UniProt: A0A091HS64

Database: UniProt
Entry: A0A091HS64_CALAN

LinkDB:  A0A091HS64_CALAN 
Original site:  A0A091HS64_CALAN

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Ontology (5)   
   GO (5)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (19)   
   InterPro (13)   
   Pfam (4)   
   PROSITE (1)   
   SMART (1)   
All databases (26)   

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ID   A0A091HS64_CALAN        Unreviewed;      1461 AA.
AC   A0A091HS64;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE            EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
DE   Flags: Fragment;
GN   ORFNames=N300_06072 {ECO:0000313|EMBL:KFO98004.1};
OS   Calypte anna (Anna's hummingbird) (Archilochus anna).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Caprimulgimorphae; Apodiformes;
OC   Trochilidae; Calypte.
OX   NCBI_TaxID=9244 {ECO:0000313|EMBL:KFO98004.1, ECO:0000313|Proteomes:UP000054308};
RN   [1] {ECO:0000313|EMBL:KFO98004.1, ECO:0000313|Proteomes:UP000054308}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N300 {ECO:0000313|EMBL:KFO98004.1};
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   -!- 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   EMBL; KL217721; KFO98004.1; -; Genomic_DNA.
DR   STRING; 9244.A0A091HS64; -.
DR   Proteomes; UP000054308; 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; 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:UP000054308};
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..58
FT                   /note="DNA polymerase alpha catalytic subunit N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12254"
FT   DOMAIN          405..700
FT                   /note="DNA-directed DNA polymerase family B exonuclease"
FT                   /evidence="ECO:0000259|Pfam:PF03104"
FT   DOMAIN          765..1216
FT                   /note="DNA-directed DNA polymerase family B
FT                   multifunctional"
FT                   /evidence="ECO:0000259|Pfam:PF00136"
FT   DOMAIN          1256..1445
FT                   /note="Zinc finger DNA-directed DNA polymerase family B
FT                   alpha"
FT                   /evidence="ECO:0000259|Pfam:PF08996"
FT   REGION          60..88
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          181..206
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFO98004.1"
FT   NON_TER         1461
FT                   /evidence="ECO:0000313|EMBL:KFO98004.1"
SQ   SEQUENCE   1461 AA;  166480 MW;  9244A19AC3A0DDE2 CRC64;
     KKAKAGEKIK YEVEEFTSVY DEIDEEEYSK MVRERQDDDW IVDDDGIGYV EDGREIFDED
     LDDDALGSNK KGKVGKTSSA GKKNIKKSVV SKPNTIKSMF IANAGRKNTD KTVDLSKDDL
     LGDILQDLNA ETVQISPPPV IMLKRKRSAG VPLNPFSVQS QTPKVITPVS KKAPAHLRKE
     ALPPASLHPK HPNYSAKSVK GSESEDTKYV QKATENGGLV KTIEEKAIED DDQGMMDFDE
     EDFDEPMEAE HVQTVPEVAE SLKRDKEMEK KETEQLESGK KETSVLCCSL PDVSCWDRID
     EDEADSVVAE VQLDPDLLPL VNGENDDQVF RFYWLDAYED QYSQPGVVFL FGKVWIESAD
     TYVSCCVTVK NIERTVYLLP RETELDLSTG KETETPVTIM SVFKEFNDCI SPKYKIMKFK
     SKKVEKYYAF EIPDVPAKSE YLEVKYSAEY PRLPQDLKGQ TFSHVFGTNT SSLELLLMSR
     KIKGPCWLEI KNPQPSNPSV SWCKVEAVAM KPGLVNVVKD LSPPPPLVVM SLSLKTTQNP
     KTHQNEIVSV AALIHQKFPL DKAPPQPPFQ THFCVVSKPS DCIFPYDFKE AIKKKNAKIE
     IAATERTLLG FFLAKIHKID PDVVVGHNIY GFDLEVLLQR INVCKVPHWS KIGRLRRSNM
     PKLGGRGGFA ERNAACGRMI CDVEISAKEL IRCKSYHLSE LVHQLLKTQK VTILPEEIPN
     MYSDSPHLIY MLENTWTDAK FILQIMCELN VLPLALQITN ISGNVMSRTM MGGRSERNEF
     LLLHAFHEKD YIVPDKQVFK KPLQKLVDDD EDFEEQNKSK IGRKKAAYAG GLVLDPKVGF
     YDKFILLLDF NSLYPSIIQE FNICFTTVQR LSSEAQKRAE GEEEEEIPEL PDPSLEMGVL
     PKEIRKLVER RRQVKQLMKQ PDLNPDLYLQ YDIRQKALKL TANSMYGCLG FSFSRFYAKP
     LAALVTHKGR EILMHTKEMV QKMNLEVIYG DTDSIMINTN STNLDEVFKL GNKIKNEVNK
     LYKLLEIDID GVFKSLLLLK KKKYAALTVE PTGDGKYITK QELKGLDIVR RDWCDLAKET
     GNYVIGQILS DQPRDIIVEN IQRRLIEIGE NVVSGQIPVN QFEINKALTK EPQDYPDKKN
     LPHVHVAMWI NSQGGRKVKA GDTVSYIICQ DGSDLSAGQR AYAPEQLQKQ DNLTVDTQYY
     LSQQIHPVVA RICEPIEGID SVLIATWLGL DPSQFRVHHH YHKDEENDAL VGGPAQLTDE
     EKYRDCERFK FCCLKCGTEN IYDNVFDGSG RSIEPSLQRC SKTDCEEPPF NHVVQMCNKL
     LLDIRRHIRK YYNGWLICEE PTCRNRTRRL PLSFSRSGPI CQACRKAILW PEYSDKALYT
     QLCFYRYIFD VDYAKDKVIT EEEREHLKKK PHREEVSEAY KRLKSTVDNC LSMSAYSEVN
     LGKLFTVSMG RSVGESSNER Q
//

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