ID K0TLR1_THAOC Unreviewed; 1428 AA.
AC K0TLR1;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EJK75536.1};
GN ORFNames=THAOC_02740 {ECO:0000313|EMBL:EJK75536.1};
OS Thalassiosira oceanica (Marine diatom).
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta;
OC Coscinodiscophyceae; Thalassiosirophycidae; Thalassiosirales;
OC Thalassiosiraceae; Thalassiosira.
OX NCBI_TaxID=159749 {ECO:0000313|EMBL:EJK75536.1, ECO:0000313|Proteomes:UP000266841};
RN [1] {ECO:0000313|EMBL:EJK75536.1, ECO:0000313|Proteomes:UP000266841}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP1005 {ECO:0000313|EMBL:EJK75536.1,
RC ECO:0000313|Proteomes:UP000266841};
RX PubMed=22835381; DOI=10.1186/gb-2012-13-7-r66;
RA Lommer M., Specht M., Roy A.S., Kraemer L., Andreson R., Gutowska M.A.,
RA Wolf J., Bergner S.V., Schilhabel M.B., Klostermeier U.C., Beiko R.G.,
RA Rosenstiel P., Hippler M., Laroche J.;
RT "Genome and low-iron response of an oceanic diatom adapted to chronic iron
RT limitation.";
RL Genome Biol. 13:R66-R66(2012).
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:EJK75536.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AGNL01002880; EJK75536.1; -; Genomic_DNA.
DR EnsemblProtists; EJK75536; EJK75536; THAOC_02740.
DR eggNOG; KOG0947; Eukaryota.
DR OMA; CGSDITR; -.
DR Proteomes; UP000266841; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
DR GO; GO:0006401; P:RNA catabolic process; IEA:InterPro.
DR CDD; cd18795; SF2_C_Ski2; 1.
DR Gene3D; 1.10.3380.30; -; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR048392; MTR4-like_stalk.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR016438; SKI2-like.
DR InterPro; IPR012961; Ski2/MTR4_C.
DR PANTHER; PTHR12131; ATP-DEPENDENT RNA AND DNA HELICASE; 1.
DR PANTHER; PTHR12131:SF8; HELICASE SKI2W; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF08148; DSHCT; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF21408; MTR4-like_stalk; 1.
DR PIRSF; PIRSF005198; Antiviral_helicase_SKI2; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM01142; DSHCT; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
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:UP000266841}.
FT DOMAIN 420..577
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 670..873
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 74..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 252..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 353..380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 628..665
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1105..1132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..270
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..286
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 644..665
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1118..1132
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1428 AA; 157793 MW; F178FD01BF199BAE CRC64;
MLPSSPGDGN ITDIGVSAGI TLPPGFNTRR DMTDASVADT LSSVQDALSA FGVISSKDDN
AACPEQIWHR PIPSNLFRPP SHAPSLTTMM PRSRLPPGAK IRETSSKDDT KEDDEDELVE
VWVYSLASEH DDNVRGNDLT QRPLQGNLSS KLVEYTRGTM GVRRPFRPGG LDDEDAGEAY
ESEYLTKEAI DNARLALTIG SKEALERGIL LTAPPGMSFS EGLRYQDVFS DAEEICIIEK
EMDEFENDPE DEFEMNWTPQ QGSSGDIVSR RSVPEETYDR SYFDEDSLFG ESSSSSDEST
DEDDDDEIED AGELPVNISQ HQIAVTKVHF QQPAAVDEVD TLLSELDMSL QTTSKTLPTK
TGTPIHPSLP KKDPKNDKSR KSWAVTDYIP LTSTNDFHTM LPNPALTFPF ELDDFQKQAV
LRLERSECVF LAAHTSAGKT VSAEYAIALA MKHCTRAIYT SPIKALSNQK YRDFKSKFGD
DVGLITGDMQ IGADGSCLIM TTEILRSMLY RGADLIRDIE WVIFDEVHYI NDSERGVVWE
EVIIMLPEYV NLIFLSATTP NTIEFSEWIG RTKRKPVHVI RTNYRPVPLS HNLWAGGKLH
KILEGKGAFD TKGYTAAAHA LLPASAREAA EMGKKGEKKK TTASGKTIPA SKPSSGSRHS
SWQQQGSKQD WIALVRFLER EGLMPTVTFS FSKRKCEELA DSLRSLDLNT QQEKNAVQSF
AIQTVNRLSP QDKILPQVIK TVEMVKRGIA VHHGGLLPIL KEMVEILFSK NLIKILFATE
TFAMGVNMPA RCVVFNTIRK HDGVQFRELQ PGEYTQMAGR AGRRGLDKVG TVILCCFGDQ
PPPQLVLRNM LTGSSTKLSS QFRLTYTMIL NLLRVEDMSV ESMIKRSFSE FATQRALTTN
EYPKLLTKGT KTLIKLDEEF KGTADSRVGA EDVEGYYFAS KNALQSNKEL LSYILSAGGT
GGGALVAGRV LLLNSGRKKG YVRACALVLR PPATSSKASV ACVDDASCVC MVLLPQGFTK
GGQSDDIKLG SLNYVGEAHG RYFAIHSISI DEILLVTTAK QKIDAKLFYN EEALKTNTRS
ADMPSMNAFA GARSMGSRQV DDPFAGMMAR GRKGGHAPKS SKSTSVSQER QQVDEAVDAL
ITAEKSELNA GLGTCDLKDC AKSMHSGNSA MEFGSTVDRF DRDMALARQF KSHYHPDLEH
HYMAVDRKET LRAKVKTLSH LLSNESLQLF PDFLQRKAML QSLGYIDEND TVCLKGRCAC
EVNTCEGLIV AEMVFEGMLN ELEPAEIVAS LSALLFQEKV DEELSKELPE RLVSSCERMQ
AIALDLGQRQ KDFGLSVDPL EYTANSLKLG LVHVVYEWAC GVPFASICEL TGVQEGSIVR
TITRLDELCR EVRNCARVVG NPTLYRKMEA SSEAIKRDIV FASSLYVS
//
