ID T1DBI4_9ZZZZ Unreviewed; 224 AA.
AC T1DBI4;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Thiamine biosynthesis/tRNA modification protein ThiI {ECO:0000313|EMBL:EQD79465.1};
GN ORFNames=B1A_01712 {ECO:0000313|EMBL:EQD79465.1};
OS mine drainage metagenome.
OC unclassified sequences; metagenomes; ecological metagenomes.
OX NCBI_TaxID=410659 {ECO:0000313|EMBL:EQD79465.1};
RN [1] {ECO:0000313|EMBL:EQD79465.1}
RP NUCLEOTIDE SEQUENCE.
RA Mendez C., Richter M., Ferrer M., Sanchez J.;
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EQD79465.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=24430486; DOI=10.1038/ismej.2013.242;
RA Mendez-Garcia C., Mesa V., Sprenger R.R., Richter M., Diez M.S., Solano J.,
RA Bargiela R., Golyshina O.V., Manteca A., Ramos J.L., Gallego J.R.,
RA Llorente I., Martins Dos Santos V.A., Jensen O.N., Pelaez A.I., Sanchez J.,
RA Ferrer M.;
RT "Microbial stratification in low pH oxic and suboxic macroscopic growths
RT along an acid mine drainage.";
RL ISME J. 8:1259-1274(2014).
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:EQD79465.1}.
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DR EMBL; AUZX01001300; EQD79465.1; -; Genomic_DNA.
DR AlphaFoldDB; T1DBI4; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004810; F:CCA tRNA nucleotidyltransferase activity; IEA:InterPro.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR CDD; cd00158; RHOD; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 3.40.250.10; Rhodanese-like domain; 1.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR036873; Rhodanese-like_dom_sf.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR020536; ThiI_AANH.
DR PANTHER; PTHR43209; TRNA SULFURTRANSFERASE; 1.
DR PANTHER; PTHR43209:SF1; TRNA SULFURTRANSFERASE; 1.
DR Pfam; PF00581; Rhodanese; 1.
DR Pfam; PF02568; ThiI; 1.
DR SMART; SM00450; RHOD; 1.
DR SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 1.
DR PROSITE; PS50206; RHODANESE_3; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW tRNA-binding {ECO:0000256|ARBA:ARBA00022555}.
FT DOMAIN 132..199
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
SQ SEQUENCE 224 AA; 25532 MW; BDDF0555E8148C01 CRC64;
MYMLGEKIAL AHDYNGIITG ESSGQVSSQT PENLKELSRG MQIPVIRPLI GFDKDEISDL
ARMIGTFPKN PLGEFCSLFS ETPITKIKEN ELKSDIEMID FIDEMYAKLT KTKSSKVKIE
LPTDELYNTT KIPDSALVVD LRSPLEFRYW HYPNSLNMPI QKAEELIESG EAPLEIVFYC
KMGLQSAYLT SLAREHGIKS RFFSTDKIKK RKKCGRSNYI NDIM
//
