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Database: UniProt
Entry: A0A2I0ADV9_9ASPA
LinkDB: A0A2I0ADV9_9ASPA
Original site: A0A2I0ADV9_9ASPA 
ID   A0A2I0ADV9_9ASPA        Unreviewed;      1297 AA.
AC   A0A2I0ADV9;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=RNA-directed DNA polymerase like {ECO:0000313|EMBL:PKA53732.1};
GN   ORFNames=AXF42_Ash021027 {ECO:0000313|EMBL:PKA53732.1};
OS   Apostasia shenzhenica.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Orchidaceae;
OC   Apostasioideae; Apostasia.
OX   NCBI_TaxID=1088818 {ECO:0000313|EMBL:PKA53732.1, ECO:0000313|Proteomes:UP000236161};
RN   [1] {ECO:0000313|EMBL:PKA53732.1, ECO:0000313|Proteomes:UP000236161}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Shenzhen {ECO:0000313|Proteomes:UP000236161};
RC   TISSUE=Stem {ECO:0000313|EMBL:PKA53732.1};
RX   PubMed=28902843; DOI=10.1038/nature23897;
RA   Zhang G.Q., Liu K.W., Li Z., Lohaus R., Hsiao Y.Y., Niu S.C., Wang J.Y.,
RA   Lin Y.C., Xu Q., Chen L.J., Yoshida K., Fujiwara S., Wang Z.W., Zhang Y.Q.,
RA   Mitsuda N., Wang M., Liu G.H., Pecoraro L., Huang H.X., Xiao X.J., Lin M.,
RA   Wu X.Y., Wu W.L., Chen Y.Y., Chang S.B., Sakamoto S., Ohme-Takagi M.,
RA   Yagi M., Zeng S.J., Shen C.Y., Yeh C.M., Luo Y.B., Tsai W.C.,
RA   Van de Peer Y., Liu Z.J.;
RT   "The Apostasia genome and the evolution of orchids.";
RL   Nature 549:379-383(2017).
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DR   EMBL; KZ451991; PKA53732.1; -; Genomic_DNA.
DR   OrthoDB; 953332at2759; -.
DR   Proteomes; UP000236161; Unassembled WGS sequence.
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-KW.
DR   GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IEA:InterPro.
DR   CDD; cd09279; RNase_HI_like; 1.
DR   CDD; cd01647; RT_LTR; 1.
DR   Gene3D; 3.30.70.270; -; 2.
DR   Gene3D; 3.10.10.10; HIV Type 1 Reverse Transcriptase, subunit A, domain 1; 1.
DR   Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR005162; Retrotrans_gag_dom.
DR   InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR002156; RNaseH_domain.
DR   InterPro; IPR036397; RNaseH_sf.
DR   InterPro; IPR000477; RT_dom.
DR   InterPro; IPR041577; RT_RNaseH_2.
DR   PANTHER; PTHR24559:SF437; RIBONUCLEASE H; 1.
DR   PANTHER; PTHR24559; TRANSPOSON TY3-I GAG-POL POLYPROTEIN; 1.
DR   Pfam; PF03732; Retrotrans_gag; 1.
DR   Pfam; PF17919; RT_RNaseH_2; 1.
DR   Pfam; PF00078; RVT_1; 1.
DR   Pfam; PF13456; RVT_3; 1.
DR   SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR   SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR   PROSITE; PS50879; RNASE_H_1; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotidyltransferase {ECO:0000313|EMBL:PKA53732.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000236161};
KW   RNA-directed DNA polymerase {ECO:0000313|EMBL:PKA53732.1};
KW   Transferase {ECO:0000313|EMBL:PKA53732.1}.
FT   DOMAIN          1144..1273
FT                   /note="RNase H type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS50879"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          67..103
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          289..340
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          422..446
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        67..81
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        295..312
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        313..337
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1297 AA;  146128 MW;  673437445947E856 CRC64;
     MEHARDENAP PPPGEQQATR LPQDDATRDD RQLQTLTNTV ATLTRTMNTF LANLPALLQQ
     PRHLPLALPL EAPPPQPGTE HVELPPEETS THAAAESRPE VYSPAPPADT IFSPAIMAAP
     APRAYKTPRV SDYNGLTDPA QHVKRFENTL ATSDPVSDAY KCRFFRNTLT GLALDWLDEI
     PHGSVQNFQQ FSEQFRTRFG TSKTTSRTIH ELWQIRQASD ESLHNYVDRF SKMNAETKDT
     TDDRSTMIFV HSILPGELYD SFVDNMPKTL MEARARAEKR IHLEDAKALK AKARQEATSP
     QTKQGETPKT DSNTPRRSFR DRNYSPTQGK RKFGDESPRP ATPVYIVEEI FSILSDKCFI
     KNRGERQPPQ PGEDPTKFCK FHQRYGYLLF ECRSSRALVN EYIENDYLTG YRKIEGPLPK
     AARPLFPSDA PKGAPSSTPT TPKSDGKKVV LSIFGYHSSL RTQRHQEVCT VKLPPLLPDI
     TFTAGDLPRG GINRDDPIVV IAEIGACDVH RTLVDTGNLV DILYLCAFNE MAVGPYKPLP
     PSMTISSFSG DIYRPAGYTT LRVALEEGPR RMEKEIDFII MDAPSGYNAI LGRPAITAFQ
     MVASTYHLCV KFLTPFGVAT IRGARAGASK CFEINARLHT DYMDPRDHAL PPVEQNDRVT
     VADGKTVLIS KNFPDNEKPA LTGLLFEYFD VFAWEPCDMP GIDRAVAEHR LSLKPGVAPV
     RQKKRTFGGE KQCAIREEVK KLLAAGFIRE ITYPSWLANV VVVKKNSGKW RMCVDFTDLN
     KACPKDFYPL PKIDRLVDSS AGYSVMSFVD AFSGYHQIRM AEDDEEHTSF ITDQGTFCYK
     VMPFGLKNAG ATYQCMIDTV FKNQRGRNIE AYVDDVLIKS VCAKQHLEDL RETLDTCRTY
     NKLNPMKSIF GSSYGKFLGH MVSARGIEAN PEKIQAIQDM KPPQTIQDIQ KLNGRVTALS
     RFISKSGERC LPFFKILRGE RQAWNEDCTK AFQSLKEYLL SPSLLSTPVQ DEDLFLYLST
     TDNSVSAVIV REEAARQHPI HYISHILHGA EVRYPPLKKL SFALISAARR LRHYFQAHPI
     KVMTDQPLRR ILHSPEISGR LQKWVVELSE FDIDFLPRTA TKSQALADFI AELTTTEQPE
     PRKRPQPWTL HVDGASGERI HGVGIVLTSP WGIRLQRSGK IHFPVTNNQA EYEALIVGLK
     FAKGLGARQL DVYSDSKLMV NQLTGSYQTK DEVLKRYFQL TKTLLQQFAQ TSLFHIPREM
     NSLADELAKE ENDNALDILF PAFEDPQIFD IESNPES
//
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