GenomeNet

Database: UniProt
Entry: A0A0F4GS49_9PEZI
LinkDB: A0A0F4GS49_9PEZI
Original site: A0A0F4GS49_9PEZI 
ID   A0A0F4GS49_9PEZI        Unreviewed;       751 AA.
AC   A0A0F4GS49;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=DNA repair and recombination protein rad54 {ECO:0000313|EMBL:KJY00247.1};
GN   ORFNames=TI39_contig338g00026 {ECO:0000313|EMBL:KJY00247.1};
OS   Zymoseptoria brevis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX   NCBI_TaxID=1047168 {ECO:0000313|EMBL:KJY00247.1, ECO:0000313|Proteomes:UP000033647};
RN   [1] {ECO:0000313|EMBL:KJY00247.1, ECO:0000313|Proteomes:UP000033647}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Zb18110 {ECO:0000313|EMBL:KJY00247.1,
RC   ECO:0000313|Proteomes:UP000033647};
RA   Grandaubert J., Bhattacharyya A., Stukenbrock E.H.;
RT   "RNA-seq based gene annotation and comparative genomics of four
RT   Zymoseptoria species reveal species-specific pathogenicity related genes
RT   and transposable element activity.";
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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:KJY00247.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LAFY01000330; KJY00247.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F4GS49; -.
DR   STRING; 1047168.A0A0F4GS49; -.
DR   OrthoDB; 5480555at2759; -.
DR   Proteomes; UP000033647; 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: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:UP000033647}.
FT   DOMAIN          234..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          1..73
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        47..73
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   751 AA;  84512 MW;  23B796C993104E54 CRC64;
     MTVADKENVP PPVAKVRGRL YGGTPQSVDR LIKPFKCPGT STPTRASEKP ARKRRKVDYA
     GGDGSVEEGD KPYTNEDRLA LATRDVNRFP VFKPKDKDSA FRSRFAVPLK NKDTTSYNSS
     RPPPLLGLRA GTVFVAKPLH DPTGEFAIVL FDPTVDGKVE LKEIEDGKDG VEGSQKKKLD
     EPLMHKSLAD ILGIKKVVDT ERPKVPVVID PRLAKVLRPH QVEGVKFMYR CTTGLIDANA
     EGCIMADEMG LGKTLQCITL MWTLLKQSPE AGKSTIQKCV IACPSSLVRN WANELVKWLG
     PDAINPFAVD GKASKEELTQ QMRSWASATG RAVTRPVLIV SYETLRLYVD ELRTPIGLML
     CDEGHRLKNG ESQTFEALNR LNVSKRVILS GTPIQNDLSE YFALLTFANP GYLGTRLEFR
     KKFEIPILRG RDASGTEADQ QKGNERLKEL LELVNKFIIR RTNDILSKYL PVKYEHVVFC
     NLAPFQLDLY NYFIKSPEIQ SLLRGKGSQP LKAIGLLKKL CNHPDLLNLP DDLPGCDSHF
     PEDFVPKDAR GRDRDVKPWY SGKMQVLDRM LARIRQDTND KIVLISNYTQ TLDVFEKLCR
     NRSYGCLRLD GTMAVNKRQK LVDKFNNPDG EEFVFLLSSK AGGCGLNLIG ANRLVLFDPD
     WNPAADQQAL ARVWRDGQKK DCFVYRFIAT GTIEEKIFQR QSHKQSLSSC VVDSAEDVER
     HFSLDSLREL FQYRPNTTSD THDTFKFGII L
//
DBGET integrated database retrieval system