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Database: UniProt
Entry: A0A131ZZ49_SARSC
LinkDB: A0A131ZZ49_SARSC
Original site: A0A131ZZ49_SARSC 
ID   A0A131ZZ49_SARSC        Unreviewed;      1201 AA.
AC   A0A131ZZ49;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   28-JUN-2023, entry version 40.
DE   SubName: Full=Phosphatidylinositol 3-kinase catalytic subunit type 3-like protein {ECO:0000313|EMBL:KPM04142.1};
GN   ORFNames=QR98_0025830 {ECO:0000313|EMBL:KPM04142.1};
OS   Sarcoptes scabiei (Itch mite) (Acarus scabiei).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC   Acariformes; Sarcoptiformes; Astigmata; Psoroptidia; Sarcoptoidea;
OC   Sarcoptidae; Sarcoptinae; Sarcoptes.
OX   NCBI_TaxID=52283 {ECO:0000313|EMBL:KPM04142.1, ECO:0000313|Proteomes:UP000616769};
RN   [1] {ECO:0000313|EMBL:KPM04142.1, ECO:0000313|Proteomes:UP000616769}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Arlian Lab {ECO:0000313|EMBL:KPM04142.1};
RX   PubMed=26555130; DOI=10.1186/s13071-015-1198-2;
RA   Rider S.D.Jr., Morgan M.S., Arlian L.G.;
RT   "Draft genome of the scabies mite.";
RL   Parasit. Vectors 8:585-585(2015).
CC   -!- SIMILARITY: Belongs to the PI3/PI4-kinase family. {ECO:0000256|PROSITE-
CC       ProRule:PRU00880}.
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:KPM04142.1}.
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DR   EMBL; JXLN01007572; KPM04142.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A131ZZ49; -.
DR   VEuPathDB; VectorBase:SSCA006890; -.
DR   OMA; LHKFAQY; -.
DR   OrthoDB; 10350at2759; -.
DR   Proteomes; UP000616769; Unassembled WGS sequence.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:InterPro.
DR   GO; GO:0048015; P:phosphatidylinositol-mediated signaling; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd00870; PI3Ka_III; 1.
DR   CDD; cd00896; PI3Kc_III; 1.
DR   Gene3D; 2.60.40.150; C2 domain; 1.
DR   Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic domain; 1.
DR   Gene3D; 1.25.40.70; Phosphatidylinositol 3-kinase, accessory domain (PIK); 1.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000403; PI3/4_kinase_cat_dom.
DR   InterPro; IPR036940; PI3/4_kinase_cat_sf.
DR   InterPro; IPR018936; PI3/4_kinase_CS.
DR   InterPro; IPR002420; PI3K-type_C2_dom.
DR   InterPro; IPR001263; PI3K_accessory_dom.
DR   InterPro; IPR042236; PI3K_accessory_sf.
DR   InterPro; IPR015433; PI_Kinase.
DR   PANTHER; PTHR10048:SF7; PHOSPHATIDYLINOSITOL 3-KINASE CATALYTIC SUBUNIT TYPE 3; 1.
DR   PANTHER; PTHR10048; PHOSPHATIDYLINOSITOL KINASE; 1.
DR   Pfam; PF00454; PI3_PI4_kinase; 1.
DR   Pfam; PF00792; PI3K_C2; 1.
DR   Pfam; PF00613; PI3Ka; 1.
DR   SMART; SM00142; PI3K_C2; 1.
DR   SMART; SM00145; PI3Ka; 1.
DR   SMART; SM00146; PI3Kc; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS51547; C2_PI3K; 1.
DR   PROSITE; PS00915; PI3_4_KINASE_1; 1.
DR   PROSITE; PS00916; PI3_4_KINASE_2; 1.
DR   PROSITE; PS50290; PI3_4_KINASE_3; 1.
DR   PROSITE; PS51545; PIK_HELICAL; 1.
PE   3: Inferred from homology;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          137..280
FT                   /note="C2 PI3K-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51547"
FT   DOMAIN          479..737
FT                   /note="PIK helical"
FT                   /evidence="ECO:0000259|PROSITE:PS51545"
FT   DOMAIN          886..1188
FT                   /note="PI3K/PI4K catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50290"
SQ   SEQUENCE   1201 AA;  137761 MW;  80063404B1E4ED23 CRC64;
     MDLNNESKKK KSNSTFNYIF TCDIEDSVFR VKIGNLDGIL PSTANNQKST TPSRYINVEN
     NYDYNIVEDM ESFDIEQFFP KKSIDKELKN KFDEVNYSGI ESDKQTPMVV NETKSFDTYS
     DQNAENQNFG LTSKEKKEKL SEIIFGSLKQ PFRALSINPY LTCDLVSSGR RLCPFQQTQY
     KQMKDCYEWN EWLVFPLSLD TMPRDTIVCF TVWDTIGPGK TRAVARTSIS LFSKRGCLRK
     GIYDLRLFFN EDCEEYYTKN YQNENIEKSE SIDSTKISLN EINFTDRTHR NKSLILPENE
     LIPILRKHLK LEDDIDKFSK AAKASHTRHT RIPKNFDFKS YFFTSTTQYH QSNLDYYPSG
     TSNKSHKIHQ LKKLKKLYQN NQIPKIDWLD RLAFLQIERD IVKDKSMSSY VYLTIEFPTI
     VMDGIEQTVV YFEDKDNHCC QFDIINGDIV TVPDPEINLP NLVEIKHHAL ARSARSGIAL
     CDLRPNATIR NQLNAIVNYP STQQLSNEEQ DLLWRFRFYL RNQKKAFAKF LKTVNWNSES
     EAEQAIDLMK EWAPMDIEDS LELLSAFFTH PAVRRYAVGR LKEAADEELV LYLLQLVQAL
     KYENFKDIKK SFEKELLAYQ QEFAQTPTNK EKKYFSESIS SSDNPVPESM KIFASTPNLD
     ATINSSKTLI SSKEDNEMKT KSSSAINQDD LATFLINRAC ENDELANHFF WYLCVECEGA
     KSLSSSIDLG NEKIFSNLTL PSVMSSAASS TSLIPPPLPH KEFDNIDSDI NSHHSRSKAM
     DSGSSFAINS VTDMYMIILK RFSTRLLCGT PEMVARRSFL LRQQDFVVKL VEIMKEVARE
     SGNRLRKIEK LQSILDSPEP QFRFNFSKKD PLPSPLNPNI RYVGVAAKEA MLYKSATMPA
     KIGFLTTDGN VFYTIFKNGD DLRQDDLILQ MINLMDKLLR KENLDLKLTP YKVLACSSKH
     GFVQFIDSLS IAEIISNEGS IQSYLRKISR SSVTPIVTST SSVNDFQLIS TGQTRFRNLP
     SSPQSSIYLA HGGVSPEIMD TYIKSCAGYC VITYLLGVGD RHLDNLMLTK TGRLFHIDFG
     FILGRDPKVR PPPMKITREM VDAMGGMDSD NFSKFCSLVR TAFLHLRRHA NLILNLFSLM
     IDANVPDIAL EPDKCVQKVQ DKFKLELDDE QADHYITEQV EYSVRSIMPV VVDQLHKMTQ
     I
//
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