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Database: UniProt
Entry: A0A075AJ37_9TREM
LinkDB: A0A075AJ37_9TREM
Original site: A0A075AJ37_9TREM 
ID   A0A075AJ37_9TREM        Unreviewed;      1984 AA.
AC   A0A075AJ37;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
DE   Flags: Fragment;
GN   ORFNames=T265_12742 {ECO:0000313|EMBL:KER32704.1};
OS   Opisthorchis viverrini.
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC   Digenea; Opisthorchiida; Opisthorchiata; Opisthorchiidae; Opisthorchis.
OX   NCBI_TaxID=6198 {ECO:0000313|EMBL:KER32704.1, ECO:0000313|Proteomes:UP000054324};
RN   [1] {ECO:0000313|EMBL:KER32704.1, ECO:0000313|Proteomes:UP000054324}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Young N.D., Nagarajan N., Lin S.J., Korhonen P.K., Jex A.R., Hall R.S.,
RA   Safavi-Hemami H., Kaewkong W., Bertrand D., Gao S., Seet Q., Wongkham S.,
RA   Teh B.T., Wongkham C., Intapan P.M., Maleewong W., Yang X., Hu M., Wang Z.,
RA   Hofmann A., Sternberg P.W., Tan P., Wang J., Gasser R.B.;
RT   "Opisthorchis viverrini - life in the bile duct.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KL596631; KER32704.1; -; Genomic_DNA.
DR   RefSeq; XP_009163529.1; XM_009165265.1.
DR   STRING; 6198.A0A075AJ37; -.
DR   GeneID; 20326910; -.
DR   KEGG; ovi:T265_12742; -.
DR   CTD; 20326910; -.
DR   OrthoDB; 2999245at2759; -.
DR   Proteomes; UP000054324; Unassembled WGS sequence.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd20813; C1_ROCK; 1.
DR   CDD; cd01650; RT_nLTR_like; 1.
DR   Gene3D; 1.10.287.1490; -; 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   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR000961; AGC-kinase_C.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR000477; RT_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR22988:SF71; CITRON RHO-INTERACTING KINASE; 1.
DR   PANTHER; PTHR22988; MYOTONIC DYSTROPHY S/T KINASE-RELATED; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   Pfam; PF00078; RVT_1; 1.
DR   SMART; SM00133; S_TK_X; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000054324};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          810..1093
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          1094..1178
FT                   /note="AGC-kinase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51285"
FT   REGION          1784..1808
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1950..1984
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1196..1223
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1259..1439
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1500..1548
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1574..1619
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1950..1968
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1970..1984
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         839
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KER32704.1"
SQ   SEQUENCE   1984 AA;  222738 MW;  2CF64974186B6D18 CRC64;
     FFSFNAFQVA LKEYQAKHFV VFVRINSKKS CNSLLLNEKP STVAADIPAD EAIAVEFVVP
     TGPEHNPMRR AIRRQVKVSL RSDREVWWTQ KAEELKEAQN AGNARKLFQL IRATGTRKPP
     VRESLKHQNG TTISNKEERL DRWAEYFEQQ MSWPPAGTHL QPTGEVEPCT VNVEPPTASE
     FYDCIFSLKR HQAPGPDDLS PGLFRDGGEV PNQYLSDLFA CIWEKESVPD NWGESVIVPI
     FKKGARSECG NHRGISLTPV VTRLLASIVL RRLTVAREML TREQQAGFRP GRGCVDQIFT
     LRQVLEQRHT YKRPTILVFL DFRGAFDSVD RSVLLETLAH QGMPRKFVNI IRSLYSQTSG
     RRSVKEITKR FGAVGATRLP GWGPRDPHCA WLNTLQDMAA NRSSLGDGAD SDAAVFVAPL
     QSGENLCPPM TSSDNLPLNE LEKQLLDPSS ECYLENLLDL VTSLVADCNY PSASNSRTVQ
     AFLNRTDRVA RPASHSAAAS ARPSSVTTLN TSKSVFKPRK PVYLGTFNVR TLKQADQHVA
     PARTLDSVCI DDASTVIELT APSLSSRFRL GTSWNSEAAA AGYAGGGRKT RKTRLAIEKL
     VEPEVKRNYQ SQLLEYLSDG TVSDINGHWE KTSKALLKAG ASACGTTQPT SSKDWISDRT
     VSLLKTRRQV PPGRHHNSTR RIIRRQKTIL VNSDLQITQL SSNLSALSAA LENVWRSDSV
     RARGRNPQMY SKTTSSQLSI IAISTDDNVT NLSSYPGRRW RTISGQMTSA ISHCMKTACG
     QRTAEAIVHH CPYKKASEVI EARRTKYADF EILKVIGQGG FGRVELCRHR RTRRVYAMKM
     MSKQHLLDHS QSGYWEERDL MVRASSEWLV ACHHAFLDKE NVYLCMEYMP GGDLYYWLEK
     YDTFNESQVR FYLAESILAL EVLHSLRFIH RDLKPDNMLL DARGHLKLAD FGSCVRVGDD
     GYHYCTSPIG TPDYISPEML NCQSKPGKVG PECDWWSLGI IAFEMLFGEP AFYGQSLVET
     YSRILAHEKS FKIPEDGDPP SPELENLIRA LLRSAATRLG SLAVVYENDQ SMLNDSNRAI
     AASTAQVKSH PFFQNVAWHQ LRSQDPPIQP VVNSETDTSN INFDENEANS FSIGVSKLPS
     TSGAFAPKKP PAPNYFTGNH LSFAGYTFNR DHIYLRGGLR GQEQVDTTPE ANRLSMSDTN
     RRLQALESEV AELRATIQTL EKQAAVDQVA LKDSQRRLGE STSELDATKT HTLELEKTLS
     DLRSRCATIQ AERDRLTKDI ASTKTQLQHT TEICEAERRK VSALEEEKTR LTTEIEQLHV
     SLQQTQVRLQ EQLKQTEQVQ GSDDPSRQRE MISALELQVA NLQAENREAR QKATVLMTEA
     SNLNRNHTKQ VAELTDQLQE AQRFCNLYQS QVTELSESCS AIESREKTLR EELNALRIQL
     DTTLASKRTL TENLFSTEST LASTLVELRS AQDDLKAARE HTATEVERLQ ALANLRLAEL
     NDVSGQLDEM RDRCTKAEES SFDLSEQVSR LQKERELQQR NMKAIVDKLL HEVEGRRPPG
     GSKKHAKDHD HSACQQLAKN YKNLQSTSEK AKADLQRTID QQKKDLAERS EMLTRLTEES
     LFKDQEISRL NALIHQLYSR LDEAPQTHST PMKGMSAAGD IGDQVSGPGS RTMIDHDSQL
     DLDELYSKSL EQVVDLDSKG RGRKKLIWSP TYAVLKPFVL AFYVSRMEKE TGVGPVEEIP
     LCRIIHVRKA TSADLIHAQS TDIVRTLQFF FQKEENPATS NTLLDSAESE TNTSNANLRA
     AGGSGSNHHA GSDNLIRWLE HTFQPIRFRI GTVLCEVCYR PCSELRNPPP ALECTKCRMR
     IHLDHVDQHQ KFASCHSAAE MRYIRLPSVA EQEKWISHMN LLVRSLRELQ QNPEKLIESG
     LSAKAALAGG VTQLGTRLAI EPLYRSIRTG SAGASQQRSE LKSPTQSSMK VKVKRRESPP
     KASF
//
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