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Database: UniProt
Entry: A0A433UQP1_ANAVA
LinkDB: A0A433UQP1_ANAVA
Original site: A0A433UQP1_ANAVA 
ID   A0A433UQP1_ANAVA        Unreviewed;       977 AA.
AC   A0A433UQP1;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=DNA polymerase I {ECO:0000256|ARBA:ARBA00020311, ECO:0000256|RuleBase:RU004460};
DE            EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417, ECO:0000256|RuleBase:RU004460};
GN   Name=polA {ECO:0000256|RuleBase:RU004460,
GN   ECO:0000313|EMBL:RUS96139.1};
GN   ORFNames=DSM107003_28010 {ECO:0000313|EMBL:RUS96139.1};
OS   Trichormus variabilis SAG 1403-4b.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae;
OC   Trichormus.
OX   NCBI_TaxID=447716 {ECO:0000313|EMBL:RUS96139.1, ECO:0000313|Proteomes:UP000276103};
RN   [1] {ECO:0000313|EMBL:RUS96139.1, ECO:0000313|Proteomes:UP000276103}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SAG 1403-4b {ECO:0000313|EMBL:RUS96139.1,
RC   ECO:0000313|Proteomes:UP000276103};
RX   PubMed=30590650;
RA   Will S.E., Henke P., Boedeker C., Huang S., Brinkmann H., Rohde M.,
RA   Jarek M., Friedl T., Seufert S., Schumacher M., Overmann J.,
RA   Neumann-Schaal M., Petersen J.;
RT   "Day and night: Metabolic profiles and evolutionary relationships of six
RT   axenic non-marine cyanobacteria.";
RL   Genome Biol. Evol. 0:0-0(2018).
CC   -!- FUNCTION: In addition to polymerase activity, this DNA polymerase
CC       exhibits 5'-3' exonuclease activity. {ECO:0000256|RuleBase:RU004460}.
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         ECO:0000256|RuleBase:RU004460};
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-A family.
CC       {ECO:0000256|ARBA:ARBA00007705, ECO:0000256|RuleBase:RU004460}.
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:RUS96139.1}.
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DR   EMBL; RSCM01000008; RUS96139.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A433UQP1; -.
DR   OrthoDB; 9806424at2; -.
DR   Proteomes; UP000276103; Unassembled WGS sequence.
DR   GO; GO:0008408; F:3'-5' exonuclease activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR   GO; GO:0006261; P:DNA-templated DNA replication; IEA:UniProtKB-UniRule.
DR   CDD; cd08637; DNA_pol_A_pol_I_C; 1.
DR   CDD; cd06139; DNA_polA_I_Ecoli_like_exo; 1.
DR   CDD; cd09898; H3TH_53EXO; 1.
DR   CDD; cd09859; PIN_53EXO; 1.
DR   Gene3D; 3.30.70.370; -; 1.
DR   Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 2.
DR   Gene3D; 3.40.50.1010; 5'-nuclease; 1.
DR   Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR   InterPro; IPR002562; 3'-5'_exonuclease_dom.
DR   InterPro; IPR020046; 5-3_exonucl_a-hlix_arch_N.
DR   InterPro; IPR002421; 5-3_exonuclease.
DR   InterPro; IPR036279; 5-3_exonuclease_C_sf.
DR   InterPro; IPR001098; DNA-dir_DNA_pol_A_palm_dom.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR020045; DNA_polI_H3TH.
DR   InterPro; IPR018320; DNA_polymerase_1.
DR   InterPro; IPR002298; DNA_polymerase_A.
DR   InterPro; IPR008918; HhH2.
DR   InterPro; IPR029060; PIN-like_dom_sf.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   NCBIfam; TIGR00593; pola; 1.
DR   PANTHER; PTHR10133; DNA POLYMERASE I; 1.
DR   PANTHER; PTHR10133:SF62; DNA POLYMERASE THETA; 1.
DR   Pfam; PF01367; 5_3_exonuc; 1.
DR   Pfam; PF02739; 5_3_exonuc_N; 1.
DR   Pfam; PF00476; DNA_pol_A; 1.
DR   Pfam; PF01612; DNA_pol_A_exo1; 1.
DR   PRINTS; PR00868; DNAPOLI.
DR   SMART; SM00474; 35EXOc; 1.
DR   SMART; SM00475; 53EXOc; 1.
DR   SMART; SM00279; HhH2; 1.
DR   SMART; SM00482; POLAc; 1.
DR   SUPFAM; SSF47807; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR   SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR   SUPFAM; SSF88723; PIN domain-like; 1.
DR   SUPFAM; SSF53098; Ribonuclease H-like; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|RuleBase:RU004460};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|RuleBase:RU004460};
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705,
KW   ECO:0000256|RuleBase:RU004460};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU004460};
KW   DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932,
KW   ECO:0000256|RuleBase:RU004460}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000256|RuleBase:RU004460};
KW   Reference proteome {ECO:0000313|Proteomes:UP000276103};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT   DOMAIN          16..287
FT                   /note="5'-3' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00475"
FT   DOMAIN          362..548
FT                   /note="3'-5' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00474"
FT   DOMAIN          720..941
FT                   /note="DNA-directed DNA polymerase family A palm"
FT                   /evidence="ECO:0000259|SMART:SM00482"
FT   COILED          580..607
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   977 AA;  108830 MW;  C06008C87F3C7720 CRC64;
     MSKHSVNQLI SDSPTSPTII LVDGHSLAFR SYFAFAKGKN GGLRTKAGIP TSVCFGFLKC
     LLEVITTQQP QAIAVAFDLK LPTFRHEADN TYKAGRAETP EDFIPDLANL QELLNGFNLP
     VLTAPGYEAD DILGTLAQKA AGAGYRVKIL SGDKDLFQLI DADKEITVLN FSPEALKRST
     NSITEFRAEQ VKEKLGVLPT QIVDFKALCG DKSDNIPGVK GIGEKTAVKL LNNYNSLDNI
     YASLNEIQGT TKEKLIAGQE NAEKSRYLAQ IVVDVPIEVD LENCKLTGFD SSIITPILEK
     LELNNFLDKI NEIQLKFGGK VESNPQVDKP EIKNIDEDHD LWFFSAADTT EAKKQTASPI
     QPQIINTEAK LIELVNLLKT FTNPEIPVAW DTETTALEPR DANLVGIGCC WGNEANEVAY
     IPLNHKVGEN LNQDLVLEAL RPILESADYP KSLQNAKFDR LIFKCQGINL TGVVFDTMLA
     SYLINPDSSH NLSDLSQRYL GLIATNYLDL VPKGKTIADI DIPAVADYCG MDVYSTFGLV
     PKLREELEKT PDLAKLLKEV EQPLEAVLAQ MEYTGVRINS DYLQELSQQL ETELAKLEIT
     ATEIAGEKFN LGSPKQMSQI LFEKLGLSTK YSRKIQTGYS TDAATLEKLQ EVDNTGFVDA
     ILEYRTLSKL KSTYVDALPA LVHPKSQRLH TDFNQAATST GRLSSSNPNL QNIPIRTAFS
     RQIRKAFLPE SGWLMVAADY SQIELRILAH LSQEPILLKA YQQNEDIHTV TAKLVFEKEE
     VTSEERRFAK TINFGVIYGM GSLKFARSTG VDKANANEFI KRFNERYPQV FKYLEGVKKQ
     AISQGYVETI LGRRRYFDFT SNSLRDLKNR NIEDIDLSKL KNLGAYDAGL LRSAANAPIQ
     GSSADIIKIA MVQLHEVLKN YQARLLLQVH DELVFEVPPQ EWEELQPQIK SVMENAVSLS
     VPLLVDVRAG ENWMETK
//
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