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Database: UniProt
Entry: A0A061H3R6_9BASI
LinkDB: A0A061H3R6_9BASI
Original site: A0A061H3R6_9BASI 
ID   A0A061H3R6_9BASI        Unreviewed;       527 AA.
AC   A0A061H3R6;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   13-SEP-2023, entry version 37.
DE   RecName: Full=DNA primase {ECO:0000256|RuleBase:RU003514};
DE            EC=2.7.7.- {ECO:0000256|RuleBase:RU003514};
GN   ORFNames=PFL1_05620 {ECO:0000313|EMBL:EPQ26984.1};
OS   Pseudozyma flocculosa PF-1.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Pseudozyma.
OX   NCBI_TaxID=1277687 {ECO:0000313|EMBL:EPQ26984.1, ECO:0000313|Proteomes:UP000053664};
RN   [1] {ECO:0000313|EMBL:EPQ26984.1, ECO:0000313|Proteomes:UP000053664}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PF-1 {ECO:0000313|EMBL:EPQ26984.1,
RC   ECO:0000313|Proteomes:UP000053664};
RX   PubMed=23800965; DOI=10.1105/tpc.113.113969;
RA   Lefebvre F., Joly D.L., Labbe C., Teichmann B., Linning R., Belzile F.,
RA   Bakkeren G., Belanger R.R.;
RT   "The transition from a phytopathogenic smut ancestor to an anamorphic
RT   biocontrol agent deciphered by comparative whole-genome analysis.";
RL   Plant Cell 25:1946-1959(2013).
CC   -!- SIMILARITY: Belongs to the eukaryotic-type primase small subunit
CC       family. {ECO:0000256|ARBA:ARBA00009762, ECO:0000256|RuleBase:RU003514}.
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DR   EMBL; KE361642; EPQ26984.1; -; Genomic_DNA.
DR   RefSeq; XP_007881345.1; XM_007883154.1.
DR   AlphaFoldDB; A0A061H3R6; -.
DR   GeneID; 19319708; -.
DR   KEGG; pfp:PFL1_05620; -.
DR   eggNOG; KOG2851; Eukaryota.
DR   HOGENOM; CLU_028288_1_0_1; -.
DR   OrthoDB; 168741at2759; -.
DR   Proteomes; UP000053664; Unassembled WGS sequence.
DR   GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR   GO; GO:0003896; F:DNA primase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd04860; AE_Prim_S; 1.
DR   Gene3D; 3.90.920.10; DNA primase, PRIM domain; 1.
DR   InterPro; IPR002755; DNA_primase_S.
DR   InterPro; IPR014052; DNA_primase_ssu_euk/arc.
DR   NCBIfam; TIGR00335; primase_sml; 1.
DR   PANTHER; PTHR10536; DNA PRIMASE SMALL SUBUNIT; 1.
DR   PANTHER; PTHR10536:SF0; DNA PRIMASE SMALL SUBUNIT; 1.
DR   Pfam; PF01896; DNA_primase_S; 1.
DR   SUPFAM; SSF56747; Prim-pol domain; 1.
PE   3: Inferred from homology;
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705,
KW   ECO:0000256|RuleBase:RU003514};
KW   DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478,
KW   ECO:0000256|RuleBase:RU003514};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW   Primosome {ECO:0000256|ARBA:ARBA00022515, ECO:0000256|RuleBase:RU003514};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053664};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003514}.
FT   REGION          10..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          436..492
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   527 AA;  59011 MW;  581161339E469995 CRC64;
     MAAVAAAAAA ATATVPAALP AARPPPPDMD VDLDLEDENS QELERAISAI DERQIDARDS
     SDPMSMRLFY RRLLPWKQLF TWLNQDLPHL PGRNWTHREF AFTLQNDAYL RYNSFANADE
     LKNQVCRLNP SRFEIGPVYS AKPKDRKTVQ KASFRPVYRE LVLDIDMTDY DEVRTCCSGK
     GICRRCWAFI AVAVDVLDEA LRTDFGFRHL LWVYSGRRGI HCWVSDKAAC ELGDDARKAI
     VGWLEVVKGS ANQVKKVDAG FTPGSATRSL HPSLRRAIGG EGPASGPLKL AFVDTVLKDQ
     DCFRRREHWE VLLQLLPSGE SEAVERLRAK WERSPNRSSL DKWGDVMEAA HKSGEVRSAK
     VWKPCLEDVI LQYTYPRIDA EVSKHLNHLL KSPFVVHPAT GKVCVPIDPR KVHEFDPETS
     CPTVAQLLRE LNSWEAKHGG GDSKASPPPP QSNMSSRYAT RRRPAAGGER KAPASVAPAA
     SSSTTAAARA DWEKTSLRPF VELFERHCNA IAKESRQARQ QRFSTDF
//
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