ID G0SFP1_CHATD Unreviewed; 1495 AA.
AC G0SFP1;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN ORFNames=CTHT_0071560 {ECO:0000313|EMBL:EGS17806.1};
OS Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)
OS (Thermochaetoides thermophila).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Thermochaetoides.
OX NCBI_TaxID=759272 {ECO:0000313|Proteomes:UP000008066};
RN [1] {ECO:0000313|EMBL:EGS17806.1, ECO:0000313|Proteomes:UP000008066}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1495 / CBS 144.50 / IMI 039719
RC {ECO:0000313|Proteomes:UP000008066};
RX PubMed=21784248; DOI=10.1016/j.cell.2011.06.039;
RA Amlacher S., Sarges P., Flemming D., van Noort V., Kunze R., Devos D.P.,
RA Arumugam M., Bork P., Hurt E.;
RT "Insight into structure and assembly of the nuclear pore complex by
RT utilizing the genome of a eukaryotic thermophile.";
RL Cell 146:277-289(2011).
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; GL988047; EGS17806.1; -; Genomic_DNA.
DR RefSeq; XP_006697424.1; XM_006697361.1.
DR STRING; 759272.G0SFP1; -.
DR GeneID; 18261194; -.
DR KEGG; cthr:CTHT_0071560; -.
DR eggNOG; KOG0970; Eukaryota.
DR HOGENOM; CLU_001718_1_0_1; -.
DR OMA; MTKMNVG; -.
DR OrthoDB; 211439at2759; -.
DR Proteomes; UP000008066; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
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; 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.
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 Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU000442};
KW Reference proteome {ECO:0000313|Proteomes:UP000008066};
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 11..75
FT /note="DNA polymerase alpha catalytic subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12254"
FT DOMAIN 414..725
FT /note="DNA-directed DNA polymerase family B exonuclease"
FT /evidence="ECO:0000259|Pfam:PF03104"
FT DOMAIN 793..1238
FT /note="DNA-directed DNA polymerase family B
FT multifunctional"
FT /evidence="ECO:0000259|Pfam:PF00136"
FT DOMAIN 1281..1486
FT /note="Zinc finger DNA-directed DNA polymerase family B
FT alpha"
FT /evidence="ECO:0000259|Pfam:PF08996"
FT REGION 58..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 151..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 276..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 830..852
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..118
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..176
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1495 AA; 169102 MW; 3203524A0ABD2AC3 CRC64;
MSNANKRNKF AELRALRQAG KKVFDTYQVA EVEDLYEEVD ENQYKKIVRA RLNQDDFVVD
DNGEGYVDDG REEWDHEEYY SDEDDEVSVR GKDRKNKKQR EQEQAKRDAS DRDITEYFTR
GAAKPQKKPK PVKTEEDEKF LADLLGEVDA NVPAPLPRIP KKRDRSAERR KVRALSPLPE
ARPPVAKRTK MLDGSASSPP AIHDAAMIED DGFIPSVESE PAAAPMSDIV MEEPELEPLP
SSPVSKVVQR RTQVKIEPDD DVDDLMEVAH AGAVTTTSVN LSGSRQARKI PKPEPHSVPA
SSSPVRPSEP EVDASAWNSI NQKLNVVSSS PTEAKTFGKI HYTDAIEEDG SLHFYWTDYT
ELNGSLCLFG KVLNKKKNHY VSCFVKVDNI LRKLYFLPRK YRMRNGVETD EPVEMMDVYN
EVDALMTKLG VDMHKIKPRK KKYAFELPGI PSEAEYLKLM YPYTKPQIEL GKTGETFSHV
FGTNTALFEQ FVLWRNIMGP CWLKIEDADF GALKNASHCR LEVLVSRPDS ISPIGDSEST
DAPPLTLMSV AIRTIFNARD NKQEILAISA RIYEDVLLND TTPADKLPCR TFTVIRPQGA
TFPIGFEKLA KERKKGLIKL MRQESDMLSF FLAQLDMVDP DVIIGHQLEG VDYSILLNRL
YERKTHQWSR LGRLRRSAWP ASIGKVGGNL FAERQIMAGR LLCDLANDAG KSVMYKCQSW
SLTEMCSMYL SGDDNRRRDI DNDAALKTWA TSKEGLMDYI SHAETDTYFI AALALRTQIL
PLTKILTNLA GNSWARTLTG TRAERNEFIL LHEFKKAGYI LPDKIPAKGR ARVDEENQDD
DGGEGGKKKD KYKGGLVFEP EKGLYDKYVL VMDFNSLYPS IIQEYNICFT TVDRSNLSDD
EDAVPAVPGK DRDQGILPRL LGKLVDRRRE VKKLMKTPRA TPEQLATWDI RQLALKLTAN
SMYGCLGYTK SRFYARPLAV LITYKGREIL RSTKALAESM SLQVIYGDTD SVMINANVDN
VLAAIEVGNK LKQEVNKLYK RLEIDIDNVF RRILLQAKKK YAAINMVEEN GRWVEKMEVK
GLDMRRREYC PLSREVSKRI LDEILSGDDT EVSVQRVHKY LREISAKMRE GAIPLNKYII
LTQLGKAPKE YPNADSMPQV QVALREMARG KVMRRGDVVS YIITTNKNNT SGSDSLPPAK
RAYTPQDVMK ADSGLVPDVE WYIGKQIMPP VERLCANIVG TSATQLAENL GLDPRHYANN
RSAAYNTADA ARDLEIHPLE SQIPDHIRFS NCARLTLRCR ACKHLFPFEG LLPLPASDAQ
QQKEAAEEQN KIITPSGIHC PSCSALLPTL TLVAQVETAV RAQTARYYET WLTCDDASCG
NRTRQMSVYG TRCLGPRGLA RDCLGRMRFE MGEREMYNQL VYFAGLWDVD KARKKVTEEK
SVSEEEKERV LALAEHNRER FGTVKGVVDK YLEKCGRQWV AMDTLFAKLG FMPTV
//
