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Database: UniProt
Entry: A0A0Q3M590_BRADI
LinkDB: A0A0Q3M590_BRADI
Original site: A0A0Q3M590_BRADI 
ID   A0A0Q3M590_BRADI        Unreviewed;      1009 AA.
AC   A0A0Q3M590;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   RecName: Full=SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 3-like 2 {ECO:0008006|Google:ProtNLM};
GN   Name=100838307 {ECO:0000313|EnsemblPlants:KQJ99685};
GN   ORFNames=BRADI_3g44690v3 {ECO:0000313|EMBL:KQJ99685.1};
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:KQJ99685.1};
RN   [1] {ECO:0000313|EMBL:KQJ99685.1, ECO:0000313|EnsemblPlants:KQJ99685}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bd21 {ECO:0000313|EMBL:KQJ99685.1,
RC   ECO:0000313|EnsemblPlants:KQJ99685};
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:KQJ99685.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Bd21 {ECO:0000313|EMBL:KQJ99685.1};
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:KQJ99685}
RP   IDENTIFICATION.
RC   STRAIN=cv. Bd21 {ECO:0000313|EnsemblPlants:KQJ99685};
RG   EnsemblPlants;
RL   Submitted (AUG-2018) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. RAD16 subfamily.
CC       {ECO:0000256|ARBA:ARBA00008438}.
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DR   EMBL; CM000882; KQJ99685.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0Q3M590; -.
DR   EnsemblPlants; KQJ99685; KQJ99685; BRADI_3g44690v3.
DR   Gramene; KQJ99685; KQJ99685; BRADI_3g44690v3.
DR   Proteomes; UP000008810; Chromosome 3.
DR   ExpressionAtlas; A0A0Q3M590; baseline.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR   GO; GO:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IEA:InterPro.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd18008; DEXDc_SHPRH-like; 1.
DR   CDD; cd18793; SF2_C_SNF; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR014905; HIRAN.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR038718; SNF2-like_sf.
DR   InterPro; IPR049730; SNF2/RAD54-like_C.
DR   InterPro; IPR000330; SNF2_N.
DR   InterPro; IPR018957; Znf_C3HC4_RING-type.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR45626:SF45; DNA REPAIR PROTEIN RAD5A; 1.
DR   PANTHER; PTHR45626; TRANSCRIPTION TERMINATION FACTOR 2-RELATED; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF08797; HIRAN; 1.
DR   Pfam; PF00176; SNF2-rel_dom; 1.
DR   Pfam; PF00097; zf-C3HC4; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00910; HIRAN; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008810};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          387..603
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          774..814
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          847..1004
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          46..104
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        49..93
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1009 AA;  111400 MW;  45B9C5544817D675 CRC64;
     MGKEDQVATV RAVLGEGTPE MDIIRALHMA GDDPTKAINI LLDFHHKLPA PPLPSPSPSQ
     SPPPVKPTNP PVESIPPPKT PSQSKPAADK PRPNPAPTGG GEHWWLVGSA EMAGLSTCKG
     RRIAAGDPVT FSFPNSAAAA APGKGRPGRL ALASCTSEIM RFSTPHNGEV GRIPNEWARC
     LLPLLKEGKI KVEGQCKSAP EVLSIMDTVL LCASVYINSS MFRDQKQSLP KAARVATDDS
     TFHPLPALFK VIGLAPFKKA AFTPEDLYSR KRPIERKSST GLPATKLTSE KLRLSCGGNE
     DDPGEGAVSD SDLDDIIGIS DSSALECDLR PYQKQALHWM LQLEKGSSSQ DAATTLHPCW
     EAYKLEDKRE LVLYVNVFSG DATTEFPSTL QLARGGILAD AMGLGKTIMT ISLLLSDSSK
     GLITTHHSTQ ISREASGLGE IHIKSQNPVK NLASPFSFSK LKKLKTPLVG GGNLIICPMT
     LLSQWKAEIE AHTKPNTMNI YVHYGQSRPK EASFIGQNDI VLTTYGVVAS EFSTESSTEN
     GGLYSVHWFR VVLDEAHMIK SSKSLISQAA AALTADRRWC LTGTPIQNNL EDIYSLFRFL
     RVEPWRNWAL WYKLVQKPFE EGDERGLKLV QTILKRVMLR RTKNSTDKEG RPILTLPPAT
     IEVKYCDLSE PEKDFYEALF RRSKVKFDQF VEQGKVLHNY ASILELLLRL RQCCDHPFLV
     MSRGDTQEYA DLNKLAKRFL HGGNSVVNGN SSSLPSKAYI EEVVQELQKG EGECPICLEA
     FEDAVLTPCA HRLCRECILS SWQSTAAGLC PVCRKSMSKQ DLITAPTDSR FQVDVEKNWI
     ESSKISFLLQ ELESLRSSGA KSIVFSQWTA FLDLLQIPLS RHGISFARLD GTLNLQQREK
     VIKEFSEDKS ILVLLMSLKA GGVGINLTAA SNAFVMDPWW NPAVEEQAVM RIHRIGQTKS
     VSIKRFIVKG TVEERMEAVQ ARKQRMISGA LTDQEVRTAR IEELKMLFS
//
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