ID A0A1A6GM31_NEOLE Unreviewed; 929 AA.
AC A0A1A6GM31;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=A6R68_04508 {ECO:0000313|EMBL:OBS66919.1};
OS Neotoma lepida (Desert woodrat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Neotominae; Neotoma.
OX NCBI_TaxID=56216 {ECO:0000313|EMBL:OBS66919.1, ECO:0000313|Proteomes:UP000092124};
RN [1] {ECO:0000313|EMBL:OBS66919.1, ECO:0000313|Proteomes:UP000092124}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=417 {ECO:0000313|EMBL:OBS66919.1};
RC TISSUE=Liver {ECO:0000313|EMBL:OBS66919.1};
RA Campbell M., Oakeson K.F., Yandell M., Halpert J.R., Dearing D.;
RT "The Draft Genome Sequence and Annotation of the Desert Woodrat Neotoma
RT lepida.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
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};
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:OBS66919.1}.
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DR EMBL; LZPO01087168; OBS66919.1; -; Genomic_DNA.
DR STRING; 56216.A0A1A6GM31; -.
DR Proteomes; UP000092124; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP 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; cd14033; STKc_WNK4; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR024678; Kinase_OSR1/WNK_CCT.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR13902; SERINE/THREONINE-PROTEIN KINASE WNK WITH NO LYSINE -RELATED; 1.
DR PANTHER; PTHR13902:SF114; SERINE_THREONINE-PROTEIN KINASE WNK4; 1.
DR Pfam; PF12202; OSR1_C; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000092124};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 159..428
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 1..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 530..567
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 583..660
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 740..808
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 894..929
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..48
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..66
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..87
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..148
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 755..769
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 896..917
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 929 AA; 102552 MW; 2C6B88BF49607480 CRC64;
MSQTEADLAL RPPPSLTSSG PIRLGPPPRR VRRFSGKAEP RPRSSRPSRR SSVDLGLLSS
WSQPASLFPE PPDPPDSAGP SRSPPPSSKE TPEGTWXGAA PVKAADSASP ELTGPSGGPG
SREPPRLLDA AARERRREQE EKEDTETQAV ATSPDGRYLK FDIEIGRGSF KTVYRGLDTD
TTVEVAWCEL QTRKLSRAER QRFSEEVEML KGLQHPNIVR FYDSWKSVLR GQVCIVLVTE
LMTSGTLKTY LRRFREMKPR VLQRWSRQIL RGLHFLHSRV PPILHRDLKC DNVFITGPSG
SVKIGDLGLA TLKRASFAKS VIGTPEFMAP EMYEEKYDEA VDVYAFGMCM LEMATSEYPY
SECQNAAQIY RKVTSATRGL TQLFXQGTKP NSFYKVKMPE VKEIIEGCIR TDKNERFTIQ
DLLAHAFFRE ERGVHVELAE EDDGEKPGLK LWLRMEDARR GGRPRDNQAI EFLFQLGRDA
AEEVAQEMVA LGLVCEADYQ PVARAVRERV AAIQRKREKL RKARELKVLP SESGAPPATV
SIAPGAPTAF PPEPEEPEAD QHQSFLFRHA SYSSTTSDCE TDGYLSSSGF LDASDPALQP
PGGVPSSPAE SHLCLPSGFA LSIPRSGPGS DFSPGDNYAS DAASGLSDMG EGGQMRKNPV
KNLRRRPRSR LRVSDQNDRV VECQLQTHNS KMVTFRFDLD GDSPEEIAAA MVYNEFILPS
ERDGFLSRIR EIIQRVETLL KRDPGPPEAA EDALSPQLTS ESSDTEDSAA GGAETREALA
ESDRAAEGLG VAVEEEGNDG VRIGGSSPLL SHPSPVWMNY SYSSLCLSSE ESESSGEDEE
FWAELQNLRQ KHLSEVEALQ TLQKKEIEDL YSRLGKQPPP GIVAPAAMLS CRQRRLSKGS
FPTSRRNSLQ RSDLPGPGSN SAVMPYPPP
//
