ID   PEO1_CHICK              Reviewed;         669 AA.
AC   Q5ZIW1;
DT   25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Twinkle mtDNA helicase {ECO:0000250|UniProtKB:Q96RR1};
DE            EC=3.6.4.12 {ECO:0000250|UniProtKB:Q96RR1};
DE   AltName: Full=Progressive external ophthalmoplegia 1 protein homolog;
DE   AltName: Full=Twinkle protein, mitochondrial {ECO:0000250|UniProtKB:Q96RR1};
DE   Flags: Precursor;
GN   Name=TWNK {ECO:0000250|UniProtKB:Q96RR1}; Synonyms=PEO1;
GN   ORFNames=RCJMB04_23c24;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CB; TISSUE=Bursa of Fabricius;
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
CC   -!- FUNCTION: Mitochondrial helicase involved in mtDNA replication and
CC       repair. Might have a role in mtDNA repair. Has DNA strand separation
CC       activity needed to form a processive replication fork for leading
CC       strand synthesis which is catalyzed by the formation of a replisome
CC       complex with POLG and mtSDB. Preferentially unwinds DNA substrates with
CC       pre-existing 5'-and 3'- single-stranded tails but is also active on a
CC       5'- flap substrate. Can dissociate the invading strand of immobile or
CC       mobile D-loop DNA structures irrespective of the single strand polarity
CC       of the third strand. In addition to its DNA strand separation activity,
CC       also has DNA strand annealing, DNA strand-exchange and DNA branch
CC       migration activities. {ECO:0000250|UniProtKB:Q96RR1}.
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:0000250|UniProtKB:Q96RR1};
CC   -!- SUBUNIT: Homohexamer (via C-terminus) which assembled in a ring-like
CC       structure. Homoheptamer which assembled in a ring-like structure.
CC       Oligomerization is Mg(2+), nucleotide and DNA-independent, however,
CC       Mg(2+) and nucleotide stabilize the homohexameric form.
CC       {ECO:0000250|UniProtKB:Q96RR1}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix, mitochondrion nucleoid
CC       {ECO:0000250|UniProtKB:Q96RR1}. Note=Colocalizes with mtDNA in
CC       mitochondrial nucleoids, a nucleoproteins complex consisting of a
CC       number of copies of proteins associated with mtDNA, probably involved
CC       in mtDNA maintenance and expression. {ECO:0000250|UniProtKB:Q96RR1}.
CC   -!- DOMAIN: N-terminus enhances protein stability and hexamer formation,
CC       which is important for DNA binding, and is required for DNA helicase
CC       activity and, ultimately, for mtDNA replisome processivity.
CC       {ECO:0000250|UniProtKB:Q96RR1}.
CC   -!- CAUTION: The N-terminus contains a putative primase-like domain;
CC       however the absence of the zinc binding domain and other motifs
CC       important for catalysis suggests that TWNK lacks primase activity.
CC       {ECO:0000250|UniProtKB:Q96RR1}.
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DR   EMBL; AJ720673; CAG32332.1; -; mRNA.
DR   RefSeq; NP_001026515.1; NM_001031344.1.
DR   AlphaFoldDB; Q5ZIW1; -.
DR   SMR; Q5ZIW1; -.
DR   STRING; 9031.ENSGALP00000028267; -.
DR   PaxDb; Q5ZIW1; -.
DR   GeneID; 425626; -.
DR   KEGG; gga:425626; -.
DR   CTD; 425626; -.
DR   VEuPathDB; HostDB:geneid_425626; -.
DR   eggNOG; KOG2373; Eukaryota.
DR   InParanoid; Q5ZIW1; -.
DR   OrthoDB; 212176at2759; -.
DR   PhylomeDB; Q5ZIW1; -.
DR   PRO; PR:Q5ZIW1; -.
DR   Proteomes; UP000000539; Unplaced.
DR   GO; GO:0042645; C:mitochondrial nucleoid; ISS:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0043139; F:5'-3' DNA helicase activity; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003678; F:DNA helicase activity; IBA:GO_Central.
DR   GO; GO:0003697; F:single-stranded DNA binding; ISS:UniProtKB.
DR   GO; GO:0006264; P:mitochondrial DNA replication; ISS:UniProtKB.
DR   CDD; cd01029; TOPRIM_primases; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR007694; DNA_helicase_DnaB-like_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR034154; TOPRIM_DnaG/twinkle.
DR   InterPro; IPR027032; Twinkle-like.
DR   PANTHER; PTHR12873; PTHR12873; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS51199; SF4_HELICASE; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Coiled coil; DNA replication; Helicase; Hydrolase;
KW   Mitochondrion; Mitochondrion nucleoid; Nucleotide-binding;
KW   Reference proteome; Transit peptide.
FT   TRANSIT         1..43
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           44..669
FT                   /note="Twinkle mtDNA helicase"
FT                   /id="PRO_0000042642"
FT   DOMAIN          390..641
FT                   /note="SF4 helicase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00596"
FT   REGION          2..120
FT                   /note="Contributes to single strand DNA binding activity"
FT                   /evidence="ECO:0000250|UniProtKB:Q96RR1"
FT   REGION          120..378
FT                   /note="Required for hexamers formation and DNA helicase
FT                   activity"
FT                   /evidence="ECO:0000250|UniProtKB:Q96RR1"
FT   REGION          133..154
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          638..669
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          141..167
FT                   /evidence="ECO:0000255"
FT   BINDING         421..428
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00596"
SQ   SEQUENCE   669 AA;  73995 MW;  8B29B7E73765D5B6 CRC64;
     MAAVPLRPCR ASGRFLPLLR GGARSRGASP WAAGPGRVAQ RRYKKDVLPE PGGAAPAVSV
     TEIRRYLRAQ GIPFQDGYSC LHAPSLFGPE LPPAAGPPFT LFIDKTTGSF LCTATLAEGG
     WQDLQAAVEL RHRGVPAPGP DEGEREEEEE AEARRAREDA RRIWERALPL GELLDEEETR
     ATKAAFGIAP LADGTLKRFG VRYLRAAKAL VFPWFAPRDA ALRGLKLLVA EQRGDAVSYT
     EETLPRFDAY RNLFGLPLIG RRDAEVVLTG SELDALALHQ ATGVPCLALP RGATILPPAL
     LPYLEQFRRV TLWLGDDLRS WEASKLFARK LNPKRCSLVQ PGDLQPRPLE ALNRGLNLTK
     ILRAALPAGH KAIVSFRQLR EEVFGELANS EQVAGVKWAR FPELNKLLKG HRRGELTVFT
     GPTGSGKTTF ISEYALDLCT QGVCTLWGSF EINNIRLAKI MLTQFATRRL EDQLELYDEW
     ADRFEDLPLY FMTFHGQQNI KTVLDTMQHA VYMYDITHVV VDNLQFMMGH EQLSADRLAA
     QDFIVGAFRK FATDNTCHIT LVIHPRKEDD EKELQTASIF GSAKASQEAD NVLILQDRKL
     TTGPGKRYLQ VSKNRFDGDV GVFPLEFSKA SLTFSSYGKS KAKLKKVKEE KGPSPKKGPS
     GGVGGSSKP