ID A0A0C2H9X6_9BILA Unreviewed; 1207 AA.
AC A0A0C2H9X6;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 47.
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=ANCDUO_03362 {ECO:0000313|EMBL:KIH66311.1};
OS Ancylostoma duodenale.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC Ancylostomatinae; Ancylostoma.
OX NCBI_TaxID=51022 {ECO:0000313|EMBL:KIH66311.1, ECO:0000313|Proteomes:UP000054047};
RN [1] {ECO:0000313|EMBL:KIH66311.1, ECO:0000313|Proteomes:UP000054047}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Zhejiang {ECO:0000313|EMBL:KIH66311.1,
RC ECO:0000313|Proteomes:UP000054047};
RA Mitreva M.;
RT "Draft genome of the parsitic nematode Ancylostoma duodenale.";
RL Submitted (DEC-2013) 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};
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DR EMBL; KN727172; KIH66311.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C2H9X6; -.
DR Proteomes; UP000054047; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd20809; C1_MRCK; 1.
DR CDD; cd00132; CRIB; 1.
DR CDD; cd01243; PH_MRCK; 1.
DR Gene3D; 3.30.60.20; -; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR001180; CNH_dom.
DR InterPro; IPR000095; CRIB_dom.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR PANTHER; PTHR22988; MYOTONIC DYSTROPHY S/T KINASE-RELATED; 1.
DR PANTHER; PTHR22988:SF66; SERINE_THREONINE-PROTEIN KINASE GENGHIS KHAN; 1.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF00780; CNH; 1.
DR SMART; SM00109; C1; 1.
DR SMART; SM00036; CNH; 1.
DR SMART; SM00285; PBD; 1.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR PROSITE; PS50219; CNH; 1.
DR PROSITE; PS50108; CRIB; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000054047};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 480..530
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 549..678
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 705..1005
FT /note="CNH"
FT /evidence="ECO:0000259|PROSITE:PS50219"
FT DOMAIN 1073..1086
FT /note="CRIB"
FT /evidence="ECO:0000259|PROSITE:PS50108"
FT REGION 287..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 421..446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1035..1082
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1121..1207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 12..91
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 132..242
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 359..386
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1053..1067
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1121..1135
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1147..1207
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1207 AA; 134171 MW; 6DD99FBD9509717D CRC64;
MVELAEPDSD LLMELEEGAE KLTIQTKEWK EAIKHRESAK ADFEELNNEL LDERSKARRL
EKEAAETETK LAQLQSRVDT LKADLRKAES ARHDIDMELT KAKQAAESER MLKEGLQAKL
AAFGDEKPGE EARRLGEELE RLNERHAEIV AQEDKKRKQL VEHYQGQLAE LQSQFDEKDV
ELRNTRARLE EERAQFALQQ EQNSKNVEVQ YDRLQKAFEE NTAQLKLEND TLRAELSRLH
AEIEMTRPGI NEQQLHEILN WVNEEKATRE EMELLTRRIT GDIETLKLQN GTNGGTPNGQ
YSNITTPASG WGSRRMNKAA KMEILDAKKA LNAEIRAKCE LQEELSKTRS ALFASKARLD
ECEERLAASR RENETLKAEL RAGNRDSVED GRAFFNMVPE GRTSTPRDSV HNSFNTDYEI
SNSRRYGGAG LASPAPPPPA YENTVRHSQT PSTASTMLVG NRGASPKVIQ SLNNALSGRG
HQFQHVHLNA PTKCGHCTSI LVGLDRQGLY CQTCHYACHV HCSSRVVPQC PVPPDARRPL
GIDPLKGVGT AYEGLVRTPR AGGVKKGWQH TYVVVCDFKL YLYDCVTDRQ NKANEIQPVI
RQVLDMRDPD FGVTGVSEQD VIHANKNDLA KIFRITTSQI QGVSMADDGA VNRQYTLLMA
DSQEERKKWV IALNELKTLL KRSRLADRSA FVVKEVFDVT SLPSIRVAQC ATVIDRTKVV
IGFADVGMYC VELDRETLVA VGGEKENKGR FVEKVEYNAS EQLLLVMVGP PKERHVRLIP
SAALDGRDLK WIKVAETKGC HLMAMGAGSI AGTASASPAG NVHYIAVAIK KSVIVYQIDR
SEKRHRKWKE LAMPGLPQSL AIEGGRLVVG FTHSFRAWAL GDQNNTKHIS LVNMEDQSLQ
FLSQSNYEAQ LMIEVAGEST EPASREYLLV FDKLGLYVDA QGRRSRSQEL MFPSAPRPGG
FAHLSPHLCV YSENQIDVFN VMSAEWIQTI NLRTAIPLTA NGLLSLCVVN DAPFVVMLCD
VLSDEDSLYV PLTTSNTSAS SIGKRSKGKR KFSVRIPGKD DSRPGDRRSN LPISGPSDFM
HIVHMGPGSV HELQSFIDLQ PQGHSQSAGD RVRGLIPIMR STSSSSTSNH PVKQLGGSKQ
DIEQLHRARP LSTTSKSSEG SSLGRDGNTT TSSTSCENPY LEPISKQQAN VTALPQSPSS
PLSRTNQ
//
