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Database: UniProt
Entry: A0A2I3GVU5_NOMLE
LinkDB: A0A2I3GVU5_NOMLE
Original site: A0A2I3GVU5_NOMLE 
ID   A0A2I3GVU5_NOMLE        Unreviewed;      1324 AA.
AC   A0A2I3GVU5;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=ribonuclease III {ECO:0000256|ARBA:ARBA00012177};
DE            EC=3.1.26.3 {ECO:0000256|ARBA:ARBA00012177};
GN   Name=DROSHA {ECO:0000313|Ensembl:ENSNLEP00000035479.1};
OS   Nomascus leucogenys (Northern white-cheeked gibbon) (Hylobates leucogenys).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hylobatidae;
OC   Nomascus.
OX   NCBI_TaxID=61853 {ECO:0000313|Ensembl:ENSNLEP00000035479.1, ECO:0000313|Proteomes:UP000001073};
RN   [1] {ECO:0000313|Ensembl:ENSNLEP00000035479.1, ECO:0000313|Proteomes:UP000001073}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Gibbon Genome Sequencing Consortium;
RL   Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSNLEP00000035479.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.3;
CC         Evidence={ECO:0000256|ARBA:ARBA00000109};
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DR   EMBL; ADFV01084394; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ADFV01084395; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ADFV01084396; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ADFV01084397; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ADFV01084398; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; ADFV01084399; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_012357088.1; XM_012501634.1.
DR   STRING; 61853.ENSNLEP00000035479; -.
DR   Ensembl; ENSNLET00000034753.1; ENSNLEP00000035479.1; ENSNLEG00000013963.3.
DR   GeneTree; ENSGT00730000111052; -.
DR   InParanoid; A0A2I3GVU5; -.
DR   OMA; ENFTIHE; -.
DR   Proteomes; UP000001073; Chromosome 6.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR   GO; GO:0070877; C:microprocessor complex; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0014069; C:postsynaptic density; IEA:Ensembl.
DR   GO; GO:0017151; F:DEAD/H-box RNA helicase binding; IEA:Ensembl.
DR   GO; GO:0001530; F:lipopolysaccharide binding; IEA:Ensembl.
DR   GO; GO:0070878; F:primary miRNA binding; IEA:Ensembl.
DR   GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR   GO; GO:0070412; F:R-SMAD binding; IEA:Ensembl.
DR   GO; GO:0004525; F:ribonuclease III activity; IEA:Ensembl.
DR   GO; GO:0050829; P:defense response to Gram-negative bacterium; IEA:Ensembl.
DR   GO; GO:0050830; P:defense response to Gram-positive bacterium; IEA:Ensembl.
DR   GO; GO:0010586; P:miRNA metabolic process; IEA:Ensembl.
DR   GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR   GO; GO:0031054; P:pre-miRNA processing; IEA:Ensembl.
DR   GO; GO:0031053; P:primary miRNA processing; IEA:Ensembl.
DR   GO; GO:0050727; P:regulation of inflammatory response; IEA:Ensembl.
DR   GO; GO:2000628; P:regulation of miRNA metabolic process; IEA:Ensembl.
DR   GO; GO:0045589; P:regulation of regulatory T cell differentiation; IEA:Ensembl.
DR   GO; GO:0006364; P:rRNA processing; IEA:InterPro.
DR   CDD; cd19877; DSRM_RNAse_III_meta_like; 1.
DR   CDD; cd00593; RIBOc; 2.
DR   Gene3D; 3.30.160.20; -; 1.
DR   Gene3D; 1.10.1520.10; Ribonuclease III domain; 2.
DR   HAMAP; MF_00104; RNase_III; 1.
DR   InterPro; IPR014720; dsRBD_dom.
DR   InterPro; IPR011907; RNase_III.
DR   InterPro; IPR000999; RNase_III_dom.
DR   InterPro; IPR044442; RNAse_III_DSRM__animal.
DR   InterPro; IPR036389; RNase_III_sf.
DR   PANTHER; PTHR11207:SF0; RIBONUCLEASE 3; 1.
DR   PANTHER; PTHR11207; RIBONUCLEASE III; 1.
DR   Pfam; PF00035; dsrm; 1.
DR   Pfam; PF14622; Ribonucleas_3_3; 1.
DR   Pfam; PF00636; Ribonuclease_3; 1.
DR   SMART; SM00358; DSRM; 1.
DR   SMART; SM00535; RIBOc; 2.
DR   SUPFAM; SSF54768; dsRNA-binding domain-like; 1.
DR   SUPFAM; SSF69065; RNase III domain-like; 2.
DR   PROSITE; PS50137; DS_RBD; 1.
DR   PROSITE; PS00517; RNASE_3_1; 2.
DR   PROSITE; PS50142; RNASE_3_2; 2.
PE   3: Inferred from homology;
KW   Endonuclease {ECO:0000256|ARBA:ARBA00022759};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001073};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW   ProRule:PRU00266}.
FT   DOMAIN          826..1006
FT                   /note="RNase III"
FT                   /evidence="ECO:0000259|PROSITE:PS50142"
FT   DOMAIN          1057..1183
FT                   /note="RNase III"
FT                   /evidence="ECO:0000259|PROSITE:PS50142"
FT   DOMAIN          1210..1284
FT                   /note="DRBM"
FT                   /evidence="ECO:0000259|PROSITE:PS50137"
FT   REGION          1..359
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          402..447
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        69..114
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        127..154
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        167..265
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        304..345
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        402..428
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        429..443
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1324 AA;  153833 MW;  1CDF2223B7FADF18 CRC64;
     MMQGNTCHRM SFHPGRGCPR GRGGHGARPS APSFRPQNLR LLHPQQPPVQ YQYEPPSAPS
     TTFSNSPAPN FLPPRPDFVP FPPPMPPSAQ GPLPMMPPPS MPHPPPPPVM PQQVNYQYPP
     GYSHHNFPPP SFNSFQNNPS SFLPSANNSS SPHFRHLPPY PLPKAPSERR SPERLKHYDD
     HRHRDHSHGR GERHRSLDRR ERGRSPDRRR QDSRYRSDYD RGRTPSRHRS YERSRERERE
     RHRHRDNRRS PSLERSYKKE YKRSGRSYGL SVVPEPAGCT PELPGEIIKN TDSWAPPLEI
     MNHCSPSREK KRARWEEEKD RWSDNQSSGK DKNYTSIKEK EPEETVPDKN EEEEEELLKP
     VWIRCTHSEN YYSSDPMDQV GDSTVVGTSR LRDLYDKFEE ELGSRQEKAK AARPPWEPPK
     TKLDEDLESS SESECESDED STCSSSSDSE VFDVIAEIKR KKAHPDRLHD ELWYNDPGQM
     NDGPLCKCSA KARRTGIRHS IYPGEEAIKP CRPMTNNAGR LFHYRITVSP PTNFLTDRPT
     VIEYDDHEYI FEGFSMFAHA PLTNIPLCKV IRFNIDYTIH FIEEMMPENF CVKGLELFSL
     FLFRDILELY DWNLKGPLFE DSPPCCPRFH FMPRFVRFLP DGGKEVLSMH QILLYLLRCS
     KALVPEEEIA NMLQWEELEW QKYAEECKGM IVTNPGTKPS SVRIDQLDRE QFNPDVITFP
     IIVHFGIRPA QLSYAGDPQY QKLWKSYVKL RHLLANSPKV KQTDKQKLAQ REEALQKIRQ
     KNTMRREVTV ELSSQGFWKT GIRSDVCQHA MMLPVLTHHI RYHQCLMHLD KLIGYTFQDR
     CLLQLAMTHP SHHLNFGMNP DHARNSLSNC GIRQPKYGDR KVHHMHMRKK GINTLINIMS
     RLGQDDPTPS RINHNERLEF LGDAVVEFLT SVHLYYLFPS LEEGGLATYR TAIVQNQHLA
     MLAKKLELDR FMLYAHGPDL CRESDLRHAM ANCFEALIGA VYLEGSLEEA KQLFGRLLFN
     DPDLREVWLN YPLHPLQLQE PNTDRQLIET SPVLQKLTEF EEAIGVIFTH VRLLARAFTL
     RTVGFNHLTL GHNQRMEFLG DSIMQLVATE YLFIHFPDHH EGHLTLLRSS LVNNRTQAKV
     AEELGMQEYA ITNDKTKRPV ALRTKTLADL LESFIAALYI DKDLEYVHTF MNVCFFPRLK
     EFILNQDWND PKSQLQQCCL TLRTEGKEPD IPLYKTLQTV GPSHARTYTV AVYFKGERIG
     CGKGPSIQQA EMGAAMDALE KYNFPQMAHQ KRFIERKYRQ ELKEMRWERE HQEREPDETE
     DVKK
//
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