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Database: UniProt
Entry: A0A1L0G652_9ASCO
LinkDB: A0A1L0G652_9ASCO
Original site: A0A1L0G652_9ASCO 
ID   A0A1L0G652_9ASCO        Unreviewed;       641 AA.
AC   A0A1L0G652;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=DNA polymerase alpha subunit B {ECO:0000256|ARBA:ARBA00018596, ECO:0000256|PIRNR:PIRNR018300};
GN   ORFNames=SAMEA4029010_CIC11G00000002665 {ECO:0000313|EMBL:SGZ52029.1};
OS   [Candida] intermedia.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Metschnikowiaceae; Metschnikowiaceae incertae sedis;
OC   Candida/Metschnikowiaceae.
OX   NCBI_TaxID=45354 {ECO:0000313|EMBL:SGZ52029.1, ECO:0000313|Proteomes:UP000182334};
RN   [1] {ECO:0000313|EMBL:SGZ52029.1, ECO:0000313|Proteomes:UP000182334}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 141442 {ECO:0000313|EMBL:SGZ52029.1,
RC   ECO:0000313|Proteomes:UP000182334};
RA   de Groot N.N.;
RL   Submitted (OCT-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; LT635758; SGZ52029.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1L0G652; -.
DR   STRING; 45354.A0A1L0G652; -.
DR   OrthoDB; 49016at2759; -.
DR   Proteomes; UP000182334; Chromosome iii.
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:UP000182334}.
FT   DOMAIN          18..217
FT                   /note="DNA polymerase alpha subunit B N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08418"
FT   DOMAIN          322..574
FT                   /note="DNA polymerase alpha/delta/epsilon subunit B"
FT                   /evidence="ECO:0000259|Pfam:PF04042"
FT   REGION          93..144
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        120..144
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   641 AA;  71386 MW;  20CD6FDBB2C66750 CRC64;
     MDGATKSWLI KKFGPSEDEV LTRLVTVQNL FNFSNEDIYI QWEAFVVTHE NGDADLSLVN
     IEKFQQYLQD LLANNHQKRT PAVKKVRDLS NKRPIDFSSS PGVVLPSTPS LKRKKPILTS
     EPDSSPSKKD VASSPIKAQS SNTVLETLNP DVEVDNIADN VQLTANFDPE KFKFRTMAMK
     LLESADVLDD QIDMFSQQLL TEYKDKDIQL GNPCMSSQFD IVCCGRIVPD SPFYDSMIVQ
     NLNDKSLFLE TSRLGGIGQR IPLDLSNLEE YSFFPGQVVG LRGRNPTGRA FVAHDVIALP
     QLGTPVSSGS ELSEFSKEGS KILIAAGPFT NQHTLDYSRL EKLVDHVNTE VKPQAVLLFG
     PFLDITNKAV ESGNVELPHT AANQQPKNLD ELFRAVVTPV LKKFDPSIQV VLLPSLKDSA
     SKHASYPQSS LDRKRLGLPK NFKCFPNPSN FSINEIMVGA SNADVFKDLK DIYKSGVSPE
     KSKLFSNRFE RIANHVFEQR RFYPVFPGSV KRVALPKEEG EKVTNLLDGM MGEELAETEV
     GGSSLEVPYI GVTELSHSLP DVLIVPSELK YFAKVIKGVV VINPGQFIRP NKDPLREDGS
     YVVMTTRGPD ANDENNIEPV EGSDLFYHNV FKRSRIDIMK T
//
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