(data stored in SCRATCH3701 zone)

HOGENOM6: MYCSS_1_PE7

ID   MYCSS_1_PE7                          STANDARD;      PRT;   1257 AA.
AC   MYCSS_1_PE7; Q1BG55;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   SubName: Full=DNA gyrase subunit A; EC=5.99.1 3; (MYCSS_1.PE7).
GN   OrderedLocusNames=Mmcs_0007;
OS   MYCOBACTERIUM SP. MCS.
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Corynebacterineae; Mycobacteriaceae; Mycobacterium.
OX   NCBI_TaxID=164756;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS MYCSS_1.PE7.
CC       Mycobacterium sp. MCS, complete genome.
CC       chromosome, complete sequence.
CC   -!- ANNOTATIONS ORIGIN:Q1BG55_MYCSS
CC   -!- FUNCTION: DNA gyrase negatively supercoils closed circular double-
CC       stranded DNA in an ATP-dependent manner and also catalyzes the
CC       interconversion of other topological isomers of double-stranded
CC       DNA rings, including catenanes and knotted rings (By similarity).
CC   -!- CATALYTIC ACTIVITY: ATP-dependent breakage, passage and rejoining
CC       of double-stranded DNA.
CC   -!- SUBUNIT: Made up of two chains. The A chain is responsible for DNA
CC       breakage and rejoining; the B chain catalyzes ATP hydrolysis. The
CC       enzyme forms an A2B2 tetramer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- GENE_FAMILY: HOG000076278 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; Q1BG55; -.
DR   EMBL; CP000384; ABG06129.1; -; Genomic_DNA.
DR   RefSeq; YP_637185.1; NC_008146.1.
DR   ProteinModelPortal; Q1BG55; -.
DR   SMR; Q1BG55; 38-130, 132-254, 499-551.
DR   STRING; Q1BG55; -.
DR   EnsemblBacteria; EBMYCT00000061387; EBMYCP00000059554; EBMYCG00000061382.
DR   GeneID; 4108932; -.
DR   GenomeReviews; CP000384_GR; Mmcs_0007.
DR   KEGG; mmc:Mmcs_0007; -.
DR   eggNOG; COG0188; -.
DR   GeneTree; EBGT00050000016653; -.
DR   OMA; TGRGRIY; -.
DR   ProtClustDB; CLSK701787; -.
DR   GO; GO:0005694; C:chromosome; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003918; F:DNA topoisomerase (ATP-hydrolyzing) activity; IEA:EC.
DR   GO; GO:0004519; F:endonuclease activity; IEA:InterPro.
DR   GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0006265; P:DNA topological change; IEA:InterPro.
DR   GO; GO:0016539; P:intein-mediated protein splicing; IEA:InterPro.
DR   InterPro; IPR020899; Arg_repress_C.
DR   InterPro; IPR005743; GyrA.
DR   InterPro; IPR006691; GyrA/parC_pinwhl.
DR   InterPro; IPR003586; Hedgehog_hint_C.
DR   InterPro; IPR003587; Hedgehog_hint_N.
DR   InterPro; IPR006142; INTEIN.
DR   InterPro; IPR004042; Intein_endonuc.
DR   InterPro; IPR006141; Intein_splice_site.
DR   InterPro; IPR002205; Topo_IIA_A/C.
DR   InterPro; IPR013758; Topo_IIA_A/C_ab.
DR   InterPro; IPR013757; Topo_IIA_A_a.
DR   InterPro; IPR013760; Topo_IIA_cen.
DR   Gene3D; G3DSA:3.30.1360.40; Arg_repress; 1.
DR   Gene3D; G3DSA:3.90.199.10; Topo_IIA_A/C_ab; 2.
DR   Gene3D; G3DSA:1.10.268.10; Topo_IIA_A_a; 1.
DR   Pfam; PF03989; DNA_gyraseA_C; 6.
DR   Pfam; PF00521; DNA_topoisoIV; 2.
DR   PRINTS; PR00379; INTEIN.
DR   SMART; SM00305; HintC; 1.
DR   SMART; SM00306; HintN; 1.
DR   SMART; SM00434; TOP4c; 1.
DR   SUPFAM; SSF56719; Topo_IIA_cen; 2.
DR   TIGRFAMs; TIGR01063; GyrA; 1.
DR   TIGRFAMs; TIGR01443; Intein_Cterm; 1.
DR   TIGRFAMs; TIGR01445; Intein_Nterm; 1.
DR   PROSITE; PS50818; INTEIN_C_TER; 1.
DR   PROSITE; PS50819; INTEIN_ENDONUCLEASE; 1.
DR   PROSITE; PS50817; INTEIN_N_TER; 1.
DR   HOGENOMDNA; MYCSS_1.PE7; -.
DR   PRODOM; MYCSS_1_PE7.
DR   SWISS-2DPAGE; MYCSS_1_PE7.
KW   DNA gyrase subunit A;
KW   ATP-binding; Complete proteome; Cytoplasm; DNA-binding; Isomerase;
KW   Nucleotide-binding; Topoisomerase.
SQ   SEQUENCE   1257 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MTDTTLPPGD EAGDRIEPVD IQQEMQRSYI DYAMSVIVGR ALPEVRDGLK PVHRRVLYAM
     FDSGFRPDRG HAKSARSVAE TMGNYHPHGD SSIYDTLVRM AQPWSLRYPL VDGQGNFGSP
     GNDPPAAMRY CVTGDALVRL PLGQSVRIDG VVPGAKPNSD NPIDLKVVDR HGDPVAADRL
     FHSGEHQTYK VTTTEGYTVT GTENHPLLCL VDVGGVPTLL WKLVEEIRPG DTVVLQRSQP
     MEFGPADWQE TLEALLAGAF ISEGFISEKR AGFNNLDRDF FNMVVAAYDA VVGGRRYVSS
     RTIASGSLLH ELDIHNLESL RRSRLGVAVG QRSADKFVPE WIWQSPAAVK RVFLQALFEG
     DGSCSRLPRN TIQVSYSTRS ERLAADVQQM LLEFGIVSRR YRHAVGEYKV ALTNRAQAEL
     FARQIGFGGA KQVKLLEILS ALPEEAAGLD RDFVPGLARF IRQHSGGRWA DKEWLRKHNV
     DRISRWQRNG AEILGRIADP EVRAVATDLT DGRFYYATVA SVADAGVQPV YSLRVDTEDH
     AFITNGFVSH NTEARLTPLA MEMLREIDEE TVDFIPNYDG RVQEPTVLPS RFPNLLANGS
     GGIAVGMATN IPPHNLRELA DAVYWCLENF EADEETTLAA VMERVKGPDF PTHGLIVGSQ
     GIEDTYKTGR GSVKMRGVVE IEEDSRGRTG IVITELPYQV NHDNFITSIA EQVRDGKLAG
     ISNIEDQSSD RVGLRIVVEL KRDAVAKVVL NNLYKHTQLQ TSFGANMLSI VDGVPRTLRL
     DQMIRYYVEH QLDVIVRRTR YRLRKANERA HILRGLVKAL DALDEVIALI RASQTVDIAR
     AGLIELLDID EIQAQAILDM QLRRLAALER QRIVDDLAKI EAEIADLEDI LAKPERQRAI
     VRDELKEIAD KYGDDRRTRI VPADGEVSDE DLIAREDVVV TITETGYAKR TKTDLYRSQK
     RGGKGVQGAG LKQDDIVNHF FVCSTHDWIL FFTTQGRVYR AKAYELPEAS RTARGQHVAN
     LLAFQPNERI AQVIQIKSYE DAPYLVLATR NGLVKKSRLT DFDSNRSGGI VAVNLRDGDE
     LVGAVLCSSE DDLLLVSAKG QSIRFSATDE ALRPMGRATS GVQGMRFNAD DELLSLNVVR
     PDTYLLVATS GGYAKRTSIE EYTAQGRGGK GILTIQYDRR RGNLVGALIV DDDTELYAIT
     SGGGVIRTAA RQVRKAGRQT KGVRLMNLGE GDTLIAIARN AEAGDSTDEV NTDPDAV
//

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