DOM34_SCHPO
ID DOM34_SCHPO Reviewed; 390 AA.
AC Q9USL5;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 117.
DE RecName: Full=Protein dom34;
DE EC=3.1.-.- {ECO:0000250|UniProtKB:P33309};
GN Name=dom34 {ECO:0000250|UniProtKB:P33309}; ORFNames=SPCC18B5.06;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1] {ECO:0000312|EMBL:CAB52153.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2] {ECO:0000305}
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: Involved in protein translation. Together with hbs1, may
CC function in recognizing stalled ribosomes and triggering
CC endonucleolytic cleavage of the mRNA, a mechanism to release non-
CC functional ribosomes and degrade damaged mRNAs. The complex formed by
CC dom34 and hbs1 has ribonuclease activity towards double-stranded RNA
CC substrates, but does not cleave single-stranded RNA. Acts as
CC endonuclease; has no exonuclease activity. Increases the affinity of
CC hbs1 for GTP, but nor for GDP. Promotes G1 progression and
CC differentiation and is involved in mitotic and meiotic cell divisions.
CC {ECO:0000250|UniProtKB:P33309}.
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250|UniProtKB:P33309};
CC -!- SUBUNIT: Monomer. Interacts with hbs1. {ECO:0000250|UniProtKB:P33309}.
CC -!- INTERACTION:
CC Q9USL5; O74774: hbs1; NbExp=5; IntAct=EBI-15882140, EBI-15882111;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
CC -!- DOMAIN: The N-terminal domain has the RNA-binding Sm fold. It harbors
CC the endoribonuclease activity. {ECO:0000250|UniProtKB:P33309}.
CC -!- SIMILARITY: Belongs to the eukaryotic release factor 1 family. Pelota
CC subfamily. {ECO:0000255}.
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DR EMBL; CU329672; CAB52153.1; -; Genomic_DNA.
DR PIR; T41199; T41199.
DR RefSeq; NP_587936.1; NM_001022927.2.
DR PDB; 3MCA; X-ray; 2.74 A; B=1-390.
DR PDBsum; 3MCA; -.
DR AlphaFoldDB; Q9USL5; -.
DR SMR; Q9USL5; -.
DR BioGRID; 275937; 18.
DR DIP; DIP-59038N; -.
DR IntAct; Q9USL5; 1.
DR STRING; 4896.SPCC18B5.06.1; -.
DR MaxQB; Q9USL5; -.
DR PaxDb; Q9USL5; -.
DR EnsemblFungi; SPCC18B5.06.1; SPCC18B5.06.1:pep; SPCC18B5.06.
DR GeneID; 2539371; -.
DR KEGG; spo:SPCC18B5.06; -.
DR PomBase; SPCC18B5.06; dom34.
DR VEuPathDB; FungiDB:SPCC18B5.06; -.
DR eggNOG; KOG2869; Eukaryota.
DR HOGENOM; CLU_023334_3_1_1; -.
DR InParanoid; Q9USL5; -.
DR OMA; DDLWHLK; -.
DR PhylomeDB; Q9USL5; -.
DR EvolutionaryTrace; Q9USL5; -.
DR PRO; PR:Q9USL5; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:1990533; C:Dom34-Hbs1 complex; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0030695; F:GTPase regulator activity; IDA:PomBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003747; F:translation release factor activity; IC:PomBase.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0002184; P:cytoplasmic translational termination; EXP:PomBase.
DR GO; GO:0030968; P:endoplasmic reticulum unfolded protein response; IMP:PomBase.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0070651; P:nonfunctional rRNA decay; IBA:GO_Central.
DR GO; GO:0070966; P:nuclear-transcribed mRNA catabolic process, no-go decay; IBA:GO_Central.
DR GO; GO:0070481; P:nuclear-transcribed mRNA catabolic process, non-stop decay; ISO:PomBase.
DR GO; GO:0032790; P:ribosome disassembly; IBA:GO_Central.
DR GO; GO:0071025; P:RNA surveillance; IEA:InterPro.
DR Gene3D; 2.30.30.870; -; 1.
DR Gene3D; 3.30.1330.30; -; 1.
DR Gene3D; 3.30.420.60; -; 1.
DR InterPro; IPR042226; eFR1_2_sf.
DR InterPro; IPR005140; eRF1_1_Pelota.
DR InterPro; IPR005141; eRF1_2.
DR InterPro; IPR005142; eRF1_3.
DR InterPro; IPR029064; L30e-like.
DR InterPro; IPR038069; Pelota/DOM34_N.
DR InterPro; IPR004405; Transl-rel_pelota.
DR PANTHER; PTHR10853; PTHR10853; 1.
DR Pfam; PF03463; eRF1_1; 1.
DR Pfam; PF03464; eRF1_2; 1.
DR Pfam; PF03465; eRF1_3; 1.
DR SMART; SM01194; eRF1_1; 1.
DR SUPFAM; SSF159065; SSF159065; 1.
DR SUPFAM; SSF55315; SSF55315; 1.
DR TIGRFAMs; TIGR00111; pelota; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell division; Cytoplasm; Endonuclease;
KW Hydrolase; Meiosis; Metal-binding; Mitosis; Nuclease; Reference proteome.
FT CHAIN 1..390
FT /note="Protein dom34"
FT /id="PRO_0000326089"
FT HELIX 24..32
FT /evidence="ECO:0007829|PDB:3MCA"
FT STRAND 38..40
FT /evidence="ECO:0007829|PDB:3MCA"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:3MCA"
FT STRAND 81..83
FT /evidence="ECO:0007829|PDB:3MCA"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:3MCA"
FT HELIX 119..125
FT /evidence="ECO:0007829|PDB:3MCA"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:3MCA"
FT STRAND 137..143
FT /evidence="ECO:0007829|PDB:3MCA"
FT STRAND 146..152
FT /evidence="ECO:0007829|PDB:3MCA"
FT STRAND 157..164
FT /evidence="ECO:0007829|PDB:3MCA"
FT HELIX 176..196
FT /evidence="ECO:0007829|PDB:3MCA"
FT TURN 199..201
FT /evidence="ECO:0007829|PDB:3MCA"
FT STRAND 203..212
FT /evidence="ECO:0007829|PDB:3MCA"
FT HELIX 213..227
FT /evidence="ECO:0007829|PDB:3MCA"
FT HELIX 231..236
FT /evidence="ECO:0007829|PDB:3MCA"
FT HELIX 237..239
FT /evidence="ECO:0007829|PDB:3MCA"
FT STRAND 240..244
FT /evidence="ECO:0007829|PDB:3MCA"
FT HELIX 250..254
FT /evidence="ECO:0007829|PDB:3MCA"
FT STRAND 256..258
FT /evidence="ECO:0007829|PDB:3MCA"
FT HELIX 260..266
FT /evidence="ECO:0007829|PDB:3MCA"
FT HELIX 270..287
FT /evidence="ECO:0007829|PDB:3MCA"
FT STRAND 291..295
FT /evidence="ECO:0007829|PDB:3MCA"
FT HELIX 296..304
FT /evidence="ECO:0007829|PDB:3MCA"
FT STRAND 308..310
FT /evidence="ECO:0007829|PDB:3MCA"
FT STRAND 312..315
FT /evidence="ECO:0007829|PDB:3MCA"
FT HELIX 323..338
FT /evidence="ECO:0007829|PDB:3MCA"
FT STRAND 343..346
FT /evidence="ECO:0007829|PDB:3MCA"
FT HELIX 351..358
FT /evidence="ECO:0007829|PDB:3MCA"
FT STRAND 361..368
FT /evidence="ECO:0007829|PDB:3MCA"
SQ SEQUENCE 390 AA; 44337 MW; 225978CC3D8F8E64 CRC64;
MKLIQKNIEK NGSGWITMCP EEPEDMWHLY NILQVGDQLK ASTVRRVVKV GATGSTSGSR
VVMKLRILVE NMDFDTKAAQ LHIKGRTTEY HPEVKMGSYH TLDLELHRNF TLYKNEWDAF
ALDRVDAACN PSRNAEIGAV VLDEGLANIC LITDYMTILR QRIDQVIPRK RRGDSSAYQK
GLDKFYDSVF QSINSEFDFD KLKVVILASP GFVARGLYDY IFSMAVKLDL KQIVKSKNKF
VILHSSTGHI HSLNEILKDP AVESKLADTK YVQEIRVLNK FYDVMNEDDR KAWYGPNHVL
KAFELGAIGE LLISDSLFRS SDIATRKKWV SLVEGVKEIN CPVYIFSSLH ESGKQLDLLS
GIAAILTYPV DEEDISEDEE DEESQNFEHS
