ID W7TN96_9STRA Unreviewed; 1680 AA.
AC W7TN96;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Zinc finger ran-binding domain-containing protein 3 {ECO:0000313|EMBL:EWM24963.1};
GN ORFNames=Naga_100148g9 {ECO:0000313|EMBL:EWM24963.1};
OS Nannochloropsis gaditana.
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; Eustigmatophyceae;
OC Eustigmatales; Monodopsidaceae; Nannochloropsis.
OX NCBI_TaxID=72520 {ECO:0000313|EMBL:EWM24963.1, ECO:0000313|Proteomes:UP000019335};
RN [1] {ECO:0000313|EMBL:EWM24963.1, ECO:0000313|Proteomes:UP000019335}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B-31 {ECO:0000313|EMBL:EWM24963.1,
RC ECO:0000313|Proteomes:UP000019335};
RX PubMed=23966634; DOI=10.1093/mp/sst120;
RA Corteggiani Carpinelli E., Telatin A., Vitulo N., Forcato C., D'Angelo M.,
RA Schiavon R., Vezzi A., Giacometti G.M., Morosinotto T., Valle G.;
RT "Chromosome Scale Genome Assembly and Transcriptome Profiling of
RT Nannochloropsis gaditana in Nitrogen Depletion.";
RL Mol. Plant 7:323-335(2014).
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:EWM24963.1}.
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DR EMBL; AZIL01001066; EWM24963.1; -; Genomic_DNA.
DR EnsemblProtists; EWM24963; EWM24963; Naga_100148g9.
DR OrthoDB; 318617at2759; -.
DR Proteomes; UP000019335; Chromosome 12.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR45766; DNA ANNEALING HELICASE AND ENDONUCLEASE ZRANB3 FAMILY MEMBER; 1.
DR PANTHER; PTHR45766:SF5; SNF2 DOMAIN-CONTAINING PROTEIN _ HELICASE DOMAIN-CONTAINING PROTEIN _ HNH ENDONUCLEASE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000019335}.
FT DOMAIN 401..566
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 761..931
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 163..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 966..1009
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1552..1572
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1617..1644
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..179
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..194
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 982..1008
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1624..1643
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1680 AA; 187579 MW; 930C54201AA14BA5 CRC64;
MHSTVNPGSK QGCRMSRRSS DEEVIDVSRS QFVGSKNGER NPQLLVVAPG PVNDAVVTQG
AHSPPDRVGV HRRLPLQETR TNSIRLHDSS IQNLRSDVWA AFCRPFEVNG VAVASKTHTR
LLQMPVTSSS RGDTIQVTKC SEPQESLKPK DCGDIHEEGA FRRESAVSDP LRKDSLRTDT
TASKSSVQHV PSGSRRNIPN CITTSVKSSP PLCWHCKHTM EDRGVCSIPR YRCQFFPRCP
GRCGTDRPQE AVFLQLRGPS LKDLCLSYPD MPATAVAFGA NWLSARLKLC GLKDAVLDKA
RGIRPVPPGQ RGGGGAWEVV LDVRECENVT RLLREHPTLD LVREVPLPTL RFVSRLLDGE
AAREEGGSGF FATPGEVERR FALLPRRVMK ALFDFQKEGV RFALRRQGRC FIGDEMGTGK
TLQALAVMVC YQTEWPLLIV VPASLRLLWA EVVEKWVPFL RPADIHVIFR EADRVSSRSE
CPPVVITSYE MLRNLEASMT AVAFHCVIFD ESQKMATTRA HSALNRVTSA ALRVASSAIR
VLLLSGTPTM ARPFEIYDQV RLLQADLLST PQGSHDGASK WEFGRNYCTG VYWQTRSQRP
PLAAAKYDGT RCDEELYWLL RNAVLIRRLK KDVMAELPSL VRTVVRVEEG KDGASIWSQQ
VDSTETEGRI ECSFEGGASL KKIRAAYDQN CAAETCLMER MEDEQTELQI TWGDSEHRDE
RKRFVGQSEY HQLGHLKLGG VKEWLADRLL GGWLDAGVVG YEEDAIVEAD APKFVIFAHH
LDVLAVLHGF LHNIFVRHRA CRRLAFHWSQ VQIQGSTPPE TRQDLVKRFK NDRYCRMALI
GITAGGSGLD LAAASTAVFV ELPNSPHWLR QAEDRLHRRG QRRRVQIYYL VLPPGSAEDK
VWQCMRRLLR ENTAVINSRE EAEELDVNRV EEFRAQASLP QDAPSQAAEL LEGGLFPLLS
KGEERENFWP GNGLSESPPE FVREASEPEG GKEHLRGESE RQADRVHDPS FPDTCLLSET
NAHSANISSP SSKPAVASVR KACNAVEDAA QTNGVNRTQE MSPPAVLASG VPVINHFLHG
RFGGEDYEWE LEALAGLTQE DADEEQTVQA ADGEGQVLQQ RSDGLPNDIK VNADFSSYER
CSAKTGTTTE GNHTGNVAED TVRCSYECAD SPVHLSPSSQ WCHPSPDKNT RTDKDITRAT
CALKGNVGCG QKPAVKLLYN LWFEVSKHTG WVHLHEHEDG SKPLGVHVDP LDYYHLTGLA
QNALSSLPLL EEIRARAADE IILEDLPPFI QVAPGEKWQL LKFMTQFQKE CARIRNQLYG
YVLQPMEGGL QGWIRKHRTN RQRAGRQKAS LPPRVLSSWD PDFGYRRHLT YEELFDPSRH
SNVTRHVLVT SGRLFRRSFR QPLDPQTHDP LCFCCGTAFS LPGGTRTLQD LLCSAACLAY
FACLSRGGLR REVGRRDRGI CEMCGLDTLG LLERVKHSSC LKSREMLVVE EVPKFKERPK
LLARLVREPK EGHVWQADHI HMVAEGGGLC DTTNGRALCV LCHASVTAEQ SRLGRGDKRR
AGREKVKKER GAGMHVERGE WGTTTGQGDA EGGARGRVVQ DYTGMKMRGR RDTEQACLNG
RTDPMEGEDG DNRGEEDIRG EASGLKKCQQ IAEDYERDEN QRLKVKAEPI EDHQLIAMCP
//
