(data stored in SCRATCH3701 zone)

HOGENOM6: ALLVD_1_PE1939

ID   ALLVD_1_PE1939                       STANDARD;      PRT;   1386 AA.
AC   ALLVD_1_PE1939; D3RUQ2;
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; (ALLVD_1.PE1939).
GN   OrderedLocusNames=Alvin_1987;
OS   ALLOCHROMATIUM VINOSUM DSM 180.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC   Chromatiaceae; Allochromatium.
OX   NCBI_TaxID=572477;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS ALLVD_1.PE1939.
CC       Allochromatium vinosum DSM 180 chromosome, complete genome.
CC       Missing 5 prime End;
CC   -!- ANNOTATIONS ORIGIN:D3RUQ2_ALLVD
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; D3RUQ2; -.
DR   EMBL; CP001896; ADC62911.1; -; Genomic_DNA.
DR   RefSeq; YP_003443943.1; NC_013851.1.
DR   GeneID; 8787351; -.
DR   GenomeReviews; CP001896_GR; Alvin_1987.
DR   KEGG; alv:Alvin_1987; -.
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   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; IPR003587; Hedgehog_hint_N.
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   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; PS50817; INTEIN_N_TER; 1.
DR   HOGENOMDNA; ALLVD_1.PE1939; -.
DR   PRODOM; ALLVD_1_PE1939.
DR   SWISS-2DPAGE; ALLVD_1_PE1939.
KW   ATP-binding; Complete proteome; Cytoplasm; DNA-binding; Isomerase;
KW   Nucleotide-binding; Topoisomerase.
SQ   SEQUENCE   1386 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MPDFAKEVLP INLEDEMRQS YLDYAMSVIV GRALPDVRDG LKPVHRRVLF SMHEQGNVWN
     RAYRKSARVV GDVMGKYHPH GDAAIYDTMV RMAQPFSLRN LLVDGQGNFG CFTGDTAIKL
     ADGTEKTFAE LAQLPPNEIF YVYAVDKTGK IVIAEGRHAR LTRPDAELLE LTLDTGDVVR
     CTPDHRFMLR DGSYKEAQDL TPDDSLMPGV FDTAPVKPGL NEYLRILQPN LGQYQFVHHL
     ADEFNAERGQ CDDVQGPFVR HHRNFDRWDN TPSNIQRLTF LEHLHLHAEQ LGELWKDPDF
     REAQKRGVQT YYSQHPEVVE ERRERFIRQN QDEHFRQLNA ARTSEGLQHY YAEHPEACAA
     IAERMRLLWQ DADYREKMSS VLSGIQKRPL SDEEQAGIRA IIAEKSRRMW GDDDKREEIV
     AAICRAMASD SIRKKISEAV KRQWQDPEYR AKFPADHFSR MAHRFWDKPE AREIHREKIS
     KQWESAEFIQ AQKQAVIDSN ARRLRENPDL MQDINRKAVE SLRTNWKAPE YRRQVMRRKI
     AGYVYDLTKR FPDCDVTPEL YESNRQQNWI PRLNKAVEYF GDFDALVTAG RHYNHRVVSQ
     RRLTERADTY DITVDHHHNF LLACGVFVHN SVDGDPPAAM RYTEVRMTRI ADTLLDDLDK
     ETVDFVPNYD NTEHEPSVLP ARFPNLLVNG SSGIAVGMAT NIPPHNLREV IDACLAIIDN
     PLVSLDELME IVPGPDFPTA GLINGVRGIR EAYRTGRGRC VMRARATTET QKRSGREAIV
     ITEIPYQVNK ARLLERIAEL VKEKKIEGIA QDGLRDESDK DGMRIVIELK RDTHSEVLLN
     NLYQHTQLQQ VFGINMVALV DGQPLTLNLK QILEYFLRHR RDVVTRRTLY ELRKARDRAH
     VLEGYAIALA NIDEVIATIK AAANPAEARE RLMERHWAPG AVTGMLERAG ADRTRPEELE
     ACFGLSDAGY RLSERQAKAI LDLQLHRLTG LEQDKILKEF EEILATIAAL LLILSDPDRL
     MEVIREELIA VRDQFGDERR TEIQLDQTDL TLEDLIAPED RVVTLSHQGY VKTQPISDYQ
     AQKRGGKGKS ATAIKEEDFI DRIFVANSHD TVLCFSSRGR VYWLKVYELP QAGRGARGRP
     MVNLLPLEAG ERITTLLPVR DYEDGSFVFM ATSAGTVKKT PLKDFSRPLS RGIIAIDLRE
     DELLVGATIT GGEQDLMLFT SAGKAVRFSE SHVRSMGRAA HGVRGVMLQE GQRVIALVAP
     EDGGTVLSVT ENGYGKRTDV DQFPTKGRGT QGVIAIDTAE RNGAQVGAIL VHPGDEIMLI
     ADDGTLIRTS VDQIPVVGRN TKGVKLINLG EGQRLVFVER IAALEGDKET GEEAAEDSEA
     SVADDA
//

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