DPOLL_MACFA
ID DPOLL_MACFA Reviewed; 575 AA.
AC Q4R380;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=DNA polymerase lambda {ECO:0000305};
DE Short=Pol Lambda {ECO:0000305};
DE EC=2.7.7.7 {ECO:0000250|UniProtKB:Q9UGP5};
DE EC=4.2.99.- {ECO:0000250|UniProtKB:Q9UGP5};
GN Name=POLL {ECO:0000250|UniProtKB:Q9UGP5};
GN ORFNames=QtsA-18827 {ECO:0000312|EMBL:BAE02437.1};
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG International consortium for macaque cDNA sequencing and analysis;
RT "DNA sequences of macaque genes expressed in brain or testis and its
RT evolutionary implications.";
RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: DNA polymerase that functions in several pathways of DNA
CC repair. Involved in base excision repair (BER) responsible for repair
CC of lesions that give rise to abasic (AP) sites in DNA. Also contributes
CC to DNA double-strand break repair by non-homologous end joining and
CC homologous recombination. Has both template-dependent and template-
CC independent (terminal transferase) DNA polymerase activities. Has also
CC a 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity.
CC {ECO:0000250|UniProtKB:Q9UGP5}.
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:Q9UGP5};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q9UGP5};
CC -!- SUBUNIT: Interacts with PCNA. Interacts with PAXX; promoting POLL
CC recruitment to double-strand breaks (DSBs) and stimulation of the end-
CC filling activity of POLL. Interacts with XRCC4; promoting POLL
CC recruitment to double-strand breaks (DSBs) and stimulation of the end-
CC filling activity of POLL. Interacts with NHEJ1/XLF; promoting POLL
CC recruitment to double-strand breaks (DSBs) and stimulation of the end-
CC filling activity of POLL. {ECO:0000250|UniProtKB:Q9UGP5}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9UGP5}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-X family. {ECO:0000305}.
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DR EMBL; AB179386; BAE02437.1; -; mRNA.
DR RefSeq; NP_001270218.1; NM_001283289.1.
DR AlphaFoldDB; Q4R380; -.
DR BMRB; Q4R380; -.
DR SMR; Q4R380; -.
DR STRING; 9541.XP_005566302.1; -.
DR GeneID; 101867295; -.
DR CTD; 27343; -.
DR eggNOG; KOG2534; Eukaryota.
DR OrthoDB; 1328151at2759; -.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0035861; C:site of double-strand break; ISS:UniProtKB.
DR GO; GO:0051575; F:5'-deoxyribose-5-phosphate lyase activity; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006287; P:base-excision repair, gap-filling; ISS:UniProtKB.
DR GO; GO:0071897; P:DNA biosynthetic process; ISS:UniProtKB.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; ISS:UniProtKB.
DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; ISS:UniProtKB.
DR CDD; cd00141; NT_POLXc; 1.
DR Gene3D; 1.10.150.110; -; 1.
DR Gene3D; 3.30.210.10; -; 1.
DR Gene3D; 3.30.460.10; -; 1.
DR Gene3D; 3.40.50.10190; -; 1.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR002054; DNA-dir_DNA_pol_X.
DR InterPro; IPR019843; DNA_pol-X_BS.
DR InterPro; IPR010996; DNA_pol_b-like_N.
DR InterPro; IPR028207; DNA_pol_B_palm_palm.
DR InterPro; IPR018944; DNA_pol_lambd_fingers_domain.
DR InterPro; IPR027421; DNA_pol_lamdba_lyase_dom_sf.
DR InterPro; IPR037160; DNA_Pol_thumb_sf.
DR InterPro; IPR022312; DNA_pol_X.
DR InterPro; IPR002008; DNA_pol_X_beta-like.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR029398; PolB_thumb.
DR PANTHER; PTHR11276; PTHR11276; 1.
DR Pfam; PF14792; DNA_pol_B_palm; 1.
DR Pfam; PF14791; DNA_pol_B_thumb; 1.
DR Pfam; PF10391; DNA_pol_lambd_f; 1.
DR Pfam; PF14716; HHH_8; 1.
DR PRINTS; PR00869; DNAPOLX.
DR PRINTS; PR00870; DNAPOLXBETA.
DR SMART; SM00483; POLXc; 1.
DR SUPFAM; SSF47802; SSF47802; 1.
DR SUPFAM; SSF52113; SSF52113; 1.
DR SUPFAM; SSF81301; SSF81301; 1.
DR PROSITE; PS50172; BRCT; 1.
DR PROSITE; PS00522; DNA_POLYMERASE_X; 1.
PE 2: Evidence at transcript level;
KW DNA damage; DNA repair; DNA replication; DNA synthesis; DNA-binding;
KW DNA-directed DNA polymerase; Lyase; Manganese; Metal-binding;
KW Nucleotidyltransferase; Nucleus; Reference proteome; Transferase.
FT CHAIN 1..575
FT /note="DNA polymerase lambda"
FT /id="PRO_0000218784"
FT DOMAIN 36..132
FT /note="BRCT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT REGION 160..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 265..279
FT /note="DNA-binding"
FT /evidence="ECO:0000250|UniProtKB:Q9UGP5"
FT REGION 345..348
FT /note="DNA-binding"
FT /evidence="ECO:0000250|UniProtKB:Q9UGP5"
FT REGION 420..429
FT /note="Involved in primer binding"
FT /evidence="ECO:0000250"
FT REGION 466..505
FT /note="DNA-binding"
FT /evidence="ECO:0000250|UniProtKB:Q9UGP5"
FT COMPBIAS 165..179
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..195
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 312
FT /note="Schiff-base intermediate with DNA"
FT /evidence="ECO:0000250|UniProtKB:Q9UGP5"
FT BINDING 386
FT /ligand="dCTP"
FT /ligand_id="ChEBI:CHEBI:61481"
FT /evidence="ECO:0000250|UniProtKB:Q9UGP5"
FT BINDING 417..420
FT /ligand="dCTP"
FT /ligand_id="ChEBI:CHEBI:61481"
FT /evidence="ECO:0000250|UniProtKB:Q9UGP5"
FT BINDING 426..429
FT /ligand="dCTP"
FT /ligand_id="ChEBI:CHEBI:61481"
FT /evidence="ECO:0000250|UniProtKB:Q9UGP5"
FT BINDING 427
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q9UGP5"
FT BINDING 429
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q9UGP5"
FT BINDING 490
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q9UGP5"
FT BINDING 513
FT /ligand="dCTP"
FT /ligand_id="ChEBI:CHEBI:61481"
FT /evidence="ECO:0000250|UniProtKB:Q9UGP5"
SQ SEQUENCE 575 AA; 63565 MW; 7CEC034FC8464256 CRC64;
MDPRGILKAF PKRKKIHADA SSKVLAKIPR KEEGEEAEEW LSSLRAHVVR TGIGRARAEL
FEKQIVQHGG QLCPVQGPGV THIVVDEGMD YERALRLLRL PRLPPGAQLV KSAWLSLCLQ
ERRLVDVAGF SIFIPSKYLD QSQPSKAEQD ASLPPGTHEA LLQTALPPPP SPTRPVSPPQ
KTKEAPNTQA QPISDDEASD GEETQVSAAD LEALISGHYP ASLEGDCDPS PAPVVLDKWV
CAQPSSQKAT NHNLHITEKL EVLAKAYSVQ GDKWRALGYA KAINALKSFH KPVTSYQEAC
SIPGIGKRMA EKIIEILESG HLRKLDHISE SVPVLELFSN IWGAGTKTAQ MWYQQGFRSL
EDIRSQASLT TQQAIGLKHY NDFLERMPRE EATEIEQTVQ KAAQAFNSGL LCVACGSYRR
GKATCGDVDV LITHPDGRSH RGIFSRLLDS LRQQGFLTDD LVSQEENGQQ QKYLGVCRLP
GPGWRHRRLD IIVVPYSEFA CALLYFTGSA HFNRSMRALA KTKGMSLSEH ALSTAVVRNT
HGCKMGPGRV LPTPTEKDVF RLLGLPYREP AERDW
