ID A0A026W0G7_OOCBI Unreviewed; 2841 AA.
AC A0A026W0G7;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE SubName: Full=Triple functional domain protein {ECO:0000313|EMBL:EZA49568.1};
GN ORFNames=X777_12113 {ECO:0000313|EMBL:EZA49568.1};
OS Ooceraea biroi (Clonal raider ant) (Cerapachys biroi).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Dorylinae; Ooceraea.
OX NCBI_TaxID=2015173 {ECO:0000313|EMBL:EZA49568.1, ECO:0000313|Proteomes:UP000053097};
RN [1] {ECO:0000313|EMBL:EZA49568.1, ECO:0000313|Proteomes:UP000053097}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24508170; DOI=10.1016/j.cub.2014.01.018;
RA Oxley P.R., Ji L., Fetter-Pruneda I., McKenzie S.K., Li C., Hu H.,
RA Zhang G., Kronauer D.J.;
RT "The genome of the clonal raider ant Cerapachys biroi.";
RL Curr. Biol. 24:451-458(2014).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. {ECO:0000256|ARBA:ARBA00006692}.
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DR EMBL; KK107503; EZA49568.1; -; Genomic_DNA.
DR STRING; 2015173.A0A026W0G7; -.
DR EnsemblMetazoa; XM_011348035.3; XP_011346337.3; LOC105284486.
DR OMA; IRYLHNC; -.
DR Proteomes; UP000053097; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0043232; C:intracellular non-membrane-bounded organelle; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0009653; P:anatomical structure morphogenesis; IEA:UniProt.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProt.
DR GO; GO:0016043; P:cellular component organization; IEA:UniProt.
DR CDD; cd00063; FN3; 1.
DR CDD; cd00096; Ig; 1.
DR CDD; cd13240; PH1_Kalirin_Trio_like; 1.
DR CDD; cd13241; PH2_Kalirin_Trio_p63RhoGEF; 1.
DR CDD; cd00160; RhoGEF; 2.
DR CDD; cd00170; SEC14; 1.
DR CDD; cd00176; SPEC; 3.
DR Gene3D; 1.20.58.60; -; 4.
DR Gene3D; 3.40.525.10; CRAL-TRIO lipid binding domain; 1.
DR Gene3D; 1.20.900.10; Dbl homology (DH) domain; 2.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 2.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR001251; CRAL-TRIO_dom.
DR InterPro; IPR036865; CRAL-TRIO_dom_sf.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR047054; Kalirin_TRIO_PH_1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR018159; Spectrin/alpha-actinin.
DR InterPro; IPR002017; Spectrin_repeat.
DR PANTHER; PTHR22826:SF210; CRAL-TRIO DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR22826; RHO GUANINE EXCHANGE FACTOR-RELATED; 1.
DR Pfam; PF13716; CRAL_TRIO_2; 1.
DR Pfam; PF07679; I-set; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF00621; RhoGEF; 2.
DR Pfam; PF00435; Spectrin; 3.
DR SMART; SM00409; IG; 1.
DR SMART; SM00233; PH; 2.
DR SMART; SM00325; RhoGEF; 2.
DR SMART; SM00220; S_TKc; 1.
DR SMART; SM00516; SEC14; 1.
DR SMART; SM00150; SPEC; 5.
DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 2.
DR SUPFAM; SSF48726; Immunoglobulin; 1.
DR SUPFAM; SSF50729; PH domain-like; 2.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF46966; Spectrin repeat; 6.
DR PROSITE; PS50191; CRAL_TRIO; 1.
DR PROSITE; PS50010; DH_2; 2.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS50003; PH_DOMAIN; 2.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Guanine-nucleotide releasing factor {ECO:0000256|ARBA:ARBA00022658};
KW Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Reference proteome {ECO:0000313|Proteomes:UP000053097}.
FT DOMAIN 9..155
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000259|PROSITE:PS50191"
FT DOMAIN 1041..1216
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 1234..1340
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 1845..2028
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT DOMAIN 2046..2156
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT DOMAIN 2355..2443
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 2551..2805
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 505..524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1346..1366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1382..1413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1499..1536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1586..1708
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1798..1818
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2180..2244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1501..1536
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1586..1610
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1632..1650
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1653..1679
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1680..1708
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1804..1818
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2218..2244
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 2580
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 2841 AA; 319498 MW; 8BE23F84C69D5755 CRC64;
MDGTRAAEVL PLLQERLAIL PGGRDRRGGP VLLFPSTPRR ERAKPEDYRR LLQYLFAIPS
DEARGLRFTV IVDMRGTTWD SVKPILKVLH EHFHRTVHIA FLIKPENFWQ KQRTSLAKQK
KYNFEINTIS LEALVKVIDP SQLTADLDGS LQYDHAQWID TRLVVEDFTW QAADLLDRLD
DLQEDLSRND FADDVAGAKH GIDLHNEMKK KIVKVPVEDI KVVGQRLLQR FNNSATATGG
EGGSIDNGAA SCADTDGRAL ATLVVQHLDS VHAAHQHLLY LWHIKKVKLD QCFQLRLFEQ
DCEKMFDWIC HNREAFLASY VEIGRSYQLA KNLQEEHKHF TMSSMNVYVN INKILTMAGR
LLETQHYAAG HIRAVAGRLD RAWKEFAAGL DERTAVLSLS VVFHHKAEQY VDNVTDWSQA
CDTSNLPNEI PVLESHIRQH QTLYEAMCQA YTEVYNAYQA LLSGLGSMLQ YSLGIWVHST
SKKLLYQLDH LVQVCNQPQG IDHVARKHSQ DGHSIDSHTG TSGNPAADYS EGASHVLAVI
HQILGHHRAL EARWHARKVK LHQRLALKLF QEDVKQVLDW LTNHGEVFIR KNTGVGRNLQ
KARVYQKSHE HFENVAQNTY TNATKLLTAA EELAHTGECA PDEIYAVAQE LEAHVSSFAA
RVEQRRRRLD LAVVFYTHEK ELTGWVDELR QELQQDEVAE NLETAERLLE QCAQHRSSCL
EACASTIAQG EALLQELRDA TDAPDTTGSI SAVESALDRL ASLRQELEDL WATRKLRLEL
CLRLRVFERD ALEASGQLEM WTQELQGPPR EGSPEQLLRV HNDGVAHMQN TAFQVLHRGQ
ELAQVLEEAG VCIMADGQHS AAARVQVLLE FLNEREMDAE DLAEMRRVRL EQASQLLQLQ
TDASHVIKWI RNGESILLAS LRIPENQQEA DLLVKEHDQF QLAIAKTHAS AVQVKQRADA
LLTANHYDPK SIREVAEDVT KRWQQLVTCA EERHKLVTAS FNFWKTVDSV RTVLDNPLLE
EKIKGKDLKE LNEEKRRSAR RKEFIMAELL QTERTYVKDL ETCIRCFLDE TRCGKGNVPL
GLQSRESIIF SNIEEIYQFH SNVFLRELEK YETMPEDVGH CFVVWAPKFD MYVTYCKNKP
ESNQFLVTHG GTWFEELQRK HRAEHPIAAY LIKPVQRITK YQLLLKDLQN CCQEGQGEIK
EGLEVMLNVP KKANDALHLS LLEGCDVSID ALGDVVLQDS FTVWDPKQLI RKGRDRHIFL
FELYLLFSKD VKDSAGKVKY IYKNRLLTSE LGVTEHIEGD ECKFAVWTGR APTSDTRIVL
RASSMEAKQL WVKRLREVIQ ETFLGKNMPK SPAKKSSSQR SSRDLEECAS LDDSVENLDR
NSLASFGSTN TTDSDKPSDR TDKNCTFPRS LKDPLPKPLA QTLALLATRM LHGSAGFLRA
CPLRQGWCDT EKAMEATARR VGWGASWVGL VIISSLERPT GVVEMTWVVA DHMAAPGSRE
LSVTKGQQVE VKASTQQQHH QQSHHHPYHQ QQISQAIVQA QQQTAVTSST TTSTLPLTGT
VNAASTAQQT ASSLTVLSSA VLSPMLSEDA ETTGSDGSGS GNTNSPGNKR RGFSGRKWLP
PPLRKLSQGK VEKTNMAVTT SSSPLIGPSL KKSNSDKRFK LPSGVEHNRP TKATFEAEAE
AQEGEEVDKE EENEEQQEIE VDVDADVTES DETAVASLQE QNGGEDADDD LELPPPMKPI
TEPILVTTAN GPSGSTIPSE LPGKRSAERT TKILDGSAAT TADLSEIEQI VKERMEQHTE
NQERQSLMRT PNGKSLNNDE EYCIATTNPV EESDKSDPEG TAIAKRQFVI RELVDTERDY
VNDLKQIVEG YMALMRNPDC EIPLPEDLRG GKDKMVFGNI EAIYEWHRDF FLKALERCLE
RPEELGPLFK RYERKLHMYV VYCQNKPVSE YIVSEYIDTY FEELRQKLGH RLQLCDLLIK
PIQRITKYQL LLREALRLTE RTERLSEIEG LRAAAHVMRV IPKAANDMMD VGRLQGFDGK
ITAQGKLLLH GPLLVSEISN VLTRGKEWQV FLFEQNIIFS ESVGKKTQFT NPAYIYKAHI
QVNKMSLEDS YDDPEKFVIR STDPRKPGLG FSCSVAEESN GPRRQEWVDT ITAILQTQRD
FLKAIQSPIA YQKELTKDPL RATTTTSEPA IRATVSVPPT LMVPGSTNRD KSNDRRTNQQ
SLQRSHTGGL DCAQPRTPSP TKSRLNFLEG FKNTLRTRSP IRNNSIPVVP GARVRLAADW
GRLHAGDEIV VSHLDGPGLV VSPVNTKDEL WIPASLVPNS AISRAWSFRP RKIDLVKSGH
SVNFRESTTP EQKSPIVLNS PMSIRAVTGE VVGLPVETRN ADGATVTWRK EGENRCIRED
DRYQFQRSAN FVYLQITGCR ASDSGIYHCR VKCEAGSCST KISLFIAGGK SGTSARVVAS
SKVEVDWEKQ DIDSASCSIE CRTLPSQQWI PVLNQANDPP AIVDVLPDTS YSFRVMGDDG
KTTSPSVVIT LSRLDVDGGA EWEAKQFIGR YLELDELGSG RFGTVRRARD KGTGQEVALK
QIPRHKQSRS LTRAEYDVLA STHHANIVRA FALFENAPRP GIDTIVLELV KGTTLFACLS
EKTKYNEATV ARYTGQLLSA LYWLHCRNQA HLDVKPENVL IDQEADQVKL IDLGEAVRTP
IDEIVPPPAD LEFAAPELVL GRPTGPYTDM WAVGVFIYVL LSGLSPFLDD SVEETTANIL
KCDFCFPDEY FETISSDAKE LLGRLLCLCG EDRLNAEICL ASPWLKVSTG AIIPSTRMAA
FIERRAHCLK LRQDHNDSFY S
//
