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Database: UniProt
Entry: A0A0C3HXU8_9PEZI
LinkDB: A0A0C3HXU8_9PEZI
Original site: A0A0C3HXU8_9PEZI 
ID   A0A0C3HXU8_9PEZI        Unreviewed;      1706 AA.
AC   A0A0C3HXU8;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   05-JUN-2019, entry version 24.
DE   RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE            EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN   ORFNames=OIDMADRAFT_151444 {ECO:0000313|EMBL:KIN07695.1};
OS   Oidiodendron maius Zn.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Myxotrichaceae; Oidiodendron.
OX   NCBI_TaxID=913774 {ECO:0000313|EMBL:KIN07695.1, ECO:0000313|Proteomes:UP000054321};
RN   [1] {ECO:0000313|EMBL:KIN07695.1, ECO:0000313|Proteomes:UP000054321}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Zn {ECO:0000313|EMBL:KIN07695.1,
RC   ECO:0000313|Proteomes:UP000054321};
RG   DOE Joint Genome Institute;
RA   Kuo A., Martino E., Perotto S., Kohler A., Nagy L.G., Floudas D.,
RA   Copeland A., Barry K.W., Cichocki N., Veneault-Fourrey C., LaButti K.,
RA   Lindquist E.A., Lipzen A., Lundell T., Morin E., Murat C., Sun H.,
RA   Tunlid A., Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.,
RA   Nordberg H.P., Cantor M.N., Hua S.X.;
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000054321}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Zn {ECO:0000313|Proteomes:UP000054321};
RG   DOE Joint Genome Institute;
RG   Mycorrhizal Genomics Consortium;
RA   Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA   Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A.,
RA   Lipzen A., Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H.,
RA   Tunlid A., Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT   "Evolutionary Origins and Diversification of the Mycorrhizal
RT   Mutualists.";
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}.
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DR   EMBL; KN832870; KIN07695.1; -; Genomic_DNA.
DR   EnsemblFungi; KIN07695; KIN07695; OIDMADRAFT_151444.
DR   OrthoDB; 20210at2759; -.
DR   Proteomes; UP000054321; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000054321};
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:UP000054321};
KW   Transferase {ECO:0000256|RuleBase:RU000442};
KW   Zinc {ECO:0000256|RuleBase:RU000442};
KW   Zinc-finger {ECO:0000256|RuleBase:RU000442}.
FT   DOMAIN       49    241       DNA_pol_B_exo1. {ECO:0000259|Pfam:
FT                                PF03104}.
FT   DOMAIN      861   1045       DNA_pol_B_exo1. {ECO:0000259|Pfam:
FT                                PF03104}.
FT   DOMAIN     1113   1558       DNA_pol_B. {ECO:0000259|Pfam:PF00136}.
FT   DOMAIN     1609   1680       zf-C4pol. {ECO:0000259|Pfam:PF14260}.
FT   REGION      284    303       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A0C3HXU8}.
FT   REGION      431    467       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A0C3HXU8}.
FT   REGION      834    858       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A0C3HXU8}.
FT   COILED     1634   1654       {ECO:0000256|SAM:Coils}.
FT   COMPBIAS    439    467       Polar. {ECO:0000256|MobiDB-lite:
FT                                A0A0C3HXU8}.
SQ   SEQUENCE   1706 AA;  194945 MW;  558ED8CE6E04581C CRC64;
     MDVFRVRLNY IDTYQASPTK YDPPLRRDVN LSHAYNENKI PIIRVFGSTE TGQKVCAHIH
     GAFPYLYIEY TGKLTTEEVG TYIHRIHLSI DYALSVSYRR DLRDGNSNFV ARVTLVKGIP
     FYGFHVGYRY FLKIYVLDPK VMTRLADLLR QGVIMKQVFQ PFEAHLQYLL QWMVDYNLYG
     CDYIDCSKAF FRFPVPSYER LSSPSHLWHH ESVPDGKVSE KSDLPRASHC SIEVDICVQD
     ILNRHDIKPR SLHHDFIEHL HPVVPDEKLV RSMASLWKDE ARRRKSRSSQ LEMGNDHSGD
     MPISMSAGLR ISEPGEWIHE VEYRERMMNL ITDEKSNNDE TTISFSTFVK HGPLDPTIRT
     SLESVEDLFP SNLNTSFGSS QETEIEINYE TGYDDRIVDE KRILTLNMND REEINSDSDS
     DSDIASELIT RGKLGDHSNE SDFNPSSSSQ EANRSTRALH TGSDISRPKI ESLSSSISFM
     EPEVKEPGHT PDDWTPLSYH LSLRHLSQIP DGSLKRLEPP ENQHNTVKKR QKIRFDQIHN
     RDARADKSVD DGNKWIETHN ATAKTTPFLI TNLSTQPTKE SPQKISIRHD RMKTHTLRFP
     IAKDSHALHT AARPSQKIAS PLYSPQNTRA NSVDDFMGYS IASSPVWPPI TNFWSSARTS
     TTNAPGLPLH IDNSFAKRLD RPSLLTFLEQ APSPDVVIST IESLGLPRVI YQDAFYSSES
     DVPDHSREWA GREFRLASLT TPFLPEFNPN GASETSCDTK PSIVLDKLKR EEEHQHRRRA
     CALQSWEIAT PPPSQSEVHR WYHAAERASI SSGIKSHETA KGGCNAREKS HLSQIDGPTQ
     KSKHGFKYTQ NTPLPINTKQ DTQYMSTMSL ELHVNTRADF VPDPEQDEVQ CLFWCFQSDE
     ARLKNIPGLQ DSRLGVVVAS EEGSMSRKIA WHRGLEIHEE SCELDLMVRM VEIVRDSDPD
     ILTGFEVHGS SWGYLIERAR LKYDYNLNDE FSRIKAQSYK RIAKDNDQWG LKTTSTIRIT
     GRHVINIWRA MRSELNLLQY TMENVAFHLL HRRIPHFTWS DLTKWYTSGK PKDISKVIAY
     YLSRVKVDVE ILEKNELIPR TSEQARVLGV DFFSVFSRGS QFKVESLMFR IAKPENFLLI
     SPSRKQIGGQ NALECLPLVM EPQSAFYNSP LLVLDFQSLY PSVMIAYNYC YSTCLGRVVN
     WRGTNKMGFT EFKRELRLLE LLKDHINIAP NGIMYTKPEI RMSLLAKMLR EILETRVMVK
     NGMKADKTDK ALQRLLNNRQ LALKLIANVT YGYTSASFSG RMPCSEIADS IVQTGRETLE
     KAIALIHSVE RWGAEVVYGD TDSLFVYLKG RTKDQAFDIG QEIAETITNM NPSPVKLKFE
     KVYFPSILLA KKRYVGFKYD SRDQVEPIFD AKGIETVRRD GTPAEQMIEE KALKILFRTS
     DLSKVKDYFQ KQCEKIMKGS VSIQDFCFAR EVKLGTYSGK GPPPPGALIS TKRMLLDARA
     EPQYGERIRY VVVTGAPGAR LIDRCVAPEE LLYDDHAELD AEYYILKNLI PPLERIFNLV
     GANVRSWYDE MPKFQRIRQV GNSAPLPGHS KEPGVNKKTL ESYMKSSSCL VCGERIDSDN
     PLCTTCYANK PLSLLSLQSR LDNAEREFLK VQKLCQSCSG ISPLDEVRCD SKDCPVFYTR
     TKQRSRLNTV RSVVEPVVEK LKTLEW
//
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