POLI_DROME
ID POLI_DROME Reviewed; 737 AA.
AC Q9VHV1;
DT 13-NOV-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=DNA polymerase iota {ECO:0000303|PubMed:11297519, ECO:0000312|FlyBase:FBgn0037554};
DE EC=2.7.7.7 {ECO:0000269|PubMed:11297519};
GN Name=PolI {ECO:0000312|FlyBase:FBgn0037554};
GN Synonyms=DNApol-iota {ECO:0000303|PubMed:11297519}, DNApolI {ECO:0000305},
GN drad30B {ECO:0000312|FlyBase:FBgn0037554};
GN ORFNames=CG7602 {ECO:0000312|FlyBase:FBgn0037554};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227 {ECO:0000312|Proteomes:UP000000803};
RN [1] {ECO:0000312|EMBL:BAB15800.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ACTIVE SITE, CATALYTIC ACTIVITY, AND
RP MUTAGENESIS OF 113-ASP-GLU-114.
RX PubMed=11297519; DOI=10.1074/jbc.m009822200;
RA Ishikawa T., Uematsu N., Mizukoshi T., Iwai S., Iwasaki H., Masutani C.,
RA Hanaoka F., Ueda R., Ohmori H., Todo T.;
RT "Mutagenic and nonmutagenic bypass of DNA lesions by Drosophila DNA
RT polymerases dpoleta and dpoliota.";
RL J. Biol. Chem. 276:15155-15163(2001).
RN [2] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3] {ECO:0000305}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4] {ECO:0000312|EMBL:AAK93186.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAK93186.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:AAK93186.1};
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
CC -!- FUNCTION: Error-prone DNA polymerase specifically involved in DNA
CC repair (PubMed:11297519). Plays an important role in translesion
CC synthesis, where the normal high-fidelity DNA polymerases cannot
CC proceed and DNA synthesis stalls (PubMed:11297519). Favors Hoogsteen
CC base-pairing in the active site (By similarity). Inserts the correct
CC base with higher fidelity opposite an adenosine template
CC (PubMed:11297519). Exhibits low fidelity and efficiency opposite a
CC thymidine template, where it will preferentially insert guanosine
CC (PubMed:11297519). Forms a Schiff base with 5'-deoxyribose phosphate at
CC abasic sites, but may not have lyase activity (By similarity).
CC {ECO:0000250|UniProtKB:Q9UNA4, ECO:0000269|PubMed:11297519}.
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:0000269|PubMed:11297519};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q9UNA4};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q9UNA4};
CC Note=Binds nucleotide much more tightly and catalyzes nucleotide
CC insertion much more efficiently in the presence of Mg(2+) than in the
CC presence of Mn(2+). {ECO:0000250|UniProtKB:Q9UNA4};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9UNA4}.
CC -!- DOMAIN: The catalytic core consists of fingers, palm and thumb
CC subdomains, but the fingers and thumb subdomains are much smaller than
CC in high-fidelity polymerases; residues from five sequence motifs of the
CC Y-family cluster around an active site cleft that can accommodate DNA
CC and nucleotide substrates with relaxed geometric constraints, with
CC consequently higher rates of misincorporation and low processivity.
CC {ECO:0000250|UniProtKB:Q9UNA4}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-Y family. {ECO:0000305}.
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DR EMBL; AB049434; BAB15800.1; -; mRNA.
DR EMBL; AE014297; AAF54198.1; -; Genomic_DNA.
DR EMBL; AE014297; AAN14307.1; -; Genomic_DNA.
DR EMBL; AE014297; AHN57226.1; -; Genomic_DNA.
DR EMBL; AY051762; AAK93186.1; -; mRNA.
DR RefSeq; NP_001287227.1; NM_001300298.1.
DR RefSeq; NP_649772.1; NM_141515.3.
DR RefSeq; NP_731214.1; NM_169207.2.
DR AlphaFoldDB; Q9VHV1; -.
DR SMR; Q9VHV1; -.
DR IntAct; Q9VHV1; 12.
DR STRING; 7227.FBpp0081293; -.
DR PaxDb; Q9VHV1; -.
DR DNASU; 40965; -.
DR EnsemblMetazoa; FBtr0081797; FBpp0081293; FBgn0037554.
DR EnsemblMetazoa; FBtr0081798; FBpp0081294; FBgn0037554.
DR EnsemblMetazoa; FBtr0339606; FBpp0308676; FBgn0037554.
DR GeneID; 40965; -.
DR KEGG; dme:Dmel_CG7602; -.
DR UCSC; CG7602-RA; d. melanogaster.
DR CTD; 40965; -.
DR FlyBase; FBgn0037554; PolI.
DR VEuPathDB; VectorBase:FBgn0037554; -.
DR eggNOG; KOG2095; Eukaryota.
DR GeneTree; ENSGT00940000159487; -.
DR HOGENOM; CLU_012348_9_0_1; -.
DR InParanoid; Q9VHV1; -.
DR OMA; KNTLYRY; -.
DR OrthoDB; 1593931at2759; -.
DR PhylomeDB; Q9VHV1; -.
DR Reactome; R-DME-5656121; Translesion synthesis by POLI.
DR SignaLink; Q9VHV1; -.
DR BioGRID-ORCS; 40965; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 40965; -.
DR PRO; PR:Q9VHV1; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0037554; Expressed in egg cell and 24 other tissues.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IDA:FlyBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0019985; P:translesion synthesis; IDA:FlyBase.
DR Gene3D; 3.30.1490.100; -; 1.
DR Gene3D; 3.30.70.270; -; 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; 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.
PE 1: Evidence at protein level;
KW DNA damage; DNA repair; DNA replication; DNA synthesis; DNA-binding;
KW DNA-directed DNA polymerase; Magnesium; Manganese; Metal-binding;
KW Nucleotidyltransferase; Nucleus; Reference proteome; Schiff base;
KW Transferase.
FT CHAIN 1..737
FT /note="DNA polymerase iota"
FT /id="PRO_0000448481"
FT DOMAIN 17..231
FT /note="UmuC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00216"
FT REGION 212..277
FT /note="DNA-binding"
FT /evidence="ECO:0000250|UniProtKB:Q9UNA4"
FT REGION 288..413
FT /note="DNA-binding"
FT /evidence="ECO:0000250|UniProtKB:Q9UNA4"
FT REGION 443..464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 482..515
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 557..581
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 607..643
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 669..686
FT /note="Ubiquitin-binding (UBM)"
FT /evidence="ECO:0000250|UniProtKB:Q6R3M4"
FT COMPBIAS 485..506
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 560..581
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 114
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00216,
FT ECO:0000269|PubMed:11297519"
FT BINDING 21
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9UNA4"
FT BINDING 26
FT /ligand="a 2'-deoxyribonucleoside 5'-triphosphate"
FT /ligand_id="ChEBI:CHEBI:61560"
FT /evidence="ECO:0000250|UniProtKB:Q9UNA4"
FT BINDING 58
FT /ligand="a 2'-deoxyribonucleoside 5'-triphosphate"
FT /ligand_id="ChEBI:CHEBI:61560"
FT /evidence="ECO:0000250|UniProtKB:Q9UNA4"
FT BINDING 113
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9UNA4"
FT MUTAGEN 113..114
FT /note="DE->AA: Loss of catalytic activity in vitro."
FT /evidence="ECO:0000269|PubMed:11297519"
SQ SEQUENCE 737 AA; 80390 MW; D2CE08BD4D999059 CRC64;
MDFASVLGKS EAHQRTIIHL DMDYFYAQVE EIRDPTLRSK ALGIQQKNIV VTCNYVARAK
GVTKLMLIAE AQRICPDLVL VNGEDLAPYR QMSQRIFDLL LNYTPLVEKL GFDENFMDVT
ALVELRQAHV AEALLRPPVG HTYPADGTPL SNCDCGCAQR LAIGTRIAQE IREELKLRLG
ITCCAGIAYN KLLAKLVGSS HEPNQQTVLV STYAEQFMRE LGDLKRVTGI GQKTQCLLLE
AGMSSVEQLQ QCDMDVMRKK FGFETATRLR DLAFGRDTSL VRPSGKPKTI GMEDACKPIS
VRTDVEERFR MLLKRLVEQV AEDGRVPIAI KVVLRKFDSQ KKSSHRETKQ ANILPSLFKT
SMCPGETGVS KVQLADGAQD KLLKIVMRLF ERIVDMSKPF NITLLGLAFS KFQERKVGSS
SIANFLIKKA DLEVQSITSL TNTSLTSPTA ESPTSDECAF RSSPTTFKPS DQFYRRRATT
ASPVPMLLDN GSESAATNSD FSDFSETEVE PSPKKSRIGR LLVSKRSRLA ADVGDSAAEV
ASPSKLRVCD LRLNSRDSEK DFPMSTTPST STSAPAPRFR TVQPPNTLLQ RIDGSLRFVT
TRTASRLSSN ASSTASSPLP SPMDDSIAMS APSTTTLPFP SPTTTAVVTS SSSTATCDAL
TNIVCPAGVD AEVFKELPVE LQTELIASWR SSLVAAVEQT NGTGAATSAA IASGAPATAT
TASGQKNTLY RYFLRNK
