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Database: UniProt
Entry: A0A0V0X471_9BILA
LinkDB: A0A0V0X471_9BILA
Original site: A0A0V0X471_9BILA 
ID   A0A0V0X471_9BILA        Unreviewed;      1093 AA.
AC   A0A0V0X471;
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=T06_16530 {ECO:0000313|EMBL:KRX82796.1};
OS   Trichinella sp. T6.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=92179 {ECO:0000313|EMBL:KRX82796.1, ECO:0000313|Proteomes:UP000054673};
RN   [1] {ECO:0000313|EMBL:KRX82796.1, ECO:0000313|Proteomes:UP000054673}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS34 {ECO:0000313|EMBL:KRX82796.1};
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:KRX82796.1}.
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DR   EMBL; JYDK01000018; KRX82796.1; -; Genomic_DNA.
DR   Proteomes; UP000054673; 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; 3.30.420.10; -; 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; IPR036397; RNaseH_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:UP000054673};
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:UP000054673};
KW   Transferase {ECO:0000256|RuleBase:RU000442};
KW   Zinc {ECO:0000256|RuleBase:RU000442};
KW   Zinc-finger {ECO:0000256|RuleBase:RU000442}.
FT   DOMAIN      115    460       DNA_pol_B_exo1. {ECO:0000259|Pfam:
FT                                PF03104}.
FT   DOMAIN      525    963       DNA_pol_B. {ECO:0000259|Pfam:PF00136}.
FT   DOMAIN     1001   1071       zf-C4pol. {ECO:0000259|Pfam:PF14260}.
FT   REGION        1     28       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A0V0X471}.
FT   COMPBIAS      1     17       Polar. {ECO:0000256|MobiDB-lite:
FT                                A0A0V0X471}.
SQ   SEQUENCE   1093 AA;  125055 MW;  169E554A73E25B13 CRC64;
     MASKRRNSGL SSSQSQFTKR RRELDEEEDR TDFELHLATF DEPDLIENGV DSQIFGSGPE
     QFETSARWAR PRLLSDIAER SVIFQCMDID YYHSDMQNGL KTDQVHAVIR MYGATKDGHS
     VCCHVHGFQP YFYVQIENFD PARASLFCDS LNQAVVQEMR TNKDIKKPIL DVEILQGRNL
     YGYNLMKSTT FVKIIVALPK IVPVARRILE 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
     NWKRIQRFDM DDF
//
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