(data stored in SCRATCH3701 zone)

HOGENOM6: PROM9_1_PE1073

ID   PROM9_1_PE1073                       STANDARD;      PRT;   863 AA.
AC   PROM9_1_PE1073; Q31AG2;
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; (PROM9_1.PE1073).
GN   OrderedLocusNames=PMT9312_1074;
OS   PROCHLOROCOCCUS MARINUS STR. MIT 9312.
OC   Bacteria; Cyanobacteria; Prochlorales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=74546;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS PROM9_1.PE1073.
CC       Prochlorococcus marinus str. MIT 9312, complete genome.
CC       genome.
CC   -!- ANNOTATIONS ORIGIN:Q31AG2_PROM9
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; Q31AG2; -.
DR   EMBL; CP000111; ABB50133.1; -; Genomic_DNA.
DR   RefSeq; YP_397569.1; NC_007577.1.
DR   ProteinModelPortal; Q31AG2; -.
DR   STRING; Q31AG2; -.
DR   GeneID; 3765877; -.
DR   GenomeReviews; CP000111_GR; PMT9312_1074.
DR   KEGG; pmi:PMT9312_1074; -.
DR   eggNOG; COG0188; -.
DR   OMA; VCLKVLG; -.
DR   ProtClustDB; PRK05560; -.
DR   BioCyc; PMAR74546:PMT9312_1074-MONOMER; -.
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:0003700; F:sequence-specific DNA binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0006265; P:DNA topological change; IEA:InterPro.
DR   InterPro; IPR020899; Arg_repress_C.
DR   InterPro; IPR005743; GyrA.
DR   InterPro; IPR006691; GyrA/parC_pinwhl.
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; 1.
DR   Gene3D; G3DSA:1.10.268.10; Topo_IIA_A_a; 1.
DR   Pfam; PF03989; DNA_gyraseA_C; 6.
DR   Pfam; PF00521; DNA_topoisoIV; 1.
DR   SMART; SM00434; TOP4c; 1.
DR   SUPFAM; SSF56719; Topo_IIA_cen; 1.
DR   TIGRFAMs; TIGR01063; GyrA; 1.
DR   HOGENOMDNA; PROM9_1.PE1073; -.
DR   PRODOM; PROM9_1_PE1073.
DR   SWISS-2DPAGE; PROM9_1_PE1073.
KW   ATP-binding; Complete proteome; Cytoplasm; DNA-binding; Isomerase;
KW   Nucleotide-binding; Topoisomerase.
SQ   SEQUENCE   863 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MSDIIDSGNS GLSEDNDRII QTDLRNEMSR SYLEYAMSVI VGRALPDARD GLKPVHRRIL
     YAMYELGLTS GRPYRKCARV VGEVLGKYHP HGDTAVYDAL VRMAQDFSMR MPLIDGHGNF
     GSVDNDPPAA MRYTESRLQS LTDESLLEDI ESETVDFSDN FDGSQQEPTV LPARIPQLLL
     NGSSGIAVGM ATNIPPHNLG ELINGLKSII NNPSIEDREL FELIKGPDFP TGGQILGRDG
     IRETFKTGRG SITMRGVANI EQIKSAGRAE KDAVIITELP FQTNKAGLIE RIADLVNERK
     LEGISDIRDE SDRDGMRIVI ELKRDAYPQV VLNNLFKLTP LQNNFSANIL ALVKGEPTTL
     SLRRMLDVFL DFRVETIRRR TGFLLRKAEE RDHIVKGLLL ALDAMDEIIN LIRSAKDTIS
     AREKLQTDHE LSSTQAEAIL QMQLRRLTAL EADKIKAEHD ELTKKINQYQ QILNSKERIF
     EIILEELNKI DERFSSPRKT EILDLGGGLD DIDLIANDRS VVLLTEAGYL KRMPVNEFES
     TSRGSRGKAG TKTQGDDEVK LFISCNDHDT LLLFSDRGVA YALPAYRVPM SSRTAKGTPS
     VQLLPIPREE KITSLVAVDS FDNDCYLLML TKSGFIKRTS LSAFSKIRSN GLIAINLEDG
     DALTWVRLSK EGDSVLIGSR TGIAIHFRLD INELRPLGRT ARGVKSMNLK KGDNLVSMDV
     LTSDLVDKLA KIDDLNKEIE ENIEVNSSDG PWVLIASAFG LGKRVPVTQF RLQKRAGMGL
     RAIKFRIQDD VLVCLKVLGE GEELLFVTEK GVIVRTNADK ISQQSRAATG VKLQRLDEGD
     HLSEVVLVPR EQIEEIDQTS PEE
//

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