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Database: UniProt
Entry: V5FV07_BYSSN
LinkDB: V5FV07_BYSSN
Original site: V5FV07_BYSSN 
ID   V5FV07_BYSSN            Unreviewed;      1172 AA.
AC   V5FV07;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   SubName: Full=SNF2 family helicase/ATPase {ECO:0000313|EMBL:GAD92427.1};
GN   ORFNames=PVAR5_1018 {ECO:0000313|EMBL:GAD92427.1};
OS   Byssochlamys spectabilis (strain No. 5 / NBRC 109023) (Paecilomyces
OS   variotii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Thermoascaceae; Paecilomyces.
OX   NCBI_TaxID=1356009 {ECO:0000313|EMBL:GAD92427.1, ECO:0000313|Proteomes:UP000018001};
RN   [1] {ECO:0000313|Proteomes:UP000018001}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=No. 5 / NBRC 109023 {ECO:0000313|Proteomes:UP000018001};
RX   PubMed=24407650; DOI=10.1128/genomeA.01162-13;
RA   Oka T., Ekino K., Fukuda K., Nomura Y.;
RT   "Draft genome sequence of the formaldehyde-resistant fungus Byssochlamys
RT   spectabilis No. 5 (anamorph Paecilomyces variotii No. 5) (NBRC109023).";
RL   Genome Announc. 2:E0116213-E0116213(2014).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC       {ECO:0000256|ARBA:ARBA00007025}.
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:GAD92427.1}.
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DR   EMBL; BAUL01000025; GAD92427.1; -; Genomic_DNA.
DR   AlphaFoldDB; V5FV07; -.
DR   eggNOG; KOG1001; Eukaryota.
DR   HOGENOM; CLU_000315_2_7_1; -.
DR   InParanoid; V5FV07; -.
DR   OrthoDB; 200191at2759; -.
DR   Proteomes; UP000018001; 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; cd18008; DEXDc_SHPRH-like; 1.
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   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 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; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR45626:SF51; SINGLE-STRANDED DNA-DEPENDENT ATPASE (EUROFUNG); 1.
DR   PANTHER; PTHR45626; TRANSCRIPTION TERMINATION FACTOR 2-RELATED; 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.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Helicase {ECO:0000313|EMBL:GAD92427.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018001};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT   DOMAIN          533..723
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          885..948
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          996..1165
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          17..141
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        79..102
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        116..141
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1172 AA;  130546 MW;  783659BC28F67F0E CRC64;
     MSSHAAMLLD PRAFRKQQIA NGNNREFPSS AHLTRGADNM RASSEPPVAL PPSISLSHLE
     PLDQGIKQSD LHMEGKRQQD AASSVNPAAP AGTTSTAHQL LNPRGGVKSR PRARSHSNPP
     KSATESNITA TKSTPAKPEM QFQFTTTEQN DSGDDSDGKR NFDQVENALV AGHKNLIEDM
     YGVERRSEQP QKRLKILKEQ EEKPVANKKS NFSMSGNVGL GEWMKEDKET SDRSTAVTPD
     VVDLTLDSVS AAAADDDLQV TGANDLSNQR VCYGKIESAS IQAHMVPKPS AKSIFGDSLH
     DWPSIRLGIH HQPSMGNRIE VSDPHNHVFG AVDAKTAAAI VPLLDTPALK VDISARLDVR
     KKSPDEWPWQ QCSALYRASI NLYGLRRNAE LVGRHLGQHN VWLGTPSLVE QGVPVFNPHA
     ERRRAQISHV PAAARGRPGV SYEVRTAEEV NNAVMKMFDQ LKSADNIPEM EPSPLIVTPL
     LRHQKQALWY MTEKEKPRKF GPNEEDNNSL WRLEYRGNGV KRYREIITGM ILSEEPPQTL
     GGLLADMMGL GKTLSILSLV MATLPESRNW EQMIPSADLV RGSPGIRNTR TTLLVSPLSA
     VNNWVTQIKE HLTEGAISYY VFHGPSRTTD VDELAKYDLV ITTYSIVLSE LSRRGSKRGV
     SPLTKMNMFR IVLDEAHTIR EQNAAQTQAI LRLNAARRWS VTGTPIQNRL EDLISVTKFL
     RLFPYDDRST FSAAILSKFK SGDANVLASL RVFVDSFTLR RVKDKIDLPP RHDKIVSLTF
     SEKEKELHDF FKRESNVMMN VIAGESKTKM GGRMYHHVLK AMMILRQVSA HGKELLDKED
     RERIKGLSVH DAIDLEEGAN DPPAATDRKA YEMFSLMQDS SADICASCGK HLEEKYSETG
     AVDKKEPIAV VLPCFDVVCT DCFSAWKDLF HGQPDSSSVN QIRCPVCEGW IPSAYSTITP
     LGFQEYWETQ AQAKQSRKHA KSLGEYEGPH TKTKALISHL LDTVEENKAL GENERPIKSV
     IFSAWTSHLD LIEIALNDNG ITGYTRLDGT MSLAARNKAL NTFRDDDRIT ILLATIGAGG
     VGLNLTSASK VYVMEPQYNP AAVAQAVDRV HRLGQTREVT TIQFIMKDSI EEKIAELAKR
     KQQLADMSMN RGRIDKKDVQ EQRMREYRSL FK
//
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