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DNAG_MYCTU
ID   DNAG_MYCTU              Reviewed;         639 AA.
AC   P9WNW1; L0TC89; P63962; P95239;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 42.
DE   RecName: Full=DNA primase {ECO:0000255|HAMAP-Rule:MF_00974};
DE            EC=2.7.7.101 {ECO:0000255|HAMAP-Rule:MF_00974};
GN   Name=dnaG {ECO:0000255|HAMAP-Rule:MF_00974}; OrderedLocusNames=Rv2343c;
GN   ORFNames=MTCY98.12c;
OS   Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83332;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=9634230; DOI=10.1038/31159;
RA   Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA   Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA   Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA   Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA   Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA   Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA   Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA   Barrell B.G.;
RT   "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT   genome sequence.";
RL   Nature 393:537-544(1998).
RN   [2]
RP   IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].
RX   PubMed=19099550; DOI=10.1186/1752-0509-2-109;
RA   Raman K., Yeturu K., Chandra N.;
RT   "targetTB: a target identification pipeline for Mycobacterium tuberculosis
RT   through an interactome, reactome and genome-scale structural analysis.";
RL   BMC Syst. Biol. 2:109-109(2008).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA   Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA   Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA   Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA   Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT   "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT   mass spectrometry.";
RL   Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN   [4]
RP   SUBUNIT.
RC   STRAIN=H37Rv;
RX   PubMed=32634279; DOI=10.1111/mmi.14571;
RA   Zaveri A., Wang R., Botella L., Sharma R., Zhu L., Wallach J.B., Song N.,
RA   Jansen R.S., Rhee K.Y., Ehrt S., Schnappinger D.;
RT   "Depletion of the DarG antitoxin in Mycobacterium tuberculosis triggers the
RT   DNA-damage response and leads to cell death.";
RL   Mol. Microbiol. 114:641-652(2020).
CC   -!- FUNCTION: RNA polymerase that catalyzes the synthesis of short RNA
CC       molecules used as primers for DNA polymerase during DNA replication.
CC       {ECO:0000255|HAMAP-Rule:MF_00974}.
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:0000255|HAMAP-Rule:MF_00974};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00974};
CC       Note=Binds 1 zinc ion per monomer. {ECO:0000255|HAMAP-Rule:MF_00974};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00974};
CC       Note=Binds two Mg(2+) per subunit. {ECO:0000255|HAMAP-Rule:MF_00974};
CC   -!- SUBUNIT: Monomer. Interacts with DnaB (By similarity). Co-
CC       immunoprecipitates with DarG in the presence and absence of darT
CC       (PubMed:32634279). {ECO:0000255|HAMAP-Rule:MF_00974,
CC       ECO:0000269|PubMed:32634279}.
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:0000255|HAMAP-Rule:MF_00974}.
CC   -!- MISCELLANEOUS: Was identified as a high-confidence drug target.
CC       {ECO:0000269|PubMed:19099550}.
CC   -!- SIMILARITY: Belongs to the DnaG primase family. {ECO:0000255|HAMAP-
CC       Rule:MF_00974}.
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DR   EMBL; AL123456; CCP45131.1; -; Genomic_DNA.
DR   PIR; H70661; H70661.
DR   RefSeq; NP_216859.1; NC_000962.3.
DR   RefSeq; WP_003412049.1; NZ_NVQJ01000012.1.
DR   PDB; 5W33; X-ray; 2.85 A; A=112-432.
DR   PDB; 5W34; X-ray; 2.95 A; A/B=112-432.
DR   PDB; 5W35; X-ray; 3.31 A; A/B=112-432.
DR   PDB; 5W36; X-ray; 2.46 A; A/B=112-432.
DR   PDBsum; 5W33; -.
DR   PDBsum; 5W34; -.
DR   PDBsum; 5W35; -.
DR   PDBsum; 5W36; -.
DR   AlphaFoldDB; P9WNW1; -.
DR   SMR; P9WNW1; -.
DR   STRING; 83332.Rv2343c; -.
DR   PaxDb; P9WNW1; -.
DR   PRIDE; P9WNW1; -.
DR   DNASU; 885996; -.
DR   GeneID; 885996; -.
DR   KEGG; mtu:Rv2343c; -.
DR   TubercuList; Rv2343c; -.
DR   eggNOG; COG0358; Bacteria.
DR   OMA; LMWPIRD; -.
DR   PhylomeDB; P9WNW1; -.
DR   BRENDA; 2.7.7.101; 3445.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
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; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006269; P:DNA replication, synthesis of RNA primer; IBA:GO_Central.
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; IPR013173; DNA_primase_DnaG_DnaB-bd_dom.
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; PF08278; DnaG_DnaB_bind; 1.
DR   Pfam; PF13662; Toprim_4; 1.
DR   Pfam; PF08275; Toprim_N; 1.
DR   Pfam; PF01807; zf-CHC2; 1.
DR   PIRSF; PIRSF002811; DnaG; 1.
DR   SMART; SM00766; DnaG_DnaB_bind; 1.
DR   SMART; SM00493; TOPRIM; 1.
DR   SMART; SM00400; ZnF_CHCC; 1.
DR   TIGRFAMs; TIGR01391; dnaG; 1.
DR   PROSITE; PS50880; TOPRIM; 1.
PE   1: Evidence at protein level;
KW   3D-structure; DNA replication; DNA-binding; DNA-directed RNA polymerase;
KW   Magnesium; Metal-binding; Nucleotidyltransferase; Primosome;
KW   Reference proteome; Transcription; Transferase; Zinc; Zinc-finger.
FT   CHAIN           1..639
FT                   /note="DNA primase"
FT                   /id="PRO_0000180506"
FT   DOMAIN          262..348
FT                   /note="Toprim"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00974"
FT   ZN_FING         41..65
FT                   /note="CHC2-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00974"
FT   REGION          460..479
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         268
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00974"
FT   BINDING         319
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00974"
FT   BINDING         319
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00974"
FT   BINDING         321
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00974"
FT   HELIX           114..131
FT                   /evidence="ECO:0007829|PDB:5W36"
FT   HELIX           135..137
FT                   /evidence="ECO:0007829|PDB:5W33"
FT   HELIX           138..145
FT                   /evidence="ECO:0007829|PDB:5W36"
FT   TURN            146..148
FT                   /evidence="ECO:0007829|PDB:5W36"
FT   HELIX           151..156
FT                   /evidence="ECO:0007829|PDB:5W36"
FT   STRAND          160..162
FT                   /evidence="ECO:0007829|PDB:5W36"
FT   STRAND          164..167
FT                   /evidence="ECO:0007829|PDB:5W36"
FT   HELIX           168..175
FT                   /evidence="ECO:0007829|PDB:5W36"
FT   HELIX           180..185
FT                   /evidence="ECO:0007829|PDB:5W36"
FT   STRAND          188..192
FT                   /evidence="ECO:0007829|PDB:5W36"
FT   STRAND          195..199
FT                   /evidence="ECO:0007829|PDB:5W36"
FT   STRAND          202..209
FT                   /evidence="ECO:0007829|PDB:5W36"
FT   STRAND          215..222
FT                   /evidence="ECO:0007829|PDB:5W36"
FT   STRAND          232..235
FT                   /evidence="ECO:0007829|PDB:5W36"
FT   TURN            244..246
FT                   /evidence="ECO:0007829|PDB:5W36"
FT   HELIX           251..261
FT                   /evidence="ECO:0007829|PDB:5W36"
FT   STRAND          263..266
FT                   /evidence="ECO:0007829|PDB:5W36"
FT   HELIX           270..278
FT                   /evidence="ECO:0007829|PDB:5W36"
FT   STRAND          284..290
FT                   /evidence="ECO:0007829|PDB:5W36"
FT   HELIX           294..304
FT                   /evidence="ECO:0007829|PDB:5W36"
FT   TURN            305..309
FT                   /evidence="ECO:0007829|PDB:5W36"
FT   STRAND          313..321
FT                   /evidence="ECO:0007829|PDB:5W36"
FT   HELIX           322..330
FT                   /evidence="ECO:0007829|PDB:5W36"
FT   STRAND          333..335
FT                   /evidence="ECO:0007829|PDB:5W36"
FT   TURN            337..341
FT                   /evidence="ECO:0007829|PDB:5W36"
FT   STRAND          342..346
FT                   /evidence="ECO:0007829|PDB:5W36"
FT   HELIX           348..350
FT                   /evidence="ECO:0007829|PDB:5W36"
FT   HELIX           353..370
FT                   /evidence="ECO:0007829|PDB:5W36"
FT   HELIX           375..384
FT                   /evidence="ECO:0007829|PDB:5W36"
FT   HELIX           392..407
FT                   /evidence="ECO:0007829|PDB:5W36"
FT   HELIX           412..426
FT                   /evidence="ECO:0007829|PDB:5W36"
SQ   SEQUENCE   639 AA;  69593 MW;  E5A4887F2357C833 CRC64;
     MSGRISDRDI AAIREGARIE DVVGDYVQLR RAGADSLKGL CPFHNEKSPS FHVRPNHGHF
     HCFGCGEGGD VYAFIQKIEH VSFVEAVELL ADRIGHTISY TGAATSVQRD RGSRSRLLAA
     NAAAAAFYAQ ALQSDEAAPA RQYLTERSFD AAAARKFGCG FAPSGWDSLT KHLQRKGFEF
     EELEAAGLSR QGRHGPMDRF HRRLLWPIRT SAGEVVGFGA RRLFDDDAME AKYVNTPETL
     LYKKSSVMFG IDLAKRDIAK GHQAVVVEGY TDVMAMHLAG VTTAVASCGT AFGGEHLAML
     RRLMMDDSFF RGELIYVFDG DEAGRAAALK AFDGEQKLAG QSFVAVAPDG MDPCDLRLKC
     GDAALRDLVA RRTPLFEFAI RAAIAEMDLD SAEGRVAALR RCVPMVGQIK DPTLRDEYAR
     QLAGWVGWAD VAQVIGRVRG EAKRTKHPRL GRLGSTTIAR AAQRPTAGPP TELAVRPDPR
     DPTLWPQREA LKSALQYPAL AGPVFDALTV EGFTHPEYAA VRAAIDTAGG TSAGLSGAQW
     LDMVRQQTTS TVTSALISEL GVEAIQVDDD KLPRYIAGVL ARLQEVWLGR QIAEVKSKLQ
     RMSPIEQGDE YHALFGDLVA MEAYRRSLLE QASGDDLTA
 
 
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