ID A0A2Y9E181_TRIMA Unreviewed; 1373 AA.
AC A0A2Y9E181;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=ribonuclease III {ECO:0000256|ARBA:ARBA00012177};
DE EC=3.1.26.3 {ECO:0000256|ARBA:ARBA00012177};
GN Name=LOC101341267 {ECO:0000313|RefSeq:XP_004385276.1};
OS Trichechus manatus latirostris (Florida manatee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Sirenia; Trichechidae; Trichechus.
OX NCBI_TaxID=127582 {ECO:0000313|Proteomes:UP000248480, ECO:0000313|RefSeq:XP_004385276.1};
RN [1] {ECO:0000313|RefSeq:XP_004385276.1}
RP IDENTIFICATION.
RG RefSeq;
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 RefSeq; XP_004385276.1; XM_004385219.2.
DR STRING; 127582.A0A2Y9E181; -.
DR GeneID; 101341267; -.
DR KEGG; tmu:101341267; -.
DR InParanoid; A0A2Y9E181; -.
DR OrthoDB; 5486676at2759; -.
DR Proteomes; UP000248480; Unplaced.
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; 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:UP000248480};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU00266}.
FT DOMAIN 875..1055
FT /note="RNase III"
FT /evidence="ECO:0000259|PROSITE:PS50142"
FT DOMAIN 1106..1232
FT /note="RNase III"
FT /evidence="ECO:0000259|PROSITE:PS50142"
FT DOMAIN 1259..1333
FT /note="DRBM"
FT /evidence="ECO:0000259|PROSITE:PS50137"
FT REGION 1..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 130..406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 451..496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..92
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..164
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..204
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..315
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 352..394
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 451..477
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 478..492
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1373 AA; 159169 MW; 23663D970AB78519 CRC64;
MMQGNTCHRM SFHPGRGCPR GRGGHGARPS APAFRPQNLR LLHPQQPPVQ YQYEPPSAPS
TTFSNSPAPN FLPPRPDFVP FPPPIPPSAQ GPIPPCPIRP PFANHQMRHP FPVPPCFPPM
PPPMPCPNNP PVPGAPPGQS TFPFMMPPPS MPHPPPPPVM PQQVNYQYPP GYSHHNFPPP
NFNSFQNNTS SFPPSASNSN SPHFRHLPPY PLTKTPSERR SPERLKHYDD HRHRDHSHGR
GERHRSLDRR ERGRSPDRRR QDSRYRSDYD RGRTPSRHRS YERSRERERE RHRHRDSRRS
PSLERPYKKE YKRSGRSYGL PVVLDPGCTP ELPGEITKNT DSLAPPLETM NHRSSSREKK
RTRWEDEKDK WSDSQSSGKE KTYTSIKEKE PEETLPDKNE EEEEELLKPV WIRCTHSENY
YSSDPMDQVG DSTVVGTSRL RDLYDKFEEE LGSRQEKAKA ARPPWEPPKT KLDEDLESSS
ESECESDEDS TCSSSSDSEV FDVIAEIKRK KAHPDRLHDE LWYNDPGQMN DGPLCKCSAK
ARRTGIRHSI YPGEEAIKPC RPMTNNAGRL FHYRITVSPP TNFLTDRPTV IEYDDHEYIF
EGFSMFAHAP LTNIPLCKVI RFNIDYTIHF IEEMMPENFC VRGLELFSLF LFRDILELYD
WNLKGPLFED NPPCCPRFHF MPRFVRFLPD GGKEVLSMHQ ILLYLLRCSK ALVPEEEIAN
MLQWEELEWQ KYAEECKGMI VTNPGTKPSS VRIDQLDREQ FNPDVITFPI IVHFGIRPAQ
LSYAGDPQYQ KLWKSYVKLR HLLANSPKVK QTDKQKLAQR EEALQKIRQK NTMRREVTVE
LSSQGFWKTG IRSDVCQHAM MLPVLTHHIR YHQCLMHLDK LIGYTFQDRC LLQLAMTHPS
HHLNFGMNPD HARNSLSNCG IRQPKYGDRK VHHMHMRKKG INTLINIMSR LGQDDPTPSR
INHNERLEFL GDAVVEFLTS VHLYYLFPSL EEGGLATYRT AIVQNQHLAM LAKKLELDRF
MLYAHGPDLC RESDLRHAMA NCFEALIGAV YLEGSLEEAK QLFGRLLFND PDLREVWLNY
PLHPLQLQEP NTDRQLIETS PVLQKLTEFE EAIGVIFTHV RLLARAFTLR TVGFNHLTLG
HNQRMEFLGD SIMQLVATEY LFIHFPDHHE GHLTLLRSSL VNNRTQAKVA EELGMQEYAI
TNDKTKRPVA LRTKTLADLL ESFIAALYID KDLEYVHTFM NVCFFPRLKE FILNQDWNDP
KSQLQQCCLT LRTEGKEPDI PLYKTLQTVG PSHARTYTVA VYFKGERIGC GKGPSIQQAE
MGAAMDALEK YNFPQMAHQK RFIERKYRQE LKEMRWEREH QEREPDETED VKK
//
