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Database: UniProt
Entry: A0A0V1CEY0_TRIBR
LinkDB: A0A0V1CEY0_TRIBR
Original site: A0A0V1CEY0_TRIBR 
ID   A0A0V1CEY0_TRIBR        Unreviewed;      1110 AA.
AC   A0A0V1CEY0;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   05-JUN-2019, entry version 16.
DE   RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE            EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN   ORFNames=T03_16083 {ECO:0000313|EMBL:KRY47883.1};
OS   Trichinella britovi (Parasitic roundworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=45882 {ECO:0000313|EMBL:KRY47883.1, ECO:0000313|Proteomes:UP000054653};
RN   [1] {ECO:0000313|EMBL:KRY47883.1, ECO:0000313|Proteomes:UP000054653}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS120 {ECO:0000313|EMBL:KRY47883.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-2015) 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-
CC         COMP:11130, Rhea:RHEA-COMP:11131, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:61560, ChEBI:CHEBI:83828; EC=2.7.7.7;
CC         Evidence={ECO:0000256|RuleBase:RU000442};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|RuleBase:RU000442};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|RuleBase:RU000442}.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-B family.
CC       {ECO:0000256|RuleBase:RU000442}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KRY47883.1}.
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DR   EMBL; JYDI01000226; KRY47883.1; -; Genomic_DNA.
DR   Proteomes; UP000054653; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.132.60; -; 1.
DR   Gene3D; 3.90.1600.10; -; 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; IPR042087; DNA_pol_B_C.
DR   InterPro; IPR023211; DNA_pol_palm_dom_sf.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR025687; Znf-C4pol.
DR   Pfam; PF00136; DNA_pol_B; 1.
DR   Pfam; PF03104; DNA_pol_B_exo1; 1.
DR   Pfam; PF14260; zf-C4pol; 1.
DR   PRINTS; PR00106; DNAPOLB.
DR   SMART; SM00486; POLBc; 1.
DR   SUPFAM; SSF53098; SSF53098; 1.
DR   PROSITE; PS00116; DNA_POLYMERASE_B; 1.
PE   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|RuleBase:RU000442};
KW   Complete proteome {ECO:0000313|Proteomes:UP000054653};
KW   DNA replication {ECO:0000256|RuleBase:RU000442};
KW   DNA-binding {ECO:0000256|RuleBase:RU000442};
KW   DNA-directed DNA polymerase {ECO:0000256|RuleBase:RU000442};
KW   Iron {ECO:0000256|RuleBase:RU000442};
KW   Iron-sulfur {ECO:0000256|RuleBase:RU000442};
KW   Metal-binding {ECO:0000256|RuleBase:RU000442};
KW   Nucleotidyltransferase {ECO:0000256|RuleBase:RU000442};
KW   Nucleus {ECO:0000256|RuleBase:RU000442};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054653};
KW   Transferase {ECO:0000256|RuleBase:RU000442};
KW   Zinc {ECO:0000256|RuleBase:RU000442};
KW   Zinc-finger {ECO:0000256|RuleBase:RU000442}.
FT   DOMAIN      115    486       DNA_pol_B_exo1. {ECO:0000259|Pfam:
FT                                PF03104}.
FT   DOMAIN      551    980       DNA_pol_B. {ECO:0000259|Pfam:PF00136}.
FT   DOMAIN     1018   1088       zf-C4pol. {ECO:0000259|Pfam:PF14260}.
FT   REGION        1     28       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A0V1CEY0}.
FT   COMPBIAS      1     17       Polar. {ECO:0000256|MobiDB-lite:
FT                                A0A0V1CEY0}.
SQ   SEQUENCE   1110 AA;  127263 MW;  437225D5D9F840EE CRC64;
     MASKRRNSGL SSSQSQFTKR RRELDEEEDR TDFELHLATF DEPDLIENGV DSQIFGSGPE
     QFETSARWAR PRLLSDIAER SVIFQCMDID YYHSDMQNGL KTDQVHAVIR MYGATKDGHS
     VCCHVHGFQP YFYVQIENFD PARASLFCDS LNQAVVQEMR TNKDIKKPIL DVEILQGRNL
     YGYNLMKSTT FVKIIVALPK IVPVGNKIII KFVNFYIFLI LKCEKTCWFL ARRILETGGW
     SCASQPINAL LTFESNIDFT IRFMIDTSMT GCCWIELKPS AFTVRNLKKM SRCQIEVDID
     WKKLVIHSPE GDWSDIAPLR ILSIDIECAG RKGVFPEAEK DPVIQIANMV LTQGEKEPFV
     RNVFTLNSCA PIVGCQVISC DTEEKMLSEW ASFVREVDPD IITGYNIQNF DLPYLIDRAQ
     TLSVKDFAFI GRIKDQKTVV HSSNVQSRQM GRRENKLCNI EGRIQFDLLQ ILFRDYKLRS
     YTLNAVSFHF LQEQKEDVHY SIITDLQNGN EQTRRRLAVY CLKDAYLPLR LLDKLMSVIN
     YIEMSRVTGV TVSNLLTRGQ QIKVISQLMR RTREQNLFLP AVRSEVGEDY TGATVIEPIK
     GYYNKPIVTL DFASLYPSIM MAHNLCYTTL IMQETVRSQL SPEDYIKTPS GHYFVKKDKC
     KGLLPEILEN LLAARKAVKQ QMKVETDAFR RQVLDGRQLA LKISANSVYG FTGAQVGKLP
     CLEISQSVTA FGRMMIDKTK EEVEKQFVKA NGYSADAKVI YGDTDSVMVD FGLDTLEKAM
     EMGREAAAFV SAKFVNPIKL EFEKVYFPYL LISKKRYAGL YFTNTQSYDK MDCKGIETVR
     RDNCPLVANV LNTCLEKILI DRDPNKAVEY TKMVISDLLC NRIDISQLII SKELTKTDKE
     YAAKQAHVEL AARMRKRDPG SAPHLGDRVP YVIIAASKGT AAYMKAEDPI YVLENSIPID
     TQYYLENQLS KPLLRIFDPI LGDKAESILL RGDHTRTKTV THSKLGGLMA FTKKQETCLN
     CRAVLSNNGA ICDHCKPKEV EIYQRELFQV QYLEERFSRL WTECQRCQGS LHEEVLCSSR
     DCPIFYMRTK VKKDLQDNWK RMQRFDMDDF
//
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