MFH2_SCHPO
ID MFH2_SCHPO Reviewed; 783 AA.
AC Q9HE09;
DT 23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Putative ATP-dependent DNA helicase fml2;
DE EC=3.6.4.12;
DE AltName: Full=FANCM-like protein 2;
GN Name=fml2 {ECO:0000303|PubMed:18851838};
GN Synonyms=mfh2 {ECO:0000312|PomBase:SPAC20H4.04};
GN ORFNames=SPAC20H4.04 {ECO:0000312|PomBase:SPAC20H4.04};
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 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 [3]
RP GENE NAME.
RX PubMed=18851838; DOI=10.1016/j.molcel.2008.08.024;
RA Sun W., Nandi S., Osman F., Ahn J.S., Jakovleska J., Lorenz A.,
RA Whitby M.C.;
RT "The FANCM ortholog Fml1 promotes recombination at stalled replication
RT forks and limits crossing over during DNA double-strand break repair.";
RL Mol. Cell 32:118-128(2008).
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=3.6.4.12;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC FANCM sub-subfamily. {ECO:0000305}.
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DR EMBL; CU329670; CAC19734.1; -; Genomic_DNA.
DR RefSeq; NP_593624.1; NM_001019055.2.
DR AlphaFoldDB; Q9HE09; -.
DR SMR; Q9HE09; -.
DR BioGRID; 278497; 55.
DR STRING; 4896.SPAC20H4.04.1; -.
DR iPTMnet; Q9HE09; -.
DR PaxDb; Q9HE09; -.
DR PRIDE; Q9HE09; -.
DR EnsemblFungi; SPAC20H4.04.1; SPAC20H4.04.1:pep; SPAC20H4.04.
DR PomBase; SPAC20H4.04; fml2.
DR VEuPathDB; FungiDB:SPAC20H4.04; -.
DR eggNOG; KOG0354; Eukaryota.
DR HOGENOM; CLU_002513_3_2_1; -.
DR InParanoid; Q9HE09; -.
DR OMA; YLLDCHG; -.
DR PhylomeDB; Q9HE09; -.
DR PRO; PR:Q9HE09; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005730; C:nucleolus; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0043138; F:3'-5' DNA helicase activity; ISO:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0000400; F:four-way junction DNA binding; IBA:GO_Central.
DR GO; GO:0009378; F:four-way junction helicase activity; IBA:GO_Central.
DR GO; GO:0045003; P:double-strand break repair via synthesis-dependent strand annealing; IBA:GO_Central.
DR GO; GO:0036297; P:interstrand cross-link repair; IBA:GO_Central.
DR GO; GO:1903461; P:Okazaki fragment processing involved in mitotic DNA replication; ISO:PomBase.
DR GO; GO:0071932; P:replication fork reversal; IBA:GO_Central.
DR CDD; cd18033; DEXDc_FANCM; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR039686; FANCM/Mph1-like.
DR InterPro; IPR044749; FANCM_DEXDc.
DR InterPro; IPR006935; Helicase/UvrB_N.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR14025:SF20; PTHR14025:SF20; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF04851; ResIII; 1.
DR SMART; SM00487; DEXDc; 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 3: Inferred from homology;
KW ATP-binding; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW Reference proteome.
FT CHAIN 1..783
FT /note="Putative ATP-dependent DNA helicase fml2"
FT /id="PRO_0000351000"
FT DOMAIN 118..286
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 450..619
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT MOTIF 234..237
FT /note="DEAH box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT BINDING 131..138
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 783 AA; 89463 MW; CD096AE05D9F0263 CRC64;
MIVLRDSSDY SDSEVDLPSI EVNGERGNVP TSVLCNVEGS LLNSNPALRQ PNLKCIKHNQ
DVENTTFQLD LRGCRVPSSQ PQVITELENN IDIPKNIDAM QNWIFPQTQQ YRNYQKEFCE
QALFHNLLLA LPTGLGKTFI AAVVMLNYFR WFPESKIIFL APTKPLLLQQ RVACSNVAGM
SPGATAELNG EVSPDRRLFE YNTKRVFFMT PQTLQNDLKE HLLDAKSIIC LIFDEAHRAT
GNHSYAQVMR AVLRSNSHFR VLGLTATPGS STASVQKVVD CLHISKLIVR NEESIDIRSY
VFHKKIQLIK VTISSEMNIL KSDFANLYRP YFNFLRQKKL IPINCECLNI KAYTLFVSLR
KYSFSSKNVQ SKEKSKIMSC FTLLISCAHI TYLLDCHGII QFYQKLVETK NKAEGKGSGQ
SFWLFTSKPF AFYLEHLHNK IQGLSLNHPK MNHLLELLKE HFKDTSEGYQ NQRVMIFTEF
RNTAEYITTT LLAIRPMVRA SLFIGQANSA YSTGMNQMQQ KETIDQFRAG VINTLVATSI
GEEGLDIGDT DMIICYDASS SPIRTIQRMG RTGRKKSGKV FVLLTEDCED SKWERSQVSY
RRVQKVIESG KKIALKKDVP RLIPSNIQPI FKFQALQNNA DATLILNSYN NNSSSLSPVN
TLANQAHSRS KRYLPFIVDD VFEDMESNLR VPTEDAKIKR FKSDYRSCIY NARRNVFSKP
TYMGDKLTKF AKVPHSLLTL SIYRRGRLLQ QCSPSSVTKY LKYEEKFKRK RMKKTSNALF
QST
