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Database: UniProt
Entry: A0A318ZTN6_9EURO
LinkDB: A0A318ZTN6_9EURO
Original site: A0A318ZTN6_9EURO 
ID   A0A318ZTN6_9EURO        Unreviewed;       500 AA.
AC   A0A318ZTN6;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   28-JAN-2026, entry version 24.
DE   RecName: Full=DNA primase large subunit {ECO:0000256|PIRNR:PIRNR009449};
GN   ORFNames=BP01DRAFT_352572 {ECO:0000313|EMBL:PYH50034.1};
OS   Aspergillus saccharolyticus JOP 1030-1.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=1450539 {ECO:0000313|EMBL:PYH50034.1, ECO:0000313|Proteomes:UP000248349};
RN   [1] {ECO:0000313|EMBL:PYH50034.1, ECO:0000313|Proteomes:UP000248349}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JOP 1030-1 {ECO:0000313|EMBL:PYH50034.1,
RC   ECO:0000313|Proteomes:UP000248349};
RG   DOE Joint Genome Institute;
RA   Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA   Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA   Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA   Mortensen U.H., Andersen M.R., Baker S.E.;
RT   "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT   speciation.";
RL   Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: DNA primase is the polymerase that synthesizes small RNA
CC       primers for the Okazaki fragments made during discontinuous DNA
CC       replication. {ECO:0000256|PIRNR:PIRNR009449}.
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|PIRNR:PIRNR009449};
CC       Note=Binds 1 [4Fe-4S] cluster. {ECO:0000256|PIRNR:PIRNR009449};
CC   -!- SIMILARITY: Belongs to the eukaryotic-type primase large subunit
CC       family. {ECO:0000256|ARBA:ARBA00010564, ECO:0000256|PIRNR:PIRNR009449}.
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DR   EMBL; KZ821218; PYH50034.1; -; Genomic_DNA.
DR   RefSeq; XP_025436016.1; XM_025573974.1.
DR   AlphaFoldDB; A0A318ZTN6; -.
DR   STRING; 1450539.A0A318ZTN6; -.
DR   GeneID; 37075202; -.
DR   OrthoDB; 421393at2759; -.
DR   Proteomes; UP000248349; Unassembled WGS sequence.
DR   GO; GO:0005658; C:alpha DNA polymerase:primase complex; IEA:TreeGrafter.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006270; P:DNA replication initiation; IEA:TreeGrafter.
DR   GO; GO:0006269; P:DNA replication, synthesis of primer; IEA:UniProtKB-KW.
DR   CDD; cd07322; PriL_PriS_Eukaryotic; 1.
DR   FunFam; 1.20.930.80:FF:000003; DNA primase large subunit; 1.
DR   Gene3D; 1.20.930.80; -; 1.
DR   InterPro; IPR058560; DNA_primase_C.
DR   InterPro; IPR016558; DNA_primase_lsu_euk.
DR   InterPro; IPR007238; DNA_primase_lsu_euk/arc.
DR   PANTHER; PTHR10537; DNA PRIMASE LARGE SUBUNIT; 1.
DR   PANTHER; PTHR10537:SF3; DNA PRIMASE LARGE SUBUNIT; 1.
DR   Pfam; PF04104; DNA_primase_lrg; 1.
DR   Pfam; PF26466; DNA_primase_lrg_N; 1.
DR   PIRSF; PIRSF009449; DNA_primase_large_subunit; 1.
DR   SUPFAM; SSF140914; PriB N-terminal domain-like; 1.
PE   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|PIRNR:PIRNR009449};
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705,
KW   ECO:0000256|PIRNR:PIRNR009449};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PIRNR:PIRNR009449};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRNR:PIRNR009449};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|PIRNR:PIRNR009449};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRNR:PIRNR009449};
KW   Primosome {ECO:0000256|ARBA:ARBA00022515, ECO:0000256|PIRNR:PIRNR009449};
KW   Reference proteome {ECO:0000313|Proteomes:UP000248349}.
FT   DOMAIN          301..484
FT                   /note="DNA primase large subunit C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF04104"
FT   BINDING         307
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009449-1"
FT   BINDING         390
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009449-1"
FT   BINDING         407
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009449-1"
FT   BINDING         448
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR009449-1"
SQ   SEQUENCE   500 AA;  58398 MW;  4D268DFF1A617E23 CRC64;
     MIRGDFLRID PKRRANLDHK KKQFAAPTFK QQDYPHRLNF YDVPPTEEIT LEQFEQWAID
     RLRVLAEIEA CSYRNKSAAE TEAHLTPLLQ KYLPLSSNTS SSHGAADQRL KNERQKDHYS
     HFILRLAFSA TEDLRRRFVR AETMLFRFRF QRDDTREKRA FIESLNLDWE PVENEERQRL
     AENLVNATPG LRRVDEEAWY KVDWERVPEL VERRAVYLYK GKAYVPGREQ LSMIIAEFTA
     RLERALELTS RALPRLDEDD RLTPILNHLS KNFGSAESVY SEGEGFVDGA AITAGNIDQL
     SQHFPLCMRS LHMNLRKNNH LKHYGRLQYT LFLKGIGLSL EECIVFWRQS FKGFTDDEFN
     SRYKYNIRHA YGDVGGDVNR RGRGYPPYSC QKILGDSNPG VGQTHGCPYR HYSIDNLIGL
     LQSTGVHDKE VLRGVREDVE KMRYHIACNR VFESTHKTEI KRVKEDGSWN QTDLDTIVHP
     NTYFKRSFLL KQTARASKNS
//
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