ID A0A1B6QED4_SORBI Unreviewed; 849 AA.
AC A0A1B6QED4;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 2.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=DNA 3'-5' helicase {ECO:0000256|ARBA:ARBA00034808};
DE EC=5.6.2.4 {ECO:0000256|ARBA:ARBA00034808};
GN ORFNames=SORBI_3002G310300 {ECO:0000313|EMBL:KXG36276.2};
OS Sorghum bicolor (Sorghum) (Sorghum vulgare).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Sorghinae; Sorghum.
OX NCBI_TaxID=4558 {ECO:0000313|EMBL:KXG36276.2, ECO:0000313|Proteomes:UP000000768};
RN [1] {ECO:0000313|EMBL:KXG36276.2, ECO:0000313|Proteomes:UP000000768}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768};
RX PubMed=19189423; DOI=10.1038/nature07723;
RA Paterson A.H., Bowers J.E., Bruggmann R., Dubchak I., Grimwood J.,
RA Gundlach H., Haberer G., Hellsten U., Mitros T., Poliakov A., Schmutz J.,
RA Spannagl M., Tang H., Wang X., Wicker T., Bharti A.K., Chapman J.,
RA Feltus F.A., Gowik U., Grigoriev I.V., Lyons E., Maher C.A., Martis M.,
RA Narechania A., Otillar R.P., Penning B.W., Salamov A.A., Wang Y., Zhang L.,
RA Carpita N.C., Freeling M., Gingle A.R., Hash C.T., Keller B., Klein P.,
RA Kresovich S., McCann M.C., Ming R., Peterson D.G., Mehboob-ur-Rahman,
RA Ware D., Westhoff P., Mayer K.F., Messing J., Rokhsar D.S.;
RT "The Sorghum bicolor genome and the diversification of grasses.";
RL Nature 457:551-556(2009).
RN [2] {ECO:0000313|Proteomes:UP000000768}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768};
RX PubMed=29161754; DOI=10.1111/tpj.13781;
RA McCormick R.F., Truong S.K., Sreedasyam A., Jenkins J., Shu S., Sims D.,
RA Kennedy M., Amirebrahimi M., Weers B.D., McKinley B., Mattison A.,
RA Morishige D.T., Grimwood J., Schmutz J., Mullet J.E.;
RT "The Sorghum bicolor reference genome: improved assembly, gene annotations,
RT a transcriptome atlas, and signatures of genome organization.";
RL Plant J. 93:338-354(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=5.6.2.4;
CC Evidence={ECO:0000256|ARBA:ARBA00034618};
CC -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily.
CC {ECO:0000256|ARBA:ARBA00009922}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00560}.
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DR EMBL; CM000761; KXG36276.2; -; Genomic_DNA.
DR AlphaFoldDB; A0A1B6QED4; -.
DR EnsemblPlants; KXG36276; KXG36276; SORBI_3002G310300.
DR Gramene; KXG36276; KXG36276; SORBI_3002G310300.
DR OMA; FILYVMM; -.
DR Proteomes; UP000000768; Chromosome 2.
DR ExpressionAtlas; A0A1B6QED4; baseline.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-UniRule.
DR CDD; cd17932; DEXQc_UvrD; 1.
DR CDD; cd18807; SF1_C_UvrD; 1.
DR Gene3D; 1.10.10.160; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR013986; DExx_box_DNA_helicase_dom_sf.
DR InterPro; IPR014017; DNA_helicase_UvrD-like_C.
DR InterPro; IPR000212; DNA_helicase_UvrD/REP.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR014016; UvrD-like_ATP-bd.
DR PANTHER; PTHR11070:SF61; DNA HELICASE; 1.
DR PANTHER; PTHR11070; UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER; 1.
DR Pfam; PF00580; UvrD-helicase; 1.
DR Pfam; PF13361; UvrD_C; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
DR PROSITE; PS51217; UVRD_HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00560};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|PROSITE-
KW ProRule:PRU00560};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU00560};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00560}; Reference proteome {ECO:0000313|Proteomes:UP000000768}.
FT DOMAIN 1..262
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51198"
FT DOMAIN 263..573
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51217"
SQ SEQUENCE 849 AA; 96597 MW; 73CECC44601DC113 CRC64;
MVGRVLTLLK EGIPPSNILA MTFTTAAASE MRERIGTVVG KAVAKEIAIS TFHSFCLQLC
RTHAEKLGRT SEFIIYGHGQ QRRAVIEAER LLENDKNNGV GDTTKQYDAD IKNSFKDKAK
KWQKFITQAK ASGRTPEDYE MKGDLTGASV LRHYNEILRS CNALDYHDFI NSSITLLTNF
PEVYKECQDM WRAIVVDEFQ DTSAMQYCLL KILASHNHIT IVGDEDQSIF SFNGADVSGF
DSFRRDFPDY KEIRLSKNYR STRAIVEAAT ALIQNNSKRH HRKLVETDNP SGCKITVKEC
HSEDSQCAFV IDKIIETTST TAEGCNFGNI AVLYRRQVTG KAFQVSFRNR KIPFNVHGVA
FYRKKVIKAI MAILRTTLPG CDDGPWCQAF KALLPCDKEE KKKIIDHVEK ISLARECSFI
SAATDIFSAK VSGTFKRSQI TQGRKVLSTL DSLSKLVERE QSVSVIISSA GDMLPQKYLL
EKRAVVDIDN GKLLNEDSDI RSVLQFLMDD VSDFLSTHFS SSVERSKTDE KGCASTLQAF
IDYISLRETE NFRSRKEENK NSITLTTIHQ SKGLEWDVVF IVQANDSEIP LLHEYNCTVK
EAGSTLEEER RLLYVAMTRA RKKLYILHVT VDSNRQLLQP SRFLREIPVH LLEVQGEETL
RKMPEQPSGD IPFDDSEGNI SIGKPIMGQN EVSPYPELAQ GCLANDFLRK FDIDDRSVVS
HIFHNWGKKQ AFQNPKRLLE KISFVIDERL RGKGYKRKDV LRKLKLFLSG DEALGYAQYV
IKWEQIPIEK RSQLMRERQE HFQKQRIENS MGSSEPTAKQ ISYLRNLGCT ITPTSRLHAS
NLIEKYKSL
//
