ID A0A3P9PHX0_POERE Unreviewed; 1478 AA.
AC A0A3P9PHX0;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
OS Poecilia reticulata (Guppy) (Acanthophacelus reticulatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=8081 {ECO:0000313|Ensembl:ENSPREP00000021442.1, ECO:0000313|Proteomes:UP000242638};
RN [1] {ECO:0000313|Proteomes:UP000242638}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Guanapo {ECO:0000313|Proteomes:UP000242638};
RA Kuenstner A., Dreyer C.;
RT "The genomic landscape of the Guanapo guppy.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPREP00000021442.1}
RP IDENTIFICATION.
RC STRAIN=Guanapo {ECO:0000313|Ensembl:ENSPREP00000021442.1};
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-B family.
CC {ECO:0000256|ARBA:ARBA00005755, ECO:0000256|RuleBase:RU000442}.
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DR RefSeq; XP_008436828.1; XM_008438606.2.
DR STRING; 8081.ENSPREP00000021442; -.
DR Ensembl; ENSPRET00000021667.1; ENSPREP00000021442.1; ENSPREG00000014453.1.
DR GeneID; 103482445; -.
DR KEGG; pret:103482445; -.
DR CTD; 5422; -.
DR GeneTree; ENSGT00550000074891; -.
DR OMA; MTKMNVG; -.
DR OrthoDB; 5477697at2759; -.
DR Proteomes; UP000242638; Unassembled WGS sequence.
DR Bgee; ENSPREG00000014453; Expressed in caudal fin and 1 other cell type or tissue.
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; 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; 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; IPR024647; DNA_pol_a_cat_su_N.
DR InterPro; IPR042087; DNA_pol_B_thumb.
DR InterPro; IPR023211; DNA_pol_palm_dom_sf.
DR InterPro; IPR038256; Pol_alpha_znc_sf.
DR InterPro; IPR045846; POLBc_alpha.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR015088; Znf_DNA-dir_DNA_pol_B_alpha.
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; PF12254; DNA_pol_alpha_N; 1.
DR Pfam; PF00136; DNA_pol_B; 1.
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; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR SUPFAM; SSF90234; Zinc finger domain of DNA polymerase-alpha; 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:UP000242638};
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 44..105
FT /note="DNA polymerase alpha catalytic subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12254"
FT DOMAIN 435..731
FT /note="DNA-directed DNA polymerase family B exonuclease"
FT /evidence="ECO:0000259|Pfam:PF03104"
FT DOMAIN 797..1245
FT /note="DNA-directed DNA polymerase family B
FT multifunctional"
FT /evidence="ECO:0000259|Pfam:PF00136"
FT DOMAIN 1285..1471
FT /note="Zinc finger DNA-directed DNA polymerase family B
FT alpha"
FT /evidence="ECO:0000259|Pfam:PF08996"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 108..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 200..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 8..42
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..132
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..242
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1478 AA; 167111 MW; 4229676BDE18B9CB CRC64;
MAPVADPDKD MDVPDGDEKG DACSLAKSRS RREKREKVGR KSALEQLKKA KKGEKIKYEV
EEITSVYEEV DEQQYSKMVR ERQEDDWIID DDGTGYVEDG REIFDDDLDD DVVESKGKGG
AKGRETKKTL KKSSVAKPNT IKSLFMNSNV KRPAEKDVDL SKDDLLGDIL QDLHNEKPSA
LTPPPLVTLK KKKTVGSIMN PFSIKPQMPK QEKPSTYGLK AKVIRPPPLD PSPQPSTRSP
PPATTEVLPE KHEAELEEPN EEREDDSLAF EGVDFDEPME VEHEEEKAVA KDEAKLEPKG
GLTATEVKVE HKAERQDPVL LPNRVGSSWG QEAAGGVSEA PAEVQVDSSK LPLVEGMDGE
QVFRFYWLDA FEDPYNQPGV VYLFGKVWIE SAQSHVSCCV TVKNIDRTMY LLPREFKTNP
KTGEVSDQPV GMMDVYQEFN ELSEKFKIMK FKSKKVEKSY AFEIPDVPSQ CDYLEVRYSA
DFPALPSDLK GTTFSHVFGT NTSSLEHFLL SRKIKGPCWL DIKTPQLMNQ PVSWCKVEAL
AVRSDLVSVI KDLPPPPVTV MSISLKTVQN PKTHHNEIVS LVALIHYSFH MDKAPPQPPY
QTHFCVISKP SDCIFPYDFK DAVKKKKVKV EMATSERTLL GCFLAKMHKI DPDVLVGHDI
FGFDLEVLLQ RINVCKVPHW SKIGRLRRAN MPKLGGRGAF AEKSATCGRL VCDVEISAKE
LIRCKSYHLT ELAAQVLKVE RVAVPQESIR NLYSDSPHLL YLLELTWTDA KLILQIMCEL
NVLPLALQIT SIAGNVLSRT LMGGRSERNE FLLLHAFHDK NFIVPDKPSF KKAHLDTVEG
EDDADAGKGK RRKKAAYAGG LVLDPKVGFY DKFVLLLDFN SLYPSIIQEF NICFTTVQRQ
AQNSRKKTDD DEPEEIPEIP DSNLEMGILP REIRKLVERR KQVKQLMKQQ DINPDLYMQY
DIRQKALKLT ANSMYGCLGF SYSRFYAKPL AALVTHKGRE ILMHTKDMVQ RMNLEVIYGD
TDSIMINTNS KSLEEVFKLG HKIKAEVNKL YKLLEIDIDG VFKSLLLLKK KKYAALVVEQ
HGEGRYSVKQ ELKGLDIVRR DWCDLAKECG NYVIGQILSD QSRDVIVDNI QKHLVEVGEK
VANGDIPLNQ YEIHKALTKD PQDYPDKKSL PHVHVALWIN SQGGRRVKAG DTISYLICKD
GSTLAASQRA YALEQLQKQE GLSVDTQYYL AQQVHPVVSR ICDPIEGIDA VLIASWLGLD
PGQFRSQQQH QREEEADGTL GAAAQLNDEE RYKDCERFTF TCPQCGTDNI YDSVFEGAGD
KAEPSLMRCC HIPCTNSPIN NVVNISNKLQ LDIRRHIKKY YSGWLVCEDQ ACQNRTRRLP
IAFSRHGPIC PACTRATLRA EYSEKALYNQ LCFYSYIFDW DYAWAKLPNS NHKTSLKRTS
STRQAYLRLK EVPDKALATS GYSEVNLAKL FQAFSSFK
//
