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Entry: A0A3B0CDM4_9FLAO
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ID   A0A3B0CDM4_9FLAO        Unreviewed;       826 AA.
AC   A0A3B0CDM4;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=DNA topoisomerase 1 {ECO:0000256|HAMAP-Rule:MF_00952};
DE            EC=5.6.2.1 {ECO:0000256|HAMAP-Rule:MF_00952};
DE   AltName: Full=DNA topoisomerase I {ECO:0000256|HAMAP-Rule:MF_00952};
GN   Name=topA {ECO:0000256|HAMAP-Rule:MF_00952,
GN   ECO:0000313|EMBL:RKN83400.1};
GN   ORFNames=D7Z94_06145 {ECO:0000313|EMBL:RKN83400.1};
OS   Ulvibacterium marinum.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Ulvibacterium.
OX   NCBI_TaxID=2419782 {ECO:0000313|EMBL:RKN83400.1, ECO:0000313|Proteomes:UP000276603};
RN   [1] {ECO:0000313|EMBL:RKN83400.1, ECO:0000313|Proteomes:UP000276603}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCMM003 {ECO:0000313|EMBL:RKN83400.1,
RC   ECO:0000313|Proteomes:UP000276603};
RA   Zhang Z.;
RT   "Ulvibacterium marinum gen. nov., sp. nov., a novel marine bacterium of the
RT   family Flavobacteriaceae, isolated from a culture of the green alga Ulva
RT   prolifera.";
RL   Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Releases the supercoiling and torsional tension of DNA, which
CC       is introduced during the DNA replication and transcription, by
CC       transiently cleaving and rejoining one strand of the DNA duplex.
CC       Introduces a single-strand break via transesterification at a target
CC       site in duplex DNA. The scissile phosphodiester is attacked by the
CC       catalytic tyrosine of the enzyme, resulting in the formation of a DNA-
CC       (5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH
CC       DNA strand. The free DNA strand then undergoes passage around the
CC       unbroken strand, thus removing DNA supercoils. Finally, in the
CC       religation step, the DNA 3'-OH attacks the covalent intermediate to
CC       expel the active-site tyrosine and restore the DNA phosphodiester
CC       backbone. {ECO:0000256|HAMAP-Rule:MF_00952}.
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, ECO:0000256|HAMAP-
CC         Rule:MF_00952};
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00952}.
CC   -!- SIMILARITY: Belongs to the type IA topoisomerase family.
CC       {ECO:0000256|ARBA:ARBA00009446, ECO:0000256|HAMAP-Rule:MF_00952}.
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:RKN83400.1}.
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DR   EMBL; RBCJ01000001; RKN83400.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3B0CDM4; -.
DR   OrthoDB; 9804262at2; -.
DR   Proteomes; UP000276603; Unassembled WGS sequence.
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-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-UniRule.
DR   CDD; cd00186; TOP1Ac; 1.
DR   CDD; cd03363; TOPRIM_TopoIA_TopoI; 1.
DR   Gene3D; 3.40.50.140; -; 1.
DR   Gene3D; 1.10.460.10; Topoisomerase I, domain 2; 2.
DR   Gene3D; 2.70.20.10; Topoisomerase I, domain 3; 1.
DR   Gene3D; 1.10.290.10; Topoisomerase I, domain 4; 1.
DR   HAMAP; MF_00952; Topoisom_1_prok; 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; IPR005733; TopoI_bac-type.
DR   InterPro; IPR028612; Topoisom_1_IA.
DR   InterPro; IPR025589; Toprim_C_rpt.
DR   InterPro; IPR006171; TOPRIM_domain.
DR   InterPro; IPR034149; TOPRIM_TopoI.
DR   NCBIfam; TIGR01051; topA_bact; 1.
DR   PANTHER; PTHR42785; DNA TOPOISOMERASE, TYPE IA, CORE; 1.
DR   PANTHER; PTHR42785:SF1; OMEGA-PROTEIN; 1.
DR   Pfam; PF01131; Topoisom_bac; 2.
DR   Pfam; PF01751; Toprim; 1.
DR   Pfam; PF13368; Toprim_C_rpt; 3.
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   PROSITE; PS00396; TOPOISOMERASE_I_PROK; 1.
DR   PROSITE; PS50880; TOPRIM; 1.
PE   3: Inferred from homology;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW   Rule:MF_00952};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_00952};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000276603};
KW   Topoisomerase {ECO:0000256|ARBA:ARBA00023029, ECO:0000256|HAMAP-
KW   Rule:MF_00952}.
FT   DOMAIN          3..113
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
FT   REGION          163..168
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT   ACT_SITE        284
FT                   /note="O-(5'-phospho-DNA)-tyrosine intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT   SITE            33
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT   SITE            139
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT   SITE            140
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT   SITE            143
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT   SITE            148
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT   SITE            155
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT   SITE            286
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
FT   SITE            475
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00952"
SQ   SEQUENCE   826 AA;  93306 MW;  8B13CFE373F19D48 CRC64;
     MAKNLVIVES PAKAKTIEKF LGKDYKVESS FGHIADLPSK ELGVDVDNNF EPKYIVDKEK
     KALVKKLKDL AKKADTIWLA SDEDREGEAI SWHLTETLDL DKKKTKRIVF NSITKSAIQK
     AIENPRDINY NLVNAQQARR VLDRLVGYQL SPVLWKKIKP GLSAGRVQSV AVRLIVERER
     DIEVFKPEAS FKISAEFKTA DGGVFMAKLN KTFASKDEAG AFLKKNLGAI FSVGNLDKKP
     AKKSPSAPFT TSTLQQEASR KLYFSVGRTM QVAQRLYEAG LITYMRTDSV NLSGEAIAMA
     KEAIIENYGN EYSSVRNFKG KSKGAQEAHE AIRPTNITNQ SPSLERDQSK LYELIWKRTI
     ASQMSDAQLE RTNVKIKSNT HGEEFTANGE VIKFDGFLKV YMEGIDDEDR AEEQEGMLPA
     MKEGDVLDNT YISATERFTR PPYRFTEASL VKKLEELGIG RPSTYAPTIS TIQNRGYVEK
     GTIEGTERNY VQLVLDSGKI QEKKLAETVG SDKGKLVPTD IGMIVNDFLV SHFANILDYN
     FTAKVEENFD EIAEGEEDWQ KIMQDFYKDF RPNVEHVEEN ADRASGERVL GTDPDTGRQV
     AVRLGRFGPM VQIGTVEEEE KPLFASLLPD QSLNTITYEE AMELFQLPRK LGAYKGEDIE
     ASVGRYGPYV RFGKKFVSLE KGESAFDVDL ERAIELIKEK EKADAPIATY EGKEVTKGKG
     RFGPFIKWDG IFINVNKKYD FENLSQENIE ELIEVKKQKE IDKLIQEWPE EGIRIEKARW
     GRHNIIKGRT KVELAKTVDV SKIKLEEAKE LLAKKAPKKR SKAKKK
//
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