ID A0A1I8F1Q5_WUCBA Unreviewed; 2548 AA.
AC A0A1I8F1Q5;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
OS Wuchereria bancrofti.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Wuchereria.
OX NCBI_TaxID=6293 {ECO:0000313|WBParaSite:maker-PairedContig_926-snap-gene-3.19-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:maker-PairedContig_926-snap-gene-3.19-mRNA-1}
RP IDENTIFICATION.
RC STRAIN=pt0022
RC {ECO:0000313|WBParaSite:maker-PairedContig_926-snap-gene-3.19-mRNA-1};
RG WormBaseParasite;
RL Submitted (NOV-2016) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001433};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1; Evidence={ECO:0000256|ARBA:ARBA00000775};
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DR STRING; 6293.A0A1I8F1Q5; -.
DR WBParaSite; maker-PairedContig_926-snap-gene-3.19-mRNA-1; maker-PairedContig_926-snap-gene-3.19-mRNA-1; maker-PairedContig_926-snap-gene-3.19.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd05170; PIKKc_SMG1; 1.
DR Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic domain; 1.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR003152; FATC_dom.
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; IPR031559; SMG1.
DR InterPro; IPR039414; SMG1_PIKKc.
DR PANTHER; PTHR11139; ATAXIA TELANGIECTASIA MUTATED ATM -RELATED; 1.
DR PANTHER; PTHR11139:SF71; SERINE_THREONINE-PROTEIN KINASE SMG1; 1.
DR Pfam; PF02260; FATC; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR Pfam; PF15785; SMG1; 2.
DR SMART; SM01343; FATC; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51190; FATC; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nonsense-mediated mRNA decay {ECO:0000256|ARBA:ARBA00023161};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1934..2271
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 2516..2548
FT /note="FATC"
FT /evidence="ECO:0000259|PROSITE:PS51190"
FT COILED 2305..2339
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 2548 AA; 289752 MW; 8740B704532F8237 CRC64;
MGCMNQRYSI SRLLRWSNAR LLIINDKKSY SKDERIAACE QLQQALTLAS DVSNIGCDWK
KLIEDLLYCI KTRQQFEVKR CVSDCLGSLG CIMFSQYNEY LKVMLGEAKL IPDKYEDDKA
LILKAIFSSL NLIGTFAWQS RIRPQDVDAL MTAMKNWLEV NDSSIVLISL LDTCLAVSKY
FPAIFKHSFD DVVDFTVGWY IEPEQPIAVL DKCHQMLVEL RPYWHSAVPA AITLMKQFLD
DASAYIEDIR MSESTPENML AKTAAILRAL STMLEVMNTP VNPLVVDFTE KVFGRIIRLL
THLNDVFAAK IGTVFGYMAE VLCVALKAYP KLDFLINSMK TLKIMLEHPS VNEKSMLKIL
GCSGKIIDNM TPEMVVEIVD YVVGDGGPLN HVITRSQRVM QAYGNVLGKL LAPKNLSTLQ
VVYNRVREDV RSKFSFSIVH RHVVTNCLNI LQATEVEAYS TNSIVIEKKL MIYINALYSL
GIVKNSLIAV RFSMMGLSPS LFTFLMTETP ITKKQFIINH PGCHYALLYI IKAHSEKHEN
FVANSSLLID KNSLTLVTEP ATAKHTTTIL NTVTKLLILD DLLWTDTRNL LVDWIHGLVF
SLTQDVLQHI LNKPETVEMR TALLDSFVRH SLPKKTSLDN KIFCNPEAFV VHWCAATTSH
RVRHFTLLRR LAVFNLIKNE KAEVTAKFVR HIFEQCHSGC QNKITGIWQA TPPVLFIRNG
LTECAQDLME FGQQKISESL FTSEHFKTFA DFLLNSVLPT YCFNNIDDGY WMSDTAATIY
AGAMGDINTN IDCISKWRWI IAQMAQFCVN NRLKTPLGKP LDTFLAFENE IRRLASNALS
RKPLPVGKGA KDEVVQKTVT ISRRGVEDED EAEVEIEREA RQLTTSEQWW RVRALLDMIE
VLDKLIVYAC HGAIFQLSTV SQVSQQFLTT NQASCANWLS RLCLPMMAVA YTSSNFAQVV
RLGGCLLRDI GKRTEEKGSK DNIDEKGLSA IECIRTAGEI DSVAHTCITW IVKALIDLGR
PQSILGLYAW VKKIYGKQYV WIKCAAHMAA GRIELALNGL QECLRNENSS ENIQKTIRQL
IIFGLEVLRN SEEIDIFWRT LYGVLDSKPN EVPDGFEELT WKRMKSLTTF DNCLKDQSVM
SVPWDIRNNF IHTELKLMEI IHDHSRDSKD NKTDVADLTR QLSEDARILV LADTGLQIFT
RASALHLLAT AVKDSRKPYH KQSIIANVVD PSFLFDWKNG PPIQRLALGQ QLSTWLQYTQ
NRENGGSSSL RIISNEAAYH LEMARLARKT KNYRLAEKHI KMHYNKRLPT LDSFQQNILR
MWSISEMADT DRARTFLQGK AFSLLMNAVA DEIDRLIYKS NLMFNGTPTV APDTLIAVLT
QQLNHHATIE VDSAVLSMGP NIVASNHHHQ EQNKVSAKAI IQLARWLQME SSLLPVAMSY
SIRIAFHMFG VEQSRLPVLG PSGIIDSLAG ALLSTSCKLS PHLAKAHLEL GNWAFKRATD
ADNEIRLSFI NEECDTMKWQ IKNACTSMED SVMENLLQTV QKCSSLAAIL PDCKALVGNS
INEQTCDLLF GPRSIVQEIW KGANSRHLAF CNCAAHSYFA YIAVSGREAK EGTIGVVMAT
LRILQLLVKQ YDALHHLILT EMLQVNELMW KDILPQLFAR LNHPVRAVRD TLCTILERIA
ATSPHALCYP AIVGTTQPIV IHNEYVDNGE VEKNDFVDVI DEEKKKRADQ DRSLMFECCQ
RIVTRIQALF PDLVKDVTEF VKELQRIDML HEERWTFVLT NLDLEMNRRI LQIEAEMMKT
LMNTHLSDDE KKEIIHEKTI IFTSLVYRIV EDLYEKTCTS VPVTINEKQF QDTYLATIEE
AMKTLRLNRS EPRQAWASFK LLLTQLNQRA NRRSFVFLQM ADISPRLTAL NKTHVPLPGQ
EHKNFCDIVM LERISKQTVI LPTKTRPRKV VFHGSDGKDY PFLFKGQEDL HLDERIMQLL
RICNLMLSTK ETDWPSYIAE NYSVIPLGSR SGLIEWVEGA TPIFQVYRKW QLRKAAENIA
NQKVNEVERP SALFFRKLRA AFQANKIPKE SITDRQKWPY PVLKGVVEDL IEETPRDLLS
RELWLRAGSS DTWFRVTERF ARSTAVMSVL GSILGLGDRH LDNVLVNFEF GHVVHIDYNV
CFDKGRNLRV PEMVPFRLTG NIVRALGPTD IEGTFRLSSE NVLRKLRAGK EILLTMLDAF
VYDPLVDWAA AQDDLGSKSM IGIATFIAVY GVVDGHSDIL HAMTLSLFAL RARELSSSWL
DNRNHLLCML SSIVSILRKL YGNTQKDAES RPQNWEEEID KLEVEKLSVE RDLKKAVAEH
HSMMHDIRPL LRSFAHASFD LAASVCQKNE SFALYLQRYK ELFSEPLIKG LKLLDDPYNS
CAACIDLFLS VIDNIPSIYD NLLLLEKVKE REELPSCSGK SSPVERHKGR IIILNGNRII
LLVYKELIYC GFEGQQQQNL HGKHVSKRIR MKLEGKVTPG INKNENTKID ANIVSEPLTP
SEQIDLLIQQ ATDISNLALM YEGWTAWV
//