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Database: UniProt
Entry: A0A1C1C9U7_9EURO
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Original site: A0A1C1C9U7_9EURO 
ID   A0A1C1C9U7_9EURO        Unreviewed;       763 AA.
AC   A0A1C1C9U7;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 29.
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:0000313|EMBL:OCT45212.1};
GN   Synonyms=PIF1 {ECO:0000256|HAMAP-Rule:MF_03176};
GN   ORFNames=CLCR_05512 {ECO:0000313|EMBL:OCT45212.1};
OS   Cladophialophora carrionii.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC   Cladophialophora.
OX   NCBI_TaxID=86049 {ECO:0000313|EMBL:OCT45212.1, ECO:0000313|Proteomes:UP000094526};
RN   [1] {ECO:0000313|Proteomes:UP000094526}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KSF {ECO:0000313|Proteomes:UP000094526};
RA   Teixeira M.M., Souza R.C., Almeida L.G., Vicente V.A., de Hoog S.,
RA   Bocca A.L., de Almeida S.R., Vasconcelos A.T., Felipe M.S.;
RL   Submitted (JUL-2015) 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:OCT45212.1}.
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DR   EMBL; LGRB01000020; OCT45212.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1C1C9U7; -.
DR   STRING; 86049.A0A1C1C9U7; -.
DR   VEuPathDB; FungiDB:CLCR_05512; -.
DR   VEuPathDB; FungiDB:G647_07869; -.
DR   eggNOG; KOG0987; Eukaryota.
DR   Proteomes; UP000094526; 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:OCT45212.1};
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:UP000094526}.
FT   DOMAIN          261..530
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DNA_BIND        678..697
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03176"
FT   REGION          1..146
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          209..235
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        15..34
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        45..74
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        209..234
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         269..276
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03176"
SQ   SEQUENCE   763 AA;  84685 MW;  892F8017C1CE7220 CRC64;
     MLGRAAHRHA STTAGDKKQS TLLSNSSATN IPPANSRKRK LDRSMSTTSS LGSLHQQSWP
     DENTEPAFVD LTNSSEKHSD IHYPILKPLD AESYPSLPPV PKHSPAEPAS SAPVAWSSSP
     AEHFEDPKTI ISSRKPPSPA PLRPAKRRVL PASFTSRPAF APRNELHGEL GKDHKLERTA
     ALKQHQGGVG REKASQVMSD MLEASSFTHQ RMGASLSRSS SERPPGSLTK QTGIPAAETE
     KVPDVFLSDE QKAVMKAVME EGKSVFFTGS AGTGKSVLMK AIIAQLRHKY RASPDRYAVT
     ASTGLASCIL EGQTLHSWSG IGLGKEPAPE LVKKVKRNQK SRQRWLRTKV LIIDEVSMVD
     GQLFDKLEQV ARTIRNNGRP FGGIQLVVTG DFFQLPPVPE KNATAKFVFE AVTWNTCIQH
     TILLTHVFRQ KDEQFASMLN EMRLGKMSPA TVREFKALSR PLKVVDELEA TELYPRREEV
     ENANTNRMRK LSGQVMTFTA VDSGNAEPNT RKALLSNFIA PEILELKKGA QVMLIKNIDG
     QLVNGSLGIV QSFMDEGTFF TYKDDEPTFL LAQEGGEDDD EEKKAAREKI REARLKNSAN
     GETRKLWPMV RFNLPDGTSR SMLCAPDEWK TEAQNGEVLA KRVQVPLILA WALSIHKAQG
     QTLSRVKVDL GKVFEKGQAY VALSRARTKE GLQVLRFDER KVMVHQKVLE FYAKLAGHET
     LNKQQAKKEV KKDLFADEDD FEDDFSIEDM LEAEKMLKAG AGF
//
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