ID A0AA88WKA9_9ASTE Unreviewed; 2245 AA.
AC A0AA88WKA9;
DT 27-MAR-2024, integrated into UniProtKB/TrEMBL.
DT 27-MAR-2024, sequence version 1.
DT 28-JAN-2026, entry version 8.
DE RecName: Full=ATP-dependent helicase BRM {ECO:0008006|Google:ProtNLM};
GN ORFNames=RJ639_037998 {ECO:0000313|EMBL:KAK3028777.1};
OS Escallonia herrerae.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Escalloniales; Escalloniaceae; Escallonia.
OX NCBI_TaxID=1293975 {ECO:0000313|EMBL:KAK3028777.1, ECO:0000313|Proteomes:UP001188597};
RN [1] {ECO:0000313|EMBL:KAK3028777.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=UCBG64.0493 {ECO:0000313|EMBL:KAK3028777.1};
RC TISSUE=Leaf {ECO:0000313|EMBL:KAK3028777.1};
RA Chanderbali A., Dervinis C., Anghel I., Soltis D., Soltis P., Zapata F.;
RT "Draft genome assemblies for two species of Escallonia (Escalloniales).";
RL Submitted (DEC-2022) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KAK3028777.1}.
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DR EMBL; JAVXUP010000404; KAK3028777.1; -; Genomic_DNA.
DR Proteomes; UP001188597; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR GO; GO:0048731; P:system development; IEA:UniProtKB-ARBA.
DR CDD; cd18793; SF2_C_SNF; 1.
DR FunFam; 3.40.50.10810:FF:000017; ATP-dependent helicase BRM; 1.
DR FunFam; 3.40.50.300:FF:000762; ATP-dependent helicase BRM; 1.
DR FunFam; 1.20.920.10:FF:000038; Brahma1; 1.
DR Gene3D; 1.20.5.170; -; 1.
DR Gene3D; 1.20.920.10; Bromodomain-like; 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 InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR014978; Gln-Leu-Gln_QLQ.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C-like.
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; PTHR10799; SNF2/RAD54 HELICASE FAMILY; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF08880; QLQ; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00951; QLQ; 1.
DR SUPFAM; SSF47370; Bromodomain; 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.
DR PROSITE; PS51666; QLQ; 1.
PE 4: Predicted;
KW Bromodomain {ECO:0000256|ARBA:ARBA00023117};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP001188597};
KW Transcription {ECO:0000256|ARBA:ARBA00023015};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 480..516
FT /note="QLQ"
FT /evidence="ECO:0000259|PROSITE:PS51666"
FT DOMAIN 1015..1186
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1338..1515
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 213..232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 309..433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 445..478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 530..558
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1628..1852
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1865..1909
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2080..2145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2166..2245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..35
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..59
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..225
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 326..339
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 340..352
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 358..367
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 368..380
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..395
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 411..433
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 447..456
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 464..478
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 538..558
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1637..1648
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1667..1679
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1680..1689
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1745..1755
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1814..1826
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1827..1845
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1865..1880
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2118..2132
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2133..2145
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2200..2219
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2245 AA; 251651 MW; 1549FB91ECBDA4F2 CRC64;
MQSGGGAQGG GGGAAGHGRN TSASASPSSS SSAVSTPHLG LDPAQQQQQQ QQRQSFQQQL
LRRPEGNEAI LAYQAGGLHG VLGGGNFASN SASMQLPQQS RNFIDMAQQH GSLHIREEGQ
NRSQAFEQQM LNPVHQAYMQ YAFQAAQQKS ALGTQPQQKM KMGMVVPPGK DQDSRMGSLQ
IQDVISGQAV NPGQASLSKK PSEHFARGEK LMEEQQRVHD QRSDPKPPTM PTSLGQLMPS
NIVRPMQAPQ TQQNIQNTAN GQLTMAAQMQ AMQALALERN IDLSHPANAH LVAQLIPLMQ
SRVAAQQKAE INMSAQPSSA PMPKQHVTSP QVASESSPRG NSSSDVSGQS GSIKVRQTVP
SGPLATTSHP SPINNSNNSP LQQFSVQGRE NQLPQRQPAM FGNGMSPMQP PQSSGNLNQG
VDNPSLAKST LTGPDTLQMH VRPLNRSSPQ SAASSSEGAL GNALSLQGGP TAQLQQQHST
FTKQQLHVLK AQILAFRRLK KGDGTLPREL LQAIAPPPLE TQMQQMFRPT GTASQDRSAG
KNVEERTRHL ESSEKDPRAV TSTTLLNNLK QEAFTGDEKP SSSTVNMQGI TALLKEPASA
APPGNEELQT AAFSAKTEQE VERGIPKAPP ISVDRGKAVA PQVSVSDTVH GIKSVQASTA
AQPKDAGSSR KYHGPLFDFP FFTRKHDTFG SAMMVNNNNN LTLAYDVKDL LLEEGVEVLN
KKRTENIKKI GGLLAVNLER KRIRPDLVLR LQIQEKKLRL FDLQARLRDE VDQQQQDIMA
MPDRPYRKFV RLCERQRMEL NRQVQASQKA TRERQLKSIF QWRKKLLEAH WGIRDARTAR
NRGVAKYHER MLREFSKRKD DDRSKRMEAL KNNDVERYRE MLLEQQTSIS GDAAERYAVL
SSFLTQTEDY LHKLGSKITA AKNQQEVEEA ANTAAAAAQS QGLSEEEVRA AAACAGEEVM
IRNRFSEMNA PKDGSSVNKY YTLAHAVNER VLRQPSMLRA GTLRDYQLVG LQWMLSLYNN
KLNGILADEM GLGKTVQVMA LIAYLMEFKG NYGPHLIIVP NAVLVNWKSE LHTWLPSVSC
IYYVGGKEQR SKLFSQEVCA MKFNVLVTTY EFIMYDRSKL SRVDWKYIII DEAQRMKDRE
SVLARDLDRY RCQRPWKTSN WVMLSVEMND LKELWSLLNL LLPEVFDNRK AFHDWFSKPF
QKEGPTHNAE DDWLETEKKV IIIHRLHQIL EPFMLRRRVE DVEGSLPPKV SIILRCKMSA
IQGAIYDWIK ATGTLRVDPE DENRRVQKNP LYQAKTFKPL NNRCMELRKA CNHPLLNYPY
FNDFSKDFLV RSCGKLFVLD RILIKLQRTG HRVLLFSTMT KLLDILEEYL QWRRLVYRRI
DGTTSLEDRE SAIVDFNSPA TDCFIFLLSI RAAGRGLNLQ SADTVIIYDP DPNPKNEEQA
VARAHRIGQT REVKVIYMEA VVDKISSHQK EDEFRSGGTI DSEDDLAGKD RYMGSIEGLI
RNNIQQYKID MADEVINAGR FDQRTTHEER RMTLENLLHD EERYQETLHD VPSLQEVNRM
IARSEEEVEL YDQMDDEFDW AEEMTRYDEV PKWLRANTRE VNTTISNLSK KPSKNGLYAG
NIGVESNEVA SGLSPKTGRR RGRPKGKKFP NYSELDDENG EFSEASSEER NEYSGHEEGE
VGELEDEELS GAVEAPPVNK DQSEEEGPVS ADEYEYTRAS ESTKNNHILG AGSSGSSSES
RRMTQRVSPS ISSRKFASLS ALEARPSSLS SRLPDELEEG EIAMSGDSHM DLQQSGSWIH
DRDEGEDEQV LQPKIKRKRS IRVRPRHAAE KPEDKAEKPF LHRGDSSQLP FQVDHKYDPQ
YKMDAEHKLP GEPSSYKHDQ SNSSVKIRRN LPSRKVPNTP KVHASLKPSR VSIPAPTEDV
AEPFVESWDR KVMNVNGSSV DGSKMSIGTQ KKCKNVINKF QRRIDKEGHQ IVPLLTDLWK
RTENSAYMSG AGSSLLDIRK LDQRLDKFEY SGVMDLVTDV QLILKSAVQY FGFSHEVRTE
ARKVHDLFFD LLKIAFPDTD FREARNAVSF SGQVAASTSA PSSKQLLAGQ GKRKKQINEV
ETDASHLQKP RLPVPTGEDT RTRSHMPQRE TRLGSSSREL GQQDSPRLFA HPGELVICKK
KRKDREKVAV AGRSPVSPSS MGRGIRSPVP GSIPRETRQS HQVAQQLGVA NQPAQQANGV
SGAIGWANPV KRMRTDAGKR RPSHL
//
