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Database: UniProt
Entry: A0A2G9FW29_9LAMI
LinkDB: A0A2G9FW29_9LAMI
Original site: A0A2G9FW29_9LAMI 
ID   A0A2G9FW29_9LAMI        Unreviewed;      1285 AA.
AC   A0A2G9FW29;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE            EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN   ORFNames=CDL12_30255 {ECO:0000313|EMBL:PIM97276.1};
OS   Handroanthus impetiginosus.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Bignoniaceae; Crescentiina; Tabebuia alliance;
OC   Handroanthus.
OX   NCBI_TaxID=429701 {ECO:0000313|EMBL:PIM97276.1, ECO:0000313|Proteomes:UP000231279};
RN   [1] {ECO:0000313|Proteomes:UP000231279}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. UFG-1 {ECO:0000313|Proteomes:UP000231279};
RX   PubMed=29253216; DOI=10.1093/gigascience/gix125;
RA   Silva-Junior O.B., Grattapaglia D., Novaes E., Collevatti R.G.;
RT   "Genome assembly of the Pink Ipe (Handroanthus impetiginosus,
RT   Bignoniaceae), a highly valued, ecologically keystone Neotropical timber
RT   forest tree.";
RL   Gigascience 7:1-16(2018).
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   -!- SIMILARITY: Belongs to the DNA polymerase type-B family.
CC       {ECO:0000256|ARBA:ARBA00005755, ECO:0000256|RuleBase:RU000442}.
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:PIM97276.1}.
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DR   EMBL; NKXS01010321; PIM97276.1; -; Genomic_DNA.
DR   STRING; 429701.A0A2G9FW29; -.
DR   OrthoDB; 211439at2759; -.
DR   Proteomes; UP000231279; Unassembled WGS sequence.
DR   GO; GO:0016035; C:zeta 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-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   GO; GO:0019985; P:translesion synthesis; IEA:InterPro.
DR   CDD; cd05778; DNA_polB_zeta_exo; 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; IPR042087; DNA_pol_B_thumb.
DR   InterPro; IPR023211; DNA_pol_palm_dom_sf.
DR   InterPro; IPR030559; PolZ_Rev3.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   PANTHER; PTHR45812; DNA POLYMERASE ZETA CATALYTIC SUBUNIT; 1.
DR   PANTHER; PTHR45812:SF1; DNA POLYMERASE ZETA CATALYTIC SUBUNIT; 1.
DR   Pfam; PF00136; DNA_pol_B; 1.
DR   Pfam; PF03104; DNA_pol_B_exo1; 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   DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204};
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   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000256|RuleBase:RU000442};
KW   Reference proteome {ECO:0000313|Proteomes:UP000231279};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000442}.
FT   DOMAIN          683..859
FT                   /note="DNA-directed DNA polymerase family B exonuclease"
FT                   /evidence="ECO:0000259|Pfam:PF03104"
FT   DOMAIN          930..1257
FT                   /note="DNA-directed DNA polymerase family B
FT                   multifunctional"
FT                   /evidence="ECO:0000259|Pfam:PF00136"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          113..165
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          577..630
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          643..662
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        118..151
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        643..660
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1285 AA;  142748 MW;  420CC2B09983A286 CRC64;
     MENVDAAETN EIDAAGKQQI SDSVGPSIAK ATDADALRLL KWLASSQAAE DINSDDELAH
     ETILSPLLPS KDIDKVLERA NVDYESESQK ECQDILDSID IPNFEESSGR DLNLAEDKHS
     SSVLSNRIIP QVDGSSDDPQ STPSSDKLLK SDNSEANPHM KVQPWPELDS NLTCTHRRKR
     PRWGSLPISC QKVSDVSHPD RFCSDDEKNE GLGTSRFMND AERLRPVKVD EKKDDSKLWS
     DVGDKNALLS PIRKPLDRNE GSKFHEKNIN STVEKCKAIH VKPTSFRFPT FGKLPLSSSK
     DSIEAGNLPK GDTPEHLVKA GCGDSYCGEN LHSCVDHELS VHDSSCEREC AHVSETEIIG
     EDFGWRVLQT GAAAAGTMPS NSALSDIVSG SDCITESGCQ TAITMCKLPD IPAEDLKGIE
     SETTLVQLKN SPYHGRNPGL ANPYNTSENV NNEAETVKLI GMTFSKKPPT IDWTYLPESE
     APVLLRNGGS NIGTSIQGRF EDNCLPFFKR NCLEELQDAS PRKCEHINNH EPLMGVPILY
     QNDGSYLFML TPALPPPSRE SVDKWLSFDC SDISRQKADA KSPSLPLSQG CSDDMMDSRD
     SQADDSNPPL PESTSLSDGS PSVPEPNQKN CRMEFMTVNK TTEKLSTGCS QDTSQISGPD
     KKMRLTPLSQ IGFRDPASIG QGQQLTLLSI EIQAESRGDL RPYPRFDAIN VIVLVFQEDD
     ESILGSYVLL CCDAAQVDKD LDAVSESNVY VFTEELQLLN HLMKVIRASD PDVLMGWDVQ
     SGSLGFLAER AAHLGIASQK EMVKEIFSES VTAEAVHLEN MIIEDEWGRT HASGIHVGGR
     IVLNIWRLMR HEVKLSMYSA EAVAETVLRL KIPYIPWKVL TKWFSSGPGR ARYRSIDYTL
     QRAKLNLQIM NQLDMINRTS ELARVFGIDF FSVLSRGSQY RVESMFLRLA HTQNYLAISP
     GNQQVANQPA MECLPLVMEP ESNFYADPVI VLDFQSLYPS MVIAYNLCFC TCLGKITPPK
     ANTLGVSSYS PDINILQNLK HELLATPNGV VYVPSKVRKG ILPRLLEEIL STRIMVKQAM
     KKLVPSERVL QRILNARQLA LKLIANVTYG YTAAGFSGRM PCAELADSIV QCGRRTLETA
     ISFVNSSDKW KARVIYGDTD SMFVLLKGRS LEEAFTIGRE IASAITEMNP SPVTLKMEKV
     YYPCFLLTKK RYVGYSYENP DQGKPIFDAK GIETVRRDTC GAVSKTMEQS LRIYFESQDI
     NKFAWVLIAQ MLLHFPLLQL WPLNQ
//
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