ID A0A0G4F816_VITBC Unreviewed; 3367 AA.
AC A0A0G4F816;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN ORFNames=Vbra_14744 {ECO:0000313|EMBL:CEM08834.1};
OS Vitrella brassicaformis (strain CCMP3155).
OC Eukaryota; Sar; Alveolata; Colpodellida; Vitrellaceae; Vitrella.
OX NCBI_TaxID=1169540 {ECO:0000313|EMBL:CEM08834.1, ECO:0000313|Proteomes:UP000041254};
RN [1] {ECO:0000313|EMBL:CEM08834.1, ECO:0000313|Proteomes:UP000041254}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Zhu J., Qi W., Song R.;
RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
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};
CC -!- SIMILARITY: Belongs to the PI3/PI4-kinase family.
CC {ECO:0000256|ARBA:ARBA00011031}.
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DR EMBL; CDMY01000387; CEM08834.1; -; Genomic_DNA.
DR STRING; 1169540.A0A0G4F816; -.
DR VEuPathDB; CryptoDB:Vbra_14744; -.
DR InParanoid; A0A0G4F816; -.
DR OMA; HYARGLQ; -.
DR OrthoDB; 8448at2759; -.
DR Proteomes; UP000041254; Unassembled WGS sequence.
DR GO; GO:0032991; C:protein-containing complex; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProt.
DR CDD; cd05169; PIKKc_TOR; 1.
DR Gene3D; 1.20.120.150; FKBP12-rapamycin binding domain; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 4.
DR Gene3D; 1.10.1070.11; Phosphatidylinositol 3-/4-kinase, catalytic domain; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR003152; FATC_dom.
DR InterPro; IPR009076; FRB_dom.
DR InterPro; IPR036738; FRB_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR024585; mTOR_dom.
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; IPR003151; PIK-rel_kinase_FAT.
DR InterPro; IPR014009; PIK_FAT.
DR InterPro; IPR026683; TOR_cat.
DR PANTHER; PTHR11139; ATAXIA TELANGIECTASIA MUTATED ATM -RELATED; 1.
DR PANTHER; PTHR11139:SF9; SERINE_THREONINE-PROTEIN KINASE MTOR; 1.
DR Pfam; PF11865; DUF3385; 1.
DR Pfam; PF02259; FAT; 2.
DR Pfam; PF02260; FATC; 1.
DR Pfam; PF08771; FRB_dom; 1.
DR Pfam; PF00454; PI3_PI4_kinase; 1.
DR SMART; SM01346; DUF3385; 1.
DR SMART; SM01343; FATC; 1.
DR SMART; SM00146; PI3Kc; 1.
DR SMART; SM01345; Rapamycin_bind; 1.
DR SUPFAM; SSF48371; ARM repeat; 2.
DR SUPFAM; SSF47212; FKBP12-rapamycin-binding domain of FKBP-rapamycin-associated protein (FRAP); 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS51189; FAT; 1.
DR PROSITE; PS51190; FATC; 1.
DR PROSITE; PS00916; PI3_4_KINASE_2; 1.
DR PROSITE; PS50290; PI3_4_KINASE_3; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000041254};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1846..2602
FT /note="FAT"
FT /evidence="ECO:0000259|PROSITE:PS51189"
FT DOMAIN 2847..3160
FT /note="PI3K/PI4K catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50290"
FT DOMAIN 3335..3367
FT /note="FATC"
FT /evidence="ECO:0000259|PROSITE:PS51190"
FT REGION 278..298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 586..621
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 700..737
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 898..939
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1532..1560
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1623..1722
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2206..2231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2378..2459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2712..2784
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3133..3265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 278..292
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 586..603
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 700..720
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 906..936
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1532..1553
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1651..1665
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1678..1698
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2208..2229
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2721..2739
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2749..2766
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3133..3157
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3158..3172
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3193..3210
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 3367 AA; 367419 MW; AECC2E1452EF916B CRC64;
MFCGRQRLKN RCELSCGELG GERKSLFFLF SLEIKAPQLK ISLLRAFDSS VPSLTYSKML
ESKYLADLKS KNESVRAKAA KNLRIHVEAE AKEMSGGTFT KFMADLNKRI YDLVSSPHQE
DKIGGIMAID ELIDVQCDEN ETKIIRFSNY LRMIFQQCSS GPLEHSILPR ATRALGHLAR
AGGTMTADFV EFELRRSLEC LQSGGGSDPR SEYHRYAAVL ILKELALNAP VLFGPHVNAF
FDHIWVAIQH EPKTVIREAG VEALRAVLQL LAQRDQNQPA VTNGTTPTPQ VSAAAAAGPG
SLDGKGGGAA VAATAGQARQ RSRYRTHISR TIWEKTQQGL RSSDALALHG SLLAVGELLT
HDLARPEQAP TPTDATSDQL VTSPRFAEIC DLVFKFKSNR HRLVQRTVLQ LLPTLAKFDP
ASFVALNYLD KAVAHLLQTI RSGGTDRELA FEALGDLILA VKEAILPYVD RILTVVHDAL
SHRLGGGGMA ASLGLSMGGG SRRRQEAQTQ EALICISKLA KAVGPQLAPQ IEQLVDKMFV
GGLSPTLLEA LNQLCKTIPS LLPVMQNRLL HSISLVLADE SVTNLDSGDT ATHPSQATSA
PSGASAAAEG GAAGAGSGAG GAPYRSEEHA RLVVLALHAL GQFGTLTYNL QTNSFVCECV
LRYLDHPMPA VRKEAALTAI QLLLPKPFSV PTVVIQPTAD AATQPSSTQD GTQTSAAGAG
GGGTRASGAS GRPTQAPNEG STILAGGFLQ HVVLCRPHQL LAISRVIRRL LTFAVADPEA
SIRHAVLEGF DFRFDPFLCE PSCLAALNQS LHDESLQVRK TAVRLMGRLC LHNPAYVLPA
LRKILIQLLT DLEFAPDARH RDEAAELLGD LILEAQQLME PYATSVIRHL ITKLKETQST
QIDPASPPGH PIPPSLTPSP SPPSLSSSPP VPSPAPSSST LIHQRAAFGY VSSHARSVSM
GLPQPPPPTP SFYTHLFTAV GYLSEVGGTE IRHLMDDLLP ILVEALQDTG TTAPSGIKRE
VAFRTLSQIV RNTGAVLEPY LKYPSLLSYM IGLLRSDSTS DVHWPWHWPL RKQIIRAIGT
LGALDPYRFH QLERLPRTQP QQTKTRGLEA PPLGANEADH RNLQWENVKL AGERHMKRQQ
EGDFEVVTGL GVAASRHGMP VLGGGGGRAA GGEDDKGVDL FSSTAIRALL RMMAENKSKG
RGSASQPASG LPGYTYWGGV AYGQTAMVGG AAGGGGGVLS SHQTSVMTAM MCIFKNLEHK
TVYFLPQVMP AFLDILHSSD GESQESLLLN LSDLIAIVGA PMARYLPALF DLLTQICQGH
LKAHQQQVII TGGGGGAQLA PANIAAAQVV GGVLQAEQAA DKTERERGTT ALLRVLEEIA
THLPNDFETY MGQLIPILLN FLQNDQSERR EVAFGVLQAL GVFGKGVQDY IYLVVPALTK
LAENEDAPPS LRIHSIYLLG HLTHTCTFPQ FSARIGHALI RILDATSLPA TSLATAGNHK
TKAAKGKTAT TITIPLQPPS IAMSAADADA TPTPSLSAVG SLTGPSEMGT TPTLPSGGVV
GGGRGWDVGV GSEGEVHEMK MAALQTLAML YRAFGADFAP FVPLVKMVTH RHRLPVFAIF
DPFSPNALPT PPPTNPFATR RGVATQSPAM PPHPDLQSNA SASLGPSDPF GAASADNKDA
SSAPQPQPTS QSVGHASQQG GGAALMGGAG GGQQRGRGMD VGVGPLQVHQ QSLKQAWETN
NRSTREEWAE WMRRFSLELL RESPSPALRT CWSLSQVYQP LSKELFPVAF LSCWLHLYDT
MQDALAKALE QALQSPNLPP DVLQTILNLA EFMEHQGSPL PLDYALLGGL AEKSHAYAKA
LHYKEREAKT AREACVEALI SLNNQLGQRE AATGVLVYAQ KHLNVTLKES WYEKLHRWED
ALEAYEIRQL DDRTNLEWTR SRMRCLHALG EWDRLSELSR KVWDSNHPGL RDPLRRHEVA
YLAAAAEFNL RKWDKMNDWV AALEATPSHT YEGCFYSALL AIHQEDYRLA TRLITKSREI
LDPELTALVG ESYERAYGAL VKVQQLTELE EIIAYKQTAS ESRRQMMRKM WATRLQGCQP
KVEVWQAILQ VRSMVLPPTE DIPIWLRFCS LCRKQEQLSL SINIVKELLT ASDTQPPMTD
SRVVVAHLKN LYAGGHKETA QSQLRDFCTS CNWYLFDQPL VPPLPTDTAS LHPTSDAAIS
DQQQQQHHPP GDFLLPLGLT SLTNVTSASA LSGWEDTHSH PHVAERVGVG VEGDGAASGG
GGGGGVGQMR GKGMRRVNKH LCHLLSKCHL KLGLWTKEVL EEKRGADWIN DQTLQEVLLY
FRASVRLSPT YYKAWNAWAN TNFHVVQLFD LYKSQHPAHV HPHACPPPPM VRSASPSQHQ
HQHHPSLPVS PAHPHHPSPY IHPISHHPLL PHHGGHASDR AMPDIHTQPP SLFAEAKDGG
EGDVEGFLSA ASSVADRERV GRGGMDLHLQ YVVEAVRGFV KSIALGTRKA RGKLNCKANL
QDVLRLLTLW FRHAGHSALE SALQEGFQTT PLETWLEVIP QILARLRSSN KALQKTIHAL
LKRIGKEYPQ ALVFPLTVAS KSAISELSKS ARQLLQEIEQ HFPVLVQQSL MVSEELIRVS
ILWHEQWYEA LEEASRLYYS ERDIDGMVQV LLPLHNMLRR GPQTLRETAF IQAFGRDLEE
TESWIKRWKR HVPANDAKDT PPPQKNGQQG GTTKGSAIGK AASGQGGGGG GGQGQQQQQQ
GKERERAPSG GTNKAGGVSS QQPQRADIDQ AWQIYYRVFQ KIHRQIQSLT HLDLQYVSPN
LLSAKDLQLA VPGTYKPDEP PVRILAFTPS IQVVNSKQKP RILQMEGSDG LKYKFLLKGH
EDLKQDERVM QVFGLINDLL LSHSEASQRD LAIARYAVVP LSTNSGLIEW VPHCDTLHSL
IKMYRDANNI TLSLEHNLMK SMYAKCDDLC LLQKVEVFQY ALDCTSGEDL EKMLWLQSSS
SEVWLARRTV YCRSLAVMSM VGYILGLGDR HPSNLMLTRS SGRVVHIDFG DCFEVAALRE
RFPEKIPFRL TRMLLNALEI SGVEGNFRHT CELVMGVLRS SKDTLMAMLE AFVDDPLITW
RLLPAAKLQL QPHQTTTTAN TTPQQPPLTQ QQQPPTTADP LPSTPPSSDQ PPSGAPLTGT
DPMGVRSGAF PKLPTHPEDR EGEQAAMREE GGDDGGGGGG GGGEGAVGQN GRQRSAAVVE
QHPREPVTTR TTAAGLPPGG DLRHGGFPQG RVSMAGDMEK DPHMVSTHIK QSRQRELKQY
LGPEGMRANP EMLSTYARSV IRRVDSKLSG TDFGSEHDIP GQVERLIQEA TSHENLCQCY
LGWCPFW
//
