ID A0A0L7RB11_9HYME Unreviewed; 1602 AA.
AC A0A0L7RB11;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
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=WH47_03265 {ECO:0000313|EMBL:KOC68107.1};
OS Habropoda laboriosa.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC Anthophila; Apidae; Habropoda.
OX NCBI_TaxID=597456 {ECO:0000313|EMBL:KOC68107.1, ECO:0000313|Proteomes:UP000053825};
RN [1] {ECO:0000313|EMBL:KOC68107.1, ECO:0000313|Proteomes:UP000053825}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0110345459 {ECO:0000313|EMBL:KOC68107.1};
RA Pan H., Kapheim K.;
RT "The genome of Habropoda laboriosa.";
RL Submitted (JUL-2015) 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; KQ414617; KOC68107.1; -; Genomic_DNA.
DR STRING; 597456.A0A0L7RB11; -.
DR Proteomes; UP000053825; 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; 1.20.5.190; -; 1.
DR Gene3D; 1.20.58.530; -; 1.
DR Gene3D; 6.20.240.20; -; 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; PF00612; IQ; 2.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00015; IQ; 2.
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:UP000053825};
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 47..317
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 368..1088
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1266..1463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1500..1584
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1296..1319
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1348..1388
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1390..1404
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1412..1442
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1449..1463
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1510..1541
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 461..468
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1602 AA; 182912 MW; E9D79A857C954FE6 CRC64;
MNDYGYGRRS GKEHRRGGRR GDEDDTEDRR TSTLQRLDSV QDPGKRYLLR ECIGSGVCGD
VYEAIDQQAG NKRVAVKVQK LTAESQSLII EEYRVLRDFA SHPNLPDFYG IYRRRSGKKT
EYDQIWFVME LCEGGPAMDL ARGLIAMDKK LREEHIGFIL REVIKAVVYL HENNVMHRDI
RGNNILLTKE GEVKLVDFGL SRTIQGEMGK RYTCIGSPSW MAPEVAMSKG ANSDSGYGNR
ADVWAIGITA IELADGKPPF QDMHPTRALF QIVRNPPPNL YRPSNWSQNF NDFITECLEK
NPENRPFMAE IAEHPFLAEL PENDYLLTQE IKVLMMDACA KGKLDRRAEV IVRKGFLKTH
QTDPLEPMFM EDLAALETLT EDAVLDELHE RLRQGYYHSF VGDILLILNP NEQQDIYGSD
YHTKYQFKSR SDNAPHIYSV ADSAYQDVMH NEEMQHILLA GESNSGKTTS MMHIVRHLMY
LGKSLQDTGA RLMRAIKVIH AFSNAATPLN PNSTRCVLEI QTTYGSSGKA SGGIFWLYQL
EKWRVSTRDR NQSNFHVFYY FYDGLDSISK LKQYLLPPGR RMRYLRISEK GTERKRSFKV
RNDPRGNVVK FDELKENLKI LEMEEYCETI WKLLAAVLTL GEIRFVEGNN GEADMDNNDA
ATKVAQLLNL DDKKFMWALL NYCVISKGTV VRRKHSCEEA KEARDVLANT IYQRLVDWIV
NNINQKFTVT RALFGDKYAI NVMDLFGFEC FSINRLEQLV VNTMNEQMQC YYNQRVFAWE
MQEQEEEDIP VQRLHFYDNK DAIDQLMSRD RGLFSIIDNA SKNMLDYPYI MKKIQERSDN
VYIKPVSSHE FTVAHYTGKL VYDASEIAEK NRDFVPPEMT ETLRQSSIET VKDMFTNKLT
KSGNLTIIVD HPKIMEKKTN KGKWGALMQE TSKPRKYNTA SRGQYSQTRK MRTCAATFKS
TSLEILKNLS AGGGSGGIHF VRCIRSDLEG APRGFYRDVV RQQIRALAIL DSAKARQRGY
PCRISFQEFL RRYQFLAFDF DENVEITKDN CRLLLIRLKM EGWMIGKTKV FLKYYNEEYL
SRLYETQVKK IIKVQCMMRA FLARKNMVSK IVSSTKKEVV KKASIKKKES VDMSEDQAAI
MIQKAYRGHV VRKETAPLMG KGKMDPETID MMKFYSSKWR SKSMFQVLLR YRAARYQDLV
QFSQQVHLFN QAIVSSLATT NDQISIDKVN PNVTVSAYLG QMKPPQVHKL PFNFYHELPF
PSAKGGMRNL GSASSSASDD EHEAWDAPLR RQTVPWAIRN SRTRDVEVQT TNSPHRVAHS
GTEGESLIDT PFSRDPNISV RCPPDETSRS RMGNSGYQQS SSNRSPAPSA NAHNPRSNYD
STGSIRSTKH APPPPIPLNQ SQPPPPRSSD NHSSDVRSKS NIDSGSHDWE FEDNRINRNT
GNANRHDEIT PPLPPPPPSL PLNPIQELQM IGRRNNNYGG NEDNDDPPFN FQAMLRKTSH
HRASMKRTPV YDSYSHSPSP LPGTGYRGNR ESDSNVVYRS GGSRRDSPEW SPNEMVRMSE
KYGKEGAWGE SSGGAGRSNK AAESVTAEIA PGIVIEGYVA EL
//
