ID A0A0V1CWS9_TRIBR Unreviewed; 2173 AA.
AC A0A0V1CWS9;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Phosphoinositide 3-kinase regulatory subunit 4 {ECO:0000313|EMBL:KRY53638.1};
DE Flags: Fragment;
GN Name=PIK3R4 {ECO:0000313|EMBL:KRY53638.1};
GN ORFNames=T03_15849 {ECO:0000313|EMBL:KRY53638.1};
OS Trichinella britovi (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=45882 {ECO:0000313|EMBL:KRY53638.1, ECO:0000313|Proteomes:UP000054653};
RN [1] {ECO:0000313|EMBL:KRY53638.1, ECO:0000313|Proteomes:UP000054653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS120 {ECO:0000313|EMBL:KRY53638.1};
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:KRY53638.1}.
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DR EMBL; JYDI01000082; KRY53638.1; -; Genomic_DNA.
DR Proteomes; UP000054653; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:UniProt.
DR GO; GO:0043186; C:P granule; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0045324; P:late endosome to vacuole transport; IEA:InterPro.
DR GO; GO:0016236; P:macroautophagy; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd18787; SF2_C_DEAD; 1.
DR CDD; cd13980; STKc_Vps15; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR045162; Vps15-like.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
DR PANTHER; PTHR17583; PHOSPHOINOSITIDE 3-KINASE REGULATORY SUBUNIT 4; 1.
DR PANTHER; PTHR17583:SF0; PHOSPHOINOSITIDE 3-KINASE REGULATORY SUBUNIT 4; 1.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00400; WD40; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00320; WD40; 3.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS00039; DEAD_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS51195; Q_MOTIF; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 1.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Kinase {ECO:0000313|EMBL:KRY53638.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000054653};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|PROSITE-
KW ProRule:PRU00221}.
FT DOMAIN 52..343
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REPEAT 1340..1374
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT DOMAIN 1792..1820
FT /note="DEAD-box RNA helicase Q"
FT /evidence="ECO:0000259|PROSITE:PS51195"
FT DOMAIN 1823..1993
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 2000..2142
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1714..1737
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1792..1820
FT /note="Q motif"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00552"
FT COMPBIAS 1716..1737
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 2173
FT /evidence="ECO:0000313|EMBL:KRY53638.1"
SQ SEQUENCE 2173 AA; 246072 MW; 0991817C4E2A59AA CRC64;
MTIVLEIGKL DILYYRIALA SDQIVYFCEA LNLHAIGLKM GSNWSATVPS NILPVESLGS
TRFMKVARIR HNTGDCVVKV FVVSDPTLPL TVYKSDVEKT RDNLKGCLNC LPYICVLSNQ
KSWYLIRQYV KHNLYDRLST RPFPVNAEKL WICFQLLKAT EQIMQNGVCH GDIKTENILL
TESGWLLLSD FAHFKPSIIP HDNSSDFTFY FDCSNRRTCY LAPERFCRFR KLHTALMHLS
KSERLVRSVI NHKMDIFSLG CVIMEMFCDD ETPFDLNRLL SYRKQKYRPK RCLDALPSPD
IREMVESMIS IHPDQRLNAG EYLEKYKGRV FPNLFYSFLY PYFKSFIELP LQTYDEMVER
VYGDLQYIKE VLRREDGKLD DYILLFLTLI TSLCRNLREL HHKLQVMNMF KDLARYLDDD
VIIDRILPYV LSYVSDESPR ARASAVYLTA HIMKNVHRVA ASEAGIFVDY IFPSLFPTVN
DKSVMVKIAI ASSLGTLMAT AKNFLMQADV TFKRDPHVEG LLRINEIEYQ REAKKLFSFA
QDMIVTLLCD PDYAVRKTLV RDSLRNLCGL LGQQKACDLL FSHIVTFLNE KQDWRLRCLF
FQCCPIMITC IGSQSWCVLT PLYQQGLHDS EDTVVFETFA SLLRLLRSGS LHRTIIFELL
DDVLPYLRHP NKLVRTGAIT YLCSVCQRMT MLEMKCKVEP RLQSFLKFPL SRIENERSLL
HALKDPLPRQ LWDMVIDTAV LEQLLEFFKE RSTIRRVGKL GSSNDGVAVM PENAKVAQLY
GKLMAQGLSE ELEDLFVAFA PNLLRIQQLR DNARPVSDVH PITGRISLTN SEATLRRADL
TTGHGPKRAI GKGSFFEPSQ TALNIEWRQM FGHIEVEEEQ ALRMGPIIAP IDYVQEASEE
ETDGNDERAE KLQSNIGSGQ LKIDELPSVD KMELCKSFSK LASKFDLMPC SSSDWESNWR
DLVNADADVH FRKEMQMSTV DTDDNGSECV VYFGDDGTVY KQFGSVVIRE EASSTQCAKQ
GQVQASFVQS ETDDFSEVEF GLGKLPNIML IQEQNAQAEV ATSAENTTLE LSSNEQIAIN
TNEIEKLTNE LIELSVKNLE NCLDLEEQLS TGSVWEKSAS VLMGDSVTKF EYDWEGELSV
NSGDSTPDMD AKLETISVDR SEEAKSPKPV ERRRLCKSIG DYEDWDRDTE DESDFDDTDL
SLSDDIEEVV TSCAKQATNA ESVDDDGSLS QASSSNSLLV LLIDGAANPQ EMPVAVEKDK
AEGSRVVMPV EVNQVAAECC VEVAVCKLQL EKYIEWQRDL WSRHALCSVD VRNGTSSLHP
RKVAVPSAAW KPRGDLLVEL REHTGSVNKL AVDYSGRYFV SISSDRTLKL WDVKQLIGRN
MAHRSLCTFK EFDGKMTCVN FVENFLACSS DDGYLRLIRL ETSGSEVPVF NPCVSYQQRD
DYIIDLWTTS EGNCLRMIGL THHGQLLGFD TRVSRPVWNV TNPCQKGVVT SMCVDEKNGN
WVVVGTESGY FILWDVRFEL NVNEFKHPAN LPVAHLYTSD GCRSRIFATY LHHDEVSEWD
LETSCRTNVI WTSDTPPLSY PTQVSADRRP ILTLCQYGGG EDSMGSILAG DDSGTIQHWN
LQSTAESTVI SSFDFKPNSV FKRQIIDGMN VYSSLAGSSS LTDESGAKPR ADVQVNTAHH
DCVTDVKICR AKNWMMLSSS YTIVADANRA NNTISPDNEA EERRARIGKE RETRRSVPAR
CRLAANAPIT RYQSMHVGSE ANNNEQREDG RHAAENLASQ HNLETNYTEM VNSFEKMGLR
EELLRGVFAY GFEKPSVIQQ LAIVPCCQRR DVIAQAQSGT GKTATFAIGL LQQINTDFND
CQALVMAPTR ELAQQIQKVI LALGDHMGVK VLTCIGGTSV ATNREKLGQG CHVAVGTPGR
VLDMIRGHHL QTKGIKTFVL DEADEMLSRG FKQQIHEVFE FMPADVQVVL LSATMPDEVL
QVTTKFMNNP VRILVRKEEL TLDGIRHISK AVIFCNSRQK VEKLARELTD RKFTVTCMHG
DMTQQDRDVI MQQFRTGSSR VLISTDLLAR GIDIQQVSIV INYDIPHNRE NYIHRIGRSG
RFGRVGVAIN FVTENDKRMM KDIEEFYHTN IRQMPADIEN GFFLLLLPSV TGACSFRCRK
WVVGSLVTCW LHW
//
