ID F0WNU3_9STRA Unreviewed; 1623 AA.
AC F0WNU3;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=Uncharacterized protein AlNc14C175G8103 {ECO:0000313|EMBL:CCA22986.1};
GN Name=AlNc14C175G8103 {ECO:0000313|EMBL:CCA22986.1};
GN ORFNames=ALNC14_091290 {ECO:0000313|EMBL:CCA22986.1};
OS Albugo laibachii Nc14.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Albuginales; Albuginaceae; Albugo.
OX NCBI_TaxID=890382 {ECO:0000313|EMBL:CCA22986.1};
RN [1] {ECO:0000313|EMBL:CCA22986.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=21750662; DOI=10.1371/journal.pbio.1001094;
RA Kemen E., Gardiner A., Schultz-Larsen T., Kemen A.C., Balmuth A.L.,
RA Robert-Seilaniantz A., Bailey K., Holub E., Studholme D.J., Maclean D.,
RA Jones J.D.;
RT "Gene gain and loss during evolution of obligate parasitism in the white
RT rust pathogen of Arabidopsis thaliana.";
RL PLoS Biol. 9:e1001094-e1001094(2011).
RN [2] {ECO:0000313|EMBL:CCA22986.1}
RP NUCLEOTIDE SEQUENCE.
RA MacLean D.;
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. SWR1 subfamily.
CC {ECO:0000256|ARBA:ARBA00009220}.
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DR EMBL; FR824220; CCA22986.1; -; Genomic_DNA.
DR EnsemblProtists; CCA22986; CCA22986; ALNC14_091290.
DR HOGENOM; CLU_243468_0_0_1; -.
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 CDD; cd18003; DEXQc_SRCAP; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 1.
DR Gene3D; 1.20.120.850; SWI2/SNF2 ATPases, N-terminal domain; 1.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR InterPro; IPR039448; Beta_helix.
DR InterPro; IPR036047; F-box-like_dom_sf.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR014012; HSA_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR InterPro; IPR001202; WW_dom.
DR PANTHER; PTHR45685:SF1; HELICASE SRCAP; 1.
DR PANTHER; PTHR45685; HELICASE SRCAP-RELATED; 1.
DR Pfam; PF13229; Beta_helix; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07529; HSA; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00573; HSA; 1.
DR SUPFAM; SSF81383; F-box domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF51126; Pectin lyase-like; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51204; HSA; 1.
DR PROSITE; PS50020; WW_DOMAIN_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 183..255
FT /note="HSA"
FT /evidence="ECO:0000259|PROSITE:PS51204"
FT DOMAIN 363..528
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 886..1036
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 1219..1247
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT REGION 1..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..87
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1623 AA; 186786 MW; A1FF0ADB4111F4BC CRC64;
MQHSGTSRPR SVAKKSSKGS SNHRQSRRIN RKLLKAPETA PTAETSEIAP PDAPKRAPNA
SARIPPVPKT TPPDSQPLHP PPPSFTASET PSFSLQSPLN TSIPDFQAPW LQRKAEILTR
LAELTFENCT SDSPSIQLSN APPMDVQKAL HSPQIRNFEQ ANPHTTPVTS GNRRLLRRKR
LRFGENPLLE RGQYHRDYLL QEMEWMAADF AQEHKWKGKT ARTLGTSLAS YHRKRANLTA
RKEKTDMKAQ RRVAGRMARD IKRFWVKIDK LVQFQHKLQA DQIRKSVMDR QLKTLVLQTE
QYASALAATF QKSSSHAPEA PMDGTEPRKK PSVWSFHSFQ RPFLLTNRLE LREYQIAGVA
WLIRMCEKRI NGILADEMGL GKTIQTITLL AHLASQHRLW GPHLIIVPTS CLVNWEMELK
RWCPAFKVLT YFGSAKRRKL LRQGWSKPNT FHVCVTSYQL VVQDAHCFKR KKWYYVILDE
AHHIKNWKSL RWQTLLTLHS QRRLLLTGTP LQNHILELWA LMHFLMPHLF ASRKEFTYWF
QQPLSVMSES SEVDHALVTQ LHGIIRPFVL RRLKKDVAKQ LPRKVEHVIH CQLSRRQQSL
YESFLAQSST RSAMSQSNGN FLSLMNILMQ LRKVCNHPDL FQARPIASPL DLPVRYFRLP
SRMYALTDEP WRLSYACTGL VDREGAFSDT YARQKRLFVE DLHVEAHGPL VCDAWMESIL
NAERSDLQAR RRSLERVYRL WHALNGSPVF GVDRRRAVSM PMLISAAMHV HKARSQARSE
MDHWLGSSLW KPLVRSPEER IAHVIDRMQF CVCVVPKARA RRPFLRPFGR GFPGFLTHLR
RRENMERAMV PLAAKLVRPY HSMYSRTQMS FPDKKLVQFD CGKLQELAVL LCRLRREGHR
CLIFTQMTSM LNILEQFLNL HGHTYFRLDG STRVEKRQML MEKFNQDSSI FCFILSTRSG
GLGINLTGAD TVIFYDSDWN PAMDAQAQDR AHRIGQTREV HIYRLVTLST VEDNILRKAQ
QKRNLETLVM TKGQFTTDFF SSWSLCELVR GPEALVEMED EEVAFKGEDL DLERMMANVE
DEDDVIAMRD AKAQALQEEL EFQDDKSVDS ESIPMEGFKL EDSLTRVHQY ALQYQRNATP
ISLQAIEHEM EAQAMERACD VERVEELKSL EDVALIEQGD LIAGVDDLQD TESYADFFKR
KRSDVHFQRR KRQLTGAAWQ SLRCKDTRHR FYYNVDTKQA VWDAPSILVE MEMYQYAKRY
KFAGLPTRVM LGMLLYLKEL HRIQSVRLVC RSWKLAADNP QLCRRLHATD AWKHAIESAC
VGETILLASG VYELDEKLCI RRPIRLLAAE DAHVELVMRS PTAQLCWEAN GGLLQGFYLA
RRSQVCGTAW QHLLCVSGGV RVVYCDFDGL SGNACIAVRG SSRCISKVYF QQNRIMNGST
GILIAKPDCQ VILHGNSIVQ NRIAGVVVLA GHVLLKQNKI ACNGRFGVRL MYHAGNVIVE
DNVFSQHLCK SLDVEKSARR FVVRWNVGIT RDQDETEMEP LPHHHGTVRV WTYAVKPRPP
VLNLCSPYSM MQTLLKARMG LPGRPQVEYE RVLMQLQSTC EIEEKIQRPK KQSKEAQAAN
LNI
//
