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Database: UniProt
Entry: E4X5C1_OIKDI
LinkDB: E4X5C1_OIKDI
Original site: E4X5C1_OIKDI 
ID   E4X5C1_OIKDI            Unreviewed;       402 AA.
AC   E4X5C1;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   RecName: Full=tRNA pseudouridine synthase {ECO:0000256|RuleBase:RU003792};
DE            EC=5.4.99.12 {ECO:0000256|RuleBase:RU003792};
GN   ORFNames=GSOID_T00002354001 {ECO:0000313|EMBL:CBY18490.1};
OS   Oikopleura dioica (Tunicate).
OC   Eukaryota; Metazoa; Chordata; Tunicata; Appendicularia; Copelata;
OC   Oikopleuridae; Oikopleura.
OX   NCBI_TaxID=34765 {ECO:0000313|EMBL:CBY18490.1};
RN   [1] {ECO:0000313|EMBL:CBY18490.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21097902; DOI=10.1126/science.1194167;
RA   Denoeud F., Henriet S., Mungpakdee S., Aury J.M., Da Silva C.,
RA   Brinkmann H., Mikhaleva J., Olsen L.C., Jubin C., Canestro C.,
RA   Bouquet J.M., Danks G., Poulain J., Campsteijn C., Adamski M., Cross I.,
RA   Yadetie F., Muffato M., Louis A., Butcher S., Tsagkogeorga G., Konrad A.,
RA   Singh S., Jensen M.F., Cong E.H., Eikeseth-Otteraa H., Noel B.,
RA   Anthouard V., Porcel B.M., Kachouri-Lafond R., Nishino A., Ugolini M.,
RA   Chourrout P., Nishida H., Aasland R., Huzurbazar S., Westhof E., Delsuc F.,
RA   Lehrach H., Reinhardt R., Weissenbach J., Roy S.W., Artiguenave F.,
RA   Postlethwait J.H., Manak J.R., Thompson E.M., Jaillon O., Du Pasquier L.,
RA   Boudinot P., Liberles D.A., Volff J.N., Philippe H., Lenhard B.,
RA   Roest Crollius H., Wincker P., Chourrout D.;
RT   "Plasticity of animal genome architecture unmasked by rapid evolution of a
RT   pelagic tunicate.";
RL   Science 330:1381-1385(2010).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=uridine(38/39/40) in tRNA = pseudouridine(38/39/40) in tRNA;
CC         Xref=Rhea:RHEA:22376, Rhea:RHEA-COMP:10085, Rhea:RHEA-COMP:10087,
CC         ChEBI:CHEBI:65314, ChEBI:CHEBI:65315; EC=5.4.99.12;
CC         Evidence={ECO:0000256|RuleBase:RU003792};
CC   -!- SIMILARITY: Belongs to the tRNA pseudouridine synthase TruA family.
CC       {ECO:0000256|ARBA:ARBA00009375, ECO:0000256|RuleBase:RU003792}.
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DR   EMBL; FN653025; CBY18490.1; -; Genomic_DNA.
DR   AlphaFoldDB; E4X5C1; -.
DR   InParanoid; E4X5C1; -.
DR   Proteomes; UP000001307; Unassembled WGS sequence.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0106029; F:tRNA pseudouridine synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0001522; P:pseudouridine synthesis; IEA:InterPro.
DR   GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.70.660; Pseudouridine synthase I, catalytic domain, C-terminal subdomain; 1.
DR   Gene3D; 3.30.70.580; Pseudouridine synthase I, catalytic domain, N-terminal subdomain; 1.
DR   HAMAP; MF_00171; TruA; 1.
DR   InterPro; IPR020103; PsdUridine_synth_cat_dom_sf.
DR   InterPro; IPR001406; PsdUridine_synth_TruA.
DR   InterPro; IPR020097; PsdUridine_synth_TruA_a/b_dom.
DR   InterPro; IPR020095; PsdUridine_synth_TruA_C.
DR   InterPro; IPR020094; TruA/RsuA/RluB/E/F_N.
DR   NCBIfam; TIGR00071; hisT_truA; 1.
DR   PANTHER; PTHR11142; PSEUDOURIDYLATE SYNTHASE; 1.
DR   PANTHER; PTHR11142:SF5; TRNA PSEUDOURIDINE(38_39) SYNTHASE; 1.
DR   Pfam; PF01416; PseudoU_synth_1; 2.
DR   SUPFAM; SSF55120; Pseudouridine synthase; 1.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU003792};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001307};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694,
KW   ECO:0000256|RuleBase:RU003792}.
FT   DOMAIN          72..156
FT                   /note="Pseudouridine synthase I TruA alpha/beta"
FT                   /evidence="ECO:0000259|Pfam:PF01416"
FT   DOMAIN          208..315
FT                   /note="Pseudouridine synthase I TruA alpha/beta"
FT                   /evidence="ECO:0000259|Pfam:PF01416"
FT   REGION          1..59
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        39..59
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   402 AA;  45713 MW;  B08CFBF6DE922CD6 CRC64;
     MSKEELHAKL EKMKKKNAQL SDQISQMKVK IAQSGLENEE EPPAKKKKKT QKGEKEQNDQ
     IFRKRKIALR FSYDGTKYNG LQRSPVPAGK TTIEDVIFDA ILRTKVVDDI GTADYIAGGR
     TDKGVHAVNN VISLFVNSRL SEDEINENVT VGERNFVAII NRQLPDDIWI TSWAPISFDF
     SARFSCKSRH YNYIFDSSGL DVELMKEAAS YLIGEHDFRN FSQAQLERQN TVRVCFAADI
     KQVPNMSSMC VFSIKASGFL YHQIRLTMAI LALVGNKLEK STIVKELLDV EKYPRRPSYK
     YANPDGLVLI DCEYENVEWI DGEDQSRFLA SKIENKMYNM KIGLSVHELI KKTLDIGKDT
     DEPHRKITGI AAKKGCHKPV LDYHPSPNAN DLLLKSQNKT KN
//
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