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Database: UniProt
Entry: A0A0K8JGQ7_9FIRM
LinkDB: A0A0K8JGQ7_9FIRM
Original site: A0A0K8JGQ7_9FIRM 
ID   A0A0K8JGQ7_9FIRM        Unreviewed;       718 AA.
AC   A0A0K8JGQ7;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=DNA topoisomerase {ECO:0000256|ARBA:ARBA00012891};
DE            EC=5.6.2.1 {ECO:0000256|ARBA:ARBA00012891};
DE   AltName: Full=Omega-protein {ECO:0000256|ARBA:ARBA00032877};
DE   AltName: Full=Relaxing enzyme {ECO:0000256|ARBA:ARBA00032235};
DE   AltName: Full=Swivelase {ECO:0000256|ARBA:ARBA00030003};
DE   AltName: Full=Untwisting enzyme {ECO:0000256|ARBA:ARBA00031985};
GN   ORFNames=P22_2613 {ECO:0000313|EMBL:CUH96523.1};
OS   Propionispora sp. 2/2-37.
OC   Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC   Propionispora.
OX   NCBI_TaxID=1677858 {ECO:0000313|EMBL:CUH96523.1, ECO:0000313|Proteomes:UP000041641};
RN   [1] {ECO:0000313|EMBL:CUH96523.1, ECO:0000313|Proteomes:UP000041641}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2/2 {ECO:0000313|EMBL:CUH96523.1};
RA   Jackson K.R., Lunt B.L., Fisher J.N.B., Gardner A.V., Bailey M.E.,
RA   Deus L.M., Earl A.S., Gibby P.D., Hartmann K.A., Liu J.E., Manci A.M.,
RA   Nielsen D.A., Solomon M.B., Breakwell D.P., Burnett S.H., Grose J.H.;
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP-independent breakage of single-stranded DNA, followed by
CC         passage and rejoining.; EC=5.6.2.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00000213};
CC   -!- SIMILARITY: Belongs to the type IA topoisomerase family.
CC       {ECO:0000256|ARBA:ARBA00009446}.
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DR   EMBL; CYSP01000011; CUH96523.1; -; Genomic_DNA.
DR   RefSeq; WP_054260664.1; NZ_CYSP01000011.1.
DR   AlphaFoldDB; A0A0K8JGQ7; -.
DR   STRING; 1677858.P22_2613; -.
DR   OrthoDB; 9803554at2; -.
DR   Proteomes; UP000041641; Unassembled WGS sequence.
DR   GO; GO:0005694; C:chromosome; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003917; F:DNA topoisomerase type I (single strand cut, ATP-independent) activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006265; P:DNA topological change; IEA:InterPro.
DR   CDD; cd00186; TOP1Ac; 1.
DR   CDD; cd03362; TOPRIM_TopoIA_TopoIII; 1.
DR   Gene3D; 3.40.50.140; -; 1.
DR   Gene3D; 3.30.65.10; Bacterial Topoisomerase I, domain 1; 2.
DR   Gene3D; 1.10.460.10; Topoisomerase I, domain 2; 1.
DR   Gene3D; 2.70.20.10; Topoisomerase I, domain 3; 1.
DR   Gene3D; 1.10.290.10; Topoisomerase I, domain 4; 1.
DR   InterPro; IPR000380; Topo_IA.
DR   InterPro; IPR003601; Topo_IA_2.
DR   InterPro; IPR023406; Topo_IA_AS.
DR   InterPro; IPR013497; Topo_IA_cen.
DR   InterPro; IPR013824; Topo_IA_cen_sub1.
DR   InterPro; IPR013825; Topo_IA_cen_sub2.
DR   InterPro; IPR013826; Topo_IA_cen_sub3.
DR   InterPro; IPR023405; Topo_IA_core_domain.
DR   InterPro; IPR003602; Topo_IA_DNA-bd_dom.
DR   InterPro; IPR013498; Topo_IA_Znf.
DR   InterPro; IPR005738; TopoIII.
DR   InterPro; IPR006171; TOPRIM_domain.
DR   InterPro; IPR034144; TOPRIM_TopoIII.
DR   NCBIfam; TIGR01056; topB; 1.
DR   PANTHER; PTHR11390:SF21; DNA TOPOISOMERASE 3-ALPHA; 1.
DR   PANTHER; PTHR11390; PROKARYOTIC DNA TOPOISOMERASE; 1.
DR   Pfam; PF01131; Topoisom_bac; 1.
DR   Pfam; PF01751; Toprim; 1.
DR   Pfam; PF01396; zf-C4_Topoisom; 2.
DR   PRINTS; PR00417; PRTPISMRASEI.
DR   SMART; SM00437; TOP1Ac; 1.
DR   SMART; SM00436; TOP1Bc; 1.
DR   SMART; SM00493; TOPRIM; 1.
DR   SUPFAM; SSF56712; Prokaryotic type I DNA topoisomerase; 1.
DR   SUPFAM; SSF57783; Zinc beta-ribbon; 2.
DR   PROSITE; PS00396; TOPOISOMERASE_I_PROK; 1.
PE   3: Inferred from homology;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000041641};
KW   Topoisomerase {ECO:0000256|ARBA:ARBA00023029};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          1..123
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|SMART:SM00493"
FT   DOMAIN          123..218
FT                   /note="DNA topoisomerase type IA"
FT                   /evidence="ECO:0000259|SMART:SM00436"
FT   DOMAIN          274..558
FT                   /note="DNA topoisomerase type IA DNA-binding"
FT                   /evidence="ECO:0000259|SMART:SM00437"
SQ   SEQUENCE   718 AA;  79852 MW;  2C71465988E87C4F CRC64;
     MRLFIAEKPS MGAEIAKCLP GPLIRRDGYI TTGAGIVTWG YGHILRQAEP EEYDARYGKW
     RLEDLPIIPA EWKLVIAESS RKQFEIVRGL IEQASEIVHA GDPDREGQLL IDEVLDYVQN
     TKPVQRILLH ALDEKSIKKA IANLRDNRDF SNLKQSALAR SRADWLIGMN LSRVYTLAAQ
     QAGHRVTLPV GRVKTPTLAL VVRREREIAN FKPADYFTVK ADFKHENGLF TAYWKPAEAQ
     PGLDSEGRLA DKTILEALTG KLSGAAEAAR IAACDTAEKR EPQRLPLSLS ALQVIAGKRY
     GYNPQNVLDT AQKLYEKKLT SYPRSDCDFL PESQHSDAGV IVGNLQAIAQ PELAGWSAGA
     DTAIRSRAWN DKKITAHHAI IPTVEPCDFS RLSDMEKHIY FLIAQAYLAQ FYPVHLYSQT
     KIEVTYAGET FTASGRIVRE AGWKALYAAE AEEKKEEEES LLPVMAEGDP ADFVQVTADK
     KTTRPPLRFT AATLLAAMKE IHKYVKNPEL KKQLKDVSGI GTEATRATMI KELGQRGFLK
     EEGKKRYLVP TDFAYLLIDA LPDDLTYPDS TALWERILYD MTNGQASLSG FLAQQIQFTQ
     SICRTAARIS FPLQGEHPCP QCGQGVLQLK KGRNGNFWGC SRYPACKASY DDQNGQPQKP
     KYSCPRCKQG ALQLINGKNG AFWGCTRYPS CRVTFNDNQG VPAALLPPDG KTREADGG
//
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