ID A0A453G0L6_AEGTS Unreviewed; 1589 AA.
AC A0A453G0L6;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
OS Aegilops tauschii subsp. strangulata (Goatgrass).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Aegilops.
OX NCBI_TaxID=200361 {ECO:0000313|EnsemblPlants:AET3Gv20847500.34, ECO:0000313|Proteomes:UP000015105};
RN [1] {ECO:0000313|Proteomes:UP000015105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. AL8/78 {ECO:0000313|Proteomes:UP000015105};
RX PubMed=25035499; DOI=10.1126/science.1250092;
RG International Wheat Genome Sequencing Consortium,;
RA Marcussen T., Sandve S.R., Heier L., Spannagl M., Pfeifer M.,
RA Jakobsen K.S., Wulff B.B., Steuernagel B., Mayer K.F., Olsen O.A.;
RT "Ancient hybridizations among the ancestral genomes of bread wheat.";
RL Science 345:1250092-1250092(2014).
RN [2] {ECO:0000313|Proteomes:UP000015105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. AL8/78 {ECO:0000313|Proteomes:UP000015105};
RX PubMed=29158546; DOI=10.1038/s41477-017-0067-8;
RA Zhao G., Zou C., Li K., Wang K., Li T., Gao L., Zhang X., Wang H., Yang Z.,
RA Liu X., Jiang W., Mao L., Kong X., Jiao Y., Jia J.;
RT "The Aegilops tauschii genome reveals multiple impacts of transposons.";
RL Nat. Plants 3:946-955(2017).
RN [3] {ECO:0000313|EnsemblPlants:AET3Gv20847500.34}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (MAR-2019) to UniProtKB.
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 STRING; 200361.A0A453G0L6; -.
DR EnsemblPlants; AET3Gv20847500.34; AET3Gv20847500.34; AET3Gv20847500.
DR Gramene; AET3Gv20847500.34; AET3Gv20847500.34; AET3Gv20847500.
DR Proteomes; UP000015105; Chromosome 3D.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:1902975; P:mitotic DNA replication initiation; IEA:InterPro.
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:UP000015105};
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 79..145
FT /note="DNA polymerase alpha catalytic subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12254"
FT DOMAIN 509..817
FT /note="DNA-directed DNA polymerase family B exonuclease"
FT /evidence="ECO:0000259|Pfam:PF03104"
FT DOMAIN 883..1344
FT /note="DNA-directed DNA polymerase family B
FT multifunctional"
FT /evidence="ECO:0000259|Pfam:PF00136"
FT DOMAIN 1384..1585
FT /note="Zinc finger DNA-directed DNA polymerase family B
FT alpha"
FT /evidence="ECO:0000259|Pfam:PF08996"
FT REGION 1..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 139..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 237..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 316..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 927..965
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..51
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 945..959
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1589 AA; 176515 MW; 3D6177741037A34D CRC64;
RQSHARTFTI DPRSPCPRLI QRKSPRERDR RERERERGRG RAREGGRGEA MDDAPADAAG
SGRRTRTRGT EAVARSAALE RLRAIRGGGA RSAAAVQVRM EDPIYDTVAE EDYAALVARR
REDAGAFIID DDGLGYVDDG REEDWTHRAL PSSSDEGSGG EDGAPRKRKQ PRPPQAKRPP
QQSAAAASLS AAAAMMGKQR LSSMFTSSVF KKPGSDRTKG SSLAADSIVD DVIAEFAPDE
NDREERRRRV GRVSAPTPTP APVAQIKAIQ AAVHAEMEVR SDNGFEPDVV SDHGNDMEVE
LQPEVELKPD VEMQPKLEAA PGSSTELVDE NKSSEELKQE ANGELKIEKV HRLNAKIKAE
GTRNGDMLSA TAGWMKICGE GENAGGEGEV SVNGNTDVDE SSEFELKDGA LPFYVLDAYE
EPFDINSGTV YLFGKVVIGK RFHSCCVVVK NMQRCIYAIP SSSVFPRDTI SRIEKNSTSS
DASLSLRATL HELSSGLKSE VAEKLSDLNV SNFVMTPVKR NYAFERTDVP IGEQYVLKIN
YPYKDPAVPA DLRGDHFHAL LGTNNSALEL FLIKRKIKGP SWLSISKFVA CPSTQRVSWC
KFEVTVDSPK DISVLMTSNT LEVPPVVVAA VNLKTIINEK HNVHEIVSAS VICCHQVKID
TPMRSEDWQK RGTISHFTVM RKLEGSIFPI GLTKEASDRN QKAGSNVLAL ESSERALLNR
LMIELSKLDC DVLVGHNISG FDLDVLLHRA QTCKVPSSMW SKIGRLRRSV MPRLTKGNTL
YGSGASPGIM SCIAGRLLCD TYLCSRDLLR EVSYSLTQLA ETQLKKDRRE VSPHDIPPMF
QSAGTLLKLV EYGETDAWLS LELMFHLSVL PLTRQLTNIS GNLWGKTLQG ARAQRVEYLL
LHSFHAKKFI IPDKFAARNK ELNSAKRKLN ADTEGGNAAD GAADPSIDDE VHHGDQGKAR
KGPSYAGGLV LEPKKGLYDK YILLLDFNSL YPSIIQEFNI CFTTVERSSD GNLPNLPTSK
ASGVLPELLK SLVERRRMVK SWLKTASGLK RQQFDIQQQA LKLTANSMYG CLGFSNSRFF
AKPLAELITL QGREILQNTV DLVQNNLNLE VIYGDTDSIM IYTGLDDISK AKAIAGKVIQ
EVNKKYRCLE IDLDGVYKRM LLLKKKKYAA IKVALDGSLR ENIERKGLDM VRRDWSMLSK
EIGDFCLNQI LSGGTCDDVI ESIHNSLVQV QAQMKSGQIE LEKYIITKSL TKAPEDYPDA
KNQPHVQVAL RLKQNGFSGC SAGDTVPYII CSQQDSDNTH SGGIAQRARH PDELKRDPNK
WMIDIEYYLS QQIHPVVSRL CASIEGTSPA RLAECLGLDS SKFQSRSIGS SNEDTSTMLL
SVIDDEDERY RGCEPLRLSC PSCTNTFECP AVSSLIASLS DPNEGKDATV NFWRRMRCPR
CPDDTDECRV SPAVLANQIK RQADNFINRY YKGLLMCDDE GCKYSTHIVN LRVMGDSERG
TICPNYPQCN GRLVRQYTEA DLYRQLSYFC YVLDATRCLD KLDQKMRLPF EKEFAVLNQT
ISSAFLEIQR IRDRCAFGWV QLTDLAVSI
//
