ID M2LFK6_BAUPA Unreviewed; 1474 AA.
AC M2LFK6;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN ORFNames=BAUCODRAFT_96163 {ECO:0000313|EMBL:EMC92827.1};
OS Baudoinia panamericana (strain UAMH 10762) (Angels' share fungus)
OS (Baudoinia compniacensis (strain UAMH 10762)).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Baudoinia.
OX NCBI_TaxID=717646 {ECO:0000313|EMBL:EMC92827.1, ECO:0000313|Proteomes:UP000011761};
RN [1] {ECO:0000313|EMBL:EMC92827.1, ECO:0000313|Proteomes:UP000011761}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 10762 {ECO:0000313|EMBL:EMC92827.1,
RC ECO:0000313|Proteomes:UP000011761};
RX PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA Grigoriev I.V.;
RT "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT genomes of eighteen Dothideomycetes fungi.";
RL PLoS Pathog. 8:E1003037-E1003037(2012).
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; KB445561; EMC92827.1; -; Genomic_DNA.
DR RefSeq; XP_007680136.1; XM_007681946.1.
DR STRING; 717646.M2LFK6; -.
DR GeneID; 19117506; -.
DR KEGG; bcom:BAUCODRAFT_96163; -.
DR eggNOG; KOG0970; Eukaryota.
DR HOGENOM; CLU_001718_1_0_1; -.
DR OMA; MTKMNVG; -.
DR OrthoDB; 211439at2759; -.
DR Proteomes; UP000011761; Unassembled WGS sequence.
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; 3.90.1600.10; Palm domain of DNA polymerase; 2.
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:UP000011761};
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 9..74
FT /note="DNA polymerase alpha catalytic subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12254"
FT DOMAIN 408..715
FT /note="DNA-directed DNA polymerase family B exonuclease"
FT /evidence="ECO:0000259|Pfam:PF03104"
FT DOMAIN 781..1227
FT /note="DNA-directed DNA polymerase family B
FT multifunctional"
FT /evidence="ECO:0000259|Pfam:PF00136"
FT DOMAIN 1268..1469
FT /note="Zinc finger DNA-directed DNA polymerase family B
FT alpha"
FT /evidence="ECO:0000259|Pfam:PF08996"
FT REGION 58..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 276..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..109
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..187
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1474 AA; 165546 MW; 6D5A7C054496687D CRC64;
MPVSRAERLA QLRALRKAGK TGFDAYEVQE ADSIYETVDD EQYKQVVRKR LDEDDFVVDD
NGAGYADDGR EDWQDQRVVY EDDESEEDLP KQSKAAKRKR EDDVERQQKL NQGISKFFSA
NAAASAPKPK PVRTAEDDDF LAGLLGEVDA NVPSRAPSYG KPIKSNDRRK TRVLSPPREE
SVRSYKRLAP ENVESTPPHP IAAVVNDNDD GYYVHPQDDD VPMSDPLPSS PAAQAGERKE
QTVIKKEAAE DDDDLMEVAE AQGHAAMKTA NVNIKGSRPA PKIVKSSYPT PDSSSPTRAP
EDGIDMTAIN NVTEKLNILS SSSSEAVSAG KIAAKDALED DGTLRFFWTD YTEVNGSLCL
FGKVKNRTKG TYVSCFVKVD NILRKLYFLP REHRQRHGRD TSDEVEMSDV YEEVDGLMTK
FKVNMHKIKP CSRKYAFELP DIPREADYLK LLYPYDKPAL PMGMTGETFS HVFGTNTALF
EQFVLWKNIM GPCWLKIEGA DFQAVNNASW CKLELQVTKP NGITTVGDSD NLEAPPMTLM
SLALRTTMNV KENKNEILVA SVRFYPDVQL TDTTPPEKLP SRTFTFMRPN GEYPLGFKLE
AEKHKGQILM EKNEPALLSK LLAIIQMHDP DAFVGHKLDD VDYNVLLTRM RDRKTPGWHR
IGRLKRSDWP KNVGKGGGSF FAERHLAAGR LLCDLANDMG KSIMTACQSW SLDEMVKLYL
GGNHVRKEID NDKALAMAAT REGLMNYVKM CELDTYFIAA IALKRQLLPL SKVLTNLAGN
SWARTLSGTR AERNEYILLH EFYRNKFICP DKVYGKGAAN KKLEDTADNG DEADAADTKK
KDKFKGGLVF EPEKGLYDKF ILVMDFNSLY PSIIQEFNIC FTTVDRSDIG ADEDKVPEVP
EDTANKGILP RLIRTLVSRR REVKKLMKDK SISEEQRQTW DVKQQALKLT ANSMYGCLGY
TKSRFYARPL AALTTSKGRE ILQSTKELAE SAHALRVIYG DTDSVMVNTN KDNILEAIKM
GNEFKKAVNE RYELLEIEID NIFRRLLLHA KKKYAAINMV EDNGVWREKM EVKGLDMRRR
EYCQLSKDTS TELLNYLLSG EEPEKVVSHI HDHLRSLGEK MRSNAIPAYK YTIYTQLGKA
PKEYPNANSM PSVQVALKLM AKGKQVRAKD VMSFIICGSS GGSAENAAKN ACTLDEVLAK
DSGLVPDVEY YLHKQILPPV ERLCVPIEGT NVSLLAECLG LDTSKYRLSG ASKTSEGGRG
DEITTLESQV PDHIRFKECE GLGLLCLGCK RHFEFRGLNH QQPSTSTPEE ETTPMAVVAH
TGLTCPREDC RRTISTLALS AQLEAQIRRH TSRYYAAYLI CDDAACGIRT RQMSVYGHRC
LGPKGLAHGC SGRMRFEYGE KALYNQLLFL QGLFDVEKAV GKLGVKGEED EKVKVMAELN
RERFGVCREV VKAYLDKSGW GWVCMEGLFG FARK
//
