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Database: UniProt
Entry: A0A1B0C5B6_9MUSC
LinkDB: A0A1B0C5B6_9MUSC
Original site: A0A1B0C5B6_9MUSC 
ID   A0A1B0C5B6_9MUSC        Unreviewed;      1901 AA.
AC   A0A1B0C5B6;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   24-JAN-2024, entry version 40.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
OS   Glossina palpalis gambiensis.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Hippoboscoidea;
OC   Glossinidae; Glossina.
OX   NCBI_TaxID=67801 {ECO:0000313|EnsemblMetazoa:GPPI049561-PA, ECO:0000313|Proteomes:UP000092460};
RN   [1] {ECO:0000313|Proteomes:UP000092460}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IAEA {ECO:0000313|Proteomes:UP000092460};
RA   Aksoy S., Warren W., Wilson R.K.;
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:GPPI049561-PA}
RP   IDENTIFICATION.
RC   STRAIN=IAEA {ECO:0000313|EnsemblMetazoa:GPPI049561-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) to UniProtKB.
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};
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DR   EMBL; JXJN01025926; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   STRING; 67801.A0A1B0C5B6; -.
DR   EnsemblMetazoa; GPPI049561-RA; GPPI049561-PA; GPPI049561.
DR   VEuPathDB; VectorBase:GPPI049561; -.
DR   Proteomes; UP000092460; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion 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   CDD; cd00029; C1; 1.
DR   Gene3D; 3.30.60.20; -; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR000961; AGC-kinase_C.
DR   InterPro; IPR046349; C1-like_sf.
DR   InterPro; IPR001180; CNH_dom.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR002219; PE/DAG-bd.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
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; PF00780; CNH; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00109; C1; 1.
DR   SMART; SM00036; CNH; 1.
DR   SMART; SM00133; S_TK_X; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR   PROSITE; PS50219; CNH; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141};
KW   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          124..386
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          387..467
FT                   /note="AGC-kinase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51285"
FT   DOMAIN          1412..1464
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50081"
FT   DOMAIN          1542..1832
FT                   /note="CNH"
FT                   /evidence="ECO:0000259|PROSITE:PS50219"
FT   REGION          1365..1396
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          475..540
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          577..679
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          719..1018
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1061..1228
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          1309..1336
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1365..1381
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         153
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1901 AA;  219202 MW;  0B2411DC7D83C30C CRC64;
     MEKIVNVSII KNTISKMAQP IDAITVRATR LNNVLLGSGR SYGISTAFSD SMTRESLLDA
     FCVLYNECDK EALRNRDKNI SEFVNKCKFL LYIDSWIWIF KSQSFPDRNV IEEARRLRVN
     VTDFNVRNLI GEGSFGNVHL VVEHQTGDVY AMKKIKKTIV TAVQVKEERD IMSRRCSEWI
     TNLQYAFQDK DYLYLVMEYL PGGDLFSLMS RHGSFDEDLT RFYLAEMTVA IHALHEMGYV
     HRDIKPENIL IDRLGHIKLA DFGNAATLNR DGHVFSLSPV GTPDYIAPEL LQSSRYKNMH
     DVSCDYWSMG IIGYELICEI TPFHDDDIHQ TYSKILSYCE ESQLKKLVAF PSELKLTEHF
     KNLIESLVTS PSNRLGYENL RKHAFFNNIE WNNLRSMVPP IIPSLKSRDD ISNFEDNARK
     KTRACAVISK NSKKSLTTAM MSNDFCGKDL PFVGYSFVHM EWQKIEQGAI DDARYIKLDN
     KLKDLQQKYK ERIDDISKLK QELLRAELTI KQSGTQSRIL QDAKDEMNNM KDIIKKKNAE
     LANCHTEIKT LRSSLRVEKE VGEKKDASVT EILRSARQKY EDALNKSDRR YERKIAEKKA
     EISAILSKLN ERDAELSAKA EEYLHLQEKM DNYKELLSQQ KQQAQKDREE FEEHKTHLIE
     TYEQKLLQMR EKIRFVRNSK SRLSMELRDV RTELNDNLNI RRSSEEAKLM TEKSNEDILQ
     RLNREIEANN ELHKTVENLE QEMQRLQRDL QVAECSKNLT ESALATPFET APGSLTDISK
     IEDQLKADLE TAKENENVQR MRADKLQETV EKLQEMLEGC NEQCTSPVKP LAAPRQKKST
     TNAGDLLEKK NEKLEDQLAT LREEMIVERR AARSANLSLW RMEKLVEKLT DEKNTLERRM
     QLTEGRIKKA QHDREDALRL CKANEEAKVE REQRIEELKQ EISALKADIK RGNAMREKCE
     QERMKCKMEV IEHIANLKKL EENLAEHRYR TQPLSDKCKE LEFENKRLIG QINDEKDRLL
     VIENQNSSLQ IKLQNQIKNY GRLKYACMIT DKQLTEIEAM LEKEQASNKA NQQKLKQLLS
     EKDQRLEIEA QLKKQLFDEK EQRQAAELNG ENLNTKLEEQ HQNIEHLQKE LEATNQRLML
     KTAELFHTQE RVEILQSEKQ NVLTRIENHA REIEIYTHEI EHLKEEKTGV ITELFHAKEA
     ANRLNMDLKD ATTQILDLQN ELKDVRGILE EKENFYLQRE IKCETTLVQH KKLIDYLQLK
     VEDLSQRKKK TFADKLFGSN TNANRSCPCS ASSRKENLCP NVIENSIVYR TLHEELRREK
     LLNKTLKEQL DRSKLNKNWL RSPLKKVEKD EQSIDDAQGL EINKTIKENA TKSPVKKGKV
     QQEQSDNQDL KKSMEKLQQI SGNSSAKYLQ LHHRFEQTRQ ESNIDASQCA VCHKALLVTS
     PYLECKVCKR VVHRKCRDDV NVPCDSIENI LNDNAIKSDC IETMALEPSA PTRTDLDTDS
     LGKYSYEAKL DNLDEANAAA LQNSYNGSLI FTIPIKNEQG TSLEVACAYE MEENRILLLG
     CNTGLYAYHV KQQHLVHIAG IDAVSCIAIS APLAKAILVS SHGESLYQCD LRHLQSRSQA
     NACLKPALEA SILDLSFDNR GTAEKWQLIQ VSEETEQPLD TVAIAATSSR IVILKYDVKQ
     QKFKPVQALD TATSVSSILF TRHTAIVSSD KFFEIDLSTY GAEEFVDIAD QSLSHSSTCQ
     PVVALRISKQ EFLLCFMECG VFVDEYGCRS RPYDINWGYT PTGFLYRAPF LYVAHFQSVQ
     IMRVHRSYSK EMSDKYIDAD TNDAVHELKK IHLSFYMPTL LCNSGKHNIY MLAKQKEIGA
     QEIYHLDALQ AFKLQYNGSQ DTVSSITTSI TAESLTTIST D
//
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