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Database: UniProt
Entry: A0A1C7MCI1_GRIFR
LinkDB: A0A1C7MCI1_GRIFR
Original site: A0A1C7MCI1_GRIFR 
ID   A0A1C7MCI1_GRIFR        Unreviewed;      1004 AA.
AC   A0A1C7MCI1;
DT   30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00012417};
DE            EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN   Name=Poll {ECO:0000313|EMBL:OBZ74633.1};
GN   ORFNames=A0H81_05614 {ECO:0000313|EMBL:OBZ74633.1};
OS   Grifola frondosa (Maitake) (Polyporus frondosus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Grifolaceae; Grifola.
OX   NCBI_TaxID=5627 {ECO:0000313|EMBL:OBZ74633.1, ECO:0000313|Proteomes:UP000092993};
RN   [1] {ECO:0000313|EMBL:OBZ74633.1, ECO:0000313|Proteomes:UP000092993}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=9006-11 {ECO:0000313|EMBL:OBZ74633.1,
RC   ECO:0000313|Proteomes:UP000092993};
RA   Min B., Park H., Kim J.-G., Cho H., Oh Y.-L., Kong W.-S., Choi I.-G.;
RT   "Whole genome sequencing of Grifola frondosa 9006-11.";
RL   Submitted (MAR-2016) 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}.
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:OBZ74633.1}.
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DR   EMBL; LUGG01000005; OBZ74633.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1C7MCI1; -.
DR   STRING; 5627.A0A1C7MCI1; -.
DR   OrthoDB; 49764at2759; -.
DR   Proteomes; UP000092993; Unassembled WGS sequence.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
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; IPR001357; BRCT_dom.
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; IPR002008; DNA_pol_X_beta-like.
DR   InterPro; IPR043519; NT_sf.
DR   InterPro; IPR029398; PolB_thumb.
DR   PANTHER; PTHR11276:SF43; DNA POLYMERASE IV; 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   PRINTS; PR00870; DNAPOLXBETA.
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; PS50172; BRCT; 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-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW   Reference proteome {ECO:0000313|Proteomes:UP000092993};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          353..440
FT                   /note="BRCT"
FT                   /evidence="ECO:0000259|PROSITE:PS50172"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          29..85
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          129..149
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          168..190
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          229..275
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          332..352
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          507..596
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          611..645
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        252..269
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        332..346
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        507..523
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        576..595
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        735
FT                   /note="Nucleophile; Schiff-base intermediate with DNA; for
FT                   5'-dRP lyase activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR622312-50"
SQ   SEQUENCE   1004 AA;  110031 MW;  CF1A57162A152681 CRC64;
     MSEVSRHTQE SFGALDAIMN LPEETSQELA ELRARAARGE RIPHPSHPSL PLMQDFNRDS
     VATAPAKESL PSPQAATDEP TSTSIRNELQ LSRTEMLIEQ HGSRLLQPGL LKSSVASGKR
     SATEALLEHA ERTKKKKKRS SSSSVHDPVV RATRTKATTN MTLITEAGPS SSAHIEVPES
     SSSAPGVNCK GKSTSSISKM SQAISAVSVP SGPLDVDMRI VDAIANIHRN VGPSSDKHKT
     GPHADTSKPV QQGPKIRVTK SSNQVASGPK PIPQDKILKI PASESDTSSA QARIACNNNI
     TTPAISEVLH ASAPSASVPE VAVKVEDKKA TASPLSKKEK GCRAGTSRGE KPTVQQYLKG
     RRIFYYGNDL RYAGVETRGR MDFIVEHGGT LVPKYDPAQI THIVTEADQL LFLSDIGLQS
     LDEIPDHIPT VEWSWVLSGL GRGGYKHPKE ANIKGKVECD DSGEQSEDEE EMLAPMDWEY
     KHASFRDQLD ADKLPWMKPG EIMPKVKGRK KQLIDKGDAS RTEIVQDSGE LSHISPFTHD
     KVPPRSATTG PPAGKQISPS SPIIPYPDDS RPGASTRNGE HSTAGKMQNT GFEPHSFSAV
     DPLAEFYARA RAESDAEPCG DDESGPSIRS DTETDDEKDL PYKRRKVARG KVTRKGGFIC
     DTKDGKKDGP CANQDVVDKL LELKKLHEAH ATNEDHWRVY SYNKSLKGIR DYPKRIKSFD
     EARTIYGVGE KTARKIMEII DKGTLDRIRF EKTEKTQVAM FFMGIYGVGP AIAENWYNAG
     CRTLEDVKAG KGGIKLTAAQ SIGLEYYSDI NTRMPRSEVE EIFNMIKPIA LEIDPDLYIE
     VMGSFRRGRA DCGDIDILIT RPTADGRTHR ENYDDLELIY RGYVARALTG CEANRSVGTL
     LASRGAALLY YTGDDGFNRS VRLKANRMGY SLNQRGLYGG VVRNPCNRRQ KTNAGAPDPP
     PSVTISPTAE FSLSLGNIIA SETEQEILAI LNVPWQEPHE RIRN
//
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