ID A0A3R7MIC9_PENVA Unreviewed; 1579 AA.
AC A0A3R7MIC9;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=DNA topoisomerase 2 {ECO:0000256|RuleBase:RU362094};
DE EC=5.6.2.2 {ECO:0000256|RuleBase:RU362094};
GN ORFNames=C7M84_004026 {ECO:0000313|EMBL:ROT77325.1};
OS Penaeus vannamei (Whiteleg shrimp) (Litopenaeus vannamei).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC Malacostraca; Eumalacostraca; Eucarida; Decapoda; Dendrobranchiata;
OC Penaeoidea; Penaeidae; Penaeus.
OX NCBI_TaxID=6689 {ECO:0000313|EMBL:ROT77325.1, ECO:0000313|Proteomes:UP000283509};
RN [1] {ECO:0000313|EMBL:ROT77325.1, ECO:0000313|Proteomes:UP000283509}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Muscle {ECO:0000313|EMBL:ROT77325.1};
RA Zhang X., Yuan J., Li F., Xiang J.;
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ROT77325.1, ECO:0000313|Proteomes:UP000283509}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Muscle {ECO:0000313|EMBL:ROT77325.1};
RA Sun Y., Gao Y., Yu Y.;
RT "The decoding of complex shrimp genome reveals the adaptation for benthos
RT swimmer, frequently molting mechanism and breeding impact on genome.";
RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Control of topological states of DNA by transient breakage
CC and subsequent rejoining of DNA strands. Topoisomerase II makes double-
CC strand breaks. {ECO:0000256|RuleBase:RU362094}.
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 ECO:0000256|RuleBase:RU362094};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|RuleBase:RU362094}.
CC -!- SIMILARITY: Belongs to the type II topoisomerase family.
CC {ECO:0000256|ARBA:ARBA00011080, ECO:0000256|RuleBase:RU362094}.
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:ROT77325.1}.
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DR EMBL; QCYY01001538; ROT77325.1; -; Genomic_DNA.
DR STRING; 6689.A0A3R7MIC9; -.
DR Proteomes; UP000283509; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003918; F:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) 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; cd16930; HATPase_TopII-like; 1.
DR CDD; cd00187; TOP4c; 1.
DR CDD; cd03481; TopoIIA_Trans_ScTopoIIA; 1.
DR CDD; cd03365; TOPRIM_TopoIIA; 1.
DR Gene3D; 3.30.1360.40; -; 1.
DR Gene3D; 3.30.1490.30; -; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.670; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.90.199.10; Topoisomerase II, domain 5; 1.
DR Gene3D; 1.10.268.10; Topoisomerase, domain 3; 1.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR InterPro; IPR001241; Topo_IIA.
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; IPR013759; Topo_IIA_B_C.
DR InterPro; IPR013506; Topo_IIA_bsu_dom2.
DR InterPro; IPR002205; Topo_IIA_dom_A.
DR InterPro; IPR001154; TopoII_euk.
DR InterPro; IPR018522; TopoIIA_CS.
DR InterPro; IPR031660; TOPRIM_C.
DR InterPro; IPR006171; TOPRIM_domain.
DR InterPro; IPR034157; TOPRIM_TopoII.
DR PANTHER; PTHR10169:SF38; DNA TOPOISOMERASE 2; 1.
DR PANTHER; PTHR10169; DNA TOPOISOMERASE/GYRASE; 1.
DR Pfam; PF00204; DNA_gyraseB; 1.
DR Pfam; PF00521; DNA_topoisoIV; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF01751; Toprim; 1.
DR Pfam; PF16898; TOPRIM_C; 1.
DR PRINTS; PR01158; TOPISMRASEII.
DR PRINTS; PR00418; TPI2FAMILY.
DR SMART; SM00433; TOP2c; 1.
DR SMART; SM00434; TOP4c; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR SUPFAM; SSF56719; Type II DNA topoisomerase; 1.
DR PROSITE; PS00177; TOPOISOMERASE_II; 1.
DR PROSITE; PS50880; TOPRIM; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU362094};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU362094};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|RuleBase:RU362094};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU362094};
KW Reference proteome {ECO:0000313|Proteomes:UP000283509};
KW Topoisomerase {ECO:0000256|RuleBase:RU362094}.
FT DOMAIN 457..574
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT REGION 1174..1563
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1174..1201
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1215..1247
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1272..1286
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1321..1359
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1437..1536
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1579 AA; 178930 MW; E9C7801341A717D3 CRC64;
MPAVNGTDVP NNIPAPAMVV QQAAKKGPKS VETVYQKKTQ LEHILLRPDT YIGSVEYTTE
QMWIFDPETD RIVQKEISFV PGLYKIYDEI LVNAADNKQR DPGMDTIKVE IDPENNVISV
YNNGKGIPVA MHKEEKMYVP TMIFGHLLTS SNYNDDEQKV TGGRNGYGAK LCNIFSNKFV
VETASKEYKK NFKQTWGTNM SKTSDAKIKD YGGEDFTKIT FSPDLVKFKM ESLDKDIVSL
MSRRAYDIAA STKGVKVYLN GKRVPVKNFK DYVDLYLKDK VDDADNPVKP VYENVNERWE
VAVALSDKGF QQMSFVNSIA TTKGGRHIDY VTDMIVKNLT ETLKKKNKSG VQIKPFQIKN
HMWIFVNCLI VNPTFDSQTK ENMTLQAKSF GSKCSLSDKF INNVMKCGIV EAVMTWARFK
QQAQLQSKCA NRKQNKLKGI PKLEDANDAG TKFSSDCTLI LTEGDSAKAL AVAGLGVVGR
DRYGVFPLRG KLLNVREASH SKILENAEIN NIIKILGLQY KKKYDSSEDL KSLRYGKLMI
MTDQDQDGSH IKGLLINFIH HNWPTLLRHT FMEEFITPIV KATKGKEELS FYSLPEFEEW
KKNKDNWPSY KIKYYKGLGT STSKEAKEYF NDMVRHRIRF NYGGAQDDHS IQMAFSKKAI
EQRKEWLTGW MEECKRRKEL GLPEVYLYER DTRAISYTDF VNKELVLFSN LDNERSIPCL
VDGLKPGQRK VLFTCLKRND KREVKVAQLA GSVAEHSAYH HGEASLMSTI INLAQNYIGS
NNINLLQPIG QFGTRLQGGK DHASPRYIFT MLSKLARYIF HPHDDPLLKS NFDDNQRIEP
EWYMPILPMV LVNGAEGIGT GWSTRIHNYN PREIVENLKR MLRGEEPTRM DFRGTVEELD
SQRCIVHGEI ANLGGNKIEI TELPVRVWTQ AYKETVLEGM LASTEKSPAM ITDYKEYHTD
TTVRFTVTIS EAKLGKAMEE GLHKTFKLTS SLSTNSMVLF DHNGVLRKFE AVEEILREFF
DLRLKYYSKR KQYLVGMIQA EASKLSNQAR FILEKCDGRL VIENKKKKDM IAELQRKGFD
SDPVKAWKRV QDREAALEEE EMQSESDREE VDLKGPDYDY LLGMAMWSLT KERKDELLKK
RDEKNQELEE LKKKTPDNLW LNDLDEFLNK LDEVEREERE SEEAANKKSS AGTKKVKKLK
NETMPSPFGE RVVPIIDPEM KKKAEKAAAA KESKGKRVKK EVVENDDFDD LVAANTGKSL
AARLGNSPDL IMKKAKAKKG DGMKQTKLNF KKGSPKKKKG KNPWESGSED DDDEDDIDAD
DVQPRERAAG RRTAAAKIKF QFSEDEESDS NESLHDNAGV EEIDSGPQQM SMLDDSIAQV
EPKNEVVISD TDSEFDVKPK KATVAPAPVQ DKPTASDLFD SMMGSSSPPK YESEPIIAKK
APAKKRTKGD SSSEDDSVPQ PKKKPGPKKK ATVVPDDMSD DEPKPKKKGR PKKKATGDND
MSDDEPKPKK KPGPKKTAAA KKKNDSDSDD MFDDIAPKGK AALNVSDDFN ISDVVPRERS
GRQKKVITYA LSDDEDSDY
//
