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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//