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Database: UniProt
Entry: I1GU88_BRADI
LinkDB: I1GU88_BRADI
Original site: I1GU88_BRADI 
ID   I1GU88_BRADI            Unreviewed;      1267 AA.
AC   I1GU88;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KQK16145.1, ECO:0000313|EnsemblPlants:KQK16145};
GN   Name=100838876 {ECO:0000313|EnsemblPlants:KQK16145};
GN   ORFNames=BRADI_1g27027v3 {ECO:0000313|EMBL:KQK16145.1};
OS   Brachypodium distachyon (Purple false brome) (Trachynia distachya).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Stipodae; Brachypodieae; Brachypodium.
OX   NCBI_TaxID=15368 {ECO:0000313|EMBL:KQK16145.1};
RN   [1] {ECO:0000313|EMBL:KQK16145.1, ECO:0000313|EnsemblPlants:KQK16145}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bd21 {ECO:0000313|EMBL:KQK16145.1,
RC   ECO:0000313|EnsemblPlants:KQK16145};
RX   PubMed=20148030; DOI=10.1038/nature08747;
RG   International Brachypodium Initiative;
RT   "Genome sequencing and analysis of the model grass Brachypodium
RT   distachyon.";
RL   Nature 463:763-768(2010).
RN   [2] {ECO:0000313|EMBL:KQK16145.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Bd21 {ECO:0000313|EMBL:KQK16145.1};
RG   The International Brachypodium Initiative;
RA   Lucas S., Harmon-Smith M., Lail K., Tice H., Grimwood J., Bruce D.,
RA   Barry K., Shu S., Lindquist E., Wang M., Pitluck S., Vogel J.P.,
RA   Garvin D.F., Mockler T.C., Schmutz J., Rokhsar D., Bevan M.W.;
RT   "WGS assembly of Brachypodium distachyon.";
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EnsemblPlants:KQK16145}
RP   IDENTIFICATION.
RC   STRAIN=cv. Bd21 {ECO:0000313|EnsemblPlants:KQK16145};
RG   EnsemblPlants;
RL   Submitted (AUG-2018) to UniProtKB.
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:0000256|ARBA:ARBA00000600};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC         Evidence={ECO:0000256|ARBA:ARBA00000600};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the DNA2/NAM7 helicase family.
CC       {ECO:0000256|ARBA:ARBA00007913}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01341}.
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DR   EMBL; CM000880; KQK16145.1; -; Genomic_DNA.
DR   RefSeq; XP_003563076.1; XM_003563028.3.
DR   AlphaFoldDB; I1GU88; -.
DR   STRING; 15368.I1GU88; -.
DR   EnsemblPlants; KQK16145; KQK16145; BRADI_1g27027v3.
DR   GeneID; 100838876; -.
DR   Gramene; KQK16145; KQK16145; BRADI_1g27027v3.
DR   KEGG; bdi:100838876; -.
DR   eggNOG; KOG1802; Eukaryota.
DR   HOGENOM; CLU_001666_4_3_1; -.
DR   InParanoid; I1GU88; -.
DR   OMA; VRSNDNQ; -.
DR   OrthoDB; 170190at2759; -.
DR   Proteomes; UP000008810; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0003724; F:RNA helicase activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IBA:GO_Central.
DR   CDD; cd21407; 1B_UPF1-like; 1.
DR   CDD; cd18039; DEXXQc_UPF1; 1.
DR   CDD; cd18808; SF1_C_Upf1; 1.
DR   CDD; cd21400; ZBD_UPF1-like; 1.
DR   Gene3D; 2.40.30.230; -; 1.
DR   Gene3D; 6.10.140.1240; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR045055; DNA2/NAM7-like.
DR   InterPro; IPR041679; DNA2/NAM7-like_C.
DR   InterPro; IPR041677; DNA2/NAM7_AAA_11.
DR   InterPro; IPR006935; Helicase/UvrB_N.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR047187; SF1_C_Upf1.
DR   InterPro; IPR040812; UPF1_1B_dom.
DR   InterPro; IPR018999; UPF1_CH/ZBD.
DR   PANTHER; PTHR10887; DNA2/NAM7 HELICASE FAMILY; 1.
DR   PANTHER; PTHR10887:SF364; REGULATOR OF NONSENSE TRANSCRIPTS 1; 1.
DR   Pfam; PF13086; AAA_11; 1.
DR   Pfam; PF13087; AAA_12; 1.
DR   Pfam; PF04851; ResIII; 1.
DR   Pfam; PF18141; UPF1_1B_dom; 1.
DR   Pfam; PF09416; UPF1_Zn_bind; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51997; UPF1_CH_RICH; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW   ProRule:PRU01341}; Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008810};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU01341};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU01341}.
FT   DOMAIN          147..306
FT                   /note="Upf1"
FT                   /evidence="ECO:0000259|PROSITE:PS51997"
FT   DOMAIN          512..644
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   REGION          1..112
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          217..247
FT                   /note="C4"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01341"
FT   REGION          1218..1242
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        87..110
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1267 AA;  138294 MW;  9E3FC501A7B25F12 CRC64;
     MATQPPSSAA AADLYETASQ PDPSASAAGD AYTFLEFNTQ GDDFEYPDFP ELSQPARSAP
     PPATVTSSTS SSWPAPPPPP DASQDPDLVP QDSTPLASSS SPSPRSSASK ARASAAVADG
     LAAGVAALSF EEPPGAGAGE DGYDYGKGDF VEHACRYCGI HSPACVARCN VPSCRKWFCN
     SRGNTSGSHL VNHLVRAKHK EVCLHKDSPL GETILECYNC GCRNVFLLGF ISAKAENVVV
     LLCREPCLNV NALKDMNWDL SQWLPLIDDR CFLSWLVKVP SEQEQLRARQ ISAQQINKVE
     ELWKTNPDAS LEDLEKPGVD DEPQPVVLKY EDAYQYQNVF APLIKLEADY DKMMKESQSK
     DSVTVRWDIG LNKKRVAYFV FPKEDNELRL VPGDELRLRY SGGTSHPAWQ SVGHVIKLTA
     QEEVALELRA SQGVPVELSH GFSVDFVWKS TSFDRMQGAM KTFAVDETSV SGYIYHHLLG
     HEVEHQIIRN TLPKRFGAPG LPELNASQVL AVKSVLQKPV SLIQGPPGTG KTVTSAAIVY
     HMAKQGQGQV LVCAPSNVAV DQLAEKISST GLKVVRLCAK SREAVSSPVE HLTLHYQVRH
     LDTSEKSEMH KLQQLKDEQG ELSSSDEKKY KALKRATERE ILQSADVICC TCVGAGDPRL
     SNFRFRQVLI DESTQATEPE CLIPLVLGVK QVVLVGDHCQ LGPVIMCKKA ARAGLAQSLF
     ERLVILGVKP FRLQVQYRMH PCLSEFPSNC FYEGTLQNGV TVNERQSTGI DFPWPVPNRP
     MFFYVQMGVE EISASGTSYL NRTEAANVEK IVTTFLRSGV VPSQIGVITP YEGQRAYIVN
     YMSRNGSLRQ QLYKEIEVAS VDSFQGREKD YIILSCVRSN EHQGIGFLND PRRLNVALTR
     ARYGIVVLGN PKVLSKQPLW NSLLTHYKEH ECLVEGPLNN LKQSMVQFQK PKKIYNDRRL
     FLGGGQGVMH GSSFGTAGSV DKRSGRGKAH PFVPFGPPNG AHKPGVHPSY PLPRMPFPPF
     PGSPHSQPYA IPTRGSLHGP IGAVPAVPQP GNRNFGAPRA NTGPIGGHLA AHQQNSQQAM
     GNVGPAYNFT GLENPSSQPS GGGPMSQPGL MTQMPVQGLS QTFRDGFAIG GMSQDFFGDD
     FKSQGSHVAY NIADFSTQAS QGGYGVEYTQ GPQSGYPGNY LNQSAHPGYP HMGATNEIVS
     QDHMAHGSHG MFTQAGYNDP SQDESSQMHY GMGAPGHLQS QSMMNPMYSQ SYAHYNTQPQ
     SLQPPPQ
//
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