ID A0A2T4BK17_9HYPO Unreviewed; 660 AA.
AC A0A2T4BK17;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=DNA polymerase alpha subunit B {ECO:0000256|ARBA:ARBA00018596, ECO:0000256|PIRNR:PIRNR018300};
GN ORFNames=BBK36DRAFT_150702 {ECO:0000313|EMBL:PTB69648.1};
OS Trichoderma citrinoviride.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=58853 {ECO:0000313|EMBL:PTB69648.1, ECO:0000313|Proteomes:UP000241546};
RN [1] {ECO:0000313|Proteomes:UP000241546}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TUCIM 6016 {ECO:0000313|Proteomes:UP000241546};
RG DOE Joint Genome Institute;
RA Atanasova L., Chenthamara K., Zhang J., Grujic M., Henrissat B., Kuo A.,
RA Aerts A., Salamov A., Lipzen A., Labutti K., Barry K., Miao Y.,
RA Rahimi M.J., Shen Q., Grigoriev I.V., Kubicek C.P., Druzhinina I.S.;
RT "Multiple horizontal gene transfer events from other fungi enriched the
RT ability of initially mycotrophic Trichoderma (Ascomycota) to feed on dead
RT plant biomass.";
RL Submitted (JUL-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; KZ680208; PTB69648.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T4BK17; -.
DR OrthoDB; 49016at2759; -.
DR Proteomes; UP000241546; 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:UP000241546}.
FT DOMAIN 18..256
FT /note="DNA polymerase alpha subunit B N-terminal"
FT /evidence="ECO:0000259|Pfam:PF08418"
FT DOMAIN 370..604
FT /note="DNA polymerase alpha/delta/epsilon subunit B"
FT /evidence="ECO:0000259|Pfam:PF04042"
FT REGION 72..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..91
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..133
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 660 AA; 71872 MW; 223A2B649FF980B5 CRC64;
MAADEMQSRF APNGALEPDV LGELQSMARL HDISAEDLYF KWESYCIKMD ADAQAVTLDG
VRGLKQSIQD ELEKSQRRVQ LKSERKSAPT PRPKAGGRGG GDVFGMLDGL VPSTPGSGAR
LLNSSSKTPG SGGQQLRRRM EMQRDIPSSP AAGLNEQLKS MQLPATSFAD RQNAGDVVEI
LNEELPPAEA PIAPFPEPRI KLTAASDQKK TGYKPLAMKL SEASEILDDR IDDFIDLVRE
HHNLEDSAFG NAATASTTEV VAVGRIASDS LEGKINAASI VLETSRRTGR GLRVPLNLDA
VRIWSFFPGQ IVALRGSNIT GDEFIVKEIL ELPLLPSAAS SRAALEAHRE KLRGDPDAMD
SDSEPAPLNI IYAAGPYTAD DNLDYEPLQA LCNQAADTYA DALVLTGPFL DIDHPLIATG
DFDLPEEASY DPDTANMNTV FKHLVAPALN RLASANPHLT VILVPSVRDV LNKHVSWPQD
TIPRRELGLP KSVRIVSNPM TLSMNEVVVG LSSQDVLYEL RSEEVSRGAP AGDLMRRLSR
HLIEQRHFFP VFPPTDRSRL PRTGTEEGLA TGAMLDVSYL KLGEMVSTRP DVLLMPSSLP
PFAKVVESVL AINPGSLSKR RGPGTYARMT LYPPPLDGEV IDGLISHRVF DRARVEIVRI
//