ID A0A177C7Y0_9PLEO Unreviewed; 680 AA.
AC A0A177C7Y0;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=DNA polymerase alpha subunit B {ECO:0000256|ARBA:ARBA00018596, ECO:0000256|PIRNR:PIRNR018300};
GN ORFNames=CC84DRAFT_1151169 {ECO:0000313|EMBL:OAG02959.1};
OS Paraphaeosphaeria sporulosa.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Massarineae; Didymosphaeriaceae;
OC Paraphaeosphaeria.
OX NCBI_TaxID=1460663 {ECO:0000313|EMBL:OAG02959.1, ECO:0000313|Proteomes:UP000077069};
RN [1] {ECO:0000313|EMBL:OAG02959.1, ECO:0000313|Proteomes:UP000077069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AP3s5-JAC2a {ECO:0000313|EMBL:OAG02959.1,
RC ECO:0000313|Proteomes:UP000077069};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) 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}.
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DR EMBL; KV441555; OAG02959.1; -; Genomic_DNA.
DR RefSeq; XP_018033324.1; XM_018176732.1.
DR AlphaFoldDB; A0A177C7Y0; -.
DR STRING; 1460663.A0A177C7Y0; -.
DR GeneID; 28760218; -.
DR InParanoid; A0A177C7Y0; -.
DR OrthoDB; 49016at2759; -.
DR Proteomes; UP000077069; 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:UP000077069}.
FT DOMAIN 25..254
FT /note="DNA polymerase alpha subunit B N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08418"
FT DOMAIN 366..622
FT /note="DNA polymerase alpha/delta/epsilon subunit B"
FT /evidence="ECO:0000259|Pfam:PF04042"
FT REGION 72..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 123..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..89
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 680 AA; 74616 MW; 9057690B0F31824A CRC64;
MDDTAELTER FERYCATKDN DVPSEILNEL QSIQRIFSIS AEELDFKWQA YNMKMGGEEK
MDLKTARDFK KDLQDSLEKE SRGKVQQRGD AKRVAPTPRA AKGGDMYDML DGMIATPRAA
PLGSAAKRRS NFDAPAGKAH KNHEMSSPAG GQTPRGEVGD ASVFDFSSRK NAGDIAEQLN
GHIALSDAPE EPPSETRIKL KANTDMSKFN YKTMAMKLSE ASEVLDDRID EFRQLLQEHL
DLEDSAFGNP SYQSPNEVIA VGRICSDTSE GKLNAASIVL EGSRRWGSGR RVPLTLDKLT
SYNFFPGQIV ALRGINASGE NFVVSEVLSF PLLTQPASTP AELDTYNARY LDTPESDPST
VRPLTVLIAS GPYTTDQNLD FAPLHTFLDN AVSASADTIV LIGPFLDAEH PLIRSGDFDI
PPHLTSPDQA TMTDLFRHFI SAPIQTFTSR LPTCNVILVP SLRDAHHHHA AFPQDKFAKK
ELGLGAAGRH VQCVTNPMTL SMNEFIVGMS SLDVLHMLQR EEIAGGKARS THLYERGAKN
VLEQRSFLPV FPPTGRDKLL APSAVEAAVF KEGVADGDTE EGPSPFLPLG TMVDTSYLKL
GEMLNVRPDV LLTPSVLQGF VKVVESVLVI NPGTLCKRRA AGTYARLVVR PADVSEEERQ
RGAAVAHKLW ERARVDIVKI
//
