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Database: UniProt
Entry: A0A420I0I1_9PEZI
LinkDB: A0A420I0I1_9PEZI
Original site: A0A420I0I1_9PEZI 
ID   A0A420I0I1_9PEZI        Unreviewed;       472 AA.
AC   A0A420I0I1;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   13-SEP-2023, entry version 12.
DE   RecName: Full=DNA primase {ECO:0000256|RuleBase:RU003514};
DE            EC=2.7.7.- {ECO:0000256|RuleBase:RU003514};
GN   ORFNames=OnM2_027047 {ECO:0000313|EMBL:RKF63173.1};
OS   Erysiphe neolycopersici.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Erysiphales; Erysiphaceae; Erysiphe.
OX   NCBI_TaxID=212602 {ECO:0000313|EMBL:RKF63173.1, ECO:0000313|Proteomes:UP000286134};
RN   [1] {ECO:0000313|EMBL:RKF63173.1, ECO:0000313|Proteomes:UP000286134}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UMSG2 {ECO:0000313|EMBL:RKF63173.1};
RX   PubMed=30253736; DOI=10.1186/s12864-018-5069-z;
RA   Wu Y., Ma X., Pan Z., Kale S.D., Song Y., King H., Zhang Q., Presley C.,
RA   Deng X., Wei C.I., Xiao S.;
RT   "Comparative genome analyses reveal sequence features reflecting distinct
RT   modes of host-adaptation between dicot and monocot powdery mildew.";
RL   BMC Genomics 19:705-705(2018).
CC   -!- SIMILARITY: Belongs to the eukaryotic-type primase small subunit
CC       family. {ECO:0000256|ARBA:ARBA00009762, ECO:0000256|RuleBase:RU003514}.
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:RKF63173.1}.
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DR   EMBL; MCFK01002753; RKF63173.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A420I0I1; -.
DR   STRING; 212602.A0A420I0I1; -.
DR   Proteomes; UP000286134; 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:UP000286134};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003514}.
FT   REGION          1..46
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   472 AA;  54513 MW;  AE2CC90603955042 CRC64;
     MNASSMECVE GESALNHGQE SKTNLEDLFP DNESEDEYGS GNDNQKAKEL RTVLTPQALD
     PEVLRSYYQR LFPWRHLFQW LNHSPVPSND FGHREFAFTL PNDAYLRYQS FPTSDVIRKD
     ILRLNPTRFE IGPVYSTNPR DRKSLTKSSS FKPISKELCF DIDLTDYDDI RTCCSKVSIC
     QKCWQFITMA IKVIDVALRE DFGFKHIMWV YSGRRGAHAW VCDKRARNLN DQKRKAIAGY
     LMVIKGGIQS GKRVDLKRPL HPHVMRSLNV LKAHFQNDIL QDQDPWETDE KFERLLQLIP
     DQNLKSALLK KWSSSPGRTS IAKWADIDSL AKSGVSKTLD ATALLEAKQD IVLEYTYPRL
     DIEVTKHLNH LLKSPFVVHP GTGRVCVPID AKKCEDFDPL AVPTVVELLR EIDEWKDDGK
     SDEKASNSAH DWDKTRLKPY IEHFRSFVIL LLKDEKDTVI KRERDENEDI KF
//
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