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Database: UniProt
Entry: A0A3Q3FSQ8_9LABR
LinkDB: A0A3Q3FSQ8_9LABR
Original site: A0A3Q3FSQ8_9LABR 
ID   A0A3Q3FSQ8_9LABR        Unreviewed;      1390 AA.
AC   A0A3Q3FSQ8;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE            EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
OS   Labrus bergylta (ballan wrasse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Labriformes; Labridae; Labrus.
OX   NCBI_TaxID=56723 {ECO:0000313|Ensembl:ENSLBEP00000022504.1, ECO:0000313|Proteomes:UP000261660};
RN   [1] {ECO:0000313|Ensembl:ENSLBEP00000022504.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-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   Ensembl; ENSLBET00000023685.1; ENSLBEP00000022504.1; ENSLBEG00000017168.1.
DR   GeneTree; ENSGT00550000074891; -.
DR   Proteomes; UP000261660; Unplaced.
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:UP000261660};
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          33..94
FT                   /note="DNA polymerase alpha catalytic subunit N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12254"
FT   DOMAIN          396..692
FT                   /note="DNA-directed DNA polymerase family B exonuclease"
FT                   /evidence="ECO:0000259|Pfam:PF03104"
FT   DOMAIN          757..1205
FT                   /note="DNA-directed DNA polymerase family B
FT                   multifunctional"
FT                   /evidence="ECO:0000259|Pfam:PF00136"
FT   DOMAIN          1245..1363
FT                   /note="Zinc finger DNA-directed DNA polymerase family B
FT                   alpha"
FT                   /evidence="ECO:0000259|Pfam:PF08996"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          96..124
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        96..122
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1390 AA;  157326 MW;  369C02A41144E41E CRC64;
     MSSRHDDGGD ACGLAKSRSR REKREKVGRK SALEQLKKAK MGEKIKYEVE EFTSVYEEVD
     EQQYSKMVRE RQEDDWIIDD DGTGYVEDGR EIFDDDLHDD VVENKKGKPG AKGADSKKNV
     KKSAVAKPNT IKSLFNNSNV KRPVEKDVDL SKDDLLGDIL QDLHSEKPSL LTPPPVVTLK
     KKKSLGTPLN PFSIKPQTPK VFLKSVKEKN QDTNVTFLFC FLSSSKLTIM TTRFSVNDAM
     AFDGVDFDEP MEVGLEEQKP EIKDAAESDP KAAAAVVAVK TESGRISTWG QEEEEGVASD
     APAEVQVDSS RLPLAEGPDG EQVFRFYWLD AFEEPYSQPG VVYLFGKVWI ESAKSHVSCC
     VSVKNIERTM YFLPREYKVN TKTGEVSGTP VGMMDVYQEF NELSEKFKIM KFKSKKVERS
     YAFEIPDVPS QCEYLEVRYS AEFPALPSDL KGATFSHIFG NNTSSLEHFL LSRKIKGPCW
     LDIKTPQLIS QPVSWCKVEA LALRSDLVTV VKDLPPPPIT VMSISLKTIQ NPKTHHNEIV
     SLAALIHYNF HMDKAAPQPP YQTHFCVVSR PADCIFPYDF KEAVRKKNGK VEIASTERTL
     LGFFLAKMHK IDPDVLVGHD IFGFDLEVIL QRINFCKVPH WSKMGRLRRA TMPKLGGRGS
     FAEKSATCGR LVCDVEISAK ELIRCKSYHL TELTAQVLKT ERVALPQENI KNLYSDSPHL
     LYLLEMTWTD AKLILQIMCE LNVLPLALQI TNIAGNVMSR TLMGGRSERN EFLLLHAFHD
     KNFIVPDKPS FKKAQLEVDG EDDADTGKGK RRKKAAYAGG LVLDPKVGFY DKFVLLLDFN
     SLYPSIIQEF NICFTTVQRE AYNAQKKNQE DESEEIPEIP DSDLEMGILP KEIRKLVERR
     KQVKQLMKQQ DINPDLYLQY DIRQKALKLT ANSMYGCLGF SYSRFYAKPL AALVTHKGRE
     ILMHTKDLVQ KMNLEVIYGD TDSIMINTNS RSLEEVFKLG NKVKAEVNKL YKLLEIDIDG
     VFKSLLLLKK KKYAALVVEN HGEGRYSVKQ ELKGLDIVRR DWCDLAKECG NYVIGQILSD
     QSRDAIVENI QKHLVEVGEK VAAGAIPLNQ YEIHKALTKD PQDYPDKKSL PHVHVALWIN
     SQGGHRVKAG DTVSYIICKD GSTLAASQRA YALEQLQKQE NLSLDTQYYL AQQVHPVVSR
     ICDPIDGIDG VLIATWLGLD PSQFRAHQQY QREDEADGTL GAPVQLTDEE RYKDCERFTF
     TCPQCGTDNT YDSVFEGAGS KMEPSLLQCC HIPCGSRPVD YVVNISNKLL LDIRRHIKKY
     YSGWLVCEDQ ACQNRIRRLP IAFSRHGPIC PACTRATLRP EVTRTIHTLT HTHTHHHTSF
     HTLEWEEQNA
//
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