ID V5B2M9_TRYCR Unreviewed; 1335 AA.
AC V5B2M9;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN ORFNames=TCDM_03897 {ECO:0000313|EMBL:ESS67450.1};
OS Trypanosoma cruzi Dm28c.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma; Schizotrypanum.
OX NCBI_TaxID=1416333 {ECO:0000313|EMBL:ESS67450.1, ECO:0000313|Proteomes:UP000017861};
RN [1] {ECO:0000313|EMBL:ESS67450.1, ECO:0000313|Proteomes:UP000017861}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Dm28c {ECO:0000313|EMBL:ESS67450.1,
RC ECO:0000313|Proteomes:UP000017861};
RX PubMed=24482508;
RA Grisard E.C., Teixeira S.M., de Almeida L.G., Stoco P.H., Gerber A.L.,
RA Talavera-Lopez C., Lima O.C., Andersson B., de Vasconcelos A.T.;
RT "Trypanosoma cruzi Clone Dm28c Draft Genome Sequence.";
RL Genome Announc. 2:e01114-13(2014).
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:ESS67450.1}.
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DR EMBL; AYLP01000031; ESS67450.1; -; Genomic_DNA.
DR EnsemblProtists; ESS67450; ESS67450; TCDM_03897.
DR VEuPathDB; TriTrypDB:TCDM_03897; -.
DR Proteomes; UP000017861; 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:1902975; P:mitotic DNA replication initiation; IEA:InterPro.
DR CDD; cd05776; DNA_polB_alpha_exo; 1.
DR CDD; cd05532; POLBc_alpha; 1.
DR Gene3D; 2.40.50.730; -; 1.
DR Gene3D; 3.30.70.2820; -; 1.
DR Gene3D; 6.10.10.100; -; 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; IPR045846; POLBc_alpha.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR NCBIfam; TIGR00592; pol2; 1.
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; 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 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:UP000017861};
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 303..601
FT /note="DNA-directed DNA polymerase family B exonuclease"
FT /evidence="ECO:0000259|Pfam:PF03104"
FT DOMAIN 673..1117
FT /note="DNA-directed DNA polymerase family B
FT multifunctional"
FT /evidence="ECO:0000259|Pfam:PF00136"
SQ SEQUENCE 1335 AA; 151005 MW; 7946B24688AEA6AE CRC64;
MEPWESCRTK EQKRETPAMV SLFSETEEEQ WQRLKEEAMI DSDEDDTNIT DGRALVLPQD
ARKRKPKKSK KSTFFSKAAH IQQQKLTQSI STSDMENLLK KYRGAVADEE DEIGIDVTKF
LQDDALESGE EEEGVTADEL ISSLLTTKNT GASKPVETTP SVPLVSLNDE IFSYEKKSVA
RQAVVNKKQN GHGSEANYVV KDTFSRDINI VTELPTHAPS KLKQSSDNVN KGYPSSGLFY
WFDAKEQPHT LSEPGTIFLF GKFYEKKREK LSFSSCCVHV KNVYRCTFLL PREGSSDTEI
IKEINDVCQK HGIGERRIRF VERYYAFEEP GIRREKNRWA KLRFPGKYPG FPIMGEFKHI
RAVMGASRSL IELFLIKKKL MGPSYLSMEN FFPATDRLSH CELEFVVDSP KNIKVDDTAR
PSPPFTLASI QLHTQLDSKG VTNEVVAASI AVYRDVNIDS GMKTEVSECF TGIRQISSDA
ALPLNLEAYC QSKGLPGVKN FGNERALLTW MASTLGNLDP DIVVGHNFIG YTIDILLNRY
HELNIPRWST IGRLDIKRFP RSQNGNSNLS NEKEACIGRL VVDTYLLSRE YYKSTNYKLE
SLATQMGVAG ITDGRGSFEP GLTVLGNDIM KSSKDLFHVL LQLLNCAVLS VRVVAFLDAI
PLTKRLTTLA GNLWSRTLYG ARSERIEYLL LHAFHDLKFV TPDKKRFDGK RGRQDLEDET
KRKTKYQGGM VLEPKSGLYS DYILLLDFNS LYPSLIQEFN ICYTTIERDE NTVSAEIPPP
ERLICTSCAA AGLPSPCSHK CVLPKVIRGL VESRREIKRL MKTEKDPSNL ATLEIRQKSL
KLTANSMYGC LGFEHSRFYA QPLAELVTRQ GRIALQNTVE LIPQISPLLR VIYGDTDSVM
IQTGIKDDIS KVRELGFEIK NKVNQRYQSL ELDIDGVFRA MLLLKKKKYA ALSVVDWQSD
GKTYKKEVKG LDMVRRDWCP LSQKVSEAVL SRVLNAEAGE DILDYVMTHM KTVADHVRAG
NYYGLEDFVI SKSLTKEPES YRGTAFPHAA VALRMKQRKE NVRVGDLIPY VICEGEHLND
KAYHVDEVRR TKGIRIDVEW YLSSQLYPPV MRLCEHIQGF SPEQLSEAMG VACHVRTERE
IQETLIVDDF SHCSLFKSRD LSECFPTAVP LQVQCTRCHQ VVPIDPHKYI NDMFSASKNS
FPNEPFELYN CVNCGQSLSV TYLANCLTQM CHKIIQQFYI SGGNAAAVRA VRAQFTYFRA
LFDVPHAPGC SPAIKAAHRN LALRCLGTDQ KLYTLSGAAR AVDVEPVDHL FFCADSFYRR
IDHLFLNVGN LFASI
//
