ID C9SIS0_VERA1 Unreviewed; 969 AA.
AC C9SIS0;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE SubName: Full=Helicase SWR1 {ECO:0000313|EMBL:EEY18843.1};
GN ORFNames=VDBG_04952 {ECO:0000313|EMBL:EEY18843.1};
OS Verticillium alfalfae (strain VaMs.102 / ATCC MYA-4576 / FGSC 10136)
OS (Verticillium wilt of alfalfa) (Verticillium albo-atrum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX NCBI_TaxID=526221 {ECO:0000313|Proteomes:UP000008698};
RN [1] {ECO:0000313|Proteomes:UP000008698}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VaMs.102 / ATCC MYA-4576 / FGSC 10136
RC {ECO:0000313|Proteomes:UP000008698};
RX PubMed=21829347; DOI=10.1371/journal.ppat.1002137;
RA Klosterman S.J., Subbarao K.V., Kang S., Veronese P., Gold S.E.,
RA Thomma B.P.H.J., Chen Z., Henrissat B., Lee Y.-H., Park J.,
RA Garcia-Pedrajas M.D., Barbara D.J., Anchieta A., de Jonge R., Santhanam P.,
RA Maruthachalam K., Atallah Z., Amyotte S.G., Paz Z., Inderbitzin P.,
RA Hayes R.J., Heiman D.I., Young S., Zeng Q., Engels R., Galagan J.,
RA Cuomo C.A., Dobinson K.F., Ma L.-J.;
RT "Comparative genomics yields insights into niche adaptation of plant
RT vascular wilt pathogens.";
RL PLoS Pathog. 7:E1002137-E1002137(2011).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; DS985218; EEY18843.1; -; Genomic_DNA.
DR RefSeq; XP_003005346.1; XM_003005300.1.
DR AlphaFoldDB; C9SIS0; -.
DR STRING; 526221.C9SIS0; -.
DR GeneID; 9536763; -.
DR KEGG; val:VDBG_04952; -.
DR eggNOG; KOG0389; Eukaryota.
DR HOGENOM; CLU_000315_16_2_1; -.
DR OMA; ELQAYND; -.
DR OrthoDB; 5482994at2759; -.
DR Proteomes; UP000008698; Unassembled WGS sequence.
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:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR CDD; cd17919; DEXHc_Snf; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 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; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR InterPro; IPR009060; UBA-like_sf.
DR PANTHER; PTHR10799; SNF2/RAD54 HELICASE FAMILY; 1.
DR PANTHER; PTHR10799:SF964; SWI_SNF-RELATED MATRIX-ASSOCIATED ACTIN-DEPENDENT REGULATOR OF CHROMATIN SUBFAMILY A CONTAINING DEAD_H BOX 1; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF46934; UBA-like; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000313|EMBL:EEY18843.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000008698}.
FT DOMAIN 482..656
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 793..962
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 89..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 201..280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 424..456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..221
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 427..453
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 969 AA; 108075 MW; DE3DF5E351A9EF95 CRC64;
MAGLAAGFSS SPPGRGFDDD DDDELARDTI PCSPYATQAT QVINRTSLLP KHTEAPSSPL
ASSVVEVPAS SPFQPKPSKA PFATRLAPAG TLFRPPPQLP RGIKRPAAEP IMISSDDEKS
PSRGDIQPTA FKKRMTAFHY EPTERIDKLE KMTALTEQVS TATGQSFPSR ACREALMACH
NNVSDAVNYL YEGKHLQKEK KHGATSAPLS AASTNPLKSK PSLAAKGNGA DFYQTPNLSP
RTPSPAKQAK PRRRLVQGRR PNRSPSPPTS QPVPEAREVI NVDDEVDEIA EDRIVIADDK
DDDYDNEDDL MEATVKESLY DKALNTINNS SIDDLSAMTN LKQDELQIIA TKRPFHDIDQ
VERVTAAKKS NGRKSNKAAI GELLVEAIME FTKAVNAIDT VVAECEKKAV RVKSEMSMWD
IDLKGHARSG TTSQTDSDDL PMTPNSSKGQ KYSPPPIPRQ PALLEGHCTM RPFQLYGLNW
MSVLYNSGYG CILADEMGLG KTCQVISLMA HLVESYDEEK DEKRPWPNLI VVPPSTLSNW
EVEFEKFAPD LSVLTYKGSQ SDRAMIAEDM LSAPEEYHVV LTSYTQVGKE EDIDALMELR
PNAAIFDEGH KMKNPKTKIY KDLIRIKADW RMLLTGTPVQ NNLMEMLSLL NFIDPKMFKG
HMEHLQYMFS QKVTTRDVNN GAFLYKRSVS AGDRTISRSC SFLQRRKQQV LSGMPNKDVQ
RRLLRAAASQ KALYDELETM FKSGPSELQQ PNMEHLIGEL KNCSDFELHL WCRDYKCLEG
FDLPEGSWME SGKVTKMLEL IHQYQANGDR VLVFSKFAKV IEILREVLHT DGIKHCVLYG
ATSVEERQGL INEFNENTDI PVFLLTTGAG GTGINLTSAN KVIIFDQSDN PQDDIQAENR
AHRLGQTRDV EVIRLLTRRT IEELIFKACE KKIELANKVT GAVEDLGTNA EINLEKEVRR
MLADQLTPP
//
