GenomeNet

Database: UniProt
Entry: Q66HH0_RAT
LinkDB: Q66HH0_RAT
Original site: Q66HH0_RAT 
ID   Q66HH0_RAT              Unreviewed;       495 AA.
AC   Q66HH0;
DT   11-OCT-2004, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2004, sequence version 1.
DT   27-MAR-2024, entry version 139.
DE   RecName: Full=DNA-directed DNA/RNA polymerase mu {ECO:0000256|PIRNR:PIRNR000817};
DE            EC=2.7.7.7 {ECO:0000256|PIRNR:PIRNR000817};
GN   Name=Polm {ECO:0000313|EMBL:AAH81868.1, ECO:0000313|RGD:1308247};
GN   ORFNames=rCG_35832 {ECO:0000313|EMBL:EDM00314.1};
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116 {ECO:0000313|EMBL:AAH81868.1};
RN   [1] {ECO:0000313|EMBL:AAH81868.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Lung {ECO:0000313|EMBL:AAH81868.1};
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RA   Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H.,
RA   Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M.,
RA   Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M.,
RA   Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F.,
RA   Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T.,
RA   Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F.,
RA   Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E.,
RA   Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y.,
RA   Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E.,
RA   Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y.,
RA   Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W.,
RA   Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J.,
RA   Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA   Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J.,
RA   Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W.,
RA   Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J.,
RA   Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I.,
RA   Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U.,
RA   Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A.,
RA   Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [2] {ECO:0000313|EMBL:EDM00314.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BN {ECO:0000313|EMBL:EDM00314.1};
RX   PubMed=15632090; DOI=10.1101/gr.2889405;
RA   Florea L., Di Francesco V., Miller J., Turner R., Yao A., Harris M.,
RA   Walenz B., Mobarry C., Merkulov G.V., Charlab R., Dew I., Deng Z.,
RA   Istrail S., Li P., Sutton G.;
RT   "Gene and alternative splicing annotation with AIR.";
RL   Genome Res. 15:54-66(2005).
RN   [3] {ECO:0000313|EMBL:EDM00314.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=BN {ECO:0000313|EMBL:EDM00314.1};
RA   Mural R.J., Li P.W., Adams M.D., Amanatides P.G., Baden-Tillson H.,
RA   Barnstead M., Chin S.H., Dew I., Evans C.A., Ferriera S., Flanigan M.,
RA   Fosler C., Glodek A., Gu Z., Holt R.A., Jennings D., Kraft C.L., Lu F.,
RA   Nguyen T., Nusskern D.R., Pfannkoch C.M., Sitter C., Sutton G.G.,
RA   Venter J.C., Wang Z., Woodage T., Zheng X.H., Zhong F.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Gap-filling polymerase involved in repair of DNA double-
CC       strand breaks by non-homologous end joining (NHEJ).
CC       {ECO:0000256|PIRNR:PIRNR000817}.
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:0000256|ARBA:ARBA00024632,
CC         ECO:0000256|PIRNR:PIRNR000817};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946,
CC         ECO:0000256|PIRNR:PIRNR000817, ECO:0000256|PIRSR:PIRSR000817-1};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC       ECO:0000256|PIRNR:PIRNR000817}.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-X family.
CC       {ECO:0000256|ARBA:ARBA00008323, ECO:0000256|PIRNR:PIRNR000817}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BC081868; AAH81868.1; -; mRNA.
DR   EMBL; CH473963; EDM00314.1; -; Genomic_DNA.
DR   RefSeq; NP_001011912.1; NM_001011912.1.
DR   SMR; Q66HH0; -.
DR   STRING; 10116.ENSRNOP00000018320; -.
DR   PhosphoSitePlus; Q66HH0; -.
DR   PaxDb; 10116-ENSRNOP00000018320; -.
DR   GeneID; 289757; -.
DR   KEGG; rno:289757; -.
DR   UCSC; RGD:1308247; rat.
DR   AGR; RGD:1308247; -.
DR   CTD; 27434; -.
DR   RGD; 1308247; Polm.
DR   VEuPathDB; HostDB:ENSRNOG00000013647; -.
DR   eggNOG; KOG2534; Eukaryota.
DR   HOGENOM; CLU_008698_0_1_1; -.
DR   OrthoDB; 3019669at2759; -.
DR   TreeFam; TF103012; -.
DR   Reactome; R-RNO-5693571; Nonhomologous End-Joining (NHEJ).
DR   Proteomes; UP000234681; Chromosome 14.
DR   Bgee; ENSRNOG00000013647; Expressed in lung and 18 other cell types or tissues.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0030183; P:B cell differentiation; ISO:RGD.
DR   GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IBA:GO_Central.
DR   GO; GO:0016446; P:somatic hypermutation of immunoglobulin genes; ISO:RGD.
DR   CDD; cd00141; NT_POLXc; 1.
DR   Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR   Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR   Gene3D; 3.40.50.10190; BRCT domain; 1.
DR   Gene3D; 1.10.150.110; DNA polymerase beta, N-terminal domain-like; 1.
DR   Gene3D; 3.30.210.10; DNA polymerase, thumb domain; 1.
DR   InterPro; IPR001357; BRCT_dom.
DR   InterPro; IPR036420; BRCT_dom_sf.
DR   InterPro; IPR002054; DNA-dir_DNA_pol_X.
DR   InterPro; IPR027249; DNA/RNApol_mu.
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; IPR043519; NT_sf.
DR   InterPro; IPR029398; PolB_thumb.
DR   InterPro; IPR001726; TdT/Mu.
DR   PANTHER; PTHR11276; DNA POLYMERASE TYPE-X FAMILY MEMBER; 1.
DR   PANTHER; PTHR11276:SF24; DNA-DIRECTED DNA_RNA POLYMERASE MU; 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   PIRSF; PIRSF000817; DNA_NT; 1.
DR   PIRSF; PIRSF501176; DNApol_mu; 1.
DR   PRINTS; PR00869; DNAPOLX.
DR   PRINTS; PR00871; DNAPOLXTDT.
DR   SMART; SM00483; POLXc; 1.
DR   SUPFAM; SSF52113; BRCT domain; 1.
DR   SUPFAM; SSF47802; DNA polymerase beta, N-terminal domain-like; 1.
DR   SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR   SUPFAM; SSF81585; PsbU/PolX domain-like; 1.
DR   PROSITE; PS50172; BRCT; 1.
DR   PROSITE; PS00522; DNA_POLYMERASE_X; 1.
PE   2: Evidence at transcript level;
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW   DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932};
KW   Magnesium {ECO:0000256|PIRNR:PIRNR000817, ECO:0000256|PIRSR:PIRSR000817-1};
KW   Metal-binding {ECO:0000256|PIRNR:PIRNR000817,
KW   ECO:0000256|PIRSR:PIRSR000817-1};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000256|PIRNR:PIRNR000817};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR000817};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000817}.
FT   DOMAIN          23..122
FT                   /note="BRCT"
FT                   /evidence="ECO:0000259|PROSITE:PS50172"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         330
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000817-1"
FT   BINDING         332
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000817-1"
FT   BINDING         419
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000817-1"
SQ   SEQUENCE   495 AA;  56178 MW;  1D72DC87969B20A8 CRC64;
     MLPKRRRRVR AGSPHSALAS STPPAARFPG VAIYLAEPRM GRSRRAFLTR LARSKGFRIL
     DVYSSEVTHV VMEETSAKEA ICWQKDMNAL LPDCPQPALL DISWFTESMA AGQPVPEEVR
     HRLEVAEPRK EPPISVTIPA YACQRPSPLT PHNTLLSEAL ETLAEAAGFE GKEGRFLTFY
     RAASMLKSLP YPVTSLSQLH GLPYFGEHSF RVIQELLEHG TCEEVEQIRC SERHQTMKLF
     THIFGVGVKT ASRWYQEGLR TLDELREQPQ RLTQQQKAGL QYYQDLSTPV SRAEAEALQQ
     LVEAAMREIL PGATVTLTGG FRRGKLQGHD VDFLITHPEE GQEVGLLPRV MRCLQSQGLV
     LYHQYHRSHL ADSAHILRQR STMDAFERSF CILRLPQSQQ AALEGPLHPC PTWKAVRVDL
     VVTPNSQFPF ALLGWTGSQF FERELRRFSR QEKGLCLNSH GLFDPERKTF FHATSEEDVF
     RFLGLKYLPP EQRNA
//
DBGET integrated database retrieval system