ID M7BAT1_CHEMY Unreviewed; 1336 AA.
AC M7BAT1;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=ribonuclease III {ECO:0000256|ARBA:ARBA00012177};
DE EC=3.1.26.3 {ECO:0000256|ARBA:ARBA00012177};
GN ORFNames=UY3_13633 {ECO:0000313|EMBL:EMP29258.1};
OS Chelonia mydas (Green sea-turtle) (Chelonia agassizi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Americhelydia; Chelonioidea; Cheloniidae; Chelonia.
OX NCBI_TaxID=8469 {ECO:0000313|EMBL:EMP29258.1, ECO:0000313|Proteomes:UP000031443};
RN [1] {ECO:0000313|Proteomes:UP000031443}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23624526; DOI=10.1038/ng.2615;
RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT into the development and evolution of the turtle-specific body plan.";
RL Nat. Genet. 45:701-706(2013).
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; KB557680; EMP29258.1; -; Genomic_DNA.
DR STRING; 8469.M7BAT1; -.
DR eggNOG; KOG1817; Eukaryota.
DR Proteomes; UP000031443; 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; PF00636; Ribonuclease_3; 2.
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:UP000031443};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU00266}.
FT DOMAIN 810..1033
FT /note="RNase III"
FT /evidence="ECO:0000259|PROSITE:PS50142"
FT DOMAIN 1069..1195
FT /note="RNase III"
FT /evidence="ECO:0000259|PROSITE:PS50142"
FT DOMAIN 1222..1296
FT /note="DRBM"
FT /evidence="ECO:0000259|PROSITE:PS50137"
FT REGION 1..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 414..457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 948..986
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 17..56
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..90
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..123
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..154
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..202
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..354
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 414..437
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1336 AA; 154916 MW; F27246F71A62506C CRC64;
MSFHSGRGCP RGRGGPGVRT STQTFRPQNL RQLHPQQPSV QYQYDQQVAP PTTYSSPPAT
GYVPPRPDFI PYPSLVPPST QSPISQCPMR PPFPNHQVRQ SFPVPPCFPP APPPVPNPSN
SPVPGAPTGQ NTFPYMMPPP AMPHPPPPPV MPQQVNYQPV YSTGYSQQSF PPPNFNSYQQ
NSNSFQSSSS SSSHFRHTSQ YQVEKAQSER RSPERSKHYD EHRHREHSHM HGDRHRPSNH
GDRRGDRGRS PDRRRQESSR HRSDYDRGRT PPRHRSYERS RERERERHRH RDSRRSPSSE
RSYRKDYKRT GSRSPSRERK RPRWEEERER WSENQSASKE KNYTAIKDKE PEEIISEKNE
EEEEELLKPV WVRCTHSESY YSNDPMDQVG DSTVVGTSRL RDLYERFEEE LGKRQAKAKA
ARPPWEPPKT KLDEDLESSS ESDCDSDDNS TCSSSSDSEV FDVIAEIKRK KAHPDRLHEE
LWYNDPGQMN DGPLCKCSAK ARRTGIRHSI YPGEEPIKPC RPMTNNAGRL YHYRITVSPP
TNFLTDRPTV IEYDDHEYIF EGFSMFAHAP LTNIPLCKVI RFNIDYTIHF IEEMMPENFC
VRGLELFSLY LFRDILELYD WNLIDGGKEV LSMHQILLYL LRCNKPLVPE EEIANMLQWE
ELEWQKYAEE CKGMIVTSPG MKPSSVRIDQ LDREQFNPDV ITFPIIVHFG IRPAQLSYAG
DPQYQKLWKS YVKLRHLLAN SPKVKQADKQ KLSQREEALQ KIRQKNTMRR EVTVELSSQG
FWKTGIRSDV CQHAMMLPVL THHIRYHQCL MHLDKLIGYT FQDRCLLQLA MTHPSHHLNF
GMNPDHARNS LSNCGIRQPK YGDRKVHHMH MRKKGINTLI NIMSRLGQDD PTPSRINHNE
RLEFLGDAVV EFLTSVHLYY LFPSLEEGGL ATYRTAIVQN QHLAMLAKSR RDKSTAKHSP
VDSGTPPPER EAQAESTGEL QLSTHRSEDT VKLELDRFML YAHGPDLCRE SDLRHAMANC
FEALIGAVYL EGSLEEAKHL FGRLLFNDTL QESNTDRQLI ETSPVLQKLT EFEEAIGVIF
THVRLLARAF TLRTVGFNHL TLGHNQRMEF LGDSIMQLVA TEYLFIHFPD HHEGHLTLLR
SSLVNNRTQA KVAEELGMQE FAITNDKTKR PVALRTKTLA DLLESFIAAL YIDKDLEYVH
TFMNVCFFPR LKEFILNQDW NDPKSQLQQC CLTLRTEGKE PDIPLYKTLQ TVGPSHARTY
TVAVYFKGER IGCGKGPSIQ QAEMGAAMDA LEKYNFPQMA HQKRFIERKY RQELKEMRWE
REHQEREPEE TEEVRK
//
