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Database: UniProt
Entry: A0A0V0SNX8_9BILA
LinkDB: A0A0V0SNX8_9BILA
Original site: A0A0V0SNX8_9BILA 
ID   A0A0V0SNX8_9BILA        Unreviewed;      1131 AA.
AC   A0A0V0SNX8;
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=T07_10447 {ECO:0000313|EMBL:KRX28051.1};
OS   Trichinella nelsoni.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=6336 {ECO:0000313|EMBL:KRX28051.1, ECO:0000313|Proteomes:UP000054630};
RN   [1] {ECO:0000313|EMBL:KRX28051.1, ECO:0000313|Proteomes:UP000054630}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS37 {ECO:0000313|EMBL:KRX28051.1};
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:KRX28051.1}.
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DR   EMBL; JYDL01000001; KRX28051.1; -; Genomic_DNA.
DR   Proteomes; UP000054630; 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:UP000054630};
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:UP000054630};
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      584   1001       DNA_pol_B. {ECO:0000259|Pfam:PF00136}.
FT   DOMAIN     1039   1109       zf-C4pol. {ECO:0000259|Pfam:PF14260}.
FT   REGION        1     28       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A0V0SNX8}.
FT   COMPBIAS      1     17       Polar. {ECO:0000256|MobiDB-lite:
FT                                A0A0V0SNX8}.
SQ   SEQUENCE   1131 AA;  129726 MW;  E2D1116924EB56ED CRC64;
     MASKRRNSGL SSSQSQFTKR RRELDEEEDR TDFELHLAAF DEPDLIENGV DSQIFGSGPE
     QFETSARWAR PRLLLDIAER SVIFQCMDID YYHSDMQNGL KTDQVHAVIR MYGATKDGHS
     VCCHVHGFQP YFYVQIENFD PARASLFCDS LNQAVVQEMR TNKDIKKPIL DVEILQGRNL
     YGYNLMKSTT FVKIIVALPK IVPVGNKIII KFVNFYIFLI LKCERTRWFL 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 LLDKLMSSDG
     CHCEQFAYSW STDQSYFTID AQGSQVEISI EKRNDIQNLN VFQTREQNLF LPAVRSEVGE
     DYTGATVIEP IKGYYNKPIV TLDFASLYPS IMMAHNLCYT TLIMQETVRS QLSPEDYIKT
     PSGHYFVKKD KCKGLLPEIL ENLLAARKAV KQQMKVETDA FRRQVLDGRQ LALKISANSV
     YGFTGAQVGK LPCLEISQSV TAFGRMMIDK TKEEVEKQFV KANGYSADAK VIYGDTDSVM
     VDFGLDTLEK AMEMGREAAA FVSAKFVNPI KLEFEKVYFP YLLISKKRYA GLYFTNTQSY
     DKMDCKGIET VRRDNCPLVA NVLNTCLEKI LIDRDPNKAV EYTKMVISDL LCNRIDISQL
     IISKELTKTD KEYAAKQAHV ELAARMRKRD PGSAPHLGDR VPYVIIAASK GTAAYMKAEV
     SSIFHTSKDP IYVLENSIPI DTQYYLENQL SKPLLRIFDP ILGDKAESIL LRGDHTRTKT
     VTHSKLGGLM AFTKKQETCL NCRAVLSNNG AICDHCKPKE VEIYQRELFQ VQYLEERFSR
     LWTECQRCQG SLHEEVLCSS RDCPIFYMRT KVKKDLQDNW KRMQRFDMDD F
//
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