ID A0A0U1M546_TALIS Unreviewed; 579 AA.
AC A0A0U1M546;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=tRNA pseudouridine synthase B {ECO:0000313|EMBL:CRG90665.1};
GN ORFNames=PISL3812_07710 {ECO:0000313|EMBL:CRG90665.1};
OS Talaromyces islandicus (Penicillium islandicum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Islandici.
OX NCBI_TaxID=28573 {ECO:0000313|EMBL:CRG90665.1, ECO:0000313|Proteomes:UP000054383};
RN [1] {ECO:0000313|EMBL:CRG90665.1, ECO:0000313|Proteomes:UP000054383}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WF-38-12 {ECO:0000313|EMBL:CRG90665.1};
RA Syromyatnikov M.Y., Popov V.N.;
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a uridine in mRNA = a pseudouridine in mRNA;
CC Xref=Rhea:RHEA:56644, Rhea:RHEA-COMP:14658, Rhea:RHEA-COMP:14659,
CC ChEBI:CHEBI:65314, ChEBI:CHEBI:65315;
CC Evidence={ECO:0000256|ARBA:ARBA00001166};
CC -!- SIMILARITY: Belongs to the pseudouridine synthase TruB family.
CC {ECO:0000256|ARBA:ARBA00008999}.
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DR EMBL; CVMT01000008; CRG90665.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0U1M546; -.
DR STRING; 28573.A0A0U1M546; -.
DR OMA; QVKIGHG; -.
DR OrthoDB; 240562at2759; -.
DR Proteomes; UP000054383; Unassembled WGS sequence.
DR GO; GO:0009982; F:pseudouridine synthase activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR GO; GO:0001522; P:pseudouridine synthesis; IEA:InterPro.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR CDD; cd10507; Zn-ribbon_RPA12; 1.
DR Gene3D; 2.20.25.10; -; 1.
DR Gene3D; 3.30.2350.10; Pseudouridine synthase; 1.
DR HAMAP; MF_01080; TruB_bact; 1.
DR InterPro; IPR019761; DNA-dir_RNA_pol-M_15_CS.
DR InterPro; IPR020103; PsdUridine_synth_cat_dom_sf.
DR InterPro; IPR002501; PsdUridine_synth_N.
DR InterPro; IPR014780; tRNA_psdUridine_synth_TruB.
DR InterPro; IPR034004; Zn_ribbon_RPA12_C.
DR InterPro; IPR001222; Znf_TFIIS.
DR PANTHER; PTHR13767:SF2; PSEUDOURIDYLATE SYNTHASE TRUB1; 1.
DR PANTHER; PTHR13767; TRNA-PSEUDOURIDINE SYNTHASE; 1.
DR Pfam; PF01096; TFIIS_C; 1.
DR Pfam; PF01509; TruB_N; 1.
DR SMART; SM00440; ZnF_C2C2; 1.
DR SUPFAM; SSF55120; Pseudouridine synthase; 1.
DR SUPFAM; SSF57783; Zinc beta-ribbon; 1.
DR PROSITE; PS01030; RNA_POL_M_15KD; 1.
DR PROSITE; PS51133; ZF_TFIIS_2; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000054383};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00472}.
FT DOMAIN 72..112
FT /note="TFIIS-type"
FT /evidence="ECO:0000259|PROSITE:PS51133"
FT REGION 408..496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 452..473
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 476..490
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 579 AA; 64534 MW; 7687EE8F9969BA5F CRC64;
MVVQFCIDCG NLLDETPQDH VTCELCGKVA KNQMFSHVQT SVSKGFPSKL RTKLTSYTQK
VTAETLGSGP TIKMECPECP SNEVTWTEAQ LRSADEGSTI FYRCVKCGHR NIEVGGIELC
APKDSLSVDE LSRPGHQYRR KAIWNKNVQR QGLRGASRYF SCIYTYTGEE KLTSESIQAI
HKPEGITSAG VLRDLQTHFN PSATFQPWIE REQERRSNDN NYQRNKHRRR YRKRPEVKIG
HGGTLDPMAT GVLITGIGQG TKHLHTFLGC TKTYETVVTF GVASDTYDCT GKTVRRAAYE
HITRTMVEEA LAKFRGKIMQ RPPIFSAKRI DGKRLYEYAR EGIEPPVEIK SVPVEVFDLE
LLEWYEPGSH EYKWPQEEMS GPERVLAEKL LDKDAAIPVA SDAEAEAVEA QAAATKSPSS
KRKASPLPEK SEVADEQGSI SATKRVKTDG EELQSTTTTT TITTTTEADS LQTSKAVPGE
EKEEAKEVQK TEMPVPGPAA ARIRMTVSGG FYVRSLAHDL GKAVGSYGIM CSLVRTRQGD
YTLDADKVIN YSELEAGEEV WGPKVKQLLS EWQEKNQTE
//