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Database: UniProt
Entry: A0A395SEE7_FUSSP
LinkDB: A0A395SEE7_FUSSP
Original site: A0A395SEE7_FUSSP 
ID   A0A395SEE7_FUSSP        Unreviewed;      1138 AA.
AC   A0A395SEE7;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00012417};
DE            EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
DE   AltName: Full=Mitochondrial DNA polymerase catalytic subunit {ECO:0000256|ARBA:ARBA00031966};
GN   ORFNames=FSPOR_3798 {ECO:0000313|EMBL:RGP70778.1};
OS   Fusarium sporotrichioides.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX   NCBI_TaxID=5514 {ECO:0000313|EMBL:RGP70778.1, ECO:0000313|Proteomes:UP000266152};
RN   [1] {ECO:0000313|EMBL:RGP70778.1, ECO:0000313|Proteomes:UP000266152}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 3299 {ECO:0000313|EMBL:RGP70778.1,
RC   ECO:0000313|Proteomes:UP000266152};
RX   PubMed=29649280; DOI=10.1371/journal.ppat.1006946;
RA   Proctor R.H., McCormick S.P., Kim H.S., Cardoza R.E., Stanley A.M.,
RA   Lindo L., Kelly A., Brown D.W., Lee T., Vaughan M.M., Alexander N.J.,
RA   Busman M., Gutierrez S.;
RT   "Evolution of structural diversity of trichothecenes, a family of toxins
RT   produced by plant pathogenic and entomopathogenic fungi.";
RL   PLoS Pathog. 14:e1006946-e1006946(2018).
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-A family.
CC       {ECO:0000256|ARBA:ARBA00007705}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RGP70778.1}.
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DR   EMBL; PXOF01000049; RGP70778.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A395SEE7; -.
DR   STRING; 5514.A0A395SEE7; -.
DR   Proteomes; UP000266152; Unassembled WGS sequence.
DR   GO; GO:0005760; C:gamma DNA polymerase complex; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006264; P:mitochondrial DNA replication; IEA:InterPro.
DR   CDD; cd08641; DNA_pol_gammaA; 1.
DR   Gene3D; 3.30.420.390; -; 2.
DR   Gene3D; 3.30.70.370; -; 1.
DR   Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR   InterPro; IPR019760; DNA-dir_DNA_pol_A_CS.
DR   InterPro; IPR002297; DNA-dir_DNA_pol_A_mt.
DR   InterPro; IPR001098; DNA-dir_DNA_pol_A_palm_dom.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR041336; DNApol_Exo.
DR   InterPro; IPR047580; POLG_palm_dom.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   PANTHER; PTHR10267; DNA POLYMERASE SUBUNIT GAMMA-1; 1.
DR   PANTHER; PTHR10267:SF0; DNA POLYMERASE SUBUNIT GAMMA-1; 1.
DR   Pfam; PF00476; DNA_pol_A; 1.
DR   Pfam; PF18136; DNApol_Exo; 1.
DR   PRINTS; PR00867; DNAPOLG.
DR   SMART; SM00482; POLAc; 1.
DR   SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR   SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR   PROSITE; PS00447; DNA_POLYMERASE_A; 1.
PE   3: Inferred from homology;
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW   Reference proteome {ECO:0000313|Proteomes:UP000266152};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          693..923
FT                   /note="DNA-directed DNA polymerase family A palm"
FT                   /evidence="ECO:0000259|SMART:SM00482"
SQ   SEQUENCE   1138 AA;  129364 MW;  303B3A5CB93D88B8 CRC64;
     MFVPAAASPF RGSTACFSRI AHHQGFRRHA LRNQVRWLAA VADNAKSEKL KTLALPSEAR
     HNEIGVQQLS SHVFEQIFPD GVKPPPQELV ELSKDHLRRH DLLGKNTDKS EPIAFDIPPL
     QGRTLDEHFH KLGIDAAEPF LTYAKQFARA NPPPKPRQWV HQSGWTKYYP DGTTEKVEAP
     DEEMLSFDTE VMWKISPFAV MACASSPTAW YAWLSPWLMG ETENDRQLIP FGDPTKDRII
     VGHNVGFDRA RVLEEYSMTQ TRNAFLDTMS LHVAVNGMCS QQRPTWMMHK KNREMRERVA
     TETPDHDLAT MLSTQGIHDE ADLWVERSSV NSLRDVAKFH LNVSIDKTIR NDFGELDREG
     VLAKLDELLT YCAADVSITH RIYQIVFPNF LSTCPHPVSF AALRHLSSVI LPVDSSWDVY
     IKNAEATYQK LSDAVQERLI GLTETALKMK DNPDEYENDP WMQQLDWSGQ EIKMAKGKGD
     EPPRPVARQK KPGMPRWYKD LFQTNDSPIN ITVRTRVAPL LLKMSWDGYP LFWSDKYGWT
     FRVPRAEATK YTAKQAVECK FDETEIKLRD DHAHSYFKLP HKDGPTARCA NPMAKGYLSY
     FESGMLSSEY TYAKEALEMN ASCSYWISAR DRIKSQMVVY DKDIRKLNKT RGRRKLNDPG
     FILPQIIPMG TITRRAVENT WLTASNAKKN RVGSELKAMV KAPKGYCFVG ADVDSEELWI
     ASLVGDATFK LHGGNAVGFM TLEGTKSAGT DLHSRTASIL GITRNNAKIF NYGRIYGAGL
     KFAATLLRQF NPNLSEKQTM DTASRLYANT KGTKTNRKVL YKRPFWRGGT ESFVFNKLEE
     FAEQDKARTP VLGAGITEAL MGRYISKGGY LTSRINWAIQ SSGVDYLHLL VVAMDYLIRR
     FNIDARVALT VHDEIRYLVN DKDKYRTALA LQVANVWTRA MFSQQVGIND LPQSCAYFSA
     VDIDHVLRKE VDMECITPSH QTPISPGESI DINTLLEKGE AARLDPAIVP DPKYAPKLDH
     IEYTPRVPVM EGIQESAQET LPFLKAQIAS DEKEIRDIVY TLQKERIAAM PKKERPLSKK
     ELQGVLPYRA YPQLMPMDEP FILTEAMKEN QNAYANKNNN KLGLGKYSNR MYRPTWRV
//
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