ID A0A0F4YX10_TALEM Unreviewed; 669 AA.
AC A0A0F4YX10;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=DNA polymerase alpha subunit B {ECO:0000256|ARBA:ARBA00018596, ECO:0000256|PIRNR:PIRNR018300};
GN ORFNames=T310_3226 {ECO:0000313|EMBL:KKA22769.1};
OS Rasamsonia emersonii CBS 393.64.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Rasamsonia.
OX NCBI_TaxID=1408163 {ECO:0000313|EMBL:KKA22769.1, ECO:0000313|Proteomes:UP000053958};
RN [1] {ECO:0000313|EMBL:KKA22769.1, ECO:0000313|Proteomes:UP000053958}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 393.64 {ECO:0000313|EMBL:KKA22769.1,
RC ECO:0000313|Proteomes:UP000053958};
RA Heijne W.H., Fedorova N.D., Nierman W.C., Vollebregt A.W., Zhao Z., Wu L.,
RA Kumar M., Stam H., van den Berg M.A., Pel H.J.;
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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:KKA22769.1}.
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DR EMBL; LASV01000127; KKA22769.1; -; Genomic_DNA.
DR RefSeq; XP_013329381.1; XM_013473927.1.
DR AlphaFoldDB; A0A0F4YX10; -.
DR STRING; 1408163.A0A0F4YX10; -.
DR GeneID; 25315576; -.
DR OrthoDB; 49016at2759; -.
DR Proteomes; UP000053958; 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:UP000053958}.
FT DOMAIN 22..263
FT /note="DNA polymerase alpha subunit B N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08418"
FT DOMAIN 368..604
FT /note="DNA polymerase alpha/delta/epsilon subunit B"
FT /evidence="ECO:0000259|Pfam:PF04042"
FT REGION 73..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..90
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..138
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 669 AA; 73240 MW; B61085BC13B1B06F CRC64;
MEDVVHELNE LFASSAPDGL PQDVLAELQS ILRLHAISPQ ELFYKWESYS LKMGSDETKL
NLDTVRAFKR DVQESLERES RGKNSHLRST EKKGGVTATP RAMNTDVFGM LDELTPNTSH
SRSANKSVNG SAKRKSTFET PSAPKVGRPE KSGTPGDFKT PLKANGAVDG PQPVPFSERQ
NPGQVLETLN GHLAMPTAPM APYAEARIRP TANTDLKKLG YKPMAMRLSE ASEVLDDRID
EFTAVFQKHY GSEVTFGSAA TQSTSEIVAV GRIASDSLEG KLNTASLVLE TSRRTGAGLR
VPLKVDSLPS VQFFPGQIVA LRGINASGQY FSVKEVLPVP LLPPAASSPA TIDTINERLG
SDQQPLNIFI ASGPYTADDN LEFEPLNELC KKAADEYADA LILMGPFVDM EHPLIASGDF
DLPDVPGIDP DTANLTTLFR HCIAAPLQRL CAAVPSITIV LVPSVRDAVS KHVSWPQEQL
PRKELGLPKQ ARMVSNPVTL SLNETVIGML SHDVLYELRK EEALGGRPAE GNLLTRLPKY
IIEQRHFYPI FPPSSRESLP RASGADSVMP LGAMLDVSYL KLGEWWNVRP DVLITPSMLP
PFVKVVESVL VINPGTLSKR RAAGTYAQMA IHPRTMTAEE RQEKQLSHKI YERARVDVAV
SGNDSMKWE
//