ID A0A0Q3TGQ3_AMAAE Unreviewed; 791 AA.
AC A0A0Q3TGQ3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Receptor-interacting serine/threonine-protein kinase 4 {ECO:0000313|EMBL:KQK79742.1};
GN ORFNames=AAES_103181 {ECO:0000313|EMBL:KQK79742.1};
OS Amazona aestiva (Blue-fronted Amazon parrot).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Psittaciformes; Psittacidae; Amazona.
OX NCBI_TaxID=12930 {ECO:0000313|EMBL:KQK79742.1, ECO:0000313|Proteomes:UP000051836};
RN [1] {ECO:0000313|EMBL:KQK79742.1, ECO:0000313|Proteomes:UP000051836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FVVF132 {ECO:0000313|EMBL:KQK79742.1};
RA Gilbert D.G.;
RL Submitted (OCT-2015) 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:KQK79742.1}.
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DR EMBL; LMAW01002568; KQK79742.1; -; Genomic_DNA.
DR STRING; 12930.A0A0Q3TGQ3; -.
DR Proteomes; UP000051836; 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 CDD; cd14025; STKc_RIP4_like; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 4.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
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; PTHR24198; ANKYRIN REPEAT AND PROTEIN KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR24198:SF65; RECEPTOR-INTERACTING SERINE_THREONINE-PROTEIN KINASE 4; 1.
DR Pfam; PF00023; Ank; 1.
DR Pfam; PF12796; Ank_2; 3.
DR Pfam; PF13857; Ank_5; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 10.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50297; ANK_REP_REGION; 9.
DR PROSITE; PS50088; ANK_REPEAT; 10.
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 ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW ProRule:PRU00023};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Kinase {ECO:0000313|EMBL:KQK79742.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Receptor {ECO:0000313|EMBL:KQK79742.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051836};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000313|EMBL:KQK79742.1}.
FT DOMAIN 22..286
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REPEAT 438..470
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 471..503
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 504..536
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 537..569
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 570..603
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 604..636
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 637..669
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 670..697
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 703..725
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 735..767
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REGION 281..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 344..363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..302
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..318
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 51
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 791 AA; 87737 MW; E4146EC0149C4C9B CRC64;
MARENVSPWA MGLLKTFEES EFGSWEKIGS GGFGQVYKVR HLHWKTWLAI KCSPSLHVDE
KERMELLEEA RKMEMAKFRY ILPVYGICKE PVGLVMEYME TGSLEKLLAS EPLPWELRFR
IIHETAVGMN FLHCMSPPLL HLDLKPANIL LDAHYHVKIS DFGLAKCNGL SHSHDISMDG
LCGTIAYLPP ERIKEKNRCF DTKHDVYSFS IVVWGVLTQK KPFAEENNIL HIMVKVVKGH
RPELPAVSKS RPHSCNNLIK LMQKCWQDDP GERPTFKEIT SETEALCEKP EDETKEMITQ
DLDTKNSQEQ QPEGISALSK TKQEPDLPLV KDYSLSELLS QLDSGISQTM EGPEDLSRSC
SESKLASSDK RLSGVSSVDS AFSSRGSLSL SFERESSGND IGTTDIQKRK LTEAILSGDT
SKLMKILQPQ DVDIVLDGNS SLLHLAVEAG QEECVKWLLL YNANPNLTNK KGSTPLHIAI
EKKFKSIVEL IMARKINVNA KDEDQWTALH FAAQNGDDFS TKMLLDKNAS LNEVDFEGRA
PIHIACQYGQ ENIVRILLRR GVNVNIKGKD DWVPLHYAAW QGHLPIVKLL AKQRGANVNV
QTVDGRTSLH LAAQRGHYRV ARLLIDLESD VNIQNGLLQT ALHIAAETGH TSTSRLLLKH
GADIEAATAE GYTALHLASR SGHLATTKLL VDEGASVLAG GPLNRTALHL AAEXGHSEVV
EELVSSENIN VSDSEGLTAL HLAARGGHTK TVEVLLKHGA YTDMQRPTCQ TLLQLAQQSS
NRSVTVLLSE T
//
