ID A0A0P9CF42_9BACL Unreviewed; 470 AA.
AC A0A0P9CF42;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=DNA polymerase {ECO:0000313|EMBL:KPV44212.1};
GN ORFNames=AN477_08315 {ECO:0000313|EMBL:KPV44212.1};
OS Alicyclobacillus ferrooxydans.
OC Bacteria; Bacillota; Bacilli; Bacillales; Alicyclobacillaceae;
OC Alicyclobacillus.
OX NCBI_TaxID=471514 {ECO:0000313|EMBL:KPV44212.1, ECO:0000313|Proteomes:UP000050482};
RN [1] {ECO:0000313|EMBL:KPV44212.1, ECO:0000313|Proteomes:UP000050482}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TC-34 {ECO:0000313|EMBL:KPV44212.1,
RC ECO:0000313|Proteomes:UP000050482};
RA Hemp J.;
RT "Draft genome sequence of Alicyclobacillus ferrooxydans DSM 22381.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the bacterial reverse transcriptase family.
CC {ECO:0000256|ARBA:ARBA00034120}.
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:KPV44212.1}.
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DR EMBL; LJCO01000039; KPV44212.1; -; Genomic_DNA.
DR RefSeq; WP_054968713.1; NZ_LJCO01000039.1.
DR AlphaFoldDB; A0A0P9CF42; -.
DR PATRIC; fig|471514.4.peg.5232; -.
DR OrthoDB; 9793236at2; -.
DR Proteomes; UP000050482; Unassembled WGS sequence.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003964; F:RNA-directed DNA polymerase activity; IEA:InterPro.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR CDD; cd01651; RT_G2_intron; 1.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR030931; Group_II_RT_mat.
DR InterPro; IPR013597; Mat_intron_G2.
DR InterPro; IPR000123; Reverse_transcriptase_msDNA.
DR InterPro; IPR000477; RT_dom.
DR NCBIfam; TIGR04416; group_II_RT_mat; 1.
DR PANTHER; PTHR34047:SF2; NUCLEAR INTRON MATURASE 1, MITOCHONDRIAL; 1.
DR PANTHER; PTHR34047; NUCLEAR INTRON MATURASE 1, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF08388; GIIM; 1.
DR Pfam; PF00078; RVT_1; 1.
DR PRINTS; PR00866; RNADNAPOLMS.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR PROSITE; PS50878; RT_POL; 1.
PE 3: Inferred from homology;
KW Antiviral defense {ECO:0000256|ARBA:ARBA00023118};
KW Reference proteome {ECO:0000313|Proteomes:UP000050482}.
FT DOMAIN 97..323
FT /note="Reverse transcriptase"
FT /evidence="ECO:0000259|PROSITE:PS50878"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 470 AA; 54600 MW; 9C197E80B0C500F8 CRC64;
MASSGEKQRQ PNIPQGSYPQ EEVVNPRGTE EAPSFSPARP NELTREEGCI DLMEQVVERE
NLLSALRRVE RNKGAAGIDG TEIKSLRPFL MEHWQRIRSE LLHGTYQPLP IRRVEIPKPD
GGKRMLGIPA VLDRLIQQAL LQVLTPIFDP EFSWYSYGFR QGRSAHQAVN QAQMYIAEGY
RFVVDMDLAQ FFDRVNHDML MARVARKVDD KRVLKLIRGY LNAGVMVHGV CVSTEEGVPQ
GGPLSPLLAN IMLDDLDREL VRRGHRFVRY ADDCNVYVKS RHAGERVMES VRRFVEERLK
LKVNVDKSAV DRPWKRKFLG FSFTPNKVPR IRVAPKSLKR FKDKVRQLTS RSRGQSMEQR
LEWLNAYLRG WAGYYRHAQT RSVFEDLDKW IRRRLRMCLL KQWKKPKTKR RNLVTLGIPE
DWAVLISASR KGYWRNAKTP QMNKALGLAY WRDRGLVSLV ERYDGIRSTT
//