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Database: UniProt
Entry: A0A0V1PL72_9BILA
LinkDB: A0A0V1PL72_9BILA
Original site: A0A0V1PL72_9BILA 
ID   A0A0V1PL72_9BILA        Unreviewed;      1113 AA.
AC   A0A0V1PL72;
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=T08_48 {ECO:0000313|EMBL:KRZ96933.1};
OS   Trichinella sp. T8.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=92180 {ECO:0000313|EMBL:KRZ96933.1, ECO:0000313|Proteomes:UP000054924};
RN   [1] {ECO:0000313|EMBL:KRZ96933.1, ECO:0000313|Proteomes:UP000054924}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS272 {ECO:0000313|EMBL:KRZ96933.1};
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:KRZ96933.1}.
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DR   EMBL; JYDM01000005; KRZ96933.1; -; Genomic_DNA.
DR   Proteomes; UP000054924; 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:UP000054924};
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:UP000054924};
KW   Transferase {ECO:0000256|RuleBase:RU000442};
KW   Zinc {ECO:0000256|RuleBase:RU000442};
KW   Zinc-finger {ECO:0000256|RuleBase:RU000442}.
FT   DOMAIN      115    480       DNA_pol_B_exo1. {ECO:0000259|Pfam:
FT                                PF03104}.
FT   DOMAIN      545    983       DNA_pol_B. {ECO:0000259|Pfam:PF00136}.
FT   DOMAIN     1021   1091       zf-C4pol. {ECO:0000259|Pfam:PF14260}.
FT   REGION        1     28       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A0V1PL72}.
FT   COMPBIAS      1     17       Polar. {ECO:0000256|MobiDB-lite:
FT                                A0A0V1PL72}.
SQ   SEQUENCE   1113 AA;  127625 MW;  9D724006288DCE44 CRC64;
     MASKRRNSGL SSSQSQFTKR RRELDEEEDR TDFELHLATF DEPDLIENGV DSQIFGSGPE
     QFETSARWAR PRLLSDIAER SVIFQCMDID YYHSDMQNGL KTDQVHAVIR MYGATKDGHS
     VCCHVHGFQP YFYVQIENFD PARASLFCDS LNQAVVQEMR TNKDIKKPIL DVEILQGRNL
     YGYNLMKSTT FVKIIVALPK IVPIKFVNFY IFLILKCEKT CWFLARRILE TGGWSCASQP
     INALLTFESN IDFTIRFMID TSMTGCCWIE LKPSAFTVRN LKKMSRCQIE VDIDWKKLVI
     HSPEGDWSDI APLRILSIDI ECAGRKGVFP EAEKDPVIQI ANMVLTQGEK EPFVRNVFTL
     NSCAPIVGCQ VISCDTEEKM LSEWASFVRE VDPDIITGYN IQNFDLPYLI DRAQTLSVKD
     FAFIGRIKDQ KTVVHSSNVQ SRQMGRRENK LCNIEGRIQF DLLQILFRDY KLRSYTLNAV
     SFHFLQEQKE DVHYSIITDL QNGNEQTRRR LAVYCLKDAY LPLRLLDKLM SVINYIEMSR
     VTGVTVSNLL TRGQQIKVIS QLMRRTREQN LFLPAVRSEV GEDYTGATVI EPIKGYYNKP
     IVTLDFASLY PSIMMAHNLC YTTLIMQETV RSQLSPEDYI KTPSGHYFVK KDKCKGLLPE
     ILENLLAARK AVKQQMKVET DAFRRQVLDG RQLALKISAN SVYGFTGAQV GKLPCLEISQ
     SVTAFGRMMI DKTKEEVEKQ FVKANGYSAD AKVIYGDTDS VMVDFGLDTL EKAMEMGREA
     AAFVSAKFVN PIKLEFEKVY FPYLLISKKR YAGLYFTNTQ SYDKMDCKGI ETVRRDNCPL
     VANVLNTCLE KILIDRDPNK AVEYTKMVIS DLLCNRIDIS QLIISKELTK TDKEYAAKQA
     HVELAARMRK RDPGSAPHLG DRVPYVIIAA SKGTAAYMKA EVSSIFHTSK DPIYVLENSI
     PIDTQYYLEN QLSKPLLRIF DPILGDKAES ILLRGDHTRT KTVTHSKLGG LMAFTKKQET
     CLNCRAVLSN NGAICDHCKP KEVEIYQREL FQVQYLEERF SRLWTECQRC QGSLHEEVLC
     SSRDCPIFYM RTKVKKDLQD NWKRMQRFDM DDF
//
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