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Database: UniProt
Entry: A0A0V1N959_9BILA
LinkDB: A0A0V1N959_9BILA
Original site: A0A0V1N959_9BILA 
ID   A0A0V1N959_9BILA        Unreviewed;      1343 AA.
AC   A0A0V1N959;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=DNA topoisomerase 2-binding protein 1 {ECO:0000313|EMBL:KRZ80373.1};
GN   Name=TOPBP1 {ECO:0000313|EMBL:KRZ80373.1};
GN   ORFNames=T10_3618 {ECO:0000313|EMBL:KRZ80373.1};
OS   Trichinella papuae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=268474 {ECO:0000313|EMBL:KRZ80373.1, ECO:0000313|Proteomes:UP000054843};
RN   [1] {ECO:0000313|EMBL:KRZ80373.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS1980 {ECO:0000313|EMBL:KRZ80373.1};
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   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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:KRZ80373.1}.
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DR   EMBL; JYDO01000003; KRZ80373.1; -; Genomic_DNA.
DR   Proteomes; UP000054843; Unassembled WGS sequence.
DR   GO; GO:0005694; C:chromosome; IEA:UniProt.
DR   GO; GO:0005634; C:nucleus; IEA:UniProt.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR   CDD; cd17731; BRCT_TopBP1_rpt2_like; 1.
DR   CDD; cd17727; BRCT_TopBP1_rpt6; 1.
DR   CDD; cd17738; BRCT_TopBP1_rpt7; 1.
DR   Gene3D; 3.40.50.10190; BRCT domain; 9.
DR   InterPro; IPR001357; BRCT_dom.
DR   InterPro; IPR036420; BRCT_dom_sf.
DR   InterPro; IPR049542; TopBP1-like_BRCT0.
DR   PANTHER; PTHR13561; DNA REPLICATION REGULATOR DPB11-RELATED; 1.
DR   PANTHER; PTHR13561:SF20; DNA TOPOISOMERASE 2-BINDING PROTEIN 1; 1.
DR   Pfam; PF00533; BRCT; 2.
DR   Pfam; PF12738; PTCB-BRCT; 2.
DR   Pfam; PF16770; RTT107_BRCT_5; 1.
DR   Pfam; PF21298; TopBP1_BRCT0; 1.
DR   SMART; SM00292; BRCT; 6.
DR   SUPFAM; SSF52113; BRCT domain; 6.
DR   PROSITE; PS50172; BRCT; 5.
PE   4: Predicted;
KW   Isomerase {ECO:0000313|EMBL:KRZ80373.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054843}.
FT   DOMAIN          110..180
FT                   /note="BRCT"
FT                   /evidence="ECO:0000259|PROSITE:PS50172"
FT   DOMAIN          208..295
FT                   /note="BRCT"
FT                   /evidence="ECO:0000259|PROSITE:PS50172"
FT   DOMAIN          391..483
FT                   /note="BRCT"
FT                   /evidence="ECO:0000259|PROSITE:PS50172"
FT   DOMAIN          649..746
FT                   /note="BRCT"
FT                   /evidence="ECO:0000259|PROSITE:PS50172"
FT   DOMAIN          883..974
FT                   /note="BRCT"
FT                   /evidence="ECO:0000259|PROSITE:PS50172"
FT   REGION          745..787
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1055..1085
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        753..785
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1055..1073
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1343 AA;  151206 MW;  CBDEB61E5953165A CRC64;
     MSSSGTSVSL EERPNIVIRI VRPKLFKENA ILTLDNIYNT LCELNHTVTW ITEEECMQIE
     KHVKYVFIFY DFYGEAFEHL RYLNCRIYGP PILLFCINNC VPLPKNRIHY FCRVMEGVTI
     SCTNVERSVR DKLHDMILWM GGSVSRSMTS KCDFLIAAEV GSLKYRAACG KVPILTPEWV
     KMAWKNRYKE KFIAADPAFT ENYKCLAFTG LTITVSGFVA SERAKLRELI EKNGGIFSGI
     MKQNETSHLV TNTTKSEKYK IAKLWTDNII KIVTADWIHK SCLAGYCLHE EDFEVQDPTK
     SRKKKMVCST PNSSFTKRRL VFLEPNCSSI RSVSINSVVT SDVIDKESNS ADPSQVEETK
     VCRVTPAATQ RSIMSTIDAN SSDLFESSIT ETSSCLEGCK VWLYGFSSDL TSKLEKYVDF
     CGGVLASIDS EITHAVIGDV IDVNTVAELL KGRDLRGCFV VRGPWLLHCF KSGRKLDESE
     FVHQIYSDLL EQVESGMVES KIEQNQEQEV IVENVEISDA DPFVENLEEK SAIENIMLTY
     LADDVGEAPF GENKVDFPNE ETTISDTLIT PTATSSSSCV EMASINDQTD DNQPLLSGKS
     FFLAGFDADK EKELSESIKL FGGTLVSKFA DFAVLPWVSS VAFLPWANHT AKPLINCVIC
     LSGFSSTERD VLALGGTRAG AKIQNHMCRQ AKPDKKFLAT THLIVKIAQG NKYEAAKKWN
     IPCMTSQWLS DCIRTRMKIE ESIYQPNQHS FDRHSTSEPK SKDVMGSDSD LKSIQTEDED
     NPLKVASSKR VPSQLETVWD GSYSFVNKTA YRAKFDFGDS FQSERTLSSS LETDVLFEQN
     LGKAARFTSA VERGMDEDRP DFNVSMESSM LSNVAEGSSE GQRSYKPLSG VVIVVSSDLL
     HLQMELHQLV IQLGGFYCWH FDPSCTHFIC QGTNVEKTRE GHKAIEAGCA LVHPRWLYQC
     KIRGCRVSES GYPPTYTSDL QLPIMTPTPG PLRTKNRRCF QKWPLRTADG SDNEEPTFVL
     QKRCRVSDPA EDDLRASLKR HLRSVLDQKP AVEESFDQSF NNPSTQGNSV FEEPASKESE
     LEEESVIAPV DWDDPNQRIA RERIGSLLKP QNEPTQQSTF DSSQPVNQNI LFQFTSLNSQ
     QKQIVLSAFS ELKVAYILDS DFYPSCTHVI AGTLGRTEKA LCALATGKWI LTFAYVEACR
     QHGFLVEEQE YEWAKFLRDS GDDVDVGMLD VAEAAVRWRK KIQREQRYAF DGWIAFIAAD
     SAKQKSLERL ICFGGGKVFT KVEDAPKGCF AFVDVNSLNF TKDFYGKLIQ QGLKCFKVEY
     ISGYLLNEPF EEDLYIIDET LWS
//
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