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Database: UniProt
Entry: A0A084QB32_STAC4
LinkDB: A0A084QB32_STAC4
Original site: A0A084QB32_STAC4 
ID   A0A084QB32_STAC4        Unreviewed;       495 AA.
AC   A0A084QB32;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   08-NOV-2023, entry version 38.
DE   RecName: Full=S5 DRBM domain-containing protein {ECO:0000259|PROSITE:PS50881};
GN   ORFNames=S40285_02195 {ECO:0000313|EMBL:KFA61167.1};
OS   Stachybotrys chlorohalonata (strain IBT 40285).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Stachybotryaceae; Stachybotrys.
OX   NCBI_TaxID=1283841 {ECO:0000313|EMBL:KFA61167.1, ECO:0000313|Proteomes:UP000028524};
RN   [1] {ECO:0000313|EMBL:KFA61167.1, ECO:0000313|Proteomes:UP000028524}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 40285 {ECO:0000313|EMBL:KFA61167.1,
RC   ECO:0000313|Proteomes:UP000028524};
RX   PubMed=25015739; DOI=10.1186/1471-2164-15-590;
RA   Semeiks J., Borek D., Otwinowski Z., Grishin N.V.;
RT   "Comparative genome sequencing reveals chemotype-specific gene clusters in
RT   the toxigenic black mold Stachybotrys.";
RL   BMC Genomics 15:590-590(2014).
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; KL660868; KFA61167.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A084QB32; -.
DR   STRING; 1283841.A0A084QB32; -.
DR   HOGENOM; CLU_037994_1_0_1; -.
DR   InParanoid; A0A084QB32; -.
DR   OMA; EPVVDHH; -.
DR   OrthoDB; 1407097at2759; -.
DR   Proteomes; UP000028524; 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:UP000028524};
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          331..394
FT                   /note="S5 DRBM"
FT                   /evidence="ECO:0000259|PROSITE:PS50881"
SQ   SEQUENCE   495 AA;  55319 MW;  AF3B0E61F175A7AC CRC64;
     MSVARPARSL LGRCVTSTRT SASIPLSARS FHTSAPCQQR RSRFRNVKAQ ELGLLKPENM
     AKLQKDKFPD YTPEELAELK QKYSPEHIES IQAGEKAVDT EDMIIQGRMR DDAYRPTYVD
     DYTVLDPRYD IKPDVPGTPQ EIHWPSRGDW IDEYGMRLSK MVEKKTDDQL TRAMIRALRK
     VKQSKGEEMI DLTVEELDEM EKNPELAKKY MVEDDDAPEP DANASGPEYL TRAQAMQLDE
     AVVAAWQEEL KKIAEHKDLT AEPSSLELMQ DGPAGVIRVH SAELPELGKV PGVEGRFLKE
     EDAEDGGSDE AAAYQELKRL TGMSLSELMS LPAKVLVRRR VTNQTRLGKV HSISIVAMAG
     NGNGYLGLGV AKSTQPEIAI ETARMLAMRN MKPIRRYENR TIFGHSTGKV SGTVVEMFTR
     PPGYGLRVPS RIFEMCRACG IHDLSVRMPR STNPMNAVKA AYQALTNQPD PAQIAIGRGK
     KMVDARKVYY GGDVH
//
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