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Database: UniProt
Entry: G3HCB2_CRIGR
LinkDB: G3HCB2_CRIGR
Original site: G3HCB2_CRIGR 
ID   G3HCB2_CRIGR            Unreviewed;      1372 AA.
AC   G3HCB2;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 67.
DE   RecName: Full=ribonuclease III {ECO:0000256|ARBA:ARBA00012177};
DE            EC=3.1.26.3 {ECO:0000256|ARBA:ARBA00012177};
GN   Name=Drosha {ECO:0000313|Ensembl:ENSCGRP00001006583.1};
GN   ORFNames=I79_008119 {ECO:0000313|EMBL:EGW01612.1};
OS   Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Cricetulus.
OX   NCBI_TaxID=10029 {ECO:0000313|EMBL:EGW01612.1, ECO:0000313|Proteomes:UP000001075};
RN   [1] {ECO:0000313|Proteomes:UP000001075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CHO K1 cell line {ECO:0000313|Proteomes:UP000001075};
RX   PubMed=21804562; DOI=10.1038/nbt.1932;
RA   Xu X., Nagarajan H., Lewis N.E., Pan S., Cai Z., Liu X., Chen W., Xie M.,
RA   Wang W., Hammond S., Andersen M.R., Neff N., Passarelli B., Koh W.,
RA   Fan H.C., Wang J., Gui Y., Lee K.H., Betenbaugh M.J., Quake S.R.,
RA   Famili I., Palsson B.O., Wang J.;
RT   "The genomic sequence of the Chinese hamster ovary (CHO)-K1 cell line.";
RL   Nat. Biotechnol. 29:735-741(2011).
RN   [2] {ECO:0000313|EMBL:EGW01612.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Xu X., Nagarajan H., Lewis N.E., Pan S., Cai Z., Liu X., Chen W., Xie M.,
RA   Wang W., Hammond S., Andersen M.R., Neff N., Passarelli B., Koh W.,
RA   Fan C.H., Wang J., Gui Y., Lee K.H., Betenbaugh M.J., Quake S.R.,
RA   Famili I., Palsson B.O., Wang J.;
RT   "The genomic sequence of the Chinese hamster ovary CHO-K1 cell line.";
RL   Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Ensembl:ENSCGRP00001006583.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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   EMBL; JH000279; EGW01612.1; -; Genomic_DNA.
DR   RefSeq; XP_003501752.1; XM_003501704.2.
DR   RefSeq; XP_007640553.1; XM_007642363.1.
DR   RefSeq; XP_016830723.1; XM_016975234.1.
DR   STRING; 10029.G3HCB2; -.
DR   PaxDb; 10029-XP_007631627-1; -.
DR   Ensembl; ENSCGRT00001010369.1; ENSCGRP00001006583.1; ENSCGRG00001008885.1.
DR   GeneID; 100766983; -.
DR   CTD; 29102; -.
DR   eggNOG; KOG1817; Eukaryota.
DR   GeneTree; ENSGT00730000111052; -.
DR   OMA; ENFTIHE; -.
DR   OrthoDB; 5486676at2759; -.
DR   Proteomes; UP000001075; Unassembled WGS sequence.
DR   Proteomes; UP000694386; 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:UP000001075};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW   ProRule:PRU00266}.
FT   DOMAIN          874..1054
FT                   /note="RNase III"
FT                   /evidence="ECO:0000259|PROSITE:PS50142"
FT   DOMAIN          1105..1231
FT                   /note="RNase III"
FT                   /evidence="ECO:0000259|PROSITE:PS50142"
FT   DOMAIN          1258..1332
FT                   /note="DRBM"
FT                   /evidence="ECO:0000259|PROSITE:PS50137"
FT   REGION          1..103
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          119..407
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          445..495
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        54..71
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        74..103
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        119..163
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        176..203
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        215..313
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        332..348
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        351..393
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        445..476
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        477..491
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1372 AA;  158932 MW;  61F832563B5D1436 CRC64;
     MQGNTCHRMS FHPGRGCPRG RGGHGARPSA PSFRPQNLRL LHPQQPPVQY QYEPPSAPST
     TFSNSQASNF MPPRPDFVPY PPPMPPSSQG PAPPCPARPP YSNHQMRHPF PVPPCFPPMP
     PPMPCPNNPP VSGAPPGQGT FPFMVPPPSM PHPPPPPVMP QQVNYQYPPG YSHNFPPPNF
     NSFQNNSSSF PPSANNSSSP HFRHLPPYSL PKAQSERRSP ERLKHYDDHR HRDHSHGRGE
     RHRSLERRER GRSPERRRPD SRYRSEYERG RTPSRHRSYE RSRERERERH RHRENRRSPS
     PERSYKKEYK RSGRSYGLPV APEPAGCTPE SPGEITKNTD SWVPPPETVN HRSPSREKKR
     ARWEEEKDRW SDSQSSGKEK SYTSIKEKEP EEAPPDRNEE EEEELLKPVW IRCTHSESYY
     SSDPMDQVGD STVVGTSRLR DLYDKFEEEL GNRQEKAKAA RPPWEPPKTK LDEDLESSSE
     SECESDEEST CSSSSDSEVF DVIAEIKRKK AHPDRLHDEL WYNDPGQMND GPLCKCSAKA
     RRTGIRHSIY PGEEAIKPCR PMTNNAGRLF HYRITVSPPT NFLTDRPTVI EYDDHEYIFE
     GFSMFAHAPL TNIPLCKVIR FNIDYTIHFI EEMMPENFCV KGLELFSLFL FRDILELYDW
     NLKGPLFEDS PPCCPRFHFM PRFVRFLPDG GKEVLSMHQI LLYLLRCSKA LVPEEEIANM
     LQWEELEWQK YAEECKGMIV TNPGTKPSSV RIDQLDREQF NPDVITFPII VHFGIRPAQL
     SYAGDPQYQK LWKSYVKLRH LLANSPKVKQ TDKQKLAQRE EALQKIRQKN TMRREVTVEL
     SSQGFWKTGI RSDVCQHAMM LPVLTHHIRY HQCLMHLDKL IGYTFQDRCL LQLAMTHPSH
     HLNFGMNPDH ARNSLSNCGI RQPKYGDRKV HHMHMRKKGI NTLINIMSRL GQDDPTPSRI
     NHNERLEFLG DAVVEFLTSV HLYYLFPSLE EGGLATYRTA IVQNQHLAML AKKLELDRFM
     LYAHGPDLCR ESDLRHAMAN CFEALIGAVY LEGSLEEARQ LFGRLLFNDP DLREVWLHYP
     LHPLQLQEPN TDRQLIETSP VLQKLTEFEE AIGVIFTHVR LLARAFTLRT VGFNHLTLGH
     NQRMEFLGDS IMQLVATEYL FIHFPDHHEG HLTLLRSSLV NNRTQAKVAE ELGMQEYAIT
     NDKTKRPVAL RTKTLADLLE SFIAALYIDK DLEYVHTFMN VCFFPRLKEF ILNQDWNDPK
     SQLQQCCLTL RTEGKEPDIP LYKTLQTVGP SHARTYTVAV YFKGERIGCG KGPSIQQAEM
     GAAMDALEKY NFPQMAHQKR FIERKYRQEL KEMRWEREHQ EREPDEAEDV KK
//
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