FANCM_ARATH
ID FANCM_ARATH Reviewed; 1344 AA.
AC I3XHK1; Q9LQE5;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2012, sequence version 1.
DT 03-AUG-2022, entry version 46.
DE RecName: Full=DEAD-box ATP-dependent RNA helicase FANCM {ECO:0000305};
DE EC=3.6.4.13 {ECO:0000305};
DE AltName: Full=Fanconia anemia complementation group M-like protein {ECO:0000305};
GN Name=FANCM {ECO:0000303|PubMed:22547783};
GN OrderedLocusNames=At1g35530 {ECO:0000312|Araport:AT1G35530};
GN ORFNames=F15O4.40 {ECO:0000312|EMBL:AAF79368.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22547783; DOI=10.1105/tpc.112.096644;
RA Knoll A., Higgins J.D., Seeliger K., Reha S.J., Dangel N.J., Bauknecht M.,
RA Schropfer S., Franklin F.C., Puchta H.;
RT "The Fanconi anemia ortholog FANCM ensures ordered homologous recombination
RT in both somatic and meiotic cells in Arabidopsis.";
RL Plant Cell 24:1448-1464(2012).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP FUNCTION.
RX PubMed=22860689; DOI=10.1111/j.1365-313x.2012.05119.x;
RA Roth N., Klimesch J., Dukowic-Schulze S., Pacher M., Mannuss A., Puchta H.;
RT "The requirement for recombination factors differs considerably between
RT different pathways of homologous double-strand break repair in somatic
RT plant cells.";
RL Plant J. 72:781-790(2012).
RN [5]
RP FUNCTION.
RX PubMed=22723424; DOI=10.1126/science.1220381;
RA Crismani W., Girard C., Froger N., Pradillo M., Santos J.L., Chelysheva L.,
RA Copenhaver G.P., Horlow C., Mercier R.;
RT "FANCM limits meiotic crossovers.";
RL Science 336:1588-1590(2012).
RN [6]
RP FUNCTION.
RX PubMed=24635147; DOI=10.1111/tpj.12507;
RA Dangel N.J., Knoll A., Puchta H.;
RT "MHF1 plays Fanconi anaemia complementation group M protein (FANCM)-
RT dependent and FANCM-independent roles in DNA repair and homologous
RT recombination in plants.";
RL Plant J. 78:822-833(2014).
RN [7]
RP FUNCTION.
RX PubMed=25038251; DOI=10.1093/nar/gku614;
RA Girard C., Crismani W., Froger N., Mazel J., Lemhemdi A., Horlow C.,
RA Mercier R.;
RT "FANCM-associated proteins MHF1 and MHF2, but not the other Fanconi anemia
RT factors, limit meiotic crossovers.";
RL Nucleic Acids Res. 42:9087-9095(2014).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=26161528; DOI=10.1371/journal.pgen.1005369;
RA Girard C., Chelysheva L., Choinard S., Froger N., Macaisne N., Lemhemdi A.,
RA Lehmemdi A., Mazel J., Crismani W., Mercier R.;
RT "AAA-ATPase FIDGETIN-LIKE 1 and helicase FANCM antagonize meiotic
RT crossovers by distinct mechanisms.";
RL PLoS Genet. 11:E1005369-E1005369(2015).
CC -!- FUNCTION: Involved in ordered homologous recombination (HR) events in
CC somatic and meiotic cells (PubMed:22547783). Involved in the
CC suppression of spontaneous HR events in somatic cells (PubMed:22547783,
CC PubMed:24635147). Has an opposite function to the DNA binding cofactor
CC MHF1 which promotes spontaneous HR. Functions in replicative repair
CC independently of MHF1 and in a parallel pathway to the endonuclease
CC MUS81 (PubMed:24635147). Acts in the same pathway as the two DNA-
CC binding cofactors MHF1 and MHF2 to restrain class II meiotic crossover
CC (CO), and acts exclusively with MHF1 and MHF2 during meiosis to repair
CC DNA interstrand cross-links (ICLs) (PubMed:24635147, PubMed:25038251).
CC This common pathway is in parallel to the pathway that involves the
CC RECQ4A helicase (PubMed:24635147). Seems to be involved in the
CC stabilization of recombination intermediates (PubMed:22860689,
CC PubMed:22723424). Involved in DNA double-strand break (DSB) repair
CC during meiosis. Required for synthesis-dependent strand annealing
CC (SDSA) and to a lesser extent for single-strand annealing (SSA)
CC (PubMed:22860689, PubMed:26161528). May process meiotic DSB repair
CC intermediates, possibly D-loops, driving them toward noncrossover (NCO)
CC resolution (PubMed:22723424, PubMed:26161528).
CC {ECO:0000269|PubMed:22547783, ECO:0000269|PubMed:22723424,
CC ECO:0000269|PubMed:22860689, ECO:0000269|PubMed:24635147,
CC ECO:0000269|PubMed:25038251, ECO:0000269|PubMed:26161528}.
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:0000305};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305|PubMed:22547783}.
CC -!- DISRUPTION PHENOTYPE: Reduced fertility. {ECO:0000269|PubMed:22547783}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC FANCM sub-subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF79368.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; JQ278026; AFL55357.1; -; mRNA.
DR EMBL; AC007887; AAF79368.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; ANM58537.1; -; Genomic_DNA.
DR RefSeq; NP_001320963.1; NM_001333162.1.
DR AlphaFoldDB; I3XHK1; -.
DR SMR; I3XHK1; -.
DR STRING; 3702.AT1G35530.2; -.
DR PRIDE; I3XHK1; -.
DR ProteomicsDB; 230828; -.
DR EnsemblPlants; AT1G35530.3; AT1G35530.3; AT1G35530.
DR GeneID; 840448; -.
DR Gramene; AT1G35530.3; AT1G35530.3; AT1G35530.
DR KEGG; ath:AT1G35530; -.
DR Araport; AT1G35530; -.
DR eggNOG; KOG0354; Eukaryota.
DR PRO; PR:I3XHK1; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; I3XHK1; baseline and differential.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0043138; F:3'-5' DNA helicase activity; 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: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:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
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: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 2: Evidence at transcript level;
KW ATP-binding; DNA damage; DNA recombination; DNA repair; DNA-binding;
KW Helicase; Hydrolase; Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..1344
FT /note="DEAD-box ATP-dependent RNA helicase FANCM"
FT /id="PRO_0000440040"
FT DOMAIN 124..292
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 450..621
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 39..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 765..790
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1110..1148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1183..1218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1307..1344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 240..243
FT /note="DEAH box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT COMPBIAS 1203..1218
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 137..144
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 1344 AA; 150190 MW; 4F6F9E8574161CA1 CRC64;
MGSRVPIETI EEDGEFDWEA AVKEIDLACL KTTNASSSSS SHFTPLANPP ITANLTKPPA
KRQSTLDKFI GRTEHKPENH QVVSECGVND NDNSPLVGID PEAAKTWIYP VNGSVPLRDY
QFAITKTALF SNTLVALPTG LGKTLIAAVV MYNYFRWFPQ GKIVFAAPSR PLVMQQIEAC
HNIVGIPQEW TIDLTGQTCP SKRAFLWKSK RVFFVTPQVL EKDIQSGTCL TNYLVCLVID
EAHRALGNYS YCVVVRELMA VPIQLRILAL TATPGSKTQA IQGIIDNLQI STLEYRNESD
HDVCPYVHDR KLEVIEVPLG QDADDVSKRL FHVIRPYAVR LKNFGVNLNR DIQTLSPHEV
LMARDKFRQA PLPGLPHVNH GDVESCFAAL ITLYHIRKLL SSHGIRPAYE MLEEKLKEGP
FARLMSKNED IRMTKLLMQQ RLSHGAPSPK LSKMLEILVD HFKVKDPKTS RVIIFSNFRG
SVRDIMNALS NIGDMVKATE FIGQSSGKTL KGQSQKIQQA VLEKFRAGGF NVIVATSIGE
EGLDIMEVDL VICFDANVSP LRMIQRMGRT GRKNNGRVVV LACEGSEKNS YMRKQASGRA
IKKHMRNGGT NSFNFHPSPR MIPHVYKPEV QHVEFSIKQF VPRGKKLQEE YATETPAFQK
KLTPAETHML AKYYNNPDEE KLRVSLIAFP HFQTLPSKVH KVMHSRQTGM LIDAMQHLQE
PTFSEQSKSF FTEFRAPLGE REELDTGLRV TNDPKDLHSV RDLEVNTSQR KAKQVESPTS
TLETTEKDYE ESSPTHRYLF SSECASVDTL GNVFVMPVPL LFFPNVLESD NTPLPKTEKQ
HSCRNTSHID LVPVDTSEKH RQDNISCKLK ERFSPDGASE TLETHSLVKR NSTRVGEDDV
ANSVGEIVLS SDEDDCEGLE LSPRLTNFIK SGIVPESPVY DQGEANREED LEFPQLSSPM
RFSNELAGES SFPERKVQHK CNDYNIVSTT TELRTPQKEV GLANGTECLA VSPIPEDWRT
PLANLTNTNS SARKDWRVSS GEKLETLRQP RKLKRLRRLG DCSSAVKENY PGITEADHIR
SRSRGKKHIR GKKKMIMDDD VQVFIDEEAE VSSGAEMSAD ENEDVTGDSF EDSFIDDGTM
PTANTQAESG KVDMMAVYRR SLLSQSPLPA RFRDLAASSL SPYSAGPLTR INESRSDSDK
SLSSLRTPKT TNSESNQDAM MIGNLSVVQI SSDSRKRKFS LCNSANAPVI NLESKFAAHA
QATEKESHEG VRSNAGALEY NDDDDDAFFA TLDFDAMEAQ ATLLLSKQRS EAKEKEDATV
IPNPGMQRSD GMEKDAPSFD LGLW
