ID A0A1F8QUY8_9CHLR Unreviewed; 545 AA.
AC A0A1F8QUY8;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE RecName: Full=YTH domain-containing protein {ECO:0000259|PROSITE:PS50882};
GN ORFNames=A2147_11735 {ECO:0000313|EMBL:OGO38982.1};
OS Chloroflexi bacterium RBG_16_57_8.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1797652 {ECO:0000313|EMBL:OGO38982.1, ECO:0000313|Proteomes:UP000178359};
RN [1] {ECO:0000313|EMBL:OGO38982.1, ECO:0000313|Proteomes:UP000178359}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
CC -!- SIMILARITY: Belongs to the TPP enzyme family.
CC {ECO:0000256|ARBA:ARBA00007812, ECO:0000256|RuleBase:RU362132}.
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:OGO38982.1}.
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DR EMBL; MGNT01000076; OGO38982.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8QUY8; -.
DR Proteomes; UP000178359; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR CDD; cd00568; TPP_enzymes; 1.
DR CDD; cd07035; TPP_PYR_POX_like; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR Gene3D; 3.40.50.1220; TPP-binding domain; 1.
DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom.
DR InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom.
DR InterPro; IPR000399; TPP-bd_CS.
DR InterPro; IPR045229; TPP_enz.
DR InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR InterPro; IPR007275; YTH_domain.
DR PANTHER; PTHR18968:SF167; 2-KETOARGININE DECARBOXYLASE ARUI-RELATED; 1.
DR PANTHER; PTHR18968; THIAMINE PYROPHOSPHATE ENZYMES; 1.
DR Pfam; PF02775; TPP_enzyme_C; 1.
DR Pfam; PF00205; TPP_enzyme_M; 1.
DR Pfam; PF02776; TPP_enzyme_N; 1.
DR SUPFAM; SSF52467; DHS-like NAD/FAD-binding domain; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR PROSITE; PS00187; TPP_ENZYMES; 1.
DR PROSITE; PS50882; YTH; 1.
PE 3: Inferred from homology;
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU362132}.
FT DOMAIN 485..545
FT /note="YTH"
FT /evidence="ECO:0000259|PROSITE:PS50882"
SQ SEQUENCE 545 AA; 58542 MW; 2B8503977F1403AF CRC64;
MALRTGGQAI VDSLRSQGVT HAFGLISVHM MDVYDALYEA RDSLQLIGGR HESAVAYMAD
GYARASSKPG VCFTSTGPGA ANSVGAVGEA YHCSSPVLNI TSNSERELIN SDRGGLHEPK
DQLGMFGSVT QWSALVPCVE AIPDHVRQAF DLFLNRRPRP VELEIPTDVL SHKADVQPAP
AVQRTRQQGD ARLVEQAARM LAAARKPVIW AGGGIPSSEA TPDLLRLAEL LGAPVTTSYG
GKGGFPDDHP LALGCSIGGR VYGRNPVFDF IESCDVALVV GARLPYRATI GVGLKLPPNL
IHIDIDGGVF GKNYQPAVAI TGDAGAVLGK LADSLEGKNV ARSESFAMEV ADLHRRVKQV
LRESGPNQQE TMEAIRGVIS RDAIIVADPT APGYWATRGM PCYEPRTYLS PHGWGGIGFA
FPAALGAKVA RPERQVIVIS GDGGFQFNIQ ELGTAAQYGI KVVVLVFNNG AWGVLRDRQR
DYFGGRYYAT ELKNPDFVRL ADSYGLPATH ARNCRDMTAA LQDALDKDEF RLIEVDISRG
FAEFV
//
