ID FANCJ_CHICK Reviewed; 1252 AA.
AC Q3YK19;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 27-MAR-2024, entry version 106.
DE RecName: Full=Fanconi anemia group J protein homolog;
DE EC=3.6.4.12 {ECO:0000250|UniProtKB:Q9BX63};
GN Name=BRIP1; Synonyms=FANCJ;
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=16116421; DOI=10.1038/ng1627;
RA Bridge W.L., Vandenberg C.J., Franklin R.J., Hiom K.;
RT "The BRIP1 helicase functions independently of BRCA1 in the Fanconi anemia
RT pathway for DNA crosslink repair.";
RL Nat. Genet. 37:953-957(2005).
CC -!- FUNCTION: DNA-dependent helicase and 5' to 3' DNA helicase required for
CC the maintenance of chromosomal stability (PubMed:16116421). Involved in
CC the repair of DNA double-strand breaks by homologous recombination (By
CC similarity). Involved in the repair of abasic sites at replication
CC forks by promoting the degradation of DNA-protein cross-links: acts by
CC catalyzing unfolding of HMCES DNA-protein cross-link via its helicase
CC activity, exposing the underlying DNA and enabling cleavage of the DNA-
CC protein adduct by the SPRTN metalloprotease (By similarity).
CC {ECO:0000250|UniProtKB:A0A8J1M587, ECO:0000250|UniProtKB:Q9BX63,
CC ECO:0000269|PubMed:16116421}.
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:Q9BX63};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC Evidence={ECO:0000250|UniProtKB:Q9BX63};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000250|UniProtKB:Q9BX63};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250|UniProtKB:Q9BX63};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9BX63}.
CC -!- DOMAIN: 4Fe-4S iron-sulfur-binding is required for helicase activity.
CC {ECO:0000250|UniProtKB:Q9BX63}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC {ECO:0000305}.
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DR EMBL; DQ109581; AAZ66861.1; -; mRNA.
DR RefSeq; NP_001028230.1; NM_001033058.1.
DR RefSeq; XP_015151274.1; XM_015295788.1.
DR RefSeq; XP_015151275.1; XM_015295789.1.
DR AlphaFoldDB; Q3YK19; -.
DR SMR; Q3YK19; -.
DR STRING; 9031.ENSGALP00000038436; -.
DR PaxDb; 9031-ENSGALP00000038436; -.
DR Ensembl; ENSGALT00000122335; ENSGALP00000074625; ENSGALG00000005279.
DR Ensembl; ENSGALT00010070905.1; ENSGALP00010043596.1; ENSGALG00010029319.1.
DR Ensembl; ENSGALT00015055209; ENSGALP00015033309; ENSGALG00015022583.
DR GeneID; 417642; -.
DR KEGG; gga:417642; -.
DR CTD; 83990; -.
DR VEuPathDB; HostDB:geneid_417642; -.
DR eggNOG; KOG1132; Eukaryota.
DR GeneTree; ENSGT00950000182970; -.
DR HOGENOM; CLU_006515_1_0_1; -.
DR InParanoid; Q3YK19; -.
DR PhylomeDB; Q3YK19; -.
DR TreeFam; TF329449; -.
DR Reactome; R-GGA-351465; Fanconi Anemia Pathway in DNA repair.
DR Reactome; R-GGA-5685938; HDR through Single Strand Annealing (SSA).
DR Reactome; R-GGA-5685942; HDR through Homologous Recombination (HRR).
DR Reactome; R-GGA-5693568; Resolution of D-loop Structures through Holliday Junction Intermediates.
DR Reactome; R-GGA-5693579; Homologous DNA Pairing and Strand Exchange.
DR Reactome; R-GGA-5693607; Processing of DNA double-strand break ends.
DR Reactome; R-GGA-5693616; Presynaptic phase of homologous DNA pairing and strand exchange.
DR PRO; PR:Q3YK19; -.
DR Proteomes; UP000000539; Chromosome 19.
DR Bgee; ENSGALG00000005279; Expressed in spermatid and 13 other cell types or tissues.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0043139; F:5'-3' 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:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003678; F:DNA helicase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0006281; P:DNA repair; TAS:Reactome.
DR GO; GO:1990918; P:double-strand break repair involved in meiotic recombination; IBA:GO_Central.
DR GO; GO:0006289; P:nucleotide-excision repair; IBA:GO_Central.
DR GO; GO:0106300; P:protein-DNA covalent cross-linking repair; ISS:UniProtKB.
DR CDD; cd18788; SF2_C_XPD; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR InterPro; IPR006555; ATP-dep_Helicase_C.
DR InterPro; IPR045028; DinG/Rad3-like.
DR InterPro; IPR014013; Helic_SF1/SF2_ATP-bd_DinG/Rad3.
DR InterPro; IPR006554; Helicase-like_DEXD_c2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR010614; RAD3-like_helicase_DEAD.
DR InterPro; IPR013020; Rad3/Chl1-like.
DR NCBIfam; TIGR00604; rad3; 1.
DR PANTHER; PTHR11472; DNA REPAIR DEAD HELICASE RAD3/XP-D SUBFAMILY MEMBER; 1.
DR PANTHER; PTHR11472:SF47; FANCONI ANEMIA GROUP J PROTEIN; 1.
DR Pfam; PF06733; DEAD_2; 1.
DR Pfam; PF13307; Helicase_C_2; 1.
DR SMART; SM00488; DEXDc2; 1.
DR SMART; SM00491; HELICc2; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51193; HELICASE_ATP_BIND_2; 1.
PE 2: Evidence at transcript level;
KW 4Fe-4S; ATP-binding; DNA damage; DNA repair; Helicase; Hydrolase; Iron;
KW Iron-sulfur; Metal-binding; Nucleotide-binding; Nucleus;
KW Reference proteome.
FT CHAIN 1..1252
FT /note="Fanconi anemia group J protein homolog"
FT /id="PRO_0000055175"
FT DOMAIN 11..452
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT REGION 919..1008
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1212..1252
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 164..181
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 403..406
FT /note="DEAH box"
FT COMPBIAS 919..933
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 947..978
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 979..1008
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1214..1232
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1237..1252
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 191..198
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT BINDING 292
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:Q4JC68"
FT BINDING 308
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:Q4JC68"
FT BINDING 320
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:Q4JC68"
FT BINDING 360
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:Q4JC68"
SQ SEQUENCE 1252 AA; 140105 MW; E209A932316E7E29 CRC64;
MSSDVSQYTI GGVKIMFPCK AYPSQLAMMN AIVKGLNNRQ HCLLESPTGS GKSLALLCSA
LSWQQSLYEK SLLKSSCEKE DREPAASLPC RCVCHSRSES SEATAGASHG AACSNNYETG
GSVKHGDQLS DTECKENNTL ASKLSAKKRA SACGNECDDF QVERKRIRPL ETEQQVRKRH
CFSKEVQLVD ALEVYNQRKN GELIVHSEKS VKNTSPQTLF SSCTECSCSS GKETRKDSGN
TKKKANGDQT FIPKIFFGTR THKQIAQITR ELKRTAYSGV PMTILSSRDY TCIHPVVSSS
NSNRNELCVE LLEGKHGKSC LYYHGVHKLS EHYALQSAHN TYQAWDIEDL VSLGKKLRAC
PYFAARELMV GADIVFCPYN YLLDPQIRES MEINLKGQVV ILDEAHNIED SAREAVSYSV
TESQLNAARE ELDFMVNNNI RQKDHEQLRA MCCSLTNWLR ESSSQLVETG YETSCKVWSG
KEMLNHFHDM GITNISFPIL QKHLSAVLEK EEKISMFGKE ELVEIPIVSS ATQIVLKGLF
MVLLYLFKDN SRFADDYRVA LQQTYAWTND NQPDVSDTSA FFTKTKHKRN LRHKTVVHML
NFWCLNPAVA FSDLNDVRTV VLTSGTLSPM DSFSSELGVK FSIQLEANHV IRNSQVWVGT
IGTGPNGRKL CATFQHTETF EFQDEVGALL LSVCQKVGQG ILCFLPSYKL LDKLKDRWIH
TGLWRNLELV KTVIAEPQGG AKSDFDELLK IYYDAIKFKG EKDGALLIAV CRGKVSEGLD
FCDENARAVI TIGIPFPNVK DLQVELKRKY NDQHKTTRGL LPGSQWYEIQ AYRALNQALG
RCIRHRSDWG ALILVDDRFR NNPNKYITGL SKWIRQQVQH HENFGSALES LHAFAERNQK
GIDFSSQCSN EVFHVPLNSK EPSSASQQEA TIHLSPDVPV KSEEQSFVPE THLTTTINSI
NPGPSNQPGG QKVDVESCSH NGIQRRKHMD STPRRPANKT EKKSDRTNSD FMKEHCCFKP
LTSTPLPVAT NCVSTASSKQ RKNVNSASEL IGGVNQCQSS FTLEHKPSIP ESHLETTNFS
VKSTEAPVAE EHLDEQKLQI EPCSELPSVG GRPELSVLEI SAEDEDESLY FTPELYDDAE
SEEQEMRPLD PDENQIECGK PTVADDLFVI STSKTLSEPK EMINDDGRNT SLHGTMLSDI
SKNSTVNIEK MTNGEEAEQV ESQEVDTKKR KISLSRSRNK GVSPFLLDST ST
//
