ID A0A3L8STQ0_CHLGU Unreviewed; 1058 AA.
AC A0A3L8STQ0;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Protein kinase domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=DV515_00003113 {ECO:0000313|EMBL:RLW08224.1};
OS Chloebia gouldiae (Gouldian finch) (Erythrura gouldiae).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Passeridae;
OC Chloebia.
OX NCBI_TaxID=44316 {ECO:0000313|EMBL:RLW08224.1, ECO:0000313|Proteomes:UP000276834};
RN [1] {ECO:0000313|EMBL:RLW08224.1, ECO:0000313|Proteomes:UP000276834}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Red01 {ECO:0000313|EMBL:RLW08224.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:RLW08224.1};
RX PubMed=30282656;
RA Toomey M.B., Marques C.I., Andrade P., Araujo P.M., Sabatino S.,
RA Gazda M.A., Afonso S., Lopes R.J., Corbo J.C., Carneiro M.;
RT "A non-coding region near Follistatin controls head colour polymorphism in
RT the Gouldian finch.";
RL Proc. R. Soc. B 285:0-0(2018).
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:RLW08224.1}.
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DR EMBL; QUSF01000006; RLW08224.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3L8STQ0; -.
DR STRING; 44316.ENSEGOP00005002017; -.
DR Proteomes; UP000276834; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd21777; MobB_LATS2; 1.
DR CDD; cd05626; STKc_LATS2; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR017892; Pkinase_C.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR009060; UBA-like_sf.
DR PANTHER; PTHR24356; SERINE/THREONINE-PROTEIN KINASE; 1.
DR PANTHER; PTHR24356:SF149; SERINE_THREONINE-PROTEIN KINASE LATS2; 1.
DR Pfam; PF00069; Pkinase; 2.
DR Pfam; PF00433; Pkinase_C; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF46934; UBA-like; 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000276834};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 638..943
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 944..1022
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT REGION 332..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 508..562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 965..998
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..352
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..384
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 518..541
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 982..998
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 667
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1058 AA; 119138 MW; BAC17ACF406D384F CRC64;
MLLDNPVVQQ ERKPLPMLVE CSQAGGLQSS AWVLSQRDSI LVYFVQEMAV RALKQTGSRS
IEAALEYISK MSYLDPRNEQ IVRVIKQTSP GKGIVPNNVT RRPSFEGSNE SFPSYHQMGN
AAYEGTGFGA EGANMLTEVP RPYMDYLIST SQSSAMTAPV QRPSGVGTHS TPTSHQQKAY
PANMESSVIN YPVANHSSQA LQLQASHGCN SQHYSRQHMM VQGEPMGYGV QRSPSFQNKM
QQEGAYANLQ NKGAVVQNNT GHAFQQAPAS LYISHSHHKQ TSPSSHQMHV ISRGPAFAND
FSDSPPQNLL TPSRNSLNMD LYDMNNPQVQ QWQAAAPSRR DSVQNPGIET SPRQHVSFRP
DATVPSRTNS FNNHQQQPQV TVSMRQVPPG KPDPSITSPN TITAVTSAHI LQPVKSMRVM
RPEPQTAVGP SHPAWLPAQA PAVDGLEMME QHVPPPGAAN AYQLDVDYGN QELRCPPPPY
PKHLLLPGTS EQFDINCLCK GMEQTLRVVP SSTSNKAEES SERNDKSSKN TKAEKPSKDK
KQIQTSPVPV RKNGKDEEKR ESRIKSYSPF AFKFYMEQHV ENVIKTYQQK INRRLQLEQE
MAKAGLCEAE QEQMRKILYQ KESNYNRLKR AKMDKSMFVK IKTLGIGAFG EVCLACKVDT
HALYAMKTLR KKDVLNRNQV AHVKAERDIL AEADNEWVVK LYYSFQDKDN LYFVMDYIPG
GDMMSLLIRM EVFPERLARF YIAELTLAIE SVHKMGFIHR DIKPDNILID LDGHIKLTDF
GLCTGFRWTH NSKYYQKGSH IRQDSMEPSD LWDDVSNCRC GDRLKTLEQR AKKQHQRCLA
HSLVGTPNYI APEVLLRKGY TQLCDWWSVG VILFEMLVGQ PPFLAPTPTE TQLKVINWES
TLHIPSQIKL SPEATDLITK LCCAAEDRLG RNGADDIKAH SFFHSMDFSA DIRRQPAPYV
PKISHPMDTS NFDPVEEESP WSDASGDSTR TWDPLASSNS KHTEHAFYEF TFRRFFDDNG
YPFRYPKPSG MEVCQSEKSD VEDKGVVDQT GACQPVYV
//
