ID A0A3F3PX30_9EURO Unreviewed; 1756 AA.
AC A0A3F3PX30;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Vacuolar protein 14 C-terminal Fig4p binding-domain-containing protein {ECO:0000313|EMBL:RDH31520.1};
GN ORFNames=BDQ94DRAFT_160522 {ECO:0000313|EMBL:RDH31520.1};
OS Aspergillus welwitschiae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1341132 {ECO:0000313|EMBL:RDH31520.1, ECO:0000313|Proteomes:UP000253729};
RN [1] {ECO:0000313|EMBL:RDH31520.1, ECO:0000313|Proteomes:UP000253729}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 139.54b {ECO:0000313|EMBL:RDH31520.1,
RC ECO:0000313|Proteomes:UP000253729};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the VAC14 family.
CC {ECO:0000256|ARBA:ARBA00010225}.
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DR EMBL; KZ852054; RDH31520.1; -; Genomic_DNA.
DR STRING; 1341132.A0A3F3PX30; -.
DR OrthoDB; 5480555at2759; -.
DR Proteomes; UP000253729; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0070772; C:PAS complex; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0016817; F:hydrolase activity, acting on acid anhydrides; IEA:InterPro.
DR GO; GO:0006661; P:phosphatidylinositol biosynthetic process; IEA:InterPro.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR021133; HEAT_type_2.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR013967; Rad54_N.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR InterPro; IPR026825; Vac14.
DR InterPro; IPR021841; VAC14_Fig4p-bd.
DR PANTHER; PTHR16023:SF0; PROTEIN VAC14 HOMOLOG; 1.
DR PANTHER; PTHR16023; TAX1 BINDING PROTEIN-RELATED; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF08658; Rad54_N; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR Pfam; PF12755; Vac14_Fab1_bd; 1.
DR Pfam; PF11916; Vac14_Fig4_bd; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS50077; HEAT_REPEAT; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000253729};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 236..414
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 569..722
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REPEAT 908..943
FT /note="HEAT"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00103"
FT REGION 814..839
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1102..1122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1261..1311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1600..1625
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1644..1756
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 821..839
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1107..1122
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1273..1304
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1600..1619
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1657..1679
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1756 AA; 195926 MW; 0859C7CF33D52AF2 CRC64;
MTFLRSPCTL SLRIQVPATA RREPRCSTNS VDRLSKPFKC PGIATATRTS DKPARKRRKV
NYAGADGTVD DDSVKPYTNE DRLALATRDA NRFPSFKVKD KEMTFKQRFK IPLINKSSDA
YNSSRPAPTL GMRQGATFVV KPLHDPSGEF AIVLYDPTVD DVNEPEVKER ATADTEEQKP
KLDEPLVHKS LADILGLKKK TEGRPKVPVV IDPRLAKVLR PHQVEGVKFL YRCTTGMVDK
NANGCIMADG MGLGKTLQCI SLMWTLLKQS PEAGVTTIQK CIIACPSSLV GNWANELVKW
LGKDAITPFA VDGKASKTEL ISQMKQWAIA SGRAIVRPVL IISYETLRLY VDTLRDSPIG
LLLCDEGHRL KNKESLTWTA LNGLNVQRRV ILSGTPIQND LSEYFALLHF ANPNLLGSQN
EFRKRFELPI LRGRDAAGTE EDLKKGDERL AELSGIVNKF IIRRTNDILS KYLPVKYEHV
VFCNMSAFQL GLYKHFIQSP EIKSLLRGKG SQPLKAIGLL KKLCNHPDLL NLSNDLPGCE
YTFPEDYVPP EARGRDRDIK SWYSGKMMVL DRMLARIRQD TNDKIVLISN YTQTLDLFEK
LCRTRGYGSL RLDGTMTVGK RQKLVDKFNN PDGEEFVFLL SSKAGGCGLN LIGANRLVLF
DPDWNPAADQ QALARVWRDG QKKDCFVYRF IATGSIEEKI FQRQSHKQSL SSCVVDSAED
VERHFSLESL RELFQFKPET RSDTHDTFKC KRCRPDGTQY IKAPAMLYGD TSTWNHFVND
GEQGALSKIQ DLLIRQETGE RDVSAVFQSL RTRESRDRRL TAQPSQTSPS RHENHLSTST
TPELTIMWRV ANAHGIITRL EKVVRDAAFR GEHEEIQKIV DQLCHDYAYA VHQPHARNGG
VAPYLKEIVP PVLACFSDQD ARVRYYACES MYNIAKVAKG EVLLFFNDIF DALSKLASDS
ELSVKNGAEL LDRLVKDIVS ESAASHISVL QLSEKEATDP EGLDDAELPT AFSLPKFIPL
LKERIHVISA FTRTFLVSWL TLLDTIPDLE LISYLPEFLG GLIKFLGDPN RDVNVATQAL
LDRFLSEIKR IARLKKGIEE SRKGQGSDIR QSATSDSMSV ATTTDQTVAV ESEVTDNAIE
DSEAGSVTDE EGLHVDGDWI PGQDVQIDYA KILDILVGFV DTSFVEEMQL TALRWIDNFF
EISPEDILPF VPRLLTQVLP AMSSGSDQVR QAANRVNTSL MEYIVTLSED ILDESRQMVL
KNNSKENTER RSSTPVSKPP ETPSSESKKQ LSQPEASVEP TPRSSISTPL PPADLDYAAA
VNSLTLQFLN ENEATRVAAL SWLIMLHRKA PKKVIAFNDG TFPALLKTLS DPAEAVVTKD
LQLLSQISRN SEDSYFKSFM VNLLQLFSTD RHLLEVRGNL IIRQLCMNLS PERIYRTLAD
CLEKEEDIEF ASIMVQNLNN NLITAPELSE LRKRLRNLDA KDGQMFFVAL FRSWCHNAVS
TFSLCLLAQA YEQAYNLLQV FAELEMTVNM LIQIDKLVQL LESPVFTYLR LQLLEPERYP
YLYKCLYGVL MLLPQSSAFA ALKNRLNSVS SIGLIHTGPR QTTLSSSTST SSTSTYDRST
NSRLKRDDPP IRWVELLDKF KTVQEKARRS QRASQRPFDA DGPSSSSNNN NNNAGDQVRG
GGGSTRDRVS ALPDTPRGIV GGNTGGGGNE GGSGRGTNEG GAGKSSPGGI LGGAHRHKSS
LSNLGRLGIG GRKSKR
//
