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Database: UniProt
Entry: E5KEH9_9PLEO
LinkDB: E5KEH9_9PLEO
Original site: E5KEH9_9PLEO 
ID   E5KEH9_9PLEO            Unreviewed;      1716 AA.
AC   E5KEH9;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   22-FEB-2023, entry version 30.
DE   SubName: Full=Polyprotein {ECO:0000313|EMBL:ADO33889.1};
OS   Pyrenophora tritici-repentis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC   Pyrenophora.
OX   NCBI_TaxID=45151 {ECO:0000313|EMBL:ADO33889.1};
RN   [1] {ECO:0000313|EMBL:ADO33889.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Maumus F.;
RT   "Pyreno elements define a new clade of Ty1/copia-like elements from
RT   ascomycetes.";
RL   Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AGW27431.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Maumus F.;
RT   "Phylogenetic clustering and taxonomic distribution suggests ancient
RT   horizontal transfer or deep eukaryotic ancestry of the RAS lineage of
RT   Ty1/Copia-like elements.";
RL   Submitted (JUL-2013) 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;
CC         Evidence={ECO:0000256|ARBA:ARBA00024557};
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=2.7.7.7;
CC         Evidence={ECO:0000256|ARBA:ARBA00024632};
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DR   EMBL; HQ113945; ADO33889.1; -; Genomic_DNA.
DR   EMBL; KF418198; AGW27431.1; -; Genomic_DNA.
DR   GO; GO:0005634; C:nucleus; IEA:UniProt.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003964; F:RNA-directed DNA polymerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0015074; P:DNA integration; IEA:InterPro.
DR   GO; GO:0032196; P:transposition; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR   InterPro; IPR001584; Integrase_cat-core.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   InterPro; IPR013103; RVT_2.
DR   Pfam; PF07727; RVT_2; 1.
DR   SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR   PROSITE; PS50994; INTEGRASE; 1.
PE   4: Predicted;
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW   Transposable element {ECO:0000256|ARBA:ARBA00022464};
KW   Transposition {ECO:0000256|ARBA:ARBA00022578}.
FT   DOMAIN          845..1013
FT                   /note="Integrase catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50994"
FT   REGION          154..258
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          522..542
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1123..1177
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        157..184
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        185..222
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        223..258
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1716 AA;  194190 MW;  32D6992961693860 CRC64;
     MASSSRRVVP TLEALLGTTN IKPREWHHID PEIWEDNVEA PDDEVGITTA TTYIARAIAD
     YTDRPTADEE LFWEFRQDFE GWTEAMFLRA QPIYTKELKR ILRFKGVYTG RINMAPSESL
     ARLLRMEEYL EWPQDVFQSA VFDTRSAAHM LQERALRQQR SEGSVQSTDR RLSSQAQSRT
     QTPVRTRGRD VDSRQTRDQD QTHARVQGRQ ETVEEEQQIQ DQLAKTIEKA QNQPIRSQPV
     ETTESAPQPA YQRVQSQQPP LTYNNFDRFR EYTPAYPQRP KGLSVPPIVP SGETDPYKAV
     PPIEFGNEKL DPKTINVFVK MWDRDKKYTG KPYDLLDDKL KIFYSICYHA DIEPGQFHAV
     FPRILDGRAE EYYLHFVDQR MDTFLTAYTK LKNHFDTDVN HGHYYADWTT TSFVKVRREN
     PEKNLHEVLD IMLDKLQLCQ RALGQQYMGE YALRTTVITA CRGVKELEMA LYKPSLECEV
     LFGDLRSSIE NSLAMTVSVN FTEADTDSQY YLDRRYNNNS SGRLRGNYNP RGGRSGFTRG
     RGGLQHRSGV NTQIDKKCYV CGKTGCWSTN HTLEERKRSK AQYITHCAIT GEQMEFSTFL
     VAYEGEEVDQ FFLEEQDEDD EDQRLAVKYL TDQAFLHHVT GEDVYRCKEP ITPATQFLIE
     DRYSRITYQG ILPDTGASNV STAGKEQFWA LQTEDPTVTL DTSTAGNASV QFGKGSVTTS
     IGTAHVSTQI GKIKFEVLNA PTPFLLCLKD MDRLHVYFNN TTDQLVQGKA TFPVIRKWGH
     PWFHLSKAER ARVFLTETEL RRLHRRFGHP AVERLIRLLK RAGHEDVDER LLREIQTFCH
     HCQAHDPAPR RFKFRLKDDR EFNFEILVDV MYLSGKPVLH VIDSATTFNG ARFLPSMSAK
     DTWEALRLLW IDTYQGPPDI VTHDAGTNFA SVEFRSEAKI MGITCKQVPT EAHWSIGKVE
     RYHAPLRRAY EILRTELDTG TSDAAVLQMA VKAVNDTAGP DGLVPTLLVF GAYPRISMDS
     PPSPSITHRA EAIQKAMRAL RKASAEHAVS NALGTRNGPT TDGVLSLPLQ SEVMVWREKN
     GWQGPYRVID MKDHDVTVDM INGPTTFRST VVKPYYRDLT TAIDGADQGT GGSPTTDEAI
     ADEPPLPVPP AEANQAAQPR KRGRPPGSKN KPKVQYLSKK EEDDYALAVK LRNDGVINVP
     GAPFEASDQK EIDDLVGRGV FSFELFDPTL HGGYRIFKSR MVREVKGKTM VPYEKSRLVV
     QGYNDEGKHE ILTQSPTIQR ASQRLILALA PALLDEGMVV ELRDITQAYP QAQTELFRTV
     LAHLPKELIT KYPKGTIIRV IKPLYGIAEA GVHWFATYQG HHCKELDMAT STYDPCLLIT
     NGRREAFGIV GLQTDDTLAI GTPAFSGAED AALQKANFRA KPKERLSKEV SLEFNGCTLT
     LRGDTILLTQ KGQGAKIEII DPKAANRAQK YMEQRARGAY IASICQPEAS FDLSAAAQIQ
     QPKDTEYVKL NRRLQWQSES IQRGLRYVPL DLATAKLVVF TDGSFANNQD LSSQLGYLLI
     LANESSRQDS TFDIRGNVIH WSSTKCKRVT RSVLASETYG MVSGVDIAIA ILTTLKIITG
     RLGLPPIPLI VCTDSYSLYE CLVKLGTTAE KRLMIDIMAL RQSYERREIT EIRWINGEDN
     PADAFTKATP NRALERFIES NKLSIRVEGS VQRPTE
//
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