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Database: UniProt
Entry: G7IUG0_MEDTR
LinkDB: G7IUG0_MEDTR
Original site: G7IUG0_MEDTR 
ID   G7IUG0_MEDTR            Unreviewed;      1269 AA.
AC   G7IUG0;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 63.
DE   RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE            EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
GN   Name=11423262 {ECO:0000313|EnsemblPlants:AES67725};
GN   OrderedLocusNames=MTR_2g098440 {ECO:0000313|EMBL:AES67725.1};
GN   ORFNames=MtrunA17_Chr2g0329131 {ECO:0000313|EMBL:RHN76170.1};
OS   Medicago truncatula (Barrel medic) (Medicago tribuloides).
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; Hologalegina; IRL clade; Trifolieae; Medicago.
OX   NCBI_TaxID=3880 {ECO:0000313|EMBL:AES67725.1, ECO:0000313|Proteomes:UP000002051};
RN   [1] {ECO:0000313|EMBL:AES67725.1, ECO:0000313|Proteomes:UP000002051}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A17 {ECO:0000313|EMBL:AES67725.1}, and cv. Jemalong A17
RC   {ECO:0000313|EnsemblPlants:AES67725,
RC   ECO:0000313|Proteomes:UP000002051};
RX   PubMed=22089132; DOI=10.1038/nature10625;
RA   Young N.D., Debelle F., Oldroyd G.E., Geurts R., Cannon S.B., Udvardi M.K.,
RA   Benedito V.A., Mayer K.F., Gouzy J., Schoof H., Van de Peer Y., Proost S.,
RA   Cook D.R., Meyers B.C., Spannagl M., Cheung F., De Mita S.,
RA   Krishnakumar V., Gundlach H., Zhou S., Mudge J., Bharti A.K., Murray J.D.,
RA   Naoumkina M.A., Rosen B., Silverstein K.A., Tang H., Rombauts S.,
RA   Zhao P.X., Zhou P., Barbe V., Bardou P., Bechner M., Bellec A., Berger A.,
RA   Berges H., Bidwell S., Bisseling T., Choisne N., Couloux A., Denny R.,
RA   Deshpande S., Dai X., Doyle J.J., Dudez A.M., Farmer A.D., Fouteau S.,
RA   Franken C., Gibelin C., Gish J., Goldstein S., Gonzalez A.J., Green P.J.,
RA   Hallab A., Hartog M., Hua A., Humphray S.J., Jeong D.H., Jing Y.,
RA   Jocker A., Kenton S.M., Kim D.J., Klee K., Lai H., Lang C., Lin S.,
RA   Macmil S.L., Magdelenat G., Matthews L., McCorrison J., Monaghan E.L.,
RA   Mun J.H., Najar F.Z., Nicholson C., Noirot C., O'Bleness M., Paule C.R.,
RA   Poulain J., Prion F., Qin B., Qu C., Retzel E.F., Riddle C., Sallet E.,
RA   Samain S., Samson N., Sanders I., Saurat O., Scarpelli C., Schiex T.,
RA   Segurens B., Severin A.J., Sherrier D.J., Shi R., Sims S., Singer S.R.,
RA   Sinharoy S., Sterck L., Viollet A., Wang B.B., Wang K., Wang M., Wang X.,
RA   Warfsmann J., Weissenbach J., White D.D., White J.D., Wiley G.B.,
RA   Wincker P., Xing Y., Yang L., Yao Z., Ying F., Zhai J., Zhou L., Zuber A.,
RA   Denarie J., Dixon R.A., May G.D., Schwartz D.C., Rogers J., Quetier F.,
RA   Town C.D., Roe B.A.;
RT   "The Medicago genome provides insight into the evolution of rhizobial
RT   symbioses.";
RL   Nature 480:520-524(2011).
RN   [2] {ECO:0000313|EMBL:AES67725.1, ECO:0000313|Proteomes:UP000002051}
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Jemalong A17 {ECO:0000313|EnsemblPlants:AES67725,
RC   ECO:0000313|Proteomes:UP000002051};
RX   PubMed=24767513; DOI=10.1186/1471-2164-15-312;
RA   Tang H., Krishnakumar V., Bidwell S., Rosen B., Chan A., Zhou S.,
RA   Gentzbittel L., Childs K.L., Yandell M., Gundlach H., Mayer K.F.,
RA   Schwartz D.C., Town C.D.;
RT   "An improved genome release (version Mt4.0) for the model legume Medicago
RT   truncatula.";
RL   BMC Genomics 15:312-312(2014).
RN   [3] {ECO:0000313|EnsemblPlants:AES67725}
RP   IDENTIFICATION.
RC   STRAIN=cv. Jemalong A17 {ECO:0000313|EnsemblPlants:AES67725};
RG   EnsemblPlants;
RL   Submitted (APR-2015) to UniProtKB.
RN   [4] {ECO:0000313|EMBL:RHN76170.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaves {ECO:0000313|EMBL:RHN76170.1};
RA   Pecrix Y., Gamas P., Carrere S.;
RT   "Whole-genome landscape of Medicago truncatula symbiotic genes.";
RL   Nat. Plants 0:0-0(2018).
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       PRP16 sub-subfamily. {ECO:0000256|ARBA:ARBA00038040}.
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DR   EMBL; CM001218; AES67725.1; -; Genomic_DNA.
DR   EMBL; PSQE01000002; RHN76170.1; -; Genomic_DNA.
DR   RefSeq; XP_003597474.1; XM_003597426.2.
DR   AlphaFoldDB; G7IUG0; -.
DR   STRING; 3880.G7IUG0; -.
DR   PaxDb; 3880-AES67725; -.
DR   EnsemblPlants; AES67725; AES67725; MTR_2g098440.
DR   GeneID; 11423262; -.
DR   Gramene; AES67725; AES67725; MTR_2g098440.
DR   KEGG; mtr:11423262; -.
DR   eggNOG; KOG0924; Eukaryota.
DR   HOGENOM; CLU_001832_6_2_1; -.
DR   OMA; SASPWDY; -.
DR   OrthoDB; 5488182at2759; -.
DR   Proteomes; UP000002051; Chromosome 2.
DR   Proteomes; UP000265566; Chromosome 2.
DR   GO; GO:0005681; C:spliceosomal complex; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004386; F:helicase activity; IBA:GO_Central.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR   CDD; cd18791; SF2_C_RHA; 1.
DR   Gene3D; 1.20.120.1080; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR048333; HA2_WH.
DR   InterPro; IPR007502; Helicase-assoc_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1.
DR   PANTHER; PTHR18934:SF91; PRE-MRNA-SPLICING FACTOR ATP-DEPENDENT RNA HELICASE PRP16; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF21010; HA2_C; 1.
DR   Pfam; PF04408; HA2_N; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF07717; OB_NTP_bind; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00847; HA2; 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   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Helicase {ECO:0000313|EMBL:AES67725.1};
KW   Hydrolase {ECO:0000313|EMBL:RHN76170.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002051}.
FT   DOMAIN          581..744
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          766..946
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          79..330
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1204..1269
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        10..24
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        101..138
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        150..239
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        285..307
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        308..330
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1204..1245
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1269 AA;  143339 MW;  13AA18D24421BC51 CRC64;
     MEKNGANAEI VDINKTTTTL EPEKSTGGGL YVPGKDRVVY VAPERKSRLG LDTLAIAKRG
     ESQSDGAFKV PKEITTSIAA AAEDEDKSES SDVVEESGQA GTRRNAHRRY RETTSETSRA
     ESSLTDDHHA DTYGNRSTER RGSDVSASPS GYDRDDHRSE RRHSRDDSRS DSREVRHRNN
     YDSRESYSGR DSRSRYYDHE YDRKRNRYEG SRRTPGRSDW DHGRWEWEDT PRRDGVSSSR
     RHQPSPSPMF VGASPDARLV SPWHTPHSSY NSPSPWDHVS PSPVPIRASG SSVKSSVSGY
     NRRSHKLAFS SENSDTYEEE IADKSDLGEE HKYEITESMR QEMEYDADRA WYDREEGSAL
     FDSDSSSLFL GDEASFQKKE AELAKRLVRR DGTKMSLSQS KKLSQLTADN AQWEDRQLLR
     SGAVRGTEVQ TEFDDEDERK VILLVHDTKP PFLDGRVVYT KQAEPIMPIK DPTSDMALIS
     RKGSALVREI HEKQSSNKSR QRFWELAGSK LGDILGVEKT AEQIDADTAV VGEDGEIDFK
     EEAKFSNHMK KGEAVSDFAM SKTLAEQRQY LPIFSVREEL LQVIRENQVV VVVGETGSGK
     TTQLTQYLYE DGYTIGGIVG CTQPRRVAAM SVAKRVSEEM DTELGDKVGY AIRFEDVTGP
     NTVIKYMTDG VLLRETLKDS DLDKYRVIVM DEAHERSLST DVLFGILKKV VAQRRDFKLI
     VTSATLNAQK FSHFFGSVPI FHIPGRTFPV NILWSKTPVE DYVEGAVKQA MTIHVTSPPG
     DILIFMTGQD EIEAACYSLA ERMEQMVSSS NKEVPKLLIL PIYSQLPADL QAKIFQKAED
     GARKCIVATN IAETSLTVDG IFFVIDTGYG KMKVYNPRMG MDALQVFPVS RAAADQRAGR
     AGRTGPGTCY RLYTESAYLN EMLASPVPEI QRTNLGNVVL LLKSLKVENL LDFDFMDPPP
     QDNILNSMYQ LWVLGALNNV GGLTELGWKM VEFPLDPPLA KMLLMGERLG CLEEVLTIVS
     MLSVPSVFFR PKDRAEESDA ARERFFVPES DHLTLYNVYQ QWKQHDYRGD WCNDHFLHVK
     GLRKAREVRS QLLDILKTLK IPLTTCFPDT DVVRKAICSA YFHNSARLKG VGEYVNTRNG
     MPCHLHPSSA LYGMGCTPDY VVYHELILTT KEYMQCATAV EPQWMAELGP MFFSVKESDT
     SLLEHKKKQK REKTAMEEEM ENLKKEQAEL ERENKRKEKE KRAKSQQQIS IPGLKKGSST
     FLRPKKFGL
//
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