UniProt: A0A2T3AUS7

Database: UniProt
Entry: A0A2T3AUS7_AMORE

LinkDB:  A0A2T3AUS7_AMORE 
Original site:  A0A2T3AUS7_AMORE

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Ontology (9)   
   GO (9)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (16)   
   InterPro (11)   
   Pfam (3)   
   PROSITE (1)   
   SMART (1)   
Literature (1)   
   PubMed (1)   
All databases (28)   

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ID   A0A2T3AUS7_AMORE        Unreviewed;      1751 AA.
AC   A0A2T3AUS7;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE            EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN   ORFNames=M430DRAFT_52710 {ECO:0000313|EMBL:PSS12408.1};
OS   Amorphotheca resinae ATCC 22711.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Amorphothecaceae; Amorphotheca.
OX   NCBI_TaxID=857342 {ECO:0000313|EMBL:PSS12408.1, ECO:0000313|Proteomes:UP000241818};
RN   [1] {ECO:0000313|EMBL:PSS12408.1, ECO:0000313|Proteomes:UP000241818}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 22711 {ECO:0000313|EMBL:PSS12408.1,
RC   ECO:0000313|Proteomes:UP000241818};
RX   PubMed=29315638; DOI=10.1111/nph.14974;
RA   Martino E., Morin E., Grelet G.A., Kuo A., Kohler A., Daghino S.,
RA   Barry K.W., Cichocki N., Clum A., Dockter R.B., Hainaut M., Kuo R.C.,
RA   LaButti K., Lindahl B.D., Lindquist E.A., Lipzen A., Khouja H.R.,
RA   Magnuson J., Murat C., Ohm R.A., Singer S.W., Spatafora J.W., Wang M.,
RA   Veneault-Fourrey C., Henrissat B., Grigoriev I.V., Martin F.M., Perotto S.;
RT   "Comparative genomics and transcriptomics depict ericoid mycorrhizal fungi
RT   as versatile saprotrophs and plant mutualists.";
RL   New Phytol. 217:1213-1229(2018).
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   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966,
CC         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|ARBA:ARBA00005755, ECO:0000256|RuleBase:RU000442}.
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DR   EMBL; KZ679015; PSS12408.1; -; Genomic_DNA.
DR   STRING; 857342.A0A2T3AUS7; -.
DR   InParanoid; A0A2T3AUS7; -.
DR   OrthoDB; 211439at2759; -.
DR   Proteomes; UP000241818; 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   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   InterPro; IPR025687; Znf-C4pol.
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   Pfam; PF14260; zf-C4pol; 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   4Fe-4S {ECO:0000256|RuleBase:RU000442};
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   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU000442};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU000442};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU000442};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000256|RuleBase:RU000442}; Nucleus {ECO:0000256|RuleBase:RU000442};
KW   Reference proteome {ECO:0000313|Proteomes:UP000241818};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000442};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU000442};
KW   Zinc-finger {ECO:0000256|RuleBase:RU000442}.
FT   DOMAIN          886..1083
FT                   /note="DNA-directed DNA polymerase family B exonuclease"
FT                   /evidence="ECO:0000259|Pfam:PF03104"
FT   DOMAIN          1150..1596
FT                   /note="DNA-directed DNA polymerase family B
FT                   multifunctional"
FT                   /evidence="ECO:0000259|Pfam:PF00136"
FT   DOMAIN          1647..1718
FT                   /note="C4-type zinc-finger of DNA polymerase delta"
FT                   /evidence="ECO:0000259|Pfam:PF14260"
FT   REGION          418..440
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          497..567
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          592..640
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        497..523
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        526..543
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        544..563
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        607..628
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1751 AA;  199365 MW;  86584F3E2379AC08 CRC64;
     MDLFRVRLNC IDSYQASPTK FDPVLRNNVK PSQAHKEPKV PIIRVFGATE TGQKVCAHIH
     GAFPYLYIEY TGSLVPDEVG AYIHRLHLSI DHALAVSYRR NIHDVNAKFV ARITLVKGIP
     FYGFHVGYRY YLKIYMLDPM VMTRLADLLR QGVVMKKVFQ PFEAHLQYLL QWMADYNLYG
     CGYIDCSVVT FRSPVPKYEE LVNMSHLWHD RSIPGELVTE DAELPRVSHC SIEVDICVQD
     IINRHDIKPR PLHHDFIERL NPLGPDEKLV HSMAGLWRDE ARRRRSRVSD PEPGSSLFPA
     EAMISMSADS RSSRSDGWVH EEEYREKVMD LIADEKGKSD GAKISFTTFV QHSPFEATVR
     TSLESVEDLF PENLRQALEL VPKTSIRSIH YDLNDQEIGD VDEKGILAFD LSGHDGGAYD
     SDDESMRGME FSQRKQGDHV EETHLDPADI IQEEHEVDNE SHRDGAQFEE QSLNLSDPDT
     LNSLTKSSAM DLTTEDAAIE PSPSNSLDSS YVSVCSGPQE NPPDHLSVQA HRKSPEKNLK
     RPESPVKQSN SVNKRQRVSL GQTRRPDISL VDPERTVDSD YVNHRNMRKV SLAETASLHE
     DSKLGQMMRS RPNTDNVSLL ATGPRRESSS QDRLYERPQM QPLRFPVVKD PHDPNTILRI
     SQKSASQLSS PERKYSVTYN PSKASEFPSS DISLRSVGIC TPRSNILVHM RNRIEKQDNS
     VILLALDELP PSSVSVISTM QNFSLPEVIY QDAFYSNERD VPERAREWAG REFKLESLTV
     PFLPEFDPTG SSEATFGDKT AIVLDKPKVE KVHESRRRAC GLRSWEMANS PPAYAEVHSW
     FRSEEAARLA NATTSHVPLR VVAGSQGKGK LSQVEGPTQK NKHGFKYTQN QATCSVQHEA
     QYMSTMSLEI HINTRGDFVP NPEHDEVQCL FWGLHSDQAE HESNSNTEGI RVGVVVLSGN
     NTMAQNIAKQ VGFEIEEESS ELDLMIHMVD IVRSYDPDIL TGYEVHGSSW GYLIERARLK
     YDYDLCDEFS RVKVQSHGRF GKDNDKWGFN NTSSIRVTGR HLINIWRAMR SELNLLQYTM
     ENVVFHLLHR RIPHFTWADL TRWYTNGRPR DLAKVIKHYI SRVQLDLQIL EQNELIARTS
     EQARLLGVDF FSVFSRGSQF KVESLMFRIA KPENFLLVSP SRKQVGGQNA LECLPLVMEP
     QSAFYTSPVL VLDFQSLYPS VMIAYNYCYS TFLGRVVDWR GTNKMGFTEF KRQQRLLELL
     QDHINIAPNG IMYTKPEIRK SLLAKMLSEI LETRVMVKSG MKLDKDDKTL QRLLNNRQLA
     LKLIANVTYG YTSASFSGRM PCSEIADSIV QTGRETLEKA IAFIHSVERW GAEVVYGDTD
     SLFVHLKGRT KDQAFDIGEE IAKAVTNMNP RPVKLKFEKV YFPCVLLAKK RYVGFKYESR
     DQTKPDFDAK GTETVRRDGI PAEQMIEEKA LKILFRTSDL SQVKSYFQNE CEKIMKGSVS
     IQDFCFAREV KLGTYSNKGP PPPGALISTK RMLEDSRAEP QYGERVPYVV ITGAPGARLI
     DRCVAPEKLL EDDHCELDAE YYISKRLIPP LERIFNLVGA NIRSWYDEMP KVQRIRRIDT
     NIQLQGQSKE LGINKKTLES YLKSSSCVVC KEKVETDGPV CPGCVANRPW SIFSLRTRLS
     HAERKFMDLQ KICQSCSGIS PLDEVKCDSK DCPVFYSRTR QKARLKTERA IIEPVMTELT
     GSCVDLESLE W
//

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