ID   DPOLQ_CAEEL             Reviewed;        1661 AA.
AC   A0FLQ6; G4SPM6;
DT   01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT   25-JAN-2012, sequence version 2.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=DNA polymerase theta {ECO:0000250|UniProtKB:O75417};
DE            EC=2.7.7.7 {ECO:0000250|UniProtKB:O75417};
GN   Name=polq-1 {ECO:0000312|WormBase:W03A3.2};
GN   ORFNames=W03A3.2 {ECO:0000312|WormBase:W03A3.2};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [2]
RP   FUNCTION.
RX   PubMed=18472307; DOI=10.1016/j.dnarep.2008.03.021;
RA   Muzzini D.M., Plevani P., Boulton S.J., Cassata G., Marini F.;
RT   "Caenorhabditis elegans POLQ-1 and HEL-308 function in two distinct DNA
RT   interstrand cross-link repair pathways.";
RL   DNA Repair 7:941-950(2008).
RN   [3]
RP   FUNCTION.
RX   PubMed=24614976; DOI=10.1101/gr.170431.113;
RA   Roerink S.F., van Schendel R., Tijsterman M.;
RT   "Polymerase theta-mediated end joining of replication-associated DNA breaks
RT   in C. elegans.";
RL   Genome Res. 24:954-962(2014).
RN   [4]
RP   FUNCTION, AND MUTAGENESIS OF PRO-1417.
RX   PubMed=24496117; DOI=10.1038/ncomms4216;
RA   Koole W., van Schendel R., Karambelas A.E., van Heteren J.T., Okihara K.L.,
RA   Tijsterman M.;
RT   "A Polymerase Theta-dependent repair pathway suppresses extensive genomic
RT   instability at endogenous G4 DNA sites.";
RL   Nat. Commun. 5:3216-3216(2014).
CC   -!- FUNCTION: DNA polymerase that promotes microhomology-mediated end-
CC       joining (MMEJ), an alternative non-homologous end-joining (NHEJ)
CC       machinery triggered in response to double-strand breaks in DNA. MMEJ is
CC       an error-prone repair pathway that produces deletions of sequences from
CC       the strand being repaired and promotes genomic rearrangements, such as
CC       telomere fusions (PubMed:24614976). Required to prevent extensive loss
CC       of sequences near G-quadruplex (G4) DNA sites, which are prone to cause
CC       genome alterations, by generating deletions (PubMed:24496117).
CC       {ECO:0000250|UniProtKB:O75417, ECO:0000250|UniProtKB:Q8CGS6,
CC       ECO:0000269|PubMed:18472307, ECO:0000269|PubMed:24496117,
CC       ECO:0000269|PubMed:24614976}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC         diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC         Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC         ChEBI:CHEBI:173112; EC=2.7.7.7;
CC         Evidence={ECO:0000250|UniProtKB:O75417};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O18475}.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-A family. {ECO:0000305}.
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DR   EMBL; FO081687; CCD73325.1; -; Genomic_DNA.
DR   EMBL; FO081686; CCD73325.1; JOINED; Genomic_DNA.
DR   RefSeq; NP_498250.3; NM_065849.4.
DR   AlphaFoldDB; A0FLQ6; -.
DR   SMR; A0FLQ6; -.
DR   STRING; 6239.W03A3.2; -.
DR   PaxDb; A0FLQ6; -.
DR   PRIDE; A0FLQ6; -.
DR   EnsemblMetazoa; W03A3.2.1; W03A3.2.1; WBGene00020964.
DR   UCSC; W03A3.2; c. elegans.
DR   WormBase; W03A3.2; CE38982; WBGene00020964; polq-1.
DR   eggNOG; KOG0950; Eukaryota.
DR   GeneTree; ENSGT00940000158694; -.
DR   HOGENOM; CLU_000818_0_0_1; -.
DR   InParanoid; A0FLQ6; -.
DR   OMA; SSMENCA; -.
DR   OrthoDB; 179246at2759; -.
DR   PhylomeDB; A0FLQ6; -.
DR   Reactome; R-CEL-5685939; HDR through MMEJ (alt-NHEJ).
DR   PRO; PR:A0FLQ6; -.
DR   Proteomes; UP000001940; Chromosome III.
DR   Bgee; WBGene00020964; Expressed in germ line (C elegans) and 4 other tissues.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IBA:GO_Central.
DR   GO; GO:0006287; P:base-excision repair, gap-filling; IMP:CACAO.
DR   GO; GO:0071479; P:cellular response to ionizing radiation; IGI:UniProtKB.
DR   GO; GO:0006261; P:DNA-templated DNA replication; IEA:InterPro.
DR   GO; GO:0006302; P:double-strand break repair; IBA:GO_Central.
DR   GO; GO:0097681; P:double-strand break repair via alternative nonhomologous end joining; IBA:GO_Central.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR019760; DNA-dir_DNA_pol_A_CS.
DR   InterPro; IPR001098; DNA-dir_DNA_pol_A_palm_dom.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR002298; DNA_polymerase_A.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR10133; PTHR10133; 3.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00476; DNA_pol_A; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   PRINTS; PR00868; DNAPOLI.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00482; POLAc; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   SUPFAM; SSF56672; SSF56672; 1.
DR   PROSITE; PS00447; DNA_POLYMERASE_A; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; DNA damage; DNA repair; DNA-directed DNA polymerase;
KW   Nucleotide-binding; Nucleotidyltransferase; Nucleus; Reference proteome;
KW   Transferase.
FT   CHAIN           1..1661
FT                   /note="DNA polymerase theta"
FT                   /id="PRO_0000432703"
FT   DOMAIN          38..208
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          283..434
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   MOTIF           149..152
FT                   /note="DEAH box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   BINDING         51..58
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   MUTAGEN         1417
FT                   /note="P->S: Loss of sequences surrounding G-quadruplex
FT                   (G4) DNA sites."
FT                   /evidence="ECO:0000269|PubMed:24496117"
SQ   SEQUENCE   1661 AA;  188679 MW;  55E26C9CDAC5B9EA CRC64;
     MDEASCRFPE WVSSKIIDYY AEQNIKALFD WQIDVLNEAR QFEDQHLIFS APTSAGKSIV
     AELLSWKVAS TGRKVLFVLP YISVAREKLH QIQRCWRRDD ISVCGFIGPQ ASNPNEWLGA
     VCTIEKAASL TNRALSEDWF EEIGMIVVDE MHMVFDSSRG AHIEHMLSKV LLWNQSALEK
     VRIIGMSATI PELYRIGKWL DGAKVFEARF RPIVLQNHIV IGSELRKSGD NKVLREFSED
     PLILLTEESF RRNSQTLVMI SSKLDAEKTA LNIASRFHEI NKTDSSLLEI LKERANGLLF
     IKHGLERNGC KDRNVMSTLA WGVAYHHAGL TMEERECIEL GFREKNIVIL VATSTLASGV
     NLPAERVLIK AQPRGPSALT SLNYRQMVGR AGRTGHATRG ETYLLIKKCD RDAVLKIIET
     PIDQGVLTRK RDAERTNLSR FILEGICTGL TTTRSQIHDL CKLLLFNSEN LQLSDIAIEM
     LLRNSFISQD ENDDQLSPTQ LGRAAIASSL PPEASLAIFE DLNSASRAIA LDTELHMLYL
     VYFYKNSRAQ IIQKIFKIYS IFILKKFKNL EPKFKKKISE NITVHITNSI RKKQHFWHVT
     PINVSVWQEC DWHHLFSIFS KLPSDHKRIA KLVGVSEKFI LDQLQGRRND KLLQIHIRFF
     SALALFDLIS EMSIYEVSHK YRIPRGCLQT LQSQSATYAA MIVAFCLRLG WTYLKALLDG
     FATRLLFGVR SELSELVAIE GIDGQRARIL HERGVTCLSH LSACDSSKLA HFLTLAVPYS
     SSNSNDGLGE WLFGEPRMRV DVAARTLKER ARKVLIRRVQ ELGISVELPK FEENEENIQE
     SCDSGLPDSC EGMEDELEEK ENIVKMEEMT KSVTEMSLTD NTISFKSEDD LFKKEIKVEE
     DEVFIKKEID EDEEEIVEET VIECLETSLL KLKASTDEVF LRRLSQTFSP IGRSRSILNN
     SLLEDSFDRP VPRSSIPILN FITPKRESPT PYFEDSFDRP IPGSLPISSS RRKSVLTNIA
     NLDSSRRESI NSNASDNNSF DVFVTPPTKS AKEEKRRIAV KHPRVGNIIY SPLTSSPVIK
     HPKLEINHFY LKDVCHDHNA WNLWTKSSTS TSSCSIRVSD DYTGIAIRTD AGNTFIPLLE
     TFGGEPSPAS KYFESFSKCI IPLNTRLEFL KTLAVTVEMY ISSMEDAFLI FEKFGIKIFR
     LKVVRIAAYL NNVIDVEQEE NSNFLPILMD RYSILDPEIR KTCSSSLHKA AVEVYSLKPI
     FEKMCCSGAS LQLEMESCQT VLNIFYSGIV FDQALCNSFI YKIRKQIENL EENIWRLAYG
     KFNIHSSNEV ANVLFYRLGL IYPETSGCKP KLRHLPTNKL ILEQMNTQHP IVGKILEYRQ
     IQHTLTQCLM PLAKFIGRIH CWFEMCTSTG RILTSVPNLQ NVPKRISSDG MSARQLFIAN
     SENLLIGADY KQLELRVLAH LSNDSNLVNL ITSDRDLFEE LSIQWNFPRD AVKQLCYGLI
     YGMGAKSLSE LTRMSIEDAE KMLKAFFAMF PGVRSYINET KEKVCKEEPI STIIGRRTII
     KASGIGEERA RIERVAVNYT IQGSASEIFK TAIVDIESKI KEFGAQIVLT IHDEVLVECP
     EIHVAAASES IENCMQNALS HLLRVPMRVS MKTGRSWADL K