ID A0A0L9THA6_PHAAN Unreviewed; 1038 AA.
AC A0A0L9THA6;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Helicase ATP-binding domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=LR48_Vigan818s001500 {ECO:0000313|EMBL:KOM29817.1};
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:KOM29817.1, 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).
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DR EMBL; KQ258551; KOM29817.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L9THA6; -.
DR STRING; 3914.A0A0L9THA6; -.
DR EnsemblPlants; KOM29817; KOM29817; LR48_Vigan818s001500.
DR Gramene; KOM29817; KOM29817; LR48_Vigan818s001500.
DR OMA; MTCHLGD; -.
DR Proteomes; UP000053144; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
DR GO; GO:0006401; P:RNA catabolic process; IEA:InterPro.
DR CDD; cd18024; DEXHc_Mtr4-like; 1.
DR CDD; cd13154; KOW_Mtr4; 1.
DR CDD; cd18795; SF2_C_Ski2; 1.
DR Gene3D; 1.10.3380.30; -; 1.
DR Gene3D; 2.40.30.300; -; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR048392; MTR4-like_stalk.
DR InterPro; IPR025696; MTR4_beta-barrel.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR016438; SKI2-like.
DR InterPro; IPR012961; Ski2/MTR4_C.
DR PANTHER; PTHR12131; ATP-DEPENDENT RNA AND DNA HELICASE; 1.
DR PANTHER; PTHR12131:SF32; DEXH-BOX ATP-DEPENDENT RNA HELICASE DEXH10; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF08148; DSHCT; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF21408; MTR4-like_stalk; 1.
DR Pfam; PF13234; MTR4_beta-barrel; 2.
DR PIRSF; PIRSF005198; Antiviral_helicase_SKI2; 3.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM01142; DSHCT; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
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:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000053144}.
FT DOMAIN 87..243
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 318..519
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 291..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1038 AA; 116521 MW; F843391E22D2641B CRC64;
MENEKKESPS LGKRREPELP VTVPETASKP KRARSAERTC VHEVAVPSGY VSSKDSELNG
TLSNPLHKGP MAKSYPFTLD PFQQVSIACL ERNESVLVSA HTSAGKTAVA EYAIAMSFRD
RQRVIYTSPL KALSNQKYRE LSQEFTDVGL MTGDVTLSPN ATCLVMTTEI LRGMLYRGSE
VLKEVAWVIF DEIHYMKDRE RGVVWEESII FLPPAIKMVF LSATMSNATE FAEWICNIHK
QPCHVVYTDF RPTPLQHYAF PIGGSGLYLV VDENEQFRED NFLKLHDTFG KQNSAEGRRG
GKGGGRGGKG GNTSGGSDIY KIVKMIMERK FQPVIIFSFS RRECEQHAMS MSKLDFNTPE
EKETVEQVFR NAVLCLNEED RCLPAIELML PLLQRGIAVH HSGLLPVIKE LVELLFQEGL
VKALFATETF AMGLNMPAKT VVFTAVKKWD GDSHRYIGSG EYIQMSGRAG RRGKDERGIC
IIMIDEQMEM NNLKDMVLGK PAPLVSTFRL SYYSILNLMS RAEGQFTAEH ALPDIEKRVS
KLEQEVNLLD ASGEAEVSEY HKLKLEIAQL EKKMMTKIIR PEIILYFLVP GRLVKIREGG
TDCGWGVVFN VVKKPSGGGY IVDTLLHCSP CSTENNSRPK PCPPRPGEKG EMHVAEVSEY
HKLKLEIAQL EKKMMTKIIR PEIILYFLVP GRLVKIREGG TDWGWGVVVN VVKKPSGGGY
IVDTLLHCSP CSTENNSRPK PCPPRPGEKG EMHVVPVQLP LISTLGKLRV SIPSDLRPLE
ARQSVLLAVQ ELVNRFPGGL PKLNPVKRQD VDQIKCFERK AEVNHEIQQL RTKMRDSQLQ
KFREELKNRS RVLKKLGHID GDGVVQLKGR AACLVDTGDE LLVTELMFNG TFNDLDHHQV
AALASCFIPG DKSNEQIQLR TELARPLQQL QDSARRIAEI QHECKLDINV DEYVESTVRP
YLMDVIYSWS KGVNFADIIQ MTDIFEGSII RSARRLDEFL NQLRAAANAV GEADLEKKFA
AASESLRRGI MFANSLYL
//
