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Database: UniProt
Entry: A0A226MLU1_CALSU
LinkDB: A0A226MLU1_CALSU
Original site: A0A226MLU1_CALSU 
ID   A0A226MLU1_CALSU        Unreviewed;      1618 AA.
AC   A0A226MLU1;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
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=ASZ78_011704 {ECO:0000313|EMBL:OXB56120.1};
OS   Callipepla squamata (Scaled quail).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Odontophoridae;
OC   Callipepla.
OX   NCBI_TaxID=9009 {ECO:0000313|EMBL:OXB56120.1, ECO:0000313|Proteomes:UP000198323};
RN   [1] {ECO:0000313|EMBL:OXB56120.1, ECO:0000313|Proteomes:UP000198323}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Texas {ECO:0000313|EMBL:OXB56120.1,
RC   ECO:0000313|Proteomes:UP000198323};
RC   TISSUE=Leg muscle {ECO:0000313|EMBL:OXB56120.1};
RA   Oldeschulte D.L., Halley Y.A., Bhattarai E.K., Brashear W.A., Hill J.,
RA   Metz R.P., Johnson C.D., Rollins D., Peterson M.J., Bickhart D.M.,
RA   Decker J.E., Seabury C.M.;
RT   "Disparate Historic Effective Population Sizes Predicted by Modern Levels
RT   of Genome Diversity for the Scaled Quail (Callipepla squamata) and the
RT   Northern Bobwhite (Colinus virginianus): Inferences from First and Second
RT   Generation Draft Genome Assemblies for Sympatric New World Quail.";
RL   Submitted (JUL-2016) 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:OXB56120.1}.
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DR   EMBL; MCFN01000671; OXB56120.1; -; Genomic_DNA.
DR   STRING; 9009.A0A226MLU1; -.
DR   Proteomes; UP000198323; Unassembled WGS sequence.
DR   GO; GO:0005694; C:chromosome; IEA:UniProt.
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; cd01093; CRIB_PAK_like; 1.
DR   CDD; cd06659; STKc_PAK6; 1.
DR   Gene3D; 1.25.40.430; -; 1.
DR   Gene3D; 3.90.810.10; CRIB domain; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2.
DR   InterPro; IPR000095; CRIB_dom.
DR   InterPro; IPR036936; CRIB_dom_sf.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR013212; Mad3/Bub1_I.
DR   InterPro; IPR033923; PAK_BD.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR035066; STKc_PAK6.
DR   PANTHER; PTHR48015; SERINE/THREONINE-PROTEIN KINASE TAO; 1.
DR   PANTHER; PTHR48015:SF19; SERINE_THREONINE-PROTEIN KINASE PAK 6; 1.
DR   Pfam; PF08311; Mad3_BUB1_I; 1.
DR   Pfam; PF00786; PBD; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00777; Mad3_BUB1_I; 1.
DR   SMART; SM00285; PBD; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS51489; BUB1_N; 1.
DR   PROSITE; PS50108; CRIB; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198323}.
FT   DOMAIN          81..240
FT                   /note="BUB1 N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51489"
FT   DOMAIN          1045..1058
FT                   /note="CRIB"
FT                   /evidence="ECO:0000259|PROSITE:PS50108"
FT   DOMAIN          1355..1595
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REGION          1..40
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          242..277
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          291..349
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          453..519
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          581..611
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1260..1330
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        248..265
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        495..512
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        581..596
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1261..1276
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1287..1324
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         1384
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1618 AA;  181713 MW;  F4E411D671D09A58 CRC64;
     MRERLATVGG LDFPAAAGPP QSRERGAQSS KMAQDCEDEW ELSKENVQPL RQGRVMAALQ
     EALAQQDTST HTAAQLRKQE FESEIRFYSG DDPLDVWDRY IKWTEQTFPQ GGKESNLSAV
     LERAVKALNK QQRYYQDPRY LSLWLKFGNC CNEPLDLYSY LHSQEIGTTL AQLYVTWAEE
     LEARGSFKKA DIIFQEGLNR KAEPLDKLQS HHRQFQTRVS RQTLLGLEEA ADEKDTALLG
     AEEPQRSTLA DLKGRGKKKV RAPVSRVGDA LKAPNQNRSF QALTSQQLSN NPGFAVFDEN
     SASASGPEIP VLTSQHWTEP PAPRAKENEL SAGPWNSGRR PRSSANSGVE VPCPMPSFTP
     YVEESAQQQV IARKPEKEED PLQRVQNHHQ DTQEKKEVVM YCKDKVYAGV EEFSFEEIRA
     EVCRKKAKKK AEEEMQTIAQ KKEEIQKKIE ELEKKLKEKG NDKQQQLHEQ PTEVTKPSAP
     LGVQEPLFSS GTELGVKQPR LQSESCLSEY DQPREPSCSE EVIKSLGACL DMEKGSVFSD
     SEDELEKQRE KANLVKRDAV FLPPPDPAPF FSILDESSAS ANQNISRSTE NAQKTTRRPL
     AVRKPSDSAV AKENLPPEYE VHGIEPLTED AIVTGSYKHK SLCANPEDTC DFVRAAHLAS
     TPFHGVAAQR IPAPAYSHVV LKEDCPEPKS APLNEKTPVC EGTYSEALCV NKLSPIMEAS
     LEDTRLSGSS VSSGSSLSSV TQISTIKYLH EKLELAQSLP AEPISDAGGT SEIITGDDVT
     QFLWTAEQRK KLLDPMPESL TASPHFHLEA GSLPVIEFEK DVELGNETYC IKWEYWTDEE
     YKMLFAIPAN FPQLDAKGFA IKVYSQPVPW DFYITLQLHE RLNADFDQSF SDNCSCFLYR
     DGCAVLHRDI NRFTLEADLV GIADIVHLML FGDHIQVHQE NSVWKISQNA SRSVGCDFWG
     KFFLQVLNAD DWRFLFSQKQ NEGGSYLGNV ASESLIRTVG GEGGFVKVNG WANTRECTTV
     LENTQLSEID KGIMFRKKKK KRPEISAPQN FEHRVHTSFD PKEGKFVGLP PQWQNILDTL
     RRPKPVVDPS RITRMQLQPM KTVVRGSTVE VEGYISGILS DIQKLSAISS NTLRGRSPTS
     RRRAQSLGLL GEDRPPDMYL QSPEADWADK YGNYLNCNGG TKVTRRQTMW PDYKPRLDGE
     THPNGMVTKA QSLGPSEFQD ADSSCLQRAS CLQHMPALLG ESDKMGKRSL EDCWPQPCLV
     RQANSRPSGE GSPSSKSREN SLKRRLLRSV FPSSSSSNKS GPSLHIKTSS SNLHLPQDSS
     GKGQPASEDP VVVTHEQFKA ALRMVVDQGD PRTLLENYIK IGEGSTGIVC IAREKHSGRQ
     VAVKMMDLRK QQRRELLFNE VVIMRDYQHV NVVEMYKSYL VGEELWVLME FLQGGALTDI
     VSQIRLNEEQ IATVCESVLQ ALSYLHSQGV IHRDIKSDSI LLTLDGRISK DVPKRKSLVG
     TPYWMAPEVI ARVPYTTEVD IWSLGIMVIE MVDGEPPYFS DSPVQAMKRL RDSPPPKLKN
     FHRTSPVLRD FLERMLTREP LERATAQELL DHPFLLQTGL PECLVPLIQQ YRKRTSTC
//
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