ID A0A1V4J3I1_PATFA Unreviewed; 1249 AA.
AC A0A1V4J3I1;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
GN Name=MAP4K4 {ECO:0000313|EMBL:OPJ66766.1};
GN ORFNames=AV530_016757 {ECO:0000313|EMBL:OPJ66766.1};
OS Patagioenas fasciata monilis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Patagioenas.
OX NCBI_TaxID=372326 {ECO:0000313|EMBL:OPJ66766.1, ECO:0000313|Proteomes:UP000190648};
RN [1] {ECO:0000313|EMBL:OPJ66766.1, ECO:0000313|Proteomes:UP000190648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BTP2013 {ECO:0000313|EMBL:OPJ66766.1};
RC TISSUE=Blood {ECO:0000313|EMBL:OPJ66766.1};
RA Soares A.E., Novak B.J., Rice E.S., O'Connell B., Chang D., Weber S.,
RA Shapiro B.;
RT "Band-tailed pigeon sequencing and assembly.";
RL Submitted (FEB-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 -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. STE20 subfamily.
CC {ECO:0000256|ARBA:ARBA00008874}.
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:OPJ66766.1}.
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DR EMBL; LSYS01009367; OPJ66766.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V4J3I1; -.
DR Proteomes; UP000190648; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR001180; CNH_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR47096:SF1; CNH DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR47096; MISSHAPEN LIKE KINASE 1; 1.
DR Pfam; PF00780; CNH; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00036; CNH; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 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.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:OPJ66766.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000190648};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:OPJ66766.1}.
FT DOMAIN 12..276
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 936..1223
FT /note="CNH"
FT /evidence="ECO:0000259|PROSITE:PS50219"
FT REGION 293..334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 459..818
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 898..925
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..307
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..324
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 459..482
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 483..510
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..545
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 559..579
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 580..594
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 597..614
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 638..672
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 687..728
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 729..748
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 781..800
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 908..924
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 41
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1249 AA; 142688 MW; 4CFCED9307AD20F5 CRC64;
MMPAHEDPAG IFELVEVVGN GTYGQVYKGR HVKTGQLAAI KVMDVTEDEE EEIKLEINML
KKYSHHRNIA TYYGAFIKKS PPGHDDQLWL VMEFCGAGSI TDLVKNTKGN TLKEDWIAYI
SREILRGLAH LHAHHVIHRD IKGQNVLLTE NAEVKLVDFG VSAQLDRTVG RRNTFIGTPY
WMAPEVIACD ENPDATYDYR SDLWSCGITA IEMAEGAPPL CDMHPMRALF LIPRNPPPRL
KSKKWSKKFF SFIEGCLVKN YMQRPSTEQL LKHPFIRDQP NERQVRIQLK DHIDRTRKKR
GEKDETEYEY SGSEEEEEEV PEQEGEPSSI VNVPGESTLR RDFLRLQQEN KERSEAFRRQ
QLLQEQQLRE QEEYKRQLLA ERQKRIEQQK EQRRRLEEEY IRRQLEEEQR HLEILQQQLL
QEQAMLLEYR WREMEEHRQA ERLQRQLQQE QAYLLSLQHD HRRQQQQQQQ QQQQQQQERN
KQSYHTPEPK PHYEPAERAR EVEERFRKTN QGSPEAQSKQ MGKVLEPPVP SRSESFSNGN
SEPAQPALQR PMEPQVQWSH LASLKNNVSP VSRSHSFSDP SPKFAHHHLR SQDPYPPSRS
EVLNQSSDSR SEVPDPTQKA WARSDSDEVP PRVPVRTTSR SPVLSRRDSP LQGSGQQNNQ
AGQRNSTSNI EPRLLWERVE KLVPRPGSGS SSGSSNSGSQ PGSHPGSQSG SGERFRMRSS
SKSEGSPSQR HESAPKKPEE KKEVFRPIKP ADLTALAKEL RAVEDVRPPH KVTDYSSSSE
ESGTTDEEDD DMEQEGADES TSGPDDVRAV STLNLSNGET ESVKTMIVHD DVESEPALTP
SKEGTLIVRQ TQSASNTLQK HKSSSSFTPF IDPRLLQISP SSGTTVTSVG FSSEAMRSEA
IRQDPTRKGS VVNVNPTNTR PQSDTPEIRK YKKRFNSEIL CAALWGVNLL VGTESGLMLL
DRSGQGKVYP LINRRRFQQM DVLEGLNVLV TISGKKNKLR VYYLSWLRNK ILHNDPEVEK
KQGWTTVGDL EGCVHYKVVK YERIKFLVIA LKSSVEVYAW APKPYHKFMA FKSFGELVHK
PLLVDLTVEE GQRLKVIYGS CAGFHAVDVD SGSVYDIYLP THIQSSIQPH AIIILPNTDG
MELLVCYEDE GVYVNTYGRI TKDVVLQWGE MPTSVAYIRS NQIMGWGEKA IEIRSVETGH
LDGVFMHKRA QRLKFLCERN DKVFFASVRS GGSSQVYFMT LGRTSLLSW
//
