(data stored in SCRATCH3701 zone)

HOGENOM6: HAINF2_1_PE536

ID   HAINF2_1_PE536                       STANDARD;      PRT;   882 AA.
AC   HAINF2_1_PE536; E7A444;
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 (HAINF2_1.PE536) (Type II topoisomerase),
DE   subunit A; .
GN   ORFNames=HIBPF06490;
OS   HAEMOPHILUS INFLUENZAE F3031.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=866630;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS HAINF2_1.PE536.
CC       Haemophilus influenzae F3031, complete genome.
CC       annotated by Ensembl
CC   -!- ANNOTATIONS ORIGIN:E7A444_HAEIF
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; E7A444; -.
DR   EMBL; FQ670178; CBY80818.1; -; Genomic_DNA.
DR   RefSeq; YP_004135153.1; NC_014920.1.
DR   ProteinModelPortal; E7A444; -.
DR   SMR; E7A444; 31-519, 533-866.
DR   GeneID; 10133411; -.
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: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   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; HAINF2_1.PE536; -.
DR   PRODOM; HAINF2_1_PE536.
DR   SWISS-2DPAGE; HAINF2_1_PE536.
KW   DNA gyrase (type ii topoisomerase), subunit a;
KW   ATP-binding; Cytoplasm; DNA-binding; Isomerase; Nucleotide-binding;
KW   Topoisomerase.
SQ   SEQUENCE   882 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MTDSIQSSIT PVNIEEELKS SYLDYAMSVI VGRALPDVRD GLKPVHRRVL FSMDREGNTA
     NKKYVKSARV VGDVIGKYHP HGDSAVYDTI VRMAQPFSLR YMLVDGQGNF GSIDGDAPAA
     MRYTEVRMQK ITQALLTDLD KETVNFSPNY DGELMIPDVL PTRIPALLAN GSSGIAVGMA
     TNIPPHNLNE VLNGCLAYID NNEITIDELM QHIPGPDFPT AALINGRKGI EEAYRTGRGK
     VYVRARATVE TNEKGREQII VSELPYQVNK AKLVEKIAEL IREKKIEGIS NITDLSNKEG
     IRIEIDIKRD AVGEVVLNHL YSLTQMQVTF GINMVALDHG QPRLFNLKEI IESFVLHRRE
     VVTRRSIFEL RKARERTHIL EGLAVARSNI DEMIAIIRNS KNREEAATAI SSRSWTLHSD
     IINLLDVSAR PDELEENLGI QGEQYYLSPA QVNAILELRL HRLTGIAFEE VIKEYEELLV
     KIADLLHILS SAERLMEVIR EELEEVKAQF GDDRLTEITA ASGDIDLEDL IAQEDVVVTL
     SHEGYVKYQP LTDYEAQRRG GKGKSATKMK EEDFIEKLLV ANTHDTILCF SSRGRLYWLK
     VYQLPQASRG ARGRPIVNIL PLQENERITA ILPVSAYEED KFVVMATAGG IVKKIALTEF
     SRPRSNGIIA LNLRDEDELI GVDITDGSNE IMLFSSQGRV VRFAENAVRA MGRLATGVRG
     IKLALTNDIS DDESAVEIED ISDDNAEASL DLNIDKVVSL VVPKGEGEIL TATQNGYGKR
     TQLSEYPTKS RNTKGVISIK VSERNGKVVA ATQVEETDQI MLITDAGTLV RTRVSEVSIV
     GRNTQGVRLI RTADDEHVVS LERVCDADED EDDSLEESNS KE
//

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