ID A0A1Q9CKT9_SYMMI Unreviewed; 1247 AA.
AC A0A1Q9CKT9;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=DNA topoisomerase {ECO:0000256|RuleBase:RU362092};
DE EC=5.6.2.1 {ECO:0000256|RuleBase:RU362092};
GN Name=pyrBI {ECO:0000313|EMBL:OLP83541.1};
GN ORFNames=AK812_SmicGene35680 {ECO:0000313|EMBL:OLP83541.1};
OS Symbiodinium microadriaticum (Dinoflagellate) (Zooxanthella
OS microadriatica).
OC Eukaryota; Sar; Alveolata; Dinophyceae; Suessiales; Symbiodiniaceae;
OC Symbiodinium.
OX NCBI_TaxID=2951 {ECO:0000313|EMBL:OLP83541.1, ECO:0000313|Proteomes:UP000186817};
RN [1] {ECO:0000313|EMBL:OLP83541.1, ECO:0000313|Proteomes:UP000186817}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP2467 {ECO:0000313|EMBL:OLP83541.1,
RC ECO:0000313|Proteomes:UP000186817};
RA Aranda M., Li Y., Liew Y.J., Baumgarten S., Simakov O., Wilson M., Piel J.,
RA Ashoor H., Bougouffa S., Bajic V.B., Ryu T., Ravasi T., Bayer T.,
RA Micklem G., Kim H., Bhak J., Lajeunesse T.C., Voolstra C.R.;
RT "Genome analysis of coral dinoflagellate symbionts highlights evolutionary
RT adaptations to a symbiotic lifestyle.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Introduces a single-strand break via transesterification at a
CC target site in duplex DNA. Releases the supercoiling and torsional
CC tension of DNA introduced during the DNA replication and transcription
CC by transiently cleaving and rejoining one strand of the DNA duplex. The
CC scissile phosphodiester is attacked by the catalytic tyrosine of the
CC enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme
CC intermediate and the expulsion of a 3'-OH DNA strand.
CC {ECO:0000256|RuleBase:RU362092}.
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|RuleBase:RU362092};
CC -!- SIMILARITY: Belongs to the type IA topoisomerase family.
CC {ECO:0000256|RuleBase:RU362092}.
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:OLP83541.1}.
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DR EMBL; LSRX01001109; OLP83541.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q9CKT9; -.
DR OrthoDB; 309at2759; -.
DR Proteomes; UP000186817; Unassembled WGS sequence.
DR GO; GO:0016597; F:amino acid binding; IEA:InterPro.
DR GO; GO:0016743; F:carboxyl- or carbamoyltransferase activity; 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:0006520; P:amino acid metabolic process; IEA:InterPro.
DR GO; GO:0006265; P:DNA topological change; IEA:InterPro.
DR CDD; cd01028; TOPRIM_TopoIA; 1.
DR Gene3D; 3.40.50.140; -; 1.
DR Gene3D; 3.30.70.140; Aspartate carbamoyltransferase regulatory subunit, N-terminal domain; 1.
DR Gene3D; 3.40.50.1370; Aspartate/ornithine carbamoyltransferase; 2.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR Gene3D; 1.10.460.10; Topoisomerase I, domain 2; 1.
DR InterPro; IPR006132; Asp/Orn_carbamoyltranf_P-bd.
DR InterPro; IPR006130; Asp/Orn_carbamoylTrfase.
DR InterPro; IPR036901; Asp/Orn_carbamoylTrfase_sf.
DR InterPro; IPR036793; Asp_carbatrfase_reg_N_sf.
DR InterPro; IPR001466; Beta-lactam-related.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR000380; Topo_IA.
DR InterPro; IPR003601; Topo_IA_2.
DR InterPro; IPR013497; Topo_IA_cen.
DR InterPro; IPR013824; Topo_IA_cen_sub1.
DR InterPro; IPR023405; Topo_IA_core_domain.
DR InterPro; IPR006171; TOPRIM_domain.
DR PANTHER; PTHR11390:SF20; DNA TOPOISOMERASE 3-BETA-1; 1.
DR PANTHER; PTHR11390; PROKARYOTIC DNA TOPOISOMERASE; 1.
DR Pfam; PF00144; Beta-lactamase; 1.
DR Pfam; PF02729; OTCace_N; 1.
DR Pfam; PF01131; Topoisom_bac; 1.
DR Pfam; PF01751; Toprim; 1.
DR SMART; SM00436; TOP1Bc; 1.
DR SMART; SM00493; TOPRIM; 1.
DR SUPFAM; SSF54893; Aspartate carbamoyltransferase, Regulatory-chain, N-terminal domain; 1.
DR SUPFAM; SSF53671; Aspartate/ornithine carbamoyltransferase; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF56712; Prokaryotic type I DNA topoisomerase; 1.
DR PROSITE; PS00097; CARBAMOYLTRANSFERASE; 1.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000256|RuleBase:RU362092};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU362092};
KW Reference proteome {ECO:0000313|Proteomes:UP000186817};
KW Topoisomerase {ECO:0000256|RuleBase:RU362092};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 484..588
FT /note="Toprim"
FT /evidence="ECO:0000259|SMART:SM00493"
FT DOMAIN 602..688
FT /note="DNA topoisomerase type IA"
FT /evidence="ECO:0000259|SMART:SM00436"
SQ SEQUENCE 1247 AA; 138781 MW; 58764C36C00544DF CRC64;
MIGGELLVLM VAEKPSIAAA LTEALCPQRS GASLSPQLGV VGGLVRNSCK ELAQAAVGSY
RREGASSKTA AVSPPAVRWG YASITKTLVG VVMQMLMANE SLPRISWNDK LHQWLPLAAG
TAYENASLLD VASHTACLIS EGAPRSQELV LAAWAQYTVG GIPASRAVYV NNSLHHPPLP
NCTPELNTEM TYVHFDGVEI LALVEETISG LDFRALTKTL IFDPLGMSTA EVVDGNAAGG
LRSTLTDLGV YGQWLLDGYN NQQDAVAKTG LTHQDFVDLL SPIHKHGVEQ TYGRTFRIYS
FDGRRAAGHG GCLGASFDVL LDDNLVMVLA FTPEDAAWKT CDLTDHWAAI LWPAVYSMYS
AFTACDGRPS HLCNATAVDS TALTCKLTDN FNLDSSTLDV PFTKTSCREE DFADRVTESL
STYLATYVER WGKAFVMLDD CQWSIVSYWP DPCVSLRESF KLCAENNWDC GVYMVGNHTY
DPSDFPCVGR RHAKFYQYPP LCRFRVTATT GHVYSLDFSQ EYNNWETHSP DALFSATTVR
TYDGRANMPA HIAAEAKDCD ILVLWLDCDR EGENICFEVL ELALPHMRPA PVGAFPDAYK
GCVYRARFSS LAPQDLQAAM MQLAQPNRDE ALSVDARQEL QTMYFRKHFG RQLGKQMVTY
GPCQIPTLWF CVHRHVAIVD FVPEPYWQLT ATVSAGHGSF QAQCDQGRIW NEAEASKAMA
GGNPEPVQDT TLDGGLAGRT IHEVRDLNMQ EQMYLYERTR RFKARKRCSA PEKAEVAEGP
ALCEIQDDAL EERVDNPDST VYLIFMEGST RTRESLRNAA VYHGVKVNEF QAETSSFQKN
ETITDTMKML SVYSTQRSVF VIRSVLEGVC SWLKTAMGAH AASMGVPAPS FLNAGDGLFT
HPIGAPRQRK ACSAVVGRRL SSILHSNKRQ VEGLKIFQKV TVDLVAPEMF GYPVEYRNRM
RENGFEVREF ASVEEYLENA AGSIADVWYF YKPQFSKCGD LTAMRLSELR TQVSFREEFL
PKLPKGVRFF QTLPRDKEFP IIPLTLDSTP LNGWEVRLSQ DAHHRDPERA RAGGPMPISD
GVVIDHVGLG PDSAACWHGL QKGNPGNFKG ILTLPRYDYQ QLRVQDVKML ASVAPGCTFN
CVAGSKVVAK YRLQVPERIY NLPNISCKNA LCMSNPKNKQ FECVAYFERV PFYTTSVLPD
CAESEFLYVC RWCRWPHVYE DIWDDLRSEQ KVDRKVRIHG GALYAAA
//
