UniProt: A0A093GZQ7

Database: UniProt
Entry: A0A093GZQ7_GAVST

LinkDB:  A0A093GZQ7_GAVST 
Original site:  A0A093GZQ7_GAVST

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Ontology (8)   
   GO (8)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (12)   
   InterPro (9)   
   Pfam (2)   
   SMART (1)   
All databases (22)   

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ID   A0A093GZQ7_GAVST        Unreviewed;      1442 AA.
AC   A0A093GZQ7;
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 epsilon catalytic subunit {ECO:0000256|RuleBase:RU365029};
DE            EC=2.7.7.7 {ECO:0000256|RuleBase:RU365029};
DE   Flags: Fragment;
GN   ORFNames=N328_11381 {ECO:0000313|EMBL:KFV47998.1};
OS   Gavia stellata (Red-throated diver) (Colymbus stellatus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Gaviiformes; Gaviidae; Gavia.
OX   NCBI_TaxID=37040 {ECO:0000313|EMBL:KFV47998.1, ECO:0000313|Proteomes:UP000054313};
RN   [1] {ECO:0000313|EMBL:KFV47998.1, ECO:0000313|Proteomes:UP000054313}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N328 {ECO:0000313|EMBL:KFV47998.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: DNA polymerase II participates in chromosomal DNA
CC       replication. {ECO:0000256|RuleBase:RU365029}.
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:RU365029};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|RuleBase:RU365029};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU365029}.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-B family.
CC       {ECO:0000256|ARBA:ARBA00005755, ECO:0000256|RuleBase:RU365029}.
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DR   EMBL; KK614700; KFV47998.1; -; Genomic_DNA.
DR   Proteomes; UP000054313; Unassembled WGS sequence.
DR   GO; GO:0008622; C:epsilon DNA polymerase complex; IEA:InterPro.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   GO; GO:0006281; P:DNA repair; IEA:InterPro.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   CDD; cd05779; DNA_polB_epsilon_exo; 1.
DR   CDD; cd05535; POLBc_epsilon; 1.
DR   Gene3D; 1.10.132.60; DNA polymerase family B, C-terminal domain; 1.
DR   Gene3D; 3.30.342.10; DNA Polymerase, chain B, domain 1; 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; 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; IPR029703; POL2.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   PANTHER; PTHR10670; DNA POLYMERASE EPSILON CATALYTIC SUBUNIT A; 1.
DR   PANTHER; PTHR10670:SF1; DNA POLYMERASE EPSILON CATALYTIC SUBUNIT A; 1.
DR   Pfam; PF00136; DNA_pol_B; 1.
DR   Pfam; PF03104; DNA_pol_B_exo1; 1.
DR   SMART; SM00486; POLBc; 1.
DR   SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR   SUPFAM; SSF53098; Ribonuclease H-like; 1.
PE   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|RuleBase:RU365029};
KW   DNA replication {ECO:0000256|RuleBase:RU365029};
KW   DNA-binding {ECO:0000256|RuleBase:RU365029};
KW   DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932,
KW   ECO:0000256|RuleBase:RU365029};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU365029};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU365029};
KW   Metal-binding {ECO:0000256|RuleBase:RU365029};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000256|RuleBase:RU365029}; Nucleus {ECO:0000256|RuleBase:RU365029};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054313};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU365029};
KW   Zinc {ECO:0000256|RuleBase:RU365029};
KW   Zinc-finger {ECO:0000256|RuleBase:RU365029}.
FT   DOMAIN          46..352
FT                   /note="DNA-directed DNA polymerase family B exonuclease"
FT                   /evidence="ECO:0000259|Pfam:PF03104"
FT   DOMAIN          722..1069
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:KFV47998.1"
FT   NON_TER         1442
FT                   /evidence="ECO:0000313|EMBL:KFV47998.1"
SQ   SEQUENCE   1442 AA;  165198 MW;  0775B47C6E143BD4 CRC64;
     DRRSVSAVDY YFIQEDGSRF KVALPYKPYF YIATQKGCER EVSSFLSKKF QGKIAKLETV
     PKEDLDLPNH LVGLKRNYIK LSFNTVDDLV KVRKEISPAV RKNRERDQAS DVYTAMLSSA
     LSGGSLSTDE EGASRKVSNQ MDNIVDMREY DVPYHVRLSI DLKIHVAHWY NVRYRGSTYP
     PEITRRDDLV ERPDPVVLAF DIETTKLPLK FPDAETDQIM MISYMIDGQG YLITNREIVS
     EDIEDFEFTP KPEYEGPFCI FNEPDEAHLI QRWFEHVQET KPTIIVTYNG DFFDWPFVEA
     RAAAHGISMY QEIGFQKDSQ GEYKASQCIH MDCLRWVKRD SYLPVGSHNL KAAAKAKLGY
     DPVELDPEEM CRMATEEPQT LATYSVSDAV ATYYMYMKYV HPFIFALCTI IPMEPDEVLR
     KGSGTLCEAL LMVQAYHANI IFPNKQEQEF NKLTEDGHVL DSETYVGGHV EALESGVFRS
     DIPCRFKMNP AAFDFLVQHV EKTLQHAIEE EEGLPLDQVT NFQEVCDEIK VKLNSLKDVP
     NRIECPLIYH LDVGAMYPNI ILTNRLQPSA MVDEATCAAC DFNKPGANCQ RRMTWQWRGE
     FMPASRSEYH RIQQQLESEK FPPLSPEGAP RAFHELSREE QAKYEKKRLA DYCRKAYKKI
     HVTKVEERVT TICQRENSFY VDTVRAFRDR RYEFKGLHKV WKKKLSAAVE TGDASEVKRC
     KNMEILYDSL QLAHKCILNS FYGYVMRKGA RWYSMEMAGI VCFTGANIIT QARELIEQIG
     RPLELDTDGI WCVLPNSFPE NFVIKSTNAK KPKVTISYPG AMLNILVKEG FTNDQYQELQ
     DPASLTYVTR SENSIFFEVD GPYLAMILPA SKEEGKKLKK RYAVFNEDGS LAELKGFEVK
     RRGELQLVKI FQSSVFEAFL KGSTLEEVYA SVAKVADYWL DVLYSKAANM PDSELFELIS
     ENRSMSRKLE DYGEQKSTSI STAKRLAEFL GDQMVKDAGL SCRFIISKKP EGSPVTERAI
     PLAIFQAEPS VRKHYLRKWL KSPSLQDFNI RAILDWDYYI ERLGSTIQKI ITIPAALQQV
     KNPVPRVRHP DWLHKKLLEK NDVYKQKKIN ELFTSEGKRQ VLANQPPVGT PSSQIGDIED
     FGAAKTVQPP VPITNKRKRV PAAEESQQMS QYLELSQSWR EILGPPPPLG TTKERAVGLL
     KPSACPWLRA TRRNTTRRWR NITTDREKQG GGGFTAGAGT YLRRTARSIL DLPWQIVQIA
     ETSQPGLFRL WAVIGSDLHC IKLSIPRVFY VNQRVPKPEE GAAYRRVNRI LPRSNLVYNL
     YEYSVPEDMY QEHINEINAD LSAPDIEGVY ETQVPLLLRA LIHLGCVCMV SRQLVKHLAG
     REAETFDIEH LEMRSLAQFT YLEPVSIRHI YLYHSSQGSK ALLGLFIPSQ RKAAVFVLDK
     VR
//

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