ID   A0A158QWM1_NIPBR        Unreviewed;       882 AA.
AC   A0A158QWM1;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 34.
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=NBR_LOCUS468 {ECO:0000313|EMBL:VDL63121.1};
OS   Nippostrongylus brasiliensis (Rat hookworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Strongyloidea; Heligmosomidae; Nippostrongylus.
OX   NCBI_TaxID=27835 {ECO:0000313|Proteomes:UP000038043, ECO:0000313|WBParaSite:NBR_0000046701-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:NBR_0000046701-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (APR-2016) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDL63121.1, ECO:0000313|Proteomes:UP000271162}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR   EMBL; UYSL01000202; VDL63121.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A158QWM1; -.
DR   STRING; 27835.A0A158QWM1; -.
DR   WBParaSite; NBR_0000046701-mRNA-1; NBR_0000046701-mRNA-1; NBR_0000046701.
DR   OMA; HHACTHV; -.
DR   Proteomes; UP000038043; Unplaced.
DR   Proteomes; UP000271162; 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:0004672; F:protein kinase activity; IEA:InterPro.
DR   CDD; cd08215; STKc_Nek; 1.
DR   Gene3D; 2.130.10.30; Regulator of chromosome condensation 1/beta-lactamase-inhibitor protein II; 2.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR009091; RCC1/BLIP-II.
DR   InterPro; IPR000408; Reg_chr_condens.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR44535; PROTEIN CBG16200; 1.
DR   PANTHER; PTHR44535:SF4; SERINE_THREONINE-PROTEIN KINASE NEK8; 1.
DR   Pfam; PF00069; Pkinase; 2.
DR   Pfam; PF00415; RCC1; 2.
DR   PRINTS; PR00633; RCCNDNSATION.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF50985; RCC1/BLIP-II; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS50012; RCC1_3; 3.
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   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000271162};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022777}.
FT   DOMAIN          21..322
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REPEAT          379..430
FT                   /note="RCC1"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT   REPEAT          431..480
FT                   /note="RCC1"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT   REPEAT          481..532
FT                   /note="RCC1"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00235"
FT   REGION          663..694
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          816..857
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        663..693
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         50
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   882 AA;  97085 MW;  C695008E04BD38C4 CRC64;
     MRARSEEPAA GERIKSASSR YERIRTVGKG AFGSAVLYRR KEDASLVIIK EINMYDLDSS
     QRQLALNEVH LLSRIEHPNI ISYYDSFEED GILMIEMEFA DGGTLAQYLM KCQNFIPEAT
     VTDLMIQMLS AVVYLHECSV LHRDLKTANV FLMKDGFVKI GDFGISKVMG TETLAQGAKT
     VVGTPYYISP EMASERSVTF TLSLLLFPSL FLSSPQNGVS LTGCKLPEIE RSGRVVCSGQ
     PYNEKSDMWA LGCILYEMTC LQKAFEGENL PALVNKIMTC TYAPVRGPYS AEIKLLIREL
     LQHDPDARPR ACQALQMLRP RLKSSVVIAR SALHATSSTL YSLDPGSITL RPVEDLPKRL
     TIKQVATSGS HTMVLSYNNE VFAWGSNEHG QLGLGDTKER LNPEKVEALR GKDVCSIGVG
     QGFSVVCCDR GTIMACGDAR LVGLGGKEDV TRPTLIDDLL RVHVSELVCG PEHCLVFTEE
     GEIYAWGNGT DGRLGNGKSE WASAPVLISG LDGVRVSSCR AGTNASALLT DEGKLLAMGS
     NQFNKLNLAQ RQGFFTRERN DNFGDILLPT MLKNFQMRCE QYVFAVLLES GEVLFMGRNT
     YCELGFGHTQ SVAFCGLRPV KTLLTKACSK LGCGDGFSLV GTAENELYFW GLKSSSTTDV
     GLQKERESKC DESTRSNGSR WGAKRKPRDA ESSADDVVQL PSLILRLDSG DSEKEIRLSS
     ITLCGTCTYV VVDTYDTEAA KTVPRSIGAR GKSAPSLHEE HDDDVNTWLK NELEEAEVIP
     IGSAQQKKER RSQSCVSQTD ASFLKASSDS ALMREIETLK QQIKDQSSTF EGHQAQMSKL
     QEKLTELQSR QAFLRKSEPP PAYVPKLPPV FSEAKSRACT LL
//