ID A0A087GH17_ARAAL Unreviewed; 1214 AA.
AC A0A087GH17;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Reverse transcriptase {ECO:0008006|Google:ProtNLM};
GN OrderedLocusNames=AALP_Aa7g098300 {ECO:0000313|EMBL:KFK29169.1};
OS Arabis alpina (Alpine rock-cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Arabideae; Arabis.
OX NCBI_TaxID=50452 {ECO:0000313|EMBL:KFK29169.1, ECO:0000313|Proteomes:UP000029120};
RN [1] {ECO:0000313|Proteomes:UP000029120}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Pajares {ECO:0000313|Proteomes:UP000029120};
RX PubMed=27246759; DOI=10.1038/nplants.2014.23;
RA Willing E.M., Rawat V., Mandakova T., Maumus F., James G.V.,
RA Nordstroem K.J., Becker C., Warthmann N., Chica C., Szarzynska B.,
RA Zytnicki M., Albani M.C., Kiefer C., Bergonzi S., Castaings L.,
RA Mateos J.L., Berns M.C., Bujdoso N., Piofczyk T., de Lorenzo L.,
RA Barrero-Sicilia C., Mateos I., Piednoel M., Hagmann J., Chen-Min-Tao R.,
RA Iglesias-Fernandez R., Schuster S.C., Alonso-Blanco C., Roudier F.,
RA Carbonero P., Paz-Ares J., Davis S.J., Pecinka A., Quesneville H.,
RA Colot V., Lysak M.A., Weigel D., Coupland G., Schneeberger K.;
RT "Genome expansion of Arabis alpina linked with retrotransposition and
RT reduced symmetric DNA methylation.";
RL Nat. Plants 1:14023-14023(2015).
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DR EMBL; CM002875; KFK29169.1; -; Genomic_DNA.
DR EnsemblPlants; KFK29169; KFK29169; AALP_AA7G098300.
DR Gramene; KFK29169; KFK29169; AALP_AA7G098300.
DR eggNOG; KOG0017; Eukaryota.
DR OMA; CENSGET; -.
DR OrthoDB; 541502at2759; -.
DR Proteomes; UP000029120; Chromosome 7.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0015074; P:DNA integration; IEA:InterPro.
DR CDD; cd00303; retropepsin_like; 1.
DR CDD; cd09274; RNase_HI_RT_Ty3; 1.
DR CDD; cd01647; RT_LTR; 1.
DR Gene3D; 2.40.50.40; -; 1.
DR Gene3D; 3.30.70.270; -; 2.
DR Gene3D; 2.40.70.10; Acid Proteases; 1.
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; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR023780; Chromo_domain.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR001584; Integrase_cat-core.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR000477; RT_dom.
DR InterPro; IPR041577; RT_RNaseH_2.
DR InterPro; IPR001878; Znf_CCHC.
DR PANTHER; PTHR24559:SF438; RT_RNASEH_2 DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR24559; TRANSPOSON TY3-I GAG-POL POLYPROTEIN; 1.
DR Pfam; PF00385; Chromo; 1.
DR Pfam; PF17919; RT_RNaseH_2; 1.
DR Pfam; PF08284; RVP_2; 1.
DR Pfam; PF00078; RVT_1; 1.
DR SMART; SM00298; CHROMO; 1.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR SUPFAM; SSF54160; Chromo domain-like; 1.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR PROSITE; PS50013; CHROMO_2; 1.
DR PROSITE; PS50994; INTEGRASE; 1.
DR PROSITE; PS50878; RT_POL; 1.
DR PROSITE; PS50158; ZF_CCHC; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Reference proteome {ECO:0000313|Proteomes:UP000029120};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00047}.
FT DOMAIN 100..115
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT DOMAIN 391..570
FT /note="Reverse transcriptase"
FT /evidence="ECO:0000259|PROSITE:PS50878"
FT DOMAIN 853..965
FT /note="Integrase catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50994"
FT DOMAIN 1109..1143
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT REGION 20..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1190..1214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..77
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1214 AA; 136815 MW; EE7BD586F5F1A99F CRC64;
MMNTTKKVAG WTGVVAQAPR YQSGEASRGG RVGSNKPSGP LTKPLTGLAA TKPTTTFGNN
KGGNTQRFDN RNPNQSGRVK PPFRKLTAAE VEWRKANGLC FRCDEKGHSR SQCTQKEFSV
LIVQDDESET EWVEEEEENE EVNRRVTKVA ELSLNSMVGI SSPRTVKLRG TIRGESIVVM
IDSGASHNFI SEKVVTRLGL TATDTTGYGV LTGGGITVQG RGVCKDVELC LQDLVIVAPF
LPLELGSADA ILGIQWLASL GDMKCNWKLQ KLAFMVGEKE VELRGDPSLC CSPISMKGLW
KALDREGQGV IIEFGGLQTE GQRRERAAPG VLQGVIYEFA SVFEEPQGLP PCRDKEHAIV
LETGASLVSV RPFRYPQVQR EELEKQVATM LAAGIIKEST SPFSSPVLLV KKKDGTWRFC
VDYRALNKVT VGDSYPIPMI DQLLDELHGA IMFSKLDMRA GYHQIRVKAE DVPKTAFRTH
DGHYEFLVMP FGLTNAPTTF QSLMDDVFRQ FLRRFVLVFF DDILIYSKTE AEHQAHVRIV
LQTLADHQLY ANAKKCEFGK SEVEYLGHVI SGRGVAADPT KVKAMVDWPP PKNVKALRGF
LGLTGYYRKF VKGYGGIARP LTALLKKDQF KWSPTAEATF QALKAAMSTV PVLALVDFSK
QFVVESDASG IGLGXXXXXX XXXXXXAYFS QALTDRHKLK SVYERELMAV VFAIQKWRHY
LLGRRFVVRT DQRSLKFLLE QREINLEYQR WLSKILGFDF EIQYKPGLEN KAADALSRVE
THQLLALSMP VAIQMSEFES EVDQDEDLSK LKKAVLANPG DHPDYSIVQG RLLRKGRLTK
YAHFIKMSHP YEAAEVALTF VKEVVRLHGY PRTIVLDRDI TFTGKFWGEL FRLAGTHLCF
STAYHPQSDG QTEVTNRGME TYLRCFCSEK PKKWSGYLVW AELSYNTSYH TAIRMTPFKA
VYGREPPTLL QFERGSTDNA TLEDQLLERD EMLGIQQQQL LRTQQIMKQQ ADNHRREVEF
AVGDMVFLKI RPYRQKTLAR RANEKLAARY YGPYEVEAKV GPVAYKLRLP PTVKIHHTFH
VSQLKAAVGS ALVPVTIPPN LNEEGMLEAE PKFVLGDRVN RETGQEEVLI QWKGLPEEDC
TWEWKSVIKA QFPHFNLEDR VNQKGAGNVR VRETLPLLYQ YRRRSGRKAL KPKGLEKQLE
EGAATSEQXX XXXE
//
