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Database: UniProt
Entry: A0A0B7NU19_9FUNG
LinkDB: A0A0B7NU19_9FUNG
Original site: A0A0B7NU19_9FUNG 
ID   A0A0B7NU19_9FUNG        Unreviewed;      1862 AA.
AC   A0A0B7NU19;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   05-JUN-2019, entry version 25.
DE   RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE            EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN   Name=PARPA_13080.1 scaffold 45923 {ECO:0000313|EMBL:CEP18773.1};
OS   Parasitella parasitica.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Parasitella.
OX   NCBI_TaxID=35722 {ECO:0000313|EMBL:CEP18773.1, ECO:0000313|Proteomes:UP000054107};
RN   [1] {ECO:0000313|EMBL:CEP18773.1, ECO:0000313|Proteomes:UP000054107}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 412.66 {ECO:0000313|EMBL:CEP18773.1,
RC   ECO:0000313|Proteomes:UP000054107};
RA   Ellenberger Sabrina;
RL   Submitted (SEP-2014) 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}.
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DR   EMBL; LN733911; CEP18773.1; -; Genomic_DNA.
DR   OrthoDB; 20210at2759; -.
DR   Proteomes; UP000054107; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016035; C:zeta 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:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   GO; GO:0019985; P:translesion synthesis; IEA:InterPro.
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; IPR030559; PolZ_Rev3.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   InterPro; IPR025687; Znf-C4pol.
DR   PANTHER; PTHR45812; PTHR45812; 1.
DR   Pfam; PF00136; DNA_pol_B; 1.
DR   Pfam; PF03104; DNA_pol_B_exo1; 2.
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:UP000054107};
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:UP000054107};
KW   Transferase {ECO:0000256|RuleBase:RU000442};
KW   Zinc {ECO:0000256|RuleBase:RU000442};
KW   Zinc-finger {ECO:0000256|RuleBase:RU000442}.
FT   DOMAIN       46    208       DNA_pol_B_exo1. {ECO:0000259|Pfam:
FT                                PF03104}.
FT   DOMAIN     1019   1196       DNA_pol_B_exo1. {ECO:0000259|Pfam:
FT                                PF03104}.
FT   DOMAIN     1263   1709       DNA_pol_B. {ECO:0000259|Pfam:PF00136}.
FT   DOMAIN     1756   1837       zf-C4pol. {ECO:0000259|Pfam:PF14260}.
FT   REGION      314    341       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A0B7NU19}.
FT   REGION      485    512       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A0B7NU19}.
FT   REGION      589    672       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A0B7NU19}.
FT   REGION      685    724       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A0B7NU19}.
FT   COMPBIAS    598    620       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                A0A0B7NU19}.
FT   COMPBIAS    632    672       Polyampholyte. {ECO:0000256|MobiDB-lite:
FT                                A0A0B7NU19}.
SQ   SEQUENCE   1862 AA;  214173 MW;  B8F28A551BF8157F CRC64;
     MTISVRIVNL DHYMADPGPL DRSYTPFSDE KLCKVPVLRI FGSTNVGQKV CLHIHQVFPY
     FFVPYDIPIG YTTDEEVQKD IFQFGTSLNE AMDLARPQKK KNQHIAAIVL VKGVPFYGYH
     VGYKTYLKIY ITNPNEKHQM LKILQSGAIQ DISFQPHEAH LNFELQFLID HNLYGMDWIH
     IEQHNISPSF KIQFRSPMLD EPKANYHRSQ SSSDISTSSH FLISLNSPQQ ENFYTSKTVP
     LDLQSDAVPR SSYCELELDI TGMSILNRHE LKERSIHSSL KREKQVQASA LNQPEEESKK
     KLVKSLESIW ADETSRRRSR GIREPIPPVT QLDEREPRKP WSAEPALRRL MEKMMTGHAF
     DEVSETQQPS ALIPQIMTVF EAIEALYPDE YFVYQQSQHI LDHPASSPVE KQHTLEFTSS
     PTNRVESTPA CTPPSYILNS NPRHFNVSAT PSRYRTLDVQ SQLNTSIIHS FIEGINSSLY
     QVDEGELPHH GDESNDDDFV EENDEFELSN EDNLRNSDIA RWLEETEREE VEARLKRRKT
     RVIAYEGDES ITYEPRKLDF KAEADRIDTI LKTEHTHKTR KEVLNFAEEE EDIEDDFKNQ
     DNDKGKGKGK GKEDKRGSES FTISDIPPEP MPRVKRSQRK RNIDQLDGSG DNEERRKDWP
     KTPAERWEDE KRSLKKIWRK KSAINKSLKK EEKRSLSTPP TLDDKLTKKS SELQRAKSDE
     SLHPKGFQKV VVKIRKRIPK KRKNPAPKVE DISIEMPLTK ELTTSTAKIV EKEKRDVEHN
     GLVEADDAVY QLEENDNEEA TSTHFTKKTE EMCLSQEAVC SSEQNRFFLK DTATIHPPMF
     DISQYSAIQT QTEKTVGEEV MRAIRSDAGH DMMGTKEFVY PSIPPRIHQG NLSQEGVVYQ
     EPFYSNPSDV PRFPTIFAGK EFKLPTVGLP ALKEFKSVYG NESTAISKEQ ITIKTWTPTK
     NPPSFTKVQD WMRTEAFRKP TKTIKKDSKT QLNQPTMSNT FNFKFSASKP VSKVKRIRDY
     IDYFSLEIHV NTRDQLLPDP QYDAVQLVFW CLQTEDLRIP SNGYQEGFYV GVIAMKDFDI
     SRIGICNSRL AVDYADTEER LFSLLIERIR YYDPDMLVGY EVQNASWGYL VDRGVQLGYH
     LLDELSRVIT TSESIIRDQW GYQKASVYKV TGRHVLNVWR LMRNELTLTS YTFENVAYNL
     LHDRVPHYSH ATLTSWYTKG LAVLKYRLFK YYMKRVQLNL DMLDASQVVS RTCESARVYG
     IDFYAVISRG SQYNVESVMF RIAKPENYVL ITPSRSQVAS QRSLEILPLI MEPISQFYSS
     PMVVLDFQSL YPSIMIAYNY CYSTCLGRIR KSDETSRFGV LPSFEPDDGL LDILKDYINV
     SPNGIMFVKP EIRKSLLAKM LSELLDTRVM VKRAMKDYKE DPGLLRMLDA KQLTLKLLAN
     VTYGYTSASF SGRMPSVEIA DSIVASGRET LERSIKLINE TEKWGARVVY GDTDSMFIYF
     PGKTKDEAFV LGNDIAETVT KLNPAPVKLK FEKVYHPAVL LAKKRYVGFK YENPSDETPV
     FEAKGIETVR RDGTAATQKV LESCLKILFR TQDMSELKAF LYDEWTKILS NRVLLQDFII
     SKEVRMGTYS SRGGPNGALI AQAQMDVDPR AEPQYGERVP YVVVYRGPHA KLKDKVVQPE
     ELLNDSSLRL DAEYYIRKQI IPPLSRVFNL MGVDILSMYE SMPRSQKAAA MNSALNTTNQ
     AKSLTRIDQY YASSHCIVCR KLADQVICKQ CKEDTSSTIF TMLSRQQISQ DKFRKLLQVC
     QDCSNVSPLD AMTVMEQEQE YADIPCNSLD CPIFYERLKG KEDVRVTDTY NALIQNFYDP
     QI
//
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