FANCM

Fanconi anemia group M protein

2048 amino acids

DNA-dependent ATPase component of the Fanconi anemia (FA) core complex (PubMed:16116422). Required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage (PubMed:16116422, PubMed:19423727, PubMed:20347428, PubMed:20347429, PubMed:29231814). In complex with CENPS and CENPX, binds double-stranded DNA (dsDNA), fork-structured DNA (fsDNA) and Holliday junction substrates (PubMed:20347428, PubMed:20347429). Its ATP-dependent DNA branch migration activity can process branched DNA structures such as a movable replication fork. This activity is strongly stimulated in the presence of CENPS and CENPX (PubMed:20347429). In complex with FAAP24, efficiently binds to single-strand DNA (ssDNA), splayed-arm DNA, and 3'-flap substrates (PubMed:17289582). In vitro, on its own, strongly binds ssDNA oligomers and weakly fsDNA, but does not bind to dsDNA (PubMed:16116434).

Belongs to the DEAD box helicase family. DEAH subfamily. FANCM sub-subfamily.

232.191 kDa

MSGRQRTLFQTWGSSISRSSGTPGCSSGTERPQSPGSSKAPLPAAAEAQLESDDDVLLVAAYEAERQLCLENGGFCTSAGALWIYPTNCPVRDYQLHISRAALFCNTLVCLPTGLGKTFIAAVVMYNFYRWFPSGKVVFMAPTKPLVTQQIEACYQVMGIPQSHMAEMTGSTQASTRKEIWCSKRVLFLTPQVMVNDLSRGACPAAEIKCLVIDEAHKALGNYAYCQVVRELVKYTNHFRILALSATPGSDIKAVQQVITNLLIGQIELRSEDSPDILTYSHERKVEKLIVPLGEELAAIQKTYIQILESFARSLIQRNVLMRRDIPNLTKYQIILARDQFRKNPSPNIVGIQQGIIEGEFAICISLYHGYELLQQMGMRSLYFFLCGIMDGTKGMTRSKNELGRNEDFMKLYNHLECMFARTRSTSANGISAIQQGDKNKKFVYSHPKLKKLEEVVIEHFKSWNAENTTEKKRDETRVMIFSSFRDSVQEIAEMLSQHQPIIRVMTFVGHASGKSTKGFTQKEQLEVVKQFRDGGYNTLVSTCVGEEGLDIGEVDLIICFDSQKSPIRLVQRMGRTGRKRQGRIVIILSEGREERIYNQSQSNKRSIYKAISSNRQVLHFYQRSPRMVPDGINPKLHKMFITHGVYEPEKPSRNLQRKSSIFSYRDGMRQSSLKKDWFLSEEEFKLWNRLYRLRDSDEIKEITLPQVQFSSLQNEENKPAQESTTGIHQLSLSEWRLWQDHPLPTHQVDHSDRCRHFIGLMQMIEGMRHEEGECSYELEVESYLQMEDVTSTFIAPRNESNNLASDTFITHKKSSFIKNINQGSSSSVIESDEECAEIVKQTHIKPTKIVSLKKKVSKEIKKDQLKKENNHGIIDSVDNDRNSTVENIFQEDLPNDKRTSDTDEIAATCTINENVIKEPCVLLTECQFTNKSTSSLAGNVLDSGYNSFNDEKSVSSNLFLPFEEELYIVRTDDQFYNCHSLTKEVLANVERFLSYSPPPLSGLSDLEYEIAKGTALENLLFLPCAEHLRSDKCTCLLSHSAVNSQQNLELNSLKCINYPSEKSCLYDIPNDNISDEPSLCDCDVHKHNQNENLVPNNRVQIHRSPAQNLVGENNHDVDNSDLPVLSTDQDESLLLFEDVNTEFDDVSLSPLNSKSESLPVSDKTAISETPLVSQFLISDELLLDNNSELQDQITRDANSFKSRDQRGVQEEKVKNHEDIFDCSRDLFSVTFDLGFCSPDSDDEILEHTSDSNRPLDDLYGRYLEIKEISDANYVSNQALIPRDHSKNFTSGTVIIPSNEDMQNPNYVHLPLSAAKNEELLSPGYSQFSLPVQKKVMSTPLSKSNTLNSFSKIRKEILKTPDSSKEKVNLQRFKEALNSTFDYSEFSLEKSKSSGPMYLHKSCHSVEDGQLLTSNESEDDEIFRRKVKRAKGNVLNSPEDQKNSEVDSPLHAVKKRRFPINRSELSSSDESENFPKPCSQLEDFKVCNGNARRGIKVPKRQSHLKHVARKFLDDEAELSEEDAEYVSSDENDESENEQDSSLLDFLNDETQLSQAINDSEMRAIYMKSLRSPMMNNKYKMIHKTHKNINIFSQIPEQDETYLEDSFCVDEEESCKGQSSEEEVCVDFNLITDDCFANSKKYKTRRAVMLKEMMEQNCAHSKKKLSRIILPDDSSEEENNVNDKRESNIAVNPSTVKKNKQQDHCLNSVPSGSSAQSKVRSTPRVNPLAKQSKQTSLNLKDTISEVSDFKPQNHNEVQSTTPPFTTVDSQKDCRKFPVPQKDGSALEDSSTSGASCSKSRPHLAGTHTSLRLPQEGKGTCILVGGHEITSGLEVISSLRAIHGLQVEVCPLNGCDYIVSNRMVVERRSQSEMLNSVNKNKFIEQIQHLQSMFERICVIVEKDREKTGDTSRMFRRTKSYDSLLTTLIGAGIRILFSSCQEETADLLKELSLVEQRKNVGIHVPTVVNSNKSEALQFYLSIPNISYITALNMCHQFSSVKRMANSSLQEISMYAQVTHQKAEEIYRYIHYVFDIQMLPNDLNQDRLKSDI

FANCM

Fanconi anemia group M protein

2041 amino acids

DNA-dependent ATPase component of the Fanconi anemia (FA) core complex (By similarity). Required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage (PubMed:16116434, PubMed:19465393). In complex with CENPS and CENPX, binds double-stranded DNA (dsDNA), fork-structured DNA (fsDNA) and Holliday junction substrates (By similarity). Its ATP-dependent DNA branch migration activity can process branched DNA structures such as a movable replication fork (By similarity). This activity is strongly stimulated in the presence of CENPS and CENPX (By similarity). In complex with FAAP24, efficiently binds to single-strand DNA (ssDNA), splayed-arm DNA, and 3'-flap substrates (By similarity). In vitro, on its own, strongly binds ssDNA oligomers and weakly fsDNA, but does not bind to dsDNA (By similarity).

Belongs to the DEAD box helicase family. DEAH subfamily. FANCM sub-subfamily.

224.006 kDa

MSGGRQRTLPEAWRRAAGPALQAGRDADGNDDDDDELLAAAAAELDPDPNPNVDPNPGPGPEAAAGGFCAAAGALWIYPTNRPERPYQLRMARAALFANTLLCLPTGLGKTFVAAVVMYNFYRWFPSGKVLFLAPTKALVAQQMEACAQLMGIPGRDMAEMTGGTQALSRRELWASRRVFFLTPQIMVNDLSRGTCPAVEVKCLVVDEAHKALGNHAYCQVVKELSRYTTQFRVLALTATPGSDTKAVQQVVSNLLIAQIELCSEDSPEIQPYSHERQVEKIVVPLGEELGGIQRAYIHVLETFAGRLIKLGVLARRDVPSLTKYQIILARDQYRKNPSPQNVGMQPGIIEGDFALCISLYHGYELLQQMGVRSLFIYLCGIMDGSKGLTRTKNELGRNEDFMRLYQQLTDMFSDTCQTSANGNLHKSRTVSENKKEFIYSHPKLKKLEEIVIEHFKSRKMGCSDQTTSGGTCVDTRVMIFSSFRDSVQEIAEMLSRFSPVVRVMTFVGHSTGKSTKGFTQKEQLEVVKRFREGGYNTLVSTCVGEEGLDIGEVDLIICFDAQKSPIRLVQRMGRTGRQRQGRVVVILAEGREERTYNQSQSNRRSIQKAISGNKMLHFYQHSPRMIPEGINPELHRMFITAEKYKPNDSGRLPKGRPSSLHHKSALFSCVTDPKEMHCHENWSLSPEEFEIWDRLYRLKENDGVKEPILPHTRFETLENLDKTSKPEEEAAHKLSLSEWSIWQSRPFPTSMVDHSDRCYHFISVMELIEVMRQEQGDCSYELELQPHLRIEDIHVRRNKGHLSTTSSAFAQKTHSSKRDMARTKRPFVPDVNDNEREFFSIFKTTNTKTPRTAPGLDLEEPELPTDTNGSEPCSARRLTLVASTDQGSPKEEEIEKVTFDLNEFNDLCDDGESTVAHESAAVKDLRLLDKHCSSVGLNHTDLGYSSFTAEKSPASSDLFYLPESHVDSFVLVSSSAELAGLEGAFSCVKGLLAHSPPPVSKLEGIEELLRHEETLCPLPKVSCRSYSGQLPHGDFPSSLAVDQSLLPAESPELEVTIGLSAAVNTCVSKPASTPTAAGGAEERPPGGGSFHSLLGKEGFTANHTDNPPNKHFVQGDEEDSEMKRDVTIDGEKSIHLFEDEHTYKVNDEMPSVDVEPLLRLGSGGHTARPSAGPASQQPPSGDSPRGDTACGEGAARGEMAPGGAWGRGSAAEQALHNSELCDYSQELFSVNFDLGFSIEECEEEIFEGDTDAMNTPKLNSASRSRADVQLTANRKSLNDGCRVQTPPKWDCKGLKGRNISTPLPLQSGHVRDTAVPGGTAGGRTGRGSPGASPPSPATPTGRRVSSAEATRRIRKKVFSTVREETPEVCPTDKVNPNSQRNSFGSSASDALHTTGGRTENLEGTNLHTSRVFPAEGTSSESEEEIVFQRKNRRNNVLRSPDVGSDSDFGSPVCAVRKRRHPLTVSDVSSDDGVDFHKNPNRGTRGCSAAGSKAQLRGVKRQKVRSKVTCKNAARQFLDEEAELSQQDESCVSSDETEDTDKELSSSLAQFLNDDAEVTQVLNDSEMRGVYLKSVRSPALGSRYRMVHREFNSTEIFSQIPEQDEAYAEDSFCVAEGDEETCNKSESSEEEEVCVNFDLLNNESFGGGGGRYLTRRRKKLHGANMEQNCSAPVQKKPSRIIVLSDSSGEETNVSNEKGTAAHCSRAGRENAELLTSMPSVSSVPHKKSAGDVSAHQSAESKSGMLLGLKASVSEVLDFHPGPRSGSGKEALQAAAQHLQLESSVKNSAGNAPGATKASPALLDGDTALCVLVDSREISSGADVISSLKAVHGLKVQVCSLGSGDYVVSNRMAVERKFQSELLSSVNRTKVTQRLQRLQGMFERVCVIVEKDRTRPGETSRFSQRTQHYDATLAALLQAGIRVLFSSCQEETAVLLKELALLEQRKNAAICVPTEVEGHKQEMLNFYLSLPNISYLAALNMCHHFSSVRTMVNSSPSDIAAGARVSLQRAEETYRYLRYGFDTQMLPESLCAKGKSNTATRS

Fancm

Fanconi anemia group M protein homolog

2021 amino acids

DNA-dependent ATPase component of the Fanconi anemia (FA) core complex. Required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. In complex with CENPS and CENPX, binds double-stranded DNA (dsDNA), fork-structured DNA (fsDNA) and Holliday junction substrates. Its ATP-dependent DNA branch migration activity can process branched DNA structures such as a movable replication fork. This activity is strongly stimulated in the presence of CENPS and CENPX. In complex with FAAP24, efficiently binds to single-strand DNA (ssDNA), splayed-arm DNA, and 3'-flap substrates. In vitro, on its own, strongly binds ssDNA oligomers and weakly fsDNA, but does not bind to dsDNA.

Belongs to the DEAD box helicase family. DEAH subfamily. FANCM sub-subfamily.

226.018 kDa

MSGRQRTLFQTWGPSLVRGSGDSGCGQPRSPAMAEALPEEDDEVLLVAAYEAERQLDPGDGGFCAAAGALWIYPTNCPVRDYQLDISRSALFCNTLVCLPTGLGKTFIAAVVMYNFYRWFPSGKVVFMAPTKPLVTQQMEACFHVMGIPQSHMAEMTGSTQAVNRKEIWSSRRVLFLTPQVMVNDLTRGAVPATHVKCLVVDEAHKALGNYAYCQVVRELVKYTTHFRILALSATPGSDIKAVQQVITNLLIGKIELRSEESPDILPYSHERRVEKLVVPLGEELGAIQKTYIQILETFASSLIHRNVLMKRDIPNLTKYQIILARDQFRKNPSPNIVGIQQGIIEGEFALCISLYHGYELLQQMGMRSLYFFLSGIMDGTKGMTRARNELSRNEDFMKLYTHLQSAFAPASTSDASAFQRGNKEKKFVYSHPKLKKLEEVILEHFKSWNAKATTEKKCHESRVMIFSSFRDSVEEIAEMLLQHRPVIRVMTFVGHASGKNTKGFTQKEQLQVVRQFRDGGYNTLVSTCVGEEGLDIGEVDLIICFDAQKSPIRLIQRMGRTGRKRQGRIVVILAEGREERTYNQSQSNKKNIYKAISGNRQVLRLYQGSPRMVPDKINPELHKMYITHGVYEPEKARSVQRRPFSSRGGIKASKSNKDGLLSEEEFNLWSRLYRLGDSDQVKGVALPQSHFPSLQEDRVIQDPTTRIHQLSLSEWSLWQDRPLPTHQVDHSDRCHHFISIMKMIEGMRHEEGECSYELKIRPFLQMEDVCSKYHAPRNGYNNVASVASSAHQKSSFRPSVDAGGSLTVIESEEEHADTVKQRDSKWTKITSLREKPCRAGRKGQTCEHSEGEGEDGDAGSSDADGQSPAEADSQVDPPSGERMADVGGISILGAVTEEDNHPGTLQMECQVTNKSCARYSLDSGYSSFSDEKSVSSNLFLPLEEELFTDRAAEQFYNCRPMTEDVLANVERFLSRSPPSLSGLSDLVYDVTQGCEFDNASCSPYPEHEHSPRPVSPASHSAGNSQQNLESNSAKRISHPTEKYCLPGTTHNKVSDRPSFCESDSEGHNIKYQNSGSNSCAQIQADLENNFVDKNSHDDSEPPVLFTDEDESLLLFEDDFKNIEDGPEELNGASLPPFNSISQPLRVSGKTLTSEMPPVSHFLISDELLLDDDSEPEDQIVCGAKSWKCQEGVEDGQEELRTDGQTFDCSVDLFSVTFDLGFRCSSGSDDEMLAGASDRTRTLGAADVSGRHSDKEIKDAGGASGPLGRAISPIPTETAQWSPWAQNKEYASFHVASSSPVKQRVRSTPLSKSHASSKTGAHMLKTLDSTKEKAGGQGFKMALNPRLGHLGFSVEETKSSDQVFVHQSPRRTEVEHLTSESEDDVFLRKTKKPKRNVLKSPEDQKNNEVDSPIHAVKKPRVLRSELASSDDESENFGRTCPRLEHFKGRNRNIRKGSAAQKNRSQVKTMARRFLDDEAEVSGEDVDCVSADEEDESENEQDSSLLDFVNDRTQLSQAINDSEMRAIYMKSVRSPLMSTKYRMVREKRPNMNIFSQIPEQDENYLEDSFCVDEEESCKSQSSEEEISVDFNLTKDSFTDEDIRYKTRYAVKIKQMNKKQNYTRPRKKLSRIILPDDDSSEEENIPKDREHSVAGGHAAAEHTQQGQLWASGPSGSSVPPQVLSDPSWNQSSRQRLQVQPSITDAVPRTLNVKAQSHNKIKSASPPCTGVESRKEYGNHPVQLKADSQEHSDTSAAPCSTSLLHVAEGHTAPRHLQEGNRACILVDSREITTGLEVISSLRTVHGLQVEICPLNGCDYIVSSRMVVVRRSQSEMLSNTSKNKFIEQMQRLQSMFQRICVIVEKDREKAGDTSKKFRRTKCYDSLLTALVGAGIRILFSSGQEETADLLKELSLVEQRKNAGIHIPAVLNTSKLEALPFYLSIPGISYITALNMCHQFSSVKKMANSSPEEISTCAQVNHQKAEEIYKYIHYIFDMQMLPNDLNQERQKPDTCLTLGVAMKELS

FANCM

DEAD-box ATP-dependent RNA helicase FANCM

1344 amino acids

Involved in ordered homologous recombination (HR) events in somatic and meiotic cells (PubMed:22547783). Involved in the suppression of spontaneous HR events in somatic cells (PubMed:22547783, PubMed:24635147). Has an opposite function to the DNA binding cofactor MHF1 which promotes spontaneous HR. Functions in replicative repair independently of MHF1 and in a parallel pathway to the endonuclease MUS81 (PubMed:24635147). Acts in the same pathway as the two DNA-binding cofactors MHF1 and MHF2 to restrain class II meiotic crossover (CO), and acts exclusively with MHF1 and MHF2 during meiosis to repair DNA interstrand cross-links (ICLs) (PubMed:24635147, PubMed:25038251). This common pathway is in parallel to the pathway that involves the RECQ4A helicase (PubMed:24635147). Seems to be involved in the stabilization of recombination intermediates (PubMed:22860689, PubMed:22723424). Involved in DNA double-strand break (DSB) repair during meiosis. Required for synthesis-dependent strand annealing (SDSA) and to a lesser extent for single-strand annealing (SSA) (PubMed:22860689, PubMed:26161528). May processes meiotic DSB repair intermediates, possibly D-loops, driving them toward noncrossover (NCO) resolution (PubMed:22723424, PubMed:26161528).

Belongs to the DEAD box helicase family. DEAH subfamily. FANCM sub-subfamily.

150.19 kDa

MGSRVPIETIEEDGEFDWEAAVKEIDLACLKTTNASSSSSSHFTPLANPPITANLTKPPAKRQSTLDKFIGRTEHKPENHQVVSECGVNDNDNSPLVGIDPEAAKTWIYPVNGSVPLRDYQFAITKTALFSNTLVALPTGLGKTLIAAVVMYNYFRWFPQGKIVFAAPSRPLVMQQIEACHNIVGIPQEWTIDLTGQTCPSKRAFLWKSKRVFFVTPQVLEKDIQSGTCLTNYLVCLVIDEAHRALGNYSYCVVVRELMAVPIQLRILALTATPGSKTQAIQGIIDNLQISTLEYRNESDHDVCPYVHDRKLEVIEVPLGQDADDVSKRLFHVIRPYAVRLKNFGVNLNRDIQTLSPHEVLMARDKFRQAPLPGLPHVNHGDVESCFAALITLYHIRKLLSSHGIRPAYEMLEEKLKEGPFARLMSKNEDIRMTKLLMQQRLSHGAPSPKLSKMLEILVDHFKVKDPKTSRVIIFSNFRGSVRDIMNALSNIGDMVKATEFIGQSSGKTLKGQSQKIQQAVLEKFRAGGFNVIVATSIGEEGLDIMEVDLVICFDANVSPLRMIQRMGRTGRKNNGRVVVLACEGSEKNSYMRKQASGRAIKKHMRNGGTNSFNFHPSPRMIPHVYKPEVQHVEFSIKQFVPRGKKLQEEYATETPAFQKKLTPAETHMLAKYYNNPDEEKLRVSLIAFPHFQTLPSKVHKVMHSRQTGMLIDAMQHLQEPTFSEQSKSFFTEFRAPLGEREELDTGLRVTNDPKDLHSVRDLEVNTSQRKAKQVESPTSTLETTEKDYEESSPTHRYLFSSECASVDTLGNVFVMPVPLLFFPNVLESDNTPLPKTEKQHSCRNTSHIDLVPVDTSEKHRQDNISCKLKERFSPDGASETLETHSLVKRNSTRVGEDDVANSVGEIVLSSDEDDCEGLELSPRLTNFIKSGIVPESPVYDQGEANREEDLEFPQLSSPMRFSNELAGESSFPERKVQHKCNDYNIVSTTTELRTPQKEVGLANGTECLAVSPIPEDWRTPLANLTNTNSSARKDWRVSSGEKLETLRQPRKLKRLRRLGDCSSAVKENYPGITEADHIRSRSRGKKHIRGKKKMIMDDDVQVFIDEEAEVSSGAEMSADENEDVTGDSFEDSFIDDGTMPTANTQAESGKVDMMAVYRRSLLSQSPLPARFRDLAASSLSPYSAGPLTRINESRSDSDKSLSSLRTPKTTNSESNQDAMMIGNLSVVQISSDSRKRKFSLCNSANAPVINLESKFAAHAQATEKESHEGVRSNAGALEYNDDDDDAFFATLDFDAMEAQATLLLSKQRSEAKEKEDATVIPNPGMQRSDGMEKDAPSFDLGLW