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Database: UniProt
Entry: S0E1K0_GIBF5
LinkDB: S0E1K0_GIBF5
Original site: S0E1K0_GIBF5 
ID   S0E1K0_GIBF5            Unreviewed;       805 AA.
AC   S0E1K0;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   SubName: Full=Probable Rad54 homolog MUS-25 {ECO:0000313|EMBL:CCT67542.1};
GN   ORFNames=FFUJ_13668 {ECO:0000313|EMBL:CCT67542.1};
OS   Gibberella fujikuroi (strain CBS 195.34 / IMI 58289 / NRRL A-6831) (Bakanae
OS   and foot rot disease fungus) (Fusarium fujikuroi).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium fujikuroi species complex.
OX   NCBI_TaxID=1279085 {ECO:0000313|EMBL:CCT67542.1, ECO:0000313|Proteomes:UP000016800};
RN   [1] {ECO:0000313|Proteomes:UP000016800}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 195.34 / IMI 58289 / NRRL A-6831
RC   {ECO:0000313|Proteomes:UP000016800};
RX   PubMed=23825955; DOI=10.1371/journal.ppat.1003475;
RA   Wiemann P., Sieber C.M., von Bargen K.W., Studt L., Niehaus E.M.,
RA   Espino J.J., Huss K., Michielse C.B., Albermann S., Wagner D.,
RA   Bergner S.V., Connolly L.R., Fischer A., Reuter G., Kleigrewe K., Bald T.,
RA   Wingfield B.D., Ophir R., Freeman S., Hippler M., Smith K.M., Brown D.W.,
RA   Proctor R.H., Munsterkotter M., Freitag M., Humpf H.U., Guldener U.,
RA   Tudzynski B.;
RT   "Deciphering the cryptic genome: genome-wide analyses of the rice pathogen
RT   Fusarium fujikuroi reveal complex regulation of secondary metabolism and
RT   novel metabolites.";
RL   PLoS Pathog. 9:E1003475-E1003475(2013).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; HF679026; CCT67542.1; -; Genomic_DNA.
DR   AlphaFoldDB; S0E1K0; -.
DR   STRING; 1279085.S0E1K0; -.
DR   EnsemblFungi; CCT67542; CCT67542; FFUJ_13668.
DR   VEuPathDB; FungiDB:FFUJ_13668; -.
DR   HOGENOM; CLU_000315_10_2_1; -.
DR   OrthoDB; 5480555at2759; -.
DR   Proteomes; UP000016800; Chromosome 4.
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:0016817; F:hydrolase activity, acting on acid anhydrides; IEA:InterPro.
DR   CDD; cd18793; SF2_C_SNF; 1.
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; 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   PANTHER; PTHR45629:SF7; DNA EXCISION REPAIR PROTEIN ERCC-6-RELATED; 1.
DR   PANTHER; PTHR45629; SNF2/RAD54 FAMILY MEMBER; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF08658; Rad54_N; 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   Helicase {ECO:0000256|ARBA:ARBA00022806};
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:UP000016800}.
FT   DOMAIN          233..411
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          566..719
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          18..76
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        48..76
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   805 AA;  90571 MW;  4F88779A3BC12188 CRC64;
     MGAVSPIVAT PLAGKDKILG KRMPTPSSID RLHKPFKCPG VAGRSPAVDR PSRKRRKVDY
     GGADGEADND KPYSNDDRLA LATRDINRFP VFQAKDKGLV FRKAFSVPLK NKDSAAYNPN
     RAPPTLGLRQ GAVFIAKPLH DPSGEFAIVL HDPTVDDKPK DVPKAIEPAR TEAADGKLDA
     PLVHKSLAEI LGIKKKVDGE HPRVPVVIDP KLAKILRPHQ VEGVKFMYRC VTGLIDEKAN
     GCIMADEMGL GKTLQCISLM WTLLKQSPDA GKPTIQKAIV VCPASLVKNW ANELVKWLGP
     NAINPFAIDG KASKEELTRQ LRQWAIASGR AVTRPVIIVS YETLRLNVEE LKHTKIGLLF
     CDEGHRLKNS DSNTFNALNS LNVSRRVILT GTPIQNDLTE YFSLTSFANP DLLGTRLEFR
     KRYEIPILRG RDADASEEDR KKGDECTAAL LNVVNKFLIR RTNDILSKYL PVKYEHVVFC
     NLAPFQFDLY NYFIKSPDIQ ALLRGKGSQP LKAINILKKL CNHPDLLNMA DDLPGSEQCF
     PDDYVPKESR GRDREIKSWY SGKMAVLDRM LARIRQDTND KIVLISNYTS TLDLFERMCR
     SRQYGCLRLD GTMNVNKRQK LVDRFNDPEG DEFVFLLSSK AGGCGINLIG ANRLVLFDPD
     WNPAADQQAL ARVWRDGQKK DCFVYRFIAT GTIEEKIFQR QSHKQSLSSC VVDSAEDVER
     HFSLDSLREL FQYRPDTKSD THETFKCKRC KPDGKQYIKA PAMLYGDTST WNHFVNEGLK
     PIQDLLLRQE YGESEVSAVF QYISH
//
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