ID D7G5A2_ECTSI Unreviewed; 1563 AA.
AC D7G5A2;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE SubName: Full=Probable chromatin remodelling complex ATPase chain {ECO:0000313|EMBL:CBJ27256.1};
GN ORFNames=Esi_0063_0083 {ECO:0000313|EMBL:CBJ27256.1};
OS Ectocarpus siliculosus (Brown alga) (Conferva siliculosa).
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; PX clade; Phaeophyceae;
OC Ectocarpales; Ectocarpaceae; Ectocarpus.
OX NCBI_TaxID=2880 {ECO:0000313|EMBL:CBJ27256.1, ECO:0000313|Proteomes:UP000002630};
RN [1] {ECO:0000313|EMBL:CBJ27256.1, ECO:0000313|Proteomes:UP000002630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ec32 / CCAP1310/4 {ECO:0000313|Proteomes:UP000002630};
RX PubMed=20520714; DOI=10.1038/nature09016;
RA Cock J.M., Sterck L., Rouze P., Scornet D., Allen A.E., Amoutzias G.,
RA Anthouard V., Artiguenave F., Aury J.M., Badger J.H., Beszteri B.,
RA Billiau K., Bonnet E., Bothwell J.H., Bowler C., Boyen C., Brownlee C.,
RA Carrano C.J., Charrier B., Cho G.Y., Coelho S.M., Collen J., Corre E.,
RA Da Silva C., Delage L., Delaroque N., Dittami S.M., Doulbeau S., Elias M.,
RA Farnham G., Gachon C.M., Gschloessl B., Heesch S., Jabbari K., Jubin C.,
RA Kawai H., Kimura K., Kloareg B., Kupper F.C., Lang D., Le Bail A.,
RA Leblanc C., Lerouge P., Lohr M., Lopez P.J., Martens C., Maumus F.,
RA Michel G., Miranda-Saavedra D., Morales J., Moreau H., Motomura T.,
RA Nagasato C., Napoli C.A., Nelson D.R., Nyvall-Collen P., Peters A.F.,
RA Pommier C., Potin P., Poulain J., Quesneville H., Read B., Rensing S.A.,
RA Ritter A., Rousvoal S., Samanta M., Samson G., Schroeder D.C., Segurens B.,
RA Strittmatter M., Tonon T., Tregear J.W., Valentin K., von Dassow P.,
RA Yamagishi T., Van de Peer Y., Wincker P.;
RT "The Ectocarpus genome and the independent evolution of multicellularity in
RT brown algae.";
RL Nature 465:617-621(2010).
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. ISWI subfamily.
CC {ECO:0000256|ARBA:ARBA00009687}.
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DR EMBL; FN648852; CBJ27256.1; -; Genomic_DNA.
DR STRING; 2880.D7G5A2; -.
DR EnsemblProtists; CBJ27256; CBJ27256; Esi_0063_0083.
DR eggNOG; KOG0385; Eukaryota.
DR InParanoid; D7G5A2; -.
DR OrthoDB; 5482994at2759; -.
DR Proteomes; UP000002630; Chromosome LG17.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR CDD; cd17997; DEXHc_SMARCA1_SMARCA5; 1.
DR CDD; cd00084; HMG-box_SF; 1.
DR CDD; cd00167; SANT; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 1.10.30.10; High mobility group box domain; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 2.
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; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR009071; HMG_box_dom.
DR InterPro; IPR036910; HMG_box_dom_sf.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR044754; Isw1/2_DEXHc.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR015195; SLIDE.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR PANTHER; PTHR45623:SF49; SWI_SNF RELATED, MATRIX ASSOCIATED, ACTIN DEPENDENT REGULATOR OF CHROMATIN, SUBFAMILY A, MEMBER 1; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00505; HMG_box; 1.
DR Pfam; PF09111; SLIDE; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00398; HMG; 1.
DR SUPFAM; SSF47095; HMG-box; 1.
DR SUPFAM; SSF46689; Homeodomain-like; 2.
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; PS50118; HMG_BOX_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA-binding {ECO:0000256|PROSITE-ProRule:PRU00267};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|PROSITE-ProRule:PRU00267};
KW Reference proteome {ECO:0000313|Proteomes:UP000002630}.
FT DOMAIN 13..81
FT /note="HMG box"
FT /evidence="ECO:0000259|PROSITE:PS50118"
FT DOMAIN 272..443
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 574..725
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DNA_BIND 13..81
FT /note="HMG box"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00267"
FT REGION 69..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 192..259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1209..1352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1438..1514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1136..1163
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 69..88
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..154
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..259
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1252..1266
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1314..1340
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1445..1460
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1461..1475
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1563 AA; 172616 MW; 08A7CC036A2CB5C2 CRC64;
MSGSGAGAFG APVKAATSAY MFFQGDQYSN HKDEFAGLAL GQQGAEISRR WRELPQEERS
RFDALAAEDR KRFQEESEAR DAEVAARQEA NRAARYADPA SSTYMRERAS VEPKKERKVT
REEDMSEERL EARRLAKEKR AKQKDARLAA EAESERQKSS IAAAAAATAR KRIKYILRQS
DIFATHFGVA LSDSDEEEEE KEKEKEEDAS KGAAAAGGSP SKRRQAGRGA ADEAMDDVNG
EDTAPTYLTK QPPSISGGTM RSYQLEGLNW MVNLQAQGTN GILADEMGLG KTLQSISILA
YMRDFQNVTG PHIILLPKSV LGNWQLEFKR FCPDIRVLRL SGTKDERAAT IRNDLKPGSP
EDERDWDVLV TTYEVANIEK TYLNKIGWRY LIIDEAHRLK NESSLFSMTV RELTTQYRLL
LTGTPLQNNL HELWALLNFL LPTVFQDSEA FSKVFDLNVD DADKKQNMIK QLHKILRPFM
LRRLKKEVEK SLPPKEETIL FTSMSEVQRK VYKGVLMRDI DTINGTSAGR TAILNIVMQL
RKCCNHPYLF PNTEDRNLDP MGEHLVENCG KMILLDKLLT RLKAAGHRVL VFSQMTRMMD
ILEDLMHMRE YKYCRIDGNT PHDTRQDLIE EYNAPGSEKF IFLLSTRAGG LGINLQSADT
CILYDSDWNP QADLQAQDRC HRIGQTKTVK VYRLVTEDTI EEKVVERAQQ KLKLDAMVVQ
RGMLQGEKKL EKDEMLAAIR FGADAVFRCK DTVMSDQDLD AVLERGAKKT KDMQSKLNVA
EKGDMLDFSF DDGTGVQNFE GINYGDRKLR DQMRAGFIDI GRRERKPATV KAYAPPPPRV
EPKKMVLKMP KELEMPKMKD HQMFDRARIV ELQDELQDNF KALKDRGTKI PVDGADIASM
LLSADKVKER AELIAQGFPG WTRGHYYSFI DGMAVYGRDR LELVATMVGK PAEEVVRYGE
VFWRQGPKTF SEEAWRRIKT RVETKEKRLN ELNRIMMVTN ELMEAVDDPW RNMEVRINQR
QGGAGTAGMQ LQREWTKDED RYLLCLTHLC GWGNWRKVRA CILASPRFTF DYYLRSLSET
ALGKHCEQLM KSSEKYLQDL QDRMKKEAKR EMEDRGALEK DEAAAAREDE EFKLRIRAAD
NMLGTAEREL AEAESNKRNL EMIAEAIKSG TVSLDNPNVR SLLESCASNG IGTTGLNTKN
AVKKSAEGVA GAGAGGRKSP GVGGKKSASP GGGGQKKAVA SKAAVPGNTG NGGGGKKTSA
ASSGTPAAAA NGDAKKSGGG GGKGKGNAVA GKKADTTSSD GKGKVDAGKG GVKSPKASSS
TSNAVDKSPA NSSGTKAKRT PTKSVGKPGL EVPKTLFPEL VRLIEKGELT SKDDMLQIFQ
KKHPAFTQVS INKAIGVLGE KASRGSKWKV LDAGKKYLSM PVYQGNVPEE VAVLSALSAK
RKSGGSESHS AKKRKSTTPS KANGESKSPI TNFFPPKTSG AADANGGGGS SAASKKRKAP
APAAPKSPGP SPGFVAFCRA NRTRVQAELP IGSSKADTAD RLLQLWGELD DKVAERWTSG
ALP
//
