(data stored in SCRATCH3701 zone)

HOGENOM6: ANAPZ_1_PE835

ID   ANAPZ_1_PE835                        STANDARD;      PRT;   906 AA.
AC   ANAPZ_1_PE835; Q2GJH7;
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, A subunit; EC=5.99.1 3; (ANAPZ_1.PE835).
GN   Name=gyrA; OrderedLocusNames=APH_0899;
OS   ANAPLASMA PHAGOCYTOPHILUM HZ.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Anaplasma; phagocytophilum group.
OX   NCBI_TaxID=212042;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ANAPZ_1.PE835.
CC       Anaplasma phagocytophilum HZ, complete genome.
CC       Missing 5 prime End;
CC   -!- ANNOTATIONS ORIGIN:Q2GJH7_ANAPZ
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; Q2GJH7; -.
DR   EMBL; CP000235; ABD44015.1; -; Genomic_DNA.
DR   RefSeq; YP_505474.1; NC_007797.1.
DR   ProteinModelPortal; Q2GJH7; -.
DR   STRING; Q2GJH7; -.
DR   GeneID; 3931204; -.
DR   GenomeReviews; CP000235_GR; APH_0899.
DR   KEGG; aph:APH_0899; -.
DR   NMPDR; fig|212042.5.peg.851; -.
DR   TIGR; APH_0899; -.
DR   eggNOG; COG0188; -.
DR   OMA; TGRGRIY; -.
DR   ProtClustDB; PRK05560; -.
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; ANAPZ_1.PE835; -.
DR   PRODOM; ANAPZ_1_PE835.
DR   SWISS-2DPAGE; ANAPZ_1_PE835.
KW   ATP-binding; Complete proteome; Cytoplasm; DNA-binding; Isomerase;
KW   Nucleotide-binding; Topoisomerase.
SQ   SEQUENCE   906 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MSDGVLPVSI EKELEDSYLS YAMSVIVSRA IPDVRDGLKP VHRRILYSMY KSGYDHDKPY
     KKAARVVGDV MGRYHPHADT AIYDALVRMA QDFSLLVPLI DSQGNFGSVD GDPPASMRYT
     EARLAQAAHF LLNDIDEDTV DFRPNYDENE QEPVVLPAEF PNVLVNGAGG VAVGMSTNIP
     SHNLGEIIDA SVMYIDNPEV TLEELMTVIP GPDFPTGGVI MGDAGIKSAF ATGRGTIIIQ
     GKTHIEELPS GRQAIIIDEI PYQTNKAKLV ERIHELVKEK KIEGVSDLRD ESNKSGIRVA
     IELKKQINSQ VVLNQLLGLT PLRTSFSINT LVLDNSRPRV MSLIEIIETF VAFRKEVLVR
     RTRYRLKKVR ERAHLFIGMY IAVLNIDEIV AIIRASKDAA EAAAALRERT WSPSEEVRGM
     IELVSDSTGV IEGGRYRLTA PQIKAILEMR LQRLTGLEKG KLEVELQSMV ALITEYTKIL
     STDSLLMCMV REGLLDVKRR VATPRRTTIE ESKGDIDAES LIPREEMVVT VTMNGFVKRV
     KLSNYRAQKR GGKGRVAQGI KEEDVTTKLF VVDTHTSVLF FSNVGKVYKL KVYKLPLGEP
     ASRGRSLVNI FPLAEGETIT SVMPLPDVGV DGGVESMDVV FATSSGNIRR NALADFQYVP
     SNGKIAMVLT PGDQLISANV CVSTDHVLLS SRMGKSIRFS VGNVRQFKGR MSDGVRAIKL
     AEGDQVISMS VLHGSEASSE VREAYLKIPV DSRIKAAESD GESIGKRVSG MLEGLQLSEE
     TFVDMVKKEQ FILTVTENGF GKRTSAYEYR TTARGGVGVL NILTTARNGK VVASFSVAHT
     DQVMLITDKG KLIRISVSDI RIIGRSTQGV TLFKTEKGEK VVSVALVIDS GDNCDDDEGI
     GGEVSA
//

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