ID A0A0V0ZNK8_9BILA Unreviewed; 2079 AA.
AC A0A0V0ZNK8;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
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=mig-15 {ECO:0000313|EMBL:KRY13986.1};
GN ORFNames=T12_12265 {ECO:0000313|EMBL:KRY13986.1};
OS Trichinella patagoniensis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=990121 {ECO:0000313|EMBL:KRY13986.1, ECO:0000313|Proteomes:UP000054783};
RN [1] {ECO:0000313|EMBL:KRY13986.1, ECO:0000313|Proteomes:UP000054783}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS2496 {ECO:0000313|EMBL:KRY13986.1};
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 -!- 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 glycosyl hydrolase 31 family.
CC {ECO:0000256|ARBA:ARBA00007806}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. STE20 subfamily.
CC {ECO:0000256|ARBA:ARBA00008874}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00779}.
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:KRY13986.1}.
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DR EMBL; JYDQ01000126; KRY13986.1; -; Genomic_DNA.
DR STRING; 990121.A0A0V0ZNK8; -.
DR Proteomes; UP000054783; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0090599; F:alpha-glucosidase activity; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd06602; GH31_MGAM_SI_GAA; 1.
DR CDD; cd14752; GH31_N; 1.
DR CDD; cd06608; STKc_myosinIII_N_like; 1.
DR CDD; cd00111; Trefoil; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.1760; glycosyl hydrolase (family 31); 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 2.
DR Gene3D; 4.10.110.10; Spasmolytic Protein, domain 1; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR001180; CNH_dom.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR030458; Glyco_hydro_31_AS.
DR InterPro; IPR048395; Glyco_hydro_31_C.
DR InterPro; IPR025887; Glyco_hydro_31_N_dom.
DR InterPro; IPR000322; Glyco_hydro_31_TIM.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000519; P_trefoil_dom.
DR InterPro; IPR044913; P_trefoil_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR47096:SF1; CNH DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR47096; MISSHAPEN LIKE KINASE 1; 1.
DR Pfam; PF00780; CNH; 1.
DR Pfam; PF13802; Gal_mutarotas_2; 1.
DR Pfam; PF01055; Glyco_hydro_31_2nd; 1.
DR Pfam; PF21365; Glyco_hydro_31_3rd; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00088; Trefoil; 1.
DR SMART; SM00036; CNH; 1.
DR SMART; SM00018; PD; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF57492; Trefoil; 1.
DR PROSITE; PS50219; CNH; 1.
DR PROSITE; PS00129; GLYCOSYL_HYDROL_F31_1; 1.
DR PROSITE; PS51448; P_TREFOIL_2; 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}; Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KRY13986.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000054783};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KRY13986.1}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..2079
FT /note="non-specific serine/threonine protein kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006873848"
FT DOMAIN 15..64
FT /note="P-type"
FT /evidence="ECO:0000259|PROSITE:PS51448"
FT DOMAIN 955..1212
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 1767..2053
FT /note="CNH"
FT /evidence="ECO:0000259|PROSITE:PS50219"
FT REGION 1240..1283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1296..1317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1349..1427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1441..1473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1523..1543
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1571..1615
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1635..1702
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1268..1283
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1399..1415
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1441..1456
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1635..1665
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1671..1701
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 984
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 2079 AA; 233633 MW; 5D84FC02AAB059AA CRC64;
MCKVALITDC FLLLLLCQMI PILNGGIILD CHPDPMATME QCHSRGCVWQ ASSEPNVPWC
RFFDNPQDPH FAGYEITSND HFTETVSPYF VANLKRKPTP TLFGDDFHQA LMKVESLSDS
IISITFTSNH SVDAAGHHVH HVHLDTALNN FRQAVLNKAP VDPLYRLYLD QDPFGFAIVR
NKTGRVLVDS RNLPGFTLAE QYSQLTFKVP SEDLYGLGEN VHEQLKHNFQ WRRWTMMARD
HPPEGGPSNL YGVHPFYLCM EDEEGNAHGV FIFNTHAMDV TLQPDPSVVT FRTIGGSLQL
FVMLGPTPAQ VVSQYLTLVG NPNFPPYWSL GFHLSRFGYK NLTMLAEVVE RNRNANIPQD
GQFLDIDYMK NRMDFVVDDD NFKNLNNFVD QLHQQYQMKL IPIIDPGIPS QPEQPYEPVE
HGLKMDIFIK DANTGQPLEG IVWPGKTYWP DFTNPDTVTY WTYFLKRFHK TVSFDGIWID
MNEPANFVDG STSGCTQNKL NQPPYNPVAG NILEKTICMD ADQYLGKHYH LHNIYGLSES
IVTHTALSNI IPGKRPFILS RSTFSGSGQF ANHWSGDNWS QWSHMRWSII NMLEFQLFGI
PMTGSDICGF NGNADEELCL RWSQLGAFYP FSRNHNTDNS DVDQDPASWS PETTAAIRKV
LLLRYSLLPY LYTLFFWAHF VGATVVRPLF FEYPADKTAR TIDDQFLWGS SLMIVPILEP
YSTLREAYFP AGRWYNLTSL EEVEIESEYR NRTVYIGKQN IGLFFKGGSI IPWQIPVNNT
HWSRQNPINL LICLDEEQRA VGNLFWDDGE AYDSVVENKH TLVDLKFEET RKFQLTAVHY
YTELTVDKVV VLGLQGGLPA GATLDGQRLP SKHFQIDPDK TILSLLHLNI TFSASSFVHL
IELECYLPLK AAKPEVSEHS RFHFLFSNKS SATMTANCSL DDIDLNALRD PAGIFDLIEV
VGNGTYGQVY KGRHVKTGQL AAIKIMNINQ DEEEEIKLEI NVLKKYSHHR NIATYYGAFI
KKQPSSTGKG DQLWLVMEYC GTKGLSLKEE WIAYVCREIL RGLAHLHANK VIHRDIKGQN
VLLTDNAEVK LVDFGVSAQL DRTVGRRNTF IGTPYWMAPE VIACDENPDA TYDSRSDLWS
LGITSLEMAE GQPPLCDMHP MRALFLIPRN APPRLRSTKR WSKKFHSFVE TVLVKDYHQR
PYTEQLLRHP FIRDLPTERQ VRIAIKDHLD RHRRLTRRDH TEYEYSGSEE EEEEEDQSRA
EINERSSKGS DGPPTSVLPV QDDNTLRKNF LKLQEGRSLF ESPAPQSVKR QPRPTAGVAR
LGAAATRALA PKSRHAHQYV APNFKYTKYG PSPEQQDVNK HHMQVKHRPL SQHSHHHDNV
AAAAKVRYRQ SAGGKCGNSS RDVERRSDRP RSHRHPSPPS NPNLQSDHSV GVFAKAVAQS
PLATSFQQQQ QQQHSAAGHH HPHHHHHHQL QLGSAVGVGS VLAQNLQRKH SAPVLNRRPE
DLDQLAAELS QMGNIKSVVN KGKSTAMNSE SPPVPPPRDA SISSSALLQE SSKEMEINGN
DDDLATVTAS EPVRPLSECK EGTLRASVSS GDMAPEKPLP PTPDASSPGD DDDGTLPAAL
IVVLKFDDIG QRTAFASSPQ FGSSSSSGGE LDSAERAQAL SRRSSTVLPD LLPKNKVSSN
VTQGNSNEAL STSSTPPPPN ALQKKEKSFI VFGFGSGAAG VGAGGSTVER PTRTQREIAD
VNVNVNPASS QSENSVPEIR KYKKKFSSEV LCAALWGVNL LIGTDSGLVL LDRSGQGKVY
HLINRRRFDQ MTVLEGQNIL VTISGKKRRI RVYYLSWLKQ KILRSEGVEK RNGFVNVGDL
QGAIHFKIVK YERIKFLVIG LESSIEIYAW APKPYHKFMA FKSFGQLTHQ PLIVDLTVEE
NARLKVLYGS SEGFHAIDLD SASIYDIHVP THVQGFIVPH CIVILPNTNG MQLLLCYDNE
GVYVNTYGKM TKNVVLQWGE MPTSVAYIST GQIMGWGNKA IEIRSVETGH LDGVFMHKKA
QKLKFLCDRN DKVFFSSAKG GGSCQIYFMT LNKPGMPNW
//
