ID A0A024TM53_9STRA Unreviewed; 1354 AA.
AC A0A024TM53;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Chromatin-remodeling complex ATPase chain {ECO:0008006|Google:ProtNLM};
GN ORFNames=H310_11393 {ECO:0000313|EMBL:ETV95118.1};
OS Aphanomyces invadans.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Aphanomyces.
OX NCBI_TaxID=157072 {ECO:0000313|EMBL:ETV95118.1};
RN [1] {ECO:0000313|EMBL:ETV95118.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NJM9701 {ECO:0000313|EMBL:ETV95118.1};
RG The Broad Institute Genomics Platform;
RA Russ C., Tyler B., van West P., Dieguez-Uribeondo J., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L., Chapman S.B.,
RA Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C., Pearson M.,
RA Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Aphanomyces invadans NJM9701.";
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. ISWI subfamily.
CC {ECO:0000256|ARBA:ARBA00009687}.
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DR EMBL; KI913982; ETV95118.1; -; Genomic_DNA.
DR RefSeq; XP_008876291.1; XM_008878069.1.
DR STRING; 157072.A0A024TM53; -.
DR EnsemblFungi; H310_11393-t26_1; H310_11393-t26_1-p1; H310_11393.
DR EnsemblProtists; ETV95118; ETV95118; H310_11393.
DR GeneID; 20088443; -.
DR VEuPathDB; FungiDB:H310_11393; -.
DR eggNOG; KOG0385; Eukaryota.
DR OrthoDB; 5482994at2759; -.
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 GO; GO:0031491; F:nucleosome binding; IEA:InterPro.
DR CDD; cd17997; DEXHc_SMARCA1_SMARCA5; 1.
DR CDD; cd00084; HMG-box_SF; 2.
DR CDD; cd00167; SANT; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 1.10.30.10; High mobility group box domain; 2.
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; IPR036306; ISWI_HAND-dom_sf.
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; PF09011; HMG_box_2; 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; 2.
DR SMART; SM00717; SANT; 2.
DR SUPFAM; SSF101224; HAND domain of the nucleosome remodeling ATPase ISWI; 1.
DR SUPFAM; SSF47095; HMG-box; 2.
DR SUPFAM; SSF46689; Homeodomain-like; 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; PS50118; HMG_BOX_2; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
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}.
FT DOMAIN 11..88
FT /note="HMG box"
FT /evidence="ECO:0000259|PROSITE:PS50118"
FT DOMAIN 257..428
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 560..711
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 1285..1354
FT /note="HMG box"
FT /evidence="ECO:0000259|PROSITE:PS50118"
FT DNA_BIND 11..88
FT /note="HMG box"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00267"
FT DNA_BIND 1285..1354
FT /note="HMG box"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00267"
FT REGION 29..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 93..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 199..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1128..1158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1228..1291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1335..1354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..43
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..223
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1234..1254
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1271..1285
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1354 AA; 155658 MW; 8409A8F14E716DC5 CRC64;
MASEQAAAAP LMKPKSAFAH FQKQVTSAVR EELKQRGNAD IADTKDNDPA NLGAVQREVS
ARWNELTPEQ REPFLDAAKA DRERYDEECL LRDRQVEEER EKRRQDRNAL DVEGKRERKV
ATDVKEKREK KPAKPLTDEQ VAAKRKRDEV SQLAKGAKDE LKAEEERQKE ELKAKKAESA
SARLNYLLSQ SDVFRHFGVK APTNKAEKGA SRKKSEREED DELLHDKHDT VRLTVQPSVI
KFGTMRQYQL EGLSWMVNLA NQGINGILAD EMGLGKTLQT ISVLGYFQEF HNISGPHLVL
VPKSTLSNWL NEFHRWCPSL RAIKFHGDKE ERDRVVDEVL CPGLAQDKRK FDVCVTTFEM
CLKAKTTLAK FAWRYLIIDE AHRIKNESSQ FSMIVRTMAT EHRLLLTGTP LQNNLHELWA
LLNFLLPDVF SSSEQFDEWF NLDTEDEEAK KQMITQLHRI LRPFMLRRLK ADVEKSLPPK
KETLLFVGMT PMQKALYKTL LLRDMNTLTG GSSASKSALQ NIVMQLRKCC GHPYLFEGQE
DRSLPPLGEH VVENCGKMIL MDKLLKRLKA RGSRVLIFSQ MTRVLDIMED FCRMRAYGYC
RIDGNTSYDD RESSIDEYNA PNSSKFIFLL STRAGGLGIN LYTADIVILY DSDWNPQADL
QAQDRAHRIG QKKEVNVYRF VTANSVEEKI IERAQQKLKL DAMVVQQGRL QEKQKNLSKN
DMLDMIRFGA DEVFRANDDE MITDEDIEAI LAKGEARTEE MNSKLQAHDK GDLLNFKLDG
GGCQVIDGVD YSKEKERLEE IKRLADLEFA RTLADGMGKR ERRTVVKADE PGFKMKSKMK
QLPKSMRLPR MDEWQFYNRS RMTEIHEMEV SAYELAKANG EAIDKSDHSY LSPALQAEKE
ELLKAAFSDW NKPHFYLFIK LMARYGRTNL TAIAREMVKP YDEVVRYADT FFKRGAELGD
WDKIRKSIEK GESKLLEIER LAEQTAIKIK RYQNPYDDLV INYQGKGGKL FTEEEDRLLL
CLVHAYGYGS WEKIKREIHA APVCAFDYYL RSRSAAELGR RCDALMRICE KDNVDYELKE
KKDRALQQEL AEQREVLAKR IAEAKAELNR NQALVDEKIM KEAKKMQAAR EAKRLKRDKK
EDAESDHYPA TSKADDVLTE ADQEELRQMI AQSTDKEAST IALKFCAKHV KCQLSQVLAI
IHQYAAPIAY SRPGQPAWRL HPEYAVPLST SRSRKRPLSD EGGPDDESKD GKRLPKSPWS
PSAMKQASAK KTKKPQVEVP AKKPPRKPRS AYVLFSLAKR NEVRSSMPEN TGIVDLMSRL
TELWLEMSDT DKAPWYEAQE HDKQRYEQEV EEAG
//
