ID A0A0T5ZGX4_9ARCH Unreviewed; 332 AA.
AC A0A0T5ZGX4;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=XU09_C0001G0136 {ECO:0000313|EMBL:KRT62074.1};
OS Thaumarchaeota archaeon CSP1-1.
OC Archaea; Nitrososphaerota.
OX NCBI_TaxID=1640512 {ECO:0000313|EMBL:KRT62074.1, ECO:0000313|Proteomes:UP000051388};
RN [1] {ECO:0000313|EMBL:KRT62074.1, ECO:0000313|Proteomes:UP000051388}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CSP1-1 {ECO:0000313|EMBL:KRT62074.1};
RA Hug L.A., Thomas B.C., Sharon I., Brown C.T., Sharma R., Hettich R.L.,
RA Wilkins M.J., Williams K.H., Singh A., Banfield J.F.;
RT "Critical biogeochemical functions in the subsurface are associated with
RT bacteria from new phyla and little studied lineages.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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:KRT62074.1}.
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DR EMBL; LDXL01000001; KRT62074.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0T5ZGX4; -.
DR STRING; 1640512.XU09_C0001G0136; -.
DR PATRIC; fig|1640512.3.peg.137; -.
DR Proteomes; UP000051388; 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; cd21148; PUA_Cbf5; 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 InterPro; IPR004521; Uncharacterised_CHP00451.
DR NCBIfam; TIGR00425; CBF5; 1.
DR NCBIfam; TIGR00451; unchar_dom_2; 1.
DR PANTHER; PTHR23127; CENTROMERE/MICROTUBULE BINDING PROTEIN CBF5; 1.
DR PANTHER; PTHR23127:SF0; H_ACA RIBONUCLEOPROTEIN COMPLEX SUBUNIT DKC1; 1.
DR Pfam; PF08068; DKCLD; 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|HAMAP-Rule:MF_01081};
KW tRNA processing {ECO:0000256|HAMAP-Rule:MF_01081}.
FT DOMAIN 1..53
FT /note="Dyskerin-like"
FT /evidence="ECO:0000259|SMART:SM01136"
FT DOMAIN 241..315
FT /note="PUA"
FT /evidence="ECO:0000259|SMART:SM00359"
FT ACT_SITE 72
FT /note="Nucleophile"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01081"
SQ SEQUENCE 332 AA; 37574 MW; 43DF210D75895825 CRC64;
MTLKQLQNLT EIDQDITDNN YGTYYDKRSL DQLLKYGFIL LDKPPGPTSH ETVAWLKRIL
KIPKAGHSGT LDPQVSGVLP MGLGDGTKAL EVLLYGPKEY HALGRLHSLP SKEKLKKVLE
EFTGEIYQKP PQRSAVLRQT RTRTIYELEL LEQKERLLLL RILCEAGTYI RKLIYDIGEI
LGPGATMIEL RRTRVHQFTE NSHLVTLHEL ANAYSLWTEK KDDSKLLELI RPIEHVLSEL
KSVVIRDSAV DALCHGAQLA IPGVLQVSPN LKKDDLVAIY TQKGEVVALA KSLLSEADIK
ENTKGYAFET KRIIMAPSTY PKRWHSKQST NK
//
