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Database: UniProt
Entry: G3B622_CANTC
LinkDB: G3B622_CANTC
Original site: G3B622_CANTC 
ID   G3B622_CANTC            Unreviewed;       573 AA.
AC   G3B622;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   RecName: Full=ribonuclease III {ECO:0000256|ARBA:ARBA00012177};
DE            EC=3.1.26.3 {ECO:0000256|ARBA:ARBA00012177};
GN   ORFNames=CANTEDRAFT_94123 {ECO:0000313|EMBL:EGV63359.1};
OS   Candida tenuis (strain ATCC 10573 / BCRC 21748 / CBS 615 / JCM 9827 / NBRC
OS   10315 / NRRL Y-1498 / VKM Y-70) (Yeast) (Yamadazyma tenuis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Yamadazyma.
OX   NCBI_TaxID=590646 {ECO:0000313|Proteomes:UP000000707};
RN   [1] {ECO:0000313|EMBL:EGV63359.1, ECO:0000313|Proteomes:UP000000707}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10573 / BCRC 21748 / CBS 615 / JCM 9827 / NBRC 10315 /
RC   NRRL Y-1498 / VKM Y-70 {ECO:0000313|Proteomes:UP000000707};
RX   PubMed=21788494; DOI=10.1073/pnas.1103039108;
RA   Wohlbach D.J., Kuo A., Sato T.K., Potts K.M., Salamov A.A., LaButti K.M.,
RA   Sun H., Clum A., Pangilinan J.L., Lindquist E.A., Lucas S., Lapidus A.,
RA   Jin M., Gunawan C., Balan V., Dale B.E., Jeffries T.W., Zinkel R.,
RA   Barry K.W., Grigoriev I.V., Gasch A.P.;
RT   "Comparative genomics of xylose-fermenting fungi for enhanced biofuel
RT   production.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:13212-13217(2011).
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; GL996524; EGV63359.1; -; Genomic_DNA.
DR   RefSeq; XP_006687152.1; XM_006687089.1.
DR   AlphaFoldDB; G3B622; -.
DR   STRING; 590646.G3B622; -.
DR   GeneID; 18250363; -.
DR   KEGG; cten:CANTEDRAFT_94123; -.
DR   eggNOG; KOG1817; Eukaryota.
DR   HOGENOM; CLU_026251_1_0_1; -.
DR   OrthoDB; 5475137at2759; -.
DR   Proteomes; UP000000707; Unassembled WGS sequence.
DR   GO; GO:0003725; F:double-stranded RNA binding; IEA:InterPro.
DR   GO; GO:0004525; F:ribonuclease III activity; IEA:InterPro.
DR   GO; GO:0006364; P:rRNA processing; IEA:InterPro.
DR   CDD; cd19876; DSRM_RNT1p-like; 1.
DR   CDD; cd00593; RIBOc; 1.
DR   Gene3D; 3.30.160.20; -; 2.
DR   Gene3D; 1.10.1520.10; Ribonuclease III domain; 1.
DR   InterPro; IPR014720; dsRBD_dom.
DR   InterPro; IPR040540; RNase_3_N.
DR   InterPro; IPR000999; RNase_III_dom.
DR   InterPro; IPR036389; RNase_III_sf.
DR   InterPro; IPR044449; Rnt1/Pac1_DSRM_fungi.
DR   PANTHER; PTHR11207:SF0; RIBONUCLEASE 3; 1.
DR   PANTHER; PTHR11207; RIBONUCLEASE III; 1.
DR   Pfam; PF00035; dsrm; 2.
DR   Pfam; PF00636; Ribonuclease_3; 1.
DR   Pfam; PF18497; RNase_3_N; 1.
DR   SMART; SM00358; DSRM; 2.
DR   SMART; SM00535; RIBOc; 1.
DR   SUPFAM; SSF54768; dsRNA-binding domain-like; 2.
DR   SUPFAM; SSF69065; RNase III domain-like; 1.
DR   PROSITE; PS50137; DS_RBD; 2.
DR   PROSITE; PS00517; RNASE_3_1; 1.
DR   PROSITE; PS50142; RNASE_3_2; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000000707};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW   ProRule:PRU00266}.
FT   DOMAIN          226..348
FT                   /note="RNase III"
FT                   /evidence="ECO:0000259|PROSITE:PS50142"
FT   DOMAIN          382..449
FT                   /note="DRBM"
FT                   /evidence="ECO:0000259|PROSITE:PS50137"
FT   DOMAIN          502..567
FT                   /note="DRBM"
FT                   /evidence="ECO:0000259|PROSITE:PS50137"
FT   REGION          1..74
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          168..194
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..25
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        26..44
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        49..71
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        169..194
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   573 AA;  64249 MW;  A216E2781ECD6744 CRC64;
     MNKDVYNPIN DSFRTFDASH TPSENESLVD QKRHMTDSAK DEGLPYPKRS GSVNSNSNVD
     LSNSSGEGLT GDGSGRPSFG FVDIKKLEHS ARMLQKNIKL IVDEAPNIEY LNQLIKSQRG
     SLDSLTYDSL RTNKLVHLAA QVKSLYEEGR LKIFDGILEN DLNKSDLSEI ETPNESPQDR
     STAPIIPSSD SENETYVSSV PDIIRNKDEE QFAVGSTDDC PELPLIKDPH LYARVFIHKS
     TINNKSYLYQ SELITSHNER LEFLGDSVLN NLATLIIYER YPTAPEGELS KMRSILVNNV
     TLAEFSIKYG FDKKLKSNIN DTILRQGKQK IFADIFEAYV GALSMEDNLE SGVLKSWLFK
     LYWSRLKVFD EEIRETEEVN KDAKSELYSL VGTAAFHPTY DVITTGDGAS KPFKVSCVMG
     DEVLGTAVAP GLKEAGLRAA MVALKNKPML EKYIQLRLNT DKTQSIVSHK QGSPMELETT
     TLVDPDIQLP LKAEKDMEFD SDARNKLYAI VSKKFNLVPE YYCEETEDRL FTAELRIDNK
     AIAFATDISK KKAMAKAAKL ALDTPAVFWN LHS
//
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