ID A0A2T7NTI5_POMCA Unreviewed; 2543 AA.
AC A0A2T7NTI5;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=C0Q70_14970 {ECO:0000313|EMBL:PVD24487.1};
OS Pomacea canaliculata (Golden apple snail).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Caenogastropoda; Architaenioglossa; Ampullarioidea; Ampullariidae; Pomacea.
OX NCBI_TaxID=400727 {ECO:0000313|EMBL:PVD24487.1, ECO:0000313|Proteomes:UP000245119};
RN [1] {ECO:0000313|EMBL:PVD24487.1, ECO:0000313|Proteomes:UP000245119}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SZHN2017 {ECO:0000313|EMBL:PVD24487.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:PVD24487.1};
RA Liu C., Liu B., Ren Y., Zhang Y., Wang H., Li S., Jiang F., Yin L.,
RA Zhang G., Qian W., Fan W.;
RT "The genome of golden apple snail Pomacea canaliculata provides insight
RT into stress tolerance and invasive adaptation.";
RL Submitted (APR-2018) 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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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:PVD24487.1}.
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DR EMBL; PZQS01000009; PVD24487.1; -; Genomic_DNA.
DR STRING; 400727.A0A2T7NTI5; -.
DR EnsemblMetazoa; XM_025251568.1; XP_025107353.1; LOC112572054.
DR Proteomes; UP000245119; Miscellaneous, Linkage group lg9.
DR GO; GO:0005829; C:cytosol; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0009966; P:regulation of signal transduction; IEA:UniProt.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 2.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 3.
DR Gene3D; 3.30.70.1390; ROC domain from the Parkinson's disease-associated leucine-rich repeat kinase 2; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR032171; COR.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR020859; ROC_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR48056:SF81; LEUCINE-RICH REPEAT CONTAINING PROTEIN; 1.
DR PANTHER; PTHR48056; LRR RECEPTOR-LIKE SERINE/THREONINE-PROTEIN KINASE-RELATED; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF16095; COR; 1.
DR Pfam; PF00560; LRR_1; 1.
DR Pfam; PF13855; LRR_8; 3.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF08477; Roc; 1.
DR Pfam; PF19056; WD40_2; 1.
DR PRINTS; PR00449; RASTRNSFRMNG.
DR SMART; SM00364; LRR_BAC; 10.
DR SMART; SM00369; LRR_TYP; 9.
DR SMART; SM00175; RAB; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF48371; ARM repeat; 2.
DR SUPFAM; SSF52058; L domain-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF69322; Tricorn protease domain 2; 1.
DR PROSITE; PS51450; LRR; 5.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR PROSITE; PS51424; ROC; 1.
PE 4: Predicted;
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000245119};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000256|ARBA:ARBA00022777}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..2543
FT /note="non-specific serine/threonine protein kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015675857"
FT DOMAIN 1338..1525
FT /note="Roc"
FT /evidence="ECO:0000259|PROSITE:PS51424"
FT DOMAIN 1901..2162
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 795..814
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 880..980
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 880..903
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 916..948
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 949..977
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2543 AA; 288380 MW; 288D3622DA0CEBC0 CRC64;
MTRKLMGLRL LSCFISMSEV MLEGMQQADI VQFLIRIVND NTSECSIQIN GMKIISKLTE
SDTVKDNMNK ASKLQLIGVA AKDMATFIDN CTLHICTINA LATLLMNDFE LQEEFARLHL
DLFLEVLHDH QGDMTVVLTC FNLLNVLSSS SSVRIRLVER GVLHQIYPCM KIWHSELSVI
ERCFDLLALL CREDKVSKEM TEKGVIMNTL LPDMLSRCDS TEIQLHGLDI FMLTAEKLLQ
SREDSGLSED DPGYHWLKVI FTSMGRHMVH ADVQEAACRA LTKLMECKPD VYMKIGDSAE
ERQFPVHTMC LGALLMYDHH CGVFTAACNA IYYLTADNDG LCRCLMEKNS YIAILQGIKL
HMGEEKAVIA GCRAIRGLCI FHDEHKEKVM TYEEDVLQLL LRVMDTYHSQ PAVQSEAISI
IACLADLDIV RHQCFVVRIH DRIISAIDSF PGDQVLQETA IEALAVLGGA AKGPELLFSL
HAVDKIMMCM KRFLFNINIQ KKGLMALQVL VDPHHLQTSA KCRELTQIIK TAMGNFISNW
TVQKEAVVAM QILAERGLEG ASEAKHSQMS ETLIDHGCHE LLFQILEKFD DSEGLHDLAS
ECLYVIGIEQ DLKSRMLVSA CSKGFLSGAE CLIEIGADVN ADYGKGTPLY CAVKKNNPNM
VYLLLKQEVR DKQTSLKLSL RQQYHEITGM LLSHMGQDKE TGTLLWCGYG LQDLRPEWLL
PSLASDNRKH VLSMTSKRFV MQLRKSEQRR NKRVTHSYSD SNLQELYRHK CFRFQKIGQD
INRQVEQVLQ IMKEKSAQKS EKTRRPHTLP KTERPKLRVK GRVIAPKGSA TLLRTTETLN
FPHIRIAEDD VSLYNAMIEE ETPRFAYSED EWEDWKQNTL TGANIPFSPK DPRQPQDSRN
GDMPNGVIKT PKGKWLRKNS SGSFPESDAT TLEFTTQSQM NSSREYISDF EYGSRRESAS
EDTDFDTSQE DPKTAPKKKL QGNTIASLDI SSNEITSLNH LIEGSYRLTS QLTKLRELNL
SSNMLHTLPE AFFKLLPELT ELNLANNQLT CFPQDIVHLC NLVNLDVSCN KILALDFTEM
NVGLKLQKLN LMSNKLNDFP ANIHCAFPHL THLILASNVI EMLPDTPLQL EELRLLDLSH
NRISCIPDQF LIQCSKLEAL EAANNKLESL PSEWVAAELV KLGTLKLSNN LISEKEPFFV
PKFVLELPNL RILDLAGNRL EGLPPPNMWK TQILKELVVS FNKISKLSFE GARAWSKLEK
LHLSRNKISE LPKEIGHLSS LQSLDISHNK LLTTLPDDLG RCSCLWEMPL DGLNLDIDFK
AGARVRELRM YLHNRLKKAQ DYYRMKLMVV GYGGRGKTSL LHALKKKVRQ SGESPPVTVG
VIVDEWKFER QRNNKTITYT LSTWDFAGQE DFYSTHQCFL SNRTLYLGVY DISLGTDEVD
RLKPWLANIH ARAPGCPVII VGTHYDKMAP EDRAKIVSEF DIKLKDLMSK PGFPEIKCSA
MVDLTRESNE MDQLRKKILS VIDEYKVRGQ PVMGQKVPAS YVKLAEVLSE EARTMTVKDF
PVLRHNQLMR IIHNENLELD EDELKQAVSF LHESGVLLHY DETALQMRDF YFINPGWLCR
MMAQVVTVPE INPFIKRDGI MKRNSAYMLF AGKAIAGDKE NSFIFPPNMI PQYLRLLEKF
EIALPRNEEE LLIPCRLPSI RPQFQVPQLD RKDMVFRFYS MPFVPIGFWS RLLTRLIVFT
QSKFMENVLM LGSKPAEVHC WQEGLFVIWK QDTFFMLDGC RGDTEEVHVT VPSSPPGVRL
LGYVVDHIDS LVDEWYPGLT SIEPLLGREL LQKFVPCTTC TGKEPHLFLF SDLVSESERS
DTVVCPQHAG DVSLSQLAPD VMLTDVESHF RLEVDKFEFK NSPENLLGDG GFGSVYKAVY
RGQTVATKVF SAIGDTHPHK MLRQEAIIMR RLKHPSVVSL VAVARTPQHL MLMEFAPGRS
LAHVLNSQIS LSRTIQHKIL LQVAEGMHYL HQLMIVYRDM KPDNVLIFSL SPDAVVNAKI
SDYGISQFTA LSGLVAQEGT YSFRAPEVIR GETYSFQADV FSFGILMYLV LTGGQHPFEE
LEFKNERDKS FADNRPVPPL IQRGCPPWAD MQDLMNQCMH QVPDYRPLSE TLCQRLNTAE
LFCLREVLPV SVGTTVECMA YQEFDDGHNM RLWVASGDNE YMQLTWFSLL DYTDEELTNR
NRHKPNGMGT MFRDGRILCV LPVNKEYVLL GTQAGKIWVF NTRNDLLHSS PPLQDSVLCL
NIITRNDDSL VLAGLANGKI ALYPLSEILQ SPQMNPIEIR LGESYEPICC ILHNIVDRRL
VVSCGTRIIV MDSREGVAVE KMITTDDNSG PASKPILTMA CGRLLYLSRR NMTEVEAWDL
QRERRKMIMD LSDVFKLQKK ESRITSMALH ENKVLWVGTG GGHVAMIDTT AWTALTITDR
HTASIRSLLS VRLTGPGKYG SSSTSIILSG GLGFKTGPDV ELERENQYGC VAVWEADYPQ
VLKTLADNSN KRRQLLEKLQ SQN
//
