ID A0A3N2PEL9_9ACTN Unreviewed; 1270 AA.
AC A0A3N2PEL9;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN ORFNames=EF879_08430 {ECO:0000313|EMBL:ROT33138.1};
OS Micromonospora sp. HM5-17.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=2487710 {ECO:0000313|EMBL:ROT33138.1, ECO:0000313|Proteomes:UP000281230};
RN [1] {ECO:0000313|EMBL:ROT33138.1, ECO:0000313|Proteomes:UP000281230}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HM5-17 {ECO:0000313|EMBL:ROT33138.1,
RC ECO:0000313|Proteomes:UP000281230};
RA Thawai C.;
RT "Micromonospora sp. HM5-17, a new actinomycetes isolated from a hot spring
RT soil.";
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP-dependent breakage, passage and rejoining of double-
CC stranded DNA.; EC=5.6.2.2; Evidence={ECO:0000256|ARBA:ARBA00000185};
CC -!- SIMILARITY: Belongs to the type II topoisomerase GyrA/ParC subunit
CC family. {ECO:0000256|ARBA:ARBA00008263}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ROT33138.1}.
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DR EMBL; RJWA01000002; ROT33138.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N2PEL9; -.
DR OrthoDB; 9806486at2; -.
DR Proteomes; UP000281230; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0034335; F:DNA negative supercoiling activity; IEA:UniProt.
DR GO; GO:0004519; F:endonuclease 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 CDD; cd00081; Hint; 1.
DR Gene3D; 3.30.1360.40; -; 1.
DR Gene3D; 2.120.10.90; DNA gyrase/topoisomerase IV, subunit A, C-terminal; 1.
DR Gene3D; 2.170.16.10; Hedgehog/Intein (Hint) domain; 2.
DR Gene3D; 3.10.28.10; Homing endonucleases; 1.
DR Gene3D; 3.90.199.10; Topoisomerase II, domain 5; 2.
DR Gene3D; 1.10.268.10; Topoisomerase, domain 3; 1.
DR InterPro; IPR006691; GyrA/parC_rep.
DR InterPro; IPR035516; Gyrase/topoIV_suA_C.
DR InterPro; IPR003587; Hint_dom_N.
DR InterPro; IPR036844; Hint_dom_sf.
DR InterPro; IPR027434; Homing_endonucl.
DR InterPro; IPR006142; INTEIN.
DR InterPro; IPR030934; Intein_C.
DR InterPro; IPR004042; Intein_endonuc.
DR InterPro; IPR006141; Intein_N.
DR InterPro; IPR004860; LAGLIDADG_2.
DR InterPro; IPR013760; Topo_IIA-like_dom_sf.
DR InterPro; IPR013758; Topo_IIA_A/C_ab.
DR InterPro; IPR013757; Topo_IIA_A_a_sf.
DR InterPro; IPR002205; Topo_IIA_dom_A.
DR NCBIfam; TIGR01445; intein_Nterm; 1.
DR PANTHER; PTHR43493:SF5; DNA GYRASE SUBUNIT A, CHLOROPLASTIC_MITOCHONDRIAL; 1.
DR PANTHER; PTHR43493; DNA GYRASE/TOPOISOMERASE SUBUNIT A; 1.
DR Pfam; PF03989; DNA_gyraseA_C; 2.
DR Pfam; PF00521; DNA_topoisoIV; 2.
DR Pfam; PF14528; LAGLIDADG_3; 1.
DR PRINTS; PR00379; INTEIN.
DR SMART; SM00306; HintN; 1.
DR SMART; SM00434; TOP4c; 1.
DR SUPFAM; SSF101904; GyrA/ParC C-terminal domain-like; 1.
DR SUPFAM; SSF51294; Hedgehog/intein (Hint) domain; 1.
DR SUPFAM; SSF55608; Homing endonucleases; 1.
DR SUPFAM; SSF56719; Type II DNA topoisomerase; 2.
DR PROSITE; PS50818; INTEIN_C_TER; 1.
DR PROSITE; PS50819; INTEIN_ENDONUCLEASE; 1.
DR PROSITE; PS50817; INTEIN_N_TER; 1.
PE 3: Inferred from homology;
KW Autocatalytic cleavage {ECO:0000256|ARBA:ARBA00022813};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:ROT33138.1};
KW Protein splicing {ECO:0000256|ARBA:ARBA00023000};
KW Reference proteome {ECO:0000313|Proteomes:UP000281230};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029}.
FT DOMAIN 260..404
FT /note="DOD-type homing endonuclease"
FT /evidence="ECO:0000259|PROSITE:PS50819"
FT DOMAIN 543..566
FT /note="Intein C-terminal splicing"
FT /evidence="ECO:0000259|PROSITE:PS50818"
FT REGION 984..1003
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1237..1270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 896..923
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 988..1003
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1270 AA; 139032 MW; BAEAF0E2148253E5 CRC64;
MARRTGNRST VDLSAFDRAG ARVTDNPLAT EVEDSYLEYA FSVIHSRALP DARDGLKPVH
RRILYSMSEQ GYRPDRPHVK SARVVGDVMG KYHPHGDAAI YDAMVRLAQN FSLNAPLIDG
HGNFGSPDDG PAAARYCVVG DTRIRLADGS SPRIADLVDL PANAERDADF EVLDKDGKAV
RVNRVFNSGV HPTIRITTTS GYSLRGSENH LVLCLENPMG VPLFQWRRLD EIQPGTVVCI
ARNAWSEVVP TAREYNLGIL AGAWVSGGWA SDSRAGFNNT DEHFFSEVLH AYDEIVGGAR
SVSERHARRD RKRVLELDVQ EFSGGMDAFR ASPLAELIGH QAREKFVPGF VWSGGWGVKR
AFLMAIFEGD GGVRVANDSL TIQYTTYSER LGQELQELLA EFGVIACRRR YTRPGGSVEH
RLVISGLRNI KAYAQRVGFL RTKQAVLQKL LRHAPLRPHR LSRDHVPFVA DYVRGALEFG
RRGSGRKWLT VHNFDRMERW ETERARIIDW VKDPEVLATI LPIMDSGYRF ETVSEVVPAE
PAEVYSVRVE SEDHSFLAGA FVNHNTEARM SREAMLLVGE LGEGTVDFRP NYDGSLTEPT
VLPAAFPNLL VNGTSGIAVG MATNMIPHNL AEVVQAARWL IDHPDASLDE LMRFVPGPDL
PTGGLLLGLD EVRKAYQTGR GVVRMRARVE IGPLEGSRGR QAITVVELPY GVGAEKVIEA
ITDEARGKLI TSGPRKGQRQ PARLQGIADV KDLTDRENGT RLVIECKVGV NPQALLADLY
RLTPLEQSFG VNNLVLVDGQ PQTLGLKELL EVFLRHRYDV VTRRTTFRRT KRQDRLHLVD
GLLMALLDID EVVRLIRGSE NAQAAKDALM AQFGLSEIQA GYILDTPLRR LTKFDRLELE
VERDRLREEI AALTEILEDE RVLRKVVSEE LAAVAREFGR ERRTTLIDGD LREVLAASAS
AGPLEVADDP CEVILSATGL VARTAAESEE TPEGRRRNGR TKHDAVRAVV PATARGQVLL
ITSAGRAFKT DVLPLPVLPE QSGTVSLSGG MATAELVPLE PGERVVGLAP FGERGAGSPG
LALGTRQGVV KVCAPEWPVR ADEFEVISLR DGDEVVGATW LVDGTETLAF VSSAASLLRF
PASLVRPQGL RGGGMAGINL GAGAEVIFFG AVRADEPEQG EPMVVTSTGS GVKVSPFSLY
PAKGRATGGV RAQRFLKGES RLVVAWIGPR PVGVTKRGDP VRLPDPDQRR DGSGAAMFGP
DFVGRLLERD
//
