MTR4_SCHPO
ID MTR4_SCHPO Reviewed; 1117 AA.
AC O14232; Q9USD3;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=ATP-dependent RNA helicase mtr4;
DE EC=3.6.4.-;
GN Name=mtr4; ORFNames=SPAC6F12.16c;
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]
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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 752-966, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=ATCC 38364 / 968;
RX PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA Hiraoka Y.;
RT "Large-scale screening of intracellular protein localization in living
RT fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL Genes Cells 5:169-190(2000).
RN [3]
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).
RN [4]
RP IDENTIFICATION IN THE TRAMP COMPLEX.
RX PubMed=17512405; DOI=10.1016/j.cell.2007.03.038;
RA Buehler M., Haas W., Gygi S.P., Moazed D.;
RT "RNAi-dependent and -independent RNA turnover mechanisms contribute to
RT heterochromatic gene silencing.";
RL Cell 129:707-721(2007).
CC -!- FUNCTION: Component of the TRAMP complex which has a poly(A) RNA
CC polymerase activity and is involved in a post-transcriptional quality
CC control mechanism limiting inappropriate expression of genetic
CC information. Polyadenylation is required for the degradative activity
CC of the exosome on several of its nuclear RNA substrates (By
CC similarity). Required for heterochromatic gene silencing at centromeric
CC repeats by either exosome- or RNAi-mediated degradation of
CC heterochromatic transcripts. {ECO:0000250}.
CC -!- SUBUNIT: Component of the TRAMP complex (also called TRF4 complex)
CC composed of at least cid14, mtr4, and air1.
CC {ECO:0000269|PubMed:17512405}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10759889,
CC ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the helicase family. SKI2 subfamily.
CC {ECO:0000305}.
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DR EMBL; CU329670; CAB11099.1; -; Genomic_DNA.
DR EMBL; AB027847; BAA87151.1; -; Genomic_DNA.
DR PIR; T11667; T11667.
DR RefSeq; NP_593302.1; NM_001018732.2.
DR AlphaFoldDB; O14232; -.
DR SMR; O14232; -.
DR BioGRID; 278135; 20.
DR ELM; O14232; -.
DR IntAct; O14232; 2.
DR STRING; 4896.SPAC6F12.16c.1; -.
DR iPTMnet; O14232; -.
DR MaxQB; O14232; -.
DR PaxDb; O14232; -.
DR PRIDE; O14232; -.
DR EnsemblFungi; SPAC6F12.16c.1; SPAC6F12.16c.1:pep; SPAC6F12.16c.
DR PomBase; SPAC6F12.16c; mtr4.
DR VEuPathDB; FungiDB:SPAC6F12.16c; -.
DR eggNOG; KOG0948; Eukaryota.
DR HOGENOM; CLU_002902_1_4_1; -.
DR InParanoid; O14232; -.
DR OMA; IMLKNYN; -.
DR PhylomeDB; O14232; -.
DR Reactome; R-SPO-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR PRO; PR:O14232; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005730; C:nucleolus; ISO:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0031499; C:TRAMP complex; IDA:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; EXP:PomBase.
DR GO; GO:0000460; P:maturation of 5.8S rRNA; IBA:GO_Central.
DR GO; GO:0043630; P:ncRNA polyadenylation involved in polyadenylation-dependent ncRNA catabolic process; ISO:PomBase.
DR GO; GO:0006401; P:RNA catabolic process; IDA:PomBase.
DR GO; GO:0090503; P:RNA phosphodiester bond hydrolysis, exonucleolytic; IEA:GOC.
DR GO; GO:0016078; P:tRNA catabolic process; ISO:PomBase.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR025696; rRNA_proc-arch_dom.
DR InterPro; IPR016438; Ski2-like.
DR InterPro; IPR012961; Ski2_C.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF08148; DSHCT; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF13234; rRNA_proc-arch; 1.
DR PIRSF; PIRSF005198; Antiviral_helicase_SKI2; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM01142; DSHCT; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW Reference proteome; rRNA processing.
FT CHAIN 1..1117
FT /note="ATP-dependent RNA helicase mtr4"
FT /id="PRO_0000102098"
FT DOMAIN 207..363
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 441..642
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 19..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 414..433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 311..314
FT /note="DEIH box"
FT COMPBIAS 24..60
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..76
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 220..227
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT CONFLICT 758
FT /note="Y -> S (in Ref. 2; BAA87151)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1117 AA; 126191 MW; B73209E68247714D CRC64;
MFGGELDDAF GVFEGKVPKS LKEESKNSQN SQNSQKIKRT LTDKNASNQE QGTKKLESSV
GEQESATKRA KIENLKDNQD LIPNNDVNGI HINNSAVADT KHKPKIGDIA ADDISNEVSI
KNEGDTIPEA TVADSFEQEA SLQVAGKVGM TEAKSSTEEV VELRHQVRHQ VSIPPNYDYV
PISKHKSPIP PARTYPFTLD PFQAVSIACI ERQESVLVSA HTSAGKTVVA EYAVAQSLRD
KQRVIYTSPI KALSNQKYRE LLAEFGDVGL MTGDVTINPD ATCLVMTTEI LRSMLYRGSE
VMREVAWVIF DEIHYMRDKE RGVVWEETII LLPDKSHFVF LSATIPNAMQ FAEWITKIHR
QPCHVVYTDF RPTPLQHYLF PSGSDGIHLV VDEKSNFREE NFQRAMSALM EKQGDDPAAM
ATKGNAKKGK TGKGGVKGPS DIYKIVKMIM VKNYNPVIVF SFSKRECEAL ALQMSKLDMN
DQTERDLVTT IFNNAVNQLS EKDRELPQIE HILPLLRRGI GIHHSGLLPI LKEVIEILFQ
EGLLKVLFAT ETFSIGLNMP AKTVVFTNVR KFDGKTFRWI SGGEYIQMSG RAGRRGLDDR
GIVILMIDEK MDPPVAKSML KGEADRLDSA FHLSYNMILN LLRVEGISPE FMLERCFFQF
QNSLEVPKLE AKLEESQQHY DSFTILDERP LEEYHTLKTQ LERYRTDVRT VVNHPNFCLS
FLQGGRLVRV KVGNEDFDWG VVVNVSKRPL PKGQSNEYLP QESYIVHTLV MVASDTGPLR
IRSGHLPEVH PPAAEDKGKF EVVPFLLSSL DGIAHIRVFL PNDLKSQGQK LTVGKALSEV
KRRFPEGITL LDPVENMNIK EPTFIKLMKK VNILESRLLS NPLHNFSELE EKYAEYLRKL
ALLEEVKDLK KKLSKARSIM QLDELNSRKR VLRRLGFTTS DDVIEVKGRV ACEISSGDGL
LLTELIFNGM FNDLTPEQCA ALLSCLVFQE KSEVENQRMK EELAGPLKIL QEMARRIAKV
SKESKQELNE EEYVNSFKPS LMEVVYAWAH GASFAQICKM TDVYEGSLIR MFRRLEELIR
QMVDAAKVIG NTSLQQKMED TIACIHRDIV FSASLYL
