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Database: UniProt
Entry: A0A0M9WFH3_9EURO
LinkDB: A0A0M9WFH3_9EURO
Original site: A0A0M9WFH3_9EURO 
ID   A0A0M9WFH3_9EURO        Unreviewed;      1059 AA.
AC   A0A0M9WFH3;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE            EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN   ORFNames=ACN38_g6256 {ECO:0000313|EMBL:KOS42855.1};
OS   Penicillium nordicum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=229535 {ECO:0000313|EMBL:KOS42855.1, ECO:0000313|Proteomes:UP000037696};
RN   [1] {ECO:0000313|EMBL:KOS42855.1, ECO:0000313|Proteomes:UP000037696}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DAOMC 185683 {ECO:0000313|EMBL:KOS42855.1,
RC   ECO:0000313|Proteomes:UP000037696};
RA   Nguyen H.D., Seifert K.A.;
RT   "Genome sequencing of Penicillium nordicum.";
RL   Submitted (AUG-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:ARBA00001665};
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:KOS42855.1}.
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DR   EMBL; LHQQ01000095; KOS42855.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M9WFH3; -.
DR   STRING; 229535.A0A0M9WFH3; -.
DR   OrthoDB; 57056at2759; -.
DR   Proteomes; UP000037696; Unassembled WGS sequence.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   CDD; cd18795; SF2_C_Ski2; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 1.10.3380.10; Sec63 N-terminal domain-like domain; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR004179; Sec63-dom.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR47835; HFM1, ATP DEPENDENT DNA HELICASE HOMOLOG; 1.
DR   PANTHER; PTHR47835:SF2; SEC63 DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF02889; Sec63; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00973; Sec63; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF158702; Sec63 N-terminal domain-like; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022806};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022806};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037696}.
FT   DOMAIN          1..174
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          580..633
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          673..699
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          734..1018
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        593..631
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        750..779
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        794..809
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        933..962
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        963..977
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        999..1018
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1059 AA;  117963 MW;  AA306A12C475B71F CRC64;
     MVFCCTRNSS LATAKELARL FTLTNPFARL WNGPKKRLEA HNEDLKTTLP AGVAFHHAGL
     GPADRHTVET GFREGNINVI CCTSTLAVGI NLPCHSVIIK NTASWQDGGF KEYSDLEMMQ
     MLGRAGRPQF DDSATAVILT RKERVAHYER LVQGSESLES CLHLNLIDHL NAEVGLGNIA
     DVESAVKWLG GTFLFVRLRR NPTHYKLKEG ANQEDEDQLL RDICEKDISL LQKYGLVEGE
     SLRSTQFGEA MARYYIQFET MKVLLSLKPK ATLSEILNVI AQGEEFREIR LKAGEKSLYR
     EINRDPGIRF PIKVDLALPA HKISLLLQSE LGAIEYPDND QLQKHKFNFQ QDKSLVFAHA
     NRLIRCLLDC QIARGDSITI LNALELARSL GAKVWDHSPL QMKQIEQVGI VTVRKLAAAG
     ITSIEVLECA EAHQIEMVLS KNPPFGSKLL SRLKEFPKLR VSVKMLGKEV KVDCVNVRFK
     AEVAFMNDKT PTYFQHHPVY VCCLIERSDG HMIDFRRTSA GKLQEKFEIE LTAELTSSEH
     VIVCHVMCDE IAGTSRQAEL RPNLPSHLFA ALRDMNTNAQ NTETSNLPSR HPERNLNSKD
     AEKPKTNTSR PHGRDMTSIK TKSRQSVDDF DGDDLQLDDF LVANEPRGKA KESTKPQSRQ
     VDGFDDIDWF SIDATPPRPA KGVPKVSNTR EDDWGVDLDE PEDEYEPVRL ANGKWACNHK
     CRDKTSCKHF CCREGLEKPP KPPKRTIPAT QKEGSLNQLT ISASITKAPT SNSSSKKQVA
     KKRVMGPKND GHVSKMKMST SQAGKKDLSQ EMSVLSERDK NVPSYKRKLE KSPAPLSSDY
     GDENFDDLPS PSRLLGSSRG SGFATWVSPV ADDQAENKIT DVPAIESKHT ETDPSHSASQ
     SDFLQLDQMK PSNPKPEHEI IEIPDDTPPD SEMTITKDPS AKQGTLPLTT KADQPSTLKR
     KASQDVTRTE HKKQVKQRPF VSALQVHASN SLDDEPPLSP EQPVSPISPA SPTSPVPPVP
     LVPPIPAVPV IGGQMDLNTT WDNNGIDLLD EFKDIIKFI
//
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