ID W6MIY5_9ASCO Unreviewed; 433 AA.
AC W6MIY5;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-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=KUCA_T00002117001 {ECO:0000313|EMBL:CDK26146.1};
OS Kuraishia capsulata CBS 1993.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetales incertae sedis; Kuraishia.
OX NCBI_TaxID=1382522 {ECO:0000313|EMBL:CDK26146.1};
RN [1] {ECO:0000313|EMBL:CDK26146.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CBS 1993 {ECO:0000313|EMBL:CDK26146.1};
RA Genoscope - CEA;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDK26146.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CBS 1993 {ECO:0000313|EMBL:CDK26146.1};
RA Morales L., Noel B., Porcel B., Marcet-Houben M., Hullo M-F., Sacerdot C.,
RA Tekaia F., Leh-Louis V., Despons L., Khanna V., Aury J-M., Barbe V.,
RA Couloux A., Labadie K., Pelletier E., Souciet J-L., Boekhout T.,
RA Gabaldon T., Wincker P., Dujon B.;
RT "Complete DNA sequence of /Kuraishia capsulata/ illustrates novel genomic
RT features among budding yeasts (/Saccharomycotina/).";
RL Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
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; HG793126; CDK26146.1; -; Genomic_DNA.
DR AlphaFoldDB; W6MIY5; -.
DR STRING; 1382522.W6MIY5; -.
DR HOGENOM; CLU_028288_1_0_1; -.
DR OrthoDB; 168741at2759; -.
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 Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003514}.
SQ SEQUENCE 433 AA; 50107 MW; 92E87BE633D94347 CRC64;
MTLEDVTNIE QEAGKLAGKP QETVTSVANV SDQPASSRIT QADFEEYYKH FLPFKSIYAW
LNHSPLPNLK FGHREFAMEH FNTQYQRYCC FTSSNEFKDA IVKASPSRFE VGAIYNENLK
NKIKGQKSAN LKPVEKELNF DIDLTDYDDI RTCCAKTDIC LKCWKFINLA VNIMDVTLRE
DFGFENLIWV FSGRRGVHCW VSDPRARVLD ESKRRSIIEY VMLKSGKNGS DKLSLRKPYH
PLVERALKMC TKSFQEIIME DQDPWRDDEK AITHLAKTFP DSKLKDALTS KWKAQPGRSS
LQKWKDVDEL IEKGQYVSSR TIAGLNQDWK REIILSCLYP KLDIEVSRQL NHLLKSPFCI
HPKTGNVCVP FDPKDGDFDP LSGPTLQKLF EERSEGRESC LKPYVEIFDR FVQGLNKEEL
AKRKTENKEN LDF
//