ID A0A0J7P137_LASNI Unreviewed; 1721 AA.
AC A0A0J7P137;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE SubName: Full=Membrane-associated guanylate ww and pdz domain-containing protein 2 {ECO:0000313|EMBL:KMQ98365.1};
GN ORFNames=RF55_1272 {ECO:0000313|EMBL:KMQ98365.1};
OS Lasius niger (Black garden ant).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Formicinae; Lasius; Lasius.
OX NCBI_TaxID=67767 {ECO:0000313|EMBL:KMQ98365.1, ECO:0000313|Proteomes:UP000036403};
RN [1] {ECO:0000313|EMBL:KMQ98365.1, ECO:0000313|Proteomes:UP000036403}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Whole {ECO:0000313|EMBL:KMQ98365.1};
RA Konorov E.A., Nikitin M.A., Kirill M.V., Chang P.;
RT "Lasius niger genome sequencing.";
RL Submitted (APR-2015) 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:KMQ98365.1}.
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DR EMBL; LBMM01000435; KMQ98365.1; -; Genomic_DNA.
DR STRING; 67767.A0A0J7P137; -.
DR PaxDb; 67767-A0A0J7P137; -.
DR OrthoDB; 2902917at2759; -.
DR Proteomes; UP000036403; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR CDD; cd00992; PDZ_signaling; 5.
DR CDD; cd00201; WW; 1.
DR Gene3D; 2.20.70.10; -; 1.
DR Gene3D; 2.30.42.10; -; 5.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2.
DR InterPro; IPR001180; CNH_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR PANTHER; PTHR10316:SF40; LD27118P; 1.
DR PANTHER; PTHR10316; MEMBRANE ASSOCIATED GUANYLATE KINASE-RELATED; 1.
DR Pfam; PF00780; CNH; 1.
DR Pfam; PF00595; PDZ; 4.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00036; CNH; 1.
DR SMART; SM00228; PDZ; 5.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00456; WW; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 5.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF51045; WW domain; 1.
DR PROSITE; PS50219; CNH; 1.
DR PROSITE; PS50106; PDZ; 5.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS01159; WW_DOMAIN_1; 1.
DR PROSITE; PS50020; WW_DOMAIN_2; 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:UP000036403}.
FT DOMAIN 1..227
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 483..807
FT /note="CNH"
FT /evidence="ECO:0000259|PROSITE:PS50219"
FT DOMAIN 833..866
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 896..979
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 1093..1156
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 1403..1486
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 1513..1595
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 1621..1704
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 268..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 391..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1205..1239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..306
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 391..421
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1217..1239
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 51
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1721 AA; 192925 MW; 43011D9DA5158654 CRC64;
MATVNANALS SDISRRNPQD EYELIQRIGS GTYGDVYKAK RLSMNDLAAI KVIKLEPVTG
PLSEIQIAYM CRETLTGLAY LHSMGKMHRD IKGANILLTE AGDVKLADFG VSAQITATIN
KRKSFIGTPY WMAPEVAAVE RKGGYNQLCD IWACGITAIE LAELQPPMFD LHPMRALFLM
SKSGFKPPTL KDRDKWSPTF HNFVKVALTK NPKKRPTAEK LLQHAFFQGE MHKRLALELL
QKVSNPSHMF ADLEADEDGA VPNVPQRIAS RHTARPRPKS PISQLDSDDQ INIDGGTLHR
DSISPSVDSN PAWDIMDIMN NVKAVHNCDV HPDCGIGSAF EDEQEKATLP LGESSNDCEV
HCPYYNVSGS QASPRRHSSV DELYGLVNNS QSLTTVNGQR QRSLSDSGPR DESAQSNGDS
NEIAADRDRE SMSPDLLSDT PPVPPRRRDR KRHTPPRPIS NGLPPTPKVH MGACFSKVFN
GCPLRIHCTA SWIHPDTRDQ HLLIAAEEGI YNLNLNELHE TAIDQLYPRR TIWMYVIKDV
LMSLSVMCIV GKTPQLYRHD LLAILSKQTH RFSLHMNKIP ERLVPRKFAL TTKVPDTKGC
TKCCVGRNPY NGYKYLCGAM PAGIFLMQWY DPLNKFMLLK HFDCVLPSPL NVFKMVITPE
MEYPMVCVSV KQPYQQNKLK LDLINMNSGA SWFHSDELED MDGSATVIPR RENLNVINVT
QFEKDAILVC YDNVVKMVTL QGKPRVSKKQ LSELQFNFQI ESIICLPDSV LAFHKHGMQG
RSFKNGEVTQ EISDPSRTYR LLGSDNHNTG TSHWLDPRLS KFQKRSLEEC LDDELPYGWE
KIDDTLYGTY FIDHVNRRTQ YENPVLQAKR AQQNLHERKS PNFTRNPDKL KGQRIRTALI
KSSRGLGFTI VGGDDTVEEF LQIKSVVPNG PAWLDGKLQT GDVLVYVNDT CVLGFTHNEM
VNVFKSIGSG ETVSLEVCRG YPLPFDPNDP NTEVVTTIAV NAPEDPAMYM DLNSSLQDNG
RFNFLDSTFL PVHSLQNGEN LTTTSVNSMP DLCISDKINT IKRPSSTDIL LSESSDLNDC
KNSPVSSKPE FLSIAIVKGA MGFGFTIADS AHGQKVKKIL DRQRCKNLME GDILVNINEI
NVRNMCHSEV VQVLKDCPRN EEALIHVQRT TTKSTKEKKE KNMQDFFRSK TPTADIYSTQ
SKTIIPSRPK TPLIDTRNHP KSPTGASRSN WNEVQGENEL NPLDNHYKYA DYSHGMYYSD
PYKANITANL SDNFAVMNLD DDSIRNVSKR DWVANDKLNI NNDVYSIDIS HHDNMLKQNG
YLHSDYYKDV YPVQSHSQYT EDYSMYSIGQ EQNVDTGEIW DKRKETTSFE HEQPHSSSIS
RYPQYTSELV CPMVPDIEWI ETLVTLVRQD TGFGFRIVGG TEEGSQQVSV GHIVPGGAAD
LDSRLNTGDL IMSVDGESVM NSSHHHVVQL MIAAAQNGRV TLGIRRRINT QEHLQENLQS
SYSRQMNLQY PYDVTVTRME NEGFGFVIIS SVNKAGSTIG RIIEGSPAER CGRLNVGDHI
LAVNHIDITN VCHKDIVNLI KDSGYSVTLT IGYPLDDCCS NTSLSQKDEL TGDGDGGQYH
AVELTRGTRG FGFSIRGGRE FQNMPLFVLQ IAENGPASID NRLRVGDQII EINGINTKNM
THTEAIEIIR NGGPSVRLLV RRGCQMPSVV GAPPHLYDMN I
//
