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POLR1_ARATH
ID   POLR1_ARATH             Reviewed;        1466 AA.
AC   Q94HW2; F7J134; Q9SLU4;
DT   25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Retrovirus-related Pol polyprotein from transposon RE1;
DE   AltName: Full=Retro element 1 {ECO:0000303|PubMed:10689195};
DE            Short=AtRE1 {ECO:0000303|PubMed:10689195};
DE   Includes:
DE     RecName: Full=Protease RE1;
DE              EC=3.4.23.-;
DE   Includes:
DE     RecName: Full=Reverse transcriptase RE1;
DE              EC=2.7.7.49;
DE   Includes:
DE     RecName: Full=Endonuclease RE1;
GN   Name=RE1; Synonyms=RF12, RF28 {ECO:0000303|PubMed:10689195};
GN   OrderedLocusNames=At1g58889 {ECO:0000305};
GN   ORFNames=R18I {ECO:0000312|EMBL:BAB84015.1};
GN   and
GN   Name=RE1; OrderedLocusNames=At1g59265 {ECO:0000305};
GN   ORFNames=T4M14.18 {ECO:0000312|EMBL:AAK62788.1};
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. C24;
RX   PubMed=24770782; DOI=10.1007/s00438-014-0855-z;
RA   Yamada M., Yamagishi Y., Akaoka M., Ito H., Kato A.;
RT   "Genomic localization of AtRE1 and AtRE2, copia-type retrotransposons, in
RT   natural variants of Arabidopsis thaliana.";
RL   Mol. Genet. Genomics 289:821-835(2014).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130712; DOI=10.1038/35048500;
RA   Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA   Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA   Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA   Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA   Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA   Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA   Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA   Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA   Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA   Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA   Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA   Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA   Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA   Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA   Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL   Nature 408:816-820(2000).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10548732; DOI=10.1016/s0378-1119(99)00403-5;
RA   Kato A., Suzuki M., Kuwahara A., Ooe H., Higano-Inaba K., Komeda Y.;
RT   "Isolation and analysis of cDNA within a 300 kb Arabidopsis thaliana
RT   genomic region located around the 100 map unit of chromosome 1.";
RL   Gene 239:309-316(1999).
RN   [5]
RP   GENE FAMILY, AND NOMENCLATURE.
RC   STRAIN=cv. Columbia;
RX   PubMed=10689195; DOI=10.1016/s0378-1119(99)00565-x;
RA   Kuwahara A., Kato A., Komeda Y.;
RT   "Isolation and characterization of copia-type retrotransposons in
RT   Arabidopsis thaliana.";
RL   Gene 244:127-136(2000).
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   -!- SEQUENCE CAUTION:
CC       Sequence=BAA87949.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AB605839; BAK41511.1; -; Genomic_DNA.
DR   EMBL; AC027036; AAK62788.1; -; Genomic_DNA.
DR   EMBL; AB078516; BAB84015.1; -; Genomic_DNA.
DR   EMBL; CP002684; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AB028223; BAA87949.1; ALT_FRAME; mRNA.
DR   PIR; T52436; T52436.
DR   AlphaFoldDB; Q94HW2; -.
DR   SMR; Q94HW2; -.
DR   MEROPS; A11.004; -.
DR   PeptideAtlas; Q94HW2; -.
DR   PRIDE; Q94HW2; -.
DR   Araport; AT1G58889; -.
DR   Araport; AT1G59265; -.
DR   PRO; PR:Q94HW2; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q94HW2; baseline and differential.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0003964; F:RNA-directed DNA polymerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0015074; P:DNA integration; IEA:UniProtKB-KW.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.420.10; -; 1.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR025724; GAG-pre-integrase_dom.
DR   InterPro; IPR001584; Integrase_cat-core.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   InterPro; IPR013103; RVT_2.
DR   Pfam; PF13976; gag_pre-integrs; 1.
DR   Pfam; PF00665; rve; 1.
DR   Pfam; PF07727; RVT_2; 1.
DR   SUPFAM; SSF53098; SSF53098; 1.
DR   SUPFAM; SSF56672; SSF56672; 1.
DR   PROSITE; PS50994; INTEGRASE; 1.
PE   2: Evidence at transcript level;
KW   Aspartyl protease; DNA integration; DNA recombination; Endonuclease;
KW   Hydrolase; Magnesium; Metal-binding; Nuclease; Protease;
KW   Reference proteome; Transferase; Zinc; Zinc-finger.
FT   CHAIN           1..1466
FT                   /note="Retrovirus-related Pol polyprotein from transposon
FT                   RE1"
FT                   /id="PRO_0000441908"
FT   DOMAIN          519..682
FT                   /note="Integrase catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00457"
FT   DOMAIN          982..1225
FT                   /note="Reverse transcriptase Ty1/copia-type"
FT                   /evidence="ECO:0000255"
FT   ZN_FING         278..294
FT                   /note="CCHC-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00047"
FT   REGION          227..270
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          772..927
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        795..831
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        839..901
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        913..927
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        334
FT                   /note="For protease activity"
FT                   /evidence="ECO:0000250"
FT   BINDING         530
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00457"
FT   BINDING         592
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00457"
FT   CONFLICT        149
FT                   /note="L -> F (in Ref. 1; BAK41511)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        235
FT                   /note="N -> T (in Ref. 4; BAA87949)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1019
FT                   /note="A -> V (in Ref. 1; BAK41511)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1466 AA;  163905 MW;  FF1A4143B1161D43 CRC64;
     MAAHAEELVL NNTSILNVNM SNVTKLTSTN YLMWSRQVHA LFDGYELAGF LDGSTTMPPA
     TIGTDAAPRV NPDYTRWKRQ DKLIYSAVLG AISMSVQPAV SRATTAAQIW ETLRKIYANP
     SYGHVTQLRT QLKQWTKGTK TIDDYMQGLV TRFDQLALLG KPMDHDEQVE RVLENLPEEY
     KPVIDQIAAK DTPPTLTEIH ERLLNHESKI LAVSSATVIP ITANAVSHRN TTTTNNNNNG
     NRNNRYDNRN NNNNSKPWQQ SSTNFHPNNN QSKPYLGKCQ ICGVQGHSAK RCSQLQHFLS
     SVNSQQPPSP FTPWQPRANL ALGSPYSSNN WLLDSGATHH ITSDFNNLSL HQPYTGGDDV
     MVADGSTIPI SHTGSTSLST KSRPLNLHNI LYVPNIHKNL ISVYRLCNAN GVSVEFFPAS
     FQVKDLNTGV PLLQGKTKDE LYEWPIASSQ PVSLFASPSS KATHSSWHAR LGHPAPSILN
     SVISNYSLSV LNPSHKFLSC SDCLINKSNK VPFSQSTINS TRPLEYIYSD VWSSPILSHD
     NYRYYVIFVD HFTRYTWLYP LKQKSQVKET FITFKNLLEN RFQTRIGTFY SDNGGEFVAL
     WEYFSQHGIS HLTSPPHTPE HNGLSERKHR HIVETGLTLL SHASIPKTYW PYAFAVAVYL
     INRLPTPLLQ LESPFQKLFG TSPNYDKLRV FGCACYPWLR PYNQHKLDDK SRQCVFLGYS
     LTQSAYLCLH LQTSRLYISR HVRFDENCFP FSNYLATLSP VQEQRRESSC VWSPHTTLPT
     RTPVLPAPSC SDPHHAATPP SSPSAPFRNS QVSSSNLDSS FSSSFPSSPE PTAPRQNGPQ
     PTTQPTQTQT QTHSSQNTSQ NNPTNESPSQ LAQSLSTPAQ SSSSSPSPTT SASSSSTSPT
     PPSILIHPPP PLAQIVNNNN QAPLNTHSMG TRAKAGIIKP NPKYSLAVSL AAESEPRTAI
     QALKDERWRN AMGSEINAQI GNHTWDLVPP PPSHVTIVGC RWIFTKKYNS DGSLNRYKAR
     LVAKGYNQRP GLDYAETFSP VIKSTSIRIV LGVAVDRSWP IRQLDVNNAF LQGTLTDDVY
     MSQPPGFIDK DRPNYVCKLR KALYGLKQAP RAWYVELRNY LLTIGFVNSV SDTSLFVLQR
     GKSIVYMLVY VDDILITGND PTLLHNTLDN LSQRFSVKDH EELHYFLGIE AKRVPTGLHL
     SQRRYILDLL ARTNMITAKP VTTPMAPSPK LSLYSGTKLT DPTEYRGIVG SLQYLAFTRP
     DISYAVNRLS QFMHMPTEEH LQALKRILRY LAGTPNHGIF LKKGNTLSLH AYSDADWAGD
     KDDYVSTNGY IVYLGHHPIS WSSKKQKGVV RSSTEAEYRS VANTSSEMQW ICSLLTELGI
     RLTRPPVIYC DNVGATYLCA NPVFHSRMKH IAIDYHFIRN QVQSGALRVV HVSTHDQLAD
     TLTKPLSRTA FQNFASKIGV TRVPPS
 
 
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