ID A0A1P8BBY0_ARATH Unreviewed; 831 AA.
AC A0A1P8BBY0;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=ATP-dependent DNA helicase {ECO:0000256|RuleBase:RU364117};
DE EC=3.6.4.12 {ECO:0000256|RuleBase:RU364117};
GN Name=RECQSIM {ECO:0000313|EMBL:ANM69092.1,
GN ECO:0000313|TAIR:AT5G27680};
GN Synonyms=RECQ helicase SIM {ECO:0000313|EMBL:ANM69092.1};
GN OrderedLocusNames=At5g27680 {ECO:0000313|Araport:AT5G27680,
GN ECO:0000313|EMBL:ANM69092.1};
GN ORFNames=T1G16.10 {ECO:0000313|EMBL:ANM69092.1}, T1G16_10
GN {ECO:0000313|EMBL:ANM69092.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702 {ECO:0000313|EMBL:ANM69092.1, ECO:0000313|Proteomes:UP000006548};
RN [1] {ECO:0000313|EMBL:ANM69092.1, ECO:0000313|Proteomes:UP000006548}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548};
RX PubMed=11130714; DOI=10.1038/35048507;
RG Kazusa DNA Research Institute;
RG Cold Spring Harbor and Washington University in St Louis Sequencing Consortium;
RG European Union Arabidopsis Genome Sequencing Consortium;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., See L.H., Vil D., Baker J.,
RA Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Dusterhoft A., Stiekema W., Pohl T., Entian K.D.,
RA Terryn N., Hartley N., Bent E., Johnson S., Langham S.A., McCullagh B.,
RA Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H.,
RA Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Lankhorst R.K., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S.,
RA Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J.,
RA Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K., Rudd S., Schoof H.,
RA Schueller C., Zaccaria P., Mewes H.W., Bevan M., Fransz P.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [2] {ECO:0000313|Proteomes:UP000006548}
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548};
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
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=3.6.4.12;
CC Evidence={ECO:0000256|RuleBase:RU364117};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU364117}.
CC -!- SIMILARITY: Belongs to the helicase family. RecQ subfamily.
CC {ECO:0000256|ARBA:ARBA00005446, ECO:0000256|RuleBase:RU364117}.
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DR EMBL; CP002688; ANM69092.1; -; Genomic_DNA.
DR RefSeq; NP_001330795.1; NM_001344031.1.
DR AlphaFoldDB; A0A1P8BBY0; -.
DR SMR; A0A1P8BBY0; -.
DR ProteomicsDB; 193763; -.
DR EnsemblPlants; AT5G27680.6; AT5G27680.6; AT5G27680.
DR GeneID; 832830; -.
DR Gramene; AT5G27680.6; AT5G27680.6; AT5G27680.
DR Araport; AT5G27680; -.
DR TAIR; AT5G27680; RECQSIM.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; A0A1P8BBY0; baseline and differential.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0006310; P:DNA recombination; IEA:InterPro.
DR CDD; cd17920; DEXHc_RecQ; 1.
DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR004589; DNA_helicase_ATP-dep_RecQ.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR032284; RecQ_Zn-bd.
DR InterPro; IPR015940; UBA.
DR InterPro; IPR009060; UBA-like_sf.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR NCBIfam; TIGR00614; recQ_fam; 1.
DR PANTHER; PTHR13710:SF69; ATP-DEPENDENT DNA HELICASE Q-LIKE SIM; 1.
DR PANTHER; PTHR13710; DNA HELICASE RECQ FAMILY MEMBER; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF16124; RecQ_Zn_bind; 1.
DR SMART; SM00487; DEXDc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF46934; UBA-like; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS50030; UBA; 1.
PE 1: Evidence at protein level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU364117};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU364117};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU364117};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU364117}; Nucleus {ECO:0000256|RuleBase:RU364117};
KW Proteomics identification {ECO:0007829|PeptideAtlas:A0A1P8BBY0};
KW Reference proteome {ECO:0000313|Proteomes:UP000006548}.
FT DOMAIN 2..44
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT DOMAIN 177..353
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT REGION 402..450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 795..831
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 402..424
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 800..823
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 831 AA; 94426 MW; E3DF3B0CD4559F61 CRC64;
MDLSSDQLVM KIVEMGFEKL DALEAVKAVG GKSCDDAVEY ILKGNHRTGG FKPASLLCSS
GSNKILGKRA MPSSFSSSES KRQSSLLDHF RSVNQNKKKG DTFGTVEVDS QLETVSEHSE
EVRKSLAPVF MESSCFPEGQ LLNGCSEASS SWEKRVNSIL RNRFGISSLR SFQREALSTW
VAHKDCLVLA ATGSGKSLCF QIPALLTGKV VVVISPLISL MHDQCLKLSR HKVSACFLGS
GQLDNCIEEK AMQGMYQIIY VCPETVVRLI KPLQKLAKTH GIALFAIDEA HCVSKWGHDF
RPHYRKLSVL RENFCASNLE FLEYDVPIMA LTATATVNVQ EDILESLHLS KETKIVLTSF
FRPNLQFSVK HSRTKFASSY AKDFQNLVDL YSEKKNSTGK KLAVISRESE EQTDFGSHDS
ENIHETDYDE DEEDQENSLA KKNSSNGKEL SEAYLEDETD IFQSVDDWDV ACGEFCAMPS
CELLEIPVPS EKQKDLEGLT IIYVPTRKES VNIAKYLCGV GLKAAAYNAS LPKKHLRQVH
QDFHDNKLQS LEAYYQEAGR AGRDGELAEC VLYADLSRAP TLLPSRRSKE QTEQAYKMLS
DCFRYGMNTS QCRAKILVEY FGEEFSSKKC NSCDVCTEGP PELVDVREEA NLLFQVITAF
HLQVDNDSEH APYEDYGLGN SKQNKLSHKP NLLFFISKLR EQCEKFKETD CLWWKGLARI
MEAEGYIKEM DNKDRRVEIK FIQPTEKGKK QLDFQDDKPL YVYPEADMLL SLKQDRTYSG
FSEWGKGWAD PEIRRQRLER RERKPRRERK PRKKRTRGRS STKLHPWRSK E
//
