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Database: UniProt
Entry: A0A2T2NF38_CORCC
LinkDB: A0A2T2NF38_CORCC
Original site: A0A2T2NF38_CORCC 
ID   A0A2T2NF38_CORCC        Unreviewed;       484 AA.
AC   A0A2T2NF38;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=ATP-dependent DNA helicase {ECO:0000256|RuleBase:RU364117};
DE            EC=3.6.4.12 {ECO:0000256|RuleBase:RU364117};
GN   ORFNames=BS50DRAFT_96831 {ECO:0000313|EMBL:PSN64054.1};
OS   Corynespora cassiicola Philippines.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Corynesporascaceae; Corynespora.
OX   NCBI_TaxID=1448308 {ECO:0000313|EMBL:PSN64054.1, ECO:0000313|Proteomes:UP000240883};
RN   [1] {ECO:0000313|EMBL:PSN64054.1, ECO:0000313|Proteomes:UP000240883}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Philippines {ECO:0000313|EMBL:PSN64054.1,
RC   ECO:0000313|Proteomes:UP000240883};
RX   PubMed=29551995; DOI=10.3389/fmicb.2018.00276;
RA   Lopez D., Ribeiro S., Label P., Fumanal B., Venisse J.S., Kohler A.,
RA   de Oliveira R.R., Labutti K., Lipzen A., Lail K., Bauer D., Ohm R.A.,
RA   Barry K.W., Spatafora J., Grigoriev I.V., Martin F.M., Pujade-Renaud V.;
RT   "Genome-Wide Analysis of Corynespora cassiicola Leaf Fall Disease Putative
RT   Effectors.";
RL   Front. Microbiol. 9:276-276(2018).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC         Evidence={ECO:0000256|RuleBase:RU364117};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU364117}.
CC   -!- SIMILARITY: Belongs to the helicase family. RecQ subfamily.
CC       {ECO:0000256|ARBA:ARBA00005446, ECO:0000256|RuleBase:RU364117}.
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DR   EMBL; KZ678139; PSN64054.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T2NF38; -.
DR   STRING; 1448308.A0A2T2NF38; -.
DR   Proteomes; UP000240883; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0006310; P:DNA recombination; IEA:InterPro.
DR   CDD; cd17920; DEXHc_RecQ; 1.
DR   CDD; cd18794; SF2_C_RecQ; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR004589; DNA_helicase_ATP-dep_RecQ.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR032284; RecQ_Zn-bd.
DR   NCBIfam; TIGR00614; recQ_fam; 1.
DR   PANTHER; PTHR13710:SF157; ATP-DEPENDENT DNA HELICASE Q-LIKE 3; 1.
DR   PANTHER; PTHR13710; DNA HELICASE RECQ FAMILY MEMBER; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF16124; RecQ_Zn_bind; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU364117};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU364117};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU364117};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU364117}; Nucleus {ECO:0000256|RuleBase:RU364117};
KW   Reference proteome {ECO:0000313|Proteomes:UP000240883}.
FT   DOMAIN          32..206
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          259..407
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
SQ   SEQUENCE   484 AA;  55308 MW;  0A1919E1CE9E5A92 CRC64;
     MPPKKKQHYD LDFTLRRVFG KRSFRPLQRE VVEATLEGED VFLQAATSFG KSLCYQLPAV
     VDFGITIVIS PLLALMNNQV ASMRKANIRV ETINSQTRPI DKRRIIEDLQ CGHPLTRLLY
     VTPEYCQLDS FRKLLRTVHS QRELARIAVD EAHCVSEWGH DFRPSFQQLS FFKTEFPDVP
     VICVTATATT RVRDDVIKTL ALDPLRLKIF RMTTSRPNLH YEIRFKSDEE DQYPDFLAWI
     KAAHARRASN PERVSQLATQ NQRADNVPGI IYTLFRKDCE RLAERLRADG IGAKPYHAGL
     PPSELKEALA GWVADQEGYD IIVATTAFGM GIDKANVRFV AHWQIPKSFE GFYQEAGRAG
     RDGKASACIM YYGREDRDRA ASMMARDHAR LPSRGVAAAA QQQQIMNRAR SLQALVAYCE
     ATDKCRHRLI ARFFGDEEVP PCDYACDWCK DPVGLVRRKE KGLASEEWCS TQREMGRYDV
     DEYE
//
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