RT162_MYXXA
ID RT162_MYXXA Reviewed; 485 AA.
AC P23072;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Retron Mx162 reverse transcriptase {ECO:0000305};
DE Short=Mx162-RT;
DE EC=2.7.7.49 {ECO:0000255|PROSITE-ProRule:PRU00405};
DE AltName: Full=RNA-directed DNA polymerase from retron Mx162;
OS Myxococcus xanthus.
OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC Cystobacterineae; Myxococcaceae; Myxococcus.
OX NCBI_TaxID=34;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2465092; DOI=10.1016/0092-8674(89)90593-x;
RA Inouye S., Hsu M.Y., Eagle S., Inouye M.;
RT "Reverse transcriptase associated with the biosynthesis of the branched
RT RNA-linked msDNA in Myxococcus xanthus.";
RL Cell 56:709-717(1989).
RN [2]
RP MSDNA IDENTIFICATION, AND ACTIVITY REGULATION.
RC STRAIN=DZF1;
RX PubMed=2446773; DOI=10.1016/0092-8674(87)90596-4;
RA Dhundale A., Lampson B., Furuichi T., Inouye M., Inouye S.;
RT "Structure of msDNA from Myxococcus xanthus: evidence for a long, self-
RT annealing RNA precursor for the covalently linked, branched RNA.";
RL Cell 51:1105-1112(1987).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=DZF1;
RX PubMed=2461359; DOI=10.1128/jb.170.12.5620-5624.1988;
RA Dhundale A., Furuichi T., Inouye M., Inouye S.;
RT "Mutations that affect production of branched RNA-linked msDNA in
RT Myxococcus xanthus.";
RL J. Bacteriol. 170:5620-5624(1988).
RN [4]
RP FUNCTION, AND MODEL OF THE REACTION MECHANISM.
RC STRAIN=DZF1;
RX PubMed=2465091; DOI=10.1016/0092-8674(89)90592-8;
RA Lampson B.C., Inouye M., Inouye S.;
RT "Reverse transcriptase with concomitant ribonuclease H activity in the
RT cell-free synthesis of branched RNA-linked msDNA of Myxococcus xanthus.";
RL Cell 56:701-707(1989).
CC -!- FUNCTION: Reverse transcriptase (RT) responsible for synthesis of
CC msDNA-Mx162 (a branched molecule with RNA linked by a 2',5'-
CC phosphodiester bond to ssDNA). The retron transcript serves as primer
CC (from a conserved internal G residue) and template for the reaction,
CC and codes for the RT (Probable). The retron is involved in antiviral
CC defense (By similarity). {ECO:0000250|UniProtKB:P71276,
CC ECO:0000305|PubMed:2446773, ECO:0000305|PubMed:2465091,
CC ECO:0000305|PubMed:2465092}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC ChEBI:CHEBI:173112; EC=2.7.7.49; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU00405, ECO:0000305|PubMed:2446773,
CC ECO:0000305|PubMed:2461359, ECO:0000305|PubMed:2465091};
CC -!- ACTIVITY REGULATION: msDNA synthesis is inhibited by rifampicin and
CC chloramphenicol. {ECO:0000269|PubMed:2446773}.
CC -!- DISRUPTION PHENOTYPE: No production of msDNA. No other visible effect
CC on growth, morphogenesis, fruiting body formation, spore germination or
CC cell motility. {ECO:0000269|PubMed:2461359}.
CC -!- MISCELLANEOUS: M.xanthus contains two independent and unlinked retrons:
CC Mx65 and Mx162.
CC -!- MISCELLANEOUS: Retrons may be the ancestors of retrovirus.
CC -!- SIMILARITY: Belongs to the bacterial reverse transcriptase family.
CC {ECO:0000305}.
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DR EMBL; M24392; AAA25405.1; -; Genomic_DNA.
DR PIR; A31878; RRYC62.
DR AlphaFoldDB; P23072; -.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003964; F:RNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR CDD; cd03487; RT_Bac_retron_II; 1.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR000123; Reverse_transcriptase_msDNA.
DR InterPro; IPR000477; RT_dom.
DR Pfam; PF00078; RVT_1; 1.
DR PRINTS; PR00866; RNADNAPOLMS.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS50878; RT_POL; 1.
PE 3: Inferred from homology;
KW Antiviral defense; Magnesium; Metal-binding; Nucleotidyltransferase;
KW RNA-directed DNA polymerase; Transferase; Transposable element.
FT CHAIN 1..485
FT /note="Retron Mx162 reverse transcriptase"
FT /id="PRO_0000097503"
FT DOMAIN 167..407
FT /note="Reverse transcriptase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 250
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT BINDING 346
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT BINDING 347
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
SQ SEQUENCE 485 AA; 53018 MW; 7361221351C4194D CRC64;
MTARLDPFVP AASPQAVPTP ELTAPSSDAA AKREARRLAH EALLVRAKAI DEAGGADDWV
QAQLVSKGLA VEDLDFSSAS EKDKKAWKEK KKAEATERRA LKRQAHEAWK ATHVGHLGAG
VHWAEDRLAD AFDVPHREER ARANGLTELD SAEALAKALG LSVSKLRWFA FHREVDTATH
YVSWTIPKRD GSKRTITSPK PELKAAQRWV LSNVVERLPV HGAAHGFVAG RSILTNALAH
QGADVVVKVD LKDFFPSVTW RRVKGLLRKG GLREGTSTLL SLLSTEAPRE AVQFRGKLLH
VAKGPRALPQ GAPTSPGITN ALCLKLDKRL SALAKRLGFT YTRYADDLTF SWTKAKQPKP
RRTQRPPVAV LLSRVQEVVE AEGFRVHPDK TRVARKGTRQ RVTGLVVNAA GKDAPAARVP
RDVVRQLRAA IHNRKKGKPG REGESLEQLK GMAAFIHMTD PAKGRAFLAQ LTELESTASA
APQAE