ID S0E5J9_GIBF5 Unreviewed; 1134 AA.
AC S0E5J9;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Related to DNA repair protein RAD16 {ECO:0000313|EMBL:CCT70026.1};
GN ORFNames=FFUJ_05960 {ECO:0000313|EMBL:CCT70026.1};
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:CCT70026.1, 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}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC {ECO:0000256|ARBA:ARBA00007025}.
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DR EMBL; HF679028; CCT70026.1; -; Genomic_DNA.
DR AlphaFoldDB; S0E5J9; -.
DR STRING; 1279085.S0E5J9; -.
DR EnsemblFungi; CCT70026; CCT70026; FFUJ_05960.
DR VEuPathDB; FungiDB:FFUJ_05960; -.
DR HOGENOM; CLU_000315_2_0_1; -.
DR OrthoDB; 200191at2759; -.
DR Proteomes; UP000016800; Chromosome 6.
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 GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR CDD; cd18008; DEXDc_SHPRH-like; 1.
DR CDD; cd16449; RING-HC; 1.
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 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; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45626:SF24; ATP-DEPENDENT HELICASE ULS1; 1.
DR PANTHER; PTHR45626; TRANSCRIPTION TERMINATION FACTOR 2-RELATED; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF57850; RING/U-box; 1.
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 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:UP000016800};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT DOMAIN 426..616
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 774..826
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 965..1122
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 59..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 174..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 848..925
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..76
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..130
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..207
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 866..880
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 894..908
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1134 AA; 127338 MW; 416162F9A1091155 CRC64;
MAATTSMSVE EIHEELTVQK VVLESLSEAT YDGAEDMRQE AHSEIVRLKK LLQTLKLKKE
PGTTTGESHH HVPKDRFLGS STLGDGEPEA SKAMQSPSRH GVWRLPDRKR GADSARLSFH
DNHAKARRIS PEDNTFSTAM AYSNDYDHID FIDLTGDDDD IGSDFIAEQL KAEERQKQEW
ADQQLARQLS SQSSSNQPSG SQSSQNNAFT RLMNSQPALS TPLDDADDDL FRIPGAYDAR
WDDSSGAGPA FNIPQRRMAP QYIPVATSSN HNAIKDDPDL IFAGSVTRQP PTPSGRPILA
SGMNYPDLSR RHPGASPAGF WPNNYNSPGS SPHLSELANL TRWSNGLDFV SGLDADGESI
NPRAMNVARE AVNFHTPQLD QGELDALLKN ISADMDLPKA GLGEAPEGLK RPLYPHQDIA
LAWMKKMESG TNKGGILADD MGLGKTISTL SLLLDRRAST RPKTNLIVAP VALLRQWEEE
IATKTKPTHR LSVYVHHGKK ASIDELLRYD VVLTTYGTVA QELKRFEKIV EDHNERGGNI
NWNDTTISSK LSLLHPVKAQ FYRVILDEAQ CIKNKDTKGA KACTQLKSIH RWCLTGTPMM
NGIIELYSLV KFLRIKPYSK WEEFRQGFGV LFGRNGDPKH VAMDKLQALL KAIMLRRKKS
SKLNGKPILV LPEKTEEIIY AELSPEERDF YSQLEKHARV QFSKYLREGT VSKNYSNILV
LLLRLRQACC HPHLNLDVDE VASSSISDED KKQLVKELDQ AIVERIKEVE AFECPICYDA
VQCPSFFIPC GHDSCSECLV KIVESASAVN LQEGNESSRA KCPVCRGQFD PVKCFSYETF
REVHMPETIK KESNFEPAAD VSGSGDDSET ESESDYESDD EVDKNGNLKG FIVNDEFPDE
DEKVSVKKQS KGKGKRKNKG KGKSLDVKPA MLKTLRKEAY KNREAFKKYM RYLRKTWEPA
AKVTECMNLI KKIEETGEKT IIFSQWTLLL DLLQVAMSHE KMAKPERYDG SMSATLRNIA
AQNFRERRDT KVMLVSLRAG NAGLNLTAAS RVIIMDPFWN PYIEMQAVDR AYRIGQQQEV
KVYRILTKET VEDRIVELQN KKKEMVEAAL DETAGSKIGR LSINDLKNLF GFNR
//
