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Database: UniProt
Entry: A0A261BI83_9PELO
LinkDB: A0A261BI83_9PELO
Original site: A0A261BI83_9PELO 
ID   A0A261BI83_9PELO        Unreviewed;      1026 AA.
AC   A0A261BI83;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=Protein kinase domain-containing protein {ECO:0000259|PROSITE:PS50011};
DE   Flags: Fragment;
GN   ORFNames=FL83_16029 {ECO:0000313|EMBL:OZG09376.1};
OS   Caenorhabditis latens.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=1503980 {ECO:0000313|EMBL:OZG09376.1, ECO:0000313|Proteomes:UP000216463};
RN   [1] {ECO:0000313|EMBL:OZG09376.1, ECO:0000313|Proteomes:UP000216463}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PX534 {ECO:0000313|EMBL:OZG09376.1,
RC   ECO:0000313|Proteomes:UP000216463};
RA   Fierst J.L.;
RT   "Caenorhabditis latens genome sequence.";
RL   Submitted (JUL-2017) 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:OZG09376.1}.
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DR   EMBL; NIPN01000142; OZG09376.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A261BI83; -.
DR   STRING; 1503980.A0A261BI83; -.
DR   Proteomes; UP000216463; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR   CDD; cd14066; STKc_IRAK; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR032319; CLP1_P.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR27006:SF554; LRR RECEPTOR-LIKE SERINE/THREONINE-PROTEIN KINASE ISOFORM 1; 1.
DR   PANTHER; PTHR27006; PROMASTIGOTE SURFACE ANTIGEN PROTEIN PSA; 1.
DR   Pfam; PF16575; CLP1_P; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 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}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000216463};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        983..1007
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          87..404
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          23..64
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          920..951
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        32..64
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         116
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:OZG09376.1"
SQ   SEQUENCE   1026 AA;  114110 MW;  745C808FBBE69426 CRC64;
     MRLMRSEVDE KYHCLETKIL NPARRFRPNI PPPGSQSASR SKKTETNEPS PAPTQASSSS
     TNDPLRVAIE GTLPVTYLEL LEATNGFAAS NVIGKGGYGT VYKGEIKATG GMVAVKRILA
     GNDSSAHGSK VEKERLRQSL TELRTLARFR HDNILPIYAY SLEGPEPCLV YQFMANGSLE
     DRILCRKGTT PLTWIQRKEI SIGAARGILF LHSFAKTPII HGDVKTANIL LDKHMEPKLG
     DFGLSRDGQV EAEATEKCPL IASHIKGTLA YLAPEFITSK ILTTKLDVYS YGIVLLEIAS
     GQRAYSDSRE TRGLVEYCQF NKELAARQNT RLREILIDKR APPLANEAEE LFLETLIEMS
     EVLRYECRDG NLEILIVKPG ERLSIYGSCS LLCLAGNASV NDFVLPTVSC EPSNFIKISA
     PQRMDVPVIL QVSNDCSAYK HARLKFRLKE VTPNNYETIM EGIGTSQPAV FVFNKILDIA
     EGTISGAISN FLIHCSIQKQ VILPPHFFIC RDDFCIFPQA QESQLRMHIN RLSDGQKTSI
     LPIGHKGAGK SHLMRSLVNR CLSNGYEHVY VLDCDIGQSE FTPSGCLSLT KVTSPILDKP
     YGHQKKTFEN SYFYGDNTVT KLPMYLDIFE RLFNKFKLIS EPGSVCIINS MGWVVDVGAE
     ILDSITKVAE PDLFIEIFRD QTEFRYNFPQ EVDHNNVIEI FANNSVGVIG LPNQKRLPAA
     LIRDLTVAGY FSSLLPRPTI ASFSAVTPYK LKFQNLHICV PVDLLVEDSH IFSSINTQLV
     ALCVKNIDLK TRKLCGKVDM PLISVLDENS PSLQCFGFGI IRGVNVEERS VYVVTPVDLL
     KLEEPPLLVR GMRIQTPSMF FTADKIIMTL PEEEIEKIKI ANRAKGHPSP PVDLPAYPPR
     VPRALPNQMM GPLEVQNPIP PPPHNNRGEA RGVQGDNHRG AAAVQGEPQG RAPLPPQNQF
     SLGFLLFLSA SSRLVSLLRS CVYIFYITFS TVSAVFFASS FTTAIYTNLF AFEEAIRPPQ
     SYRNRQ
//
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