ID   I0XR22_9LEPT            Unreviewed;       606 AA.
AC   I0XR22;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   SubName: Full=ThiF family protein {ECO:0000313|EMBL:EIE01330.1};
GN   ORFNames=LEP1GSC185_3448 {ECO:0000313|EMBL:EIE01330.1};
OS   Leptospira licerasiae serovar Varillal str. VAR 010.
OC   Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC   Leptospira.
OX   NCBI_TaxID=1049972 {ECO:0000313|EMBL:EIE01330.1, ECO:0000313|Proteomes:UP000004889};
RN   [1] {ECO:0000313|EMBL:EIE01330.1, ECO:0000313|Proteomes:UP000004889}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VAR 010 {ECO:0000313|EMBL:EIE01330.1};
RX   PubMed=23145189; DOI=10.1371/journal.pntd.0001853;
RA   Ricaldi J.N., Fouts D.E., Selengut J.D., Harkins D.M., Patra K.P.,
RA   Moreno A., Lehmann J.S., Purushe J., Sanka R., Torres M., Webster N.J.,
RA   Vinetz J.M., Matthias M.A.;
RT   "Whole Genome Analysis of Leptospira licerasiae Provides Insight into
RT   Leptospiral Evolution and Pathogenicity.";
RL   PLoS Negl. Trop. Dis. 6:E1853-E1853(2012).
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:EIE01330.1}.
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DR   EMBL; AHOO02000008; EIE01330.1; -; Genomic_DNA.
DR   RefSeq; WP_008589660.1; NZ_AHOO02000008.1.
DR   AlphaFoldDB; I0XR22; -.
DR   PATRIC; fig|1049972.3.peg.2144; -.
DR   OrthoDB; 4088010at2; -.
DR   Proteomes; UP000004889; Unassembled WGS sequence.
DR   GO; GO:0008641; F:ubiquitin-like modifier activating enzyme activity; IEA:InterPro.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR045886; ThiF/MoeB/HesA.
DR   InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR   InterPro; IPR035985; Ubiquitin-activating_enz.
DR   PANTHER; PTHR43267; TRNA THREONYLCARBAMOYLADENOSINE DEHYDRATASE; 1.
DR   PANTHER; PTHR43267:SF1; TRNA THREONYLCARBAMOYLADENOSINE DEHYDRATASE; 1.
DR   Pfam; PF00899; ThiF; 1.
DR   SUPFAM; SSF69572; Activating enzymes of the ubiquitin-like proteins; 1.
PE   4: Predicted;
FT   DOMAIN          371..479
FT                   /note="THIF-type NAD/FAD binding fold"
FT                   /evidence="ECO:0000259|Pfam:PF00899"
SQ   SEQUENCE   606 AA;  69701 MW;  07A0AFA284941CE8 CRC64;
     MLLRLKKDIE LLDIFDWVKV HSIDELEKQK VRIELSIRVD LPDIPVQYKK YSLSNWIFVI
     DNPYPRGVIE VYPAIDNGLN LTFPHQLDNS SVNKEYNSRS GKVCLADYFN KAKNRTDLFS
     SNFEGVVLHR HIVRLRAYLE CAFQKKLQNP GEYFELPSIP GLSGRARNEL YILFQETTES
     FLKWNKEARH FGYFEYVKTK PHAGRDFIFP CRFLDTNSDE VMLYHWSKEI LNQNSEEKIG
     IWVKCEKYPF QKDWAFPKTY GDLLNVYPEI LNRLQNSLLK AASVKGSLSK EKKVLVLLGF
     PVPLKYGDAC SEIFWIAFSV DLKEVQKFPG SRKNIKLSKY LQVVFESASS LNIAWQKTEN
     WAKGNLIQRG KSLALENLSA VIVGGGALGS VLIENLVRLG MDKIQIHDGD TIEAGNLSRF
     SASLTEVGIP KSIFLKKKLE LVRPGVEVTA HAHIFHRGPD IESWGAYDIL IDISADATVL
     SIFENYNPKK EKIWITVFLG MNAQRLYFFA SKSSKFMVQR FRDEYAKWAQ VEYSEQNLHR
     SDFRPEGTGC WDPLFPARLD DIISFTSAII TNIEKATKLA SGEFHFSVYE KVINEDMDYL
     GIRKVS
//