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Database: UniProt
Entry: A0A0V1D347_TRIBR
LinkDB: A0A0V1D347_TRIBR
Original site: A0A0V1D347_TRIBR 
ID   A0A0V1D347_TRIBR        Unreviewed;      1262 AA.
AC   A0A0V1D347;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Helicase SKI2W {ECO:0000313|EMBL:KRY55411.1};
DE   Flags: Fragment;
GN   Name=SKIV2L {ECO:0000313|EMBL:KRY55411.1};
GN   ORFNames=T03_10610 {ECO:0000313|EMBL:KRY55411.1};
OS   Trichinella britovi (Parasitic roundworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=45882 {ECO:0000313|EMBL:KRY55411.1, ECO:0000313|Proteomes:UP000054653};
RN   [1] {ECO:0000313|EMBL:KRY55411.1, ECO:0000313|Proteomes:UP000054653}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS120 {ECO:0000313|EMBL:KRY55411.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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:KRY55411.1}.
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DR   EMBL; JYDI01000056; KRY55411.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V1D347; -.
DR   Proteomes; UP000054653; Unassembled WGS sequence.
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; -; 1.
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; 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; 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, ECO:0000313|EMBL:KRY55411.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054653};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884}.
FT   DOMAIN          299..455
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          534..735
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          164..188
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          209..234
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        210..233
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KRY55411.1"
SQ   SEQUENCE   1262 AA;  144923 MW;  D4583D315320B3C2 CRC64;
     LLIMENNNGK ENFKNPFQSW LSITQKHELT IEAKALVIDE VLKECCVSSV SCLEADEVPE
     YYDTSFEQVS SFTTVDRDYR TGAPIGIIEP LPSDSDSHTT PPLDFTREYN TNSAGVFGNP
     QSVPFLPGGM EEDVQKRTSK AKNNNAVYYT AFSGEYLTCA PGLSRGRNFN NSESELSSEE
     ESGDDEGKVT VVKSDEQAVL LNEYPANEKK TESTVIEDKR ENEKEETVKE TKAQKNEAPI
     VTDNHLHNDE ALNELYKDRA YYYASWTESE ESLAAFELLR PRMAKTFPFE LDLFQKQAIL
     CLESGESVFV AAHTSAGKTV VADYAVALAH LNMTRVIYTS PIKALSNQKY RDFKRDYDNV
     GIVTGDVQMN PDAFCIVMTT EILRSMLYNG SEVLRELEWV IFDEVHYVNN PERGVVWEEV
     IIMLPKHVKL ILLSATVSDV MEFAEWIGRI KQRKIFVVKT SSRPVPLEHH LYLGDIGTTK
     NVQIQIVDKD GNFLAENFDH AVRQKENSKA ATSYKNIYKP YTGSGAAEKN LWLSLIQHLK
     EKSLLPMVIF VFSRKVCDTL ALMLLKSSLD LTTSSEKRII RKFFKKSISK LSANNKALRQ
     VTQLQKMCQI GIAVHHSGVL PLMKEIVEML FQEGRVRVLF ATETFSMGIN MPAKTVVFNS
     IDKHDGRTVR LLNPGEYTQM AGRAGRRGLD SSGTVILLCR DKIPHVSDLR TMILGSSPRI
     ESQFRVTFTM ILNLLRCQPL SPEMMLMRSF VENLSFRDIM VLNKNIETLM AEQNESQFAN
     CVLCSQGNIQ KFYRVAEECY EVARCIIWNV TKLIEPGMVI VVQLLDKWLL GLVLKKHFYK
     NEWIFEVFVP YRNLKPKNDK LTPDERCNQF LFYSTELECN LVEPDFRYYS ILEFSLSSIV
     HLSNASFSVS NHQIFDDWGL SQNKHNECEN DAILTLIRNL YGVYEYYKSN GTRMRVPLEW
     CSLRNARLDI TYLNRLRSSA VKFRCFCCDK FREHFYELYQ IEEKQAEVDD MKRKVDCFKL
     RLGPSYEKKR AVLRMMKYID YGDVIQFPGR IACAINQNPL LYSQLLLNNK FADVTPDEVA
     AILSASACQY KCKFIAFREP RLQELMNMVC DMDRRIRLVR ERCDDVDDDI DDQLNFGLME
     VIQKWSLGMP FGELLKITDA QEGAIVRCIQ RVCELCRDLK TASSLMGNST LTTLLEDTMN
     SLKRDIVFTD SLLFSAFFCF VFSPLSVFHF LKAIPEEEKL ACNCYLQKYQ ERNNIEMFPF
     SR
//
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