FBH1_CHICK
ID FBH1_CHICK Reviewed; 1012 AA.
AC F1ND48; A1YKW0;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2013, sequence version 2.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=F-box DNA helicase 1 {ECO:0000303|PubMed:17283053};
DE EC=3.6.4.12 {ECO:0000250|UniProtKB:Q8NFZ0};
DE AltName: Full=F-box only protein 18;
GN Name=FBH1 {ECO:0000303|PubMed:17283053}; Synonyms=FBX18, FBXO18;
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 [MRNA], AND FUNCTION.
RX PubMed=17283053; DOI=10.1128/mcb.02043-06;
RA Kohzaki M., Hatanaka A., Sonoda E., Yamazoe M., Kikuchi K., Vu Trung N.,
RA Szuts D., Sale J.E., Shinagawa H., Watanabe M., Takeda S.;
RT "Cooperative roles of vertebrate Fbh1 and Blm DNA helicases in avoidance of
RT crossovers during recombination initiated by replication fork collapse.";
RL Mol. Cell. Biol. 27:2812-2820(2007).
RN [2]
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).
CC -!- FUNCTION: 3'-5' DNA helicase and substrate-recognition component of the
CC SCF(FBH1) E3 ubiquitin ligase complex that plays a key role in response
CC to stalled/damaged replication forks (By similarity). Involved in
CC genome maintenance by acting as an anti-recombinogenic helicase and
CC preventing extensive strand exchange during homologous recombination:
CC promotes RAD51 filament dissolution from stalled forks, thereby
CC inhibiting homologous recombination and preventing excessive
CC recombination (PubMed:17283053). Also promotes cell death and DNA
CC double-strand breakage in response to replication stress: promotes the
CC endonucleolytic DNA cleavage following prolonged replication stress via
CC its helicase activity, possibly to eliminate cells with excessive
CC replication stress. {ECO:0000250|UniProtKB:Q8NFZ0,
CC ECO:0000269|PubMed:17283053}.
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 Evidence={ECO:0000250|UniProtKB:Q8NFZ0};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:Q8NFZ0}.
CC -!- SUBUNIT: Part of the SCF (SKP1-CUL1-F-box) E3 ubiquitin-protein ligase
CC complex SCF(FBH1) (By similarity). {ECO:0000250|UniProtKB:Q8NFZ0}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8NFZ0}.
CC Chromosome {ECO:0000250|UniProtKB:Q8NFZ0}. Note=Accumulates at sites of
CC DNA damage or replication stress. Localizes to the nucleoplasm in
CC absence of DNA damage. {ECO:0000250|UniProtKB:Q8NFZ0}.
CC -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily.
CC {ECO:0000305}.
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DR EMBL; EF066526; ABM05617.1; -; mRNA.
DR EMBL; AADN03001147; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001073679.1; NM_001080210.1.
DR RefSeq; XP_015139126.1; XM_015283640.1.
DR AlphaFoldDB; F1ND48; -.
DR STRING; 9031.ENSGALP00000013249; -.
DR PaxDb; F1ND48; -.
DR GeneID; 416687; -.
DR KEGG; gga:416687; -.
DR CTD; 567995; -.
DR VEuPathDB; HostDB:geneid_416687; -.
DR eggNOG; KOG2108; Eukaryota.
DR HOGENOM; CLU_009740_0_0_1; -.
DR InParanoid; F1ND48; -.
DR OrthoDB; 245505at2759; -.
DR TreeFam; TF329020; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:F1ND48; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0000785; C:chromatin; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0019005; C:SCF ubiquitin ligase complex; ISS:UniProtKB.
DR GO; GO:0043138; F:3'-5' DNA helicase activity; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003678; F:DNA helicase activity; ISS:UniProtKB.
DR GO; GO:0003690; F:double-stranded DNA binding; ISS:UniProtKB.
DR GO; GO:0003697; F:single-stranded DNA binding; ISS:UniProtKB.
DR GO; GO:0008219; P:cell death; ISS:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IMP:UniProtKB.
DR GO; GO:2000042; P:negative regulation of double-strand break repair via homologous recombination; ISS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
DR GO; GO:0000725; P:recombinational repair; IBA:GO_Central.
DR GO; GO:0031297; P:replication fork processing; IMP:UniProtKB.
DR GO; GO:0048478; P:replication fork protection; ISS:UniProtKB.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR014017; DNA_helicase_UvrD-like_C.
DR InterPro; IPR000212; DNA_helicase_UvrD/REP.
DR InterPro; IPR036047; F-box-like_dom_sf.
DR InterPro; IPR001810; F-box_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR11070; PTHR11070; 1.
DR Pfam; PF12937; F-box-like; 1.
DR Pfam; PF13361; UvrD_C; 1.
DR SMART; SM00256; FBOX; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF81383; SSF81383; 1.
DR PROSITE; PS50181; FBOX; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Chromosome; DNA damage; DNA repair; DNA-binding; Helicase;
KW Hydrolase; Nucleotide-binding; Nucleus; Reference proteome;
KW Ubl conjugation pathway.
FT CHAIN 1..1012
FT /note="F-box DNA helicase 1"
FT /id="PRO_0000434112"
FT DOMAIN 185..234
FT /note="F-box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00080"
FT DOMAIN 427..692
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00560"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 448..455
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00560"
FT CONFLICT 112
FT /note="N -> D (in Ref. 1; ABM05617)"
FT /evidence="ECO:0000305"
FT CONFLICT 565
FT /note="V -> I (in Ref. 1; ABM05617)"
FT /evidence="ECO:0000305"
FT CONFLICT 951
FT /note="T -> A (in Ref. 1; ABM05617)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1012 AA; 114957 MW; 58A7B804176B3402 CRC64;
MHLTADDCEA LSRSTEGLSS LTQPLNQRRS RGDVNRGLQP THRTRTQPGA QGRQKNIMDY
FKVSQRQQAV AGRTKDISIK EEVLDPFFAE DDESSISSVM ETSGDSSSFL ENEYMGNSRK
RPLSSTAPGR LQIENDLWGE PEKKAVVVHP EHSQIKQELD DEIEIEPVPD SHYGLLGTRN
WEVPQGSIED LPDEVLRSIF AFLPVTDLYQ SLSLVCRRWR IIVGDPWFIP WKKLYHQYLV
KEDMALRRVE QVLQDFAITG QHKECILGLI RCVSTIPTSR NVDPSAVLQC LKGHHLFSRA
EVCITNKLPH LQSKTGPEYM WAIITAMVLF SDGVRDIQRL MACLQRPCSS LSIVDVTETL
YCIATLLYAM REKNINITNR IHYNIFYCLY LMENASVTAP QVVEEETPSS RCRQDFWSSS
LSEVKLTHEQ QRILNHKIER GQIVKIMAFA GTGKTSTLVK YAEKFADLSF LYVTFNKAVA
ERGRLVFPRN VTCKTFHSLA FGSVGKLYKE KGKLNFSKLS AYSVSFLIQN REGQSIFIRG
KTVSQTLENF FASSDEEICE EHTPVWFKNT HGERKLVTPE EKRINVEEAK EIWRNMKKLD
GDVERKYKIT CDGYLKLWQL SKPQLSGYDA IFVDEAQDCT PAIVDIVLSQ TCGVILVGDP
HQQIYSFRGA VNTLYTVPHT HIYYLTQSFR FGPEIAYVGA TILDVCKGIR NKTLVGGNQE
GDVRGSMEGK ITMLSRSNFT VFEDAAKLAG RERQIKIHII GGLVRFGLSK IYDIWKLSQP
ADEREKANLV INDSFIKRWE ENEGFIGLKD YATRVDDKEL EMKIRIVEKF KERIPELVQK
IESSHVLQEA MADYLIGTVH QAKGLEFDTV LIADDFVDVP CARDNNQRRP QFIIGMCPED
EWNLLYVAVT RAKKCLLMSQ SLEHLLALAG EHFLRVELMG EAVKTGVACS TQQCTQTLQS
GIRLVVKKLP LIHSNGSRDM GGYLCYSCVQ KRFGSMTPLA FLPALQEEPI VL
