ID A0A1J4L180_9EUKA Unreviewed; 1343 AA.
AC A0A1J4L180;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN ORFNames=TRFO_41265 {ECO:0000313|EMBL:OHT17170.1};
OS Tritrichomonas foetus.
OC Eukaryota; Metamonada; Parabasalia; Tritrichomonadida; Tritrichomonadidae;
OC Tritrichomonas.
OX NCBI_TaxID=1144522 {ECO:0000313|EMBL:OHT17170.1, ECO:0000313|Proteomes:UP000179807};
RN [1] {ECO:0000313|Proteomes:UP000179807}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K {ECO:0000313|Proteomes:UP000179807};
RA Benchimol M., Almeida L.G., Vasconcelos A.T., Perreira-Neves A., Rosa I.A.,
RA Tasca T., Bogo M.R., de Souza W.;
RL Submitted (OCT-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|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:OHT17170.1}.
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DR EMBL; MLAK01000033; OHT17170.1; -; Genomic_DNA.
DR VEuPathDB; TrichDB:TRFO_41265; -.
DR OrthoDB; 211439at2759; -.
DR Proteomes; UP000179807; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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 CDD; cd05776; DNA_polB_alpha_exo; 1.
DR Gene3D; 2.40.50.730; -; 1.
DR Gene3D; 3.30.70.2820; -; 1.
DR Gene3D; 1.10.3200.20; DNA Polymerase alpha, zinc finger; 1.
DR Gene3D; 1.10.132.60; DNA polymerase family B, C-terminal domain; 2.
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; IPR038256; Pol_alpha_znc_sf.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR015088; Znf_DNA-dir_DNA_pol_B_alpha.
DR PANTHER; PTHR45861; DNA POLYMERASE ALPHA CATALYTIC SUBUNIT; 1.
DR PANTHER; PTHR45861:SF1; DNA POLYMERASE ALPHA CATALYTIC SUBUNIT; 1.
DR Pfam; PF00136; DNA_pol_B; 3.
DR Pfam; PF03104; DNA_pol_B_exo1; 1.
DR Pfam; PF08996; zf-DNA_Pol; 1.
DR PRINTS; PR00106; DNAPOLB.
DR SMART; SM00486; POLBc; 1.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 2.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR PROSITE; PS00116; DNA_POLYMERASE_B; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU000442};
KW Reference proteome {ECO:0000313|Proteomes:UP000179807};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000442};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 131..395
FT /note="DNA-directed DNA polymerase family B exonuclease"
FT /evidence="ECO:0000259|Pfam:PF03104"
FT DOMAIN 460..582
FT /note="DNA-directed DNA polymerase family B
FT multifunctional"
FT /evidence="ECO:0000259|Pfam:PF00136"
FT DOMAIN 678..867
FT /note="DNA-directed DNA polymerase family B
FT multifunctional"
FT /evidence="ECO:0000259|Pfam:PF00136"
FT DOMAIN 1037..1130
FT /note="DNA-directed DNA polymerase family B
FT multifunctional"
FT /evidence="ECO:0000259|Pfam:PF00136"
FT DOMAIN 1168..1283
FT /note="Zinc finger DNA-directed DNA polymerase family B
FT alpha"
FT /evidence="ECO:0000259|Pfam:PF08996"
FT REGION 862..884
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1316..1343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 565..606
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1316..1335
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1343 AA; 152167 MW; F6F976E910B8DF53 CRC64;
MTEDTKKPAN KSFLSDTSSD CDNEIFFENS DFIIFPVDSI DQGDASITPP PKVSLQLPAS
KTVDLFLFHV HEEGEKLYLF GKHRVGENFY TICIEVSNPY YYLQFLPIAG HEFDIAEEVC
NIAHKCKGSL VHKEMKEMRY SFDNSLIPKR ANYLCATFSS DSILSRIRPN GIHYSHVFGV
TATLSENLFV RRKIFCPSWI RATNCTKKSR YTTVPMLSVP DIDSISPISV IGTPPMNLCT
ISIRSMFKTN EIFMISTRIF CEWDLDEFTG KGTKTTTYVC SSSGGAVSPD VKPNQNLRIF
RTEKELLAAF AKLIDDYDID IMVSYGLIPN DIPLLFNRLK VKKVDDWWRI GRIRRSTSIK
NGKINPTYAL SGRIPCDIQI SFSDFIKAKS NDLSAAVHAQ FGFERQQIDH YEVVGEVKNA
EKLYNLVNYN VRDTLFIAQL VNAREILPLG LQIAQLSGCQ WSRVLLSHAS FLCEAMLIRA
YYDHGFVLPD KCITNQPKYP SFPGGLVLQP KRGFYENCVV ALDYYSLYPS IIIEYNICFT
TVNLKNPNAE ESKNSKIKGI LPEVMADLLN EREKVKVKME KLIEGLKKIE GKIEKLQKQK
SRIYLEPRSD GTLKTNHKNG HKADFKNALN LDEKADIGKI FTKNKNFVRK GSQFAQSPCS
QNASQIEDFE KKKFEMELEL QRLNTKQTAI KVLANAMYGY LGYRHSRFLA NALAALVASK
GREILQRTVE IVEKNGKDSI IYGDTDSVMI DSGTKDPIEA LAKGKEIAET VSSQFTHLKF
GVEGVFLKLL LVQKKRYVAL VYDEPGKSHQ LTKGIELVRR DWCGLTKYVS AYILEQFLYS
DDKDTATSNI LSELSRISEM LRNNGVPPTE SEKNNPNDQS SSSLSCSASN IVFTGSAAFS
NDSYTSTYTT SVSANSTNNT SNCLVNSTRD TQVQNGSDFH GPLILPTVSF PQMYGACNRR
YPTQLPRSQF QTQRSQFQTQ AQRQKQQELK VKLKDLRAGT RSTLSILREY GISSKFAPSN
ENDQNKLLER VTPLEYITIE HLIIHMTLTK AISKYQDKMA PHVMVAMRME ERGEHVLPNT
TIKYIISNFA SREIGEKARI PDEISEVSDC DAEWYLSNQI MAPIWRLCEP FGGMDAAMIA
RALGLVIPQT FGLPERDECV QVVIPHTSEL MYNCIKCGES IIIDNRMKTN LKCMKCGEFH
NWKYVSNILT NFVRNFIMKA NSAKCDGNLC DFQTIQIPIN NEISLHENCS GTLKQVYSCV
SIFNTLKYFR SLFERSNIAE DDKFSEFRDY MRLVMDNFLD AHGFMRIQLN SIFSSLSNSS
SSRTSTGSAS SNSMKTDESP RRK
//
