(data stored in SCRATCH3701 zone)

HOGENOM6: ACIFV_1_PE11

ID   ACIFV_1_PE11                         STANDARD;      PRT;   831 AA.
AC   ACIFV_1_PE11; D2RMU1;
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; (ACIFV_1.PE11).
GN   OrderedLocusNames=Acfer_0011;
OS   ACIDAMINOCOCCUS FERMENTANS DSM 20731.
OC   Bacteria; Firmicutes; Negativicutes; Selenomonadales; Acidaminococcaceae;
OC   Acidaminococcus.
OX   NCBI_TaxID=591001;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ACIFV_1.PE11.
CC       Acidaminococcus fermentans DSM 20731, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:D2RMU1_ACIFV
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; D2RMU1; -.
DR   EMBL; CP001859; ADB46421.1; -; Genomic_DNA.
DR   RefSeq; YP_003397736.1; NC_013740.1.
DR   GeneID; 8736441; -.
DR   GenomeReviews; CP001859_GR; Acfer_0011.
DR   KEGG; afn:Acfer_0011; -.
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; ACIFV_1.PE11; -.
DR   PRODOM; ACIFV_1_PE11.
DR   SWISS-2DPAGE; ACIFV_1_PE11.
KW   ATP-binding; Complete proteome; Cytoplasm; DNA-binding; Isomerase;
KW   Nucleotide-binding; Topoisomerase.
SQ   SEQUENCE   831 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MDDQQNDKQT ISAGKVIPVY VEDEMQKCYI DYAMSVIVQR ALPDVRDGLK PVHRRILYAM
     NEAGMLPNKA YKKSARIVGD VLGKYHPHGD SSVYDAIVRL AQDFSTRYLM VDGHGNFGSV
     DGDPAAAMRY TEVRMGKIAV EMLRDIEKDT VDFIPNYDES LKEPTVLPAK VPALLINGSA
     GIAVGMATNI PPHNLGEVVD ACVMLIDHPD ATVEQLMTAV KGPDFPTGAK ILGLSGIRQA
     YTTGRGVVKV RAKTHVEPMP KNKNRIVVTE IPYQVNKAKL IENIAHLVQD KTLEGITDLR
     DESDRKGMRI VIELRSDVVP EIMLNKLYKH TQLQDSFGII MLALVNGHPR ILNLKQILEY
     YLDHQKDVIT RKCRYELKKA KERAHILEGL KIALDHLDEV IATIRASANG EVAKAALMEK
     FGLSDRQAQA ILDMRLQRLT GLERQKIEDE YKEVMATIAY LEDVLSDEHK IMGIAREDLL
     DVKKRFGDAR RTSIVPDTGD LETEDLIAEE DVVITISHQS YIKRQALTNF RNQNRGGRGI
     KAGSGKIVKE DNKVKGDFSE HLLMASTHDN ILFFTNRGRV YRQKGFEIPE ASRTAKGTFI
     RNLLPLEENE KVNAVIAVKS GISEDEKKFL FMATNLGYVK RTSVSEFKSA RKGGLIAINL
     GEGEELIDVK LTSGHNDILL ATRDGYAIHF LEDDVRPMGR TSHGVRGISL RPHDSVVSMD
     SCVDDTGEVL TVTDKGQGKR TDISEYRVQT RGGKGIINLK VTDRTGLIVG SKFINETHDI
     MLISAAGIII RMNAADISTY GRNAQGVKLM DLEAGDKVAA LAIVNTVSED E
//

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