UniProt: A0A2V1ECI0

Database: UniProt
Entry: A0A2V1ECI0_9PLEO

LinkDB:  A0A2V1ECI0_9PLEO 
Original site:  A0A2V1ECI0_9PLEO

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Ontology (5)   
   GO (5)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (21)   
   InterPro (14)   
   Pfam (4)   
   PROSITE (2)   
   SMART (1)   
Literature (1)   
   PubMed (1)   
All databases (29)   

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ID   A0A2V1ECI0_9PLEO        Unreviewed;      1464 AA.
AC   A0A2V1ECI0;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE            EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN   ORFNames=DM02DRAFT_703350 {ECO:0000313|EMBL:PVI07384.1};
OS   Periconia macrospinosa.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Massarineae; Periconiaceae; Periconia.
OX   NCBI_TaxID=97972 {ECO:0000313|EMBL:PVI07384.1, ECO:0000313|Proteomes:UP000244855};
RN   [1] {ECO:0000313|EMBL:PVI07384.1, ECO:0000313|Proteomes:UP000244855}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSE2036 {ECO:0000313|EMBL:PVI07384.1,
RC   ECO:0000313|Proteomes:UP000244855};
RX   PubMed=29679020; DOI=10.1038/s41598-018-24686-4;
RA   Knapp D.G., Nemeth J.B., Barry K., Hainaut M., Henrissat B., Johnson J.,
RA   Kuo A., Lim J.H.P., Lipzen A., Nolan M., Ohm R.A., Tamas L.,
RA   Grigoriev I.V., Spatafora J.W., Nagy L.G., Kovacs G.M.;
RT   "Comparative genomics provides insights into the lifestyle and reveals
RT   functional heterogeneity of dark septate endophytic fungi.";
RL   Sci. Rep. 8:6321-6321(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   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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; KZ805304; PVI07384.1; -; Genomic_DNA.
DR   STRING; 97972.A0A2V1ECI0; -.
DR   Proteomes; UP000244855; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:1902975; P:mitotic DNA replication initiation; IEA:InterPro.
DR   CDD; cd05776; DNA_polB_alpha_exo; 1.
DR   CDD; cd05532; POLBc_alpha; 1.
DR   Gene3D; 2.40.50.730; -; 1.
DR   Gene3D; 3.30.70.2820; -; 1.
DR   Gene3D; 1.10.3200.20; DNA Polymerase alpha, zinc finger; 1.
DR   Gene3D; 1.10.132.60; DNA polymerase family B, C-terminal domain; 1.
DR   Gene3D; 3.90.1600.10; Palm domain of DNA polymerase; 2.
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; IPR024647; DNA_pol_a_cat_su_N.
DR   InterPro; IPR042087; DNA_pol_B_thumb.
DR   InterPro; IPR023211; DNA_pol_palm_dom_sf.
DR   InterPro; IPR038256; Pol_alpha_znc_sf.
DR   InterPro; IPR045846; POLBc_alpha.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   InterPro; IPR015088; Znf_DNA-dir_DNA_pol_B_alpha.
DR   NCBIfam; TIGR00592; pol2; 1.
DR   PANTHER; PTHR45861; DNA POLYMERASE ALPHA CATALYTIC SUBUNIT; 1.
DR   PANTHER; PTHR45861:SF1; DNA POLYMERASE ALPHA CATALYTIC SUBUNIT; 1.
DR   Pfam; PF12254; DNA_pol_alpha_N; 1.
DR   Pfam; PF00136; DNA_pol_B; 1.
DR   Pfam; PF03104; DNA_pol_B_exo1; 1.
DR   Pfam; PF08996; zf-DNA_Pol; 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.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE   3: Inferred from homology;
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   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000256|RuleBase:RU000442};
KW   Reference proteome {ECO:0000313|Proteomes:UP000244855};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000442};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          1280..1302
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS00028"
FT   REGION          57..131
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          149..237
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        66..114
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        158..172
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1464 AA;  165228 MW;  78D8AFA8E8F85C9F CRC64;
     MSRAAKLAEL RALRASGKTR LSTYEVEEEE QLYDEVDEEG YKKLVRGRLE EDDFIVDDNG
     EGYVDDGREE WDGHQNGYRY ASESEDDARP SKGKAAKRKR EEDKEQRDKQ NRKINSFFSA
     KNAAAAPKPV ATAEENDFME DLLGEINTNV PRAAPRMRPV KTESRRKTRV LSPPVSENRA
     HAAKKQAADS DNFMPETPPA ENTYDDDPLP TLGDDDDIPM SDPVPQSSPV AKAVERKSQP
     MVKIEEENDD DGMEVEQVVG HSGVASASVN ISGKRPVPRI KKAEYPTPAS SSPVGPTVAP
     AVDASSWNNV TSKLNVVSSP APNINNNAGM GKLNPESAVE NDGSLHMFWI DYTEINGSLC
     LFGKVKDRTT GKYVSCFVKV DNILRKLYFL PREYRVRRGH QTDEEVEMGD VSDEIDDIMS
     KHRVTMHKIK PSSRKYAFEL PNIPREADYI KLLYGYDKMP LSADIQGETF SHVFGTNTSL
     FEQFVLWKNI MGPCWLKIED ANFNAVTNAS WCKLELAVTK PNSITVLPNT ENIDAPPLTL
     MSISLRTTFN AKDNKQEILM ASAMVYDNFS LTDPTPAEQL PCKSFTIMRP HGEAYPTGFK
     METEKQKSTI MLRKTEQDLL SYFMAMFQRH DPDVLIGHRL DDIDFSVLLN RMREKKTPGW
     HRIGRLRRSE WPKNMGKGGG SFFAERQLAS GRLLCDLAND LGKSLMTKCQ SWSLEEMCQL
     VLDKRRDELD NEAALKTWAT TKEGLMNYVK HCQADAFFIA AISIKVQMLS LSKVLTNLAG
     NSWARTLSGT RAERNEYILL HEFYKNKYIC PDKQWGKGKA KVEDVAGEGE EGVDAKKKDK
     FKGGLVFEPE KGLYDKFILV MDFNSLYPSI IQEFNICFTT VERSDLTEDD DKVPEVPGEE
     QEKGILPRLI ANLVHRRREV KKLMKSPTAT PDQITTWDIK QLALKLTANS MYGCLGYSKS
     RFYARPLAML TTYKGREILR RTKDMAEEKM LRVIYGDTDS VMINTNVDNI QEALKLGEDF
     KKQVNGSYKL LEIDIDNVFR RILLHAKKKY AAINMIRVED KYIEKLEVKG LDMRRREYCA
     LSKNTSEELL RFLLSGEDPE TVVEKIHEHL RTLAENMRSF TIPTWKYTIY TQLGKHPKDY
     PNGNSMPSVQ VANRLIAKGK HVKAKDVMSF IITGDSSGSA ENAAKNAYPV DEVLKADSGL
     KPDIDYYLHK QILPPVERLC APISGTNITM LAACLGLDTT KYRVTTVSGS NTQDIEIQPL
     ESQIPDSVRF QECVPLFLRC RSCHTAFPFN GISSVHTTTV THDGLQCPNA SCRAILSNLS
     VVAQLESAIR QTISSYYTGT VVCNDPACAS RTRQISVYGH RCLGPKGLAK DCLGRMSYTY
     SDKDVWNQLL YFASLFDVER AGKEPDGING VKVEGASEKR EKLKILAEVN RERFNTLKGV
     VDRWLEKNGR QWVQMDSLFA FALK
//

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