ID A0A1S3K4H1_LINUN Unreviewed; 1263 AA.
AC A0A1S3K4H1;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Helicase SKI2W isoform X1 {ECO:0000313|RefSeq:XP_013417313.1, ECO:0000313|RefSeq:XP_013417314.1};
GN Name=LOC106178605 {ECO:0000313|RefSeq:XP_013417313.1,
GN ECO:0000313|RefSeq:XP_013417314.1};
OS Lingula unguis.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Brachiopoda; Linguliformea;
OC Lingulata; Lingulida; Linguloidea; Lingulidae; Lingula.
OX NCBI_TaxID=7574 {ECO:0000313|Proteomes:UP000085678, ECO:0000313|RefSeq:XP_013417314.1};
RN [1] {ECO:0000313|RefSeq:XP_013417313.1, ECO:0000313|RefSeq:XP_013417314.1}
RP IDENTIFICATION.
RC TISSUE=Gonads {ECO:0000313|RefSeq:XP_013417313.1,
RC ECO:0000313|RefSeq:XP_013417314.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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DR RefSeq; XP_013417313.1; XM_013561859.1.
DR RefSeq; XP_013417314.1; XM_013561860.1.
DR STRING; 7574.A0A1S3K4H1; -.
DR EnsemblMetazoa; XM_013561859.1; XP_013417313.1; LOC106178605.
DR EnsemblMetazoa; XM_013561860.1; XP_013417314.1; LOC106178605.
DR GeneID; 106178605; -.
DR KEGG; lak:106178605; -.
DR OrthoDB; 1352at2759; -.
DR Proteomes; UP000085678; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; IPR025696; MTR4_beta-barrel.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR016438; SKI2-like.
DR InterPro; IPR012961; Ski2/MTR4_C.
DR InterPro; IPR040801; Ski2_N.
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 Pfam; PF13234; MTR4_beta-barrel; 1.
DR Pfam; PF17911; Ski2_N; 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 ECO:0000313|RefSeq:XP_013417313.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000085678};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT DOMAIN 331..490
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 599..769
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 123..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 235..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..151
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1263 AA; 141766 MW; 06C23FA2CB1F4B96 CRC64;
MSAMAGQVVD GIDIDGLSIL SVGTCNNFDV IERRKSSDTS LPLETLPLGL PPVLPTLKAD
LEEYLSHPEK LPVYDIERTQ RFFSSKGCPD NLYLAEPTPV QTTIRVDRDM TTGQLLGYKE
EFLDDTGSSA KNSTSLSRPP GPPSEGIKGN STNYPFWPGG LEEPVFTDLA ADNLTQIDFE
TDLLSCPPGF DHGIVFECKS RTENPEGTLQ KEASQTPNLL KLSDILEADD LDFSVGEEEE
EEDKEKEGAD KDKFQNSADI QDLPRSESFE NLVTNTDSDL GDVVTRQQEE PLENWAIPID
LTDPVSDFHK RIPEMACTWP FEPDIFQKQA ILRLEQGESV FVAAHTSAGK TVVAEYAIAL
SMKHMTRTIY TSPIKALSNQ KFRDFKQRFS NEGDVGLVTG DVQIHPEASC LIMTTEILRS
MLYNGSDVVR DLEWVIFDEV HYINDPERGV VWEEVLIMLP HHVNIILLSA TVPNTREFAG
WVGRTKKKKM YVISTPKRPV PLEHFLFTGN SNKTSHELFL LQDAKGNFLT KGYYQAIEAK
KERTSKSSQS FGPKGARGGN PAQDKNVWLS VIDMLKKKDK LPAVAFTFSK KKIEDNASNL
SSVDLTTQSE KSEIHIFFQK SIAKLKGSDK TLPQVLHMQD ILKRGIGIHH SGILPILKEV
VEMCFQRGLV KVLFATETFA MGVNMPARTV IFDSIRKHDG TAFRDLLPGE YIQMAGRAGR
RGLDATGTVM ILCKGDVPEM ADLHKMMLGK PTLLQSQFRL TYSMILNLLR VEQLRIEDMM
KRSFSEFHSQ KSTTERKKTM ADLQEKMSTM QDLDCNVCCI DLEGYYKACR EYCITKTELQ
KKVLTHPAAI KALSPGRVVI VDTELYQNTL ATVLKSTLGQ NNERMFTCLV ICEKNASSAD
SASNATKTVE GPLIKPVLVN QVLFQPEGPS GHVIVDLTAE HIGAISNVAL KVNADRILED
FKKRQIARFK NDPPGQSVVT TTQELLRLAE SDPHGLPSLD PVKDFGLRDI DLVEQFRRLQ
FLQEELKNFA CVTCSNFRKH FEEKHNYMRL KEEYAHLQFL LSDESLTLLP EYQQRVQVLR
ALKYIDNTNT VQLKGRVACE LGNQEIIITE LVFENILTDL HPTEIAALLS CVVFEQKRCS
EPSLTPDLQK GKDLILKIAT SIGETQRACG LLTPVDEIVE SLKFGLTEVV FEWARGMPFS
EITGLTDVQE GIIVRCIQRL DETLKDVRNA ARIIGDPVLY RKMEEASKLI KRDIVFAASL
YIQ
//