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Database: UniProt
Entry: A0A371EJU5_MUCPR
LinkDB: A0A371EJU5_MUCPR
Original site: A0A371EJU5_MUCPR 
ID   A0A371EJU5_MUCPR        Unreviewed;      1323 AA.
AC   A0A371EJU5;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=ATP-dependent helicase BRM {ECO:0000313|EMBL:RDX66322.1};
DE   Flags: Fragment;
GN   Name=BRM {ECO:0000313|EMBL:RDX66322.1};
GN   ORFNames=CR513_54922 {ECO:0000313|EMBL:RDX66322.1};
OS   Mucuna pruriens (Velvet bean) (Dolichos pruriens).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Mucuna.
OX   NCBI_TaxID=157652 {ECO:0000313|EMBL:RDX66322.1, ECO:0000313|Proteomes:UP000257109};
RN   [1] {ECO:0000313|EMBL:RDX66322.1, ECO:0000313|Proteomes:UP000257109}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Jos {ECO:0000313|Proteomes:UP000257109};
RC   TISSUE=Seed {ECO:0000313|EMBL:RDX66322.1};
RA   Nnadi N.E., Vos R., Hasami M.H., Devisetty U.K., Aguiy J.C.;
RT   "Draft genome of Mucuna pruriens seed.";
RL   Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
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:RDX66322.1}.
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DR   EMBL; QJKJ01013489; RDX66322.1; -; Genomic_DNA.
DR   STRING; 157652.A0A371EJU5; -.
DR   Proteomes; UP000257109; 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:0004386; F:helicase activity; IEA:UniProtKB-KW.
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   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; PTHR10799:SF978; ATP-DEPENDENT HELICASE BRM; 1.
DR   PANTHER; PTHR10799; SNF2/RAD54 HELICASE FAMILY; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00176; SNF2-rel_dom; 1.
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   Helicase {ECO:0000313|EMBL:RDX66322.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT   DOMAIN          81..259
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          413..590
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          701..746
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          778..826
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          847..886
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          891..910
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          928..1011
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1170..1323
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        782..826
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        858..879
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        891..906
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        936..950
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        951..981
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        997..1011
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1197..1211
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1241..1255
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1262..1276
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1289..1303
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:RDX66322.1"
SQ   SEQUENCE   1323 AA;  149892 MW;  A902F56AE6813E80 CRC64;
     MKYPVAWGLS EEEVRAAAAC AGEEVMIRNR FMEMNAPRDS SSVSKYYHLA HAVSEKVVSQ
     PSMLRAGTLR DYQLVGLQWM LSLYNNKLNG ILADEMGLGK TVQVMALIAY LMEFKGNYGP
     HLIIVPNAVM VNWKVSFQLF HFTDIFSSEL HTWLPSVSCI FYAGGKDYRS KLYSQEILAM
     KFNVLVTTYE FIMYDRSRLS KIDWKYIIID EAQRMKDRDS VLARDLDRYR CQRRLLLTGT
     PLQNDLKELW SLLNLLLPEV FDNKKAFNDW FSKPFQKEVS TQNTEDDWLE TEKKVIIIHR
     LHQILEPFML RRRVEDVEGS LPPKISVVLR CKMSAVQSAI YDWVKSTGTL RLDPEGENLK
     IQKNPLYQAK QYKTLNNRCM ELRKTCNHPY LNYPLLSELS TDLVVKSCGK LWILDRILIK
     LQRTGHRVLL FSTMTKLLDI LEDYLNWRRL VYRRIDGTTN LDDRESAIMD FNGPDSDCFI
     FLLSIRAAGR GLNLQSADTV VIYDPDPNPK NEEQAVARAH RIGQKREVKV IYMEAVVDKI
     SSHQKEDELR SGGSVDMEDE LVGKDRYIGS IESLIRNNIQ QYKIDMADEV INAGRFDQRT
     THEERRLTLE TLLHDEERYQ ETVHNVPSLQ EVNRMIARSE EEVELFDQMD EELDWPEDMM
     QHDEVPEWLR ANTREVNAAI AALSKRPSKN TLLGGSVAIE SSEVGSERRR GRPKGKKHPN
     YKELEDENGE YSEASSEDRN GYSAQEEGEI GEFEDDGYSG ADVNRLGEDG LTFEAGYEIP
     RSSESARNNH VVEEAGSSGS SSDSQRLTQT VSPSVSSQKF GSLSALDCRP NSISKRMADE
     LEEGEIAVSG DSHMDHQQSG SWIHDRDEGE DEQVLQKPKI KRKRSLRVRP RGLAVERHED
     KSGSEMISLQ RGESSLLADY KYQMQTRIDP ESKPFGDSSA SKHDKNESSL KNKQNLPSRK
     VANTSKLQGS PKSNRLNCTS APSEDGAEHP KESWERKSLN PNGSSVHGTK MTEIIQRGCK
     NVISKLQRRI DKEGYQIVPL LTDLWKRIEN SGYAGGSGNN LLDLRKIDQR IDRMDYSGVM
     ELVFDVQFML RGAMNFYGYS YEVRFLIRVM YKLMEAYTDL YLENLLVRSE ARKVHDLFFD
     ILKIAFPDTD FGEVRGALSL SSQNPANVAA STRQVTVGSG KRHRATNDVE TDPCPLQKPP
     QSGSASNGES GRFKGKDSRG GSGGGGSGRE QPLTHPGQLV VCKKKRNDRE KSLGKGRSGS
     SAAPVSPPSA IRSSGSTPKD AKLPLPHQGW GTQPSQHSNG SLGWANPVKR LRTDSGKRRP
     SHM
//
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