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Database: UniProt
Entry: A0A1S3K4H1_LINUN
LinkDB: A0A1S3K4H1_LINUN
Original site: A0A1S3K4H1_LINUN 
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
//
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