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Database: UniProt
Entry: A0A3Q2HAH2_HORSE
LinkDB: A0A3Q2HAH2_HORSE
Original site: A0A3Q2HAH2_HORSE 
ID   A0A3Q2HAH2_HORSE        Unreviewed;      1418 AA.
AC   A0A3Q2HAH2;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2023, sequence version 2.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE            EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN   Name=POLA1 {ECO:0000313|Ensembl:ENSECAP00000030292.2,
GN   ECO:0000313|VGNC:VGNC:21649};
OS   Equus caballus (Horse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX   NCBI_TaxID=9796 {ECO:0000313|Ensembl:ENSECAP00000030292.2, ECO:0000313|Proteomes:UP000002281};
RN   [1] {ECO:0000313|Ensembl:ENSECAP00000030292.2, ECO:0000313|Proteomes:UP000002281}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000030292.2,
RC   ECO:0000313|Proteomes:UP000002281};
RX   PubMed=19892987; DOI=10.1126/science.1178158;
RG   Broad Institute Genome Sequencing Platform;
RG   Broad Institute Whole Genome Assembly Team;
RA   Wade C.M., Giulotto E., Sigurdsson S., Zoli M., Gnerre S., Imsland F.,
RA   Lear T.L., Adelson D.L., Bailey E., Bellone R.R., Bloecker H., Distl O.,
RA   Edgar R.C., Garber M., Leeb T., Mauceli E., MacLeod J.N., Penedo M.C.T.,
RA   Raison J.M., Sharpe T., Vogel J., Andersson L., Antczak D.F., Biagi T.,
RA   Binns M.M., Chowdhary B.P., Coleman S.J., Della Valle G., Fryc S.,
RA   Guerin G., Hasegawa T., Hill E.W., Jurka J., Kiialainen A., Lindgren G.,
RA   Liu J., Magnani E., Mickelson J.R., Murray J., Nergadze S.G., Onofrio R.,
RA   Pedroni S., Piras M.F., Raudsepp T., Rocchi M., Roeed K.H., Ryder O.A.,
RA   Searle S., Skow L., Swinburne J.E., Syvaenen A.C., Tozaki T., Valberg S.J.,
RA   Vaudin M., White J.R., Zody M.C., Lander E.S., Lindblad-Toh K.;
RT   "Genome sequence, comparative analysis, and population genetics of the
RT   domestic horse.";
RL   Science 326:865-867(2009).
RN   [2] {ECO:0000313|Ensembl:ENSECAP00000030292.2}
RP   IDENTIFICATION.
RC   STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000030292.2};
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; ENSECAT00000056088.2; ENSECAP00000030292.2; ENSECAG00000013090.3.
DR   VGNC; VGNC:21649; POLA1.
DR   GeneTree; ENSGT00550000074891; -.
DR   Proteomes; UP000002281; Chromosome X.
DR   Bgee; ENSECAG00000013090; Expressed in inner cell mass and 23 other cell types or tissues.
DR   ExpressionAtlas; A0A3Q2HAH2; baseline.
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; 2.
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; 2.
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; 2.
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:UP000002281};
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          41..102
FT                   /note="DNA polymerase alpha catalytic subunit N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12254"
FT   DOMAIN          407..707
FT                   /note="DNA-directed DNA polymerase family B exonuclease"
FT                   /evidence="ECO:0000259|Pfam:PF03104"
FT   DOMAIN          772..930
FT                   /note="DNA-directed DNA polymerase family B
FT                   multifunctional"
FT                   /evidence="ECO:0000259|Pfam:PF00136"
FT   DOMAIN          942..1183
FT                   /note="DNA-directed DNA polymerase family B
FT                   multifunctional"
FT                   /evidence="ECO:0000259|Pfam:PF00136"
FT   DOMAIN          1222..1411
FT                   /note="Zinc finger DNA-directed DNA polymerase family B
FT                   alpha"
FT                   /evidence="ECO:0000259|Pfam:PF08996"
FT   REGION          20..39
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          105..131
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          197..224
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        110..131
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1418 AA;  161420 MW;  0462A91683E0529B CRC64;
     MAPVHGEDCE LAASAVSDSG SFVASRSRRE KKSKKGRQEA LERLKKAKAG EKYKYEVEDL
     TSVYEEVDEE QYSKLVQARQ DDDWIVDDDG IGYVEDGREI FDDDLEDDAL DSHEKGKDDK
     ARNKDKRNVK KAVVTRPNSI KSMFMASAGR KTADKAVDLS KDDLLGDILQ DLNSEPPQIT
     PPPVMILKKK RSTGASLNPF SVHTPKAVPS GKTASAVSRK EPSLTPVALK RAEFADEKEE
     SGAMDFEDGD FDEPMDAVEV DMETVAAKTW DQEREPAEGV KHEADPGKGT TSYLESFLPD
     VSCWDIDQED DSSFSAQEVQ VDSNHLPLVK GADEEQVFQF YWLDAYEDQY NQPGVVFLFG
     KVWIELAETY VSCCVMVKNI ERTLYFLPCE TKIDLNTGKE TGTPVRMKDV YDEFDEKIAT
     KYKIMKFKSK IVEKNYAFEI PDVPEKSEYL EVRYSAELPQ LPQDLKGETF SHVFGTNTSS
     LELFLMNRKI KGPCWLEVKN PQLLNQPISW CKVEAMVSKP DLVNVIKDVS PPPLVVMSFS
     MKTMQSAKTH QNEIIAMAAL VHHSFALDKA PPQPPFQSHF CVVSKPKDCI FPHSFLEDIK
     EKNVKVEVAA TERTLLGFFL AKVHKIDPDV IVGHNIYGFE LEVLLQRINV CKVPHWSKIG
     RLKRSNMPKL GGRSGFGERN ATCGRMICDV EISAKELIRC KSYHLSELVQ QILKTERIVI
     PMENVQNMYS ESSHLLYLLE HTWKDARFIL QIMCELNVLP LALQITNIAG NIMSRTLMGG
     RSERNEFLLL HAFYENNYIV PDKQIFRKPQ QKLGDEDEDI DGDTNKYKKG RKKAAYAGGL
     VLDPKVGFYD KFILLLDFNS LYPSIIQEFN ICFTTVQRVA SEAQRVTEDG EQEQIPELPD
     PSLEMGILPR EIRKLVERRK QVKQLMKQQD LNPDLVLQIL MHTKEMVQKM NLEVIYGDTD
     SIMINTNSTN LEEVFKLGNK VKSEVNRLYK LLEIDIDGVF KSLLLLKKKK YAALVVEPTS
     DGNYFTKQEL KGLDIVRRDW CDLAKDTGNF VIGQILSDQS RDTIVENIQK RLIEIGENVL
     NGSVPVSQFE INKALTKDPQ DYPDKKSLPH VHVALWINSQ GGRKVKAGDT VSYVICQDGS
     NLTASQRAYA PEQLQKQDNL TIDTQYYLAQ QIHPVVARIC EPIDGIDAVL IATWLGLDPT
     QFRVHHYHKD EENDALLGGP AQLTDEEKYR DCERFKCPCP TCGTENIYDS VFDGSGKDME
     PSLYRCSNID CKASPLTFMV QLSNKLIMDI RRCIKKYYEG WLICEEPTCR NRTRHLPLQF
     SRNGPLCQVC MKAVLRPEYS DKSLYTQLCF YRYIFDVDCA LEKLITDHEK EKLKTQYLTP
     RVREDYKKLK STAEQFLSRS GYSEVNLSKL FADCAVKS
//
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