FANCM_CHICK
ID FANCM_CHICK Reviewed; 2041 AA.
AC A0A1D5PRR9;
DT 15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2016, sequence version 1.
DT 03-AUG-2022, entry version 30.
DE RecName: Full=Fanconi anemia group M protein;
DE Short=Protein FACM;
DE EC=3.6.4.13 {ECO:0000250|UniProtKB:Q8IYD8};
DE AltName: Full=ATP-dependent RNA helicase FANCM;
DE AltName: Full=Fanconi anemia-associated polypeptide of 250 kDa;
DE Short=FAAP250;
DE AltName: Full=Protein Hef ortholog {ECO:0000303|PubMed:16116434};
GN Name=FANCM;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Red jungle fowl;
RX PubMed=15592404; DOI=10.1038/nature03154;
RA Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., Ponting C.P.,
RA Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B.,
RA Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C.,
RA Fulton R.S., Graves T.A., Kremitzki C., Layman D., Magrini V.,
RA McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O.,
RA Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W.,
RA Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D.,
RA Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K.,
RA Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L.,
RA Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B.,
RA Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M.,
RA Arakawa H., Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K.,
RA Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E.,
RA Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M.,
RA Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., Miller M.M.,
RA Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S.,
RA Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M.,
RA Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M.,
RA Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A.,
RA Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S.,
RA Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J.,
RA Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J.,
RA Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E.,
RA Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M.,
RA Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A.,
RA Mourelatos Z., Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M.,
RA Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O.,
RA Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., Betran E.,
RA Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S.,
RA Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E.,
RA Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R.,
RA Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R.,
RA Wilson R.K.;
RT "Sequence and comparative analysis of the chicken genome provide unique
RT perspectives on vertebrate evolution.";
RL Nature 432:695-716(2004).
RN [2]
RP FUNCTION, IDENTIFICATION IN THE FA COMPLEX, AND MUTAGENESIS OF ASP-207.
RX PubMed=16116434; DOI=10.1038/nsmb981;
RA Mosedale G., Niedzwiedz W., Alpi A., Perrina F., Pereira-Leal J.B.,
RA Johnson M., Langevin F., Pace P., Patel K.J.;
RT "The vertebrate Hef ortholog is a component of the Fanconi anemia tumor-
RT suppressor pathway.";
RL Nat. Struct. Mol. Biol. 12:763-771(2005).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RX PubMed=19465393; DOI=10.1093/nar/gkp365;
RA Rosado I.V., Niedzwiedz W., Alpi A.F., Patel K.J.;
RT "The Walker B motif in avian FANCM is required to limit sister chromatid
RT exchanges but is dispensable for DNA crosslink repair.";
RL Nucleic Acids Res. 37:4360-4370(2009).
CC -!- FUNCTION: DNA-dependent ATPase component of the Fanconi anemia (FA)
CC core complex (By similarity). Required for the normal activation of the
CC FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex
CC in response to DNA damage, cellular resistance to DNA cross-linking
CC drugs, and prevention of chromosomal breakage (PubMed:16116434,
CC PubMed:19465393). In complex with CENPS and CENPX, binds double-
CC stranded DNA (dsDNA), fork-structured DNA (fsDNA) and Holliday junction
CC substrates (By similarity). Its ATP-dependent DNA branch migration
CC activity can process branched DNA structures such as a movable
CC replication fork (By similarity). This activity is strongly stimulated
CC in the presence of CENPS and CENPX (By similarity). In complex with
CC FAAP24, efficiently binds to single-strand DNA (ssDNA), splayed-arm
CC DNA, and 3'-flap substrates (By similarity). In vitro, on its own,
CC strongly binds ssDNA oligomers and weakly fsDNA, but does not bind to
CC dsDNA (By similarity). {ECO:0000250|UniProtKB:Q8IYD8,
CC ECO:0000269|PubMed:16116434, ECO:0000269|PubMed:19465393}.
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:Q8IYD8};
CC -!- SUBUNIT: Component of the Fanconi anemia (FA) core complex. The FA core
CC complex associates with Bloom syndrome (BLM) complex. This supercomplex
CC between FA and BLM complexes has been called BRAFT.
CC {ECO:0000250|UniProtKB:Q8IYD8}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19465393}.
CC -!- PTM: Phosphorylated; hyperphosphorylated in response to genotoxic
CC stress. {ECO:0000269|PubMed:19465393}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC FANCM sub-subfamily. {ECO:0000305}.
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DR EMBL; AADN04000285; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_015132266.1; XM_015276780.1.
DR PDB; 7DA2; X-ray; 2.79 A; E=660-804.
DR PDBsum; 7DA2; -.
DR AlphaFoldDB; A0A1D5PRR9; -.
DR SMR; A0A1D5PRR9; -.
DR STRING; 9031.ENSGALP00000020332; -.
DR GeneID; 100857997; -.
DR KEGG; gga:100857997; -.
DR CTD; 57697; -.
DR VEuPathDB; HostDB:geneid_100857997; -.
DR eggNOG; KOG0354; Eukaryota.
DR eggNOG; KOG0442; Eukaryota.
DR OrthoDB; 989616at2759; -.
DR PRO; PR:A0A1D5PRR9; -.
DR Proteomes; UP000000539; Unplaced.
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:0004518; F:nuclease activity; IEA:InterPro.
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; IPR006166; ERCC4_domain.
DR InterPro; IPR031879; FANCM-MHF-bd.
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 InterPro; IPR011335; Restrct_endonuc-II-like.
DR InterPro; IPR010994; RuvA_2-like.
DR PANTHER; PTHR14025:SF20; PTHR14025:SF20; 1.
DR Pfam; PF02732; ERCC4; 1.
DR Pfam; PF16783; FANCM-MHF_bd; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF04851; ResIII; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00891; ERCC4; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF47781; SSF47781; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF52980; SSF52980; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; DNA damage; DNA repair; DNA-binding; Helicase;
KW Hydrolase; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..2041
FT /note="Fanconi anemia group M protein"
FT /id="PRO_0000439248"
FT DOMAIN 91..259
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 447..631
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 802..822
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 848..874
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1070..1124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1158..1208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1301..1403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1465..1491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1685..1740
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 207..210
FT /note="DEAH box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT COMPBIAS 1170..1184
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1348..1370
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1372..1403
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1465..1479
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1685..1699
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 104..111
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MUTAGEN 207
FT /note="D->A: Increased sister chromatid exchanges. No
FT effect on FANCD2 monoubiquitination, nor on cisplatin
FT sensitivity."
FT /evidence="ECO:0000269|PubMed:16116434"
FT HELIX 675..678
FT /evidence="ECO:0007829|PDB:7DA2"
FT STRAND 681..684
FT /evidence="ECO:0007829|PDB:7DA2"
FT HELIX 687..696
FT /evidence="ECO:0007829|PDB:7DA2"
FT STRAND 707..709
FT /evidence="ECO:0007829|PDB:7DA2"
FT STRAND 716..718
FT /evidence="ECO:0007829|PDB:7DA2"
FT TURN 727..730
FT /evidence="ECO:0007829|PDB:7DA2"
FT STRAND 731..734
FT /evidence="ECO:0007829|PDB:7DA2"
FT HELIX 741..745
FT /evidence="ECO:0007829|PDB:7DA2"
FT STRAND 751..753
FT /evidence="ECO:0007829|PDB:7DA2"
FT HELIX 757..773
FT /evidence="ECO:0007829|PDB:7DA2"
FT HELIX 776..785
FT /evidence="ECO:0007829|PDB:7DA2"
FT HELIX 786..788
FT /evidence="ECO:0007829|PDB:7DA2"
FT HELIX 791..793
FT /evidence="ECO:0007829|PDB:7DA2"
SQ SEQUENCE 2041 AA; 224006 MW; 691CC9D89A35486D CRC64;
MSGGRQRTLP EAWRRAAGPA LQAGRDADGN DDDDDELLAA AAAELDPDPN PNVDPNPGPG
PEAAAGGFCA AAGALWIYPT NRPERPYQLR MARAALFANT LLCLPTGLGK TFVAAVVMYN
FYRWFPSGKV LFLAPTKALV AQQMEACAQL MGIPGRDMAE MTGGTQALSR RELWASRRVF
FLTPQIMVND LSRGTCPAVE VKCLVVDEAH KALGNHAYCQ VVKELSRYTT QFRVLALTAT
PGSDTKAVQQ VVSNLLIAQI ELCSEDSPEI QPYSHERQVE KIVVPLGEEL GGIQRAYIHV
LETFAGRLIK LGVLARRDVP SLTKYQIILA RDQYRKNPSP QNVGMQPGII EGDFALCISL
YHGYELLQQM GVRSLFIYLC GIMDGSKGLT RTKNELGRNE DFMRLYQQLT DMFSDTCQTS
ANGNLHKSRT VSENKKEFIY SHPKLKKLEE IVIEHFKSRK MGCSDQTTSG GTCVDTRVMI
FSSFRDSVQE IAEMLSRFSP VVRVMTFVGH STGKSTKGFT QKEQLEVVKR FREGGYNTLV
STCVGEEGLD IGEVDLIICF DAQKSPIRLV QRMGRTGRQR QGRVVVILAE GREERTYNQS
QSNRRSIQKA ISGNKMLHFY QHSPRMIPEG INPELHRMFI TAEKYKPNDS GRLPKGRPSS
LHHKSALFSC VTDPKEMHCH ENWSLSPEEF EIWDRLYRLK ENDGVKEPIL PHTRFETLEN
LDKTSKPEEE AAHKLSLSEW SIWQSRPFPT SMVDHSDRCY HFISVMELIE VMRQEQGDCS
YELELQPHLR IEDIHVRRNK GHLSTTSSAF AQKTHSSKRD MARTKRPFVP DVNDNEREFF
SIFKTTNTKT PRTAPGLDLE EPELPTDTNG SEPCSARRLT LVASTDQGSP KEEEIEKVTF
DLNEFNDLCD DGESTVAHES AAVKDLRLLD KHCSSVGLNH TDLGYSSFTA EKSPASSDLF
YLPESHVDSF VLVSSSAELA GLEGAFSCVK GLLAHSPPPV SKLEGIEELL RHEETLCPLP
KVSCRSYSGQ LPHGDFPSSL AVDQSLLPAE SPELEVTIGL SAAVNTCVSK PASTPTAAGG
AEERPPGGGS FHSLLGKEGF TANHTDNPPN KHFVQGDEED SEMKRDVTID GEKSIHLFED
EHTYKVNDEM PSVDVEPLLR LGSGGHTARP SAGPASQQPP SGDSPRGDTA CGEGAARGEM
APGGAWGRGS AAEQALHNSE LCDYSQELFS VNFDLGFSIE ECEEEIFEGD TDAMNTPKLN
SASRSRADVQ LTANRKSLND GCRVQTPPKW DCKGLKGRNI STPLPLQSGH VRDTAVPGGT
AGGRTGRGSP GASPPSPATP TGRRVSSAEA TRRIRKKVFS TVREETPEVC PTDKVNPNSQ
RNSFGSSASD ALHTTGGRTE NLEGTNLHTS RVFPAEGTSS ESEEEIVFQR KNRRNNVLRS
PDVGSDSDFG SPVCAVRKRR HPLTVSDVSS DDGVDFHKNP NRGTRGCSAA GSKAQLRGVK
RQKVRSKVTC KNAARQFLDE EAELSQQDES CVSSDETEDT DKELSSSLAQ FLNDDAEVTQ
VLNDSEMRGV YLKSVRSPAL GSRYRMVHRE FNSTEIFSQI PEQDEAYAED SFCVAEGDEE
TCNKSESSEE EEVCVNFDLL NNESFGGGGG RYLTRRRKKL HGANMEQNCS APVQKKPSRI
IVLSDSSGEE TNVSNEKGTA AHCSRAGREN AELLTSMPSV SSVPHKKSAG DVSAHQSAES
KSGMLLGLKA SVSEVLDFHP GPRSGSGKEA LQAAAQHLQL ESSVKNSAGN APGATKASPA
LLDGDTALCV LVDSREISSG ADVISSLKAV HGLKVQVCSL GSGDYVVSNR MAVERKFQSE
LLSSVNRTKV TQRLQRLQGM FERVCVIVEK DRTRPGETSR FSQRTQHYDA TLAALLQAGI
RVLFSSCQEE TAVLLKELAL LEQRKNAAIC VPTEVEGHKQ EMLNFYLSLP NISYLAALNM
CHHFSSVRTM VNSSPSDIAA GARVSLQRAE ETYRYLRYGF DTQMLPESLC AKGKSNTATR
S
