ID S9Y6T9_CAMFR Unreviewed; 918 AA.
AC S9Y6T9;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
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=CB1_000900004 {ECO:0000313|EMBL:EPY79700.1};
OS Camelus ferus (Wild bactrian camel) (Camelus bactrianus ferus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Tylopoda; Camelidae; Camelus.
OX NCBI_TaxID=419612 {ECO:0000313|EMBL:EPY79700.1, ECO:0000313|Proteomes:UP000030684};
RN [1] {ECO:0000313|EMBL:EPY79700.1, ECO:0000313|Proteomes:UP000030684}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=bactrian camel {ECO:0000313|Proteomes:UP000030684};
RX PubMed=23149746;
RG Bactrian Camels Genome Sequencing and Analysis Consortium;
RA Jirimutu, Wang Z., Ding G., Chen G., Sun Y., Sun Z., Zhang H., Wang L.,
RA Hasi S., Zhang Y., Li J., Shi Y., Xu Z., He C., Yu S., Li S., Zhang W.,
RA Batmunkh M., Ts B., Narenbatu, Unierhu, Bat-Ireedui S., Gao H.,
RA Baysgalan B., Li Q., Jia Z., Turigenbayila, Subudenggerile, Narenmanduhu,
RA Wang Z., Wang J., Pan L., Chen Y., Ganerdene Y., Dabxilt, Erdemt, Altansha,
RA Altansukh, Liu T., Cao M., Aruuntsever, Bayart, Hosblig, He F., Zha-ti A.,
RA Zheng G., Qiu F., Sun Z., Zhao L., Zhao W., Liu B., Li C., Chen Y.,
RA Tang X., Guo C., Liu W., Ming L., Temuulen, Cui A., Li Y., Gao J., Li J.,
RA Wurentaodi, Niu S., Sun T., Zhai Z., Zhang M., Chen C., Baldan T.,
RA Bayaer T., Li Y., Meng H.;
RT "Genome sequences of wild and domestic bactrian camels.";
RL Nat. Commun. 3:1202-1202(2012).
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; KB017144; EPY79700.1; -; Genomic_DNA.
DR AlphaFoldDB; S9Y6T9; -.
DR Proteomes; UP000030684; 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; 1.
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:UP000030684};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU00266}.
FT DOMAIN 547..635
FT /note="RNase III"
FT /evidence="ECO:0000259|PROSITE:PS50142"
FT DOMAIN 655..781
FT /note="RNase III"
FT /evidence="ECO:0000259|PROSITE:PS50142"
FT DOMAIN 808..869
FT /note="DRBM"
FT /evidence="ECO:0000259|PROSITE:PS50137"
FT REGION 1..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 225..269
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 894..918
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..168
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..251
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 252..266
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 918 AA; 106038 MW; 35D78864E926CC87 CRC64;
MPQQVNYQYP PGYSHHNFPP PNFNSFQNNS SSFPPSANNS SSPHFRHLPP YPLPKAPSER
RSPERLKHYD DHRHRDHSHG RGERHRSLDR RERGRSPDRR RQDSRYRSDY DRGRTPSRHR
SYERSSRSPS REKKRARWEE EKDRWSDNQS SGKEKNYTSI KEKEPEEVLP DKNEEEEEEL
LKPVWIRCTH SENYYSSDPM DQVGDSTVVG TSRLRDLYDK FEEELGSRQE KAKAARPPWE
PPKTKLDEDL ESSSESECES DEDSTCSSSS DSEVFDVIAE IKRKKAHPDR LHDELWYNDP
GQAIKPCRPM TNNAGRLFHY RITVSPPTNF LTDRPTVIEY DDHEYIFEGF SMFAHAPLTN
VNGGKEVLSM HQILLYLLRC SKALVPEEEI ANMLQWEELE WQKYAEECKG MIVTNPGTKP
SSVRIDQLDR EQFNPDVITF PIIVHFGIRP AQLSYAGDPQ YQKLWKSYVK LRHLLANSPK
VKQTDKQKLA QREEALQKIR QKNTMRREVT VELSSQGFWK TGIRSDVCQH AMMLPVLTHH
IRYHQCLMHL DKLIGYTFQD RCLLQAAPVP PAKAIRAADY EEINHNERLE FLGDAVVEFL
TSVHLYYLFP SLEEGGLATY RTAIVQNQHL AMLAKLQEPN TDRQLIETSP VLQKLTEFED
AIGVIFTHVR LLARAFTLRT VGFNHLTLGH NQRMEFLGDS IMQLVATEYL FIHFPDHHEG
HLTLLRSSLV NNRTQAKVAE ELGMQEYAIT NDKTKRPVAL RTKTLADLLE SFIAALYIDK
DLEYVHTFMN VCFFPRLKEF ILNQDWNDPK SQLQQCCLTL RTEGKEPDIP LYKTLQTVGP
SHARTYTVAV YFKGERIGCG KGPRNSEAEV KRMTMAVSAP SLDLLHLDLA ENPVLEPDSM
SPGGSSRKQG SLASLVFP
//
