ID A0A091LGE3_CATAU Unreviewed; 807 AA.
AC A0A091LGE3;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
DE Flags: Fragment;
GN ORFNames=N323_08234 {ECO:0000313|EMBL:KFP55793.1};
OS Cathartes aura (Turkey vulture) (Vultur aura).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Accipitriformes; Cathartidae; Cathartes.
OX NCBI_TaxID=43455 {ECO:0000313|EMBL:KFP55793.1, ECO:0000313|Proteomes:UP000053745};
RN [1] {ECO:0000313|EMBL:KFP55793.1, ECO:0000313|Proteomes:UP000053745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N323 {ECO:0000313|EMBL:KFP55793.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) 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}.
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DR EMBL; KL324405; KFP55793.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091LGE3; -.
DR Proteomes; UP000053745; Unassembled WGS sequence.
DR GO; GO:0031981; C:nuclear lumen; IEA:UniProt.
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; 3.30.70.2820; -; 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:UP000053745};
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 2..278
FT /note="DNA-directed DNA polymerase family B exonuclease"
FT /evidence="ECO:0000259|Pfam:PF03104"
FT DOMAIN 343..794
FT /note="DNA-directed DNA polymerase family B
FT multifunctional"
FT /evidence="ECO:0000259|Pfam:PF00136"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFP55793.1"
FT NON_TER 807
FT /evidence="ECO:0000313|EMBL:KFP55793.1"
SQ SEQUENCE 807 AA; 91868 MW; 146C5AF8B5198486 CRC64;
KVEKYYAFEI PDVPAKSEYL EVKYSAECPR LPQDLKGQTF SHVFGTNTSS LELLLLSRKI
KGPCWLEIKN PQLSNQSVSW CKVEAVAMKP GLVNVVKDLS PPPPLVVMSF SMKTTQNPKT
HQNEIVAVAA LIHQKFPLDK APPQPPFQTH FCVVSKPNDC IFPYDFKEAI KKKNAKIEIA
ATERTLLGFF LAKIHKIDPD VVVGHNIYGF DLEVLLQRIN VCKVPHWSKI GRLRRSNMPK
LGGRGGFAER NAACGRMICD VEISAKELIR CKSYHLSELV RQILKTERIT VLPEEIRNMY
SDSPRLMFML ENTWTDAKFI LQIMCELNVL PLALQITNIS GNVMSRTMMG GRSERNEFLL
LHAFHEKDYI VPDKQVFKKP LQKLVDEDED FEDQNKSKIG KKKAAYAGGL VLDPKVGFYD
KFILLLDFNS LYPSIIQEFN ICFTTVQRLS SEAQKRAEVE EEEEIPELPD PSLEMGVLPK
EIRKLVERRR QVKQLMKQPD VNPDLYLQYD IRQKALKLTA NSMYGCLGFS YSRFYAKPLA
ALVTHKGREI LMHTKEMVQK MNLEVIYGDT DSIMINTNST SLDEVFKLGN KIKSEVNKLY
KLLEIDIDGV FKSLLLLKKK KYAALTVEPT GDGKYVTKQE LKGLDIVRRD WCDLAKETGN
YVIGQILSDQ PRDIIVENIQ RRLIEIGENV INGQIPVNQF EINKALTKDP QDYPDKKSLP
HVHVAMWINS QGGRKVKAGD TVSYIICQDG SDLSANQRAY APEQLQKQDN LTVDTQYYLS
QQIHPVVARI CEPIDGIDSV LIATWLG
//
