ID A0A0E0N6J2_ORYRU Unreviewed; 1618 AA.
AC A0A0E0N6J2;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblPlants:ORUFI01G44580.1};
OS Oryza rufipogon (Brownbeard rice) (Asian wild rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4529 {ECO:0000313|EnsemblPlants:ORUFI01G44580.1, ECO:0000313|Proteomes:UP000008022};
RN [1] {ECO:0000313|Proteomes:UP000008022}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. W1943 {ECO:0000313|Proteomes:UP000008022};
RA Zhao Q.;
RL Submitted (JUN-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:ORUFI01G44580.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (JUN-2015) to UniProtKB.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SUBUNIT: May interact with ARGONAUTE1 or PINHEAD through their common
CC PAZ domains. {ECO:0000256|ARBA:ARBA00011499}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the helicase family. Dicer subfamily.
CC {ECO:0000256|ARBA:ARBA00035116, ECO:0000256|PROSITE-ProRule:PRU00657}.
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DR STRING; 4529.A0A0E0N6J2; -.
DR EnsemblPlants; ORUFI01G44580.1; ORUFI01G44580.1; ORUFI01G44580.
DR Gramene; ORUFI01G44580.1; ORUFI01G44580.1; ORUFI01G44580.
DR eggNOG; KOG0701; Eukaryota.
DR HOGENOM; CLU_000907_4_4_1; -.
DR OMA; TRKNHAY; -.
DR Proteomes; UP000008022; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0004525; F:ribonuclease III activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0031047; P:regulatory ncRNA-mediated gene silencing; IEA:UniProtKB-KW.
DR GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR CDD; cd18034; DEXHc_dicer; 1.
DR CDD; cd02844; PAZ_CAF_like; 1.
DR CDD; cd00593; RIBOc; 2.
DR CDD; cd18802; SF2_C_dicer; 1.
DR Gene3D; 3.30.160.20; -; 1.
DR Gene3D; 3.30.160.380; Dicer dimerisation domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 2.170.260.10; paz domain; 1.
DR Gene3D; 1.10.1520.10; Ribonuclease III domain; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR038248; Dicer_dimer_sf.
DR InterPro; IPR005034; Dicer_dimerisation_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR003100; PAZ_dom.
DR InterPro; IPR036085; PAZ_dom_sf.
DR InterPro; IPR000999; RNase_III_dom.
DR InterPro; IPR036389; RNase_III_sf.
DR PANTHER; PTHR14950; DICER-RELATED; 1.
DR PANTHER; PTHR14950:SF46; ENDORIBONUCLEASE DICER HOMOLOG 3; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF03368; Dicer_dimer; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF02170; PAZ; 1.
DR Pfam; PF00636; Ribonuclease_3; 2.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00949; PAZ; 1.
DR SMART; SM00535; RIBOc; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF101690; PAZ domain; 1.
DR SUPFAM; SSF69065; RNase III domain-like; 2.
DR PROSITE; PS51327; DICER_DSRBF; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS50821; PAZ; 1.
DR PROSITE; PS00517; RNASE_3_1; 1.
DR PROSITE; PS50142; RNASE_3_2; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Endonuclease {ECO:0000256|ARBA:ARBA00022759};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000008022};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00657};
KW RNA-mediated gene silencing {ECO:0000256|ARBA:ARBA00023158}.
FT DOMAIN 39..159
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 372..533
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 557..647
FT /note="Dicer dsRNA-binding fold"
FT /evidence="ECO:0000259|PROSITE:PS51327"
FT DOMAIN 863..949
FT /note="PAZ"
FT /evidence="ECO:0000259|PROSITE:PS50821"
FT DOMAIN 1001..1170
FT /note="RNase III"
FT /evidence="ECO:0000259|PROSITE:PS50142"
FT DOMAIN 1211..1359
FT /note="RNase III"
FT /evidence="ECO:0000259|PROSITE:PS50142"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..25
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1618 AA; 181067 MW; 4E0B50C8217A71DF CRC64;
MNPLKRSLES SSQEHEAGKQ KLQKRECQDF TPRRYQLDVY EVAMRRNTIA MLDTGAGKTM
IAVMLIKEFG KINRTKNAGK VIIFLAPTVQ LVTQQCEVIE IHTDFEVEQY YGAKGVMVMT
PQVFLQALRN AFLILDMVSL MIFDECHHAT GNHPYTRIMK EFYHKSEHKP SISSHLDCEG
QFCELENLLD AKIYTVSDRE EIEFCVPSAK EMCRYYDSKP VCFEDLSEEL GVLCSKYDAL
ITELQNKRSD MYKDADDITK ESKRRLSKSI AKICYCLDDV GLICASEATK ICIERGQEKG
WLKEVVDATD QQTDANGSRL FAENSALHMK FFEEALHLID KRLQQGIDML LNSESGCVEA
AKTGYISPKL YELIQIFHSF SNSRHARCLI FVDRKITARV IDRMIKKIGH LAHFTVSFLT
GGRSSVDALT PKMQKDTLDS FRSGKVNLLF TTDVAEEGIH VPECSCVIRF DLPRTTRSYV
QSRGRARQED SQYILMIERG NVKQNDLISA IVRSETSMVK IASSRESGNL SPGFVPNEEI
NEYHVGTTGA KVTADSSISI VYRYCEKLPQ DKCYSPKPTF EFTHHDDGYV CTLALPPSAV
LQILVGPKAR NMHKAKQLVC LDACKKLHEL GALDDHLCLS VEDPVPEIVS KNKGTGIGTT
KRKELHGTTR IHAWSGNWVS KKTALKLQSY KMNFVCDQAG QIYSEFVLLI DATLPDEVAT
LEIDLYLHDK MVKTSVSSCG LLELDAQQME QAKLFQGLLF NGLFGKLFTR SKVPNAPREF
ILNKEDTFVW NTASVYLLLP TNPSFDSNVC INWSVIDAAA TAVKLMRRIY SENKRELLGI
FDSDQNVGDL IHLANKSCKA NSLKDMVVLA VHTGKIYTAL DITELSGDSA FDGASDKKEC
KFRTFAEYFK KKYGIVLRHP SQPLLVLKPS HNPHNLLSSK FRDEGNVVEN MSNGTPVVNK
TSNRVHMPPE LLIPLDLPVE ILRSFYLFPA LMYRIESLTL ASQLRSEIGY SDSNISSFLI
LEAITTLRCS EDFSMECLEL LGDSVLKYAV SCHLFLKFPN KDEGQLSSIR CHMICNATLY
KLGIERNVQG YVRDAAFDPR RWLAPGQLSI RPSPCECPVK SEVVTDDIHI IDDKAIVLGK
ACDKGHRWMC SKTIADCVEA IIGAYYAGGG LRAAMAVLKW LGIGAEIEED LIVQAILSAS
VQTYLPKDNV FEMLEAKLGY SFSVKGLLVE ALTHPSQQEL GAKYCYERLE FLGDAVLDIL
LTRYLFNSHK DTNEGELTDL RSASVNNENF AQVAVKHNFH HFLQHSSGLL LDQITEYVNR
LEGSSMDKVE LLSDGLPKGP KVLGDIVESI AGAILLDTKL DLDVVWGIFE PLLSPIVTPE
NLELPPYREL IEWCGKHGYF VGINCRDQGD TVVATLDVQL KEVLLVRQGF SKKRKDAKAH
ASSLLLKDLE EKGLIIPKNA SKTEQFEKHC GSTNPFNNLH VDAMDTQTPK PTKEKNAADS
RNISDPLLVH VIVKTSKGGP RIALYELCKK LQWPMPTMES EKVQPSFSSV CSSPGGSSQK
ATPQAFAFAS TITLHIPNAD VISLTGDGRA DKKSSQDSAA LFLLYELQRR GTLQLQEV
//
