ID A0A423W9I2_9PEZI Unreviewed; 1072 AA.
AC A0A423W9I2;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=ATP-dependent helicase fft2 {ECO:0008006|Google:ProtNLM};
GN ORFNames=VMCG_06171 {ECO:0000313|EMBL:ROV99986.1};
OS Valsa malicola.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Valsaceae; Valsa.
OX NCBI_TaxID=356882 {ECO:0000313|EMBL:ROV99986.1, ECO:0000313|Proteomes:UP000283895};
RN [1] {ECO:0000313|EMBL:ROV99986.1, ECO:0000313|Proteomes:UP000283895}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=03-1 {ECO:0000313|EMBL:ROV99986.1,
RC ECO:0000313|Proteomes:UP000283895};
RA Yin Z., Huang L.;
RT "Host preference determinants of Valsa canker pathogens revealed by
RT comparative genomics.";
RL Submitted (SEP-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:ROV99986.1}.
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DR EMBL; LKEA01000022; ROV99986.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A423W9I2; -.
DR STRING; 356882.A0A423W9I2; -.
DR Proteomes; UP000283895; 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; 2.
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:UP000283895}.
FT DOMAIN 529..703
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 890..1056
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 253..377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..117
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..177
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..292
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..327
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 331..365
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1072 AA; 119782 MW; 78D8E11E37FC3EAE CRC64;
MNFSSPDRAV IPASSPVAGL HEDPITICDS SDDSQASPYF TQPTQVVNRP TLGANKRMET
QSTQIVDRPV LGLTSKARTS SVQPSSPRSA NEIEVPASSP FQKQPRTSPS KQISNLMAPA
GTFYRRPVNP PIVNKAGRRS TPEKRKHNDL SEDELNSSPR KRADSSSPER PARGDIQRSS
FERQGQRAVS PVKSKHISPV RKRGDQFNDK FDGRIQQLAN KARKELKGKH SLDLCANVMK
AYKGNYTSAL RTLSDMSPRP AKAVKSSSTS SSLSSTVASP SQPSRVSSQS SAPPRSPSPP
PKRRRLVRGR NPKTSTGSSQ DQQAPATLIS LVDDDDDEEE PISNDKDDGD NYQSDGEEES
AEESEGEGER PGKPAEKVLV GSKRTAKILQ YLNVCSIGSL TADAKIKKDE AKHMISKRPF
RSADQVKAVS NFKTIRGKKV KQPLGEEVFD ELVGYMKRLD AIDRIVEYCD TQGYRAKTKM
ACWKMDRTGR VNDSANSSGP ILPHPKEPKA LQGHCKMQPY QLFGMNWMWQ IYSQGLGGIL
ADDMGLGKTC EVVSFLALLK DMHDAGKIQG QKRPNLVVVP PSVLRNWALE FEKFAPELSV
ITYTGAPEVR DEIAYEIKEA PEEYDAILTS YSQMNRPRDT NAMNSIGINA AIFDEGHQLK
NPNAKIYNDL IRISADWKLI LTGTPIQNNI MEMMSLLKFL SPHVFQNDSR HIEELFAQRA
SLQEVSEGAV LLSDRVKRAR SILDPFILKR SKEEVMTDMP SKVRKLAYCE MHEGQKALYN
DLASKFRDAK AHKAMRGGRK NDMNNPWIQL RKAAIHPQLF RRFFDDRKCE EMAKILMDTV
SQDDLRQPNI QHLINELKGE SDFQLHLWCR DYPCIRKFDC PDDTWLESGK VEKLLGLIGE
FQKNKDRVLV FSRFSLVVSI LEECFAQAGI NYRVLQGETA VGQRQDIVDE FNADESITVF
LLTTKAGGTG LNLTSANKVI LFDQSDNPQD DIQAENRAHR MGQKREVEVV RLLSKGTIDE
LIYKACQKKL ELAGQITGHN EDISGEEVQA MVTKMLLEQP APGLVTPPKS EL
//
