SLH1_SCHPO
ID SLH1_SCHPO Reviewed; 1935 AA.
AC O60072;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=RQC trigger complex helicase slh1 {ECO:0000250|UniProtKB:P53327};
DE AltName: Full=Meiotically up-regulated gene 81 protein;
DE AltName: Full=Putative helicase mug81;
DE EC=3.6.4.13 {ECO:0000250|UniProtKB:P53327};
GN Name=slh1 {ECO:0000312|PomBase:SPBC13G1.10c};
GN Synonyms=mug81 {ECO:0000303|PubMed:16303567};
GN ORFNames=SPBC13G1.10c {ECO:0000312|PomBase:SPBC13G1.10c};
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 FUNCTION IN MEIOSIS.
RX PubMed=16303567; DOI=10.1016/j.cub.2005.10.038;
RA Martin-Castellanos C., Blanco M., Rozalen A.E., Perez-Hidalgo L.,
RA Garcia A.I., Conde F., Mata J., Ellermeier C., Davis L., San-Segundo P.,
RA Smith G.R., Moreno S.;
RT "A large-scale screen in S. pombe identifies seven novel genes required for
RT critical meiotic events.";
RL Curr. Biol. 15:2056-2062(2005).
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).
CC -!- FUNCTION: Involved in activation of the ribosome quality control (RQC)
CC pathway, a pathway that degrades nascent peptide chains during
CC problematic translation (By similarity). Drives the splitting of
CC stalled ribosomes that are polyubiquitinated, as part of the ribosome
CC quality control trigger (RQT) complex (By similarity). Has a role in
CC meiosis (PubMed:16303567). {ECO:0000250|UniProtKB:P53327,
CC ECO:0000269|PubMed:16303567}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC Evidence={ECO:0000250|UniProtKB:P53327};
CC -!- SUBUNIT: Component of the RQT (ribosome quality control trigger)
CC complex. {ECO:0000250|UniProtKB:P53327}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
CC -!- DOMAIN: Composed of two similar domains.
CC -!- SIMILARITY: Belongs to the helicase family. SKI2 subfamily.
CC {ECO:0000305}.
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DR EMBL; CU329671; CAA18663.1; -; Genomic_DNA.
DR PIR; T39411; T39411.
DR RefSeq; NP_596560.1; NM_001022481.2.
DR AlphaFoldDB; O60072; -.
DR SMR; O60072; -.
DR BioGRID; 276228; 90.
DR STRING; 4896.SPBC13G1.10c.1; -.
DR iPTMnet; O60072; -.
DR MaxQB; O60072; -.
DR PaxDb; O60072; -.
DR PRIDE; O60072; -.
DR EnsemblFungi; SPBC13G1.10c.1; SPBC13G1.10c.1:pep; SPBC13G1.10c.
DR GeneID; 2539673; -.
DR KEGG; spo:SPBC13G1.10c; -.
DR PomBase; SPBC13G1.10c; slh1.
DR VEuPathDB; FungiDB:SPBC13G1.10c; -.
DR eggNOG; KOG0952; Eukaryota.
DR HOGENOM; CLU_000335_2_0_1; -.
DR InParanoid; O60072; -.
DR OMA; GTHHAGM; -.
DR PhylomeDB; O60072; -.
DR PRO; PR:O60072; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0099053; C:activating signal cointegrator 1 complex; ISO:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; ISO:PomBase.
DR GO; GO:0002181; P:cytoplasmic translation; ISO:PomBase.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0090304; P:nucleic acid metabolic process; IEA:UniProt.
DR Gene3D; 1.10.10.10; -; 2.
DR Gene3D; 2.60.40.150; -; 2.
DR Gene3D; 3.40.50.300; -; 4.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR004179; Sec63-dom.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF00270; DEAD; 2.
DR Pfam; PF00271; Helicase_C; 2.
DR Pfam; PF02889; Sec63; 2.
DR SMART; SM00382; AAA; 2.
DR SMART; SM00487; DEXDc; 2.
DR SMART; SM00490; HELICc; 2.
DR SMART; SM00973; Sec63; 2.
DR SUPFAM; SSF46785; SSF46785; 2.
DR SUPFAM; SSF52540; SSF52540; 3.
DR SUPFAM; SSF81296; SSF81296; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 2.
DR PROSITE; PS51194; HELICASE_CTER; 2.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Helicase; Hydrolase; Meiosis; Nucleotide-binding;
KW Reference proteome; Repeat.
FT CHAIN 1..1935
FT /note="RQC trigger complex helicase slh1"
FT /id="PRO_0000102100"
FT DOMAIN 287..479
FT /note="Helicase ATP-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 513..723
FT /note="Helicase C-terminal 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 787..1093
FT /note="SEC63 1"
FT DOMAIN 1144..1319
FT /note="Helicase ATP-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1351..1546
FT /note="Helicase C-terminal 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 1618..1934
FT /note="SEC63 2"
FT MOTIF 421..424
FT /note="DEVH box"
FT MOTIF 1261..1264
FT /note="DEIH box"
FT BINDING 300..307
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT BINDING 1157..1164
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 1935 AA; 218565 MW; 0D2C5981BAC5D1CC CRC64;
MEVELNYVVN HLEKLGPASF CDTPYSFSLS DSNAELGALS LKVDEILKTN YNLINPEDVT
DSDNNEFALK DLTWLQNCCN EISQSSSTEL DASVLFEAVI MSLKATEDQC AIQEDLLNLV
GLDHIDLISD IVANSSNLIE EYMNQNDTSI AAQLSDGYTS EAGSSATHGQ GLLDSLKSRP
RRFSRSRDNR GPLFTGQQVF EVEKYPHVYG DKRLGNTISV IGKKFALPAG SEREDYQKYE
EIIVPHAQRA PQMQGEKLLE ISSMDILCRK TFLSYQTLNR IQSLVYPIAY KTNENMLICA
PTGAGKTDVA LLAMLQTISN YVESMNLMDE SEPLDVHRDD FKIVYIAPMK ALAAEVVEKM
GKRLAWLGLK TRELTGDMQL TKTEIAETQI LVTTPEKWDV VTRKSVGDTQ LAEKVRLVII
DEVHMLHDER GAVIESLVAR TQRLVETSQQ MIRIVGLSAT LPNYLDVADF LGVNRYKGLF
YFSSAFRPCP IEQHFIGAKG SPKIVNSNID EACFDKVLKL IQEGHQVMIF VHSRKETINS
AKKLREQFFH EGEADLLDNS QHEKYSLAQR DVSKSKNKEL KELFKYSMGI HNAGMLRSDR
HLTERLFSMG ILKILCCTAT LAWGVNLPAY AVLIKGTQLY DPQKGSFVDL GVLDVLQIFG
RAGRPQFESS AVAYIITTHD KLSHYISVVT QQSPIESRFT DRLVDNLNAE VSLGTVTNID
EAVSWLGYTY LYIRMRRNPL VYGIAYDELV EDPLLGSKRR ELVSVAAGRL ADNQMIVYNK
KNGYLIPKDL GRIASNYYIN YQTVSTLNNL LKSKMSEADI IALLSQCSEF SQIKSRENEH
RELESLMENS SPCQLRDSIS NTSGKVNVIL QSYISRAHVE DFTLTSDTNY VAQNAGRITR
ALFEIAMSRT WASAFTILSL NKSIDRRQWS FEHPLLQFDL PHDLAVKVEN QCGSLSLEEL
SDMSTGELGD LIHNRKMGPT VKKFISKLPL LNINVDLLPL TKNVLRLVLN ITPNFNWDMR
YHGNSQMFWI FVEDSNGLEI LHHEQLLLNK RNVSTSHLLS FTIPVSNPLP SQLYIIAVSD
KWLGAETVTP VSLSNVVFHD DSNPITELLD LQPLPITALH DPVLEGICAK RFSFFNAVQT
QFFHTIYHTD TNIFVGAPTG SGKTMAAELA TWRALHNYPK SKVVYIAPMK ALVKERVKDW
GHRLVEPMGI SMIELTGDTN PDVKAVTNAN IIITTPEKWD GITRSWKSRK YVQDVSLIIL
DEIHLLGSDR GPVLEMIVSR MNYVASQTNK KVRVLGLSTA VANANDLANW LNIRDGLFNF
RHSVRPVPLE IYIDGFPGRA YCPRMMSMNK PAFQAIKTHS PTQPVLIFVS SRRQTRLTAK
DLIAFCGLED NPRRFLYMDE EELEMIVSEV EDKSLKLALP FGIALHHAGL TENDRKISEE
LFVNNKVQIL IATSTLAWGV NTPAHLVIVK GTEYYDAKIG GYKDMDLTDV LQMLGRAGRP
QFDNSGVARI FVQDIKKSFY KHFLHSGFPV ESYLHKVLDN HLNAEIATGT IDCIQGAMDF
LTCTYFYRRV HQNPVYYGAD GDDQKSIDTY LSKLVVTAFN ELEKSACIYR VNEETYAPTT
LGRIVSYYYL FHTTIRNFVQ KITENAEFDL ALQLLAEASE FDDLAIRHNE DLINIEINKS
LKYSAACLNL PMVDAHVKAF ILTQAHMARL KLPVDDYVTD TSTVLDQVIR IIQSYIDVSA
ELGYSHVCLQ YISLMQCLKQ ACYPSEIYRA SLPGLNASSE KEARDYLNKF AGNKTDELYQ
MLCNDPNVFD IESLVNSLIS YPKMNIEVSQ SSSDKLLLYL RRLNQPLNPD FYIFAPLFPK
PQSEGFFVLI IDSETQELFA IRRASFAGRR NDDSIRLSLR ISMDIPPTCR NRNVKVMVVC
DGYPLIYEHK IVLMI
