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Database: UniProt
Entry: A0A087TLY4_STEMI
LinkDB: A0A087TLY4_STEMI
Original site: A0A087TLY4_STEMI 
ID   A0A087TLY4_STEMI        Unreviewed;      2347 AA.
AC   A0A087TLY4;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   02-APR-2025, entry version 60.
DE   RecName: Full=RNA helicase {ECO:0000256|ARBA:ARBA00012552};
DE            EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
DE   Flags: Fragment;
GN   ORFNames=X975_02723 {ECO:0000313|EMBL:KFM66123.1};
OS   Stegodyphus mimosarum (African social velvet spider).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Araneae;
OC   Araneomorphae; Entelegynae; Eresoidea; Eresidae; Stegodyphus.
OX   NCBI_TaxID=407821 {ECO:0000313|EMBL:KFM66123.1, ECO:0000313|Proteomes:UP000054359};
RN   [1] {ECO:0000313|EMBL:KFM66123.1, ECO:0000313|Proteomes:UP000054359}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Bechsgaard J.;
RT   "Genome sequencing of Stegodyphus mimosarum.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC       PRP16 sub-subfamily. {ECO:0000256|ARBA:ARBA00038040}.
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DR   EMBL; KK115830; KFM66123.1; -; Genomic_DNA.
DR   STRING; 407821.A0A087TLY4; -.
DR   EnsemblMetazoa; KFM66123; KFM66123; X975_02723.
DR   OMA; KEWEAFP; -.
DR   OrthoDB; 10009520at2759; -.
DR   Proteomes; UP000054359; Unassembled WGS sequence.
DR   GO; GO:0034458; F:3'-5' RNA helicase activity; IEA:TreeGrafter.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:TreeGrafter.
DR   GO; GO:0004540; F:RNA nuclease activity; IEA:InterPro.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0060255; P:regulation of macromolecule metabolic process; IEA:UniProtKB-ARBA.
DR   CDD; cd20335; BRcat_RBR; 1.
DR   CDD; cd17917; DEXHc_RHA-like; 1.
DR   CDD; cd10910; PIN_limkain_b1_N_like; 1.
DR   CDD; cd00590; RRM_SF; 1.
DR   CDD; cd18791; SF2_C_RHA; 1.
DR   Gene3D; 1.20.120.1080; -; 1.
DR   Gene3D; 1.20.120.1750; -; 1.
DR   Gene3D; 3.40.50.1010; 5'-nuclease; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR   InterPro; IPR048333; HA2_WH.
DR   InterPro; IPR007502; Helicase-assoc_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C-like.
DR   InterPro; IPR002867; IBR_dom.
DR   InterPro; IPR056245; KH_DEAH11/12.
DR   InterPro; IPR021139; NYN.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR035979; RBD_domain_sf.
DR   InterPro; IPR044066; TRIAD_supradom.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1.
DR   PANTHER; PTHR18934:SF91; PRE-MRNA-SPLICING FACTOR ATP-DEPENDENT RNA HELICASE PRP16; 1.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF04408; HA2_N; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF01485; IBR; 1.
DR   Pfam; PF22191; IBR_1; 1.
DR   Pfam; PF24471; KH_DEAH11; 1.
DR   Pfam; PF01936; NYN; 1.
DR   Pfam; PF07717; OB_NTP_bind; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00847; HA2; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00647; IBR; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF57850; RING/U-box; 3.
DR   SUPFAM; SSF54928; RNA-binding domain, RBD; 1.
DR   PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS51873; TRIAD; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054359};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          917..1080
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          1109..1284
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   DOMAIN          2138..2346
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51873"
FT   DOMAIN          2142..2186
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          1..88
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          363..405
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          684..703
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..11
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        23..34
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        39..53
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        62..73
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        378..392
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        393..404
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        684..694
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         2347
FT                   /evidence="ECO:0000313|EMBL:KFM66123.1"
SQ   SEQUENCE   2347 AA;  265559 MW;  93642ACB5A463F95 CRC64;
     MNSGKSGKKY YAKPTKSNGS TQGKKDQPQK KKSGDVQGKC NQSQKKKQPQ PTVSGEFRCE
     NFTHTGKPES NLSYHGKHGG KKQSNSSNEK EIYNKEMHYR SSPGLLFQRD GKLDQDRHHS
     LLSFSTGFQS SNQNSQQFPS AHFHGAHHQK TQNLVKSISP LKHNVNEKQK MTHPSHSGNY
     SKFHGIHNSM PAQVRVFHGN YEYGSSQPTN PQKNSHPIKQ NISSHQNFKP PSVRNISSSI
     TVSNVRNGLP CFRGNTKPSH YNSQILSSVR AEKHINDFRM SSNLNKFTSV SNTVTSKQFP
     LKNPVFKFKS SKVVKPENKA KQTHKKKKRV KKVNFWKDTK NSNIGVTPLL SFQRISENSS
     LDWTSVKSKE SDDDDDNASI SHKSSDGSNV SDIETDGTSS DESEFSIVSS VKDSEIGSCK
     SDFMPLNASQ TEKFVIVCWD IENCSLPSTK SAVDFVKHVR NKFYDGRTET QFIVACDVSN
     LNDALVKDLD EASVTIIHKS SRSKNAADQK LMIILMDFQN THRRSDSAVV LISGDSDFAS
     YLSDMRYKHH IYVNLICKKN AKTSLISAAD RVVFFEDFIK DVAERSREED TQFFINVSNL
     PKQMNKKQIK KYLTEKITGI KGRVKILNES LAIICFPDLC AREKAVSRLS SCILGDCKLQ
     ITCSEGILEG NKLGAVNKND NKIKLPDSKR KSSEKVNSSL DDNSGKGGTL YVYVSERFGD
     VEYWKNELGK LWNISDLALN WDGNSEEGFF MVNFKSLSKA QKAKKKLLKK QMKDPMAPKF
     LKLVKHDELG FNTFCVNALD NMQDLNKKKI NDYICMVEKK KDYFLNKHQE EVSKLKKSPI
     PQVPGAKEVL SEKLNEMNEQ KVTFLNFTSE IINKLNKADI CSENLEHCLD DILREYSREC
     NCFSSALPIY AKKNTILKKI KKHQVTIIRA ETGSGKSTQL TQYVWGEQIL SKHGVIMCTQ
     PRKIAAISLA KYVSSQVGCS LGDIVGYEVG MSTKKSNKTA ILYVTDFTML KMVINNEIEN
     ASCIIVDEAH ERTVYTDLLL GMLKSYLKAK PSLKLVITSA TIDTSIFRDY FNVTDDAVLH
     VSGRIYPVED IWCNEDVSLG WDFFQKTVDT VHDILNTEKE PGDILAFLTT PAETEKAVDA
     LNKKVKDENY NHKIKILQLH GKLDVQEQQK IFERIPVGMR KVVFSTNCAE TSVTIPGIRY
     VVDCGMVKES QYDSVRNMSI LCVGFVSRSS AEQRRGRAGR TQVGKCFRLY SKKNYDNMAE
     GNVPEILRVN LGQALLKLMQ MGVKNPVQFD FVQSPSEESL KLAMKQLTHL GAVNETDLSL
     TALGRQMSYL PVEPRLSFLV LKGVDSNIGF EAVSLASLIT VSRSIFFRNS ENKNEADKKK
     MRFCQNESDF LTYLDVYKEW FSVPKVSKSK WCVLNCINAQ SMRTVHNLVN ELILILTKEI
     NLKIPAKFND DLHHEELLKI IFYSFSENIC VFSGHVRYGY RSTKIPGELM IHPSSSLSTF
     GNWRPQFLVY DTILKTNMTY LINISPITKD MILEAIKLHV LKINLEALES LHLRNLCISP
     IGKTVLLREI IGKNGVHRKF LENKLKVLVG SDSVILDVDI SKGEVKIFAP EPKFEIIESV
     ICPIIEKAKE TLAIEEKEFC LLENSELTGI VSTGAEIKDV VIPGEFRDLK VTVNNNDSIQ
     TIVEKLQICG TISTVREWKN YFKITFQSPV HAKQALNMFR NEQSFSLQSI IKTAVSDNRR
     CMYRVVVSYM RRPCTGEAFV SFESDAFLPL ISNSVCNRSI TYRNMPIRCS ISKKSQDLRF
     SGLPCDTNRE EFETLVKSLM PDDIKLTKCI IVRKKVYESS QDELEIVKQG LISKFGAFTP
     KDKLHIDLKK PSPKDFTWNA FIFFENMYDG ENAVNMLKNR ICYSYPGFKM KPCLQTTLFC
     KTEIFSAVKE QIDDALKYFK DTSDSDKTLD ITAVPKDSST VKIQITSNNV SDATDARRAI
     QNILYGDQIK CAGNPVLERL FLEDSLAYIR KISKDKLNCF VDANKYRKVI SIFGNASVCN
     LIKLKVNSFL SAIAENSVRE ISLLPKHGRV GVIKELFKRY GSNLENLVET SGVSGIDVNL
     YKHKLTVKGT ESSVFKCLEL VEEVVKELGN SDDDDGDDDE VCALCYDKIL NEFYRLEYCG
     HAYCKTCILH LFENSSDFPL SCVGCKAPTV LADLYWATKQ VQQLEKIVLK KSLDFFIKNR
     DDIGYCPSPD CPMIYRVAKD GKTLFECPVC SNVICTNCGD LYHYGMSCSL YQCSKHDDDY
     SLKVWMLADE ANRKLCPSCS SPIEKNEGCN HMTCWKCRAH MCWLCLQVFP SAGLVYNHQA
     ICPKRKV
//
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