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Database: UniProt
Entry: A0A093Q7U7_9PASS
LinkDB: A0A093Q7U7_9PASS
Original site: A0A093Q7U7_9PASS 
ID   A0A093Q7U7_9PASS        Unreviewed;       850 AA.
AC   A0A093Q7U7;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   RecName: Full=non-specific serine/threonine protein kinase {ECO:0000256|ARBA:ARBA00012513};
DE            EC=2.7.11.1 {ECO:0000256|ARBA:ARBA00012513};
DE   Flags: Fragment;
GN   ORFNames=N305_07145 {ECO:0000313|EMBL:KFW80257.1};
OS   Manacus vitellinus (golden-collared manakin).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Pipridae; Manacus.
OX   NCBI_TaxID=328815 {ECO:0000313|EMBL:KFW80257.1, ECO:0000313|Proteomes:UP000053258};
RN   [1] {ECO:0000313|EMBL:KFW80257.1, ECO:0000313|Proteomes:UP000053258}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N305 {ECO:0000313|EMBL:KFW80257.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (JUN-2014) 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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
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DR   EMBL; KL670767; KFW80257.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A093Q7U7; -.
DR   Proteomes; UP000053258; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0048583; P:regulation of response to stimulus; IEA:UniProt.
DR   CDD; cd14194; STKc_DAPK1; 1.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 2.
DR   Gene3D; 1.20.5.460; Single helix bin; 1.
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; IPR020676; DAPK1_cat.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR020859; ROC_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR24342:SF17; DEATH-ASSOCIATED PROTEIN KINASE 1; 1.
DR   PANTHER; PTHR24342; SERINE/THREONINE-PROTEIN KINASE 17; 1.
DR   Pfam; PF00023; Ank; 1.
DR   Pfam; PF12796; Ank_2; 2.
DR   Pfam; PF13637; Ank_4; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   PRINTS; PR01415; ANKYRIN.
DR   SMART; SM00248; ANK; 9.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 7.
DR   PROSITE; PS50088; ANK_REPEAT; 7.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   PROSITE; PS51424; ROC; 1.
PE   4: Predicted;
KW   ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KFW80257.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053258};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          1..255
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   REPEAT          358..390
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          424..456
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          457..489
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          490..522
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          523..555
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          556..588
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          589..621
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   DOMAIN          661..850
FT                   /note="Roc"
FT                   /evidence="ECO:0000259|PROSITE:PS51424"
FT   REGION          703..722
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        705..722
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFW80257.1"
FT   NON_TER         850
FT                   /evidence="ECO:0000313|EMBL:KFW80257.1"
SQ   SEQUENCE   850 AA;  95246 MW;  4F02A9A09B18144D CRC64;
     SGQFAVVKKC REKSTGQQFA AKFIKKRRTK SSRRGVSRED IEREVGILKE IRHPNVITLH
     DVYENKTDVI LILELVAGGE LFDFLAEKES LTEEEATEFL KQILNGVQYL HSLQIAHFDL
     KPENIMLLDR NVPKPRIKII DFGLAHKIDF GNEFKNIFGT PEFVAPEIVN YEPLGLEADM
     WSIGVITYIL LSGASPFLGE TKQETLANVS AVNYEFEEEF FSNTSALAKD FIRRLLVKDP
     KKRMTIQDSL LHPWIKPKDT QQALSRKASA VNMEKFKKFA ARRKWKQSVR LISLCQRLSR
     SFLSRSNMSV ARSDDTLDEE DSFVMKAIIH AINDDNVPGL QHLLGSLTNY DVNQPNKHGT
     PPLLIAAGCG NIQMLQLLLK RGSRIDVQDK AGSNAIYWAS RHGHVETLKF LNDNECPLDV
     KDKSGETALH VAARYGHVDV VQFLCRIGSN PNFQDKEEET PLHCAAWHGY YSVAKALCEA
     GCNVNIKNKE GETALLTASA RGYHDIVECL AEHRADLHAT DKDGHIALHL AVRRCQTEVV
     KTLISQGCFV DFQDRHGNTP LHVACKDGNV PIVMALCEAN CSLDVTNKYG RTPLHLSASN
     GILDVVRFLC VTGANVEALT SDGKTAEDLA RAEQHEHVAN LLARLKKDTH RGLFIQQLRH
     TQNPQPRIKL KLFGHSGAGK TTLVESLKCG LIRSFFRRRR PRLSSTNSSR FPPSPLSSKP
     SVSVSITNLY PGCENVSVRS RSMMFEPGLT KGVLGTLVSP AHHSHFSADD QSTKAIDIQN
     AYLHGVGDFS IWEFSGNPVY FCCYDYFAAN DHTAIHIVLF SLEEPYEIQL NQVTFWLNFL
     KSLVPVEEPI
//
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