen A., Tritt A., Sun H., Haridas S.,
RA LaButti K., Ohm R.A., Kues U., Blanchette R.A., Grigoriev I.V., Minto R.E.,
RA Hibbett D.S.;
RT "Evolution of novel wood decay mechanisms in Agaricales revealed by the
RT genome sequences of Fistulina hepatica and Cylindrobasidium torrendii.";
RL Fungal Genet. Biol. 76:78-92(2015).
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS5 family.
CC {ECO:0000256|ARBA:ARBA00008945, ECO:0000256|RuleBase:RU003823}.
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DR EMBL; KN881942; KIY47394.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D7AAH0; -.
DR OrthoDB; 1407097at2759; -.
DR Proteomes; UP000054144; Unassembled WGS sequence.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:UniProtKB-UniRule.
DR GO; GO:0006412; P:translation; IEA:InterPro.
DR Gene3D; 3.30.160.20; -; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR000851; Ribosomal_uS5.
DR InterPro; IPR005324; Ribosomal_uS5_C.
DR InterPro; IPR013810; Ribosomal_uS5_N.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR PANTHER; PTHR48277; MITOCHONDRIAL RIBOSOMAL PROTEIN S5; 1.
DR PANTHER; PTHR48277:SF1; MITOCHONDRIAL RIBOSOMAL PROTEIN S5; 1.
DR Pfam; PF00333; Ribosomal_S5; 1.
DR Pfam; PF03719; Ribosomal_S5_C; 1.
DR SUPFAM; SSF54768; dsRNA-binding domain-like; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR PROSITE; PS50881; S5_DSRBD; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000054144};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274, ECO:0000256|PROSITE-
KW ProRule:PRU00268};
KW Ribosomal protein {ECO:0000256|ARBA:ARBA00022980, ECO:0000256|PROSITE-
KW ProRule:PRU00268}.
FT DOMAIN 46..99
FT /note="S5 DRBM"
FT /evidence="ECO:0000259|PROSITE:PS50881"
SQ SEQUENCE 217 AA; 24158 MW; 3BABBB6767A232BC CRC64;
MERSDFDFRS VTWKPNDTKG SVSASLNSEV PKRPFPFVYD LLSRIVKQQT GKGKIARIER
ICIVGNGKGM VGLGIGKDAE GHRALDRARG RAVKNMDFVE RFEERTIYTE MQAKLGSTRI
IMRPRPVGFG LRCNPYMHQI FRACGIKDIS AKVWGSRNPI NVMHATLRML QSGHAPILMG
DGLGGPGRKL SKGSGIMSQE AVERSRGRRL ATLRKTT
//
