ID A0A345XW04_9ACTN Unreviewed; 1016 AA.
AC A0A345XW04;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=Topoisomerase II {ECO:0000313|EMBL:AXK35820.1};
GN ORFNames=DVA86_27510 {ECO:0000313|EMBL:AXK35820.1};
OS Streptomyces armeniacus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=83291 {ECO:0000313|EMBL:AXK35820.1, ECO:0000313|Proteomes:UP000254425};
RN [1] {ECO:0000313|EMBL:AXK35820.1, ECO:0000313|Proteomes:UP000254425}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15676 {ECO:0000313|EMBL:AXK35820.1,
RC ECO:0000313|Proteomes:UP000254425};
RA Labana P., Gosse J.T., Boddy C.N.;
RT "Draft genome of the type strain Streptomyces armeniacus ATCC 15676.";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP031320; AXK35820.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A345XW04; -.
DR Proteomes; UP000254425; Chromosome.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR002586; CobQ/CobB/MinD/ParA_Nub-bd_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR047739; SCO5717-like_N.
DR NCBIfam; NF041021; SCO5717_Nterm; 1.
DR PANTHER; PTHR43384:SF14; ESX-1 SECRETION-ASSOCIATED PROTEIN ESPI; 1.
DR PANTHER; PTHR43384; SEPTUM SITE-DETERMINING PROTEIN MIND HOMOLOG, CHLOROPLASTIC-RELATED; 1.
DR Pfam; PF01656; CbiA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 4: Predicted;
KW Isomerase {ECO:0000313|EMBL:AXK35820.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000254425}.
FT DOMAIN 703..806
FT /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT /evidence="ECO:0000259|Pfam:PF01656"
FT REGION 1..685
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 949..1016
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..112
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..158
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..337
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..358
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..399
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 447..464
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 505..519
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 541..570
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 577..601
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 604..625
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 626..641
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 959..973
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 976..1016
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1016 AA; 104149 MW; 1C1ED541C7BB09E0 CRC64;
MSSDRDEIRV GGSTPATDRL DAEAESEHET ETTGQFTIDY TPPAWYTQDS PATDGRGEPV
APLGLDRDAS AGADAAFPSA PLPLGGEEKD ESDEAPASVD SPDTSETASG EGSSEPDGAP
AGSETDARGA RPGASTPDGT VDSPETVRFS SASLRQEISR FRNGGEPDGP GDGADQGGTA
AASDDLDGAG DPDPDAPDSG GSAAASHGAT ASGKAGTAAD AGPEAFPEGV TEDGADAGTK
SPTPDSGSVP GVGGPRDAEP QDAVPQDAIP PGHVPGADRV DDAAPAGAAE GAPEPRDTPP
AHPLSSTPQQ AAPWPAAPGS AGTPPGGLPP LPPDFQPANP QQAADAQPAP PPPGTPWLTA
PDAAHDAAAP AVPDQRAEQA PPAAPQHGPG APVPPAGTGP AQDAPHGQPA LPAGGHGTVP
GSAPLPPAVP QGGQGGHPEQ PGAQGQFALG QPGQQAQQAP GQQAPQTPGQ PPVQPGGYGF
PQPGQSGAQP PAAGQGGYGY PQSFPPAQGQ HQGQGQPEAL SPAQPGGYGF PQPAQPQQPG
QPPAQQHGGQ QHGRQPAPPQ HQQQAPGAIE PNASAQHGGS GYPQQLPPGQ GGQNPGQALQ
PHAPNVPQAP PPQQQQPPQP QPQSQQQSPD PRRQSHSGDG SPLGYTAAVE LSSDRLLSDK
KKPRSQNPAR GGGRFRFGGR KDDTERQRKL ELIRTPVLSC YRIAVISLKG GVGKTTTTTA
LGSTLATERQ DKVIAIDANP DAGTLGRRVR RETGATIRDL VTAIPYLNSY MDIRRFTSQA
PSGLEILAND VDPAVSTTFN DDDYRRVIDV LGKQYPIILT DSGTGLLYSA MRGVLDLAHQ
LIVISTPSVD GASSASTTLD WLSAHGYGDL VQRSVTVISG VRETGKMIKV EDIVAHFQTR
CRGVVTIPFD EHLSAGAELD LDMMRPRTRE AYFNLSAMIA EDFSRVQQEQ GLWTADGNPP
PQLAPPLPGQ SVPGQPYVPG QGQQPYQQQP YAQQPQQPQQ PGQQQGGWPQ QPPQQP
//