ID A0A1V9Z5F7_9STRA Unreviewed; 1707 AA.
AC A0A1V9Z5F7;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=IQ and AAA domain-containing protein {ECO:0000313|EMBL:OQR93162.1};
GN ORFNames=THRCLA_08533 {ECO:0000313|EMBL:OQR93162.1};
OS Thraustotheca clavata.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Thraustotheca.
OX NCBI_TaxID=74557 {ECO:0000313|EMBL:OQR93162.1, ECO:0000313|Proteomes:UP000243217};
RN [1] {ECO:0000313|EMBL:OQR93162.1, ECO:0000313|Proteomes:UP000243217}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 34112 {ECO:0000313|EMBL:OQR93162.1,
RC ECO:0000313|Proteomes:UP000243217};
RX PubMed=25527045; DOI=10.1093/gbe/evu276;
RA Misner I., Blouin N., Leonard G., Richards T.A., Lane C.E.;
RT "The secreted proteins of Achlya hypogyna and Thraustotheca clavata
RT identify the ancestral oomycete secretome and reveal gene acquisitions by
RT horizontal gene transfer.";
RL Genome Biol. Evol. 7:120-135(2014).
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:OQR93162.1}.
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DR EMBL; JNBS01002273; OQR93162.1; -; Genomic_DNA.
DR STRING; 74557.A0A1V9Z5F7; -.
DR OrthoDB; 75454at2759; -.
DR Proteomes; UP000243217; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR14690:SF0; IQ AND AAA DOMAIN-CONTAINING PROTEIN 1; 1.
DR PANTHER; PTHR14690; UNCHARACTERIZED; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50096; IQ; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000243217}.
FT DOMAIN 23..282
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 288..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1175..1241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1305..1343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1683..1707
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1186..1228
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1312..1334
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1683..1698
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 52
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1707 AA; 193183 MW; 323688B7DCA1CF15 CRC64;
MEALKVFNVN LVLNTFYLME EQYELGELLG TGSSAQVYWA ERLRDKNVVA IKVVDKLQHA
QLRTQSKSIA QSEELQELAI QQTLDHPNVL KVLDVFQDAR NVFIVLEPCA NGSLQALVKG
KRAIPEEEAK FYVNQLIAGV DYLHRAHIIH RDLKLSNLLL TENRVLKIAD FGLATNVTTN
IIPSTICGTP NFIAPEVLLG KSYSYAADLW SIGCIVYTLL TGSPPFQGEN VSETLRNISA
QTSSLIFPSY VSPIAKDFVQ SLLCMEPTER LPCHALLHHP WLHQNPIRRK VKRTKPTAPR
TPRRPQPQPT FHVAANENSS PTSSVHLEDD EIDDTDIAKL QTMLDKISQD PRPQRALKQE
PDIIPIAEPI PLLPEFPDSI EFNVEYHTIL DLPPDEIVAN LRCIWTPQNF TLQSRLNELV
VYTIADNRIS GKLQNDVVFD EDLTSISNTI PRIVTWVRLA QICLSLHLSS PKTHLFRLPD
TTIEALQRGE DMERQLRSQQ MAPHTRSANH VRSAELFSIG RGECLDDGTL RIAFVDGSEL
MLDACASSVE FRNFDEPFAK KNRCNYGRLF KVFLEAMDEA KIESSNNSEV PLAPATTDYV
PQDHVLVEDM LIAIASNMNA FYLALDDITL PVVVYISLAL TKLQPAVIQA SHETMVYLRV
ILSIDTIISW LRKYPEVHLQ NLFKTAIIKQ RESHETMAKQ PIILTSFNIA SAIIHVGEQL
QTVQSTSIIE HEQEPCKIES PKKRRQSKPK VEEVKHAAIP KEGLHVLLAE VVYKYQHRAI
ARKPQFTINS SKSDTSIAAS RRHRSLSFAK RRNGQLVRTS LRMKLMLRST FDTKWQSAMT
ELNEQVHIED HTLDAEEGQE VQPPPEVSML EAFQHYACLY IKYVQIFTTL EECYDQMVHP
QKRIDVKRIM ELVMTRVVEL KHDLVKWNPP NPDVRTTPEQ NFPWEYVNLD DLLVDLKLPP
SLLEVPVPKY FVEDNSVELK KRDRLVKGYM KLKLGVEALY VEDTETSVSM ADAMSLDEAL
QIIQRNERGR QGRQRGILVY ELREEEKQRR IYDNTQTPEM DPELAAANIQ RVFRGHNSRG
KAAVERDEEL VFIGMKPPLV DKAVELENAL ALAKIKRKTQ QADNKEEYEK SLTDIHEIVR
NEEGPFMKEK MLEERRKWIS DMMAQGQLPE DLAGYYLMIN PPPPEAEPKE EVKDKKGKKE
EKGKKGKKEE KGKKGKKDEA KDEAEAAPER PPPLTGPSEL CTKMATGVDM FEKVWLERDE
ADNFHQKYDI DLAKDVVRAP VETQVRAQVD EMLVLQLANI KAQLEAAASG KKKKGKKGKK
GKKGKKGKKD KKGKKGKALP GDKIAELKGR TPDTMLAILV EQKMVNNVKP CHVNEFIGEF
NYLGTVYQSS DRRDRFGNWV PQDPSAAQLR AAVVEYAILP LGSPPVREKV KHIRSILFYG
PKGSGKTMMA RAIAHETGAL FFNISASNLV GKFSGKNGPT KCIHMIWTLA KAMQPAVIYI
DECEQIFAPG KKKASDGPTG YRKDLITYLK SLVVTDRVLI IGTSSNPMAG EVKDFRAFFD
KFLYFPYPDY PSRVLLWRKT IQDTIDSRAT SLPVKPRIPD DLDVSTLAHI SEGYSSGSVR
MAVDQTITAR RVERMEKRPL REDEFISALS RQTATFADDN DKFKNFTAQI TGLKETRDKI
RKAALGDGDA ADDKKGKKGA KGKKGKK
//
