ID A0A445FMR4_GLYSO Unreviewed; 1729 AA.
AC A0A445FMR4;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN ORFNames=D0Y65_047211 {ECO:0000313|EMBL:RZB50174.1};
OS Glycine soja (Wild soybean).
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; Glycine;
OC Glycine subgen. Soja.
OX NCBI_TaxID=3848 {ECO:0000313|EMBL:RZB50174.1, ECO:0000313|Proteomes:UP000289340};
RN [1] {ECO:0000313|EMBL:RZB50174.1, ECO:0000313|Proteomes:UP000289340}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. W05 {ECO:0000313|Proteomes:UP000289340};
RC TISSUE=Hypocotyl of etiolated seedlings {ECO:0000313|EMBL:RZB50174.1};
RA Xie M., Chung C.Y.L., Li M.-W., Wong F.-L., Chan T.-F., Lam H.-M.;
RT "A high-quality reference genome of wild soybean provides a powerful tool
RT to mine soybean genomes.";
RL Submitted (SEP-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC Evidence={ECO:0000256|ARBA:ARBA00001556};
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC {ECO:0000256|ARBA:ARBA00008792}.
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:RZB50174.1}.
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DR EMBL; QZWG01000018; RZB50174.1; -; Genomic_DNA.
DR SMR; A0A445FMR4; -.
DR OrthoDB; 443445at2759; -.
DR Proteomes; UP000289340; Chromosome 18.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd20335; BRcat_RBR; 1.
DR CDD; cd17917; DEXHc_RHA-like; 1.
DR CDD; cd22585; Rcat_RBR_DEAH12-like; 1.
DR CDD; cd18791; SF2_C_RHA; 1.
DR Gene3D; 1.20.120.1750; -; 1.
DR Gene3D; 1.10.10.2130; DEAH helicase family, winged-helix domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR042035; DEAH_win-hel_dom.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR007502; Helicase-assoc_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR002867; IBR_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR044066; TRIAD_supradom.
DR InterPro; IPR013087; Znf_C2H2_type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1.
DR PANTHER; PTHR18934:SF81; ATP-DEPENDENT RNA HELICASE DEAH11, CHLOROPLASTIC-RELATED; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF01485; IBR; 1.
DR Pfam; PF07717; OB_NTP_bind; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00847; HA2; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00647; IBR; 2.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF57850; RING/U-box; 3.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51873; TRIAD; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Helicase {ECO:0000313|EMBL:RZB50174.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000289340};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 277..441
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 471..637
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 1517..1725
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS51873"
FT DOMAIN 1521..1563
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 164..221
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1729 AA; 196090 MW; 4E8A03E2D0841D37 CRC64;
MKKSSYPNPT PRRHDFHRPP PPTHGCGWAP RPAYHRPYHQ WRPRFHPHAA RIDRPPEPYF
RVELRLGSSP LHRDDVEALI DECHSRHDTF TFYPVDDVAA VLSYRSWEQA RDAVVWFWEA
RLAEKHDFTP TLDSNVVVVK DDVDCRLRPV FARHVKGLTE GKEVKRWMEE SERLSKEISR
LSSSLSKPLR LGVHNELVEK KKGLVDEKNL VERRLKEFES AMQCLLKYLE GGVDVEGVTV
FRFDGGFDWK RIHCLIKREC RRLEDGLPIY AYRSDILQEI HYQQIMVLIG ETGSGKSTQL
VQFLADSGIG TDESIVCTQP RKIAAKSVAQ RVQEESIGCY EGQSIKCCST FSSSREFDSR
IAFMTDHCLL QHYMSDNNLS GVSCIIIDEA HERSLNTDLL LTLLKSLLCR RVEMRLIIMS
ATADAKQLSD YFFACGIFRV LGRSFPVDIK YVPSDYAGDS GSAVVASYVS DVVRMATEVH
KTEKEGTILA FLTSQIEVEW ACEKFQAPSA VALPLHGKLS SDEQFRVFQN YTGKRKVIFS
TNLAETSLTI PGVRYVIDSG LVKDSRFDPG SGMNVLKVCW ISQSSADQRA GRAGRTEPGV
CYRLYTEADY QSMDLNQEPE IRRVHLGVAV LRILALGVKD VQGFDFVDAP SPSSIDMAIR
NLIQLGAIEL NNDVHDLTSE GWCLVRMGIE PRLGKLILGC FKHGLGREGI ILAAVMANAS
SIFCRVGNEF DKQRSDCLKV QFCHCDGDLF TLLSVYKEWE ALPRERKNKW CWENSINAKS
MRRCQDTILE LETCLEREHD VVTPSYWRWD PCMPSNHDKN LKRVILFSLA ENVAMYSGCN
QLGYEVAQTG QHVQLHPSCS LLVFAQKPSW VVFGELLSIS NQYLVCVSAF DFQSLYDLCP
APLFDVSKME ERKLLMKTLS GLGCILLKRF CGKANCNLLA LVSRIRKACM DERIFIEVNV
DNNEIHLYAS SNDMDIALGL VNDVLEYERK WLRTECMDKF LYHGSGFSPP VALFGSGAEI
KHLELEKRSL SVDVCHPNIN EIDDKELLMF FEKNTSGCIC AVHKFTGNTR DEDRDKWGRI
TFMSPDIVRR AAELDGREFC GSSLKVVPSQ LGGDKTFSFP AVKARISWPR RLSRGFAIVK
CDIKDVDYIL RDFYNLAVGG RYVRCEVGKK SMDSVVINGL DKELSEAEIS DVLRTATTRR
ILDFFLVRGE AVGNPPCSAL EEALLKEIYP FLPKRNPHIS PCRVQVFAPE PKDAFMRALI
TFDGRLHLEA AKALEQIEGK VLPGCLSWQK IKCQQLFHSS LTFPTPVYRV IKEQLDEVLA
SFRNLKGLEC NLDRTFNGSH RVKITANATR TVAEVRRPLE ELLRGKTIEH DSLTPAVLQL
MLSRDGFSLK NSLQQETGTY ILFDRHNLNL RVFGSPNMVA LAQEKVIQSL LSLHEEKQLE
IHLRGRDLPP DLMKQMIKNF GPDLHGLKER VPGVDLTLNI RRHIIILHGS KELKPRVEEI
VFEIARSSHH LVERFGNGPS CPICLCEVED GYRLEGCGHL FCRMCLVEQF ESAIKNQGTF
PVCCTHRDCG DPILLTDLRS LLFGDKLEDL FRASLGAFVA TSGGTYRFCP SPDCPSIYRV
ADPGSAGEPF VCRACYSETC TRCHLEYHPY LSCERYKEFK EDPDSSLIEW CRGKEQVKCC
SACGYVIEKV DGCNHVECKC GKHVCWVCLE FFSTSNDCYD HLRTIHLTI
//
