ID A0A139HPD3_9PEZI Unreviewed; 717 AA.
AC A0A139HPD3;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
DE Flags: Fragment;
GN ORFNames=AC578_7951 {ECO:0000313|EMBL:KXT04242.1};
OS Pseudocercospora eumusae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX NCBI_TaxID=321146 {ECO:0000313|EMBL:KXT04242.1, ECO:0000313|Proteomes:UP000070133};
RN [1] {ECO:0000313|EMBL:KXT04242.1, ECO:0000313|Proteomes:UP000070133}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 114824 {ECO:0000313|EMBL:KXT04242.1,
RC ECO:0000313|Proteomes:UP000070133};
RA Chang T.-C., Salvucci A., Crous P.W., Stergiopoulos I.;
RT "Comparative genomics of the Sigatoka disease complex on banana suggests a
RT link between parallel evolutionary changes in Pseudocercospora fijiensis
RT and Pseudocercospora eumusae and increased virulence on the banana host.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00000600};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC Evidence={ECO:0000256|ARBA:ARBA00000600};
CC -!- SIMILARITY: Belongs to the DNA2/NAM7 helicase family.
CC {ECO:0000256|ARBA:ARBA00007913}.
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:KXT04242.1}.
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DR EMBL; LFZN01000022; KXT04242.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A139HPD3; -.
DR OrthoDB; 170190at2759; -.
DR Proteomes; UP000070133; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR CDD; cd18044; DEXXQc_SMUBP2; 1.
DR CDD; cd18808; SF1_C_Upf1; 1.
DR Gene3D; 2.40.30.270; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041679; DNA2/NAM7-like_C.
DR InterPro; IPR041677; DNA2/NAM7_AAA_11.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR047187; SF1_C_Upf1.
DR InterPro; IPR048761; SMUBP-2_HCS1_1B.
DR PANTHER; PTHR43788:SF19; DNA-BINDING PROTEIN SMUBP-2; 1.
DR PANTHER; PTHR43788; DNA2/NAM7 HELICASE FAMILY MEMBER; 1.
DR Pfam; PF13086; AAA_11; 1.
DR Pfam; PF13087; AAA_12; 1.
DR Pfam; PF21138; SMUBP-2_HCS1_1B; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00487; DEXDc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
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:UP000070133}.
FT DOMAIN 208..508
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|SMART:SM00487"
FT DOMAIN 226..597
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 106..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 426..449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 432..449
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KXT04242.1"
SQ SEQUENCE 717 AA; 79193 MW; C0BD0CB513B3B074 CRC64;
LHLASPSVAS MKETDIAAFA ARQISLLDNE RHTEVAEMQL LTQTHAPTTL QRAGLALLNL
AISSQRTGFG GKTLLELSLD PAISSSPELP EHGLRVGDIC AVAEQPKGAE KKKEREKMEK
KGVEGVVTKT HKSTITVALD QEDADVPTGK LWLVKLANDV TYKRLNQTMT RLQKMQPSEQ
STLTQVLFGQ SSPIPISESG LKAEIQWHDP TLNESQKEAI QFALASRDVV LIHGPPGTGK
THTLIELILQ LLKQNLRLLV CGPSNISVDN IVERLAPHKV NMVRLGHPAR LLPSVISHSM
EVLTKTSDAA AIVTDIRAEM DSKQASIRKT RNGRERKAIY GELKHLRKEY REREGRVVRE
LLQQSQVVLS TLHGSGGFQL KDQNFDVVIV DEASQALEAQ CWIPVLTSGA SKLVLAGDHL
QLPPTIKSSN SEVDKKQLKS KTKVEDTTDG LAKASLTDEK STHRAAKTKD DDVRLETTLF
DRLLKLHGNK IKRMLTTQYR MHEKIMHFPS HALYEDKLIA ADAVKARLLR DLPYGVEEND
NTSESLIFFD TQGGEFPEKT EDEDAGKGKS SLLAESKVNE AEALIVRDHI MNLVDSGVKA
EDIAVVTPYN GQLALLSQML KEQVPGLELG SVDGFQGREK EAVIVSLVRS NAEHEVGFLS
EKRRLNVAMT RPKRQLCVIG DSETISSGSK FLKSWMAHLE ENADLRYPDL SDFSQAG
//
