ID A0A371HLA4_MUCPR Unreviewed; 2134 AA.
AC A0A371HLA4;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Endoribonuclease Dicer-like 1 {ECO:0000313|EMBL:RDY03585.1};
DE Flags: Fragment;
GN Name=DCL1 {ECO:0000313|EMBL:RDY03585.1};
GN ORFNames=CR513_12811 {ECO:0000313|EMBL:RDY03585.1};
OS Mucuna pruriens (Velvet bean) (Dolichos pruriens).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Mucuna.
OX NCBI_TaxID=157652 {ECO:0000313|EMBL:RDY03585.1, ECO:0000313|Proteomes:UP000257109};
RN [1] {ECO:0000313|EMBL:RDY03585.1, ECO:0000313|Proteomes:UP000257109}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Jos {ECO:0000313|Proteomes:UP000257109};
RC TISSUE=Seed {ECO:0000313|EMBL:RDY03585.1};
RA Nnadi N.E., Vos R., Hasami M.H., Devisetty U.K., Aguiy J.C.;
RT "Draft genome of Mucuna pruriens seed.";
RL Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the helicase family. Dicer subfamily.
CC {ECO:0000256|ARBA:ARBA00035116}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RDY03585.1}.
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DR EMBL; QJKJ01002264; RDY03585.1; -; Genomic_DNA.
DR STRING; 157652.A0A371HLA4; -.
DR Proteomes; UP000257109; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; 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; cd19869; DSRM_DCL_plant; 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; -; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
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; IPR014720; dsRBD_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:SF37; ENDORIBONUCLEASE DICER; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF14709; DND1_DSRM; 1.
DR Pfam; PF00035; dsrm; 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; SM00358; DSRM; 2.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00949; PAZ; 1.
DR SMART; SM00535; RIBOc; 2.
DR SUPFAM; SSF54768; dsRNA-binding domain-like; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF101690; PAZ domain; 1.
DR SUPFAM; SSF69065; RNase III domain-like; 2.
DR PROSITE; PS50137; DS_RBD; 2.
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 Hydrolase {ECO:0000256|ARBA:ARBA00022722};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU00266};
KW RNA-mediated gene silencing {ECO:0000256|ARBA:ARBA00023158}.
FT DOMAIN 296..620
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 846..1017
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 1354..1494
FT /note="PAZ"
FT /evidence="ECO:0000259|PROSITE:PS50821"
FT DOMAIN 1537..1697
FT /note="RNase III"
FT /evidence="ECO:0000259|PROSITE:PS50142"
FT DOMAIN 1738..1886
FT /note="RNase III"
FT /evidence="ECO:0000259|PROSITE:PS50142"
FT DOMAIN 1912..1975
FT /note="DRBM"
FT /evidence="ECO:0000259|PROSITE:PS50137"
FT DOMAIN 1998..2073
FT /note="DRBM"
FT /evidence="ECO:0000259|PROSITE:PS50137"
FT REGION 94..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 257..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 784..820
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1097..1124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1976..1997
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..131
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..153
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 797..814
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1100..1124
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1976..1991
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:RDY03585.1"
SQ SEQUENCE 2134 AA; 240360 MW; 998E1E33826F47A5 CRC64;
MEDGSRVPAG EDPSYWLDAC EDISCDFIDF DVSSIVSDQP DNASNQDFFG GIDKILDSIK
NGAGLPLHAE PNSNSNVTAG GEVWLPNDAS NATLEDGENC PPAPAADAFD HSGGARNNGS
SKLSNGSEGG VLVNHSHERV SLTRNEGHDI DGEERCSKRA RLGGYKNERP FYGRGNYQGK
ERERCFNNRK RLRDRDEVDR RDKDGARRRE HYGACGRRDV RDRDWRDRES RGYWERDKSG
SHDMVFRVGA WEPDRNREDK MISDAKQENN GKLDKKSEEA KERVPEEKAR QYQLDVLEQA
KKKNTIAFLE TGAGKTLIAV LLIKSIQESL QKQNNKMLAV FLVPKVPLVY QQAEVIRERT
GYQVGHYCGE MGQDFWDARR WQREFDTKHT SEGLVVFLKF KAFRLITSQC RRQEPPTSQL
PLEPSDSLPS LTCRPSPQLL FTKYAFTSTL SFVSIPKAVQ ELFPIQDVYV DDIVIIVNDH
TGIQHLKEHL FHHFETNDLE WARSPCDRRS TSGYLYTLGE ISFHGKARNK MWLQDQVLVM
TAQILLNILR HSIIKMEAIN LLILDECHHA VKKHPYSLVM SEFYHTTPKE KRPSVFGMTA
SPVNLKGVSS QVDCAIKIRN LESKLDSIVC TIKDRKELEK HVPMPSEIVV EYDKAASLCY
LHEQIKQMEV EVEEAAKSSS RRSKWQFMGA RDAGAKEELR QVYGVSERTE SDGAANLIQK
LRAVNYALGE LGQWCAYKVA QSFLAALQND ERANYQLDVK FQESYLSKVV SLLKCQLSEG
AVSDKNASIE DSENGATQNG SEHEEMEEGE LPDSHGEPVV SGGEHVDVII GAAVADGKVT
PKVQALIKIL LKYQHTEDFR AIIFVERVVS ALVLPKVFAE LPSLSFVKCA SLIGHNNSQE
MRTYQMQDTI AKFRDGRVTL LVATSVAEEG LDIRQCNVVI RFDLAKTVLA YIQSRGRARK
PGSDYILMVE RQYQELKLYK ERGNLSHEAF LRNARNSEET LRKEAIERTD LSHLKDTSRL
ISVDTRPGTV YQVKSTGAVV SLNSAVDIQF FVLSLLWRGT KNQEVPRNIL ASFNCRAVCL
AACKKLHEMG AFTDMLLPDK GSGGEREKDE QTDEGDPLPG TARHREFYPE GVADTLKGEW
ILSGKDACNN SKLLHLYMYA VKCENIGYSK DPFLTQVSNF AVLFGNELDA EVLSMSMDLF
IARTVTTKAS LVFRGSINIT ESQLASLKSF HVRLMSIVLD VDVEPSTTPW DPAKAYLFVP
MVGDKSVDPM NQIDWHLVET IIGADAWKNP LQKARPDVYL GTNERTLGGD RREYGFGKLR
HGMAFGQKSH PTYGIRGAVA QFDVVKASGL VPNRDVMQTQ KHINMTTNGK LMMADTCANA
EDLVGKIVTA AHSGKRFYVD SIRYDMSADN SFPRKEGYLG PLEYSSYADY YKQKYGVDLI
YKQQPLIRGR GVSYCKNLLS PRFEHSEAHE GESEETLDKT YYVFLPPELC LLHPLPGSLV
RGAQRLPSIM RRVESMLLAV QLKNMINYPV QALKILEALT AASCQETFCY ERAELLGDAY
LKWVVSRFLF LKYPQKHEGQ LTRMRQQMVS NMVLYQYALS KGLQSYIQAD RFAPSRWAAP
GVLPVFDEDT KDGESSLFDQ ERSISKTERM DCQTNGYEDE MEDGELESDS SSYRVLSSKT
LADVVEALIG VYYVEGGKNA ANHLMKWIGI QIGFDPDEME CTRKPFNVPD SILRGVDFDA
LEGALNMKFK DKGLLIESIT HASRPSSGVS CYQRLEFVGD AVLDHLITRH LFFTYTNLPP
GRLTDLRAAA VNNENFARVA VKHNLHVHLR HGSSALEKQI KEFVKEVQDE LSKPGFNSFG
LGDCKAPKVL GDIVESIAGA IFLDSGRDTT VVWKVFQPLL HPMVTPETLP MHPVRELQER
CQQQAEGLEY KASRIGNLAT VEVFIDGVQV GAAQNPQKKM AQKLAARNAL AALKEKEEVG
KTQEKNDENG KKNGNQTFTR QTLNDICLRR NWPMPFYRCV NEGGPAHAKR FTFAVRVNTT
DRGWTDECIG EPMPSVKKAK DSAAYMNIAY QAQLILSIPI STVSNPNRLR FILIDGDRRI
VFLSIASRCA EYTLRRDPCT KSESSKKRRI SERR
//
