ID E9FQT7_DAPPU Unreviewed; 1738 AA.
AC E9FQT7;
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=FHA domain-containing protein {ECO:0000259|PROSITE:PS50006};
GN ORFNames=DAPPUDRAFT_309786 {ECO:0000313|EMBL:EFX90315.1};
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:EFX90315.1, ECO:0000313|Proteomes:UP000000305};
RN [1] {ECO:0000313|EMBL:EFX90315.1, 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; GL732523; EFX90315.1; -; Genomic_DNA.
DR STRING; 6669.E9FQT7; -.
DR EnsemblMetazoa; EFX90315; EFX90315; DAPPUDRAFT_309786.
DR KEGG; dpx:DAPPUDRAFT_309786; -.
DR eggNOG; KOG1801; Eukaryota.
DR HOGENOM; CLU_239769_0_0_1; -.
DR InParanoid; E9FQT7; -.
DR Proteomes; UP000000305; Unassembled WGS sequence.
DR GO; GO:0016604; C:nuclear body; IBA:GO_Central.
DR GO; GO:0004386; F:helicase activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0001147; F:transcription termination site sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0006369; P:termination of RNA polymerase II transcription; IBA:GO_Central.
DR CDD; cd18042; DEXXQc_SETX; 1.
DR CDD; cd22663; FHA_RNF8; 1.
DR CDD; cd18808; SF1_C_Upf1; 1.
DR Gene3D; 2.60.200.20; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR045055; DNA2/NAM7-like.
DR InterPro; IPR041679; DNA2/NAM7-like_C.
DR InterPro; IPR041677; DNA2/NAM7_AAA_11.
DR InterPro; IPR000253; FHA_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR047187; SF1_C_Upf1.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR PANTHER; PTHR10887; DNA2/NAM7 HELICASE FAMILY; 1.
DR PANTHER; PTHR10887:SF322; RNA HELICASE MOV10L1; 1.
DR Pfam; PF13086; AAA_11; 1.
DR Pfam; PF13087; AAA_12; 1.
DR Pfam; PF00498; FHA; 1.
DR SMART; SM00240; FHA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR PROSITE; PS50006; FHA_DOMAIN; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000000305}.
FT DOMAIN 28..79
FT /note="FHA"
FT /evidence="ECO:0000259|PROSITE:PS50006"
FT REGION 136..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 218..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 312..339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 441..620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 639..902
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1337..1364
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 139..168
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..183
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..239
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 312..327
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 450..464
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 465..480
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 482..496
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 513..531
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 536..555
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 576..592
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 639..655
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 656..684
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 696..719
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 720..760
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 775..789
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 799..836
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 865..886
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1738 AA; 194506 MW; 9105745B40E68D20 CRC64;
MEDWYLERLG HQNSRHHLNI LLGPREKLTI GRKAGGVVDI VCNGKTVSRE HCVLKYVDSC
WSIEDLKSMN GVFLNKNRIP ANTPTILRER DILGVGAIET TEPDYYVFNV LKNTVKDENE
NDGDLMIVEV PSVSAARDPL EESECRTDPL SNDIEKGKPS DDPDKSETPR GQNATSDDSQ
PIKIQNFPEV ILPPSPIFSE KSDIQEIFIG ESCVSQEKTT RSCTAEESST ASNSHQQKRS
QEKTPVRNDD AKMISALSNS KPVRPSLDDA KLKLDCKVVI EGLPKQYLNG GIAHSKATKK
RLNGKKRLLL YSSDSDSDNE DSSKNIANHH AKNSLAGVES KGKALKKVIH LNERTSSSED
SSDDDALFSS NAASVCKVPK SVFVVEKLSR EAGSEQRIPS RSGRMAPASA PQIENLVEDS
DDCAVVKANV VCGKRKDPES DEDVIILSSG DEETFSSQSR FKQEPLDSPV RKHADDHHGK
SPLVISSSSS DEDSPFFPEL SQAFLKEIAE EEEEETSLSK KISRKGTDVD KLNSLVKSGR
FNQKGKTTLE TEPQNLHTPV RGRFSLATAG DSSRRETDNQ LAEDDQRKKL QSKVTTPRVP
IIIPPKPQTG RKRKSANGIG SVREKLCKEH GMESYRVCVN EASKKKAKNR PMNDRRLNEQ
PSTSVDPTKK FLTPRPSTQV PKEPKSSAPI PVKAKVTKKS RGDLFLKDFV GEENGPKEGT
KKATSSSLPG FNIPRLPKTS NAEGVSNDQD ASNSASSSAH KRKYPGDDNE SEPMGADSME
SSETPSVSYS FKKPHVRVAR RVSVSEDGDK NEASSGHSKH SSRYQDRSRD EAQPLGRNKK
WVPPNSIRNA RREGREIPSL PGQHQHPAPS YSNASPMASS NPNDETIPLP APDYEIQGPR
PISDNGMRGI LKYRGLKNGL YRPKKVSIVE VNNKIHEIES RPPTPPLPTK TPVRPVDRVA
LTNDILYRIC NWCYDWIEEQ KKQKNDVPPP LLNALQRENG RSLPELSLLP VVSAYDSLES
YCSIFTPLML HETWASLCKD IETSQHDSIR PLIYSKPKFC DGFALLQCEA LSPIRIIDME
LVTLTVHISP QKPPVKFFGV AEQVVTRNWR AEDVDPRLLE TCQRQNVLYF RMSFVLWIKM
SNVPKELDKI FSVTKISRLN TVVKQFILNA ELARSPLCDV ILHPSDYVDA FKLDTVDVEE
NHPVLNPCQY QAVESITRTM VCASDREPKV ALLQGPPGTG KSHVIVELIS RMMFMHYEKT
SSFPRILVCA PSNNAIDEIA NRLMIARDEK KSRYNIVRIG VLASMHPNVA RISLDELTRK
FQRDTIATKD SPESGKLRTL TEELNSLRKN KTSLIASIDA ANKRGQSDEA RMHGRKLEQL
EIQIDGVDRS YQECYKTHAK YFNSDKERLA MKKHLISRAQ IICTTLNSCR SREMETLFIE
ERSSKSFLCC ILDEASQCTE PESLTPLAFG ISKLVLIGDP DQLPATVTSQ VAAKNRFDQS
LFNRFYSNRM ITNRENEEGV MMLNTQYRMA PSICEWPSKY FYGGKLVTAE GLIRNGPCYE
YRVLNVIDGL EQLADQSFKN EKEATLVAKI VMLIVNSPLT RGKSVGVITF YRSQQQCIVK
KMTEEVNRIN ASRVEVNTVD SFQGREKDIV IVSCVRAREV RNLGGDIGFV SSLQRMNVAM
TRAKESLIVC GHFQTLQMNE TWQDLINNAR SRDVAHVVTS DYTSDNLRPL LLRPVPNV
//
