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Database: UniProt
Entry: A0A0H2S450_9AGAM
LinkDB: A0A0H2S450_9AGAM
Original site: A0A0H2S450_9AGAM 
ID   A0A0H2S450_9AGAM        Unreviewed;       560 AA.
AC   A0A0H2S450;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00012417};
DE            EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN   ORFNames=SCHPADRAFT_865782 {ECO:0000313|EMBL:KLO18882.1};
OS   Schizopora paradoxa.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Hymenochaetales; Schizoporaceae; Schizopora.
OX   NCBI_TaxID=27342 {ECO:0000313|EMBL:KLO18882.1, ECO:0000313|Proteomes:UP000053477};
RN   [1] {ECO:0000313|EMBL:KLO18882.1, ECO:0000313|Proteomes:UP000053477}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KUC8140 {ECO:0000313|EMBL:KLO18882.1,
RC   ECO:0000313|Proteomes:UP000053477};
RG   DOE Joint Genome Institute;
RA   Min B., Park H., Jang Y., Kim J.-J., Kim K.H., Pangilinan J., Lipzen A.,
RA   Riley R., Grigoriev I.V., Spatafora J.W., Choi I.-G.;
RT   "Complete genome sequence of Schizopora paradoxa KUC8140, a cosmopolitan
RT   wood degrader in East Asia.";
RL   Submitted (APR-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-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|ARBA:ARBA00024632};
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-X family.
CC       {ECO:0000256|ARBA:ARBA00008323}.
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DR   EMBL; KQ085890; KLO18882.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0H2S450; -.
DR   STRING; 27342.A0A0H2S450; -.
DR   InParanoid; A0A0H2S450; -.
DR   OrthoDB; 1367231at2759; -.
DR   Proteomes; UP000053477; Unassembled WGS sequence.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:InterPro.
DR   GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR   CDD; cd00141; NT_POLXc; 1.
DR   Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR   Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR   Gene3D; 1.10.150.110; DNA polymerase beta, N-terminal domain-like; 1.
DR   Gene3D; 3.30.210.10; DNA polymerase, thumb domain; 1.
DR   InterPro; IPR002054; DNA-dir_DNA_pol_X.
DR   InterPro; IPR019843; DNA_pol-X_BS.
DR   InterPro; IPR010996; DNA_pol_b-like_N.
DR   InterPro; IPR028207; DNA_pol_B_palm_palm.
DR   InterPro; IPR018944; DNA_pol_lambd_fingers_domain.
DR   InterPro; IPR027421; DNA_pol_lamdba_lyase_dom_sf.
DR   InterPro; IPR037160; DNA_Pol_thumb_sf.
DR   InterPro; IPR022312; DNA_pol_X.
DR   InterPro; IPR043519; NT_sf.
DR   InterPro; IPR029398; PolB_thumb.
DR   PANTHER; PTHR11276:SF42; DNA POLYMERASE BETA; 1.
DR   PANTHER; PTHR11276; DNA POLYMERASE TYPE-X FAMILY MEMBER; 1.
DR   Pfam; PF14792; DNA_pol_B_palm; 1.
DR   Pfam; PF14791; DNA_pol_B_thumb; 1.
DR   Pfam; PF10391; DNA_pol_lambd_f; 1.
DR   Pfam; PF14716; HHH_8; 1.
DR   PRINTS; PR00869; DNAPOLX.
DR   SMART; SM00483; POLXc; 1.
DR   SUPFAM; SSF47802; DNA polymerase beta, N-terminal domain-like; 1.
DR   SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR   SUPFAM; SSF81585; PsbU/PolX domain-like; 1.
DR   PROSITE; PS00522; DNA_POLYMERASE_X; 1.
PE   3: Inferred from homology;
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053477};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KLO18882.1}.
FT   DOMAIN          202..558
FT                   /note="DNA-directed DNA polymerase X"
FT                   /evidence="ECO:0000259|SMART:SM00483"
SQ   SEQUENCE   560 AA;  62616 MW;  36A4522EFA647F65 CRC64;
     MNSDDDESMD SPETSSSTTN SLKGIKIFIL QAKINPEVMG ALMDDAEGAG IKLVGRPEDA
     EIIVTEIRMR KRLERHMDWE VAKTKPLVTS AWLTSSAKAG YPFPCGEFAA VKDLAGETIR
     NCPDSTTCKG CAKCFSNSRS SSMQLTPDAL SPPPNPLSPP TFSPATGVTL VSDSLAWDLE
     RAKDKFDNSS RYACTRLCPL VCPNQGLVEE LRVMKQAREL EGEPRSVLAY SRAIAAIKSF
     PHRITSERQV TDLPYIGTKI GTMVADYIRT GHIPEAQAFS TSIRFRALKE LTSVHGIGPL
     TARRLYDLGL RNITDLRNYY GVNPDNDSQD IESLTPDDIQ DGKESEVGIK AVLRVYDDIT
     TLIPRAEVEE IARCVYAELC VVQKGCAYTI TGGYRRGKLM SNDVDIVFTH PTPMVDRGLC
     KKLVERLRSR RMVSHVMHLS SFRAPSALRK SQWDTLEKAL TVFRLPPETK FYDGGKRIHR
     RVDLIFAPVE VYWCAVIGWT GSTMFERDLR QWTKDKRGWK FDSTGIVKLS NSEPVLATSE
     RHVFELCGLE WIDPTMRNAD
//
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