ID E9GFR3_DAPPU Unreviewed; 1535 AA.
AC E9GFR3;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=Tower domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=DAPPUDRAFT_303344 {ECO:0000313|EMBL:EFX81680.1};
OS Daphnia pulex (Water flea).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Branchiopoda;
OC Diplostraca; Cladocera; Anomopoda; Daphniidae; Daphnia.
OX NCBI_TaxID=6669 {ECO:0000313|EMBL:EFX81680.1, ECO:0000313|Proteomes:UP000000305};
RN [1] {ECO:0000313|EMBL:EFX81680.1, ECO:0000313|Proteomes:UP000000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21292972; DOI=10.1126/science.1197761;
RA Colbourne J.K., Pfrender M.E., Gilbert D., Thomas W.K., Tucker A.,
RA Oakley T.H., Tokishita S., Aerts A., Arnold G.J., Basu M.K., Bauer D.J.,
RA Caceres C.E., Carmel L., Casola C., Choi J.H., Detter J.C., Dong Q.,
RA Dusheyko S., Eads B.D., Frohlich T., Geiler-Samerotte K.A., Gerlach D.,
RA Hatcher P., Jogdeo S., Krijgsveld J., Kriventseva E.V., Kultz D.,
RA Laforsch C., Lindquist E., Lopez J., Manak J.R., Muller J., Pangilinan J.,
RA Patwardhan R.P., Pitluck S., Pritham E.J., Rechtsteiner A., Rho M.,
RA Rogozin I.B., Sakarya O., Salamov A., Schaack S., Shapiro H., Shiga Y.,
RA Skalitzky C., Smith Z., Souvorov A., Sung W., Tang Z., Tsuchiya D., Tu H.,
RA Vos H., Wang M., Wolf Y.I., Yamagata H., Yamada T., Ye Y., Shaw J.R.,
RA Andrews J., Crease T.J., Tang H., Lucas S.M., Robertson H.M., Bork P.,
RA Koonin E.V., Zdobnov E.M., Grigoriev I.V., Lynch M., Boore J.L.;
RT "The ecoresponsive genome of Daphnia pulex.";
RL Science 331:555-561(2011).
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DR EMBL; GL732542; EFX81680.1; -; Genomic_DNA.
DR STRING; 6669.E9GFR3; -.
DR EnsemblMetazoa; EFX81680; EFX81680; DAPPUDRAFT_303344.
DR KEGG; dpx:DAPPUDRAFT_303344; -.
DR eggNOG; KOG4751; Eukaryota.
DR HOGENOM; CLU_247064_0_0_1; -.
DR InParanoid; E9GFR3; -.
DR OMA; FRCSDFY; -.
DR PhylomeDB; E9GFR3; -.
DR Proteomes; UP000000305; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IBA:GO_Central.
DR CDD; cd04493; BRCA2DBD_OB1; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 3.
DR InterPro; IPR015525; BRCA2.
DR InterPro; IPR015252; BRCA2_hlx.
DR InterPro; IPR036315; BRCA2_hlx_sf.
DR InterPro; IPR015187; BRCA2_OB_1.
DR InterPro; IPR015188; BRCA2_OB_3.
DR InterPro; IPR002093; BRCA2_repeat.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR PANTHER; PTHR11289:SF0; BREAST CANCER TYPE 2 SUSCEPTIBILITY PROTEIN; 1.
DR PANTHER; PTHR11289; BREAST CANCER TYPE 2 SUSCEPTIBILITY PROTEIN BRCA2; 1.
DR Pfam; PF09169; BRCA-2_helical; 1.
DR Pfam; PF09103; BRCA-2_OB1; 1.
DR Pfam; PF09104; BRCA-2_OB3; 1.
DR Pfam; PF00634; BRCA2; 2.
DR Pfam; PF21318; BRCA2DBD_OB2; 1.
DR SUPFAM; SSF81872; BRCA2 helical domain; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 3.
DR PROSITE; PS50138; BRCA2_REPEAT; 5.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA recombination {ECO:0000256|ARBA:ARBA00023172};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Reference proteome {ECO:0000313|Proteomes:UP000000305};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 809..996
FT /note="Breast cancer type 2 susceptibility protein helical"
FT /evidence="ECO:0000259|Pfam:PF09169"
FT DOMAIN 999..1105
FT /note="BRCA2 OB1"
FT /evidence="ECO:0000259|Pfam:PF09103"
FT DOMAIN 1310..1448
FT /note="BRCA2 OB3"
FT /evidence="ECO:0000259|Pfam:PF09104"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 651..672
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 728..791
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1165..1196
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 739..759
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1535 AA; 171434 MW; 14E15E3CDA2E50EB CRC64;
MNRNNHQIAT PDRPDRDVTN VFRTPVNPKP CSWSPILHAI TPDLNAPDSE CEGTPSLIRS
LGIDPELNVS WSANMETPTQ TQVSLPGFTR IDEQQNFDSK AKPLQPRHLF QNENNPNVGM
VKEMLPSGKA SNQKKCENTF QHNSNTEDLF RLLKRPALKF IYPQPVYINV HSKTQPMFST
KQLNKQTSGI KTENQSVMYL DSPQSNLQEM KKSLDFSSEP VVNVLPDRSS PISPDVAFQQ
KEVHVIDSLP TKFATDNECL KQISLNLDET KDLPFSRNQG EAHYSTSSND DQKHCEIIAS
RNVFESVGFS TAAGKKVSIS EKAMIQARAR LEEIDKEEIG SKTNPSIPKE SNILIKKQLP
EKNWNSENTL QNLDHLKTAG FSLTAKGKPV HVSDEALSKG RAMFAEVNEA PASDVLKYQE
AVGFRTAGGK KFSISEKAMI RARAKFEEID EEDLTITKHQ VTRSNTKINN SREKWMAEND
WNCDNMLPQN SDIPKAVGFS KGKPIHISDE AMAKGQTMFA EVSGAPLSNP SSITSAYPET
VGFSTAGGKK VAISETAIAQ AKSLFSELED VNVDPAEFPA TASFSRANGK KSVVSKEAIA
RGQALLEDVC EKNTENEHGG TTKTSGKYAA VAKQTLSRSG DSRIRAKTSS FKAPRRVTPV
PEPASHGLET TDCNPVQVPL TVGFNLASGK EVKVSELALS RARKNFEEPL VIEDIPKIVE
TVQAVKINHN SSPSPFPVKD ESADKKRKME EEDDKDYWVS SPTIGKTKKA KKRKNFNDSP
RSQLTQMATP GTPSAFESFM VSAKIRALRR KAREEQNAVI QRKRSTGRKT SPKAGYLYQL
KKDGTCRKTW KELIDNSSLP EILAPYKLLE DHGMLAEVYQ VQASNASSFN FCAWDHFHIE
DCLQNSKGVQ LGEFLVIFSE ENIIGYEEIG ASLLASENVD PTLISYDWIR NHYRWIVWKL
ASMELRMPSL FARTCLTISN VLEQLKYRYD KEIDRCERSA LRRIIEQDDT AAKTMILCVA
EIRSTGPAIL ELTDGWYSIE AHCDTAMQQL IEKNKIFAGL KLVISCAELV SPGPSAPLEK
GSDTFLKISA NSTRRARWDS KLGFYSKPLP FPISLASILP EGGVVSHIRV NVIRVYPMMY
MEKAADGKTI FRGERQYRRI TESAAMRFER MMEKVVEDIE REEDEQERKR IRADGNRHRN
KEINLTDEEK RSRILAEAQK RMQMSMKSIE GVPMLKLRLV DCRATHLNSA IISIWRPNEE
LQYNLKEGRA YHLYNVNAAG LRFGELQLNA MKNTMWKEMK QSNLTPGLDR SVIAFSTANQ
PGFKPMFNEL DIVGLVVFVG LQQRPFQTAI LSDGNTYFGV KCWASLEDYA LADIIVVGAF
LAFSNLQWRA TACRTVSKMQ FAFIHEGTLV SSRPALKHLD AALNDLKQSV KDPAACVAEA
EGQVDTLLGS ATPQSATPKY GTEVSRRGGM FTPTGVEYFG DGKKNETPTS SNVVINRARL
LEKYPNPPAL SPWNGCASPL VRQKFKPPAR KPPAV
//
