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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