ID A0A2A3E6B9_APICC Unreviewed; 1607 AA.
AC A0A2A3E6B9;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=APICC_08469 {ECO:0000313|EMBL:PBC26822.1};
OS Apis cerana cerana (Oriental honeybee).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC Anthophila; Apidae; Apis.
OX NCBI_TaxID=94128 {ECO:0000313|EMBL:PBC26822.1, ECO:0000313|Proteomes:UP000242457};
RN [1] {ECO:0000313|EMBL:PBC26822.1, ECO:0000313|Proteomes:UP000242457}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Pupae without intestine {ECO:0000313|EMBL:PBC26822.1};
RA Diao Q., Sun L., Zheng H., Zheng H., Xu S., Wang S., Zeng Z., Hu F., Su S.,
RA Wu J.;
RT "Genomic and transcriptomic analysis on Apis cerana provide comprehensive
RT insights into honey bee biology.";
RL Submitted (JUL-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 -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000256|ARBA:ARBA00004245}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000256|PROSITE-ProRule:PRU00782}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the TRAFAC class
CC myosin-kinesin ATPase superfamily. Myosin family.
CC {ECO:0000256|ARBA:ARBA00006998}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00782}.
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DR EMBL; KZ288367; PBC26822.1; -; Genomic_DNA.
DR STRING; 94128.A0A2A3E6B9; -.
DR Proteomes; UP000242457; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003774; F:cytoskeletal motor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.5.4820; -; 1.
DR Gene3D; 1.20.58.530; -; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR PANTHER; PTHR46256; AGAP011099-PA; 1.
DR PANTHER; PTHR46256:SF2; NEITHER INACTIVATION NOR AFTERPOTENTIAL PROTEIN C; 1.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00242; MYSc; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50096; IQ; 1.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 3: Inferred from homology;
KW Actin-binding {ECO:0000256|PROSITE-ProRule:PRU00782};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00782}; Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Motor protein {ECO:0000256|ARBA:ARBA00023175, ECO:0000256|PROSITE-
KW ProRule:PRU00782};
KW Myosin {ECO:0000256|ARBA:ARBA00023123, ECO:0000256|PROSITE-
KW ProRule:PRU00782};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00782}; Reference proteome {ECO:0000313|Proteomes:UP000242457};
KW Sensory transduction {ECO:0000256|ARBA:ARBA00022606};
KW Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Vision {ECO:0000256|ARBA:ARBA00023305}.
FT DOMAIN 1..295
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 346..1066
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1271..1395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1456..1497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1565..1597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..31
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1271..1296
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1322..1352
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1370..1395
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1460..1491
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 439..446
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1607 AA; 184028 MW; D03CDACF2C8455D9 CRC64;
MSDYGYGDRG MREQRRRRQN REEDFNDRGR SAVQRLDSIQ DPGKRYLLRD CIGSGVCGDV
YEAIDRQAGI EYRILRDYTS HPNLPDFYGI YRRRSGKKTE YDQIWFVMEL CDGGTVMDLV
HGLLAMNKKM REEHIGFILR EVIQAMIYLN ENNVMHRDIR GSNILLTKEG EIKLVDFGLS
RTCQSEIGKR YTCVGSPSWM APEVAMSKGN NSEGYGNRAD VWAIGITAIE LADGRPPFQD
MHPTRALFQI IRNPPPTLYR PSNWSQNFND FISECLEKNP ENRPFMGEII EHPFLADLPD
NDFLLTKEIK ILMMDACEKG KQERKLEILV RKGFLKTHQT DPLEPMFMED LAALETLTED
AILDELHERL RQGYYHSFIG DILLILNPNE QQDIYGSDFH TKYQLKSRSD NAPHIYSVAD
SAYQDVMHNN EAQHILLAGE SNSGKTTNMM YLIEHLMYLG KSLQDIGGRF IRAIKLIQAF
SNAATPLNPN STRCVFQVQT TYGSSGKASG GIFWLYQLEK WRVSTRDRNQ SNFHVLYYFY
DGMDSINKLK QYHLPPGRRM RYLRISEKGT ERKRSFKVRN DPRGNVTKFE DFKESLKILE
MEEHCEMIWN VLAAILILGE IRFIEDSNGE ADMDNNDAAN KVAELLKLDE KKFSWALLNY
CMIVNGNAVR RKHTYEEAKD ARDVLANTIY QRLVDWIVNT INVKFTLTRS LFGDKYAINV
MDLFGFECFA VNRLEQLVVN TMNEQMQCYY NQRVFAWEMQ EQEEEAIPMQ RLQFYDNKNA
IDNLMGKDRG LFNVIDEASK NMLDYTHVIS KIQNRAGNVY VKVVSSHEFT VAHYTGKLIY
DASEIAEKNR DFLPPEMIET LRQSTIETVK EMFTNKLTKS GNLTIIDEHS KVEEKKTNKS
KWGTLMQEAS KLRRFNTTSR GQFSQIRKMR TCAATFKSTS LEILKNLSIG GGSGGMHFIR
CIRSDLEGTP RGFYREVVRQ QIRALAVLDT AKARQYGYPH RITFPEFLRR YQFLAFDFDE
TVEINKDNCR LLLIRLKLEG WIIGKTKVFL KYYNEEYLSR LYETQVKKII KVQCMMRAFL
ARKNMASKIT SNIKKETGSE ESVYKGKECS GADGRRGSCS CSESVQGTFS ESGNEASFNE
GEDEYANDRY DEVLQQQMEI EEHISSSSTV PCSPVHLFNQ AIVVSLVTTN KGISIDKVNT
NVSPSTYLGQ TRPPEVHKLP FNFYSELPFT YPNKGIKNVG YASSLASDEE HEAWDAPLQR
HTVPWATRNS RTKDVEVQTT NSPHRVHSNT EGQDLIDTPF SRDPNVSIRC PPDALSQGRM
DDSGYQYASR SITPVPPANA HNPRSNYDNI GSIRSRKHAP PPPVSFNQPQ PPLIRSTDNY
SSNIQSKSNI DSATHNWEYN ENKTNKSSGN PNRINPIQEL QMIGRRDNYD GNEDSDEPPF
NFQAMLRKTP YRASLKRPSV FESHSHSPSP LPSTGYRGNR ESESNVVYKS GGSRRDSLEW
SPNEMVRMSE KYAKEGAWGG EDRSGIGGNA PSESVTAEIA PGIVIEGYVA ELYLHCYTTN
NNNNNNNNNY NYNNDNGNSN GNGNDNDNNN DNDNNNKKLL KILSQCT
//
