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Database: UniProt
Entry: A0A1T4XAA5_9CLOT
LinkDB: A0A1T4XAA5_9CLOT
Original site: A0A1T4XAA5_9CLOT 
ID   A0A1T4XAA5_9CLOT        Unreviewed;       594 AA.
AC   A0A1T4XAA5;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=DNA primase {ECO:0000256|HAMAP-Rule:MF_00974, ECO:0000256|PIRNR:PIRNR002811};
DE            EC=2.7.7.101 {ECO:0000256|HAMAP-Rule:MF_00974};
GN   Name=dnaG {ECO:0000256|HAMAP-Rule:MF_00974};
GN   ORFNames=SAMN05443428_10728 {ECO:0000313|EMBL:SKA86028.1};
OS   Caloramator quimbayensis.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Caloramator.
OX   NCBI_TaxID=1147123 {ECO:0000313|EMBL:SKA86028.1, ECO:0000313|Proteomes:UP000190105};
RN   [1] {ECO:0000313|EMBL:SKA86028.1, ECO:0000313|Proteomes:UP000190105}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=USBA 833 {ECO:0000313|EMBL:SKA86028.1,
RC   ECO:0000313|Proteomes:UP000190105};
RA   Peterson S.W.;
RL   Submitted (FEB-2017) 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 replication.
CC       {ECO:0000256|HAMAP-Rule:MF_00974, ECO:0000256|PIRNR:PIRNR002811}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.;
CC         EC=2.7.7.101; Evidence={ECO:0000256|HAMAP-Rule:MF_00974};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00974,
CC         ECO:0000256|PIRNR:PIRNR002811, ECO:0000256|PIRSR:PIRSR002811-1};
CC       Note=Binds 1 zinc ion per monomer. {ECO:0000256|HAMAP-Rule:MF_00974,
CC       ECO:0000256|PIRNR:PIRNR002811, ECO:0000256|PIRSR:PIRSR002811-1};
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. {ECO:0000256|HAMAP-
CC       Rule:MF_00974, ECO:0000256|PIRNR:PIRNR002811}.
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DR   EMBL; FUYH01000007; SKA86028.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1T4XAA5; -.
DR   STRING; 1147123.SAMN05443428_10728; -.
DR   OrthoDB; 9803773at2; -.
DR   Proteomes; UP000190105; Unassembled WGS sequence.
DR   GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR   GO; GO:1990077; C:primosome complex; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
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; 3.40.1360.10; -; 1.
DR   Gene3D; 3.90.980.10; DNA primase, catalytic core, N-terminal domain; 1.
DR   Gene3D; 3.90.580.10; Zinc finger, CHC2-type domain; 1.
DR   HAMAP; MF_00974; DNA_primase_DnaG; 1.
DR   InterPro; IPR036185; DNA_heli_DnaB-like_N_sf.
DR   InterPro; IPR016136; DNA_helicase_N/primase_C.
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; IPR013264; DNAG_N.
DR   InterPro; IPR034151; TOPRIM_DnaG_bac.
DR   InterPro; IPR006171; TOPRIM_domain.
DR   InterPro; IPR002694; Znf_CHC2.
DR   NCBIfam; TIGR01391; dnaG; 1.
DR   PANTHER; PTHR30313; DNA PRIMASE; 1.
DR   PANTHER; PTHR30313:SF2; DNA PRIMASE; 1.
DR   Pfam; PF10410; DnaB_bind; 1.
DR   Pfam; PF08275; DNAG_N; 1.
DR   Pfam; PF13155; Toprim_2; 1.
DR   Pfam; PF01807; zf-CHC2; 1.
DR   PIRSF; PIRSF002811; DnaG; 1.
DR   SMART; SM00493; TOPRIM; 1.
DR   SMART; SM00400; ZnF_CHCC; 1.
DR   SUPFAM; SSF56731; DNA primase core; 1.
DR   SUPFAM; SSF48024; N-terminal domain of DnaB helicase; 1.
DR   SUPFAM; SSF57783; Zinc beta-ribbon; 1.
DR   PROSITE; PS50880; TOPRIM; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705, ECO:0000256|HAMAP-
KW   Rule:MF_00974};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW   Rule:MF_00974};
KW   DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478,
KW   ECO:0000256|HAMAP-Rule:MF_00974};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00974};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW   Rule:MF_00974};
KW   Primosome {ECO:0000256|ARBA:ARBA00022515, ECO:0000256|HAMAP-Rule:MF_00974};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW   Rule:MF_00974};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00974};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00974};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|HAMAP-
KW   Rule:MF_00974}.
FT   DOMAIN          254..335
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
FT   ZN_FING         39..63
FT                   /note="CHC2-type"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00974,
FT                   ECO:0000256|PIRSR:PIRSR002811-1"
FT   COILED          415..442
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          551..578
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   594 AA;  68041 MW;  B96EC2E3006F3BF3 CRC64;
     MGRIPQNIIE KIVERSDIVD VVSEFVPLRK SGRNYMGVCP FHNDKGPSLS VSQDKQLFHC
     FGCGASGNVI GFIMRIKNIE YIDAIAYLAD RANVTIEFSD NDRKTDEENK VKDEIFKANI
     EAARLYFSNL KKSKRAYEYL KKRNVDDTII LKFGLGYSIE SYNFIYNNLR NKGFSEEILL
     KAGLIIKGQK GYYDRFRNRI MFPVIDIKGR IIGFGGRVLD DSKPKYLNSP ETPVFKKGTN
     LYGLNLAAKQ PSIENIIIVE GYMDCISLHQ YGVNNAVASL GTSLTLEQAK LLKRYSKDIF
     ICYDADTAGQ AATLRGLSIL ESAGCEVKII EIPKGKDPDE FIKNYGVEEF KNLMKNALPV
     LEYRIQKAKN GKDLKDIKQK SLFINEVANI LSEVDNPIDV QLFAAKVFDE TGIAVQSILE
     QIKKLKNKKS NNENNKNNRR DNIVNGNIYN VEPAYKKAER LILNLCLKDS ELFRFISKRI
     KPEEFITDEY KISAEYIFEK CSNEEKIDAN ELLLKFENND DISNISSIFI EYEFNEDLFK
     LSEDLIKTIR RHKLESMIND LNADIKKYEE ANDIEKSAAL FQELIKLRKQ LNLL
//
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