ID A0A139B040_GONPJ Unreviewed; 1508 AA.
AC A0A139B040;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN ORFNames=M427DRAFT_163586 {ECO:0000313|EMBL:KXS22075.1};
OS Gonapodya prolifera (strain JEL478) (Monoblepharis prolifera).
OC Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC Chytridiomycota incertae sedis; Monoblepharidomycetes; Monoblepharidales;
OC Gonapodyaceae; Gonapodya.
OX NCBI_TaxID=1344416 {ECO:0000313|EMBL:KXS22075.1, ECO:0000313|Proteomes:UP000070544};
RN [1] {ECO:0000313|EMBL:KXS22075.1, ECO:0000313|Proteomes:UP000070544}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEL478 {ECO:0000313|EMBL:KXS22075.1,
RC ECO:0000313|Proteomes:UP000070544};
RX PubMed=25977457; DOI=10.1093/gbe/evv090;
RA Chang Y., Wang S., Sekimoto S., Aerts A.L., Choi C., Clum A., LaButti K.M.,
RA Lindquist E.A., Yee Ngan C., Ohm R.A., Salamov A.A., Grigoriev I.V.,
RA Spatafora J.W., Berbee M.L.;
RT "Phylogenomic Analyses Indicate that Early Fungi Evolved Digesting Cell
RT Walls of Algal Ancestors of Land Plants.";
RL Genome Biol. Evol. 7:1590-1601(2015).
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}.
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; KQ965731; KXS22075.1; -; Genomic_DNA.
DR STRING; 1344416.A0A139B040; -.
DR OMA; MTKMNVG; -.
DR OrthoDB; 211439at2759; -.
DR Proteomes; UP000070544; 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; 6.10.10.100; -; 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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000070544};
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 17..81
FT /note="DNA polymerase alpha catalytic subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12254"
FT DOMAIN 432..734
FT /note="DNA-directed DNA polymerase family B exonuclease"
FT /evidence="ECO:0000259|Pfam:PF03104"
FT DOMAIN 801..1267
FT /note="DNA-directed DNA polymerase family B
FT multifunctional"
FT /evidence="ECO:0000259|Pfam:PF00136"
FT DOMAIN 1307..1492
FT /note="Zinc finger DNA-directed DNA polymerase family B
FT alpha"
FT /evidence="ECO:0000259|Pfam:PF08996"
FT REGION 65..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 838..877
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1453..1480
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 65..104
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..196
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1508 AA; 169008 MW; C5B4A2E09CADF72C CRC64;
MSRRRDADEG SGLSAIRKLK EAKKKGISRL EELKFDDDES IFEQVSEEDY DQIVRNRLKE
DDFVVDDDGR GYVDNGEEVW ERHHEYADNG SSEEAEEDNG RAGKRKRKKE SKVKPEARIT
TMFSKMTSKP GAAKPASAPK PAKPDSRADE DLLASVLGNL DSVVEEPAPK RPKLPTTAST
GSAVRGAPTS ASSSTVRELE RIAVFGKASD ARSAATEIAI KDFNNDNFST VAPNGDLEFN
WDDSNDVKPM EISDPLCSAE AEASSSPQAP ATAAAPALKV RAIQTRPTTS KAESSSLLPT
FAPLVEPSGN PTAATVVSAP ENSRAAGWQT VVANMSGSGE PENVSSPATT GGVPMLEAGG
SLRMYWLDAH ERAGIVYLFG KVKDKSGRFL SCCVTVNGME RNLIVVPRPY KLDESGHPTD
VPVEFLDVYN EFNELRTKYK IGEWRCKPAM RKYAFEVEGV PQEESEHLKV KYSFQQPEMK
DVPPGKTFSH VFGTGTSAME LFLLKRKVMG PCWLEIKEPQ FSSKSISWCK FEVVVSDPKQ
INAVPENEQP PSPPLTVMVI NTKTVMNQQK RTNEIVAISA LVYGAMSIED ASSRAEQSHF
RFTVIRQYND FPVPAGFQEL VAASKEKVEV CRNERGLLNF FIAQIGRHDP DVLVGHNFIG
FDLDVLLHRM KTHKVDHWSR LGRLRRTVWP KLQSGAGGTG DATFAERQVA SGRLIVDTYL
AAKEHVRSKS YSLTQLSLSQ LNIAREEIDF ERIPAYFSGS ARDLMLFVRL SQTDVYLVAK
LMFKIQILPL SKQLTNLAGN LWSRTLMGGR AERNEFLLLH EFHKLKYILP DKSFANSKKN
KQGAATAPEL DGDDEGDDEK PQDERRRGTT GRRKPAYSGG LVLEPKKGFY DMFVLLLDFN
SLYPSIIQEY NIDFTTIQRS YGDESEETLP ELPDPQAQTG VLPKILKTLV DRRRQVKSLM
KSAQGADYSS LDIRQKALKL TANSMYGCLG FSHSRFYAKP LAMLITAKGR EILQNTVDLA
TQQKLEVIYG DTDSIFLNTN TDDIKEVRRM GAEFKKVVNQ RYRLLEIEMD ALFRRMLLLK
KKKYAALVVD EKDGKLEMTM ETKGLDMVRR DWCGLSHDVS NFVLEKILSS DEGGREEIVD
KIHKYLEQVG KETRAGLIPI DKFVINKQLT KNVEDYNDAK SQPHVQVALR LKAANKTVRV
GDTVPYVIAL KTDSGSDAYG SKKEDSFAAR AYHPDDFKKD GSTLKVDVEW YLSNQVHPPI
ARLIAPIEGS DTGRIADCLG LDASKFRSNP AGVQAEMGSE VHTLDSLITD EERFKNVDKW
CPRCRHCGQQ NEFEIIRRKR AELPAIGLQC PNPECKQMMQ LPSLLAQLMD AIRTHIARYE
LFWHCCDDLG CRCETRQVSV YGRRCLMLGC RGQMNLTYTD AMLFTQLSYY ESLFDVDRLR
QKMENQPSGG GWLDAAVAVA SQYEAQLSKL REQVHRYLSK NARQFVDLSS LFKMMNLGGQ
KRQVAPIM
//
