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Description:
DNA polymerase delta catalytic subunit (EC 2.7.7.7) (DNA polymeraseIII).
Molecular weight: 1235
View which proteins in this organism that is involved with DNA Repair;
classified after biological processes (using data from the GOA project):
DNA repair synthesis( GO:0000731 )
Important dates:
01-APR-1993, integrated into UniProtKB/Swiss-Prot.
11-JAN-2001, sequence version 2.
07-MAR-2006, entry version 53.
Phylogenetic order:
Eukaryota Fungi Ascomycota Schizosaccharomycetes Schizosaccharomycetales Schizosaccharomycetaceae Schizosaccharomyces.
To calculate the pI (Isoelectric point - the pH where a protein has a neutral charge),
go to this page and enter the protein ID (e.g 3MG_ECOLI): http://us.expasy.org/tools/pi_tool.html
Links to references in other databases for protein DPOD_SCHPO:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | X59278 | CAA41968.1 | - |
| EMBL | L07734 | AAA35303.1 | - |
| EMBL | AL121815 | CAB58156.1 | - |
| EMBL | AB027796 | BAA87100.1 | - |
| PIR | S19661 | S19661. | |
| PIR | T40242 | T40242. | |
| PIR | T43266 | T43266. | |
| HSSP | Q56366 | 1QHT | |
| GeneDB_Spombe | SPBC336.04 | -.1 | |
| BioCyc | SPOM-XXX-01:SPOM-XXX-01-004163-MONOMER | -.1 | |
| GO | GO:0005659 | C:delta DNA polymerase complex | TAS. |
| GO | GO:0003887 | F:DNA-directed DNA polymerase activity | TAS. |
| GO | GO:0005515 | F:protein binding | IPI. |
| GO | GO:0006271 | P:DNA strand elongation | TAS. |
| GO | GO:0000731 | P:DNA synthesis during DNA repair | TAS. |
| InterPro | IPR006172 | DNA_pol_B. | |
| InterPro | IPR006133 | DNA_pol_B_exo. | |
| InterPro | IPR006134 | DNA_pol_B_region. | |
| InterPro | IPR004578 | Pol2. | |
| InterPro | IPR012337 | RNaseH_fold. | |
| Pfam | PF00136 | DNA_pol_B | 1. |
| Pfam | PF03104 | DNA_pol_B_exo | 1. |
| PRINTS | PR00106 | DNAPOLB. | |
| SMART | SM00486 | POLBc | 1. |
| TIGRFAMs | TIGR00592 | pol2 | 1. |
| PROSITE | PS00116 | DNA_POLYMERASE_B | 1. |
Keywords:
Complete proteome; DNA replication; DNA-binding; DNA-directed DNA polymerase; Exonuclease; Hydrolase; Metal-binding; Nuclear protein; Nuclease; Nucleotidyltransferase; Transferase; Zinc; Zinc-finger.
References:
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX MEDLINE=92071954; PubMed=1960723;
RA Pignede G., Bouvier D., de Recondo A.M., Baldacci G.;
RT "Characterization of the POL3 gene product from Schizosaccharomyces
RT pombe indicates inter-species conservation of the catalytic subunit of
RT DNA polymerase delta.";
RL J. Mol. Biol. 222:209-218(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX MEDLINE=93184400; PubMed=8443413;
RA Park H., Francesconi S., Wang T.S.F.;
RT "Cell cycle expression of two replicative DNA polymerases alpha and
RT delta from Schizosaccharomyces pombe.";
RL Mol. Biol. Cell 4:145-157(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972;
RX MEDLINE=21848401; 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.,
RA Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
RA Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
RA Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
RA James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
RA Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
RA Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
RA Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
RA Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
RA Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
RA Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
RA Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
RA Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
RA Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
RA Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
RA Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
RA Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
RA Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
RA Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
RA Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
RA Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
RA Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 272-455.
RC STRAIN=968 h90;
RX MEDLINE=20223868; PubMed=10759889;
RX DOI=10.1046/j.1365-2443.2000.00317.x;
RA Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA Hiraoka Y.;
RT "Large-scale screening of intracellular protein localization in living
RT fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL Genes Cells 5:169-190(2000).
Feature:
CHAIN 1 1086 DNA polymerase delta catalytic subunit.
/FTId=PRO_0000046453.
ZN_FING 993 1011 C4-type (Potential).
ZN_FING 1040 1058 C4-type (Potential).
CONFLICT 102 102 Q -> E (in Ref. 1).
CONFLICT 290 290 K -> Q (in Ref. 4).
CONFLICT 419 419 T -> S (in Ref. 1).
CONFLICT 545 545 R -> C (in Ref. 1 and 2).
CONFLICT 777 784 KLEFEKVY -> NWSFST (in Ref. 1).
CONFLICT 866 866 L -> H (in Ref. 1).
Comments:
-!- FUNCTION: This polymerase possesses two enzymatic activities: DNA
synthesis (polymerase) and an exonucleolytic activity that
degrades single stranded DNA in the 3' to 5' direction.
-!- CATALYTIC ACTIVITY: Deoxynucleoside triphosphate + DNA(n) =
diphosphate + DNA(n+1).
-!- SUBUNIT: Heterotetramer that consist of the pol3, cdc1, cdc27 and
cdm1 subunits. The pol3 subunit contains the polymerase active
site and most likely the active site for the 3'-5' exonuclease
activity.
-!- SUBCELLULAR LOCATION: Nucleus.
-!- MISCELLANEOUS: In eukaryotes there are five DNA polymerases:
alpha, beta, gamma, delta, and epsilon which are responsible for
different reactions of DNA synthesis.
-!- SIMILARITY: Belongs to the DNA polymerase type-B family.
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Sequence length: 1086
MTDRSSNEGV VLNKENYPFP RRNGSIHGEI TDVKRRRLSE RNGYGDKKGS SSKEKTSSFE
DELAEYASQL DQDEIKSSKD QQWQRPALPA INPEKDDIYF QQIDSEEFTE GSVPSIRLFG
VTDNGNSILV HVVGFLPYFY VKAPVGFRPE MLERFTQDLD ATCNGGVIDH CIIEMKENLY
GFQGNEKSPF IKIFTTNPRI LSRARNVFER GEFNFEELFP VGVGVTTFES NTQYLLRFMI
DCDVVGMNWI HLPASKYQFR YQNRVSNCQI EAWINYKDLI SLPAEGQWSK MAPLRIMSFD
IECAGRKGVF PDPSIDPVIQ IASIVTQYGD STPFVRNVFC VDTCSQIVGT QVYEFQNQAE
MLSSWSKFVR DVDPDVLIGY NICNFDIPYL LDRAKSLRIH NFPLLGRIHN FFSVAKETTF
SSKAYGTRES KTTSIPGRLQ LDMLQVMQRD FKLRSYSLNA VCSQFLGEQK EDVHYSIITD
LQNGTADSRR RLAIYCLKDA YLPQRLMDKL MCFVNYTEMA RVTGVPFNFL LARGQQIKVI
SQLFRKALQH DLVVPNIRVN GTDEQYEGAT VIEPIKGYYD TPIATLDFSS LYPSIMQAHN
LCYTTLLDSN TAELLKLKQD VDYSVTPNGD YFVKPHVRKG LLPIILADLL NARKKAKADL
KKETDPFKKA VLDGRQLALK VSANSVYGFT GATNGRLPCL AISSSVTSYG RQMIEKTKDV
VEKRYRIENG YSHDAVVIYG DTDSVMVKFG VKTLPEAMKL GEEAANYVSD QFPNPIKLEF
EKVYFPYLLI SKKRYAGLFW TRTDTYDKMD SKGIETVRRD NCPLVSYVID TALRKMLIDQ
DVEGAQLFTK KVISDLLQNK IDMSQLVITK ALSKTDYAAK MAHVELAERM RKRDAGSAPA
IGDRVAYVII KGAQGDQFYM RSEDPIYVLE NNIPIDAKYY LENQLSKPLL RIFEPILGEK
ASSLLHGDHT RTISMAAPSV GGIMKFAVKV ETCLGCKAPI KKGKTALCEN CLNRSAELYQ
RQVAQVNDLE VRFARLWTQC QRCQGSMHQD VICTSRDCPI FYMRIAEHKK LQQSVDLLKR
FDEMSW