ID   K1RU45_9ZZZZ            Unreviewed;       393 AA.
AC   K1RU45;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Thiamine biosynthesis/tRNA modification protein ThiI {ECO:0000313|EMBL:EKC45015.1};
GN   ORFNames=OBE_17170 {ECO:0000313|EMBL:EKC45015.1};
OS   human gut metagenome.
OC   unclassified sequences; metagenomes; organismal metagenomes.
OX   NCBI_TaxID=408170 {ECO:0000313|EMBL:EKC45015.1};
RN   [1] {ECO:0000313|EMBL:EKC45015.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=22891823; DOI=10.1111/j.1462-2920.2012.02845.x;
RA   Ferrer M., Ruiz A., Lanza F., Haange S.B., Oberbach A., Till H.,
RA   Bargiela R., Campoy C., Segura M.T., Richter M., von Bergen M., Seifert J.,
RA   Suarez A.;
RT   "Microbiota from the distal guts of lean and obese adolescents exhibit
RT   partial functional redundancy besides clear differences in community
RT   structure.";
RL   Environ. Microbiol. 15:211-226(2013).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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:EKC45015.1}.
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DR   EMBL; AJWZ01011491; EKC45015.1; -; Genomic_DNA.
DR   AlphaFoldDB; K1RU45; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004810; F:CCA tRNA nucleotidyltransferase activity; IEA:InterPro.
DR   GO; GO:0016783; F:sulfurtransferase activity; IEA:InterPro.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0034227; P:tRNA thio-modification; IEA:InterPro.
DR   CDD; cd01712; ThiI; 1.
DR   CDD; cd11716; THUMP_ThiI; 1.
DR   Gene3D; 3.30.2130.30; -; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   HAMAP; MF_00021; ThiI; 1.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR020536; ThiI_AANH.
DR   InterPro; IPR004114; THUMP_dom.
DR   InterPro; IPR003720; tRNA_STrfase.
DR   NCBIfam; TIGR00342; tRNA uracil 4-sulfurtransferase ThiI; 1.
DR   PANTHER; PTHR43209; TRNA SULFURTRANSFERASE; 1.
DR   PANTHER; PTHR43209:SF1; TRNA SULFURTRANSFERASE; 1.
DR   Pfam; PF02568; ThiI; 1.
DR   Pfam; PF02926; THUMP; 1.
DR   SMART; SM00981; THUMP; 1.
DR   SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR   SUPFAM; SSF143437; THUMP domain-like; 1.
DR   PROSITE; PS51165; THUMP; 1.
PE   3: Inferred from homology;
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   Thiamine biosynthesis {ECO:0000256|ARBA:ARBA00022977};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   tRNA-binding {ECO:0000256|ARBA:ARBA00022555}.
FT   DOMAIN          58..161
FT                   /note="THUMP"
FT                   /evidence="ECO:0000259|PROSITE:PS51165"
SQ   SEQUENCE   393 AA;  44902 MW;  D6E7EC86C6F32910 CRC64;
     MNRLILIKYG ELTTKKGNRN FFIKTLTKNI EHKLSNFNIK IKKDLSRMCI YFNDCDLKKI
     IDTIKDIFGI HAYHVAYITN TNIDDIASTV LELLKEKKFK TFKIETKRGD KSFPLSSPEV
     SKKLGGHILK NIPNINVDVH NPEVLVKVEI TATETYIYLD SYKGSGGYPV GTQPRALLML
     SGGIDSPVAG YLAMKRGIKL DCVYFEAIPH TSMQAREKVI ELTKKLVKYT DSINLHIVNF
     TPIQEEIYKT SDPNYVITIM RRMMYRIMER LAKRNKAYAI INGESIGQVA SQTLVSMRTI
     NSVTNFPVIR PVACLDKLEI IDIAQKIDTY ETSILPYEDC CTVFVPKHPV INPNMYTCEE
     LEKKFNFEEM VSVAVKNTMT IKIKDIDDVN DLL
//