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Database: UniProt
Entry: V9H7I7_9NEIS
LinkDB: V9H7I7_9NEIS
Original site: V9H7I7_9NEIS 
ID   V9H7I7_9NEIS            Unreviewed;       261 AA.
AC   V9H7I7;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   24-JAN-2024, entry version 54.
DE   RecName: Full=tRNA pseudouridine synthase A {ECO:0000256|HAMAP-Rule:MF_00171};
DE            EC=5.4.99.12 {ECO:0000256|HAMAP-Rule:MF_00171};
DE   AltName: Full=tRNA pseudouridine(38-40) synthase {ECO:0000256|HAMAP-Rule:MF_00171};
DE   AltName: Full=tRNA pseudouridylate synthase I {ECO:0000256|HAMAP-Rule:MF_00171};
DE   AltName: Full=tRNA-uridine isomerase I {ECO:0000256|HAMAP-Rule:MF_00171};
GN   Name=truA {ECO:0000256|HAMAP-Rule:MF_00171};
GN   ORFNames=HMPREF9021_02009 {ECO:0000313|EMBL:EFG30104.1};
OS   Simonsiella muelleri ATCC 29453.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Simonsiella.
OX   NCBI_TaxID=641147 {ECO:0000313|EMBL:EFG30104.1, ECO:0000313|Proteomes:UP000017813};
RN   [1] {ECO:0000313|EMBL:EFG30104.1, ECO:0000313|Proteomes:UP000017813}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29453 {ECO:0000313|EMBL:EFG30104.1,
RC   ECO:0000313|Proteomes:UP000017813};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ward D., Earl A., Feldgarden M., Gevers D., Young S., Zeng Q., Koehrsen M.,
RA   Alvarado L., Berlin A.M., Borenstein D., Chapman S.B., Chen Z., Engels R.,
RA   Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E.R.,
RA   Heiman D.I., Hepburn T.A., Howarth C., Jen D., Larson L., Mehta T.,
RA   Park D., Pearson M., Richards J., Roberts A., Saif S., Shea T.D.,
RA   Shenoy N., Sisk P., Stolte C., Sykes S.N., Walk T., White J., Yandava C.,
RA   Izard J., Baranova O.V., Blanton J.M., Tanner A.C., Dewhirst F., Haas B.,
RA   Nusbaum C., Birren B.;
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EFG30104.1, ECO:0000313|Proteomes:UP000017813}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29453 {ECO:0000313|EMBL:EFG30104.1,
RC   ECO:0000313|Proteomes:UP000017813};
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Izard J., Baranova O.V.,
RA   Blanton J.M., Tanner A.C., Dewhirst F., Young S.K., Zeng Q., Gargeya S.,
RA   Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA   Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E.,
RA   Gearin G., Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C.,
RA   Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C., Neiman D.,
RA   Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P.,
RA   Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Simonsiella muelleri ATCC 29453.";
RL   Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Formation of pseudouridine at positions 38, 39 and 40 in the
CC       anticodon stem and loop of transfer RNAs. {ECO:0000256|HAMAP-
CC       Rule:MF_00171}.
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|HAMAP-Rule:MF_00171,
CC         ECO:0000256|RuleBase:RU003792};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00171}.
CC   -!- SIMILARITY: Belongs to the tRNA pseudouridine synthase TruA family.
CC       {ECO:0000256|ARBA:ARBA00009375, ECO:0000256|HAMAP-Rule:MF_00171,
CC       ECO:0000256|RuleBase:RU003792}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00171}.
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:EFG30104.1}.
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DR   EMBL; ADCY02000054; EFG30104.1; -; Genomic_DNA.
DR   RefSeq; WP_002642866.1; NZ_JH815309.1.
DR   AlphaFoldDB; V9H7I7; -.
DR   STRING; 641147.HMPREF9021_02009; -.
DR   KEGG; smur:BWP33_02770; -.
DR   eggNOG; COG0101; Bacteria.
DR   HOGENOM; CLU_014673_0_2_4; -.
DR   OrthoDB; 9811823at2; -.
DR   Proteomes; UP000017813; 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:0031119; P:tRNA pseudouridine synthesis; IEA:UniProtKB-UniRule.
DR   CDD; cd02570; PseudoU_synth_EcTruA; 1.
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:SF0; TRNA PSEUDOURIDINE SYNTHASE-LIKE 1; 1.
DR   Pfam; PF01416; PseudoU_synth_1; 2.
DR   PIRSF; PIRSF001430; tRNA_psdUrid_synth; 1.
DR   SUPFAM; SSF55120; Pseudouridine synthase; 1.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_00171};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017813};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW   Rule:MF_00171}.
FT   DOMAIN          10..106
FT                   /note="Pseudouridine synthase I TruA alpha/beta"
FT                   /evidence="ECO:0000259|Pfam:PF01416"
FT   DOMAIN          145..247
FT                   /note="Pseudouridine synthase I TruA alpha/beta"
FT                   /evidence="ECO:0000259|Pfam:PF01416"
FT   ACT_SITE        54
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00171,
FT                   ECO:0000256|PIRSR:PIRSR001430-1"
FT   BINDING         112
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00171,
FT                   ECO:0000256|PIRSR:PIRSR001430-2"
SQ   SEQUENCE   261 AA;  29012 MW;  468017D3E6F53235 CRC64;
     MTTRYVLTLA YNGSAFYGWQ KQTADVPTVQ SALEHALSVI AQQPIKVTAA GRTDTGVHAT
     AQVVHFDSDA NRPISAWVRG VNAHLPNDVA VLHAQAVASE FHARFDAFAR RYRYVLQFAP
     VRSPLLVGRA GWTHYNLDIN NIQAACQFLL GEHDFSSFRA AECQAKSPIK TMYSIDIQAM
     GDLIKLDFHA NAFLHHMIRN IVGALVYVGS GRLSVNEFAE LIEKRSRLDA PPTFMPDGLY
     FAGADYPEHF GLMRVPLPVW L
//
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