ID A0A137QEN3_9AGAR Unreviewed; 1483 AA.
AC A0A137QEN3;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Putative SWI/SNF-like matrix-associated actin-dependent regulator {ECO:0000313|EMBL:KXN85676.1};
GN ORFNames=AN958_10859 {ECO:0000313|EMBL:KXN85676.1};
OS Leucoagaricus sp. SymC.cos.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Agaricaceae; Leucoagaricus.
OX NCBI_TaxID=1714833 {ECO:0000313|EMBL:KXN85676.1, ECO:0000313|Proteomes:UP000070249};
RN [1] {ECO:0000313|EMBL:KXN85676.1, ECO:0000313|Proteomes:UP000070249}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SymC.cos {ECO:0000313|EMBL:KXN85676.1,
RC ECO:0000313|Proteomes:UP000070249};
RA Hu H.;
RT "Leucoagaricus sp. SymC.cos WGS genome.";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KQ962440; KXN85676.1; -; Genomic_DNA.
DR STRING; 1714833.A0A137QEN3; -.
DR OrthoDB; 200191at2759; -.
DR Proteomes; UP000070249; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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; 2.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 2.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
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 PANTHER; PTHR45626:SF51; SINGLE-STRANDED DNA-DEPENDENT ATPASE (EUROFUNG); 1.
DR PANTHER; PTHR45626; TRANSCRIPTION TERMINATION FACTOR 2-RELATED; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 2.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000070249}.
FT DOMAIN 480..853
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1325..1483
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 542..567
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 621..668
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 714..786
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1033..1073
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1128..1152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..50
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..92
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..114
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..153
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 621..663
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1130..1152
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1483 AA; 163146 MW; A5994B87872ECC5D CRC64;
MAATAGSGPP ISSLGIHSRN NPIDLTQDDD EPGVPQWNSH RSKRAREDSV YDNISTGPCS
SPPPFHPPMN STAHNSSPHS FSIPNSDHFF LRPQSSAPPL LPLSSPPATP YRPPFAGSNL
PSVMNPYPQP HPQFSQSLPS LAPPPPRDFH LPPPFPFVLN QRQSLPPNPT PTPGVGPQVI
DLTDSPSPPP AAVQNVPPGL SPVNPNDPPK TPVCIGQLTV NALILYPINY LMSHDPSTEY
EWAAVRLQYE HDPHRMGNPD TIHIRTPSER SPTGEVIPGE NFAVVEQKVA TTLGGMLGKG
LIRLEAKIRR GKPNLPVMQL QLLVYTPKGN IMVVGNYLQQ CNLLLDHPIP PFDHDCRLAQ
YPYYNPHNPP PGGHSRPLML NNRLYTPSAT IGKTQDVQRT QVDELFRNLK DGVELSETES
HPDVATKLYP HQKKALTFLL DREREKPIIE GHFSTLWRTH IDSMSQQKRW VNIVTEEEAA
SEPKEARGSI LADDMGLGKT ITCVSLIAAT LQSAKAFAAQ PLEQLQLPPK KSQHPNASHF
AGAVWGMPES PAPTDSKSKK AERDQERLDA EYVRACRIKA RSRATLIICP LSTVANWEDQ
FREHWRGEVT VVGGSGNCVN STATSTASSS STAASTNGAN TPDSSQGDST TASSSSPNGT
AAKSEKSYRV RDGTPLRVYI YHGNARRPDP AFLTDFDAVI TTYATLASEF SKQNRTAQAA
NEDGEDTAGG GSSDGGISGS GDRWRGGGDP ELEIVEVQTS GMSLEANPKP KKTGTKRKKP
MTTVSSTEVA SPLQSIHWFR VVLDEAHSIK EIQTVGCRAS CDLIADRRLC LTGTPVQNKL
DDMFALIKFL RLTPFDDKNV WTKHISAPAK FGQREGIIRL RTIMDCITLR RTKETKSQDG
RRILALPPRE DTLVRLELSK EEQEIYHQYF SESKAEFTDL SNKNQVMKNY VGILQKLLRL
RQICDHKDLI EVKSATDSVV SYEEIVAAIA KEGINPSRAS AIFTLLREAT TTQCTECGGE
LCAIAEGANG DAGGLGTDSA ADGPPPNKRG RKSKGQTSSR APTRASSPSG GPRPILTRCQ
HLFCIECYRS SICPGWPDVP STLVMPCSAC QTELQPMDVV EIKPDMIAEG AGGEGKDGKD
GKKVKKKTKE ERMKKLEKRL QEIEARLIQE QDCPMQQSQS QMQTQQTFNS KADIELGGQY
LSQTRSLFDS ELDIKHNVFK PELDIKPAEM SLPSLLSQPS SFYSGPSETQ DYDMRFEMDI
SSLGLPPPNI REQATAILQE EICERSTKIK ALIGRLMPFS TANPHSANYN PGVLDVQIVD
SDGNGSTDNV IKTVVFSQWT SMLDKIEDAL LIHKIRYDRL DGTMKREERS KALDALKYDP
SCEVLLVSLK AGGVGLNLTA AQRVILMDPC WNPAVENQAV DRIHRLGQTK PVLSIRFIIS
NSVEESMLKI QARKNRLADL TLGARNKSEL MEQRMEELKE IFK
//
