ID   A0A154PT20_DUFNO        Unreviewed;      1347 AA.
AC   A0A154PT20;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Activated CDC42 kinase 1 {ECO:0000313|EMBL:KZC14408.1};
GN   ORFNames=WN55_07068 {ECO:0000313|EMBL:KZC14408.1};
OS   Dufourea novaeangliae (Sweat bee).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC   Anthophila; Halictidae; Rophitinae; Dufourea.
OX   NCBI_TaxID=178035 {ECO:0000313|EMBL:KZC14408.1, ECO:0000313|Proteomes:UP000076502};
RN   [1] {ECO:0000313|EMBL:KZC14408.1, ECO:0000313|Proteomes:UP000076502}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=0120121106 {ECO:0000313|EMBL:KZC14408.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:KZC14408.1};
RA   Pan H., Kapheim K.;
RT   "The genome of Dufourea novaeangliae.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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};
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DR   EMBL; KQ435074; KZC14408.1; -; Genomic_DNA.
DR   STRING; 178035.A0A154PT20; -.
DR   EnsemblMetazoa; XM_015581779.1; XP_015437265.1; LOC107192502.
DR   Proteomes; UP000076502; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016043; P:cellular component organization; IEA:UniProt.
DR   GO; GO:0002009; P:morphogenesis of an epithelium; IEA:UniProt.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd05040; PTKc_Ack_like; 1.
DR   CDD; cd09539; SAM_TNK-like; 1.
DR   Gene3D; 4.10.680.10; Cdc42-like binding domain; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR015116; Cdc42-bd-like.
DR   InterPro; IPR037085; Cdc42-bd-like_dom_sf.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR032065; RNF31-UBA.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR049587; TNK-like_SAM.
DR   InterPro; IPR008266; Tyr_kinase_AS.
DR   InterPro; IPR020635; Tyr_kinase_cat_dom.
DR   InterPro; IPR015940; UBA.
DR   PANTHER; PTHR24418:SF294; NON-SPECIFIC PROTEIN-TYROSINE KINASE; 1.
DR   PANTHER; PTHR24418; TYROSINE-PROTEIN KINASE; 1.
DR   Pfam; PF09027; GTPase_binding; 1.
DR   Pfam; PF16678; HOIP-UBA; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00326; SH3; 1.
DR   SMART; SM00219; TyrKc; 1.
DR   SMART; SM00165; UBA; 2.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF50044; SH3-domain; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR   PROSITE; PS50002; SH3; 1.
DR   PROSITE; PS50030; UBA; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KZC14408.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141}; Reference proteome {ECO:0000313|Proteomes:UP000076502};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          110..376
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   DOMAIN          372..432
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          1225..1267
FT                   /note="UBA"
FT                   /evidence="ECO:0000259|PROSITE:PS50030"
FT   REGION          635..654
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          725..753
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          788..874
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1025..1097
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        791..816
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        832..874
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1025..1060
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         142
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   1347 AA;  150215 MW;  02EE6D28470349D8 CRC64;
     MADDEGTEWL QELLHDVQLS QFFTRIRDDL QVTRLHHFDY VQPEDLEKIG LGKPGIRRLL
     DAVKKKRNTQ WKKNLITKIR PGSSTKTTKR TSQPVEGSSV LTCLIQDKDV TLSTKLGDGS
     FGVVRRGEWT SPSGRTLPVA VKVLKADALT QPSVIEDFVS EVQAMHTLDH HNLIRLYGVV
     LSQPMMMVTE LAPFGALLDY LRKQCGRISV LTLCNYALQV ATGMAYLEAK RFLHRDLACR
     NVLLSSVDKV KIGDFGLMRA LPQQEDCYVM TEHKKVPFPW CAPESLKARQ FSHASDVWMF
     GVTLWEMLTF GEEPWVGLNG SEILRKIDKD GERLHEPEGT PPVMYQLMLR CWAREPSERP
     TFTSLRTSLT GMVPTVMKAV NHFEEAEKMT IEQGDQIVIL DGRPENYWWK GQNQRTFQIG
     LFPRCLVDPM RRKQPEDISK PLENSFIHTG HGAPFGKSWG SPIYIDDVYL RNPMEPPDVV
     GVTTAPDSHL KKKFFSTTPR SRKQFNYTKF QNDIRASSVK STNATGSSSQ EGSLIDLSPE
     EIVNTSVAQS DTACRRVVNI LDEPIDDMER QQPVNWQEDD PRTYANFPEN VDPAYSDPFD
     TSSVFLKLPH SRYYSQVPPD MNSRYYKTQA YGNVQNQDAS SCPDSTNYFT PESGSDVSHY
     SINLSKENRN DSINLNVNVD AEDSNAYSQN HYSEIDKPSP PQTSWSTWPE DLQNEAQQTY
     VNVSSRNLPS SDVPPLPLMA PDESPPKPKS NHDLAQSLNE LTINTRTVSP KKLDPTFLAE
     LEKHLGEKEA SKNMNASQET ASSSESYSSV NKLQENTIPA LRPPPQSAKP KSPQIDHRTS
     NLPTKVQNSW PSKTTNIQQP RPQPEQRVSE TPTDQMVCQI WQQSQASQQN PYPNETSINR
     VHSNPPTNLN LLQIAPSNLG NQYNVTKTNI SHAQNSIAAS PASHFQNPIL PIASHGITQI
     QNDLQQAHSS NVPSKPASAV FSEQVYAELK QTVPNLEQLS QNEFNTLYNK TVQQNILRNY
     YAASTSSAPD SSNLSHSHYL EGAAGSSQQQ QQQPPRAGQT RSFPVQGHPC DFSPHLKQPP
     VYNPPPQPAW SPMKSIQNGL VPGQCPVMKT NLGNSGNLLQ LVHPNLPQEA AMVSQAPTLR
     SGVPPQMNET VVNTQLAPST SAYPSGVSPP LTGASQQLVM SLNDEFRANK VMKVQREASD
     ASQQEILTAL QATGWDTNQA AKQILKDRQA KIESLVRLGL AGRQECEGAL KQTEYDVDLA
     ASLLLDQEVD LPLDDGALLP DATSLFSTST LLTLNVLMLD VHLGCPEPGI ASLWNSCKAY
     NMWVQGHLEY LGYIDSKTSK ALRVSRL
//