ID A0A371DGV1_9APHY Unreviewed; 414 AA.
AC A0A371DGV1;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, 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=OH76DRAFT_1554789 {ECO:0000313|EMBL:RDX51765.1};
OS Polyporus brumalis.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Polyporaceae; Polyporus.
OX NCBI_TaxID=139420 {ECO:0000313|EMBL:RDX51765.1, ECO:0000313|Proteomes:UP000256964};
RN [1] {ECO:0000313|EMBL:RDX51765.1, ECO:0000313|Proteomes:UP000256964}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRFM 1820 {ECO:0000313|EMBL:RDX51765.1,
RC ECO:0000313|Proteomes:UP000256964};
RX PubMed=30061923; DOI=10.1186/s13068-018-1198-5;
RA Miyauchi S., Rancon A., Drula E., Hage H., Chaduli D., Favel A., Grisel S.,
RA Henrissat B., Herpoel-Gimbert I., Ruiz-Duenas F.J., Chevret D., Hainaut M.,
RA Lin J., Wang M., Pangilinan J., Lipzen A., Lesage-Meessen L., Navarro D.,
RA Riley R., Grigoriev I.V., Zhou S., Raouche S., Rosso M.N.;
RT "Integrative visual omics of the white-rot fungus Polyporus brumalis
RT exposes the biotechnological potential of its oxidative enzymes for
RT delignifying raw plant biomass.";
RL Biotechnol. Biofuels 11:201-201(2018).
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; KZ857393; RDX51765.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A371DGV1; -.
DR STRING; 139420.A0A371DGV1; -.
DR Proteomes; UP000256964; 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:UP000256964};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003514}.
SQ SEQUENCE 414 AA; 47937 MW; D1BDC90338454B88 CRC64;
MAVPDAEPTT PDIMLAFYRR LYPFKSIFTW LNHEHAPTKL FTHREFAFTL QGDVYLRYNS
FSNADELKKQ VCTLNPTRFE IGPVYSARPR DKKTVRPAAF SPQLRELVFD IDMTDYDSIR
TCCSGADICK RCWTFISAAV RVLDRALRDQ FGYKHLLWVY SGRRGIHLWI SDREALELTD
EQRRALVGWL TVIQGGKEMH KKVNVRMGLK PLPPSIASAY KMLLPVFHDL ILEDQDCFAS
EEGWQALLHL IPDKDIVRSL EDKWEDDPKR SSEDKWQDVE DEIERKKGKG SAILNAAKED
IVLQYTYPRL DAEVSKHRNH LLKAPFCIHP KTGRVCVPVD PRTIDKFDPA RVPTVSQLLN
ELDKLALPQA GESAEHHADW ERTSLKPYVE MLDKHVMGLM EETRKSKQKM DLSW
//
