ID A0A0L9TUD0_PHAAN Unreviewed; 1988 AA.
AC A0A0L9TUD0;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Protein PHOTOPERIOD-INDEPENDENT EARLY FLOWERING 1 {ECO:0008006|Google:ProtNLM};
GN ORFNames=LR48_Vigan02g025600 {ECO:0000313|EMBL:KOM34106.1};
OS Phaseolus angularis (Azuki bean) (Vigna angularis).
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; Vigna.
OX NCBI_TaxID=3914 {ECO:0000313|EMBL:KOM34106.1, ECO:0000313|Proteomes:UP000053144};
RN [1] {ECO:0000313|Proteomes:UP000053144}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. Jingnong 6 {ECO:0000313|Proteomes:UP000053144};
RX PubMed=26460024; DOI=10.1073/pnas.1420949112;
RA Yang K., Tian Z., Chen C., Luo L., Zhao B., Wang Z., Yu L., Li Y., Sun Y.,
RA Li W., Chen Y., Li Y., Zhang Y., Ai D., Zhao J., Shang C., Ma Y., Wu B.,
RA Wang M., Gao L., Sun D., Zhang P., Guo F., Wang W., Li Y., Wang J.,
RA Varshney R.K., Wang J., Ling H.Q., Wan P.;
RT "Genome sequencing of adzuki bean (Vigna angularis) provides insight into
RT high starch and low fat accumulation and domestication.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:13213-13218(2015).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. SWR1 subfamily.
CC {ECO:0000256|ARBA:ARBA00009220}.
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DR EMBL; CM003372; KOM34106.1; -; Genomic_DNA.
DR STRING; 3914.A0A0L9TUD0; -.
DR EnsemblPlants; KOM34106; KOM34106; LR48_Vigan02g025600.
DR Gramene; KOM34106; KOM34106; LR48_Vigan02g025600.
DR OMA; VCWCSKS; -.
DR Proteomes; UP000053144; Chromosome 2.
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 CDD; cd18003; DEXQc_SRCAP; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.20.120.850; SWI2/SNF2 ATPases, N-terminal domain; 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; IPR009057; Homeobox-like_sf.
DR InterPro; IPR014012; HSA_dom.
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; PTHR45685:SF1; HELICASE SRCAP; 1.
DR PANTHER; PTHR45685; HELICASE SRCAP-RELATED; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07529; HSA; 1.
DR Pfam; PF13921; Myb_DNA-bind_6; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00573; HSA; 1.
DR SUPFAM; SSF46689; Homeodomain-like; 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; PS51204; HSA; 1.
PE 3: Inferred from homology;
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:UP000053144}.
FT DOMAIN 1..53
FT /note="HSA"
FT /evidence="ECO:0000259|PROSITE:PS51204"
FT DOMAIN 473..638
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1005..1155
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 115..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 148..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 209..394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 401..420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1411..1512
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1859..1908
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..174
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..243
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..259
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..289
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..313
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 314..357
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..394
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1411..1426
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1484..1511
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1859..1890
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1891..1908
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1988 AA; 226483 MW; 906526089A492797 CRC64;
MVWLSKDFES ERKWKLAQAK KVALRASKGM IDQATRGEKK MKEEEQRLRK VALNISKDVK
KFWTKIEKLV LYKHQMELDE KKKKALDKQL EFLLGQTERY STMLAENLVD AHKSGENNSA
EHHMSIQRKD AHGDVINEPK EADVVEYQSD AADNDDEYDV QSDDESEDDE QTIEQDEALI
TKEERQEELE ALQNEMNLPI EELLKRYAGE KGESMMKESS PEHSEDVEKI VGTTGDENGD
DHLSVSKNGT NNSSMVSGRR CDESDGDMAT PTKNLSQYEE GQSENLKEVP SETANEDFSY
DFTDEEDDET TLSEEEKLER VDAIDPKDEI ALLQKESDMP VEELLARYKR DPSDNEDGGY
ETDYASALSE DHSDSPVHED AEQKDSAIPM DEDIKSGEHL ATTQSQTEEH WESPHENLDQ
RESEHIIADA AAAARSAQPT GNTFSTTNVR TKFPFLLKYS LREYQHIGLD WLVTMYEKRL
NGILADEMGL GKTIMTISLL AHLACEKGIW GPHLIVVPTS VMLNWETEFL KWCPAFKILT
YFGSAKERKF KRQGWLKPNS FHICITTYRL VIQDSKVFKR KKWKYLILDE AHLIKNWKSQ
RWQTLLNFNS KRRILLTGTP LQNDLMELWS LMHFLMPHVF QSHQEFKDWF SNPISGMVEG
EEKINKEVVD RLHNVLRPFL LRRLKRDVEK QLPMKHEHVI YCRLSKRQRN LYEDFIASSE
TQATLASANF FGMISIIMQL RKVCNHPDLF EGRPIVSSFD ICGIDVQLSS SVCSMLLPSP
FSVVDLRGLG LLFTDLDYSM TAWESDEVGA IETPGTSIME RTDIDELEVI RPLNCQKRLQ
GTNIFEDIQR KIWEERLKQA KERATAIAWW NSLRCKKRPM YSTTLRNLVT LRHPVYDIHL
VKANPTSYMY STKLADIVLS PIERFQKMTD VVESFMFAIP AARAPSPVCW CSKSETNVFL
QPSYKQKCSE VLLPLLSPIR PAIVRRQVYF PDRRLIQFDC GKLQELANLL RKLKSEGHRA
LIFTQMTKML DILEAFINLY GYTYMRLDGS TQPEERQTLM QRFNTNPKYF LFILSTRSGG
VGINLVGADT VIFYDSDWNP AMDQQAQDRC HRIGQTREVH IYRLISESTI EENILKKANQ
KRALDNLVIQ SGSYNTEFFK KLDPMELFSG HRTLSIKNML KEKNQNNGEV SVTNADVEAA
LKCVEDEADY MALKKVELEE AVDNQEFTEE AIGRLEEDEY VNEDDETAEL GESVSNLNKE
NALVLNGSDQ KEDRPPNSVV VKEDDADVLA DVKQMAAAAA AAGQAISAFE NELRPIDRYA
IRFLELWDPI IDKTALESEV RIEDTEWELD RIEKYKEEME AEIDEDEEPL VYESWDADFA
TMAYRQQVEA LAQHQLMEEL EYEARLKEAE EEACDSKKTT PGDLKPKPKK KPKKAKFKSL
KKGSLTSGLK PVKEESQAEP MNIDDEDITG LEFVSPNSSM QKKRKSKATT DGEEKRLKKS
KKSKRDPPDI YASDLESNAL VVQYEHAESK TSESLVDLEQ KTAGRGKMGG KISITPMPVK
RIWTIKPEKM RKGNHWSKDC IPSADFWLAQ EDAILCAVVH EYGPNWSLVS DILNSMTAGG
SYRGRYRHPV HCCERFRELF QKNVLSMDNA NNEKAITPGS GKALLKVTED NIRMLLDVAS
EQANRELLLQ KHFFALLSSA WKVASHVDRR QNPSPTCNGL YFDQGLFTSI GQPSQNSLKK
SSERVPFANL VQSKKLVAAA LDDSTTGQVN DRVILPNQGE GLPVSADRLD ITLEFPKEES
DVLALFPSVI NLSIHGTDPT PSLSKQTGED GFKIGLFMAE NRFREATRIC EEDVSGWASS
AFPTSDARSR PGSRIQSSGK QKSSISDSAK PSRSKSKRAS IDVSEMHHHQ ADSIVQSVPS
LKDLRFDLTS FTTDEIGLTA VDTCFPFDLN VESSWEMEGV GMIPHDYVTG LISDLDDCTT
FPEYTDIR
//
