ID Q5P8H7_AROAE Unreviewed; 639 AA.
AC Q5P8H7;
DT 04-JAN-2005, integrated into UniProtKB/TrEMBL.
DT 04-JAN-2005, sequence version 1.
DT 27-MAR-2024, entry version 88.
DE RecName: Full=RNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00012493};
DE EC=2.7.7.49 {ECO:0000256|ARBA:ARBA00012493};
GN ORFNames=ebA511 {ECO:0000313|EMBL:CAI06382.1};
OS Aromatoleum aromaticum (strain EbN1) (Azoarcus sp. (strain EbN1)).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales;
OC Rhodocyclaceae; Aromatoleum.
OX NCBI_TaxID=76114 {ECO:0000313|EMBL:CAI06382.1, ECO:0000313|Proteomes:UP000006552};
RN [1] {ECO:0000313|EMBL:CAI06382.1, ECO:0000313|Proteomes:UP000006552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EbN1 {ECO:0000313|EMBL:CAI06382.1,
RC ECO:0000313|Proteomes:UP000006552};
RX PubMed=15551059; DOI=10.1007/s00203-004-0742-9;
RA Rabus R., Kube M., Heider J., Beck A., Heitmann K., Widdel F.,
RA Reinhardt R.;
RT "The genome sequence of an anaerobic aromatic-degrading denitrifying
RT bacterium, strain EbN1.";
RL Arch. Microbiol. 183:27-36(2005).
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;
CC Evidence={ECO:0000256|ARBA:ARBA00024557};
CC -!- SIMILARITY: Belongs to the bacterial reverse transcriptase family.
CC {ECO:0000256|ARBA:ARBA00034120}.
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DR EMBL; CR555306; CAI06382.1; -; Genomic_DNA.
DR AlphaFoldDB; Q5P8H7; -.
DR STRING; 76114.ebA511; -.
DR KEGG; eba:ebA511; -.
DR eggNOG; COG0265; Bacteria.
DR eggNOG; COG3344; Bacteria.
DR HOGENOM; CLU_034461_0_0_4; -.
DR OrthoDB; 7055795at2; -.
DR Proteomes; UP000006552; Chromosome.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003964; F:RNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR CDD; cd03487; RT_Bac_retron_II; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR000123; Reverse_transcriptase_msDNA.
DR InterPro; IPR000477; RT_dom.
DR PANTHER; PTHR34047; NUCLEAR INTRON MATURASE 1, MITOCHONDRIAL-RELATED; 1.
DR PANTHER; PTHR34047:SF7; RNA-DIRECTED DNA POLYMERASE; 1.
DR Pfam; PF00078; RVT_1; 1.
DR Pfam; PF13365; Trypsin_2; 1.
DR PRINTS; PR00866; RNADNAPOLMS.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS50878; RT_POL; 1.
PE 3: Inferred from homology;
KW Antiviral defense {ECO:0000256|ARBA:ARBA00023118};
KW Nucleotidyltransferase {ECO:0000313|EMBL:CAI06382.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006552};
KW RNA-directed DNA polymerase {ECO:0000313|EMBL:CAI06382.1};
KW Transferase {ECO:0000313|EMBL:CAI06382.1}.
FT DOMAIN 30..262
FT /note="Reverse transcriptase"
FT /evidence="ECO:0000259|PROSITE:PS50878"
FT REGION 613..639
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 621..639
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 639 AA; 71303 MW; 895CBC502B07A1F1 CRC64;
MAILLSLDQI VEALVRSEPA SFSRDVLGMP YDSLKAIIYP RPPYKSFTIK KRDGSDRTIF
EPRKRLKVIQ LKVLDFLQKR STPLKPAVHG FVAKRSILTN AQVHCSPKNH HIFNIDLEDF
FPSITFYRVR GVLLHHPFKF SHEVATVIAH ICTLDKTLPQ GAPTSPFLSN LVCRTLDRDL
TELARRCLAR YSRYADDITF SFRTRKTIKL PAAICSVDSD GDTVIGTELH DIIVNQHHFK
INSAKTRLCD RNRRMEVTGL TINQFPNVPR VFIDRIRGAL IAWESHGYAA ANKVWNERVT
AARSGAYEKK PWKRQTRRGQ VPDLKNVLWG KLLYLRMVRG KDDLIYTRLA ERYNSAVLIT
AATGTFTAPK LPVEPVVRDK ETARDACFVV EWMGDYDEPG VGTEVPISQG TAFVYRELNL
LVTCNHVLEW QNGEEGKFLA QIDYESPFLS DKALKLIQPG TKKSWDAKIL YRNEQMDFAL
LAFEDPPQHR YFSAMDNPIE PGAKGFLIGY PAWKQWNLAD VNSQTVLNRT SPHAGMNSFT
ITGAGSIRPG NSGGPFTDDR FRVAGMAQRG AYMGDGHDEN LCIEIIDELI AAYKASLVAP
AVLVPAASAA APASPATAAP SAKPTAPPPA PTPPPPVMP
//