SEN1_SCHPO
ID SEN1_SCHPO Reviewed; 1687 AA.
AC Q92355;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Helicase sen1;
DE EC=3.6.4.-;
GN Name=sen1; ORFNames=SPAC6G9.10c;
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 PROTEIN SEQUENCE OF 1230-1241 AND 1489-1493, FUNCTION, AND SUBUNIT.
RC STRAIN=972 / ATCC 24843;
RX PubMed=10545196; DOI=10.1021/bi991470c;
RA Kim H.-D., Choe J., Seo Y.-S.;
RT "The sen1(+) gene of Schizosaccharomyces pombe, a homologue of budding
RT yeast SEN1, encodes an RNA and DNA helicase.";
RL Biochemistry 38:14697-14710(1999).
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: ATP-dependent 5'->3' DNA/RNA helicase required for the
CC expression and maturation of diverse classes of non-protein-coding RNAs
CC like precursor tRNAs, rRNAs and small nuclear (snRNA) and nucleolar
CC (snoRNA) RNAs. Directs RNA polymerase II transcription termination on
CC snoRNAs as well as on several short protein-coding genes. May also play
CC a role in transcription-coupled nucleotide excision repair (By
CC similarity). {ECO:0000250, ECO:0000269|PubMed:10545196}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:10545196}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the DNA2/NAM7 helicase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CU329670; CAB03612.1; -; Genomic_DNA.
DR PIR; T39072; T39072.
DR RefSeq; NP_594119.1; NM_001019543.2.
DR AlphaFoldDB; Q92355; -.
DR SMR; Q92355; -.
DR BioGRID; 278055; 36.
DR STRING; 4896.SPAC6G9.10c.1; -.
DR iPTMnet; Q92355; -.
DR MaxQB; Q92355; -.
DR PaxDb; Q92355; -.
DR PRIDE; Q92355; -.
DR EnsemblFungi; SPAC6G9.10c.1; SPAC6G9.10c.1:pep; SPAC6G9.10c.
DR GeneID; 2541556; -.
DR KEGG; spo:SPAC6G9.10c; -.
DR PomBase; SPAC6G9.10c; sen1.
DR VEuPathDB; FungiDB:SPAC6G9.10c; -.
DR eggNOG; KOG1801; Eukaryota.
DR HOGENOM; CLU_000459_2_0_1; -.
DR InParanoid; Q92355; -.
DR OMA; MIFMECW; -.
DR PhylomeDB; Q92355; -.
DR PRO; PR:Q92355; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0000785; C:chromatin; IDA:PomBase.
DR GO; GO:0016604; C:nuclear body; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0033678; F:5'-3' DNA/RNA helicase activity; IDA:PomBase.
DR GO; GO:0032574; F:5'-3' RNA helicase activity; 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; IBA:GO_Central.
DR GO; GO:0001147; F:transcription termination site sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0006369; P:termination of RNA polymerase II transcription; IBA:GO_Central.
DR GO; GO:0006386; P:termination of RNA polymerase III transcription; IMP:PomBase.
DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR CDD; cd18808; SF1_C_Upf1; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR045055; DNA2/NAM7-like.
DR InterPro; IPR041679; DNA2/NAM7-like_C.
DR InterPro; IPR041677; DNA2/NAM7_AAA_11.
DR InterPro; IPR024481; Helicase_Sen1_N.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR026121; Sen1.
DR PANTHER; PTHR10887; PTHR10887; 1.
DR PANTHER; PTHR10887:SF487; PTHR10887:SF487; 1.
DR Pfam; PF13086; AAA_11; 1.
DR Pfam; PF13087; AAA_12; 1.
DR Pfam; PF12726; SEN1_N; 2.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Direct protein sequencing; Helicase; Hydrolase;
KW mRNA processing; Nucleotide-binding; Nucleus; Reference proteome;
KW rRNA processing; tRNA processing.
FT CHAIN 1..1687
FT /note="Helicase sen1"
FT /id="PRO_0000080723"
FT REGION 781..801
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1661..1687
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1134
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 1155..1159
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 1407
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 1445
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 1574
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1687 AA; 192548 MW; 92C82F2049E2680D CRC64;
MAENLSDQDC FEKLSSSKEG QHWFCSGLLT QYIQPTFFWF AHDETPSFKW VLNAYHERLR
SCTSCIQAYY ELRNESLAKG SYSFTGFSIT DLQEKWNKWD IIRVLEDFKA LEDETIDFTS
LPCLIFETLL NPKLFTCKNI YKNAIDAFNG LLSDWCSNIF LPGYLLFFYE ASHPDVLEWV
HSFFKENTEI RISSATVDAV FNTVVFESQN SSDSDCNFVS ISSPEFWERT YMFLELLPLQ
SITAACESIL KDYLLNLVKT SESLSSQQMS CLRICCNSSS FWSAADSFKE VSSFLKNLLK
NVTATPFEVS DMNWAYIIAS FFRTCLNDFV SVFPEWLKGF VEEKRTIGFI IYSVLDALFD
LLSLDYSSPS FLNNTLSLMN ANSITILQDY PEYMLKLRLH SLLYDIAFIS WSHKAITKNP
SFVFDPSYEL SPFWKLDNLQ EEKISDVLFS KISSCCFAHD IEISENSTPS GTMVQFAELW
QVMSEYISGF LKGFSEKSST EISNMLGDSS KFDTVVSFLL SPTQPLYVSA FHIVQIITNC
TKNRNEALKK LVAMDFRGIV HGLADAVLNW QSILSFFPAL RIMRFLSITN KSLSSDNSAF
TENDIPTLGA YWQCIWNILD LVFSNVARWS LNNPADTVKA LMKLTLKFVD DLFQNDGIFI
KLLAKFDSLI LLGETSESLF SFIMWLKIND LELRGIVINS LCKLFTKFSN FDYLFEDRTV
TFLTDFIIRK QKAHLSADQC KQLANVLTQA SPEAKTVLEQ HRLSEMRKTK KQTELTNSAH
VIKPSPTPQI TVKQNTTKSS SAPRMGMLEQ LKQEYLTKRN FESKLKSSAV SSRKPTFNEV
KPANLLAEDL SDNEDDIDRK QGLFSLAKAN KIPEIRQQER RQVQLLSNST IKMHPSQIRM
MTNRNVANVK ARLFPSMTDF YKEILSWEPA NQSPNPVLKF HKLDGKIIDS FKTVEHYMEV
LQPMIFMECW SQIQSTKLDL KFSPVEGIMV ERTAVNNFVD IGVSVAPKDL YGYPLYDTEV
VSLAFNKEDA SSMKGLCCFA KVERIVRQTN GVLVVLRTLP SMEILNKLQG NCALWFLKLT
NLATFTRQYA GIRGLPYFHL ADDIIRARPC SQPVKHSSSE IKAAMKRYQV NEPQAKAIMC
ALDNNGFTLI QGPPGTGKTK TIIGIISALL VDLSRYHITR PNQQSKSTES KQQILLCAPS
NAAVDEVLLR LKRGFLLENG EKYIPRVVRI GNPETINVSV RDLSLEYQTE KQLLEVNQGA
IDLGSLQELT RWRDTFYDCI QKIEELEKQI DVARDVAEDT KSLGKELQNK INEKNLAEQK
VEELQSQSFT KNKEVDLLRK KAQKAILKQA DVVCATLSGS GHDLVAHSSL NFSTVIIDEA
AQAVELDTII PLRYGAKKCI LVGDPNQLPP TVLSKKAASL NYSQSLFVRI QKNFSNQMCL
LSIQYRMHPD ISHFPSKKFY DSRLEDGDNM AEKTQQVWHV NPKFTQYRLF DVRGKERTSN
TMSTYNLEEV EYLVNMVDEL LNKFPDVNFT GRIGVITPYR SQLHELRRAF KVKYGKSFMS
TIDIQTVDGF QGQEKDIIFF SCVKSYSKHG IGFLRDFRRL NVALTRARSS LLIIGNMETL
KTDDLWGSLV DDALSRKLVE SPHIDSEGRL ITISRTSEKR MKNEEFVEPP SKKLANSEPS
KEIRQRS
