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Database: UniProt
Entry: S7Z9A9_PENO1
LinkDB: S7Z9A9_PENO1
Original site: S7Z9A9_PENO1 
ID   S7Z9A9_PENO1            Unreviewed;       508 AA.
AC   S7Z9A9;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   13-SEP-2023, entry version 30.
DE   RecName: Full=DNA primase {ECO:0000256|RuleBase:RU003514};
DE            EC=2.7.7.- {ECO:0000256|RuleBase:RU003514};
GN   ORFNames=PDE_01738 {ECO:0000313|EMBL:EPS26799.1};
OS   Penicillium oxalicum (strain 114-2 / CGMCC 5302) (Penicillium decumbens).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=933388 {ECO:0000313|EMBL:EPS26799.1, ECO:0000313|Proteomes:UP000019376};
RN   [1] {ECO:0000313|EMBL:EPS26799.1, ECO:0000313|Proteomes:UP000019376}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=114-2 / CGMCC 5302 {ECO:0000313|Proteomes:UP000019376};
RX   PubMed=23383313; DOI=10.1371/journal.pone.0055185;
RA   Liu G., Zhang L., Wei X., Zou G., Qin Y., Ma L., Li J., Zheng H., Wang S.,
RA   Wang C., Xun L., Zhao G.-P., Zhou Z., Qu Y.;
RT   "Genomic and secretomic analyses reveal unique features of the
RT   lignocellulolytic enzyme system of Penicillium decumbens.";
RL   PLoS ONE 8:E55185-E55185(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; KB644409; EPS26799.1; -; Genomic_DNA.
DR   AlphaFoldDB; S7Z9A9; -.
DR   STRING; 933388.S7Z9A9; -.
DR   eggNOG; KOG2851; Eukaryota.
DR   HOGENOM; CLU_028288_1_0_1; -.
DR   OrthoDB; 168741at2759; -.
DR   PhylomeDB; S7Z9A9; -.
DR   Proteomes; UP000019376; 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:UP000019376};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003514}.
FT   REGION          1..69
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          487..508
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..33
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   508 AA;  57215 MW;  6844482EBF7E50F5 CRC64;
     MPHSVSPKSP RGDDEELPDA PSVGEKEVSG VKLEDMFDDE DDDFPASSAQ DVKMESSPAP
     APASAPTAAP AGVDTDVMLA FYQRLFPFRY LFQWLNHGVV PTKDFGNREF ALTLQNDAYL
     RYQSYPTADL FRKDILKMNP SRFEIGPVYS TNPRDRKTLR GGQMKPVSKE LVFDIDMTDY
     DDIRTCCQKA NICHKCWAFV TMAIKVIDSA LREDFGFEHI LWVYSGRRGA HAWVCDARAR
     NLPDDRRRAI AGYLEILRGG SQSGKRVNIR RPLHPHINRS LDILKTYFAQ TTLKDQNTFA
     SAEQAEKLLG LLPDKTLNES LKRKWDSSPD RPSTSKWADI DALAKTGKSN TLNTSALRDA
     KQDIVLEYTY PRLDAEVSKK MIHLLKSPFV IHPGTGRICV PIDPHKAEEF DPLSVPTVME
     LLGEIDAYDA KHPPVGSEDG AVPEIEGSMP NGSDMRGARK IQDYEKTSLK PYIEFFRSFI
     ANLLKEERAG KRERDETAPP LKADPMEF
//
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