UniProt: A0A428SWJ7

Database: UniProt
Entry: A0A428SWJ7_9HYPO

LinkDB:  A0A428SWJ7_9HYPO 
Original site:  A0A428SWJ7_9HYPO

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Ontology (7)   
   GO (7)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (14)   
   InterPro (10)   
   Pfam (2)   
   PROSITE (1)   
   SMART (1)   
All databases (23)   

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ID   A0A428SWJ7_9HYPO        Unreviewed;      1591 AA.
AC   A0A428SWJ7;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE            EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN   ORFNames=CEP52_012829 {ECO:0000313|EMBL:RSL94138.1};
OS   Fusarium oligoseptatum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium solani species complex.
OX   NCBI_TaxID=2604345 {ECO:0000313|EMBL:RSL94138.1, ECO:0000313|Proteomes:UP000287144};
RN   [1] {ECO:0000313|EMBL:RSL94138.1, ECO:0000313|Proteomes:UP000287144}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL62579 {ECO:0000313|EMBL:RSL94138.1,
RC   ECO:0000313|Proteomes:UP000287144};
RA   Stajich J.E., Carrillo J., Kijimoto T., Eskalen A., O'Donnell K.,
RA   Kasson M.;
RT   "Comparative genomic analysis of Ambrosia Fusariam Clade fungi.";
RL   Submitted (JUN-2017) 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-COMP:17339,
CC         Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC         ChEBI:CHEBI:173112; EC=2.7.7.7;
CC         Evidence={ECO:0000256|RuleBase:RU000442};
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-B family.
CC       {ECO:0000256|ARBA:ARBA00005755, ECO:0000256|RuleBase:RU000442}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RSL94138.1}.
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DR   EMBL; NKCK01000172; RSL94138.1; -; Genomic_DNA.
DR   STRING; 1325735.A0A428SWJ7; -.
DR   Proteomes; UP000287144; Unassembled WGS sequence.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
DR   GO; GO:0016035; C:zeta DNA polymerase complex; IEA:InterPro.
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: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   CDD; cd05778; DNA_polB_zeta_exo; 1.
DR   CDD; cd05534; POLBc_zeta; 1.
DR   Gene3D; 1.10.132.60; DNA polymerase family B, C-terminal domain; 1.
DR   Gene3D; 3.30.342.10; DNA Polymerase, chain B, domain 1; 1.
DR   Gene3D; 1.10.287.690; Helix hairpin bin; 1.
DR   Gene3D; 3.90.1600.10; Palm domain of DNA polymerase; 1.
DR   Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 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; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR042087; DNA_pol_B_thumb.
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   PANTHER; PTHR45812; DNA POLYMERASE ZETA CATALYTIC SUBUNIT; 1.
DR   PANTHER; PTHR45812:SF1; DNA POLYMERASE ZETA CATALYTIC SUBUNIT; 1.
DR   Pfam; PF00136; DNA_pol_B; 1.
DR   Pfam; PF03104; DNA_pol_B_exo1; 1.
DR   PRINTS; PR00106; DNAPOLB.
DR   SMART; SM00486; POLBc; 1.
DR   SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR   SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR   PROSITE; PS00116; DNA_POLYMERASE_B; 1.
PE   3: Inferred from homology;
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW   DNA replication {ECO:0000256|RuleBase:RU000442};
KW   DNA-binding {ECO:0000256|RuleBase:RU000442};
KW   DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932,
KW   ECO:0000256|RuleBase:RU000442};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000256|RuleBase:RU000442};
KW   Reference proteome {ECO:0000313|Proteomes:UP000287144};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000442}.
FT   DOMAIN          823..1005
FT                   /note="DNA-directed DNA polymerase family B exonuclease"
FT                   /evidence="ECO:0000259|Pfam:PF03104"
FT   DOMAIN          1072..1518
FT                   /note="DNA-directed DNA polymerase family B
FT                   multifunctional"
FT                   /evidence="ECO:0000259|Pfam:PF00136"
FT   REGION          434..454
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          548..627
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        551..624
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1591 AA;  180852 MW;  661312E37B6413D5 CRC64;
     MDLFRVRLNC IDHYQATPTR YDPQLRNDVR PSQISKGPKV PVVRIFGSTE TGQKVCAHVH
     GAFPYLYVEY QGGLAPDEVG AYIYRFHLSI DHALAVSYRR DKKGDNARFV ARITLVKGVP
     FYGFHVGYRF FLKIYMFNPV VMSRLADLLQ QGVIMKQKFQ PYEAHLQYLL QFMTDFNLYG
     CDYLDASSTR FRSPVPEYDE GSNSSHLWHT RSIPEGYITD ETTLPRASHC SIEVDICVQD
     IINRKKVRER LLHHNFTERT SPIPGDMKYV YSMAGLWKDE TKRRKRKMQN PGPESSPFPP
     EVLVSMSANV RDSQPQGWIH EDEYRAQIQE LILAERGATS DELSFDNFAK ALPYEEQVRT
     TLQSVEDLFP STLAPALGLP SGVEEAKKDP ASSIEVDERK VHQVGDLEDD FFPEDSDEEA
     IAMMVSLEKA AAKGARGSAA QSSEARRKQD TTVDAMDDME DDSLDSLLGI CQSGLKTGRL
     PDIPLSKELL ELAENEGLIG RTWKTAPSNA PLQLKRPLPS LTSILSPNKR PRLDEQLLID
     DDEMHLVPFP SDSTKPSTST FRTHSILKGR SPVTKTSTSP SKEVVGSNSK LHFPTVKDQN
     DPNTKLRLSQ MSQKSASQQS EDGHFTKHVS FDPSTFAPGP EKGLSQVTLS SSLLSSIALE
     DEESDSQESK IYRAIEKFSG PQVHFILPPP PSAAFVASSL KDYCLPDAIY EDAYYSKEKD
     VPGRMREYAG KEFRLEGNTL PFLPEFDPTA TSPANYGIKH GPLDKTRMNL QLERRGKKCS
     WRGWEIANPP PTYHEIDGPT PKNKHGFKYT QGKKSTSVEH EAQYMSTMSL EVHVNTRGKF
     VPNPEEDEVQ CVFWALKSDE TVIGSQNQAE AVQTGILVLA GDSDLTERIR RQTTAEVIEE
     ASELDLMVRM VEIVRTHDPD ILTGYEVHGS SWGYMIERAR LKYDYNLCDE FSRMKTESHG
     RFGKENDRWG FNTTSTIRVT GRHMINVWRA MRGELNLLQY TMENVVWHLL HRRIPHYSWR
     SLTSWYKSGK HRELSRMLRY YQNRTRLDIE ILEANELIAR TSEQARLLGV DFFSVFSRGS
     QFKVESIMFR IAKPENFLLV SPSRKQVGGQ NALECLPLVM EPQSAFYNSP LVVLDFQSLY
     PSVMIAYNYC YSTFLGRITN WRGMNKMGFT EYKRQQGLLA LLEDYINIAP NGMMYAKTEI
     RKSLLAKMLT EILETRVMVK SGMKQDKDDK VLQQLLNNRQ LALKLLANVT YGYTSASFSG
     RMPCSEIADS IVQTGRETLE RAIAYIHSVE KWGAEVVYGD TDSLFIYMKG RTREQAFDIG
     NEIAKAITEM NPQPIKLKFE KVYHPCVLLA KKRYVGYKYE SKDQVKPEFD AKGIETVRRD
     GTPAEQKIEE KALRLLFETA DLSQIKAYFQ KQCHKIMRNN VSVQDFCFAK EVRLGTYSNK
     GPPPAGALIS TKRMLEDARA EPQYGERVPY VVITGAPGAR LIDRCVAPEE LLSNPHWQLD
     AEYYISKNLI PPLERIFNLV GANVRQWYDE MPKVQRIRHA TTLGKRKTTL ESYMKSSHCL
     ICNKKFTNED NPLYTSIDRG ASLAGGIIAL S
//

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