ID A0A0V0RM18_9BILA Unreviewed; 1083 AA.
AC A0A0V0RM18;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=DNA topoisomerase (ATP-hydrolyzing) {ECO:0000256|ARBA:ARBA00012895};
DE EC=5.6.2.2 {ECO:0000256|ARBA:ARBA00012895};
GN ORFNames=T07_3873 {ECO:0000313|EMBL:KRX15502.1};
OS Trichinella nelsoni.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6336 {ECO:0000313|EMBL:KRX15502.1, ECO:0000313|Proteomes:UP000054630};
RN [1] {ECO:0000313|EMBL:KRX15502.1, ECO:0000313|Proteomes:UP000054630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS37 {ECO:0000313|EMBL:KRX15502.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the TOP6A family.
CC {ECO:0000256|ARBA:ARBA00006559}.
CC -!- SIMILARITY: Belongs to the peptidase M14 family.
CC {ECO:0000256|ARBA:ARBA00005988}.
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:KRX15502.1}.
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DR EMBL; JYDL01000129; KRX15502.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0RM18; -.
DR Proteomes; UP000054630; Unassembled WGS sequence.
DR GO; GO:0005694; C:chromosome; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003918; F:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity; IEA:InterPro.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006259; P:DNA metabolic process; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd03860; M14_CP_A-B_like; 1.
DR CDD; cd00223; TOPRIM_TopoIIB_SPO; 1.
DR Gene3D; 3.40.1360.10; -; 1.
DR Gene3D; 3.30.70.340; Metallocarboxypeptidase-like; 1.
DR Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR029033; His_PPase_superfam.
DR InterPro; IPR036990; M14A-like_propep.
DR InterPro; IPR003146; M14A_act_pep.
DR InterPro; IPR000834; Peptidase_M14.
DR InterPro; IPR002815; Spo11/TopoVI_A.
DR InterPro; IPR013049; Spo11/TopoVI_A_N.
DR InterPro; IPR036078; Spo11/TopoVI_A_sf.
DR InterPro; IPR034136; TOPRIM_Topo6A/Spo11.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR PANTHER; PTHR11705:SF91; CARBOXYPEPTIDASE A1 (PANCREATIC)-RELATED; 1.
DR PANTHER; PTHR11705; PROTEASE FAMILY M14 CARBOXYPEPTIDASE A,B; 1.
DR Pfam; PF00246; Peptidase_M14; 2.
DR Pfam; PF02244; Propep_M14; 1.
DR Pfam; PF21180; TOP6A-Spo11_Toprim; 1.
DR Pfam; PF04406; TP6A_N; 1.
DR PRINTS; PR01550; TOP6AFAMILY.
DR SMART; SM00631; Zn_pept; 1.
DR SUPFAM; SSF56726; DNA topoisomerase IV, alpha subunit; 1.
DR SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
DR SUPFAM; SSF54897; Protease propeptides/inhibitors; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS00132; CARBOXYPEPT_ZN_1; 1.
DR PROSITE; PS00133; CARBOXYPEPT_ZN_2; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645,
KW ECO:0000313|EMBL:KRX15502.1};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000054630};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Topoisomerase {ECO:0000256|ARBA:ARBA00023029};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..1083
FT /note="DNA topoisomerase (ATP-hydrolyzing)"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006868027"
FT DOMAIN 174..196
FT /note="Peptidase M14 carboxypeptidase A"
FT /evidence="ECO:0000259|PROSITE:PS00132"
FT DOMAIN 321..331
FT /note="Peptidase M14 carboxypeptidase A"
FT /evidence="ECO:0000259|PROSITE:PS00133"
SQ SEQUENCE 1083 AA; 123836 MW; C0BBC9AFDFE6F7BC CRC64;
MLQLVSLIFP FFMLITATAD KENYTMQSNA VYKVMRTVPT NESQLKFLQI MYQHADGDQI
DFWRPPAFLN STVDIMVNDM SMEKFLFQCE EHNISLSISI PDVEKSRGRV RRFNYLTTPY
FDISVYHSYS EIQNYMRNLE KQYPHIAKVH TIGYTHENRE INLIQIGRFY SSQPAIWIDA
GIHAREWIAP STALYIINYL VTRYDFDMEV QKYVNGLTWY ILPVVNPDGY EFSRSSLNPR
VRLWRKNRSP ANCQPFKNSY CCRGVDLNRN FDFKWNQQGG SQDPCQETYS GRSAFSEPET
QAIERFILQR ADQLGAFLTL HSYSQIWMYP YGNQRYSYPK DVHDLNTVCR VILDPASGGS
EDWAKAVAGI KYSFLVELRP EEDNQDGFIL DESHIIPTGK ETLEGIKEVA MVLLPGNHNS
YFPNTAASSV CQDFHPMCKI WAVFGACLND TEVRRLCVKS CELCSELDDQ DEKLFIAIGA
AESAKDIYGD ADWLPGMEDK GALSSISRII SKMKSQSFPL PENSVCQIGN ANLPRTLMWR
KGGKAAWLAD PPLTIVGCNT AKMYAEGLVS VNVLNAQLLG NCVYAAPNFR CVQTADIILK
VVDPSGRIKI RIEPKLEADS QHMDKNPWWH MKIDQFSAHN IHRVDISHKS KKRMKDFSQR
NDILDEIRRN HDGNVALFIV SDWNIRDLCY TICNCNISSE NNAVCENRAV SLLRPRPALY
LPRAKEYALE MTTRNCHMFP IVLCLLSESY SLLSNSQYCT KRNLYYKHRY LFRSEGDLDR
AIRAICKILV TPRYKFNILS SPKGLVLGDL VFQLGNAEIV DCNSISTIPT RSDEFQVLTT
SATFILIVEK DSIFEKLAME KANSVLRSAI LITAKGYPDF PTRLFLRKLY DYLKLPMFAL
MDADPCGIEI FLTYKYGPMN VSYESGVNVL LPWMKWIGVY PSEISSLNLS DTQKLMLGTR
ERKLIYSLLN RFEASGDHFL ISQLHELNKI DFHSSTCEQA RIILLARCIS IHCSPLASRR
VEPRGRGIAT ALIKFYASPS GEKRNCESNK DLIKSISSVQ RGPNCFDLET QKYLADLSEV
NIL
//
