ID A0A372QB81_9GLOM Unreviewed; 969 AA.
AC A0A372QB81;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=DNA polymerase {ECO:0000256|RuleBase:RU000442};
DE EC=2.7.7.7 {ECO:0000256|RuleBase:RU000442};
GN ORFNames=C1646_771967 {ECO:0000313|EMBL:RGB25281.1};
OS Rhizophagus sp. MUCL 43196.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC Glomeromycetes; Glomerales; Glomeraceae; Rhizophagus.
OX NCBI_TaxID=1803374 {ECO:0000313|EMBL:RGB25281.1, ECO:0000313|Proteomes:UP000263633};
RN [1] {ECO:0000313|EMBL:RGB25281.1, ECO:0000313|Proteomes:UP000263633}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MUCL 43196 {ECO:0000313|EMBL:RGB25281.1,
RC ECO:0000313|Proteomes:UP000263633};
RA Morin E., San Clemente H., Chen E.C.H., De La Providencia I., Hainaut M.,
RA Kuo A., Kohler A., Murat C., Tang N., Roy S., Loubradou J., Henrissat B.,
RA Grigoriev I.V., Corradi N., Roux C., Martin F.M.;
RT "Comparative genomics reveals the genomic features of Rhizophagus
RT irregularis, R. cerebriforme, R. diaphanum and Gigaspora rosea, and their
RT symbiotic lifestyle signature.";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00024632,
CC ECO:0000256|RuleBase:RU000442};
CC -!- SIMILARITY: Belongs to the DNA polymerase type-B family.
CC {ECO:0000256|ARBA:ARBA00005755, ECO:0000256|RuleBase:RU000442}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RGB25281.1}.
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DR EMBL; QKKE01000725; RGB25281.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A372QB81; -.
DR STRING; 1803374.A0A372QB81; -.
DR InParanoid; A0A372QB81; -.
DR Proteomes; UP000263633; Unassembled WGS sequence.
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:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR Gene3D; 1.10.132.60; DNA polymerase family B, C-terminal domain; 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; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR PANTHER; PTHR10322; DNA POLYMERASE CATALYTIC SUBUNIT; 1.
DR PANTHER; PTHR10322:SF23; DNA POLYMERASE DELTA CATALYTIC SUBUNIT; 1.
DR Pfam; PF00136; DNA_pol_B; 2.
DR Pfam; PF03104; DNA_pol_B_exo1; 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|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU000442};
KW DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932,
KW ECO:0000256|RuleBase:RU000442};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000256|RuleBase:RU000442};
KW Reference proteome {ECO:0000313|Proteomes:UP000263633};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000442}.
FT DOMAIN 214..298
FT /note="DNA-directed DNA polymerase family B exonuclease"
FT /evidence="ECO:0000259|Pfam:PF03104"
FT DOMAIN 355..547
FT /note="DNA-directed DNA polymerase family B
FT multifunctional"
FT /evidence="ECO:0000259|Pfam:PF00136"
FT DOMAIN 601..793
FT /note="DNA-directed DNA polymerase family B
FT multifunctional"
FT /evidence="ECO:0000259|Pfam:PF00136"
FT REGION 820..850
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 827..849
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 969 AA; 112182 MW; 6554B5EAF6C32D35 CRC64;
MHTPTNFDQT DRTRTLACYD GASPLTGILS RNDIVAEFNN GMTAILQQSL SGKQPIHFMP
TEVIPEEMPL STFKTRLVNI LSNTLKGTSK FGIENISAFP LQGYHIEKKL SSDDLTPIYY
YRKVACEERL PLSSWAVLTN YSYTLSENGY LFRVSMGNYS SISDEDYNNP LISSALSDES
NVFMICMTVH WKDDPNPLKQ ICLVDVETAP DPPPDIEVGF NISQYDWRFI VKKAKKLGVL
EWMFNQMSLK PSSLEKITKW QYQYNAIKVN DIPFHSKHLK IPGCVAIDVR PCFMKFYSKA
EKSSLAFYLN ECGLESKLDM PFNHMFKYYR NALKEADATT AKQMREIAEY WMKVSNLLSA
SAWRKGILTS TISERTETEL FPGAYVYPPI KGLENRRPIT GLDFASLYLS LIMTYNLSPD
KIILSRKHAE SPRDKKGLYA IMLEYLYYKW IEVKKRLALL KDKKEDMELV IGLMGKGLSL
PEAIEQVLAN VEGKKRVSLT KNLYHFINKA RYEFMAEYDS ICFDYSCLDA EQNALKVYMN
TFYGTAGDNF VKSKGFQIKY GDTDSLYLVP PERCFQKCNE AYDNGNGISK EEYWSRMVNV
SMEVMEKLRD EVNNFLRKDN GSSYLKMAYE KVLFPVVFTG KKKYYGIPHE RKRIMDESMR
VNNTHTLHQI VEDMLKGTVK DISQTDLNEI IKTAVWRPDK NNKSVQRFIS RMRDRHTREE
ADAKRLIKRG LTPEPYLYEI PELGERFEYV VVENDSSDKV RDKMEYPEVV RRLDKKIDIS
YYLKPVVTLC ARFINYDERY QPSSEIVLGG LKKFKDGNKV EDNKADDGGI DEDDLDDDEE
DEDEMDEDEV SKIRDSLAQK SAERARIYAK KLFDITYADK GERLTNNAYY HSFLNALDKQ
EESIRLKLSS LLKEISEVNI EYRDSMYKLV TKKRAMSLEQ YLTSYCLMSN DKKDDSSGAD
IDEIIELYS
//
