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Database: UniProt
Entry: A0A0C3P3Z2_PISTI
LinkDB: A0A0C3P3Z2_PISTI
Original site: A0A0C3P3Z2_PISTI 
ID   A0A0C3P3Z2_PISTI        Unreviewed;      1076 AA.
AC   A0A0C3P3Z2;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   05-JUN-2019, entry version 25.
DE   RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE            EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN   ORFNames=M404DRAFT_997911 {ECO:0000313|EMBL:KIO07765.1};
OS   Pisolithus tinctorius Marx 270.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Agaricomycetes; Agaricomycetidae; Boletales; Sclerodermatineae;
OC   Pisolithaceae; Pisolithus.
OX   NCBI_TaxID=870435 {ECO:0000313|EMBL:KIO07765.1, ECO:0000313|Proteomes:UP000054217};
RN   [1] {ECO:0000313|EMBL:KIO07765.1, ECO:0000313|Proteomes:UP000054217}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Marx 270 {ECO:0000313|EMBL:KIO07765.1,
RC   ECO:0000313|Proteomes:UP000054217};
RG   DOE Joint Genome Institute;
RA   Kuo A., Kohler A., Costa M.D., Nagy L.G., Floudas D., Copeland A.,
RA   Barry K.W., Cichocki N., Veneault-Fourrey C., LaButti K.,
RA   Lindquist E.A., Lipzen A., Lundell T., Morin E., Murat C., Sun H.,
RA   Tunlid A., Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.,
RA   Nordberg H.P., Cantor M.N., Hua S.X.;
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000054217}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Marx 270 {ECO:0000313|Proteomes:UP000054217};
RG   DOE Joint Genome Institute;
RG   Mycorrhizal Genomics Consortium;
RA   Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA   Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A.,
RA   Lipzen A., Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H.,
RA   Tunlid A., Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT   "Evolutionary Origins and Diversification of the Mycorrhizal
RT   Mutualists.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC         diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-
CC         COMP:11130, Rhea:RHEA-COMP:11131, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:61560, ChEBI:CHEBI:83828; EC=2.7.7.7;
CC         Evidence={ECO:0000256|RuleBase:RU000442};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|RuleBase:RU000442};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU000442}.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-B family.
CC       {ECO:0000256|RuleBase:RU000442}.
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DR   EMBL; KN831959; KIO07765.1; -; Genomic_DNA.
DR   EnsemblFungi; KIO07765; KIO07765; M404DRAFT_997911.
DR   OrthoDB; 20210at2759; -.
DR   Proteomes; UP000054217; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005657; C:replication fork; IEA:EnsemblFungi.
DR   GO; GO:0008296; F:3'-5'-exodeoxyribonuclease activity; IEA:EnsemblFungi.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0043137; P:DNA replication, removal of RNA primer; IEA:EnsemblFungi.
DR   GO; GO:0045005; P:DNA-dependent DNA replication maintenance of fidelity; IEA:EnsemblFungi.
DR   GO; GO:0006278; P:RNA-dependent DNA biosynthetic process; IEA:EnsemblFungi.
DR   Gene3D; 1.10.132.60; -; 1.
DR   Gene3D; 3.30.420.10; -; 1.
DR   Gene3D; 3.90.1600.10; -; 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; IPR042087; DNA_pol_B_C.
DR   InterPro; IPR023211; DNA_pol_palm_dom_sf.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   InterPro; IPR025687; Znf-C4pol.
DR   Pfam; PF00136; DNA_pol_B; 1.
DR   Pfam; PF03104; DNA_pol_B_exo1; 1.
DR   Pfam; PF14260; zf-C4pol; 1.
DR   PRINTS; PR00106; DNAPOLB.
DR   SMART; SM00486; POLBc; 1.
DR   SUPFAM; SSF53098; SSF53098; 1.
DR   PROSITE; PS00116; DNA_POLYMERASE_B; 1.
PE   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|RuleBase:RU000442};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000054217};
KW   DNA replication {ECO:0000256|RuleBase:RU000442};
KW   DNA-binding {ECO:0000256|RuleBase:RU000442};
KW   DNA-directed DNA polymerase {ECO:0000256|RuleBase:RU000442};
KW   Iron {ECO:0000256|RuleBase:RU000442};
KW   Iron-sulfur {ECO:0000256|RuleBase:RU000442};
KW   Metal-binding {ECO:0000256|RuleBase:RU000442};
KW   Nucleotidyltransferase {ECO:0000256|RuleBase:RU000442};
KW   Nucleus {ECO:0000256|RuleBase:RU000442};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054217};
KW   Transferase {ECO:0000256|RuleBase:RU000442};
KW   Zinc {ECO:0000256|RuleBase:RU000442};
KW   Zinc-finger {ECO:0000256|RuleBase:RU000442}.
FT   DOMAIN      108    447       DNA_pol_B_exo1. {ECO:0000259|Pfam:
FT                                PF03104}.
FT   DOMAIN      511    942       DNA_pol_B. {ECO:0000259|Pfam:PF00136}.
FT   DOMAIN      979   1054       zf-C4pol. {ECO:0000259|Pfam:PF14260}.
FT   REGION        1     41       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A0C3P3Z2}.
FT   COILED     1054   1074       {ECO:0000256|SAM:Coils}.
FT   COMPBIAS      1     18       Polar. {ECO:0000256|MobiDB-lite:
FT                                A0A0C3P3Z2}.
SQ   SEQUENCE   1076 AA;  121513 MW;  693742322AAED571 CRC64;
     MPSKNGAGLQ STQTKSRTDT EPSLKRRKLG PSGSQSTQQS SFADVLEQLT IEQSQNGAVS
     EGGADCWSRP LLKPINEKRD TIIFQQIDIE EGTDYSNGNI ILRMFGVTED GHSVMANVTD
     FPPYFYVPVP RGFDASDSGS LTEALNKASG GNYVRKIEIV MKRSLWGYRG DDWIPFMKLT
     TSEARSLPKV RGLFERGECQ FRDFFPLGQP YPTFESNVPY VLRFMIDTKV VGMNWIEIPA
     GKYKLVSEGR KSTCQIELSM RYDAFISHSP EGDWQKIAPL RILSFDIECA GRKGIFPEAN
     VDPVIQIANM VTRQGESQPF IRNVFTLKSC SHIVGSQVLS FEDEDEMLQA WRDFIEEVDP
     DLVIGYNMTN FDFPYLMDRA KHLKMTKFPY LGRLRGVKTQ VKDTHFSSKA YGQRDSKDTV
     LEGRLQLDVL QFMQREHKLR SYTLNSVCAK FLGEQKEDVH HSVITELQLG TPESRRRLAV
     YCLKDAYLPQ RLLDKLMCFV NYVEMARVTG VPFNYLLSRG QSIKVLSQLF RKANEEGYVV
     PSLKGEGTDE QYEGATVIEP KKGYYDSPIA TLDFSSLYPS IMMAHNLCYT TLLDKATIDR
     LNLVKDVDYI QTPNNDLFAT KARRKGLLPT VLEDLIGARK RAKADLKKET DPFKRAVLDG
     RQLALKISAN SVYGFTGATI GKLPCLPISS SVTSYGRQMI ERTKQEVEAE FCISNGHSHN
     AEVIYGDTDS VMVKFGPTEL KAVMDLGSQA AEFVTAKFVK PIKLEFEKVY FPYLLISKKR
     YAGLYWTKPE KYDKMDSKGI ETVRRDNCRL VQTVIETCLH KMLIDRDVQG AEEYTKRIIS
     DLLQNKVDMS QLVITKALAK SDYAAKQAHV ELAERMRQRD AGSAPALGDR VAYVIVKGIK
     GAAAYEKSED PLYVLENNIP IDTKYYLENQ LAKPLMRIFE PILGEKANSL LSGGHTRSIA
     IATPSVGGLM KFAVKTAICL GCKTPLRPNN SVLNGAVCNN CRPRIGELYR KQVSFASEQQ
     IRFSRLWTQC QRCQGSLHQD VLCSSKDCPI FYMRKKAQKD VEDANAIMER FDADLW
//
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