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FANCJ_CHICK
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   03-AUG-2022, entry version 98.
DE   RecName: Full=Fanconi anemia group J protein homolog;
DE            Short=Protein FACJ;
DE            EC=3.6.4.13 {ECO:0000250|UniProtKB:Q9BX63};
DE   AltName: Full=ATP-dependent RNA helicase BRIP1;
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 ATPase and 5' to 3' DNA helicase required for
CC       the maintenance of chromosomal stability. Acts late in the 'Fanconi
CC       anemia' pathway of DNA repair, after FANCD2 ubiquitination. Probably
CC       not involved in the repair of DNA double-strand breaks by homologous
CC       recombination. {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=3.6.4.13;
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; Evidence={ECO:0000250};
CC       Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
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; Q3YK19; -.
DR   Ensembl; ENSGALT00000039225; ENSGALP00000038436; ENSGALG00000005279.
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   OMA; CHSKNFT; -.
DR   OrthoDB; 186062at2759; -.
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   PRO; PR:Q3YK19; -.
DR   Proteomes; UP000000539; Chromosome 19.
DR   Bgee; ENSGALG00000005279; Expressed in spermatid and 13 other 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: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   Gene3D; 3.40.50.300; -; 3.
DR   InterPro; IPR006555; ATP-dep_Helicase_C.
DR   InterPro; IPR010614; DEAD_2.
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; IPR013020; Rad3/Chl1-like.
DR   PANTHER; PTHR11472; PTHR11472; 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; SSF52540; 2.
DR   TIGRFAMs; TIGR00604; rad3; 1.
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"
FT   BINDING         308
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         320
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
FT   BINDING         360
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250"
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
 
 
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