ID A0A1V6V0V5_9EURO Unreviewed; 715 AA.
AC A0A1V6V0V5;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=ATP-dependent DNA helicase PIF1 {ECO:0000256|HAMAP-Rule:MF_03176};
DE EC=3.6.4.12 {ECO:0000256|HAMAP-Rule:MF_03176};
DE AltName: Full=DNA repair and recombination helicase PIF1 {ECO:0000256|HAMAP-Rule:MF_03176};
GN Name=PIF1 {ECO:0000256|HAMAP-Rule:MF_03176};
GN ORFNames=PENCOP_c002G03937 {ECO:0000313|EMBL:OQE44304.1};
OS Penicillium coprophilum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=36646 {ECO:0000313|EMBL:OQE44304.1, ECO:0000313|Proteomes:UP000191500};
RN [1] {ECO:0000313|Proteomes:UP000191500}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 31321 {ECO:0000313|Proteomes:UP000191500};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
CC -!- FUNCTION: DNA-dependent ATPase and 5'-3' DNA helicase required for the
CC maintenance of both mitochondrial and nuclear genome stability.
CC {ECO:0000256|HAMAP-Rule:MF_03176}.
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|HAMAP-Rule:MF_03176};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03176};
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_03176}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|HAMAP-Rule:MF_03176}.
CC Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03176}.
CC -!- SIMILARITY: Belongs to the helicase family. PIF1 subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_03176}.
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:OQE44304.1}.
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DR EMBL; MDDG01000002; OQE44304.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6V0V5; -.
DR STRING; 36646.A0A1V6V0V5; -.
DR OrthoDB; 5474774at2759; -.
DR Proteomes; UP000191500; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0043139; F:5'-3' DNA helicase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-UniRule.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR GO; GO:0000002; P:mitochondrial genome maintenance; IEA:UniProtKB-UniRule.
DR GO; GO:0000723; P:telomere maintenance; IEA:InterPro.
DR CDD; cd18037; DEXSc_Pif1_like; 1.
DR CDD; cd18809; SF1_C_RecD; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_03176; PIF1; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR010285; DNA_helicase_pif1-like.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR049163; Pif1-like_2B_dom.
DR InterPro; IPR048293; PIF1_RRM3_pfh1.
DR PANTHER; PTHR47642; ATP-DEPENDENT DNA HELICASE; 1.
DR PANTHER; PTHR47642:SF5; ATP-DEPENDENT DNA HELICASE; 1.
DR Pfam; PF05970; PIF1; 1.
DR Pfam; PF21530; Pif1_2B_dom; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_03176}; DNA damage {ECO:0000256|HAMAP-Rule:MF_03176};
KW DNA recombination {ECO:0000256|ARBA:ARBA00023172, ECO:0000256|HAMAP-
KW Rule:MF_03176}; DNA repair {ECO:0000256|HAMAP-Rule:MF_03176};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_03176}; Helicase {ECO:0000256|HAMAP-Rule:MF_03176};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_03176};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128, ECO:0000256|HAMAP-
KW Rule:MF_03176};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_03176};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|HAMAP-Rule:MF_03176};
KW Reference proteome {ECO:0000313|Proteomes:UP000191500}.
FT DOMAIN 240..446
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DNA_BIND 653..672
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03176"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 66..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..112
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..142
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..178
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..222
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 248..255
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03176"
SQ SEQUENCE 715 AA; 80004 MW; 40C7A9961482F2FB CRC64;
MFKKALQDHP GSGLKPLHQT DLLRANATAP SKPQSQPQSG GVKRKIEIAG SSLGSLHNAV
YFDENDFDDD LDLDEPQPLI APRVNGSTIP ETVTYPSLDT SRIGQSVYGN ENLADINYPD
LPSISQEAAV PPSSIQLPWS SSPPAHFQPP VKKPRTLPWT KEEEEPREDK KKSFVTPKRS
KPAEPWNKSE STIKAEQKEL RQEYKKTQKS DRKPKQQDSK IARVFLSDEQ KAVLDAVVER
GKSMFFTGSA GTGKSVLMRE IIAKLRNKYR KEPDRIAVTA STGLAACNIG GVTLHSFAGI
GLGKEPVPEL IKKNQKARNR WLRTKVLVVD EVSMVDGDLF DKLEEIARRI RNNGRPFGGI
QLVVTGDFFQ LPPVPDGSNR EAKFAFAAAS WTTCIQHTIL LTNIFRQRDP EFANMLNEMR
LGKITPSTIE AFRRLSRPLD VNDQIEATEL FPTRAEVDGA NSARMGRLSG EVMRFNAVDS
GTIQDPQHRD RLLSNCMAPP MIQLKKGAQV MLIKNMEDSL VNGSIGKVVA FMSEDYFDSY
KENDKNFTDD ATASDDERAH RARKKLKPMG YKEGPASMAR KWPLVSFLQP DGSERHLLCQ
PETWKIELPN GEVQAQRQQV PLILAWALSI HKAQGQTLQR VKVDLGRVFE KGQAYVALSR
AVSQEGLQVT RFEPRKVMVH PKVVDFYSNL VSITELNKSK TSHALNPDDF DDEDF
//
