ID A0A2T7PMT3_POMCA Unreviewed; 1799 AA.
AC A0A2T7PMT3;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=C0Q70_06006 {ECO:0000313|EMBL:PVD34729.1};
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:PVD34729.1, ECO:0000313|Proteomes:UP000245119};
RN [1] {ECO:0000313|EMBL:PVD34729.1, ECO:0000313|Proteomes:UP000245119}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SZHN2017 {ECO:0000313|EMBL:PVD34729.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:PVD34729.1};
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 -!- 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:PVD34729.1}.
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DR EMBL; PZQS01000003; PVD34729.1; -; Genomic_DNA.
DR STRING; 400727.A0A2T7PMT3; -.
DR Proteomes; UP000245119; Miscellaneous, Linkage group lg3.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR CDD; cd09487; SAM_superfamily; 1.
DR Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR PANTHER; PTHR44329; SERINE/THREONINE-PROTEIN KINASE TNNI3K-RELATED; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF00536; SAM_1; 1.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00454; SAM; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 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:UP000245119}.
FT DOMAIN 342..403
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT DOMAIN 812..1140
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 130..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 420..450
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 577..624
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 796..834
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1207..1236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1499..1519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1627..1653
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1678..1698
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..188
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..217
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 588..609
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 610..624
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 796..815
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1499..1513
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1633..1650
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 953
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1799 AA; 199865 MW; C7E12692BA48BC20 CRC64;
METESSLLEP SVLSCENADE GAQVKSIGII PAKLKGKSLA KKYQKASKVV DRKSFTTWDT
RPGESKVEGR NIDYGRFMSV GDFLHNEGIN YDEEISFEET SMGRLTDSPQ ESEMTVVDEK
FGQDFSLMST PVGAYKKPKN RSEDVTDSLT LQMSPKQTDS ENWTNNSDRI VMQDVSSGTS
QSSPDNDTAY PREENHHHNS LIKKSIENDD NKDSEKEQQI WSIQTVKPQI ITSRDTAIPR
ALAEWIQKSV GLDSQDIEQK GVTEWDLVSD ENPATGVIRS SMIESSQNVV REQSLQTSCI
DKQVKRLPIF FDLDAEENIH KLENSIRASE VSIQALDCDS RVAAWLASLG LANVATFQQI
FAEHQVDFSD LYFLTVSMLQ EMGISRLGPI MKILRGIDKL KEEKENKLVQ LDKVENKMLR
RDRSKRAWPE TGDDRGQERG KKDSLPRRRD CVSKSFKRDH IGSQNKKSVE KALQLEKFDD
HKTLTADNAK TISSKKIYSL LCDGGSESYS AWRNPSIVTP SFDQNLTSKA LVEKTKSKTS
LKFSKPSSVI SSRTAVSCVQ NRDCKSSYKT DVKFKNETSD VKETSHQDTL QPKTSNGGLS
TACVLKRKSA KSQQESKGDI LDQHPDQLHN AMAARNKVTD HSKVADNDLE SSQSNQQLRD
PQAEQQISYR EETLNAVRDL QHKLQQLEHC ILHKKTTSTS SVAAGATLKK TDAAYNLDFR
KTDHTGDLYY SELQRALTNT KRNVTSVSKG NQCNGLNNTV TVGHANDIYS NGCSAWGTQN
HDSVTEDSIC EDVHGTVKHK QQKEDSEDLK KRSGVSKHQQ NSIGGLMNKS SRMEKEMHVP
EEVLVVAGMK CGRDENDGED SPDRCITEIV TFEKKQPMSK RQLRDEIRRE RDEHRKNVRH
LKLELSKLQH YDPMKNSEID RATILFRESD LIGEGSFSQV FKGQYQGAEV AVKRLRTPLC
LQDRTYFASE IARDVGSGMV YLHHHHPPVL HLNLKSMNVL LTTSHHAKIA DFGFSKLKLV
FVGFRVHDAD KKVKKATRNK NIKVSPAWMA PELLHGGEIT PKADVFSFGI ILWEMMSGKH
PYEGCTVFQI LELVRTNKRP DICETCPADL HELISVCWAQ NPAVRPNFKE VLQKIEDLSF
PAGWRELFKD ARIPNEALED VPSTSEIISL VTSTLESSAA KKTLHTMEMT SFNIKEKEPG
ITTFLTTDNA NDKAETEEPQ NDTTTHNQKP NLAQRQGVES IQIKLPMDMM KENKSCSFSK
CHTTKLTTSL DAIQSTDCLA TTMTTSTNFH HSSTAGCNAT LSDSLDVVSS LSTSSSLSSS
SSACSKDSLE ANTIPITTNR ESAQEDRPYY LGPSQDTRNV STCFDRLSIP ASNELSAPKK
HLVQSSIGSF SLNSDEASAK LVLSTQVYDP SVLTYRKKDA LNAPPCFSSP AISYISHLDA
SDSKNPTTLS GTIKAKQDGE VKGEEHIEKY VHAEKNSCAR LSAREARRLG VSRRSSDVWS
SSSCASTGEN RGLATASDDG LSDMQGLTAY VLNDSSLAGN KLMDSRLLLD LNNNSDTDTA
ESNVTAGGTH QELVSVNMNV VDQNSSQPDA CVVPVENDVR DICEGKVQGH KEEDGYKHIK
GVKNSGSLSS SCAIIPPPPP PPPPPPLAAS STPHFSTAQV CQNGFLADVQ DDSQQSVSKE
TLASSSKHSL KERYRGNPHI SVEASELMRQ KDQLRPTAQP HPSQLQEVST TAQEFTSLAD
IFKKIKVLNI KKYSLGGKSH SEFFLQAMVN RRFAMEGNSL ATSTNSQEFS DVNWSLQED
//
