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Database: UniProt
Entry: A0A067TYF1_GALM3
LinkDB: A0A067TYF1_GALM3
Original site: A0A067TYF1_GALM3 
ID   A0A067TYF1_GALM3        Unreviewed;      1638 AA.
AC   A0A067TYF1;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   05-JUN-2019, entry version 23.
DE   RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE            EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN   ORFNames=GALMADRAFT_131759 {ECO:0000313|EMBL:KDR84999.1};
OS   Galerina marginata (strain CBS 339.88).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Agaricomycetes; Agaricomycetidae; Agaricales; Strophariaceae;
OC   Galerina.
OX   NCBI_TaxID=685588 {ECO:0000313|EMBL:KDR84999.1, ECO:0000313|Proteomes:UP000027222};
RN   [1] {ECO:0000313|Proteomes:UP000027222}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 339.88 {ECO:0000313|Proteomes:UP000027222};
RX   PubMed=24958869; DOI=10.1073/pnas.1400592111;
RA   Riley R., Salamov A.A., Brown D.W., Nagy L.G., Floudas D., Held B.W.,
RA   Levasseur A., Lombard V., Morin E., Otillar R., Lindquist E.A.,
RA   Sun H., LaButti K.M., Schmutz J., Jabbour D., Luo H., Baker S.E.,
RA   Pisabarro A.G., Walton J.D., Blanchette R.A., Henrissat B., Martin F.,
RA   Cullen D., Hibbett D.S., Grigoriev I.V.;
RT   "Extensive sampling of basidiomycete genomes demonstrates inadequacy
RT   of the white-rot/brown-rot paradigm for wood decay fungi.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:9923-9928(2014).
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; KL142367; KDR84999.1; -; Genomic_DNA.
DR   EnsemblFungi; KDR84999; KDR84999; GALMADRAFT_131759.
DR   OrthoDB; 20210at2759; -.
DR   Proteomes; UP000027222; 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:UP000027222};
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:UP000027222};
KW   Transferase {ECO:0000256|RuleBase:RU000442};
KW   Zinc {ECO:0000256|RuleBase:RU000442};
KW   Zinc-finger {ECO:0000256|RuleBase:RU000442}.
FT   DOMAIN       52    189       DNA_pol_B_exo1. {ECO:0000259|Pfam:
FT                                PF03104}.
FT   DOMAIN      809    981       DNA_pol_B_exo1. {ECO:0000259|Pfam:
FT                                PF03104}.
FT   DOMAIN     1034   1450       DNA_pol_B. {ECO:0000259|Pfam:PF00136}.
FT   DOMAIN     1524   1593       zf-C4pol. {ECO:0000259|Pfam:PF14260}.
FT   REGION      274    297       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A067TYF1}.
FT   REGION      424    590       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A067TYF1}.
FT   REGION     1619   1638       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A067TYF1}.
FT   COMPBIAS    429    445       Acidic. {ECO:0000256|MobiDB-lite:
FT                                A0A067TYF1}.
FT   COMPBIAS    472    486       Polar. {ECO:0000256|MobiDB-lite:
FT                                A0A067TYF1}.
SQ   SEQUENCE   1638 AA;  184993 MW;  57E524DBD7841FE9 CRC64;
     MTDNAVSPVA GKKSAQLHVR INHIDHTLIP PGNLDNSTLP RVPVLRVFGR SSTGQTTCVH
     VHQVYPYFFV GYPGKLSPRH VKKHISKLFR SLNHAIALSL KRNPLSGKSN FIRAILLVKG
     IDFYGFHASY DPFLKILVAD PAHVTRTVTI LQSGSVMGTR FTVYESHLSY ILQFLCDFGL
     YGCGLIELEE VFERCGEEPE ETTTPTTNKF GVSSYFRESR LPLEVDVIAP HILNRHSLVA
     RNMHHRLEIP TPFLSQEPLV LSVRELWQDE RNHRRGLGLD PSPEVPIDPS ESSRAGGGDW
     VAEARWWDEI RKRIGSNSAQ EKPISTELKQ TWELFVMTTF ESVEAIWEKQ YKTWKPSKEK
     AEIDAPEVDK SEQIPHLQDY VWDDITQEIT DGKDEQIEVD ISMLSNQDIN RLDQEEADFL
     NKEELQEPPG AEENEDAEDS VYEDEQDSKD PANGDSERES SGPLYWRPSK FANQNGRLST
     RKNFGSPPSP RLLGQDRIGS PTPTKLMRGH PGTHNVVTEE AEKTEEVEND DDTDERDLTP
     TRFNEYLPGS RKTEIRFATA RDNPPEPLDV ENDGDMDESD QTPTKSNKYL WSPKTKFATS
     RDDLPQLPDA NQQDTMLSDI QEELSVTPAV LDAKERSSLI AARAVQLSKA FNTCKATSTN
     QYVYFLQPPT WLDLHLGLQN LGLSSKIYQT PYYSEDVDIP DNPKEYAGLT YHLKGGQGIA
     SLDDWYTEPA SDANQTVRNS PCLNPIGVGG WEYASHLPSM KEIRRTMELL EIRTNNKMKK
     QKLTSQIEGP TQANIYGFKT SPIADLSASR ENANLAVMSV EIFVPTKDDK VPNAASDQVF
     AVFYAYHISG MEIIHTGILV ARNSQIHEHR TRHIKFEIVE TELDLLNRLV DLVVEHDPDI
     LTGWELQLNS WGYLDARCNT YGLAFPDVIS RAPPRHSGGS EIDQWGLRKT STFKTAGRHV
     LNLWRIMRSE KTLTIYTFEN VVFEVLGKRP VPAHAVLVVE HLLMRVITNL ELLEATETIT
     KTAEFARVFG VDFFSVLSRG SQFKVESFMF RIAKPESFVL ISPSRNDVGK QNAAECMPLI
     LEPASAFYSS PLLVLDFQSL YPSIMIAYNY CYSTCLGRIT DFQGTYKFGV VNNLEISTEL
     LEKLRSHITV APNGIMYVKH DVRRGLLGRM LAELLDTRVM VKQAMKRADG DKARKRILDA
     RQLSLKYIAN VTYGYTSATF SGRMPAVEIA DSIVQTGRET LEKAIDVIEN TTKWDAKAWT
     CCDPVVYGDT DSVFVYLPGR TKRQAFAIGN EIADTITSLN PAPIKLKFEK VYLPCVLMAK
     KRYVGFKYES IDDTEPAFDA KGIETVRRDG VLAQPHDSNV FKGSRILFRT QNLSEVKDYC
     CRSWTKLLEN KASVQDFIFA KEVKMGTYSD RGPPPPGVVV AARRMIFDPN NEAQYGDRIP
     YVIVRSTSGA PSQLQLDAHY YITRVLIPPL ERIFNLAGAD VRQWFNDMPK SIVPELVSPR
     KPKGVPASSP DRMNISEHFT GTQCLSCGGP SPEGLCDECC FSPQESIVNL ELRIRTREER
     LTSTHRICST CTGSTPSDPI HCESLDCQWF FARRKAEAGM ELVPLFEELI EELETLPERD
     GIRTEEPEMD FYEAEDDL
//
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