PO21_NASVI
ID PO21_NASVI Reviewed; 1025 AA.
AC Q03278;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Retrovirus-related Pol polyprotein from type-1 retrotransposable element R2;
DE AltName: Full=Retrovirus-related Pol polyprotein from type I retrotransposable element R2;
DE Includes:
DE RecName: Full=Reverse transcriptase;
DE EC=2.7.7.49;
DE Includes:
DE RecName: Full=Endonuclease;
DE Flags: Fragment;
OS Nasonia vitripennis (Parasitic wasp).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Parasitoida; Chalcidoidea;
OC Pteromalidae; Pteromalinae; Nasonia.
OX NCBI_TaxID=7425;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8383793; DOI=10.1093/oxfordjournals.molbev.a039990;
RA Burke W.D., Eickbush D.G., Xiong Y., Jakubczak J.L., Eickbush T.H.;
RT "Sequence relationship of retrotransposable elements R1 and R2 within and
RT between divergent insect species.";
RL Mol. Biol. Evol. 10:163-185(1993).
RN [2]
RP SEQUENCE REVISION.
RA Burke W.D., Eickbush D.G., Xiong Y., Jakubczak J.L., Eickbush T.H.;
RL Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
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};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L00950; AAC34927.1; -; Genomic_DNA.
DR PIR; T10259; T10259.
DR AlphaFoldDB; Q03278; -.
DR PRIDE; Q03278; -.
DR Proteomes; UP000002358; Unplaced.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003964; F:RNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.70.270; -; 1.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR000477; RT_dom.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00078; RVT_1; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS50878; RT_POL; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 4: Predicted;
KW Endonuclease; Hydrolase; Metal-binding; Nuclease; Nucleotidyltransferase;
KW Reference proteome; RNA-directed DNA polymerase; Transferase;
KW Transposable element; Zinc; Zinc-finger.
FT CHAIN <1..1025
FT /note="Retrovirus-related Pol polyprotein from type-1
FT retrotransposable element R2"
FT /id="PRO_0000058497"
FT DOMAIN 358..635
FT /note="Reverse transcriptase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00405"
FT ZN_FING 46..69
FT /note="C2H2-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 146..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 755..1025
FT /note="Nucleic acid-binding endonuclease"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..162
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
SQ SEQUENCE 1025 AA; 115885 MW; 387BDE63BCF5C518 CRC64;
NQIKKSNTST GARIPKAMTN PADNFAGGQW KPPGRRSART SATGMFVCEH CLRAFTTNTG
RGLHIKRAHE EQANEAITTE RSRARWTNEE MEAVQAEIDC EGRTAINQEI LRIIPYQRTI
DAIKCLRKQQ KYKTIRERVA NRRAENRARE TELTRLETAD EDPASQEQDN PNMSLKNWLK
EVIESDDDRL CADLRTAIEM ALAGQSPLDV CTVGCYQYTM TNLPLVPVRL GGPIYWCNAQ
SRSNPGETQR RQTIKESNNS WKKNMSKAAH IVLDGDTDAC PAGLEGTEAS GAIMRAGCPT
TRHLRSRMQG EIKNLWRPIS NDEIKEVEAC KRTAAGPDGM TTTAWNSIDE CIKSLFNMIM
YHGQCPRRYL DSRTVLIPKE PGTMDPACFR PLSIASVALR HFHRILANRI GEHGLLDTRQ
RAFIVADGVA ENTSLLSAMI KEARMKIKGL YIAILDVKKA FDSVEHRSIL DALRRKKLPL
EMRNYIMWVY RNSKTRLEVV KTKGRWIRPA RGVRQGDPLS PLLFNCVMDA VLRRLPENTG
FLMGAEKIGA LVFADDLVLL AETREGLQAS LSRIEAGLQE QGLEMMPRKC HTLALVPSGK
EKKIKVETHK PFTVGNQEIT QLGHADQWKY LGVVYNSYGP IQVKINIAGD LQRVTAAPLK
PQQRMAILGM FLIPRFIHKL VLGRTSNADV RKGDKIIRKT VRGWLRLPHD TPIGYFHAPI
KEGGLGIPAF ESRIPELLKS RIEALGASNM QTARSLLGGD WVAERKKWIN TQKIKNSEWA
QKLHLTTDGK DLRDTRKAEA SYSWIRDIHV AIPASVWIKY HHTRINALPT LMRMSRGRRT
NGNALCRAGC GLPETLYHVV QQCPRTHGGR VLRHDKIAEQ VAIFMQEKGW LVLREAHIRT
SVGLRKPDII ARKGQDCKII DCQIVTTGND IRIQHERKIQ YYASNWELRR SAATMIGHQG
QVSVEAITIS WKGVWEPRSY CLLRDCGIPK VKIKGLTTRV LLGAYLNFNT FSKATYRTER
RRTAN