JHS1_ARATH
ID JHS1_ARATH Reviewed; 1331 AA.
AC A0A1P8ASY1; A0A1P8ASV1; F4HXR6; O04043; O04044;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2017, sequence version 1.
DT 03-AUG-2022, entry version 33.
DE RecName: Full=DNA replication ATP-dependent helicase/nuclease JHS1;
DE AltName: Full=Protein EMBRYO DEFECTIVE 2411 {ECO:0000303|PubMed:15266054};
DE AltName: Full=Protein JING HE SHENG 1 {ECO:0000303|PubMed:26951435};
DE Includes:
DE RecName: Full=DNA replication nuclease JHS1;
DE EC=3.1.-.-;
DE Includes:
DE RecName: Full=DNA replication ATP-dependent helicase JHS1;
DE EC=3.6.4.12 {ECO:0000250|UniProtKB:P51530};
GN Name=JHS1 {ECO:0000303|PubMed:26951435};
GN Synonyms=EMB2411 {ECO:0000303|PubMed:15266054};
GN OrderedLocusNames=At1g08840 {ECO:0000312|Araport:AT1G08840};
GN ORFNames=F7G19.26 {ECO:0000312|EMBL:AAB70418.1};
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
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).
RN [3]
RP FUNCTION [LARGE SCALE ANALYSIS], AND DISRUPTION PHENOTYPE [LARGE SCALE
RP ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=15266054; DOI=10.1104/pp.104.045179;
RA Tzafrir I., Pena-Muralla R., Dickerman A., Berg M., Rogers R., Hutchens S.,
RA Sweeney T.C., McElver J., Aux G., Patton D., Meinke D.;
RT "Identification of genes required for embryo development in Arabidopsis.";
RL Plant Physiol. 135:1206-1220(2004).
RN [4]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=cv. Columbia;
RX PubMed=26951435; DOI=10.1104/pp.16.00312;
RA Jia N., Liu X., Gao H.;
RT "A DNA2 homolog is required for DNA damage repair, cell cycle regulation,
RT and meristem maintenance in plants.";
RL Plant Physiol. 171:318-333(2016).
CC -!- FUNCTION: Essential protein required during embryogenesis
CC (PubMed:15266054). Key enzyme involved in DNA replication and damage
CC repair, shoot apical meristem (SAM) maintenance, and development
CC (PubMed:26951435). Involved in Okazaki fragments processing. Possesses
CC different enzymatic activities, such as single-stranded DNA (ssDNA)-
CC dependent ATPase, 5'-3' helicase and endonuclease activities. While the
CC ATPase and endonuclease activities are well-defined and play a key role
CC in Okazaki fragments processing and DSB repair, the 5'-3' DNA helicase
CC activity is atypical: it cannot load onto its tracking strand
CC internally and has an absolute free 5'-end requirement (By similarity).
CC {ECO:0000250|UniProtKB:Q9URU2, ECO:0000269|PubMed:15266054,
CC ECO:0000269|PubMed:26951435}.
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:0000250|UniProtKB:P51530};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000250|UniProtKB:P38859};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250|UniProtKB:P38859};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26951435}. Chromosome
CC {ECO:0000250|UniProtKB:P51530}. Note=Localized to nuclear foci in
CC response to DNA damage. {ECO:0000269|PubMed:26951435}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=A0A1P8ASY1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A0A1P8ASY1-2; Sequence=VSP_060109;
CC Name=3;
CC IsoId=A0A1P8ASY1-3; Sequence=VSP_060110;
CC -!- TISSUE SPECIFICITY: Strongly expressed in meristems, including both
CC root and shoot apical meristems (RAM and SAM) (PubMed:26951435). Also
CC present in the vasculature and in young floral tissues
CC (PubMed:26951435). {ECO:0000269|PubMed:26951435}.
CC -!- DISRUPTION PHENOTYPE: Defective embryo arrested at preglobular/early
CC globular stage with the formation of giant endosperm nuclei
CC (PubMed:15266054). In jhs1, retarded growth, abnormal pattern of shoot
CC apical meristem (SAM) cell division and differentiation, and
CC morphological defects such as fasciation, irregular arrangement of
CC siliques and phyllotaxy, and short roots (PubMed:26951435). Increased
CC sensitivity to DNA damage stress (PubMed:26951435). Increased DNA
CC damage response, including increased expression of genes involved in
CC DNA damage repair and cell cycle regulation, and a higher frequency of
CC homologous recombination (PubMed:26951435). Meristems exhibit a delayed
CC cell cycle progression at the G2 or late S phase, and a misregulation
CC of genes essential for meristem maintenance (PubMed:26951435).
CC {ECO:0000269|PubMed:15266054, ECO:0000269|PubMed:26951435}.
CC -!- MISCELLANEOUS: 'Jing he sheng' means fasciated stem in Chinese.
CC {ECO:0000305|PubMed:26951435}.
CC -!- SIMILARITY: Belongs to the DNA2/NAM7 helicase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB70418.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Seed defective Arabidopsis mutants;
CC URL="http://seedgenes.org/MutantList";
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DR EMBL; AC000106; AAB70418.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE28357.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM59735.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM59736.1; -; Genomic_DNA.
DR PIR; C86220; C86220.
DR RefSeq; NP_001184943.1; NM_001198014.1. [A0A1P8ASY1-2]
DR RefSeq; NP_001322072.1; NM_001331795.1. [A0A1P8ASY1-1]
DR RefSeq; NP_001322073.1; NM_001331796.1. [A0A1P8ASY1-3]
DR AlphaFoldDB; A0A1P8ASY1; -.
DR SMR; A0A1P8ASY1; -.
DR STRING; 3702.AT1G08840.2; -.
DR iPTMnet; A0A1P8ASY1; -.
DR ProMEX; A0A1P8ASY1; -.
DR ProteomicsDB; 197793; -.
DR ProteomicsDB; 203611; -. [A0A1P8ASY1-1]
DR ProteomicsDB; 213725; -.
DR EnsemblPlants; AT1G08840.2; AT1G08840.2; AT1G08840. [A0A1P8ASY1-2]
DR EnsemblPlants; AT1G08840.3; AT1G08840.3; AT1G08840. [A0A1P8ASY1-1]
DR EnsemblPlants; AT1G08840.4; AT1G08840.4; AT1G08840. [A0A1P8ASY1-3]
DR GeneID; 837406; -.
DR Gramene; AT1G08840.2; AT1G08840.2; AT1G08840. [A0A1P8ASY1-2]
DR Gramene; AT1G08840.3; AT1G08840.3; AT1G08840. [A0A1P8ASY1-1]
DR Gramene; AT1G08840.4; AT1G08840.4; AT1G08840. [A0A1P8ASY1-3]
DR KEGG; ath:AT1G08840; -.
DR Araport; AT1G08840; -.
DR TAIR; locus:2025610; AT1G08840.
DR eggNOG; KOG1805; Eukaryota.
DR HOGENOM; CLU_001666_2_2_1; -.
DR OMA; NYCEAAI; -.
DR OrthoDB; 633768at2759; -.
DR PRO; PR:A0A1P8ASY1; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; A0A1P8ASY1; baseline and differential.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0017108; F:5'-flap endonuclease activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0017116; F:single-stranded DNA helicase activity; IEA:InterPro.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:TAIR.
DR GO; GO:0006281; P:DNA repair; IMP:UniProtKB.
DR GO; GO:0006260; P:DNA replication; IMP:UniProtKB.
DR GO; GO:0033567; P:DNA replication, Okazaki fragment processing; IEA:InterPro.
DR GO; GO:0010073; P:meristem maintenance; IMP:UniProtKB.
DR GO; GO:0071932; P:replication fork reversal; IBA:GO_Central.
DR CDD; cd18808; SF1_C_Upf1; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR Gene3D; 3.90.320.10; -; 1.
DR InterPro; IPR026851; Dna2.
DR InterPro; IPR045055; DNA2/NAM7-like.
DR InterPro; IPR041679; DNA2/NAM7-like_C.
DR InterPro; IPR041677; DNA2/NAM7_AAA_11.
DR InterPro; IPR014808; DNA_replication_fac_Dna2_N.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR011604; PDDEXK-like_dom_sf.
DR PANTHER; PTHR10887; PTHR10887; 1.
DR PANTHER; PTHR10887:SF433; PTHR10887:SF433; 1.
DR Pfam; PF13086; AAA_11; 2.
DR Pfam; PF13087; AAA_12; 1.
DR Pfam; PF08696; Dna2; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 2: Evidence at transcript level;
KW 4Fe-4S; Alternative splicing; ATP-binding; Chromosome; DNA damage;
KW DNA repair; DNA replication; DNA-binding; Helicase; Hydrolase; Iron;
KW Iron-sulfur; Metal-binding; Multifunctional enzyme; Nuclease;
KW Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..1331
FT /note="DNA replication ATP-dependent helicase/nuclease
FT JHS1"
FT /id="PRO_0000446895"
FT DOMAIN 924..1271
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00560"
FT REGION 1..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 362..811
FT /note="Nuclease activity"
FT /evidence="ECO:0000250|UniProtKB:P38859"
FT REGION 812..1331
FT /note="Helicase activity"
FT /evidence="ECO:0000250|UniProtKB:P38859"
FT MOTIF 2..8
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000303|PubMed:26951435"
FT COMPBIAS 12..81
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 422
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P38859"
FT BINDING 666
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P38859"
FT BINDING 669
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P38859"
FT BINDING 675
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:P38859"
FT BINDING 945..952
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00560"
FT VAR_SEQ 156..171
FT /note="Missing (in isoform 2)"
FT /id="VSP_060109"
FT VAR_SEQ 169..171
FT /note="Missing (in isoform 3)"
FT /id="VSP_060110"
SQ SEQUENCE 1331 AA; 147286 MW; 9B3876BB875300D2 CRC64;
MPPRKKPKSS ALKSNKQSSA NHSSQPSTFG IQQLFLRHIQ NSQSTSNSHT STADPVDQQN
VNGLASDTAV LTPQNPLGTS NEKPDESKDM DQQLTEASPK ISKNLKRFSP GMLIKQSQDD
CGGEITWKIS PVNERLRAAA KNIPKMMDLT ENSLGVKSST IRPCSLNKLV QKQCPTSGIT
SKVEQWLSSP SKKASKRPAF ATNRVMERVN PSPDAEFEIV NTSSSGNSPF QTPPSLSCPH
NKLPCTVTCS GACGSMGAGQ HKKALLELLD QVEDVIAVDD KTTDDVGIVM PQARVKDDII
SSVVDCAVDE GPVSLPKMQN SINPDSYFLV LEVSEKRGSG SSSKGQCPYK VLRLLDEHTG
VECALYLWDE WFYSTVSPGD SINVIGEFDG DGKCDVDRQN NFLIVHPDTL VAGTRVAASF
GCPRRTVLDE RLRSNEHATV ALLGTLQHQV FQAGLSQESP SVDGLQEYAS TVIEKSIESL
YACGVHEGDV RSTLFKAIPK MLNWIEHFRY SKDSEVSKVD FGSTIGKKAV KVSEVIDIEE
MSWAPKYGLK GMIDASVRVI VESDMNTVNE KIMPLEFKSG KAPSGQSSIE HSAQVILYTL
LMSERYLKHI DNGLLYYLQS DQTQGISVQR SDLVGLIIRR NELANDILVA STTQQLPPML
RNPNICRNCR HLDVCTIYHK ADGGNTESSG LGDVFDTHVS HLSTLHFNFL RHWDRLIDLE
GREMQLLRKD IAHPHGSKGS HSASYLSSMV LDVTNGFQHH NSHKETRFIY RFVRQKSSES
RERVTSEDMI RTGNLATDDL DCKLRTGDRV ILRTEVSHLT VANGIIADIS RTHISVSLSK
RLRLPWSEPS SEVSNLSHEL WRIYKDEFMT SFSVMRFNLM QLFVQNGHNI RKMIVDLEPP
RFDNGSILSQ DPAISYIWSE KSLNNDQRQA ILKILTAKDY ALILGMPGTG KTSTMVHAVK
ALLIRGSSIL LASYTNSAVD NLLIKLKAQG IEFLRIGRDE AVHEEVRESC FSAMNMCSVE
DIKKKLDQVK VVASTCLGIN SPLLVNRRFD VCIIDEAGQI ALPVSIGPLL FASTFVLVGD
HYQLPPLVQS TEARENGMGI SLFRRLSEAH PQAISVLQNQ YRMCRGIMEL SNALIYGDRL
CCGSAEVADA TLVLSTSSST SPWLKKVLEP TRTVVFVNTD MLRAFEARDQ NAINNPVEAS
IIAEIVEELV NNGVDSKDIG IITPYNSQAS LIQHAIPTTP VEIHTIDKYQ GRDKDCILVS
FVRSREKPRS SASSLLGDWH RINVALTRAK KKLIMVGSQR TLSRVPLLML LLNKVKEQSG
ILNLLPGDLK P
