ID Q5JET1_THEKO Unreviewed; 735 AA. AC Q5JET1; DT 15-FEB-2005, integrated into UniProtKB/TrEMBL. DT 15-FEB-2005, sequence version 1. DT 27-SEP-2017, entry version 89. DE RecName: Full=DNA polymerase II small subunit {ECO:0000256|HAMAP-Rule:MF_00325}; DE Short=Pol II {ECO:0000256|HAMAP-Rule:MF_00325}; DE EC=2.7.7.7 {ECO:0000256|HAMAP-Rule:MF_00325}; GN Name=polB {ECO:0000256|HAMAP-Rule:MF_00325}; GN OrderedLocusNames=TK1902 {ECO:0000313|EMBL:BAD86091.1}; OS Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1) OS (Pyrococcus kodakaraensis (strain KOD1)). OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae; OC Thermococcus. OX NCBI_TaxID=69014 {ECO:0000313|EMBL:BAD86091.1, ECO:0000313|Proteomes:UP000000536}; RN [1] {ECO:0000313|EMBL:BAD86091.1, ECO:0000313|Proteomes:UP000000536} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1 RC {ECO:0000313|Proteomes:UP000000536}; RX PubMed=15710748; DOI=10.1101/gr.3003105; RA Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.; RT "Complete genome sequence of the hyperthermophilic archaeon RT Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus RT genomes."; RL Genome Res. 15:352-363(2005). CC -!- FUNCTION: Possesses two activities: a DNA synthesis (polymerase) CC and an exonucleolytic activity that degrades single-stranded DNA CC in the 3' to 5' direction. Has a template-primer preference which CC is characteristic of a replicative DNA polymerase. CC {ECO:0000256|HAMAP-Rule:MF_00325}. CC -!- CATALYTIC ACTIVITY: Degradation of single-stranded DNA. It acts CC progressively in a 3'- to 5'-direction, releasing nucleoside 5'- CC phosphates. {ECO:0000256|HAMAP-Rule:MF_00325}. CC -!- CATALYTIC ACTIVITY: Deoxynucleoside triphosphate + DNA(n) = CC diphosphate + DNA(n+1). {ECO:0000256|HAMAP-Rule:MF_00325}. CC -!- SUBUNIT: Heterodimer of a large subunit and a small subunit. CC {ECO:0000256|HAMAP-Rule:MF_00325}. CC -!- SIMILARITY: Belongs to the DNA polymerase delta/II small subunit CC family. {ECO:0000256|HAMAP-Rule:MF_00325}. 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; AP006878; BAD86091.1; -; Genomic_DNA. DR ProteinModelPortal; Q5JET1; -. DR STRING; 69014.TK1902; -. DR EnsemblBacteria; BAD86091; BAD86091; TK1902. DR KEGG; tko:TK1902; -. DR PATRIC; fig|69014.16.peg.1860; -. DR eggNOG; arCOG04455; Archaea. DR eggNOG; COG1311; LUCA. DR HOGENOM; HOG000073628; -. DR InParanoid; Q5JET1; -. DR KO; K02323; -. DR OMA; FQKMVNI; -. DR OrthoDB; POG093Z01XN; -. DR Proteomes; UP000000536; Chromosome. DR GO; GO:0042575; C:DNA polymerase complex; IBA:GO_Central. DR GO; GO:0008408; F:3'-5' exonuclease activity; IEA:UniProtKB-UniRule. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule. DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-UniRule. DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IBA:GO_Central. DR GO; GO:0000738; P:DNA catabolic process, exonucleolytic; IEA:UniProtKB-UniRule. DR GO; GO:0006271; P:DNA strand elongation involved in DNA replication; IBA:GO_Central. DR Gene3D; 3.60.21.10; -; 1. DR HAMAP; MF_00325; DNApol_II_A_arch; 1. DR InterPro; IPR007185; DNA_pol_alpha/epsilon_bsu. DR InterPro; IPR024826; DNA_pol_delta/II_ssu. DR InterPro; IPR029052; Metallo-depent_PP-like. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR011149; Pol2_small_arc. DR PANTHER; PTHR10416; PTHR10416; 1. DR Pfam; PF04042; DNA_pol_E_B; 1. DR PIRSF; PIRSF000803; Arc_Pol2_small; 1. DR SUPFAM; SSF50249; SSF50249; 1. DR SUPFAM; SSF56300; SSF56300; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000000536}; KW DNA replication {ECO:0000256|HAMAP-Rule:MF_00325}; KW DNA-binding {ECO:0000256|HAMAP-Rule:MF_00325}; KW DNA-directed DNA polymerase {ECO:0000256|HAMAP-Rule:MF_00325}; KW Exonuclease {ECO:0000256|HAMAP-Rule:MF_00325}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_00325}; KW Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_00325}; KW Nuclease {ECO:0000256|HAMAP-Rule:MF_00325}; KW Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_00325}; KW Reference proteome {ECO:0000313|Proteomes:UP000000536}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00325}. FT DOMAIN 470 673 DNA_pol_E_B. {ECO:0000259|Pfam:PF04042}. SQ SEQUENCE 735 AA; 80784 MW; A84B94CBC2614C3B CRC64; MLVEDLLKNN YLITPSAYYL LSDHYKKAFT LAELIKFAKN RGTFVVDSNL AREFLAEKGI ISSGNGALDG SVLSGISVSE SPVKPNGEAV LESESDESGA IESSLQEGVE DGVESIAEPS AASVEDVVVA GESSLASEGS SLEDEINTEP ELSSSMDDGA EVVQSSEGDE TSISTGNALG SVDYGGSDSE SEALEEASSG GESFISTGTP EDEALLEESP EGEFPDENGF SDESLPVENG SENGYGDSEE YYENGDNGVK PKIVYGDYGV PIAYVADETP EEEKAYSTYS DLVIAPKEGF HYRAKEIPDE WELAFDVKNV KFEVPKVKNA QSKEGEVIIQ AYSSYFKSRL KKMRRIFREN PEIGTIVDIA KLSYVREDDV TIIGLVNEKR ETRKGYLFEI EDATGRIKVF IGSDKEGANE AYSTIMPDSV VAFRGTPGKG IFFANRVFLP DVPKFKRSKP PLEEKVYAIL LSDIHVGSNK FCEEAFIKFL EWLNGEVNSR TEEELVSRIK YIIIGGDVVD GVGIYPGQYN ELAIPDIFDQ YEALANLLKQ VPDHITMFIG PGNHDAARTA LPQPGFYEEY AKPLYKLKNA VIISNPAVIR LHGRDFLVAH GRGIEDVVDF VPNRSHHRPA EAMVELLKLR HIAPTFGNKV PIAPDPEDTL VIESVPDLFQ AGHVHVMQYK TYNGVFVINT GTWQAQTEFQ KMVNIIPTPA RVPIIDVETA RLRAVVRFDQ FCEGV //