POLK_SCHPO
ID POLK_SCHPO Reviewed; 547 AA.
AC O74944;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 3.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=DNA polymerase kappa;
DE EC=2.7.7.7;
DE AltName: Full=Meiotically up-regulated gene 40 protein;
GN Name=mug40; ORFNames=SPCC553.07c;
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, INTERACTION WITH HUS1 AND RAD17, AND SUBCELLULAR LOCATION.
RX PubMed=12514100; DOI=10.1101/gad.1043203;
RA Kai M., Wang T.S.-F.;
RT "Checkpoint activation regulates mutagenic translesion synthesis.";
RL Genes Dev. 17:64-76(2003).
RN [3]
RP FUNCTION IN MEIOSIS.
RX PubMed=16303567; DOI=10.1016/j.cub.2005.10.038;
RA Martin-Castellanos C., Blanco M., Rozalen A.E., Perez-Hidalgo L.,
RA Garcia A.I., Conde F., Mata J., Ellermeier C., Davis L., San-Segundo P.,
RA Smith G.R., Moreno S.;
RT "A large-scale screen in S. pombe identifies seven novel genes required for
RT critical meiotic events.";
RL Curr. Biol. 15:2056-2062(2005).
RN [4]
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: DNA polymerase specifically involved in DNA repair. Plays an
CC important role in translesion synthesis, where the normal high-fidelity
CC DNA polymerases cannot proceed and DNA synthesis stalls. Has a role in
CC meiosis. {ECO:0000269|PubMed:12514100, ECO:0000269|PubMed:16303567}.
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 -!- SUBUNIT: Interacts with hus1 and rad17. {ECO:0000269|PubMed:12514100}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Associates with
CC chromatin.
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DR EMBL; CU329672; CAA19259.2; -; Genomic_DNA.
DR PIR; T41397; T41397.
DR RefSeq; NP_587767.2; NM_001022760.2.
DR AlphaFoldDB; O74944; -.
DR SMR; O74944; -.
DR BioGRID; 276108; 11.
DR STRING; 4896.SPCC553.07c.1; -.
DR MaxQB; O74944; -.
DR PaxDb; O74944; -.
DR PRIDE; O74944; -.
DR EnsemblFungi; SPCC553.07c.1; SPCC553.07c.1:pep; SPCC553.07c.
DR GeneID; 2539547; -.
DR KEGG; spo:SPCC553.07c; -.
DR PomBase; SPCC553.07c; -.
DR VEuPathDB; FungiDB:SPCC553.07c; -.
DR eggNOG; KOG2094; Eukaryota.
DR HOGENOM; CLU_012348_11_2_1; -.
DR InParanoid; O74944; -.
DR OMA; RTQFKGR; -.
DR PhylomeDB; O74944; -.
DR Reactome; R-SPO-5655862; Translesion synthesis by POLK.
DR Reactome; R-SPO-5696397; Gap-filling DNA repair synthesis and ligation in GG-NER.
DR Reactome; R-SPO-5696400; Dual Incision in GG-NER.
DR Reactome; R-SPO-6782135; Dual incision in TC-NER.
DR Reactome; R-SPO-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR PRO; PR:O74944; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0000785; C:chromatin; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; ISM:PomBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:PomBase.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0070987; P:error-free translesion synthesis; IMP:PomBase.
DR GO; GO:0042276; P:error-prone translesion synthesis; IBA:GO_Central.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0072429; P:response to intra-S DNA damage checkpoint signaling; IEP:PomBase.
DR GO; GO:0019985; P:translesion synthesis; IMP:PomBase.
DR CDD; cd03586; PolY_Pol_IV_kappa; 1.
DR Gene3D; 3.30.1490.100; -; 1.
DR Gene3D; 3.30.70.270; -; 1.
DR HAMAP; MF_01113; DNApol_IV; 1.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR036775; DNA_pol_Y-fam_lit_finger_sf.
DR InterPro; IPR017961; DNA_pol_Y-fam_little_finger.
DR InterPro; IPR022880; DNApol_IV.
DR InterPro; IPR006642; Rad18_UBZ4.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR001126; UmuC.
DR Pfam; PF00817; IMS; 1.
DR Pfam; PF11799; IMS_C; 1.
DR SUPFAM; SSF100879; SSF100879; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS50173; UMUC; 1.
DR PROSITE; PS51908; ZF_UBZ4; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; DNA damage; DNA repair; DNA replication;
KW DNA synthesis; DNA-binding; DNA-directed DNA polymerase; Magnesium;
KW Meiosis; Metal-binding; Nucleotidyltransferase; Nucleus;
KW Reference proteome; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..547
FT /note="DNA polymerase kappa"
FT /id="PRO_0000278522"
FT DOMAIN 132..316
FT /note="UmuC"
FT ZN_FING 489..518
FT /note="UBZ4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT REGION 18..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 136
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 226
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 492
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT BINDING 495
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT BINDING 509
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
FT BINDING 513
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01256"
SQ SEQUENCE 547 AA; 62055 MW; C18B08BF11336C71 CRC64;
MENAKDFIGE TIKENGLLTI EDDGSSSSDE EATLKRRLAG PSVLKSGQEN VNQKKINEII
YEASKGSKFF EAEQKRDREL RLRIEKVQVE VEKYQSKLRF DKAFQREWTI RQESVDTTVE
DFRAKRDLTQ IIVHVDCDAF YASIEELKNP KLKSLPMAVG KSVLCTANYV ARKFGVRSAM
PEFIARKICP DLVVIPLNLS EYAIKSKEIQ NVLAQYDSNL CPASIDEFYM NLTSHLRLQE
LAFTVENITM VVEKIRKQVH EETGVTVSCG IAANKLLAKI ASNKRKPNNQ FFIPFDEIGI
SKFMNDLPVR EVSGIGRVLE QQLLGLEIKT CGDIQRNLVI LSYIFLPKSF QNLLRCSYGF
GTTILDEYGE SKRKTIGSEA TFSSNLSSPS IIEYKLRLLV QNVSENLQKR GLVTNSIAIK
YKTSEFQVHT KQKSIGQFIH SESDLLKPAL QLLRQSYPMT IRLLGVRATK LVSKSRCLAM
QLKFQSQNTV PCPVCQKNIE NELGILNQHV DLCLNVETVK SLINTDHTAN PTIKKRKSNT
LDTYFLE
