ID A0A1Q7UPC6_9CHLR Unreviewed; 401 AA.
AC A0A1Q7UPC6;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=PUA domain-containing protein {ECO:0000259|SMART:SM00359};
GN ORFNames=AUG82_07930 {ECO:0000313|EMBL:OLE02622.1};
OS Ktedonobacter sp. 13_1_20CM_4_53_11.
OC Bacteria; Chloroflexota; Ktedonobacteria; Ktedonobacterales;
OC Ktedonobacteraceae; Ktedonobacter.
OX NCBI_TaxID=1805225 {ECO:0000313|EMBL:OLE02622.1, ECO:0000313|Proteomes:UP000186213};
RN [1] {ECO:0000313|EMBL:OLE02622.1, ECO:0000313|Proteomes:UP000186213}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27843720;
RA Butterfield C.N., Li Z., Andeer P.F., Spaulding S., Thomas B.C., Singh A.,
RA Hettich R.L., Suttle K.B., Probst A.J., Tringe S.G., Northen T., Pan C.,
RA Banfield J.F.;
RT "Proteogenomic analyses indicate bacterial methylotrophy and archaeal
RT heterotrophy are prevalent below the grass root zone.";
RL PeerJ 4:E2687-E2687(2016).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. RlmI family.
CC {ECO:0000256|ARBA:ARBA00038091}.
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:OLE02622.1}.
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DR EMBL; MNIY01000151; OLE02622.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q7UPC6; -.
DR STRING; 1805225.AUG82_07930; -.
DR Proteomes; UP000186213; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR CDD; cd02440; AdoMet_MTases; 1.
DR CDD; cd21153; PUA_RlmI; 1.
DR CDD; cd11572; RlmI_M_like; 1.
DR Gene3D; 2.30.130.10; PUA domain; 1.
DR Gene3D; 3.30.750.80; RNA methyltransferase domain (HRMD) like; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR002478; PUA.
DR InterPro; IPR015947; PUA-like_sf.
DR InterPro; IPR036974; PUA_sf.
DR InterPro; IPR041532; RlmI-like_PUA.
DR InterPro; IPR019614; SAM-dep_methyl-trfase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR42873:SF1; METHYLTRANS_SAM DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR42873; RIBOSOMAL RNA LARGE SUBUNIT METHYLTRANSFERASE; 1.
DR Pfam; PF10672; Methyltrans_SAM; 1.
DR Pfam; PF17785; PUA_3; 1.
DR SMART; SM00359; PUA; 1.
DR SUPFAM; SSF88697; PUA domain-like; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS50890; PUA; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW rRNA processing {ECO:0000256|ARBA:ARBA00022552};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 8..93
FT /note="PUA"
FT /evidence="ECO:0000259|SMART:SM00359"
SQ SEQUENCE 401 AA; 44678 MW; 82340EE4481031EB CRC64;
MSSSVHYPSA SLKPHREESL QSGHLWIFSG ALQQPPHWIE PGGLVDVKSS TGKFVARGYY
NPHTDIAIRI LTNDIEEAID REFLRRRIRS AIELRQIFDA DRTNTYRLIH SEGDGLPGLV
VDRYADILVA QIHTAGMDRL RPLLIDAFME ETGAAGMLFR NEGQSRRREG LELEEPVVAA
GIVPDHVTVQ ENGVQFIIDP WHGQKTGFFL DQRDKREALR KYARNKRVLN CFSYTGGFSV
YAALNGDTTT VTSVDISASA IDMARSHFVL NGLDPDAHAF LVADVFDYLE EAQQHGEQFD
VVVLDPPAFA KTQAARSQAL KAYRRLNMLG IQVLRPGGIL LTCSCSGVVG MDDLLGTLSQ
VARHLRRPVQ LLESYTHGAD HPINLVMPET VYLKAVYCRV G
//
