ID A0A2V1C0K9_9HELO Unreviewed; 661 AA.
AC A0A2V1C0K9;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=DNA polymerase alpha subunit B {ECO:0000256|ARBA:ARBA00018596, ECO:0000256|PIRNR:PIRNR018300};
GN ORFNames=DL98DRAFT_229474 {ECO:0000313|EMBL:PVH79141.1};
OS Cadophora sp. DSE1049.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Helotiales incertae sedis; Cadophora.
OX NCBI_TaxID=1485229 {ECO:0000313|EMBL:PVH79141.1, ECO:0000313|Proteomes:UP000244409};
RN [1] {ECO:0000313|EMBL:PVH79141.1, ECO:0000313|Proteomes:UP000244409}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSE1049 {ECO:0000313|EMBL:PVH79141.1,
RC ECO:0000313|Proteomes:UP000244409};
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 -!- FUNCTION: Accessory subunit of the DNA polymerase alpha complex (also
CC known as the alpha DNA polymerase-primase complex) which plays an
CC essential role in the initiation of DNA synthesis.
CC {ECO:0000256|PIRNR:PIRNR018300}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|PIRNR:PIRNR018300}.
CC -!- SIMILARITY: Belongs to the DNA polymerase alpha subunit B family.
CC {ECO:0000256|ARBA:ARBA00007299, ECO:0000256|PIRNR:PIRNR018300}.
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DR EMBL; KZ804157; PVH79141.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V1C0K9; -.
DR STRING; 1485229.A0A2V1C0K9; -.
DR Proteomes; UP000244409; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR Gene3D; 3.60.21.60; -; 2.
DR InterPro; IPR007185; DNA_pol_a/d/e_bsu.
DR InterPro; IPR016722; DNA_pol_alpha_bsu.
DR InterPro; IPR013627; Pol_alpha_B_N.
DR PANTHER; PTHR23061; DNA POLYMERASE 2 ALPHA 70 KDA SUBUNIT; 1.
DR PANTHER; PTHR23061:SF12; DNA POLYMERASE ALPHA SUBUNIT B; 1.
DR Pfam; PF04042; DNA_pol_E_B; 1.
DR Pfam; PF08418; Pol_alpha_B_N; 1.
DR PIRSF; PIRSF018300; DNA_pol_alph_2; 1.
PE 3: Inferred from homology;
KW DNA replication {ECO:0000256|ARBA:ARBA00022705,
KW ECO:0000256|PIRNR:PIRNR018300}; Nucleus {ECO:0000256|PIRNR:PIRNR018300};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000244409}.
FT DOMAIN 22..255
FT /note="DNA polymerase alpha subunit B N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08418"
FT DOMAIN 369..604
FT /note="DNA polymerase alpha/delta/epsilon subunit B"
FT /evidence="ECO:0000259|Pfam:PF04042"
FT REGION 71..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 116..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..86
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 661 AA; 71800 MW; AC23D4BCD0DE33C2 CRC64;
MAEPTNSEIQ ERFESAGGNL EDDVLAELQS IMRLHSIDVE ELWYKWESYS MKMGSDDMKL
NIETARALKK DVQDGLERDN RSKQHLQSNK RAAATPRSAA TNGDVFGILD GLVPNTPRTG
SANRASAAKR KFETPSMSRV KAEPASSPPE FKTPYKPGEH AGVAVSFHDR KNAGQAVEVL
NDHIKISEPP MAPFSEPRIK LIANSDMKKL SYKPMAMKSS EASEILDDKI DEFMQLIQAH
HKLDDSDFGS AASQSTNEIV AVGRIASDSL TGKLNASSLV LETSRRMGAG LRIPLKVDSL
PGYQFFPGQI VAMKGINASG ENFAVREILE APFLPGAAST PAGLETHIQR LRGGPDTMDS
DTDPAPLSIL LGAGPYTADD NLDFEPLHAL CSQAADSYAD ALILTGPFLD IDHPLIATGD
FDLPEEAMTE PDTATMTTVF KYLISPAFIQ LVAANPHITI LLIPSVKDVI NKHVSWPQEP
FPRKDLGLPK SVKIIGNPMT LSLNEIAVGV SSQDILTELR SSEVIGGKPK ESSVLARLPT
YLIEQRNFFP LFPPVDRESL PKTGTASGIP TGAMLDTSYL KLGEMINVRP DILIVPSALP
PFAKVVEGVL VVNPGYLSKR KAAGTYTKMT IMPASLTDED RGSSVLAHKV FERARVDIIR
I
//
