ID S0E2D0_GIBF5 Unreviewed; 1157 AA.
AC S0E2D0;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=Related to RAD5-DNA helicase {ECO:0000313|EMBL:CCT68860.1};
GN ORFNames=FFUJ_07681 {ECO:0000313|EMBL:CCT68860.1};
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:CCT68860.1, 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; HF679027; CCT68860.1; -; Genomic_DNA.
DR AlphaFoldDB; S0E2D0; -.
DR STRING; 1279085.S0E2D0; -.
DR EnsemblFungi; CCT68860; CCT68860; FFUJ_07681.
DR VEuPathDB; FungiDB:FFUJ_07681; -.
DR HOGENOM; CLU_000315_2_5_1; -.
DR OrthoDB; 200191at2759; -.
DR Proteomes; UP000016800; Chromosome 5.
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:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IEA:InterPro.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd18008; DEXDc_SHPRH-like; 1.
DR CDD; cd16572; RING-HC_SpRad8-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; IPR014905; HIRAN.
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:SF22; DNA REPAIR PROTEIN RAD5; 1.
DR PANTHER; PTHR45626; TRANSCRIPTION TERMINATION FACTOR 2-RELATED; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF08797; HIRAN; 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; SM00910; HIRAN; 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 Helicase {ECO:0000313|EMBL:CCT68860.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000016800};
KW Zinc {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-ProRule:PRU00175};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 508..718
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 902..947
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 988..1147
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 142..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 370..409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..35
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..176
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 370..389
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1157 AA; 130348 MW; DF48D42F4A1697CE CRC64;
MTLSYQKKHP DDHIDPEPPA KRRRFFADPD ELSSDPVSHD QSPLSQPKRF FKDEDDVEEE
DEYKDNFGET HDDDLPVTSP SRPPALQQES SVSFDQETFE AFVGDKVSTD VLSAIRDHCG
NDLERAVNMY FDGTYKKFVK KPPWKTPLRP ASTTSSSRSP SVPNERKPSI KTSQRMPKQR
YIGAFGVEGW ATRSGVNVLK HGDAVKIERQ KLQPPQSVRG KGKTGQVTPS RGFAAAAARR
VDVIVRFTTQ NGSEVGRLAK ETANWVSALI DEKVCKFEGT VVYAPERIRT NDTIFLQLRC
SLLDSAFFSR SFKLADDRSA AFFEQNETND EKTLRLRQVA LVKLFQEINL QPTMSNSAAE
DGRKGLLQAA EQDEQKQKEA KKANGDANRN GKEADSSQSS ETEEGEELEQ DQLDALYKKA
QSFDFSTPEA EPADTFAMTL RSYQKQALHW MMAKEKDEKS NREPSMHPLW EEYDWPLKDV
DDKNVPQVEG QPKFYVNPYS GDLSLDFPVQ EQHCLGGILA DEMGLGKTIQ MLSLVHTHRS
EIALEARRAA VELSSVNQLT RLGKNSESVL DAPCTTLVIA PMSLLSQWQS EAAKASKDGT
MKIELYYGNE KSSNLQALCC ASNASNAPDL VITSYGVVLS EFSSIAARKG DKSFHNGLFS
LKFFRIIIDE AHHIKNRSSK TAKACYEISA YHRWALTGTP IVNKLEDLFS LVRFLGVEPW
NNFSFWRTFI TVPFESGDFM RALDVVQTVL EPLVLRRTKD MKTPDGKPLV LLPPKQVEIV
DVELSETERD VYSYIFNKAK RTFSQNVEAG TVMKAFTTIF AQILRLRQSC CHPILVRNRD
TVADEEEAGA AADAAAGLAD DMDLESLITS FTAETDEASK ETNQTFGAHA LEQIRDEAEN
ECPLCFEEPM NDQTVTGCWH SACKKCLLDY IKHQIGKGEV PRCFSCREPI NKRDLFEVIR
HDDDPDMMMS KKPKISLQRV GVNASSAKVV ALMSELRNLR REHPKMKSVV FSQFTSFLSL
IEPALTRANI KFLRLDGSMA QKARAAVLNE FTERKGFTIL LLSLRAGGVG LNLTTAGRVF
MMDPWWSFAV EAQAIDRVHR MGQESEVQVK RFVVKESVEE RMLKVQERKK FIATSLGMMS
DEEKKLQRIE DIKELLS
//
