ID A0A0V0ZUV8_9BILA Unreviewed; 832 AA.
AC A0A0V0ZUV8;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, 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};
GN Name=aak-2 {ECO:0000313|EMBL:KRY16237.1};
GN ORFNames=T12_10318 {ECO:0000313|EMBL:KRY16237.1};
OS Trichinella patagoniensis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=990121 {ECO:0000313|EMBL:KRY16237.1, ECO:0000313|Proteomes:UP000054783};
RN [1] {ECO:0000313|EMBL:KRY16237.1, ECO:0000313|Proteomes:UP000054783}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS2496 {ECO:0000313|EMBL:KRY16237.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the acetate uptake transporter (AceTr) (TC
CC 2.A.96) family. {ECO:0000256|ARBA:ARBA00005587}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. SNF1 subfamily. {ECO:0000256|ARBA:ARBA00006234}.
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:KRY16237.1}.
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DR EMBL; JYDQ01000081; KRY16237.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0ZUV8; -.
DR STRING; 990121.A0A0V0ZUV8; -.
DR Proteomes; UP000054783; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004679; F:AMP-activated protein kinase activity; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProt.
DR CDD; cd12122; AMPKA_C; 1.
DR CDD; cd14079; STKc_AMPK_alpha; 1.
DR CDD; cd14336; UBA_AID_AMPKalpha; 1.
DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR Gene3D; 3.30.310.80; Kinase associated domain 1, KA1; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR032270; AMPK_C.
DR InterPro; IPR000791; Gpr1/Fun34/SatP-like.
DR InterPro; IPR028375; KA1/Ssp2_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR049020; PRKAA1/2_AID.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24346; MAP/MICROTUBULE AFFINITY-REGULATING KINASE; 1.
DR PANTHER; PTHR24346:SF82; SERINE_THREONINE-PROTEIN KINASE MARK-A-RELATED; 1.
DR Pfam; PF16579; AdenylateSensor; 1.
DR Pfam; PF21147; AMPK_alpha_AID; 1.
DR Pfam; PF01184; Gpr1_Fun34_YaaH; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF103243; KA1-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:KRY16237.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000054783};
KW Transferase {ECO:0000313|EMBL:KRY16237.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 541..559
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 632..651
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 657..676
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 688..713
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 733..759
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 771..792
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 16..268
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 498..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..528
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 45
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 832 AA; 93970 MW; 8123E1C58E30B8F4 CRC64;
MVDLLKEKPV VKIYHYILGE TLGVGTFGKV KVGVHDVTGH RVAIKILNRQ KIKNLDVVGK
IRREIQNLRL FRHPHIIRLY EVISTPTDIF MVMEYVSGGE LFDYIVKRGR LQEDDARRFF
QQIISGVDYC HRHMVVHRDL KPENLLLDSE NNVKIADFGL SNILTDGEFL RTSCGSPNYA
APEVISGQLY AGPEVDIWSC GIILYAFLCG TLPFDDEHVP SLFRKIKAGQ FPIPSYLDDS
VVDLLLRMLQ VDPMKRATIK DIVAHEWFKK DLPAYLFPPL NEQEASIVDM DAVRELSEKF
RCDEEEITVA LMANDPHNHL VIAYNLILDN KRIATETAKL TMEEFYSPDL PTDRPASIIA
RHPERIDATR TFTPTLESVP NAQPGNGLQV TVSRPLVQSL RRARWHLGIR SQSRPEDIMI
EVLRAMKALD YEWKMINPYH VIVRRRLNPT WPKMSLQLYQ VDQKGYLLDF KSLSSDDLLD
CHLAGSCGSC RHRLAASSDR TQSLPNNPAQ SSADAEPSTS SAATEQPPSE GAAQPKPPQT
MLFFEMCAAL IGSLALVYFG KTLSNSNNTN NNNKMDDSIQ KEKQHIVIDA ESMVSDSSLY
KQFKEKDDYL LRQIENLSGQ LRRARSLDTT EPAIIGFGGL GFAILTSQFH RFGHTSVGLN
ACVTFLFGGI LQFLAGVQLH KRNNAFSYGI FCMFGVYSML LGVITFCHLG NFFEVKPLDM
LPLNIMFALY NGFWLAPTMT MSIASFALTC SFFGAFVFLC LGEAVPPHVE YCTSLASSVC
FIAGGILSWY FMLNLVYVEI YHRDVFPLGP PPVKLFQNWI GYFKKHKKRS TI
//
