ID A0A2B7ZAZ8_9EURO Unreviewed; 802 AA.
AC A0A2B7ZAZ8;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
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=GX50_06846 {ECO:0000313|EMBL:PGH30369.1};
OS Emmonsia crescens.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Emmonsia.
OX NCBI_TaxID=73230 {ECO:0000313|EMBL:PGH30369.1, ECO:0000313|Proteomes:UP000226031};
RN [1] {ECO:0000313|EMBL:PGH30369.1, ECO:0000313|Proteomes:UP000226031}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH4076 {ECO:0000313|EMBL:PGH30369.1,
RC ECO:0000313|Proteomes:UP000226031};
RA Munoz J.F., Mcewen J.G., Clay O.K., Cuomo C.A.;
RT "Comparative genomics in systemic dimorphic fungi from Ajellomycetaceae.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
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:PGH30369.1}.
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DR EMBL; PDND01000176; PGH30369.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2B7ZAZ8; -.
DR STRING; 73230.A0A2B7ZAZ8; -.
DR VEuPathDB; FungiDB:EMCG_07806; -.
DR OrthoDB; 5474774at2759; -.
DR Proteomes; UP000226031; 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};
KW Helicase {ECO:0000256|HAMAP-Rule:MF_03176, ECO:0000313|EMBL:PGH30369.1};
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:UP000226031}.
FT DOMAIN 272..459
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DNA_BIND 684..703
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03176"
FT REGION 134..214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..167
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..198
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 280..287
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03176"
SQ SEQUENCE 802 AA; 88811 MW; 43A5A7A8886594BB CRC64;
MSRYTPLARA STAIVTPSFI RLASQWPCSF TCHRGREFAM FNQAVRKHTA PAKAPFPNVT
PLNRAVPLSS SQTAGIKRKL DAVQPPPSET PLAVLHSNVY FDENDFDDDI DLDEPTSFSI
NLAQSQSFTS SRIQLPELPP PLEQPAPPSD NAPPSTLPLP WSSSPPTNLL PPAKRRTLPW
QENKKPEAET RPRINQERRF VTRTPAPNKS SSLPWDKTMS AVKEEQKELR KQQKIRVSSE
KNPNQLGTRV PKVASIFLSE EQKRVVEAIV KDSKSIFFTG SAGTGKSVLM REIIRKLRER
YKGEPDRVAV TASTGLAACN IEGVTLHSFA GIGLGKEPVA DLVKKVKRNQ KNRTRWLRTK
VLIIDEISMV DGDLFDKLEE IARKIRNNGR PFGGIQLVVT GDFFQLPPVP DSTKMAKFAF
SASSWNTTIQ HTILLTHVFR QKDPKFAAML NEMRLGKLSP ETIASFKQLS RPLNFHDALE
ATELFPTRSE VENANSARMS RLSGETMVFT AVDGGTMQNE AQRSQLLADC VAHTIHLKKG
AQVMLIKNMD ETLVNGSLGK VVAFMDEARF DYYSKTDENF AGDPANDDHN AQAINKLKSY
ENKPGSVSAK GKWPVVCFVQ PDGTERHLLC QPETWKIELP NGEIKAQRTQ VPLILAWALS
IHKAQGQTLQ RVKVDLGRVF EKGQAYVALS RATSQAGLQV SRFDPRRVMV HPKVLEFYSN
LSSIHNIKDA ANANANALAG AGANDNVSVS ASVSAGANIN TNTNTNTNAN AKQIRDQAKI
VKRTATDYLD DFDDDLLESV HA
//
