ID A7ERU2_SCLS1 Unreviewed; 1660 AA.
AC A7ERU2;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=Reverse transcriptase {ECO:0008006|Google:ProtNLM};
GN ORFNames=SS1G_08046 {ECO:0000313|EMBL:EDN92184.1};
OS Sclerotinia sclerotiorum (strain ATCC 18683 / 1980 / Ss-1) (White mold)
OS (Whetzelinia sclerotiorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Sclerotinia.
OX NCBI_TaxID=665079 {ECO:0000313|EMBL:EDN92184.1, ECO:0000313|Proteomes:UP000001312};
RN [1] {ECO:0000313|Proteomes:UP000001312}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18683 / 1980 / Ss-1 {ECO:0000313|Proteomes:UP000001312};
RX PubMed=21876677; DOI=.1371/journal.pgen.1002230;
RA Amselem J., Cuomo C.A., van Kan J.A., Viaud M., Benito E.P., Couloux A.,
RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.M.,
RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA Grossetete S., Guldener U., Henrissat B., Howlett B.J., Kodira C.,
RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA Zeng Q., Rollins J.A., Lebrun M.H., Dickman M.;
RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT sclerotiorum and Botrytis cinerea.";
RL PLoS Genet. 7:E1002230-E1002230(2011).
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DR EMBL; CH476630; EDN92184.1; -; Genomic_DNA.
DR RefSeq; XP_001591420.1; XM_001591370.1.
DR GeneID; 5487597; -.
DR KEGG; ssl:SS1G_08046; -.
DR InParanoid; A7ERU2; -.
DR OMA; FFQTHNL; -.
DR OrthoDB; 1804362at2759; -.
DR Proteomes; UP000001312; Unassembled WGS sequence.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IEA:InterPro.
DR CDD; cd09276; Rnase_HI_RT_non_LTR; 1.
DR CDD; cd01650; RT_nLTR_like; 1.
DR Gene3D; 3.60.10.10; Endonuclease/exonuclease/phosphatase; 1.
DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR InterPro; IPR005135; Endo/exonuclease/phosphatase.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR002156; RNaseH_domain.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR000477; RT_dom.
DR PANTHER; PTHR33481; REVERSE TRANSCRIPTASE; 1.
DR PANTHER; PTHR33481:SF1; REVERSE TRANSCRIPTASE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF14529; Exo_endo_phos_2; 1.
DR Pfam; PF00075; RNase_H; 1.
DR Pfam; PF00078; RVT_1; 1.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR SUPFAM; SSF56219; DNase I-like; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR PROSITE; PS50879; RNASE_H_1; 1.
DR PROSITE; PS50878; RT_POL; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000001312}.
FT DOMAIN 860..1130
FT /note="Reverse transcriptase"
FT /evidence="ECO:0000259|PROSITE:PS50878"
FT DOMAIN 1342..1481
FT /note="RNase H type-1"
FT /evidence="ECO:0000259|PROSITE:PS50879"
FT REGION 19..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1639..1660
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..86
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1645..1660
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1660 AA; 187185 MW; 4147564EC9766863 CRC64;
MAGTMHAHMK FAEHAPTGSD ATYARKSPPF ILSSPTPSQP FNFQTQCNTL SSDDPFKSPI
NRPTFQLNNK RRRQPSHSEP HINSPKEAIQ KARSLLILAA SLEEDTEEQS KVLDLVEIFR
EYLEKGKLTK ASNIITSQIS HLENATKRIE KQANHLSNLP NHIIPPTINA PGIKASYATI
TKTSGEWNLV TKGKPTKQKT TEQKEEAPSK RLILIKPLIY QPHSFTPLNT RNKVNEAFKK
AGINGPIISA ITTTRSGNFI LTTNSPFNAQ FLMEKKEIWD KILDAARIQI DKPWHKVIIH
KIPIQEFSGL KGMDLIKEEV NTFNPGLSIM GTPYWLTNAS KRAKQQDGAI VIAFATQKEA
DIAIQKRLYI AGISVRVERF YHLLLHPNAQ MPGIRAITNH TAKNLQLADF ALLLKLLGDN
PSNLRPRTMI YISKGFKPLV ALAPNSPNDP DIQIIDITQG KHTIQLINIY NEADQAKEKG
HTIERCLYNT PLTHHTILVG DFNSHHPWWD PFSNKSSNAD LLTEWFEDHN LILFNEPGTS
TFYRTNMTNP SVLDLTLATD SVSPYITDWQ VLPDLGSDHL SILFEVKGTL SRTTNIAQPA
RFNTKLADWE KFANTLKSKI SISTTLNSSE YLNIATSESN SLDSLLDKSQ YIQVLDEAAK
EFTRIITYSA ETSIPRIKST KRAKPWWSPE LKALRKRLSN AFENAKIYPE DDMFKKIYRS
ARNHYFQAIK TAKKNHWNEF LEKEDTQSIF KAMSYTKDIQ TERIPNIRSN PSKLENSFEG
KCSAFRSTLF PPPPCTPPPN WESYKQSKKW EWPDLTESEL LNACSAKIKG KTPGPDGITQ
DIIIQAYKAI PKAFSTLFSH LINLGYHPSC WKQATGAILK KPSKPDYSAP KAYRVIALLN
CLGKISERIL AQRLSYLAET TQLLHYSQMG GRQKKSAIDT AILLTTEIER NSRSKKKTST
LFLDVKGAFD HVSMNKLLDI CKNLNLPTSL IAWISSFLKE RLLKLSFDGQ IETFKPINTG
IPQGSPISPI LFLIYIRDLF SANSIKYLSY IDDIALTTFS TSWKKNIISL ERATKQIYAL
GKENAIQFDL AKTELIHFST SKDTKTASIK LPNEEIIQPS TLVRLLGIWF DPGLSFKQHV
TIRATQAKTS FYRMARLANS EKGFSPKAMR QLYMACVTSI ADYGSILWWK GQNQFKKILQ
SLQNLALRKI LGVFKTSPIK PIEIEAALCP PEVRLNAGIK QYAFRLLKIS PSHPVNLIAT
KLATEKENQD VVATPQRKQL KPTQLEKIKN SIQKDFDPLT LERIHHFYFP PWKKEVPYRV
NISKLGKEEA AMIHNLAFKY RCKNTITIYT DASSTLEGIG VGIGIVVILP NGRNSYQETI
NIGVNQLVYN GELLGVTKAI EYANSIAQPG NKFKIYSDNQ AGLFRLKTPS DSPGQSCQIK
AIKAAEAIQN KGAEISLNWV PGHTSVQGNE LADSLAKEAT KIPSSSHETS YASIGMDIKR
MKSENWIAIL NTNNFHQPSS TYSRNYPWKI SSKIRIPGNI KRSTICALFQ LKIGHGYFKS
YLKRFGISSN DNCRCGGKES PDHLLLSCPL YKMARKTLNK DNPIVRPTMK YLLHTKAGII
KTLEFIEATR IATRSWHLNR MHEEEEEEGG EEGGGPEDCD
//
