ID Q53JS3_ORYSJ Unreviewed; 1398 AA.
AC Q53JS3;
DT 24-MAY-2005, integrated into UniProtKB/TrEMBL.
DT 24-MAY-2005, sequence version 1.
DT 27-MAR-2024, entry version 120.
DE SubName: Full=Retrotransposon protein, putative, Ty3-gypsy subclass {ECO:0000313|EMBL:ABA93390.1};
GN OrderedLocusNames=LOC_Os11g26500 {ECO:0000313|EMBL:ABA93390.1};
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947 {ECO:0000313|EMBL:ABA93390.1};
RN [1] {ECO:0000313|EMBL:ABA93390.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16188032; DOI=10.1186/1741-7007-3-20;
RG The rice chromosomes 11 and 12 sequencing consortia;
RT "The sequence of rice chromosomes 11 and 12, rich in disease resistance
RT genes and recent gene duplications.";
RL BMC Biol. 3:20-20(2005).
RN [2] {ECO:0000313|EMBL:ABA93390.1}
RP NUCLEOTIDE SEQUENCE.
RA Buell C.R., Wing R.A., McCombie W.A., Ouyang S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:ABA93390.1}
RP NUCLEOTIDE SEQUENCE.
RA Buell R.;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; DP000010; ABA93390.1; -; Genomic_DNA.
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; cd01647; RT_LTR; 1.
DR Gene3D; 1.10.340.70; -; 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 Gene3D; 4.10.60.10; Zinc finger, CCHC-type; 1.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR001584; Integrase_cat-core.
DR InterPro; IPR041588; Integrase_H2C2.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR InterPro; IPR005162; Retrotrans_gag_dom.
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 InterPro; IPR036875; Znf_CCHC_sf.
DR PANTHER; PTHR45835:SF87; RNA-DIRECTED DNA POLYMERASE; 1.
DR PANTHER; PTHR45835; YALI0A06105P; 1.
DR Pfam; PF17921; Integrase_H2C2; 1.
DR Pfam; PF03732; Retrotrans_gag; 1.
DR Pfam; PF17919; RT_RNaseH_2; 1.
DR Pfam; PF08284; RVP_2; 1.
DR Pfam; PF00078; RVT_1; 1.
DR Pfam; PF00098; zf-CCHC; 1.
DR SMART; SM00343; ZnF_C2HC; 1.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR SUPFAM; SSF54160; Chromo domain-like; 1.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR SUPFAM; SSF57756; Retrovirus zinc finger-like domains; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 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 Zinc {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00047}.
FT DOMAIN 283..298
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT DOMAIN 531..710
FT /note="Reverse transcriptase"
FT /evidence="ECO:0000259|PROSITE:PS50878"
FT DOMAIN 1029..1192
FT /note="Integrase catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50994"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 241..279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..275
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1398 AA; 160133 MW; 9CD9577FC5576768 CRC64;
MVLTRSNGNG PNNNNNNNNN GENPTLAQVL AQQAQLMNMM MQQLQNQQNQ GNNHAPPQNK
LAKFFRVRPP IFSSTINPVE AGDWLHAIEK KLDLLQCTDQ EKVSFASHQL HGPASEWWDH
FRLNRTTAEP ITWLEFTAAF RKTHIPSGVV SLKKREFRSL TQGSRSVTEY LHEFNRLARY
APEDVRTDEE RQEKFLEGLN DELSYPLMIG DYPDFHKLVD KAIRQEDKYN RMEQKKRRIA
QFKTQQGNNQ KPRLTLGPQS MPQGASTQQQ PAKREQGSKP VVCFNCGDPG HYADKCPKPR
RVKVVPTQSN STVPASKARV NHVAAAEAQD APDVILGTFL VNLVPATVLF DSGATHSFLS
MSFAGNHGME VEDLRRPLMV SAPSNQALSL QRSPSVRIEI QGVPFLANLI LLESKDLDVI
LGMDWLARYK GVIDCANRKV TLTSNDGRVV TVHALSSESL RSRLNQITLE EIPIVREYPD
VFPDDLPGMP PKRDIEFRID LVPGTTPIHK RPYRMATNEF AEVKRQVDDL LQKGYIRPSS
SPWGAPVIFV EKKDHTQRMC VDYRALNDVT IKNKYPLPRI DDLFDQLKGA TIFSKIDLRS
GYHQLRIKEE DIPKTAFTTR YGLFECTVMS FGLTNAPTFF MNLMNKVFME YLDKFVVVFI
DDILIYSRTK EEHEEHLRLA LEKLREHQLY AKFSKCEFWL SEVKFLGHVI SAGGVAVDPS
NVESVTNWKQ PKTVSEIRSF LGLAGYYRRF IENFSKIAKP MTRLLQKDVK YKWSEECEQS
FQELKDRLIS APILILPDPK KGFQVYCDAS KLGLGCVLMQ DGKVVAYASR QLRPHEENYP
THDLKLAAVD YDMGIHYHPG KANVVADALS RKGYCNATKG RQLPLELCKE FERFNLGIAS
RGFVAALEAK PILIDQVREA QINDPDILEI KKNMRRGKAI GFLEDEQGTV WLGERICVPD
NKDLKDAILK EAHDTLYSIH LGSTKMYQDL KERFWWASMK REIAEYVAVC DVCQRVKAEH
QKPAGLLQPL KIPEWKWEEI GMDFITGLPR TSSGHDSIWV IVDRLTKVAH FIPVNTTYSG
SRLAELYMAR IVCLHGVPKK IVSDRGSQFT SNFWKKLQEE MGSKLNFSTA YHPQTDGQTE
RVNQILEDML RACALDFGGS WDKNLPCAEF SYNNSYQASL QMAPYEALYG RKCRTPLLWD
QTGERQVFGT DILREAEEKV KFIQERLRVA QSRHKSYADN RRRDLSFEEG DYVYLRVTPL
RGVHRFHTKG KLAPRFVGPY KIVSRRGEVA YQLELPQSLA GVHNVFHVSQ LKKCLRVPIE
EANLEQIEVQ EDLTYVERPI RILEIDERRT RNPVIRFCKV QWSNHSEEES TWEREDELKS
AHPHLFASSS ESRGRDSV
//