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Database: UniProt
Entry: A0A0C3QH83_9AGAM
LinkDB: A0A0C3QH83_9AGAM
Original site: A0A0C3QH83_9AGAM 
ID   A0A0C3QH83_9AGAM        Unreviewed;       992 AA.
AC   A0A0C3QH83;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00012417};
DE            EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
DE   Flags: Fragment;
GN   ORFNames=M407DRAFT_24793 {ECO:0000313|EMBL:KIO25836.1};
OS   Tulasnella calospora MUT 4182.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Cantharellales; Tulasnellaceae; Tulasnella.
OX   NCBI_TaxID=1051891 {ECO:0000313|EMBL:KIO25836.1, ECO:0000313|Proteomes:UP000054248};
RN   [1] {ECO:0000313|EMBL:KIO25836.1, ECO:0000313|Proteomes:UP000054248}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MUT 4182 {ECO:0000313|EMBL:KIO25836.1,
RC   ECO:0000313|Proteomes:UP000054248};
RG   DOE Joint Genome Institute;
RA   Kuo A., Girlanda M., 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:UP000054248}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MUT 4182 {ECO:0000313|Proteomes:UP000054248};
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., Lipzen A.,
RA   Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA   Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT   "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-B family.
CC       {ECO:0000256|ARBA:ARBA00005755}.
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DR   EMBL; KN823034; KIO25836.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C3QH83; -.
DR   STRING; 1051891.A0A0C3QH83; -.
DR   HOGENOM; CLU_001718_1_0_1; -.
DR   OrthoDB; 211439at2759; -.
DR   Proteomes; UP000054248; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR   CDD; cd05776; DNA_polB_alpha_exo; 1.
DR   Gene3D; 2.40.50.730; -; 1.
DR   Gene3D; 3.30.70.2820; -; 1.
DR   Gene3D; 6.10.10.100; -; 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; 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; IPR023211; DNA_pol_palm_dom_sf.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
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   SMART; SM00486; POLBc; 1.
DR   SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR   SUPFAM; SSF53098; Ribonuclease H-like; 1.
PE   3: Inferred from homology;
KW   DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054248};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          9..73
FT                   /note="DNA polymerase alpha catalytic subunit N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12254"
FT   DOMAIN          488..759
FT                   /note="DNA-directed DNA polymerase family B exonuclease"
FT                   /evidence="ECO:0000259|Pfam:PF03104"
FT   DOMAIN          827..987
FT                   /note="DNA-directed DNA polymerase family B
FT                   multifunctional"
FT                   /evidence="ECO:0000259|Pfam:PF00136"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          48..144
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          164..318
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          344..366
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          871..891
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        67..99
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        100..115
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        229..245
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        249..263
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        280..296
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        352..366
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         992
FT                   /evidence="ECO:0000313|EMBL:KIO25836.1"
SQ   SEQUENCE   992 AA;  111114 MW;  AD8C2D2D3EB8004A CRC64;
     MSSKNKGALA QLKASRAGQK RTDQYKVNRD TRIYDVVDES VYKTVVAGRT LEDDFVEDDG
     DHGYADNGEE DWDRGGYDDE RMDVDSEEEE REARRRAKTA KASSSSKSKK PSKPKVKAKA
     SSEGEEDDDA PAVSIDAYRK PIAPEKENDF LNSILNDLDT KTAVLPSAPS APKRNGAAHT
     TKSVARKRKP SMSDSSDGYG FEDFNNHRES AGFGPSSDVG LQSSPLKPAK KAKLEEVEPK
     LGDSSDGDFD TFLTDEDDAA FADLDFNDLQ FEETKPKPTI PPKPEPAKQP PKPPAIKAEP
     VDEKPVLSSA SKSKPVMMTD REVKNLDLEV PSWLQVNDIS NVKAKSGDDE GLGPLNSSTN
     GATSSSTVNA FEEDGSLRFF WLDYLELDGK LYFVGKVLDR GADGKKRNWV SCCVTVDGIE
     RNLFVRPREF RLDKEGLGTD EEVDQDDVYA DFDAIRRSCK VKSWAGKWVR RKYVFDDVEE
     GMEAEQDYLK VVYSFGGKYI CSGIEPLIPE EAQSPNIERI YGTKTSAFEL FVLKRKIMGP
     CWLNIQNPTI STKGVSWCKL EIEVDNPKTV SPFSESDDNA PRDVPPLTIM SVSLRTIVNH
     QTNQREIVSV AVRFWKDMNI DDPTPPEKQE SSAHIVIRCL DKYPAQFEDT ARRQTPVINA
     VRNEKALLSS LLTVIKTRDP DVIVGHEFLG VYLDVILMRL KQLKVEPWSC IGRFRRSKWP
     TIGRQGSNIR FLQGRLLCDL ASDAAKSMIT STTWSLTEMC GAHLSFNRQE IDPEDTAMYF
     DSTVASPDRL LGFVRHCEVD AFLHMALCAK VQMLPLTKQL TSLAGNSWNK TLNGGRAERN
     EYILLHEFHR LKYICPDKTW TKKVPAANVK PEVKEEAEDG ENGGAQPVAK PKKDKYKGGL
     VFDPKRGLWD TYVLVMDFNS LYPSIIQEFN IDFTTVLKAE IYEGDEEKIP DVPDGGTPQG
     VLPRLIATLV NRRRQVKNLM KDPKATESQL MQ
//
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