ID A0A0N5D3N1_THECL Unreviewed; 1324 AA.
AC A0A0N5D3N1;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 2.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=ribonuclease III {ECO:0000256|ARBA:ARBA00012177};
DE EC=3.1.26.3 {ECO:0000256|ARBA:ARBA00012177};
GN ORFNames=TCLT_LOCUS7534 {ECO:0000313|EMBL:VDN05000.1};
OS Thelazia callipaeda (Oriental eyeworm) (Parasitic nematode).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Thelazioidea; Thelaziidae; Thelazia.
OX NCBI_TaxID=103827 {ECO:0000313|Proteomes:UP000046394, ECO:0000313|WBParaSite:TCLT_0000754501-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:TCLT_0000754501-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (APR-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDN05000.1, ECO:0000313|Proteomes:UP000276776}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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; UYYF01004518; VDN05000.1; -; Genomic_DNA.
DR STRING; 103827.A0A0N5D3N1; -.
DR WBParaSite; TCLT_0000754501-mRNA-1; TCLT_0000754501-mRNA-1; TCLT_0000754501.
DR OMA; NDGPECR; -.
DR Proteomes; UP000046394; Unplaced.
DR Proteomes; UP000276776; Unassembled WGS sequence.
DR GO; GO:0004525; F:ribonuclease III activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0031054; P:pre-miRNA processing; IEA:InterPro.
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; 1.
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:UP000276776};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU00266}.
FT DOMAIN 785..963
FT /note="RNase III"
FT /evidence="ECO:0000259|PROSITE:PS50142"
FT DOMAIN 1015..1143
FT /note="RNase III"
FT /evidence="ECO:0000259|PROSITE:PS50142"
FT DOMAIN 1170..1245
FT /note="DRBM"
FT /evidence="ECO:0000259|PROSITE:PS50137"
FT REGION 164..198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 346..397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1255..1305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..192
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..397
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1269..1304
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1324 AA; 151118 MW; F51D7BEE9E100D18 CRC64;
MFPNQEHYFP RSNLSQQVLR PALAFPRYAY NNAFVPPSLN VHSTTSGQPP VFPLITPHAS
TTNLLTLRPL LSVPNSAAQA PVLRGLSYGA QRGIPGRLRP VFCSADKYPW QSANARQFVR
LPVNCSQVSV TSSRDMPRVA IKQNSHPREV MTSDVAIPVP ASDCMESAEE SADASDIDLK
HEGKEEGQKN KNWKKIKRQR RKRKRELCSS DGSDSEHIKS YFHLCILKNH LFSAALEHGS
SKDVPRWQKL TEEDFVDTIL SDTDDEADQL EQTVACSGFH LKCILDSRFY STNNAGDACA
TNELKKLQTK FKKEVIEKIA IEKENQPKSD PPEVIAFHEN CKCGHHSDTE TESESSDSDQ
CNDDSDDKGV DTSVTGSVAD NRRRINPEKL SESKKHSTVA KEEASSYFLS FVSRKRNHPA
VLHADVCFNE AGQVNDGPEC RCSWTAKKSG VRHNKYAGET VIKKCDPYSS NAHRLWHYIL
YTEPNPNTIA RRSTKINHEG KVFELEGFSV FFHRPLPLNF PQTPLSKWTS EYSMKFMKEA
TPTNFTVEDL ELFHHYLFID VMEMYDLKRY PLDDTEGCPY YHCMPRFVCN VQADEKEILP
MSVVLDFIIN SYHPFMTESQ ALIFKTDSEA YREFTETVRG SLVMDASKRP STIRADLIDS
PDFLPNNPDT LYPLITHFGV RPSSHTYNSN TEYQRMSKDY LKMRKILAMK PRVSAEERGK
LAQKASQLKA LRNDSQLRRD FVMSISSRNF YHTGLFPDIV QHGLLLILAC SHVRFQWSLE
VYEQERIHYV FKNRSLLELA LTHPSYRSSY GTNSDHARNT LNNCGVRSSK QRAHDRLVQQ
QLSAKKRGFH TLMEIMSKLG SKRVEQSPLN HNERLEFLGD AVIEFITTIH LFYMFSELDE
GGLATYRSAM VQNKNLALLA KKIGLDEFML YAHGPDLCHE SDLRHAMANA FEAMMAAIYL
DAGIDECDRI FGHAMFSDSE ELLSTWFNLE EHPLKRDNPN GDRHLINNIP ALQLLTQLEQ
NIGITFKHIR VLAKAFTRRN IGFNNLTLGH NQRLEFLGDT VLQLITTDYL YKHFPYHHEG
HLSILRTCLV SNRTQSVICD DIGMSKYVVT PKVMQKSGLP QLRVKDKADL VEAFLGALYV
DRGLDYCKVF CRICFFPRLK FFIISQHWND PKSQLQQCCL TLRQMDGSEP DIPEYKTIAV
EGPTNTRVYK VAVYFRNKRL AVGCGHTMQL AQMHAAENAL IKRADLFPTL KSAKHNTEQH
KHENNQTIKM KQESSNIRKQ QTSSDSSQSF QRDASASVTD DCQTPKPPIL SLLDLKFDED
GYLL
//
