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Database: UniProt
Entry: A0A0M6XST8_9RHOB
LinkDB: A0A0M6XST8_9RHOB
Original site: A0A0M6XST8_9RHOB 
ID   A0A0M6XST8_9RHOB        Unreviewed;       648 AA.
AC   A0A0M6XST8;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   31-JUL-2019, entry version 19.
DE   RecName: Full=DNA primase {ECO:0000256|HAMAP-Rule:MF_00974, ECO:0000256|SAAS:SAAS00993443};
DE            EC=2.7.7.- {ECO:0000256|HAMAP-Rule:MF_00974, ECO:0000256|SAAS:SAAS00993444};
GN   Name=dnaG {ECO:0000256|HAMAP-Rule:MF_00974,
GN   ECO:0000313|EMBL:CTQ33878.1};
GN   ORFNames=JAN5088_02664 {ECO:0000313|EMBL:CTQ33878.1};
OS   Jannaschia rubra.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Jannaschia.
OX   NCBI_TaxID=282197 {ECO:0000313|EMBL:CTQ33878.1, ECO:0000313|Proteomes:UP000048908};
RN   [1] {ECO:0000313|EMBL:CTQ33878.1, ECO:0000313|Proteomes:UP000048908}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 5088 {ECO:0000313|EMBL:CTQ33878.1,
RC   ECO:0000313|Proteomes:UP000048908};
RA   Noorani M.;
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: RNA polymerase that catalyzes the synthesis of short RNA
CC       molecules used as primers for DNA polymerase during DNA
CC       replication. {ECO:0000256|HAMAP-Rule:MF_00974,
CC       ECO:0000256|SAAS:SAAS00709340}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|SAAS:SAAS00709317};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00974};
CC       Note=Binds 1 zinc ion per monomer. {ECO:0000256|HAMAP-
CC       Rule:MF_00974};
CC   -!- SUBUNIT: Monomer. Interacts with DnaB. {ECO:0000256|HAMAP-
CC       Rule:MF_00974}.
CC   -!- DOMAIN: Contains an N-terminal zinc-binding domain, a central core
CC       domain that contains the primase activity, and a C-terminal DnaB-
CC       binding domain. {ECO:0000256|HAMAP-Rule:MF_00974}.
CC   -!- SIMILARITY: Belongs to the DnaG primase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00974, ECO:0000256|SAAS:SAAS00709351}.
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DR   EMBL; CXPG01000020; CTQ33878.1; -; Genomic_DNA.
DR   RefSeq; WP_055683232.1; NZ_FOOS01000002.1.
DR   EnsemblBacteria; CTQ33878; CTQ33878; JAN5088_02664.
DR   OrthoDB; 1071997at2; -.
DR   Proteomes; UP000048908; Unassembled WGS sequence.
DR   GO; GO:1990077; C:primosome complex; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003896; F:DNA primase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   CDD; cd03364; TOPRIM_DnaG_primases; 1.
DR   Gene3D; 3.90.580.10; -; 1.
DR   Gene3D; 3.90.980.10; -; 1.
DR   HAMAP; MF_00974; DNA_primase_DnaG; 1.
DR   InterPro; IPR013264; DNA_primase_core_N.
DR   InterPro; IPR037068; DNA_primase_core_N_sf.
DR   InterPro; IPR019475; DNA_primase_DnaB-bd.
DR   InterPro; IPR006295; DNA_primase_DnaG.
DR   InterPro; IPR036977; DNA_primase_Znf_CHC2.
DR   InterPro; IPR030846; DnaG_bac.
DR   InterPro; IPR034151; TOPRIM_DnaG_bac.
DR   InterPro; IPR006171; TOPRIM_domain.
DR   InterPro; IPR002694; Znf_CHC2.
DR   Pfam; PF10410; DnaB_bind; 1.
DR   Pfam; PF13662; Toprim_4; 1.
DR   Pfam; PF08275; Toprim_N; 1.
DR   Pfam; PF01807; zf-CHC2; 1.
DR   SMART; SM00493; TOPRIM; 1.
DR   SMART; SM00400; ZnF_CHCC; 1.
DR   TIGRFAMs; TIGR01391; dnaG; 1.
DR   PROSITE; PS50880; TOPRIM; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000048908};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|SAAS:SAAS00993445};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|SAAS:SAAS00709369};
KW   DNA-directed RNA polymerase {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|SAAS:SAAS00709327};
KW   Magnesium {ECO:0000256|SAAS:SAAS00709345};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|SAAS:SAAS00709338};
KW   Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|SAAS:SAAS00709339, ECO:0000313|EMBL:CTQ33878.1};
KW   Primosome {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|SAAS:SAAS00709304};
KW   Reference proteome {ECO:0000313|Proteomes:UP000048908};
KW   Transcription {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|SAAS:SAAS00709341};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|SAAS:SAAS00993442, ECO:0000313|EMBL:CTQ33878.1};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00974, ECO:0000256|SAAS:SAAS00709300};
KW   Zinc-finger {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|SAAS:SAAS00709301}.
FT   DOMAIN      262    343       Toprim. {ECO:0000259|PROSITE:PS50880}.
FT   ZN_FING      43     67       CHC2-type. {ECO:0000256|HAMAP-Rule:
FT                                MF_00974}.
FT   REGION      430    464       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   REGION      603    630       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS    442    462       Pro-rich. {ECO:0000256|SAM:MobiDB-lite}.
FT   COMPBIAS    603    623       Polyampholyte. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
SQ   SEQUENCE   648 AA;  71648 MW;  14928845A4565C35 CRC64;
     MRLPDSFLDD LRNRLSLSQV VGRRVTWDMK KTNQAKGDWW APCPFHQEKS PSFHVDDRKG
     FYYCFGCQAK GNVFGFVQET ENVGFMEAVE ILAAEAGMPM PARDPRAAEK ADLRTRLAEV
     TEQAVAWFRL QLKTGAAAEA RAYLDRRGLT PATLDRFEIG FAPDTSDAFV SAMADRGVPF
     DLLEGAGLAV PPEDGRPARD RFIHRIVFPI RDPRGRCIGF GGRAMNPNAK AKYLNSPETA
     LFDKGSNLYN LGPARAAAGK GQKLVVAEGY MDVIALAQAG FDAAVAPLGT AVTERQLQML
     WRVTPEPLIA LDGDAAGQRA GLRVADLALP LIEAGQSLRF AVLPEGQDPD DLIRARGAAA
     MQAVLDEARP MLSLLWQREV EGKSFDSPER RAMLDRDLRA LLHRIKDPML RRHYGEEIAR
     LRADLFGTPL NARQDDRPFQ PRPRTPWVPG RRWQPPPAPP SVTARASALA SGTSDPDLLL
     EQVALAGFVR HPSLIAEFAH DLETVPWTGG HGRLAAALLS LDPGGDMRAA IDAELGPQPL
     ETLFAQRHLG ISPVTRADAN GARHCIRDAL DRLDARRGAD RERREAIEDF DESADEAMTW
     RLAQASRRRE ETQRARRDED MGSDDDVGLS DYLQGLLDTK VWEKTKKK
//
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