ID D8RS54_SELML Unreviewed; 1419 AA.
AC D8RS54;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN ORFNames=SELMODRAFT_232193 {ECO:0000313|EMBL:EFJ25004.1};
OS Selaginella moellendorffii (Spikemoss).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Lycopodiopsida; Selaginellales; Selaginellaceae; Selaginella.
OX NCBI_TaxID=88036 {ECO:0000313|Proteomes:UP000001514};
RN [1] {ECO:0000313|EMBL:EFJ25004.1, ECO:0000313|Proteomes:UP000001514}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551031; DOI=10.1126/science.1203810;
RA Banks J.A., Nishiyama T., Hasebe M., Bowman J.L., Gribskov M.,
RA dePamphilis C., Albert V.A., Aono N., Aoyama T., Ambrose B.A., Ashton N.W.,
RA Axtell M.J., Barker E., Barker M.S., Bennetzen J.L., Bonawitz N.D.,
RA Chapple C., Cheng C., Correa L.G., Dacre M., DeBarry J., Dreyer I.,
RA Elias M., Engstrom E.M., Estelle M., Feng L., Finet C., Floyd S.K.,
RA Frommer W.B., Fujita T., Gramzow L., Gutensohn M., Harholt J., Hattori M.,
RA Heyl A., Hirai T., Hiwatashi Y., Ishikawa M., Iwata M., Karol K.G.,
RA Koehler B., Kolukisaoglu U., Kubo M., Kurata T., Lalonde S., Li K., Li Y.,
RA Litt A., Lyons E., Manning G., Maruyama T., Michael T.P., Mikami K.,
RA Miyazaki S., Morinaga S., Murata T., Mueller-Roeber B., Nelson D.R.,
RA Obara M., Oguri Y., Olmstead R.G., Onodera N., Petersen B.L., Pils B.,
RA Prigge M., Rensing S.A., Riano-Pachon D.M., Roberts A.W., Sato Y.,
RA Scheller H.V., Schulz B., Schulz C., Shakirov E.V., Shibagaki N.,
RA Shinohara N., Shippen D.E., Soerensen I., Sotooka R., Sugimoto N.,
RA Sugita M., Sumikawa N., Tanurdzic M., Theissen G., Ulvskov P., Wakazuki S.,
RA Weng J.K., Willats W.W., Wipf D., Wolf P.G., Yang L., Zimmer A.D., Zhu Q.,
RA Mitros T., Hellsten U., Loque D., Otillar R., Salamov A., Schmutz J.,
RA Shapiro H., Lindquist E., Lucas S., Rokhsar D., Grigoriev I.V.;
RT "The Selaginella genome identifies genetic changes associated with the
RT evolution of vascular plants.";
RL Science 332:960-963(2011).
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|RuleBase:RU000442};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-B family.
CC {ECO:0000256|ARBA:ARBA00005755, ECO:0000256|RuleBase:RU000442}.
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DR EMBL; GL377588; EFJ25004.1; -; Genomic_DNA.
DR RefSeq; XP_002974049.1; XM_002974003.1.
DR STRING; 88036.D8RS54; -.
DR EnsemblPlants; EFJ25004; EFJ25004; SELMODRAFT_232193.
DR Gramene; EFJ25004; EFJ25004; SELMODRAFT_232193.
DR KEGG; smo:SELMODRAFT_232193; -.
DR eggNOG; KOG0970; Eukaryota.
DR HOGENOM; CLU_001718_0_1_1; -.
DR InParanoid; D8RS54; -.
DR OMA; WNERTAD; -.
DR Proteomes; UP000001514; Unassembled WGS sequence.
DR GO; GO:0005658; C:alpha DNA polymerase:primase complex; IBA:GO_Central.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0003688; F:DNA replication origin binding; IBA:GO_Central.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IBA:GO_Central.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0006273; P:lagging strand elongation; IBA:GO_Central.
DR GO; GO:0006272; P:leading strand elongation; IBA:GO_Central.
DR GO; GO:1902975; P:mitotic DNA replication initiation; IBA:GO_Central.
DR CDD; cd05776; DNA_polB_alpha_exo; 1.
DR CDD; cd05532; POLBc_alpha; 1.
DR Gene3D; 2.40.50.730; -; 1.
DR Gene3D; 3.30.70.2820; -; 1.
DR Gene3D; 1.10.3200.20; DNA Polymerase alpha, zinc finger; 1.
DR Gene3D; 1.10.132.60; DNA polymerase family B, C-terminal domain; 1.
DR Gene3D; 1.10.287.690; Helix hairpin bin; 1.
DR Gene3D; 3.90.1600.10; Palm domain of DNA polymerase; 1.
DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR InterPro; IPR006172; DNA-dir_DNA_pol_B.
DR InterPro; IPR017964; DNA-dir_DNA_pol_B_CS.
DR InterPro; IPR006133; DNA-dir_DNA_pol_B_exonuc.
DR InterPro; IPR006134; DNA-dir_DNA_pol_B_multi_dom.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR024647; DNA_pol_a_cat_su_N.
DR InterPro; IPR042087; DNA_pol_B_thumb.
DR InterPro; IPR023211; DNA_pol_palm_dom_sf.
DR InterPro; IPR038256; Pol_alpha_znc_sf.
DR InterPro; IPR045846; POLBc_alpha.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR015088; Znf_DNA-dir_DNA_pol_B_alpha.
DR NCBIfam; TIGR00592; pol2; 1.
DR PANTHER; PTHR45861; DNA POLYMERASE ALPHA CATALYTIC SUBUNIT; 1.
DR PANTHER; PTHR45861:SF1; DNA POLYMERASE ALPHA CATALYTIC SUBUNIT; 1.
DR Pfam; PF12254; DNA_pol_alpha_N; 1.
DR Pfam; PF00136; DNA_pol_B; 1.
DR Pfam; PF03104; DNA_pol_B_exo1; 1.
DR Pfam; PF08996; zf-DNA_Pol; 1.
DR PRINTS; PR00106; DNAPOLB.
DR SMART; SM00486; POLBc; 1.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR PROSITE; PS00116; DNA_POLYMERASE_B; 1.
PE 3: Inferred from homology;
KW DNA replication {ECO:0000256|RuleBase:RU000442};
KW DNA-binding {ECO:0000256|RuleBase:RU000442};
KW DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932,
KW ECO:0000256|RuleBase:RU000442};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU000442};
KW Reference proteome {ECO:0000313|Proteomes:UP000001514};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000442};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 24..91
FT /note="DNA polymerase alpha catalytic subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12254"
FT DOMAIN 363..686
FT /note="DNA-directed DNA polymerase family B exonuclease"
FT /evidence="ECO:0000259|Pfam:PF03104"
FT DOMAIN 752..1200
FT /note="DNA-directed DNA polymerase family B
FT multifunctional"
FT /evidence="ECO:0000259|Pfam:PF00136"
FT DOMAIN 1217..1415
FT /note="Zinc finger DNA-directed DNA polymerase family B
FT alpha"
FT /evidence="ECO:0000259|Pfam:PF08996"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 86..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 179..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 785..814
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..126
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..203
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1419 AA; 158214 MW; F5BC624B1248FAFE CRC64;
MGSRENARRA AGAAGQASAR SAALEQLKRL REGGGRRVDT FELKVEEQIF DRLDEKDYAL
LVAKRRLESQ DFVVDDDGLG YADIGEEENW DVGAMPESSD EEDGAAKKKK IADPKKKRDV
PSRKERELMA AASLMGKQSV SSMFAAAGSG MSVKSSKARD FDGADQVLDD VLAAVGADSV
HRERKKKHRQ TSEAKEDTAK VEEDSLPPPP STSEKQAEDS AVSTSLVADA EVKIKVEEPS
RELPPLPFNA DHSTSENERI KAAEDSFGLG EMSALPADEM GNLSFFFLDA YEEAFGANSG
TVFLFGKVQR GGKYVSCCVA VRNIQRCVFA VPGPSVFPDG LVNTLEQEAT SSELKLKLQE
MAREMKMELS EKLMELNVSK FSMIPVKRSY AFDRMDVRSG AHYYLKLSYP FKDPTLPGDL
RGAHFTSLFG TRTSALETFL IKRRIKGPCW LSISNPHQIP CSSQISWCKV EVSVDSPKDV
ANISTLKPAF EIPRLIVASI SLKTVVNQKQ NLNEIVSASV VFCERVKVDA PMPQSEWNKQ
EMLEHFSIVR KLDGGVYPMG FSSEVSLINN KSGCSVLSCE GSERALLNCL MIKLHQLDPD
VLVGHNISGF DLDVLLHRLQ ACKVPSNVWS RVGRLKRSQM PRLVGGGNNF GGGAGPGVMS
CVAGRLLCDT YLSSRELVKE VSYTLTQLSK SQLGKERKEI SPSEIPNMFQ TSSTLFELIQ
SGETDAWLSL SLMFHLSVLP LTRQLTNISG NLWSKTLQGA RAQRVEYLLL HEFYGRKYIV
PDKVSASEKE KDNEKKRKKA QQDEDFEPDS AVEAKNKKAP AYTGGLVLEP KKGLYDKYIL
LLDFNSLYPS IIQEYNICFT TVERSSDGSI SSLPNADAPG VLPQVLKALV DRRKQVKQWL
KKTTDVLKYQ QMDIQQQALK LTANSMYGCL GFPNSRFYAK FIAELITSQG REILQSTVDL
VQNVLNLEVI YGDTDSIMIN TGLDDLLKAK SIAAQVIKEV NKKYKLLEID LDGVFKRMLL
LKKKKYACVK VETSADGKLR EVIEQRGLDI VRRDWSLLSK DVGNFILEQI LSEGSREDVV
DAIHDKLRKL QDDMRNGRIE LEKYVITKSL SKRPEDYPDS KNQPHVQVAL RRKQEGHKCF
PGDTIPYVIC CQEGVLGVPL AERARHPDEL KAGGGGCIID VDYYLSQQIH PVVSRLCTPI
EGTDPSHIAD CLGLDPSKDR YNRCEALELL CSSCAARYPF PGVSHVLTLV GEDQSEDENA
GTQSLLTHQS GTSFIFCTSD EPLSIVSPQV LDRAAEFIQR YYDCWMVCDD EMCNHTSRDT
ILRIVGDAER GAVCPNFPRC NGRLVRQYSQ VDLYNQLTHF FRLLDVNRVL QKIPERNLKA
AVAVNNLRPL VDLPAQEIKN IRDRCAYRWV QMSSLCVSV
//
