ID A0A074XWN6_AURPU Unreviewed; 502 AA.
AC A0A074XWN6;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 13-SEP-2023, entry version 28.
DE RecName: Full=DNA primase {ECO:0000256|RuleBase:RU003514};
DE EC=2.7.7.- {ECO:0000256|RuleBase:RU003514};
GN ORFNames=M438DRAFT_264201 {ECO:0000313|EMBL:KEQ90003.1};
OS Aureobasidium pullulans EXF-150.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX NCBI_TaxID=1043002 {ECO:0000313|EMBL:KEQ90003.1, ECO:0000313|Proteomes:UP000030706};
RN [1] {ECO:0000313|EMBL:KEQ90003.1, ECO:0000313|Proteomes:UP000030706}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EXF-150 {ECO:0000313|EMBL:KEQ90003.1,
RC ECO:0000313|Proteomes:UP000030706};
RX PubMed=24984952;
RA Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J., Zalar P.,
RA Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y., Lipzen A.,
RA Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT "Genome sequencing of four Aureobasidium pullulans varieties:
RT biotechnological potential, stress tolerance, and description of new
RT species.";
RL BMC Genomics 15:549-549(2014).
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; KL584974; KEQ90003.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A074XWN6; -.
DR STRING; 1043002.A0A074XWN6; -.
DR HOGENOM; CLU_028288_1_0_1; -.
DR OrthoDB; 168741at2759; -.
DR Proteomes; UP000030706; 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:UP000030706};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003514}.
FT REGION 1..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..69
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 502 AA; 57071 MW; 3EA6CD30297A4AF7 CRC64;
MPHAESPNPP SSPPVEDTVM SEAAPGALDE QAESQNETTQ SSPAPAVDEV EKASLEDMFD
DDDMDDDDEF SSSAQVKPQP SSQPEPKPGN SNVGKDAEVL RAFYQRLFPF KYLFQWLNHS
PTTTTDFSNR ELAFVLPNDA YIRYQSFNTA EDLRKQCIQL TPTRFEIGPV YSANPRDRKT
LRNASAFRPL AKELVFDIDM TDYDEIRTCC SGASICQKCW QFITMAIKVI DKALRDDFGF
KHIMWVYSGR RGAHAWISDK RAREMDDNKR RSIAGYLELL KGGDKTGKKV NLKRPLHPHI
DRSLKILNGY FQTDVLLEQD PWASPDKAAH LLQLLPDKNL TAALQRKWDS TPHRSSIQKW
ADIDAVASVS GSLSSLTPET LVHAKQDIRL EYTYPRLDAE VSKKLNHLLK SPFVIHPGTG
RVCVPIDIRR FEEFEPEKVP TVQQLLSEID SWQGNDDKIQ DWQKTSLKPY IELFRDHVNA
IMKDERAAEK RGREESGEGV DF
//
