DPO4_SCHPO
ID DPO4_SCHPO Reviewed; 506 AA.
AC Q09693;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=DNA polymerase type-X family protein pol4;
DE EC=2.7.7.7;
GN Name=pol4; ORFNames=SPAC2F7.06c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP FUNCTION.
RX PubMed=16120966; DOI=10.1093/nar/gki780;
RA Gonzalez-Barrera S., Sanchez A., Ruiz J.F., Juarez R., Picher A.J.,
RA Terrados G., Andrade P., Blanco L.;
RT "Characterization of SpPol4, a unique X-family DNA polymerase in
RT Schizosaccharomyces pombe.";
RL Nucleic Acids Res. 33:4762-4774(2005).
RN [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
CC -!- FUNCTION: Repair polymerase. Involved in gap-filling in DNA non-
CC homologous end joining (NHEJ) required for double-strand break repair.
CC Can incorporate a ribonucleotide (rNTP) into a primer DNA.
CC {ECO:0000269|PubMed:16120966}.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-X family. {ECO:0000305}.
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DR EMBL; CU329670; CAA90493.1; -; Genomic_DNA.
DR PIR; T38554; S58150.
DR RefSeq; NP_592977.1; NM_001018377.2.
DR AlphaFoldDB; Q09693; -.
DR SMR; Q09693; -.
DR BioGRID; 278134; 4.
DR STRING; 4896.SPAC2F7.06c.1; -.
DR iPTMnet; Q09693; -.
DR MaxQB; Q09693; -.
DR PaxDb; Q09693; -.
DR PRIDE; Q09693; -.
DR EnsemblFungi; SPAC2F7.06c.1; SPAC2F7.06c.1:pep; SPAC2F7.06c.
DR GeneID; 2541638; -.
DR KEGG; spo:SPAC2F7.06c; -.
DR PomBase; SPAC2F7.06c; pol4.
DR VEuPathDB; FungiDB:SPAC2F7.06c; -.
DR eggNOG; KOG2534; Eukaryota.
DR HOGENOM; CLU_008698_1_1_1; -.
DR InParanoid; Q09693; -.
DR OMA; ITDMLME; -.
DR PhylomeDB; Q09693; -.
DR PRO; PR:Q09693; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0051575; F:5'-deoxyribose-5-phosphate lyase activity; IDA:PomBase.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IDA:PomBase.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IDA:PomBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:1990165; F:single-strand break-containing DNA binding; IDA:PomBase.
DR GO; GO:0006284; P:base-excision repair; IC:PomBase.
DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IDA:PomBase.
DR GO; GO:0042276; P:error-prone translesion synthesis; IDA:PomBase.
DR GO; GO:0061674; P:gap filling involved in double-strand break repair via nonhomologous end joining; IMP:PomBase.
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 InterPro; IPR001357; BRCT_dom.
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; 2.
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; SSF81301; SSF81301; 1.
DR PROSITE; PS50172; BRCT; 1.
DR PROSITE; PS00522; DNA_POLYMERASE_X; 1.
PE 3: Inferred from homology;
KW Cytoplasm; DNA damage; DNA repair; DNA-directed DNA polymerase; Magnesium;
KW Metal-binding; Nucleotidyltransferase; Nucleus; Reference proteome;
KW Transferase.
FT CHAIN 1..506
FT /note="DNA polymerase type-X family protein pol4"
FT /id="PRO_0000218800"
FT DOMAIN 1..98
FT /note="BRCT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00033"
FT REGION 106..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 348..357
FT /note="Involved in ssDNA binding"
FT /evidence="ECO:0000250"
FT COMPBIAS 134..150
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 355
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 357
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 419
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 506 AA; 57396 MW; F9A51ED54D428134 CRC64;
MKILASSTNY VLHNRLSNSQ YEDARSKIVN FGGEFTNDAA KADYIFVNYS QINRVRRELR
TIGTPLETCV SCKLIVKIDW LNEPKESLTP GNPYVIWHRK PEMKVGSPYT PSTRPASHTE
APNDFENHET PNTENNNEVK SIDNVDQEGS VYPTTKEYPY VLEIPRYACQ RKTPLKCVNQ
AFVNALSVLK TCREVNGESV RTRAYGMAIA TIKAFPLPID SAEQLEKMPG CGPKIVHLWK
EFASTGTLKE AEEFQKDPAS KILLLFYNIF GVGASHAAEW YQKGWRTIEQ VRKHKDSFTK
QIKVGLEFYE DFCKTVTIEE ATEIYETIVS RMPDGIKIQS CLVGGFRRGK PVGADVDMVL
SPSHTHSTKH LVDVLLRILD EEFQFRLISV QEHSCGGKKG YVMLAVILSN SSKINRRVDI
IVVPPAYIGS AVLGWSGGIF FLRDLKLYAN SHLGLSYDSF EIINLKTGKD ICPDEFNEWK
DPVEAEKDIF RYFSLEYIEP KFRNTG
