ID A0A0F4ZB32_9PEZI Unreviewed; 989 AA.
AC A0A0F4ZB32;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Helicase C-terminal domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=TD95_005386 {ECO:0000313|EMBL:KKA27068.1};
OS Thielaviopsis punctulata.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Microascales; Ceratocystidaceae; Thielaviopsis.
OX NCBI_TaxID=72032 {ECO:0000313|EMBL:KKA27068.1, ECO:0000313|Proteomes:UP000033483};
RN [1] {ECO:0000313|EMBL:KKA27068.1, ECO:0000313|Proteomes:UP000033483}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CR-DP1 {ECO:0000313|EMBL:KKA27068.1};
RA Radwan O., Al-Naeli F.A., Rendon G.A., Fields C.;
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KKA27068.1}.
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DR EMBL; LAEV01001905; KKA27068.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F4ZB32; -.
DR OrthoDB; 5482994at2759; -.
DR Proteomes; UP000033483; 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:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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; 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 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 PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
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:UP000033483}.
FT DOMAIN 436..610
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 803..969
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 124..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 177..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..66
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 177..191
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..217
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 989 AA; 111218 MW; B81EADD0783D4DF0 CRC64;
MPNPRFTSPE FRDSQEEREE QEQEENESPY VETVPLDLVI PCSSPLQRTQ PLADSYPPPA
PRSPTPIRSS SPIASMIEVP RSSPLQPARA PPPTKQGTLS MFFKPKPVAA VTTKTNPAKR
TFDAIEISDD EDEAEDDRAD IRRTQFVASS KDKPVSSAKK LKSLDFARLD ISSYEYVAPS
PKSSNSPGFK DAPQPPSRVN CPPALQSPEP TPITSSPEKP RPRRRLVRGL RPERSVSPDP
VQEPIRLTTP LPVKKKLAPM YNVVSSDDEL NDDDAFVGRE SSPEIIGKSG NNIVDLLNAI
EMSDLVALTG DKEDTLAYLT KQRPFKSIAQ IKGISKKKTV RGKSQMVNIG ADIVEKVSSF
SRAINAVDMI VIESDRRAQL IKHEIECWGV DNVGKKTERS ANKTRSGGLW RPGQPVGMNA
SLPMHDYQVF GVNWMNMLSR KGFGGILADD MGLGKTCQVI GLMCRLAQDY DEGIVDDMPF
PNLIVVPPST LDNWLAEFSK FAPDLVVTKY SGSQETRNLI VDDMLNDEEV HHVVLTSYTQ
LSSNLDIQNM NRLSIRNAIF DEGQVLKNPT TKQYQRLARL RVHWRLLLSG TPIQNHLMEM
ISLLSFVDPD LFAAHMEDIQ YVFDHKIHSK NLSNTALLYG ERVNRARSIL EPFILQRLKH
QVGQNLPEKT QRIVHCDLPL EQRKLYNKYE ELFRNEGEQK GVAKKAGARE NDMNNVWIQL
KKAALHPQLF RQHFTDSMVH DMAKVLYNKV DHRELDLAES KFELLHNDMR SRSDFDLHLY
CSDFPKYLKQ YDIEVGSWKN SGKVQRLLEM IDEYRKNGDR ALVFSKFSMV IDILSYTLNR
DGIPHCQLTG QSAVGDRQAE INRFQKNADI PVFLLTTGAG GTGINLTAAN KVIIFDMSSN
PQDDKQAENR AHRLGQTRPV EVIHLIARNT VEELIYLTCQ KKIELADKVI TSGAGTGSAA
ANDAASELQL KNRVRDMMDQ GFTTELDKA
//
