ID A0A178VTI3_ARATH Unreviewed; 3575 AA.
AC A0A178VTI3; A0A1P8B2X1;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=P-loop containing nucleoside triphosphate hydrolases superfamily protein {ECO:0000313|EMBL:ANM63246.1};
GN Name=SYD {ECO:0000313|EMBL:ANM63246.1, ECO:0000313|TAIR:AT2G28290};
GN Synonyms=CHR3 {ECO:0000313|EMBL:ANM63246.1}, SPLAYED
GN {ECO:0000313|EMBL:ANM63246.1};
GN OrderedLocusNames=At2g28290 {ECO:0000313|Araport:AT2G28290,
GN ECO:0000313|EMBL:ANM63246.1};
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:ANM63246.1, ECO:0000313|Proteomes:UP000006548};
RN [1] {ECO:0000313|EMBL:ANM63246.1, ECO:0000313|Proteomes:UP000006548}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia {ECO:0000313|Proteomes:UP000006548};
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S., Shea T.P., Benito M.I., Town C.D.,
RA Fujii C.Y., Mason T., Bowman C.L., Barnstead M., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [2] {ECO:0007829|PubMed:18433157}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18433157; DOI=10.1021/pr8000173;
RA de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,
RA Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J.,
RA Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H.;
RT "Site-specific phosphorylation profiling of Arabidopsis proteins by mass
RT spectrometry and peptide chip analysis.";
RL J. Proteome Res. 7:2458-2470(2008).
RN [3] {ECO:0007829|PubMed:19376835}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
RN [4] {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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; CP002685; ANM63246.1; -; Genomic_DNA.
DR RefSeq; NP_001325348.1; NM_001336159.1.
DR SMR; A0A178VTI3; -.
DR ProteomicsDB; 195511; -.
DR EnsemblPlants; AT2G28290.5; AT2G28290.5; AT2G28290.
DR GeneID; 817375; -.
DR Gramene; AT2G28290.5; AT2G28290.5; AT2G28290.
DR Araport; AT2G28290; -.
DR TAIR; AT2G28290; SYD.
DR OrthoDB; 1221768at2759; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; A0A178VTI3; baseline and differential.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0042393; F:histone binding; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR GO; GO:0048731; P:system development; IEA:UniProt.
DR CDD; cd17996; DEXHc_SMARCA2_SMARCA4; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR InterPro; IPR014978; Gln-Leu-Gln_QLQ.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR014012; HSA_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR029295; SnAC.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR10799:SF973; ATP-DEPENDENT HELICASE BRM; 1.
DR PANTHER; PTHR10799; SNF2/RAD54 HELICASE FAMILY; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF14619; SnAC; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00951; QLQ; 1.
DR SMART; SM01314; SnAC; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51204; HSA; 1.
PE 1: Evidence at protein level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ANM63246.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Proteomics identification {ECO:0007829|PeptideAtlas:A0A178VTI3,
KW ECO:0007829|ProteomicsDB:A0A178VTI3};
KW Reference proteome {ECO:0000313|Proteomes:UP000006548}.
FT DOMAIN 574..648
FT /note="HSA"
FT /evidence="ECO:0000259|PROSITE:PS51204"
FT DOMAIN 767..934
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1078..1224
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 76..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 123..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 328..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1343..1473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1501..1576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1589..1638
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1691..1812
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1831..1870
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2041..2069
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2090..2116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2144..2163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2180..2223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2236..2452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2518..2539
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2723..2760
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2866..2885
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3018..3046
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3190..3209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3318..3338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3513..3575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..172
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..192
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 356..372
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1357..1383
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1384..1434
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1437..1452
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1501..1516
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1555..1574
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1594..1615
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1691..1757
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1773..1787
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1796..1812
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1837..1866
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2041..2062
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2090..2106
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2180..2197
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2286..2313
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2323..2337
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2372..2395
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2404..2421
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2433..2452
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2518..2532
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2723..2741
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2742..2759
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3520..3538
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3539..3563
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3575 AA; 389935 MW; CE3690FE2EA84A1B CRC64;
MTSSSHNIEL EAAKFLHKLI QDSKDEPAKL ATKLYVILQH MKTSGKENTM PYQVISRAMD
TVVNQHGLDI EALKSSCLPH PGGTQTEDSG SAHLAGSSQA VGVSNEGKAT LVENEMTKYD
AFTSGRQLGG SNSASQTFYQ GSGTQSNRSF DRESPSNLDS TSGISQPHNR SETMNQRDVK
SSGKRKRGES SLSWDQNMDN SQIFDSHKID DQTGEVSKIE MPGNSGDIRN LHVGLSSDAF
TTPQCGWQSS EATAIRPAIH KEPGNNVAGE GFLPSGSPFR EQQLKQLRAQ CLVFLALRNG
LVPKKLHVEI ALRNTFREED GFRGELFDPK GRTHTSSDLG GIPDVSALLS RTDNPTGRLD
EMDFSSKETE RSRLGEKSFA NTVFSDGQKL LASRIPSSQA QTQVAVSHSQ LTFSPGLTKN
TPSEMVGWTG VIKTNDLSTS AVQLDEFHSS ADEEEGNLQP SPKYTMSQKW IMGRQNKRLL
VDRSWSLKQQ KADQAIGSRF NELKESVSLS DDISAKTKSV IELKKLQLLN LQRRLRSEFV
YNFFKPIATD VEHLKSYKKH KHGRRIKQLE KYEQKMKEER QRRIRERQKE FFGGLEVHKE
KLEDLFKVRR ERLKGFNRYA KEFHKRKERL HREKIDKIQR EKINLLKIND VEGYLRMVQD
AKSDRVKQLL KETEKYLQKL GSKLKEAKLL TSRFENEADE TRTSNATDDE TLIENEDESD
QAKHYLESNE KYYLMAHSIK ENINEQPSSL VGGKLREYQM NGLRWLVSLY NNHLNGILAD
EMGLGKTVQV ISLICYLMET KNDRGPFLVV VPSSVLPGWQ SEINFWAPSI HKIVYCGTPD
ERRKLFKEQI VHQKFNVLLT TYEYLMNKHD RPKLSKIHWH YIIIDEGHRI KNASCKLNAD
LKHYVSSHRL LLTGTPLQNN LEELWALLNF LLPNIFNSSE DFSQWFNKPF QSNGESSAEE
ALLSEEENLL IINRLHQVLR PFVLRRLKHK VENELPEKIE RLIRCEASAY QKLLMKRVED
NLGSIGNAKS RAVHNSVMEL RNICNHPYLS QLHSEEVNNI IPKHFLPPIV RLCGKLEMLD
RMLPKLKATD HRVLFFSTMT RLLDVMEDYL TLKGYKYLRL DGQTSGGDRG ALIDGFNKSG
SPFFIFLLSI RAGGVGVNLQ AADTVILFDT DWNPQVDLQA QARAHRIGQK KDVLVLRFET
VNSVEEQVRA SAEHKLGVAN QSITAGFFDN NTSAEDRKEY LESLLRESKK EEDAPVLDDD
ALNDLIARRE SEIDIFESID KQRKENEMET WNTLVHGPGS DSFAHIPSIP SRLVTEDDLK
LLYETMKLND VPMVAKESTV GMKRKDGSMG GLDTHQYGRG KRAREVRSYE EKLTEEEFEK
LCQTESPDSP QGKGEGSERS LANDTSNIPV ENSSDTLLPT SPTQAITVQP MEPVRPQSHT
LKEETQPIKR GRGRPKRTDK ALTPVSLSAV SRTQATGNAI SSAATGLDFV SSDKRLEAAS
HPTSSLALTS PDLSGPPGFQ SLPASPAPTP IRGRGRGRSR GRGAGRGRRV EGVLHGSNSS
ITQRTETATS LASDAEATKF ALPRSASEIV SRVPKANEGS TSNPDQVSPV HSATTALRSD
KAADKDLDAP PGFDSGSHVQ TLNVLENSSE RKAFAVKKRP LIQGVSSQHP GPNKQPLDLP
VSTSSTLLGG GPVQNQNAVS SVCDGSKSPS EGRTYTALQG VTTAPSDATL PMSSQPSDAT
LPMSSQPVGS TVEAQEANVP SLPAALPAKR RVRNLPSRGE TPKRQGKRRG QPLPATDASS
ARSTGLTPQI EVKVGNLSGT KAKFDAVAKE QPHFSQSVAP DIHSSGSLSQ EIRRDTSGTG
GSARKQTADV TDVARVMKEI FSETSLLKHK VGEPSATTRT NVPDAQSPGE MNLHTVETHK
AEDSSGLKNQ EALYNLSKAD KLVSDIPHPV PGDLTTSGSV ANKDVDIGSS KVAAENELVK
IPGGDVDSSV IQLSLGNTLT AKSSLEKCTA DQLLGEKLSQ EGETTPASDG ETCHLAEETA
SSLSYVRSEP TASASTTAEP LPTDKLEKNI SFQDEVKTLN GDKREAILLS SEEQTNVNSK
IETNSEELQA SRTDEVPHVD GKSVDVANQT VKEDEAKHSV EIQSSMLEPD ELPNAGQKGH
SSIDLQPLVL VTSNENAMSL DDKDYDPISK SADIEQDPEE SVFVQGVGRP KVGTADTQME
DTNDAKLLVG CSVESEEKEK TLQSLIPGDD ADTEQDPEES VSDQRPKVGS AYTQMEDTDE
AKLLMGCSVE SEEKEKTLQS HIPGDDADTE KNPEESVSVQ GVDRPKVGTT DTQMEDTNDA
KLLVGCSVAS EEKEKTLQSH IPGDDADTEQ NPEESVSVQG VNRPKVGNAN TQMEDTDEAK
VLVGCSVESE EKEKTLQSHI PGDDADTEQN PEESVSNFDR PKDGTADTHM EDIDDAKLLV
GCSVESEEKE KSLQSHMPSD DAVLHAPFEN TKDSKGDDLH GESLVSCPTM EVMEQKGFES
ETHARTDSGG IDRGNEVSEN MSDGVKMNIS SVQVPDASHD LNVSQDQTDI PLVGGIDPEH
VQENVDVPAS PHGAAPNIVI FQSEGHLSPS ILPDDVAGQL ESMSNDEKTN ISSEQVPDVS
HDLKVSQDQT DIPPVGGIVP ENLQEIVDVP ASPHGVVPDV VVSQSEEIQS PSILPDDVPG
QPDDGNCEKM DTMQNNTSID IGITSGKTCQ PSSSTQPEDE NRNSLSHCEP SEVVEQRDSR
DQVCIGSVES QVEISSAILE NRSADIQPPQ SILVDQKDIE ESKEPGIESA DVSLHQLADI
QAEPSNLVDQ MDIEESKEPG TESADVSLHQ LADIQPGPSI LVDQMDTEKS KEPGTESADV
SLHQLADIQP GPSILVDQMD TEKSKEPGTE SADVSLHQLA DIQPGPSILV DQMDTEEFKN
PDVSLHQLAD IEPSLSISAV QKNIEDKDQS HVETAGSELV DVSAECSTEP QVQLPPSSEP
VGDMHVHLGA SKSEIVAEGT DFSSSLPKTE EENAKSQLAD TEPSSSLTAV QKNIEDQVET
AGCEFVVVST GCSTEPQVQL PPSAEPVVAE GTEFPSSLLM TGVDNSSHLM TGVDNAKTHL
ADVVPSSSPT TMEKNIEAQD QDQVTTGGCG LVDVLTECSS EPQLQLPPSA EPVISEGTEL
ATLPLTEEEN ADSQLANIEP SSSPSVVEKN IEAQDQDQVK TAGCELVSTG CSSEPQVHLP
PSAEPDGDIH VHLKETEKSE SMVVVGEGTA FPSSLPVTEE GNAESQLADT EPFTSPTVVE
KNIKDQEQVE TTGCGLVDDS TGCSSEPQVQ LPPSAEPMEG THMHLEETKK SETVVTEIQL
ADIDPSFSLI VVQTNIEDQD QIETGGCDLI NVPSGCSTEP QIQLSSSAEP EEGMHIHLEA
AMNSETVVTE GSELPSSLPM TEDENADGQL AEVEPSVSLT VEQTNIEEKD HIETAECELV
DVSPGCSSQP EVKFPPSPDA VGGMDVHLET VVTEDTDSNS SLPKTEEKDA ENPSDRLDGE
SDGTTVATVE GTCVESNSLV AEESNIEVPK DNEDV
//
