ID A0A218UGC9_9PASE Unreviewed; 1125 AA.
AC A0A218UGC9;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=LATS2 {ECO:0000313|EMBL:OWK52641.1};
GN ORFNames=RLOC_00000651 {ECO:0000313|EMBL:OWK52641.1};
OS Lonchura striata domestica (Bengalese finch).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Estrildidae;
OC Estrildinae; Lonchura.
OX NCBI_TaxID=299123 {ECO:0000313|EMBL:OWK52641.1, ECO:0000313|Proteomes:UP000197619};
RN [1] {ECO:0000313|EMBL:OWK52641.1, ECO:0000313|Proteomes:UP000197619}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=White83orange57 {ECO:0000313|EMBL:OWK52641.1};
RA Colquitt B.M., Brainard M.S.;
RT "Genome of assembly of the Bengalese finch, Lonchura striata domestica.";
RL Submitted (MAY-2017) 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:OWK52641.1}.
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DR EMBL; MUZQ01000333; OWK52641.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A218UGC9; -.
DR STRING; 299123.ENSLSDP00000011046; -.
DR OrthoDB; 5348633at2759; -.
DR Proteomes; UP000197619; 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 CDD; cd14398; UBA_LATS2; 1.
DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 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; IPR015940; UBA.
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.
DR PROSITE; PS50030; UBA; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:OWK52641.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000197619};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 97..138
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT DOMAIN 705..1010
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 1011..1089
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51285"
FT REGION 23..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 399..467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 573..629
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1030..1065
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..40
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 399..419
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 428..451
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 585..608
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1040..1065
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 734
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1125 AA; 126468 MW; 08B168861DE90412 CRC64;
MRPKTFPATT YSGNSRQRLQ EIREGLKQPS KSSGQGLPIG AGSETSLDPK ILIGKDAARQ
QQMRQTPKFG PYQKALREIR YSLLPFANES STTAAVEVNR QMLQELVNAG CDQEMAVRAL
KQTGSRSIEA ALEYISKMSY LDPRNEQIVR VIKQTSPGKG IVPNNVTRRP SFEGSNESFP
SYHQIGNAAY EGTGFGAEGA NMLTEVPRPY MDYLISTSQS SAMTAPVQRP AGVGTHSTPT
SLQQKAYPAN MESSVINYPV ANHSSQALQL QVSHGCNSQH YSRQHMMVQG EPMGYGVQRS
PSFQNKMQQE GGYANLQNKG AVVQNNTGHA FQQAPASLYI SHSHHKQTSP SSHQMHVISR
GPAFANDFSD SPPQNLLTPS RNSLNMDLYD MNNPQVQQWQ AAAPSRRDSV QNPGIETSPR
QHVSFRPDAT VPSRTNSFNN HQQQPQVTVS MRQVPPGKPD PSITSPNTIT AVTSAHILQP
VKSMRVMRPE PQTAVGPSHP AWLPAQAPAV DGLEIMEQHV PPPGAANAYQ LDVDYGNQEL
RCPPPPYPKH LLLPGTSEQF DINSLCKGME QTLRVVPSST SNKAEESSER NDKSSKSTKA
EKPSKDKKQI QTSPVPVRKN GKDEEKRESR IKSYSPFAFK FYMEQHVENV IKTYQQKMNR
RLQLEQEMAK AGLCEAEQEQ MRKILYQKES NYNRLKRAKM DKSMFVKIKT LGIGAFGEVC
LACKVDTHAL YAMKTLRKKD VLNRNQVAHV KAERDILAEA DNEWVVKLYY SFQDKDNLYF
VMDYIPGGDM MSLLIRMEVF PERLARFYIA ELTLAIESVH KMGFIHRDIK PDNILIDLDG
HIKLTDFGLC TGFRWTHNSK YYQKGSHMRQ DSMEPSDLWD DVSNCRCGDR LKTLEQRAKK
QHQRCLAHSL VGTPNYIAPE VLLRKGYTQL CDWWSVGVIL FEMLVGQPPF LAPTPTETQL
KVINWESTLH IPSQIKLSPE ATDLITKLCC AAEDRLGRNG ADDIKAHSFF HSMDFSTDIR
RQRAPYVPKI SHPMDTSNFD PVEEESSWSD ASGDSTRTWD PLASSNSKHT EHAFYEFTFR
RFFDDNGYPF RYPKPSGMEV CQSEKSDVED KGVVDQTGAC QPVYV
//
