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Database: UniProt
Entry: S0AQB7_FERAC
LinkDB: S0AQB7_FERAC
Original site: S0AQB7_FERAC 
ID   S0AQB7_FERAC            Unreviewed;       351 AA.
AC   S0AQB7;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   24-JAN-2024, entry version 57.
DE   RecName: Full=Probable tRNA pseudouridine synthase B {ECO:0000256|HAMAP-Rule:MF_01081};
DE            EC=5.4.99.25 {ECO:0000256|HAMAP-Rule:MF_01081};
DE   AltName: Full=tRNA pseudouridine(55) synthase {ECO:0000256|HAMAP-Rule:MF_01081};
DE            Short=Psi55 synthase {ECO:0000256|HAMAP-Rule:MF_01081};
DE   AltName: Full=tRNA pseudouridylate synthase {ECO:0000256|HAMAP-Rule:MF_01081};
DE   AltName: Full=tRNA-uridine isomerase {ECO:0000256|HAMAP-Rule:MF_01081};
GN   Name=truB {ECO:0000256|HAMAP-Rule:MF_01081};
GN   ORFNames=FACI_IFERC00001G1161 {ECO:0000313|EMBL:AGO61141.1};
OS   Ferroplasma acidarmanus Fer1.
OC   Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC   Ferroplasmaceae; Ferroplasma.
OX   NCBI_TaxID=333146 {ECO:0000313|EMBL:AGO61141.1, ECO:0000313|Proteomes:UP000014660};
RN   [1] {ECO:0000313|EMBL:AGO61141.1, ECO:0000313|Proteomes:UP000014660}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=fer1 {ECO:0000313|Proteomes:UP000014660};
RX   PubMed=17267615; DOI=10.1073/pnas.0604851104;
RA   Allen E.E., Tyson G.W., Whitaker R.J., Detter J.C., Richardson P.M.,
RA   Banfield J.F.;
RT   "Genome dynamics in a natural archaeal population.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1883-1888(2007).
CC   -!- FUNCTION: Could be responsible for synthesis of pseudouridine from
CC       uracil-55 in the psi GC loop of transfer RNAs. {ECO:0000256|HAMAP-
CC       Rule:MF_01081}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=uridine(55) in tRNA = pseudouridine(55) in tRNA;
CC         Xref=Rhea:RHEA:42532, Rhea:RHEA-COMP:10101, Rhea:RHEA-COMP:10102,
CC         ChEBI:CHEBI:65314, ChEBI:CHEBI:65315; EC=5.4.99.25;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01081};
CC   -!- SIMILARITY: Belongs to the pseudouridine synthase TruB family. Type 2
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_01081}.
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DR   EMBL; CP004145; AGO61141.1; -; Genomic_DNA.
DR   RefSeq; WP_009887191.1; NC_021592.1.
DR   AlphaFoldDB; S0AQB7; -.
DR   GeneID; 84218675; -.
DR   KEGG; fac:FACI_IFERC01G1161; -.
DR   PATRIC; fig|333146.12.peg.1178; -.
DR   HOGENOM; CLU_032087_3_0_2; -.
DR   Proteomes; UP000014660; Chromosome.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0106029; F:tRNA pseudouridine synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0031119; P:tRNA pseudouridine synthesis; IEA:UniProtKB-UniRule.
DR   CDD; cd07953; PUA; 1.
DR   Gene3D; 3.30.2350.10; Pseudouridine synthase; 1.
DR   Gene3D; 2.30.130.10; PUA domain; 1.
DR   HAMAP; MF_01081; TruB_arch; 1.
DR   InterPro; IPR012960; Dyskerin-like.
DR   InterPro; IPR020103; PsdUridine_synth_cat_dom_sf.
DR   InterPro; IPR002501; PsdUridine_synth_N.
DR   InterPro; IPR002478; PUA.
DR   InterPro; IPR015947; PUA-like_sf.
DR   InterPro; IPR036974; PUA_sf.
DR   InterPro; IPR004802; tRNA_PsdUridine_synth_B_fam.
DR   InterPro; IPR026326; TruB_arch.
DR   InterPro; IPR032819; TruB_C.
DR   NCBIfam; TIGR00425; CBF5; 1.
DR   PANTHER; PTHR23127; CENTROMERE/MICROTUBULE BINDING PROTEIN CBF5; 1.
DR   PANTHER; PTHR23127:SF0; H/ACA RIBONUCLEOPROTEIN COMPLEX SUBUNIT DKC1; 1.
DR   Pfam; PF01472; PUA; 1.
DR   Pfam; PF16198; TruB_C_2; 1.
DR   Pfam; PF01509; TruB_N; 1.
DR   SMART; SM01136; DKCLD; 1.
DR   SMART; SM00359; PUA; 1.
DR   SUPFAM; SSF55120; Pseudouridine synthase; 1.
DR   SUPFAM; SSF88697; PUA domain-like; 1.
DR   PROSITE; PS50890; PUA; 1.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01081};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014660};
KW   tRNA processing {ECO:0000256|HAMAP-Rule:MF_01081}.
FT   DOMAIN          2..29
FT                   /note="Dyskerin-like"
FT                   /evidence="ECO:0000259|SMART:SM01136"
FT   DOMAIN          215..292
FT                   /note="PUA"
FT                   /evidence="ECO:0000259|SMART:SM00359"
FT   REGION          305..351
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        306..328
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        48
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01081"
SQ   SEQUENCE   351 AA;  39457 MW;  ADE4AAB993634788 CRC64;
     MYASNSTPEE INGFIVIDKP KGPTSHQIDA WVREITGEKR VGHIGTLDPN VSGVLVMALG
     KATKLIDIVH ERPKEYISVM RLYSTADTDN IMKVFKEFTG KIYQLPPVRS AVSRQVRERT
     IYNMDVLEIQ EKLILFRVKC ESGTYIRTLC TDMGYVIGTG AQMADLRRLS TGQFNESHIH
     TLQELSDSVV LKKQGDTSLF DNMVIPMDFV FADSPKVVVK NTAIKNIMHG SDIYPSGIKA
     LIGDIHKGSR VAIYSGDNEL LAFGTMLVDS LNDLKAVDLD GILSDKYGEN NVVRKNNRQK
     NIPVQKPAKR LHEHIRKPEA RDNPGNGRDM FRKNPGFKGN PSKIRKRKNK F
//
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