ID A0A091VY07_OPIHO Unreviewed; 995 AA.
AC A0A091VY07;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 28-JUN-2023, entry version 33.
DE RecName: Full=DNA topoisomerase {ECO:0000256|ARBA:ARBA00012891, ECO:0000256|RuleBase:RU362092};
DE EC=5.6.2.1 {ECO:0000256|ARBA:ARBA00012891, ECO:0000256|RuleBase:RU362092};
DE Flags: Fragment;
GN ORFNames=N306_14337 {ECO:0000313|EMBL:KFR08069.1};
OS Opisthocomus hoazin (Hoatzin) (Phasianus hoazin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Opisthocomiformes; Opisthocomidae;
OC Opisthocomus.
OX NCBI_TaxID=30419 {ECO:0000313|EMBL:KFR08069.1, ECO:0000313|Proteomes:UP000053605};
RN [1] {ECO:0000313|EMBL:KFR08069.1, ECO:0000313|Proteomes:UP000053605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N306 {ECO:0000313|EMBL:KFR08069.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) 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|ARBA:ARBA00000213,
CC ECO:0000256|RuleBase:RU362092};
CC -!- SIMILARITY: Belongs to the type IA topoisomerase family.
CC {ECO:0000256|ARBA:ARBA00009446, ECO:0000256|RuleBase:RU362092}.
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DR EMBL; KK734455; KFR08069.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091VY07; -.
DR STRING; 30419.A0A091VY07; -.
DR PhylomeDB; A0A091VY07; -.
DR Proteomes; UP000053605; 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:0008270; F:zinc ion binding; IEA:InterPro.
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; 1.
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; IPR006171; TOPRIM_domain.
DR InterPro; IPR034144; TOPRIM_TopoIII.
DR InterPro; IPR010666; Znf_GRF.
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; 1.
DR Pfam; PF06839; zf-GRF; 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; 1.
DR PROSITE; PS00396; TOPOISOMERASE_I_PROK; 1.
DR PROSITE; PS50880; TOPRIM; 1.
DR PROSITE; PS51999; ZF_GRF; 2.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU362092};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU362092};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000053605};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029,
KW ECO:0000256|RuleBase:RU362092}; Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU01343}.
FT DOMAIN 17..161
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT DOMAIN 805..844
FT /note="GRF-type"
FT /evidence="ECO:0000259|PROSITE:PS51999"
FT DOMAIN 895..937
FT /note="GRF-type"
FT /evidence="ECO:0000259|PROSITE:PS51999"
FT REGION 761..799
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 846..892
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 956..976
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 761..788
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFR08069.1"
FT NON_TER 995
FT /evidence="ECO:0000313|EMBL:KFR08069.1"
SQ SEQUENCE 995 AA; 111078 MW; 4D1AEDA8D1E8777C CRC64;
RLFSRAAEDT ALQGIRRVLC VAEKNDAARG IADLLSSSRM RRREGFSKFN KIYEYDYQMF
GQNVTMVMTS VSGHLLAHDF KLPFRKWHSC NPLALFDAEI EKYCPENYVD IKRTLEREVR
QCQALVIWTD CDREGENIGF EIIHVCKAVK PNLRVFRARF SEITLHAVRT ACENLTQPDQ
KTSDAVDVRQ ELDLRIGAAF TRFQTLRLRK IFPDILADQL ISYGSCQFPT LGFVVERFKA
IQAFVPEAFY KIKVTHDHED GSVVFNWKRN RLFNHTACLV LYQMCMEDPV ATVVEVGSKP
KSKWRPLPLD TVELEKLASR KLKINAKETM RIAEKLYTQG FISYPRTETN IFPKELNLSA
LVQQQTQDPN WGAFAQRILD QGGPTPRSGT KSDQAHPPIH PTKYTANLQG SEQRLYEFIV
RHFLACCSQD AKGQETTVEI DIANERFIAQ GLMILARNYL EVYPYEKWSD KVIPLYQKGS
RFQPTTVEMV DGETSPPLLL TEADLIALME KHGIGTDATH AEHIETIKTR MYVGLTADQR
FLPGHLGMGL VEGYDSMGYE MSKPDLRAEL EADLKLICEG KKDKSAVLQQ QVQKYKHVFI
EAVARANKLD QALAQYFGEA TEIAEQEEVF PATPVSVRKC PQCNNDMVLK AKKNGGFYLS
CTGYPACKTA VWFPDFVLDV ARDESVCAVC EPHPVHRLKF KFKRGSVPPV MPLEFVGCIG
GCDEMLKELL DLKYLHRSSQ PASSASQQAN HLQVNNSFNR ASGENRHARG TTNLAPGHLL
SSSKTRTPRP APAAAPDNGN NAVVCNCGNE ALLLTVRKEG PNQGRQFYKC SASTCNFFLW
ADEQSEDRGN AAPRGSALPQ PFAGRGPAGF QRPGGGRGPE LFGSNSSDSG GGTVCKCDQP
AVTRTVQKDG PNKGRQFHTC SKPREQQCGF FQWADENVAP GKAGLGVRCK GRRLGLGSKA
KRPSSLSSGA AAKKPRTCSI CHQSGHTRKT CPQNH
//
